doc_id	sent_index	relation_id	relation	trigger	trigger_offset	arg_num	arg_head	arg_protein	arg_domain	arg_site	arg_sugar	arg_head_offset	arg_base_np	arg_base_np_offset	arg_np	arg_np_offset	sent_text
27480293	0	0	theme	Mouse	95:99	arg1	Brain					101:105	Mouse Brain	95:105	Mouse Brain	95:105	Evaluation of Different N-Glycopeptide Enrichment Methods for N-Glycosylation Sites Mapping in Mouse Brain.
27480293	4	1	from	1891	622:625	arg1	basis					558:562	the basis	554:562	the basis of our results	554:577	On the basis of our results, the identified N-glycosylation sites were 1891, 1241, 891, 869, and 710 and the FDR values were 3.29, 5.62, 9.54, 9.54, and 20.02%, respectively.
27480293	1	2	theme	many	161:164	arg1	pathways					177:184	many biological pathways	161:184	many biological pathways	161:184	N-Glycosylation of proteins plays a critical role in many biological pathways.
27480293	4	3	theme	identified	584:593	arg1	1891					622:625	1891	622:625	1891	622:625	On the basis of our results, the identified N-glycosylation sites were 1891, 1241, 891, 869, and 710 and the FDR values were 3.29, 5.62, 9.54, 9.54, and 20.02%, respectively.
27480293	4	3	theme	identified	584:593	arg1	sites					611:615	the identified N-glycosylation sites	580:615	the identified N-glycosylation sites	580:615	On the basis of our results, the identified N-glycosylation sites were 1891, 1241, 891, 869, and 710 and the FDR values were 3.29, 5.62, 9.54, 9.54, and 20.02%, respectively.
27480293	3	4	theme	enrichment	347:356	arg1	affinity					419:426	lectin affinity	412:426	lectin affinity	412:426	Five enrichment methods, including IP-ZIC-HILIC, hydrazide chemistry, lectin affinity, ZIC-HILIC-FA, and TiO2 affinity were evaluated and compared in the study of mapping N-glycosylation sites in mouse brain.
27480293	3	4	theme	enrichment	347:356	arg1	affinity					452:459	TiO2 affinity	447:459	TiO2 affinity	447:459	Five enrichment methods, including IP-ZIC-HILIC, hydrazide chemistry, lectin affinity, ZIC-HILIC-FA, and TiO2 affinity were evaluated and compared in the study of mapping N-glycosylation sites in mouse brain.
27480293	3	4	theme	enrichment	347:356	arg1	IP-ZIC-HILIC					377:388	IP-ZIC-HILIC	377:388	IP-ZIC-HILIC	377:388	Five enrichment methods, including IP-ZIC-HILIC, hydrazide chemistry, lectin affinity, ZIC-HILIC-FA, and TiO2 affinity were evaluated and compared in the study of mapping N-glycosylation sites in mouse brain.
27480293	3	4	theme	enrichment	347:356	arg1	ZIC-HILIC-FA					429:440	ZIC-HILIC-FA	429:440	ZIC-HILIC-FA	429:440	Five enrichment methods, including IP-ZIC-HILIC, hydrazide chemistry, lectin affinity, ZIC-HILIC-FA, and TiO2 affinity were evaluated and compared in the study of mapping N-glycosylation sites in mouse brain.
27480293	3	4	theme	enrichment	347:356	arg1	methods					358:364	Five enrichment methods	342:364	Five enrichment methods	342:364	Five enrichment methods, including IP-ZIC-HILIC, hydrazide chemistry, lectin affinity, ZIC-HILIC-FA, and TiO2 affinity were evaluated and compared in the study of mapping N-glycosylation sites in mouse brain.
27480293	3	4	theme	enrichment	347:356	arg1	chemistry					401:409	hydrazide chemistry	391:409	hydrazide chemistry	391:409	Five enrichment methods, including IP-ZIC-HILIC, hydrazide chemistry, lectin affinity, ZIC-HILIC-FA, and TiO2 affinity were evaluated and compared in the study of mapping N-glycosylation sites in mouse brain.
27480293	3	5	from	sites	529:533	arg1	brain					544:548	mouse brain	538:548	mouse brain	538:548	Five enrichment methods, including IP-ZIC-HILIC, hydrazide chemistry, lectin affinity, ZIC-HILIC-FA, and TiO2 affinity were evaluated and compared in the study of mapping N-glycosylation sites in mouse brain.
27480293	1	6	theme	biological	166:175	arg1	pathways					177:184	many biological pathways	161:184	many biological pathways	161:184	N-Glycosylation of proteins plays a critical role in many biological pathways.
27480293	7	7	theme	transmembrane	1111:1123	arg1	N-glycoproteins					1125:1139	the 57 novel transmembrane N-glycoproteins	1098:1139	the 57 novel transmembrane N-glycoproteins	1098:1139	N-glycosylation site information was used to confirm or correct the transmembrane topology of the 57 novel transmembrane N-glycoproteins.
27480293	6	8	dep	N-X-T/S/C	941:949	arg1	P					956:956	X ≠ P	952:956	N-X-T/S/C; X ≠ P	941:956	In this work, we identified a total of 3446 unique glycosylation sites conforming to the N-glycosylation consensus motif (N-X-T/S/C; X ≠ P) with (18)O labeling in 1597 N-glycoproteins.
27480293	6	9	gly	N-glycoproteins	987:1001	arg1	N-glycoproteins					987:1001	1597 N-glycoproteins	982:1001	1597 N-glycoproteins	982:1001	In this work, we identified a total of 3446 unique glycosylation sites conforming to the N-glycosylation consensus motif (N-X-T/S/C; X ≠ P) with (18)O labeling in 1597 N-glycoproteins.
27480293	7	10	gly	N-glycoproteins	1125:1139	arg1	N-glycoproteins					1125:1139	the 57 novel transmembrane N-glycoproteins	1098:1139	the 57 novel transmembrane N-glycoproteins	1098:1139	N-glycosylation site information was used to confirm or correct the transmembrane topology of the 57 novel transmembrane N-glycoproteins.
27480293	3	11	theme	hydrazide	391:399	arg1	chemistry					401:409	hydrazide chemistry	391:409	hydrazide chemistry	391:409	Five enrichment methods, including IP-ZIC-HILIC, hydrazide chemistry, lectin affinity, ZIC-HILIC-FA, and TiO2 affinity were evaluated and compared in the study of mapping N-glycosylation sites in mouse brain.
27480293	3	12	theme	sites	529:533	arg1	study					496:500	the study	492:500	the study of mapping N-glycosylation sites in mouse brain	492:548	Five enrichment methods, including IP-ZIC-HILIC, hydrazide chemistry, lectin affinity, ZIC-HILIC-FA, and TiO2 affinity were evaluated and compared in the study of mapping N-glycosylation sites in mouse brain.
27480293	4	13	theme	N-glycosylation	595:609	arg1	1891					622:625	1891	622:625	1891	622:625	On the basis of our results, the identified N-glycosylation sites were 1891, 1241, 891, 869, and 710 and the FDR values were 3.29, 5.62, 9.54, 9.54, and 20.02%, respectively.
27480293	4	13	theme	N-glycosylation	595:609	arg1	sites					611:615	the identified N-glycosylation sites	580:615	the identified N-glycosylation sites	580:615	On the basis of our results, the identified N-glycosylation sites were 1891, 1241, 891, 869, and 710 and the FDR values were 3.29, 5.62, 9.54, 9.54, and 20.02%, respectively.
27480293	2	14	from	present	236:242	arg1	sources					258:264	biological sources	247:264	biological sources	247:264	Because highly heterogeneous N-glycopeptides are present in biological sources, the enrichment procedure is a crucial step for mass spectrometry analysis.
27480293	3	15	theme	mapping	505:511	arg1	sites					529:533	mapping N-glycosylation sites	505:533	mapping N-glycosylation sites in mouse brain	505:548	Five enrichment methods, including IP-ZIC-HILIC, hydrazide chemistry, lectin affinity, ZIC-HILIC-FA, and TiO2 affinity were evaluated and compared in the study of mapping N-glycosylation sites in mouse brain.
27480293	5	16	theme	highest	782:788	arg1	sensitivity					790:800	sensitivity	790:800	sensitivity	790:800	Therefore, IP-ZIC-HILIC enrichment method displayed the highest sensitivity and specificity.
27480293	3	17	from	brain	544:548	arg1	study					496:500	the study	492:500	the study of mapping N-glycosylation sites in mouse brain	492:548	Five enrichment methods, including IP-ZIC-HILIC, hydrazide chemistry, lectin affinity, ZIC-HILIC-FA, and TiO2 affinity were evaluated and compared in the study of mapping N-glycosylation sites in mouse brain.
27480293	2	18	theme	crucial	297:303	arg1	step					305:308	a crucial step	295:308	a crucial step for mass spectrometry analysis	295:339	Because highly heterogeneous N-glycopeptides are present in biological sources, the enrichment procedure is a crucial step for mass spectrometry analysis.
27480293	2	18	theme	crucial	297:303	arg1	procedure					282:290	the enrichment procedure	267:290	the enrichment procedure	267:290	Because highly heterogeneous N-glycopeptides are present in biological sources, the enrichment procedure is a crucial step for mass spectrometry analysis.
27480293	1	19	gly	N-Glycosylation	108:122	arg1	proteins					127:134	proteins	127:134	proteins	127:134	N-Glycosylation of proteins plays a critical role in many biological pathways.
27480293	7	20	theme	site	1020:1023	arg1	information					1025:1035	N-glycosylation site information	1004:1035	N-glycosylation site information	1004:1035	N-glycosylation site information was used to confirm or correct the transmembrane topology of the 57 novel transmembrane N-glycoproteins.
27480293	3	21	from	study	496:500	arg1	brain					544:548	mouse brain	538:548	mouse brain	538:548	Five enrichment methods, including IP-ZIC-HILIC, hydrazide chemistry, lectin affinity, ZIC-HILIC-FA, and TiO2 affinity were evaluated and compared in the study of mapping N-glycosylation sites in mouse brain.
27480293	6	22	dep	motif	934:938	arg1	N-X-T/S/C					941:949	N-X-T/S/C	941:949	N-X-T/S/C; X ≠ P	941:956	In this work, we identified a total of 3446 unique glycosylation sites conforming to the N-glycosylation consensus motif (N-X-T/S/C; X ≠ P) with (18)O labeling in 1597 N-glycoproteins.
27480293	2	23	attach	present	236:242	arg1	sources					258:264	biological sources	247:264	biological sources	247:264	Because highly heterogeneous N-glycopeptides are present in biological sources, the enrichment procedure is a crucial step for mass spectrometry analysis.
27480293	2	23	attach	present	236:242	arg2	N-glycopeptides					216:230	highly heterogeneous N-glycopeptides	195:230	highly heterogeneous N-glycopeptides	195:230	Because highly heterogeneous N-glycopeptides are present in biological sources, the enrichment procedure is a crucial step for mass spectrometry analysis.
27480293	3	24	theme	lectin	412:417	arg1	affinity					419:426	lectin affinity	412:426	lectin affinity	412:426	Five enrichment methods, including IP-ZIC-HILIC, hydrazide chemistry, lectin affinity, ZIC-HILIC-FA, and TiO2 affinity were evaluated and compared in the study of mapping N-glycosylation sites in mouse brain.
27480293	7	25	used	used	1041:1044	arg2	information					1025:1035	N-glycosylation site information	1004:1035	N-glycosylation site information	1004:1035	N-glycosylation site information was used to confirm or correct the transmembrane topology of the 57 novel transmembrane N-glycoproteins.
27480293	3	26	gly	N-glycosylation	513:527	arg2	sites					529:533	mapping N-glycosylation sites	505:533	mapping N-glycosylation sites in mouse brain	505:548	Five enrichment methods, including IP-ZIC-HILIC, hydrazide chemistry, lectin affinity, ZIC-HILIC-FA, and TiO2 affinity were evaluated and compared in the study of mapping N-glycosylation sites in mouse brain.
27480293	2	27	from	sources	258:264	arg1	present					236:242	present	236:242	present	236:242	Because highly heterogeneous N-glycopeptides are present in biological sources, the enrichment procedure is a crucial step for mass spectrometry analysis.
27480293	3	28	theme	TiO2	447:450	arg1	affinity					452:459	TiO2 affinity	447:459	TiO2 affinity	447:459	Five enrichment methods, including IP-ZIC-HILIC, hydrazide chemistry, lectin affinity, ZIC-HILIC-FA, and TiO2 affinity were evaluated and compared in the study of mapping N-glycosylation sites in mouse brain.
27480293	5	29	theme	enrichment	750:759	arg1	method					761:766	IP-ZIC-HILIC enrichment method	737:766	IP-ZIC-HILIC enrichment method	737:766	Therefore, IP-ZIC-HILIC enrichment method displayed the highest sensitivity and specificity.
27480293	6	30	theme	consensus	924:932	arg1	motif					934:938	the N-glycosylation consensus motif	904:938	the N-glycosylation consensus motif (N-X-T/S/C; X ≠ P)	904:957	In this work, we identified a total of 3446 unique glycosylation sites conforming to the N-glycosylation consensus motif (N-X-T/S/C; X ≠ P) with (18)O labeling in 1597 N-glycoproteins.
27480293	4	31	gly	N-glycosylation	595:609	arg2	1891					622:625	1891	622:625	1891	622:625	On the basis of our results, the identified N-glycosylation sites were 1891, 1241, 891, 869, and 710 and the FDR values were 3.29, 5.62, 9.54, 9.54, and 20.02%, respectively.
27480293	4	31	gly	N-glycosylation	595:609	arg2	sites					611:615	the identified N-glycosylation sites	580:615	the identified N-glycosylation sites	580:615	On the basis of our results, the identified N-glycosylation sites were 1891, 1241, 891, 869, and 710 and the FDR values were 3.29, 5.62, 9.54, 9.54, and 20.02%, respectively.
27480293	7	32	theme	N-glycosylation	1004:1018	arg1	information					1025:1035	N-glycosylation site information	1004:1035	N-glycosylation site information	1004:1035	N-glycosylation site information was used to confirm or correct the transmembrane topology of the 57 novel transmembrane N-glycoproteins.
27480293	6	33	theme	O	968:968	arg1	labeling					970:977	(18)O labeling	964:977	(18)O labeling in 1597 N-glycoproteins	964:1001	In this work, we identified a total of 3446 unique glycosylation sites conforming to the N-glycosylation consensus motif (N-X-T/S/C; X ≠ P) with (18)O labeling in 1597 N-glycoproteins.
27480293	0	34	theme	N-Glycopeptide	24:37	arg1	Methods					50:56	Different N-Glycopeptide Enrichment Methods	14:56	Different N-Glycopeptide Enrichment Methods	14:56	Evaluation of Different N-Glycopeptide Enrichment Methods for N-Glycosylation Sites Mapping in Mouse Brain.
27480293	6	35	theme	N-glycosylation	908:922	arg1	motif					934:938	the N-glycosylation consensus motif	904:938	the N-glycosylation consensus motif (N-X-T/S/C; X ≠ P)	904:957	In this work, we identified a total of 3446 unique glycosylation sites conforming to the N-glycosylation consensus motif (N-X-T/S/C; X ≠ P) with (18)O labeling in 1597 N-glycoproteins.
27480293	6	36	gly	glycosylation	870:882	arg2	3446					858:861	3446	858:861	3446	858:861	In this work, we identified a total of 3446 unique glycosylation sites conforming to the N-glycosylation consensus motif (N-X-T/S/C; X ≠ P) with (18)O labeling in 1597 N-glycoproteins.
27480293	6	36	gly	glycosylation	870:882	arg2	sites					884:888	3446 unique glycosylation sites	858:888	3446 unique glycosylation sites conforming to the N-glycosylation consensus motif (N-X-T/S/C; X ≠ P)	858:957	In this work, we identified a total of 3446 unique glycosylation sites conforming to the N-glycosylation consensus motif (N-X-T/S/C; X ≠ P) with (18)O labeling in 1597 N-glycoproteins.
27480293	2	37	theme	spectrometry	319:330	arg1	analysis					332:339	mass spectrometry analysis	314:339	mass spectrometry analysis	314:339	Because highly heterogeneous N-glycopeptides are present in biological sources, the enrichment procedure is a crucial step for mass spectrometry analysis.
27480293	6	38	from	labeling	970:977	arg1	N-glycoproteins					987:1001	1597 N-glycoproteins	982:1001	1597 N-glycoproteins	982:1001	In this work, we identified a total of 3446 unique glycosylation sites conforming to the N-glycosylation consensus motif (N-X-T/S/C; X ≠ P) with (18)O labeling in 1597 N-glycoproteins.
27480293	0	39	theme	Different	14:22	arg1	Methods					50:56	Different N-Glycopeptide Enrichment Methods	14:56	Different N-Glycopeptide Enrichment Methods	14:56	Evaluation of Different N-Glycopeptide Enrichment Methods for N-Glycosylation Sites Mapping in Mouse Brain.
27480293	2	40	theme	mass	314:317	arg1	analysis					332:339	mass spectrometry analysis	314:339	mass spectrometry analysis	314:339	Because highly heterogeneous N-glycopeptides are present in biological sources, the enrichment procedure is a crucial step for mass spectrometry analysis.
27480293	4	41	theme	FDR	660:662	arg1	values					664:669	the FDR values	656:669	the FDR values	656:669	On the basis of our results, the identified N-glycosylation sites were 1891, 1241, 891, 869, and 710 and the FDR values were 3.29, 5.62, 9.54, 9.54, and 20.02%, respectively.
27480293	4	41	theme	FDR	660:662	arg1	%					709:709	3.29, 5.62, 9.54, 9.54, and 20.02%	676:709	3.29, 5.62, 9.54, 9.54, and 20.02%	676:709	On the basis of our results, the identified N-glycosylation sites were 1891, 1241, 891, 869, and 710 and the FDR values were 3.29, 5.62, 9.54, 9.54, and 20.02%, respectively.
27480293	0	42	theme	Methods	50:56	arg1	Evaluation					0:9	Evaluation	0:9	Evaluation of Different N-Glycopeptide Enrichment Methods for N-Glycosylation Sites	0:82	Evaluation of Different N-Glycopeptide Enrichment Methods for N-Glycosylation Sites Mapping in Mouse Brain.
27480293	4	43	theme	results	571:577	arg1	basis					558:562	the basis	554:562	the basis of our results	554:577	On the basis of our results, the identified N-glycosylation sites were 1891, 1241, 891, 869, and 710 and the FDR values were 3.29, 5.62, 9.54, 9.54, and 20.02%, respectively.
27480293	2	44	gly	N-glycopeptides	216:230	arg2	N-glycopeptides					216:230	highly heterogeneous N-glycopeptides	195:230	highly heterogeneous N-glycopeptides	195:230	Because highly heterogeneous N-glycopeptides are present in biological sources, the enrichment procedure is a crucial step for mass spectrometry analysis.
27480293	0	45	theme	Enrichment	39:48	arg1	Methods					50:56	Different N-Glycopeptide Enrichment Methods	14:56	Different N-Glycopeptide Enrichment Methods	14:56	Evaluation of Different N-Glycopeptide Enrichment Methods for N-Glycosylation Sites Mapping in Mouse Brain.
27480293	0	46	from	Mapping	84:90	arg1	Brain					101:105	Mouse Brain	95:105	Mouse Brain	95:105	Evaluation of Different N-Glycopeptide Enrichment Methods for N-Glycosylation Sites Mapping in Mouse Brain.
27480293	7	47	theme	transmembrane	1072:1084	arg1	topology					1086:1093	the transmembrane topology	1068:1093	the transmembrane topology of the 57 novel transmembrane N-glycoproteins	1068:1139	N-glycosylation site information was used to confirm or correct the transmembrane topology of the 57 novel transmembrane N-glycoproteins.
27480293	7	48	theme	novel	1105:1109	arg1	N-glycoproteins					1125:1139	the 57 novel transmembrane N-glycoproteins	1098:1139	the 57 novel transmembrane N-glycoproteins	1098:1139	N-glycosylation site information was used to confirm or correct the transmembrane topology of the 57 novel transmembrane N-glycoproteins.
27480293	0	49	theme	N-Glycosylation	62:76	arg1	Sites					78:82	N-Glycosylation Sites	62:82	N-Glycosylation Sites	62:82	Evaluation of Different N-Glycopeptide Enrichment Methods for N-Glycosylation Sites Mapping in Mouse Brain.
27480293	6	50	theme	sites	884:888	arg1	total					849:853	a total	847:853	a total of 3446 unique glycosylation sites conforming to the N-glycosylation consensus motif (N-X-T/S/C; X ≠ P)	847:957	In this work, we identified a total of 3446 unique glycosylation sites conforming to the N-glycosylation consensus motif (N-X-T/S/C; X ≠ P) with (18)O labeling in 1597 N-glycoproteins.
27480293	2	51	theme	biological	247:256	arg1	sources					258:264	biological sources	247:264	biological sources	247:264	Because highly heterogeneous N-glycopeptides are present in biological sources, the enrichment procedure is a crucial step for mass spectrometry analysis.
27480293	1	52	theme	proteins	127:134	arg1	N-Glycosylation					108:122	N-Glycosylation	108:122	N-Glycosylation of proteins	108:134	N-Glycosylation of proteins plays a critical role in many biological pathways.
27480293	6	53	theme	glycosylation	870:882	arg1	sites					884:888	3446 unique glycosylation sites	858:888	3446 unique glycosylation sites conforming to the N-glycosylation consensus motif (N-X-T/S/C; X ≠ P)	858:957	In this work, we identified a total of 3446 unique glycosylation sites conforming to the N-glycosylation consensus motif (N-X-T/S/C; X ≠ P) with (18)O labeling in 1597 N-glycoproteins.
27480293	7	54	theme	N-glycoproteins	1125:1139	arg1	topology					1086:1093	the transmembrane topology	1068:1093	the transmembrane topology of the 57 novel transmembrane N-glycoproteins	1068:1139	N-glycosylation site information was used to confirm or correct the transmembrane topology of the 57 novel transmembrane N-glycoproteins.
27480293	3	55	theme	N-glycosylation	513:527	arg1	sites					529:533	mapping N-glycosylation sites	505:533	mapping N-glycosylation sites in mouse brain	505:548	Five enrichment methods, including IP-ZIC-HILIC, hydrazide chemistry, lectin affinity, ZIC-HILIC-FA, and TiO2 affinity were evaluated and compared in the study of mapping N-glycosylation sites in mouse brain.
27480293	6	56	theme	unique	863:868	arg1	sites					884:888	3446 unique glycosylation sites	858:888	3446 unique glycosylation sites conforming to the N-glycosylation consensus motif (N-X-T/S/C; X ≠ P)	858:957	In this work, we identified a total of 3446 unique glycosylation sites conforming to the N-glycosylation consensus motif (N-X-T/S/C; X ≠ P) with (18)O labeling in 1597 N-glycoproteins.
27480293	6	57	gly	N-glycosylation	908:922	arg2	motif					934:938	the N-glycosylation consensus motif	904:938	the N-glycosylation consensus motif (N-X-T/S/C; X ≠ P)	904:957	In this work, we identified a total of 3446 unique glycosylation sites conforming to the N-glycosylation consensus motif (N-X-T/S/C; X ≠ P) with (18)O labeling in 1597 N-glycoproteins.
27480293	7	58	gly	N-glycosylation	1004:1018	arg2	site					1020:1023	N-glycosylation site information	1004:1035	N-glycosylation site information	1004:1035	N-glycosylation site information was used to confirm or correct the transmembrane topology of the 57 novel transmembrane N-glycoproteins.
27480293	7	58	gly	N-glycosylation	1004:1018	arg2	information					1025:1035	N-glycosylation site information	1004:1035	N-glycosylation site information	1004:1035	N-glycosylation site information was used to confirm or correct the transmembrane topology of the 57 novel transmembrane N-glycoproteins.
27480293	1	59	theme	critical	144:151	arg1	role					153:156	a critical role	142:156	a critical role	142:156	N-Glycosylation of proteins plays a critical role in many biological pathways.
27480293	2	60	theme	heterogeneous	202:214	arg1	N-glycopeptides					216:230	highly heterogeneous N-glycopeptides	195:230	highly heterogeneous N-glycopeptides	195:230	Because highly heterogeneous N-glycopeptides are present in biological sources, the enrichment procedure is a crucial step for mass spectrometry analysis.
27480293	2	61	theme	enrichment	271:280	arg1	step					305:308	a crucial step	295:308	a crucial step for mass spectrometry analysis	295:339	Because highly heterogeneous N-glycopeptides are present in biological sources, the enrichment procedure is a crucial step for mass spectrometry analysis.
27480293	2	61	theme	enrichment	271:280	arg1	procedure					282:290	the enrichment procedure	267:290	the enrichment procedure	267:290	Because highly heterogeneous N-glycopeptides are present in biological sources, the enrichment procedure is a crucial step for mass spectrometry analysis.
27480293	3	62	theme	mouse	538:542	arg1	brain					544:548	mouse brain	538:548	mouse brain	538:548	Five enrichment methods, including IP-ZIC-HILIC, hydrazide chemistry, lectin affinity, ZIC-HILIC-FA, and TiO2 affinity were evaluated and compared in the study of mapping N-glycosylation sites in mouse brain.
27480293	2	63	located	present	236:242	arg1	sources					258:264	biological sources	247:264	biological sources	247:264	Because highly heterogeneous N-glycopeptides are present in biological sources, the enrichment procedure is a crucial step for mass spectrometry analysis.
27480293	2	63	located	present	236:242	arg2	N-glycopeptides					216:230	highly heterogeneous N-glycopeptides	195:230	highly heterogeneous N-glycopeptides	195:230	Because highly heterogeneous N-glycopeptides are present in biological sources, the enrichment procedure is a crucial step for mass spectrometry analysis.
27480293	6	64	theme	≠	954:954	arg1	P					956:956	X ≠ P	952:956	N-X-T/S/C; X ≠ P	941:956	In this work, we identified a total of 3446 unique glycosylation sites conforming to the N-glycosylation consensus motif (N-X-T/S/C; X ≠ P) with (18)O labeling in 1597 N-glycoproteins.
27480293	5	65	theme	IP-ZIC-HILIC	737:748	arg1	method					761:766	IP-ZIC-HILIC enrichment method	737:766	IP-ZIC-HILIC enrichment method	737:766	Therefore, IP-ZIC-HILIC enrichment method displayed the highest sensitivity and specificity.
27480293	6	66	theme	X	952:952	arg1	P					956:956	X ≠ P	952:956	N-X-T/S/C; X ≠ P	941:956	In this work, we identified a total of 3446 unique glycosylation sites conforming to the N-glycosylation consensus motif (N-X-T/S/C; X ≠ P) with (18)O labeling in 1597 N-glycoproteins.
30903686	0	0	theme	mouse	72:76	arg1	proteins					78:85	human and mouse proteins	62:85	human and mouse proteins	62:85	SPRINT-Gly: predicting N- and O-linked glycosylation sites of human and mouse proteins by using sequence and predicted structural properties.
30903686	4	1	theme	mouse	912:916	arg1	sites					932:936	human and mouse glycosylation sites	902:936	human and mouse glycosylation sites	902:936	RESULTS: The method, called SPRINT-Gly, achieved consistent results between ten-fold cross validation and independent test for predicting human and mouse glycosylation sites.
30903686	1	2	theme	important	251:259	arg1	role					261:264	an important role	248:264	an important role	248:264	MOTIVATION: Protein glycosylation is one of the most abundant post-translational modifications that plays an important role in immune responses, intercellular signaling, inflammation and host-pathogen interactions.
30903686	2	3	gly	glycosylation	456:468	arg2	sites					470:474	glycosylation sites	456:474	glycosylation sites	456:474	However, due to the poor ionization efficiency and microheterogeneity of glycopeptides identifying glycosylation sites is a challenging task, and there is a demand for computational methods.
30903686	9	4	dep	INFORMATION	1479:1489	arg1	available					1515:1523	available	1515:1523	available	1515:1523	SUPPLEMENTARY INFORMATION: Supplementary data are available at Bioinformatics online.
30903686	1	5	theme	Protein	154:160	arg1	glycosylation					162:174	MOTIVATION: Protein glycosylation	142:174	MOTIVATION: Protein glycosylation	142:174	MOTIVATION: Protein glycosylation is one of the most abundant post-translational modifications that plays an important role in immune responses, intercellular signaling, inflammation and host-pathogen interactions.
30903686	9	6	theme	Supplementary	1492:1504	arg1	data					1506:1509	Supplementary data	1492:1509	Supplementary data	1492:1509	SUPPLEMENTARY INFORMATION: Supplementary data are available at Bioinformatics online.
30903686	3	7	theme	N-/O-linked	717:727	arg1	sites					743:747	N-/O-linked glycosylation sites	717:747	N-/O-linked glycosylation sites	717:747	Here, we constructed the largest dataset of human and mouse glycosylation sites to train deep learning neural networks and support vector machine classifiers to predict N-/O-linked glycosylation sites, respectively.
30903686	5	8	dep	model	976:980	arg1	performs					982:989	performs	982:989	performs equally well in human glycoproteins and vice versa	982:1040	For N-glycosylation, a mouse-trained model performs equally well in human glycoproteins and vice versa, however, due to significant differences in O-linked sites separate models were generated.
30903686	0	9	theme	proteins	78:85	arg1	N-					23:24	N-	23:24	N-	23:24	SPRINT-Gly: predicting N- and O-linked glycosylation sites of human and mouse proteins by using sequence and predicted structural properties.
30903686	0	9	theme	proteins	78:85	arg1	glycosylation					39:51	O-linked glycosylation	30:51	O-linked glycosylation	30:51	SPRINT-Gly: predicting N- and O-linked glycosylation sites of human and mouse proteins by using sequence and predicted structural properties.
30903686	6	10	theme	Matthews	1178:1185	arg1	coefficient					1199:1209	Matthews correlation coefficient	1178:1209	Matthews correlation coefficient	1178:1209	Overall, SPRINT-Gly is 18% and 50% higher in Matthews correlation coefficient than the next best method compared in N-linked and O-linked sites, respectively.
30903686	2	11	gly	glycopeptides	430:442	arg2	glycopeptides					430:442	glycopeptides	430:442	glycopeptides identifying glycosylation sites	430:474	However, due to the poor ionization efficiency and microheterogeneity of glycopeptides identifying glycosylation sites is a challenging task, and there is a demand for computational methods.
30903686	5	12	dep	performs	982:989	arg1	glycoproteins					1013:1025	human glycoproteins	1007:1025	human glycoproteins	1007:1025	For N-glycosylation, a mouse-trained model performs equally well in human glycoproteins and vice versa, however, due to significant differences in O-linked sites separate models were generated.
30903686	5	12	dep	performs	982:989	arg1	versa					1036:1040	versa	1036:1040	versa	1036:1040	For N-glycosylation, a mouse-trained model performs equally well in human glycoproteins and vice versa, however, due to significant differences in O-linked sites separate models were generated.
30903686	1	13	theme	immune	269:274	arg1	responses					276:284	immune responses	269:284	immune responses	269:284	MOTIVATION: Protein glycosylation is one of the most abundant post-translational modifications that plays an important role in immune responses, intercellular signaling, inflammation and host-pathogen interactions.
30903686	5	14	link	O-linked	1086:1093	arg1	sites					1095:1099	O-linked sites	1086:1099	O-linked sites	1086:1099	For N-glycosylation, a mouse-trained model performs equally well in human glycoproteins and vice versa, however, due to significant differences in O-linked sites separate models were generated.
30903686	2	15	theme	computational	525:537	arg1	methods					539:545	computational methods	525:545	computational methods	525:545	However, due to the poor ionization efficiency and microheterogeneity of glycopeptides identifying glycosylation sites is a challenging task, and there is a demand for computational methods.
30903686	2	16	gly	microheterogeneity	408:425	arg1	glycopeptides					430:442	glycopeptides	430:442	glycopeptides identifying glycosylation sites	430:474	However, due to the poor ionization efficiency and microheterogeneity of glycopeptides identifying glycosylation sites is a challenging task, and there is a demand for computational methods.
30903686	4	17	theme	consistent	813:822	arg1	results					824:830	consistent results	813:830	consistent results between ten-fold cross validation and independent test for predicting human and mouse glycosylation sites	813:936	RESULTS: The method, called SPRINT-Gly, achieved consistent results between ten-fold cross validation and independent test for predicting human and mouse glycosylation sites.
30903686	2	18	theme	challenging	481:491	arg1	task					493:496	a challenging task	479:496	a challenging task	479:496	However, due to the poor ionization efficiency and microheterogeneity of glycopeptides identifying glycosylation sites is a challenging task, and there is a demand for computational methods.
30903686	6	19	link	O-linked	1262:1269	arg1	sites					1271:1275	N-linked and O-linked sites	1249:1275	N-linked and O-linked sites	1249:1275	Overall, SPRINT-Gly is 18% and 50% higher in Matthews correlation coefficient than the next best method compared in N-linked and O-linked sites, respectively.
30903686	4	20	theme	human	902:906	arg1	sites					932:936	human and mouse glycosylation sites	902:936	human and mouse glycosylation sites	902:936	RESULTS: The method, called SPRINT-Gly, achieved consistent results between ten-fold cross validation and independent test for predicting human and mouse glycosylation sites.
30903686	6	21	theme	correlation	1187:1197	arg1	coefficient					1199:1209	Matthews correlation coefficient	1178:1209	Matthews correlation coefficient	1178:1209	Overall, SPRINT-Gly is 18% and 50% higher in Matthews correlation coefficient than the next best method compared in N-linked and O-linked sites, respectively.
30903686	4	22	gly	glycosylation	918:930	arg2	sites					932:936	human and mouse glycosylation sites	902:936	human and mouse glycosylation sites	902:936	RESULTS: The method, called SPRINT-Gly, achieved consistent results between ten-fold cross validation and independent test for predicting human and mouse glycosylation sites.
30903686	7	23	theme	novel	1345:1349	arg1	structure					1351:1359	novel structure	1345:1359	novel structure	1345:1359	This improved performance is due to the inclusion of novel structure and sequence-based features.
30903686	0	24	link	O-linked	30:37	arg1	glycosylation					39:51	O-linked glycosylation	30:51	O-linked glycosylation	30:51	SPRINT-Gly: predicting N- and O-linked glycosylation sites of human and mouse proteins by using sequence and predicted structural properties.
30903686	3	25	theme	deep	637:640	arg1	networks					658:665	deep learning neural networks	637:665	deep learning neural networks	637:665	Here, we constructed the largest dataset of human and mouse glycosylation sites to train deep learning neural networks and support vector machine classifiers to predict N-/O-linked glycosylation sites, respectively.
30903686	5	26	from	differences	1071:1081	arg1	sites					1095:1099	O-linked sites	1086:1099	O-linked sites	1086:1099	For N-glycosylation, a mouse-trained model performs equally well in human glycoproteins and vice versa, however, due to significant differences in O-linked sites separate models were generated.
30903686	2	27	theme	ionization	382:391	arg1	efficiency					393:402	poor ionization efficiency	377:402	poor ionization efficiency	377:402	However, due to the poor ionization efficiency and microheterogeneity of glycopeptides identifying glycosylation sites is a challenging task, and there is a demand for computational methods.
30903686	4	28	theme	ten-fold	840:847	arg1	validation					855:864	ten-fold cross validation	840:864	ten-fold cross validation	840:864	RESULTS: The method, called SPRINT-Gly, achieved consistent results between ten-fold cross validation and independent test for predicting human and mouse glycosylation sites.
30903686	0	29	theme	predicted	109:117	arg1	properties					130:139	predicted structural properties	109:139	predicted structural properties	109:139	SPRINT-Gly: predicting N- and O-linked glycosylation sites of human and mouse proteins by using sequence and predicted structural properties.
30903686	6	30	theme	N-linked	1249:1256	arg1	sites					1271:1275	N-linked and O-linked sites	1249:1275	N-linked and O-linked sites	1249:1275	Overall, SPRINT-Gly is 18% and 50% higher in Matthews correlation coefficient than the next best method compared in N-linked and O-linked sites, respectively.
30903686	3	31	theme	largest	573:579	arg1	dataset					581:587	the largest dataset	569:587	the largest dataset of human and mouse glycosylation sites	569:626	Here, we constructed the largest dataset of human and mouse glycosylation sites to train deep learning neural networks and support vector machine classifiers to predict N-/O-linked glycosylation sites, respectively.
30903686	3	32	link	N-/O-linked	717:727	arg1	sites					743:747	N-/O-linked glycosylation sites	717:747	N-/O-linked glycosylation sites	717:747	Here, we constructed the largest dataset of human and mouse glycosylation sites to train deep learning neural networks and support vector machine classifiers to predict N-/O-linked glycosylation sites, respectively.
30903686	2	33	theme	glycosylation	456:468	arg1	sites					470:474	glycosylation sites	456:474	glycosylation sites	456:474	However, due to the poor ionization efficiency and microheterogeneity of glycopeptides identifying glycosylation sites is a challenging task, and there is a demand for computational methods.
30903686	3	34	theme	human	592:596	arg1	sites					622:626	human and mouse glycosylation sites	592:626	human and mouse glycosylation sites	592:626	Here, we constructed the largest dataset of human and mouse glycosylation sites to train deep learning neural networks and support vector machine classifiers to predict N-/O-linked glycosylation sites, respectively.
30903686	1	35	theme	intercellular	287:299	arg1	signaling					301:309	intercellular signaling	287:309	intercellular signaling	287:309	MOTIVATION: Protein glycosylation is one of the most abundant post-translational modifications that plays an important role in immune responses, intercellular signaling, inflammation and host-pathogen interactions.
30903686	6	36	theme	next	1220:1223	arg1	method					1230:1235	the next best method	1216:1235	the next best method compared in N-linked and O-linked sites, respectively	1216:1289	Overall, SPRINT-Gly is 18% and 50% higher in Matthews correlation coefficient than the next best method compared in N-linked and O-linked sites, respectively.
30903686	5	37	theme	human	1007:1011	arg1	glycoproteins					1013:1025	human glycoproteins	1007:1025	human glycoproteins	1007:1025	For N-glycosylation, a mouse-trained model performs equally well in human glycoproteins and vice versa, however, due to significant differences in O-linked sites separate models were generated.
30903686	3	38	gly	glycosylation	608:620	arg2	sites					622:626	human and mouse glycosylation sites	592:626	human and mouse glycosylation sites	592:626	Here, we constructed the largest dataset of human and mouse glycosylation sites to train deep learning neural networks and support vector machine classifiers to predict N-/O-linked glycosylation sites, respectively.
30903686	0	39	theme	O-linked	30:37	arg1	glycosylation					39:51	O-linked glycosylation	30:51	O-linked glycosylation	30:51	SPRINT-Gly: predicting N- and O-linked glycosylation sites of human and mouse proteins by using sequence and predicted structural properties.
30903686	3	40	theme	support	671:677	arg1	machine					686:692	support vector machine	671:692	support vector machine classifiers	671:704	Here, we constructed the largest dataset of human and mouse glycosylation sites to train deep learning neural networks and support vector machine classifiers to predict N-/O-linked glycosylation sites, respectively.
30903686	2	41	theme	glycopeptides	430:442	arg1	microheterogeneity					408:425	microheterogeneity	408:425	microheterogeneity	408:425	However, due to the poor ionization efficiency and microheterogeneity of glycopeptides identifying glycosylation sites is a challenging task, and there is a demand for computational methods.
30903686	2	41	theme	glycopeptides	430:442	arg1	efficiency					393:402	poor ionization efficiency	377:402	poor ionization efficiency	377:402	However, due to the poor ionization efficiency and microheterogeneity of glycopeptides identifying glycosylation sites is a challenging task, and there is a demand for computational methods.
30903686	3	42	theme	glycosylation	608:620	arg1	sites					622:626	human and mouse glycosylation sites	592:626	human and mouse glycosylation sites	592:626	Here, we constructed the largest dataset of human and mouse glycosylation sites to train deep learning neural networks and support vector machine classifiers to predict N-/O-linked glycosylation sites, respectively.
30903686	6	43	theme	best	1225:1228	arg1	method					1230:1235	the next best method	1216:1235	the next best method compared in N-linked and O-linked sites, respectively	1216:1289	Overall, SPRINT-Gly is 18% and 50% higher in Matthews correlation coefficient than the next best method compared in N-linked and O-linked sites, respectively.
30903686	1	44	theme	abundant	195:202	arg1	modifications					223:235	the most abundant post-translational modifications	186:235	the most abundant post-translational modifications	186:235	MOTIVATION: Protein glycosylation is one of the most abundant post-translational modifications that plays an important role in immune responses, intercellular signaling, inflammation and host-pathogen interactions.
30903686	0	45	theme	structural	119:128	arg1	properties					130:139	predicted structural properties	109:139	predicted structural properties	109:139	SPRINT-Gly: predicting N- and O-linked glycosylation sites of human and mouse proteins by using sequence and predicted structural properties.
30903686	3	46	theme	neural	651:656	arg1	networks					658:665	deep learning neural networks	637:665	deep learning neural networks	637:665	Here, we constructed the largest dataset of human and mouse glycosylation sites to train deep learning neural networks and support vector machine classifiers to predict N-/O-linked glycosylation sites, respectively.
30903686	3	47	theme	sites	622:626	arg1	dataset					581:587	the largest dataset	569:587	the largest dataset of human and mouse glycosylation sites	569:626	Here, we constructed the largest dataset of human and mouse glycosylation sites to train deep learning neural networks and support vector machine classifiers to predict N-/O-linked glycosylation sites, respectively.
30903686	1	48	theme	post-translational	204:221	arg1	modifications					223:235	the most abundant post-translational modifications	186:235	the most abundant post-translational modifications	186:235	MOTIVATION: Protein glycosylation is one of the most abundant post-translational modifications that plays an important role in immune responses, intercellular signaling, inflammation and host-pathogen interactions.
30903686	8	49	dep	//sparks-lab.org/server/SPRINT-Gly/	1428:1462	arg1	AVAILABILITY					1390:1401	AVAILABILITY	1390:1401	AVAILABILITY	1390:1401	AVAILABILITY AND IMPLEMENTATION: http://sparks-lab.org/server/SPRINT-Gly/.
30903686	8	49	dep	//sparks-lab.org/server/SPRINT-Gly/	1428:1462	arg1	http					1423:1426	http	1423:1426	http	1423:1426	AVAILABILITY AND IMPLEMENTATION: http://sparks-lab.org/server/SPRINT-Gly/.
30903686	8	49	dep	//sparks-lab.org/server/SPRINT-Gly/	1428:1462	arg1	IMPLEMENTATION					1407:1420	IMPLEMENTATION	1407:1420	IMPLEMENTATION	1407:1420	AVAILABILITY AND IMPLEMENTATION: http://sparks-lab.org/server/SPRINT-Gly/.
30903686	3	50	gly	glycosylation	729:741	arg2	sites					743:747	N-/O-linked glycosylation sites	717:747	N-/O-linked glycosylation sites	717:747	Here, we constructed the largest dataset of human and mouse glycosylation sites to train deep learning neural networks and support vector machine classifiers to predict N-/O-linked glycosylation sites, respectively.
30903686	7	51	theme	features	1380:1387	arg1	inclusion					1332:1340	the inclusion	1328:1340	the inclusion of novel structure and sequence-based features	1328:1387	This improved performance is due to the inclusion of novel structure and sequence-based features.
30903686	6	52	link	N-linked	1249:1256	arg1	sites					1271:1275	N-linked and O-linked sites	1249:1275	N-linked and O-linked sites	1249:1275	Overall, SPRINT-Gly is 18% and 50% higher in Matthews correlation coefficient than the next best method compared in N-linked and O-linked sites, respectively.
30903686	4	53	theme	independent	870:880	arg1	test					882:885	independent test	870:885	independent test	870:885	RESULTS: The method, called SPRINT-Gly, achieved consistent results between ten-fold cross validation and independent test for predicting human and mouse glycosylation sites.
30903686	6	54	theme	O-linked	1262:1269	arg1	sites					1271:1275	N-linked and O-linked sites	1249:1275	N-linked and O-linked sites	1249:1275	Overall, SPRINT-Gly is 18% and 50% higher in Matthews correlation coefficient than the next best method compared in N-linked and O-linked sites, respectively.
30903686	7	55	theme	structure	1351:1359	arg1	inclusion					1332:1340	the inclusion	1328:1340	the inclusion of novel structure and sequence-based features	1328:1387	This improved performance is due to the inclusion of novel structure and sequence-based features.
30903686	5	56	theme	O-linked	1086:1093	arg1	sites					1095:1099	O-linked sites	1086:1099	O-linked sites	1086:1099	For N-glycosylation, a mouse-trained model performs equally well in human glycoproteins and vice versa, however, due to significant differences in O-linked sites separate models were generated.
30903686	3	57	theme	mouse	602:606	arg1	sites					622:626	human and mouse glycosylation sites	592:626	human and mouse glycosylation sites	592:626	Here, we constructed the largest dataset of human and mouse glycosylation sites to train deep learning neural networks and support vector machine classifiers to predict N-/O-linked glycosylation sites, respectively.
30903686	5	58	theme	mouse-trained	962:974	arg1	model					976:980	a mouse-trained model	960:980	a mouse-trained model performs equally well in human glycoproteins and vice versa	960:1040	For N-glycosylation, a mouse-trained model performs equally well in human glycoproteins and vice versa, however, due to significant differences in O-linked sites separate models were generated.
30903686	1	59	theme	host-pathogen	329:341	arg1	interactions					343:354	host-pathogen interactions	329:354	host-pathogen interactions	329:354	MOTIVATION: Protein glycosylation is one of the most abundant post-translational modifications that plays an important role in immune responses, intercellular signaling, inflammation and host-pathogen interactions.
30903686	5	60	theme	significant	1059:1069	arg1	differences					1071:1081	significant differences	1059:1081	significant differences in O-linked sites	1059:1099	For N-glycosylation, a mouse-trained model performs equally well in human glycoproteins and vice versa, however, due to significant differences in O-linked sites separate models were generated.
30903686	2	61	dep	efficiency	393:402	arg1	the					373:375	the	373:375	the	373:375	However, due to the poor ionization efficiency and microheterogeneity of glycopeptides identifying glycosylation sites is a challenging task, and there is a demand for computational methods.
30903686	0	62	dep	N-	23:24	arg1	sites					53:57	sites	53:57	sites	53:57	SPRINT-Gly: predicting N- and O-linked glycosylation sites of human and mouse proteins by using sequence and predicted structural properties.
30903686	4	63	theme	cross	849:853	arg1	validation					855:864	ten-fold cross validation	840:864	ten-fold cross validation	840:864	RESULTS: The method, called SPRINT-Gly, achieved consistent results between ten-fold cross validation and independent test for predicting human and mouse glycosylation sites.
30903686	7	64	theme	improved	1297:1304	arg1	performance					1306:1316	This improved performance	1292:1316	This improved performance	1292:1316	This improved performance is due to the inclusion of novel structure and sequence-based features.
30903686	1	65	theme	modifications	223:235	arg1	one					179:181	one	179:181	one	179:181	MOTIVATION: Protein glycosylation is one of the most abundant post-translational modifications that plays an important role in immune responses, intercellular signaling, inflammation and host-pathogen interactions.
30903686	1	65	theme	modifications	223:235	arg1	modifications					223:235	the most abundant post-translational modifications	186:235	the most abundant post-translational modifications	186:235	MOTIVATION: Protein glycosylation is one of the most abundant post-translational modifications that plays an important role in immune responses, intercellular signaling, inflammation and host-pathogen interactions.
30903686	3	66	theme	vector	679:684	arg1	machine					686:692	support vector machine	671:692	support vector machine classifiers	671:704	Here, we constructed the largest dataset of human and mouse glycosylation sites to train deep learning neural networks and support vector machine classifiers to predict N-/O-linked glycosylation sites, respectively.
30903686	3	67	theme	learning	642:649	arg1	networks					658:665	deep learning neural networks	637:665	deep learning neural networks	637:665	Here, we constructed the largest dataset of human and mouse glycosylation sites to train deep learning neural networks and support vector machine classifiers to predict N-/O-linked glycosylation sites, respectively.
30903686	9	68	theme	Bioinformatics	1528:1541	arg1	online					1543:1548	Bioinformatics online	1528:1548	Bioinformatics online	1528:1548	SUPPLEMENTARY INFORMATION: Supplementary data are available at Bioinformatics online.
30903686	4	69	theme	glycosylation	918:930	arg1	sites					932:936	human and mouse glycosylation sites	902:936	human and mouse glycosylation sites	902:936	RESULTS: The method, called SPRINT-Gly, achieved consistent results between ten-fold cross validation and independent test for predicting human and mouse glycosylation sites.
30903686	5	70	theme	separate	1101:1108	arg1	models					1110:1115	due to significant differences in O-linked sites separate models	1052:1115	due to significant differences in O-linked sites separate models	1052:1115	For N-glycosylation, a mouse-trained model performs equally well in human glycoproteins and vice versa, however, due to significant differences in O-linked sites separate models were generated.
30903686	0	71	theme	human	62:66	arg1	proteins					78:85	human and mouse proteins	62:85	human and mouse proteins	62:85	SPRINT-Gly: predicting N- and O-linked glycosylation sites of human and mouse proteins by using sequence and predicted structural properties.
30903686	3	72	theme	machine	686:692	arg1	classifiers					694:704	support vector machine classifiers	671:704	support vector machine classifiers	671:704	Here, we constructed the largest dataset of human and mouse glycosylation sites to train deep learning neural networks and support vector machine classifiers to predict N-/O-linked glycosylation sites, respectively.
30903686	0	73	gly	glycosylation	39:51	arg1	proteins					78:85	human and mouse proteins	62:85	human and mouse proteins	62:85	SPRINT-Gly: predicting N- and O-linked glycosylation sites of human and mouse proteins by using sequence and predicted structural properties.
30903686	9	74	from	online	1543:1548	arg1	available					1515:1523	available	1515:1523	available	1515:1523	SUPPLEMENTARY INFORMATION: Supplementary data are available at Bioinformatics online.
30903686	2	75	theme	poor	377:380	arg1	efficiency					393:402	poor ionization efficiency	377:402	poor ionization efficiency	377:402	However, due to the poor ionization efficiency and microheterogeneity of glycopeptides identifying glycosylation sites is a challenging task, and there is a demand for computational methods.
30903686	7	76	theme	sequence-based	1365:1378	arg1	features					1380:1387	sequence-based features	1365:1387	sequence-based features	1365:1387	This improved performance is due to the inclusion of novel structure and sequence-based features.
30903686	9	77	theme	SUPPLEMENTARY	1465:1477	arg1	INFORMATION					1479:1489	SUPPLEMENTARY INFORMATION	1465:1489	SUPPLEMENTARY INFORMATION: Supplementary data are available at Bioinformatics online.	1465:1549	SUPPLEMENTARY INFORMATION: Supplementary data are available at Bioinformatics online.
30903686	5	78	gly	glycoproteins	1013:1025	arg1	glycoproteins					1013:1025	human glycoproteins	1007:1025	human glycoproteins	1007:1025	For N-glycosylation, a mouse-trained model performs equally well in human glycoproteins and vice versa, however, due to significant differences in O-linked sites separate models were generated.
30903686	3	79	theme	glycosylation	729:741	arg1	sites					743:747	N-/O-linked glycosylation sites	717:747	N-/O-linked glycosylation sites	717:747	Here, we constructed the largest dataset of human and mouse glycosylation sites to train deep learning neural networks and support vector machine classifiers to predict N-/O-linked glycosylation sites, respectively.
30903686	5	80	theme	due	1052:1054	arg1	models					1110:1115	due to significant differences in O-linked sites separate models	1052:1115	due to significant differences in O-linked sites separate models	1052:1115	For N-glycosylation, a mouse-trained model performs equally well in human glycoproteins and vice versa, however, due to significant differences in O-linked sites separate models were generated.
30903686	1	81	theme	MOTIVATION	142:151	arg1	glycosylation					162:174	MOTIVATION: Protein glycosylation	142:174	MOTIVATION: Protein glycosylation	142:174	MOTIVATION: Protein glycosylation is one of the most abundant post-translational modifications that plays an important role in immune responses, intercellular signaling, inflammation and host-pathogen interactions.
31577193	9	0	gly	N-glycosylation	1116:1130	arg2	sites					1132:1136	human and mouse N-glycosylation sites	1100:1136	human and mouse N-glycosylation sites	1100:1136	Further, the performance of Nglyc was evaluated using human and mouse N-glycosylation sites.
31577193	2	1	dep	other	287:291	arg1	than					293:296	than	293:296	than	293:296	N-glycosylation predominantly occurs in N-X-[S/T] sequon where X is any amino acid other than proline.
31577193	15	2	theme	//github.com/bioinformaticsML/	1735:1764	arg1	Ngly					1766:1769	https://github.com/bioinformaticsML/ Ngly	1729:1769	https://github.com/bioinformaticsML/ Ngly	1729:1769	Nglyc method is freely available at https://github.com/bioinformaticsML/ Ngly.
31577193	5	3	gly	Nglycosylation	572:585	arg2	sites					587:591	Nglycosylation sites	572:591	Nglycosylation sites	572:591	OBJECTIVE: In this article, our motivation is to develop a computational method to predict Nglycosylation sites in eukaryotic protein sequences.
31577193	0	4	theme	Sites	64:68	arg1	Prediction					34:43	Prediction	34:43	Prediction of N-Glycosylation Sites in Eukaryotic Protein Sequence	34:99	Nglyc: A Random Forest Method for Prediction of N-Glycosylation Sites in Eukaryotic Protein Sequence.
31577193	14	5	theme	human	1654:1658	arg1	sites					1686:1690	human and mouse N-glycosylation sites	1654:1690	human and mouse N-glycosylation sites	1654:1690	Applicability and success of our method was further evaluated using human and mouse N-glycosylation sites.
31577193	4	6	theme	accurate	383:390	arg1	prediction					392:401	accurate prediction	383:401	accurate prediction of N-glycosylation sites	383:426	Therefore, accurate prediction of N-glycosylation sites is essential to understand Nglycosylation mechanism.
31577193	13	7	theme	Comparison	1507:1516	arg1	study					1518:1522	Comparison study	1507:1522	Comparison study	1507:1522	Comparison study shows that our method performs better than the other methods.
31577193	7	8	gly	non-glycosylation	947:963	arg2	sites					965:969	253 non-glycosylation sites	943:969	253 non-glycosylation sites	943:969	The method was trained using a dataset of 600 N-glycosylation sites and 600 non-glycosylation sites and tested on the dataset containing 295 Nglycosylation sites and 253 non-glycosylation sites.
31577193	7	8	gly	non-glycosylation	947:963	arg2	253					943:945	253	943:945	253	943:945	The method was trained using a dataset of 600 N-glycosylation sites and 600 non-glycosylation sites and tested on the dataset containing 295 Nglycosylation sites and 253 non-glycosylation sites.
31577193	0	9	theme	Protein	84:90	arg1	Sequence					92:99	Eukaryotic Protein Sequence	73:99	Eukaryotic Protein Sequence	73:99	Nglyc: A Random Forest Method for Prediction of N-Glycosylation Sites in Eukaryotic Protein Sequence.
31577193	12	10	theme	0.8248	1452:1457	arg1	accuracy					1440:1447	an overall accuracy	1429:1447	an overall accuracy of 0.8248 with 0.8305 sensitivity and 0.8182 specificity	1429:1504	CONCLUSION: Our method achieved an overall accuracy of 0.8248 with 0.8305 sensitivity and 0.8182 specificity.
31577193	5	11	theme	protein	607:613	arg1	sequences					615:623	eukaryotic protein sequences	596:623	eukaryotic protein sequences	596:623	OBJECTIVE: In this article, our motivation is to develop a computational method to predict Nglycosylation sites in eukaryotic protein sequences.
31577193	7	12	theme	non-glycosylation	853:869	arg1	sites					871:875	600 non-glycosylation sites	849:875	600 non-glycosylation sites	849:875	The method was trained using a dataset of 600 N-glycosylation sites and 600 non-glycosylation sites and tested on the dataset containing 295 Nglycosylation sites and 253 non-glycosylation sites.
31577193	10	13	dep	RESULT	1139:1144	arg1	method					1153:1158	Nglyc method	1147:1158	RESULT: Nglyc method	1139:1158	RESULT: Nglyc method achieved an overall training accuracy of 0.8033 with all 315 features.
31577193	0	14	theme	Eukaryotic	73:82	arg1	Sequence					92:99	Eukaryotic Protein Sequence	73:99	Eukaryotic Protein Sequence	73:99	Nglyc: A Random Forest Method for Prediction of N-Glycosylation Sites in Eukaryotic Protein Sequence.
31577193	0	15	from	Prediction	34:43	arg1	Sequence					92:99	Eukaryotic Protein Sequence	73:99	Eukaryotic Protein Sequence	73:99	Nglyc: A Random Forest Method for Prediction of N-Glycosylation Sites in Eukaryotic Protein Sequence.
31577193	9	16	theme	N-glycosylation	1116:1130	arg1	sites					1132:1136	human and mouse N-glycosylation sites	1100:1136	human and mouse N-glycosylation sites	1100:1136	Further, the performance of Nglyc was evaluated using human and mouse N-glycosylation sites.
31577193	14	17	gly	N-glycosylation	1670:1684	arg2	sites					1686:1690	human and mouse N-glycosylation sites	1654:1690	human and mouse N-glycosylation sites	1654:1690	Applicability and success of our method was further evaluated using human and mouse N-glycosylation sites.
31577193	9	18	theme	human	1100:1104	arg1	sites					1132:1136	human and mouse N-glycosylation sites	1100:1136	human and mouse N-glycosylation sites	1100:1136	Further, the performance of Nglyc was evaluated using human and mouse N-glycosylation sites.
31577193	7	19	theme	sites	839:843	arg1	dataset					808:814	a dataset	806:814	a dataset of 600 N-glycosylation sites and 600 non-glycosylation sites	806:875	The method was trained using a dataset of 600 N-glycosylation sites and 600 non-glycosylation sites and tested on the dataset containing 295 Nglycosylation sites and 253 non-glycosylation sites.
31577193	2	20	theme	amino	276:280	arg1	acid					282:285	any amino acid	272:285	any amino acid other than proline	272:304	N-glycosylation predominantly occurs in N-X-[S/T] sequon where X is any amino acid other than proline.
31577193	8	21	dep	NetNGlyc	1007:1014	arg1	methods					1037:1043	methods	1037:1043	methods	1037:1043	Nglyc prediction was compared with NetNGlyc, EnsembleGly and GPP methods.
31577193	1	22	theme	important	149:157	arg1	mechanisms					178:187	the most important post-translational mechanisms	140:187	the most important post-translational mechanisms in eukaryotes	140:201	BACKGROUND: N-Glycosylation is one of the most important post-translational mechanisms in eukaryotes.
31577193	15	23	theme	Nglyc	1693:1697	arg1	method					1699:1704	Nglyc method	1693:1704	Nglyc method	1693:1704	Nglyc method is freely available at https://github.com/bioinformaticsML/ Ngly.
31577193	7	24	gly	N-glycosylation	823:837	arg2	sites					839:843	600 N-glycosylation sites	819:843	600 N-glycosylation sites	819:843	The method was trained using a dataset of 600 N-glycosylation sites and 600 non-glycosylation sites and tested on the dataset containing 295 Nglycosylation sites and 253 non-glycosylation sites.
31577193	7	24	gly	N-glycosylation	823:837	arg2	600					819:821	600	819:821	600	819:821	The method was trained using a dataset of 600 N-glycosylation sites and 600 non-glycosylation sites and tested on the dataset containing 295 Nglycosylation sites and 253 non-glycosylation sites.
31577193	7	25	theme	Nglycosylation	918:931	arg1	sites					933:937	295 Nglycosylation sites	914:937	295 Nglycosylation sites	914:937	The method was trained using a dataset of 600 N-glycosylation sites and 600 non-glycosylation sites and tested on the dataset containing 295 Nglycosylation sites and 253 non-glycosylation sites.
31577193	10	26	theme	overall	1172:1178	arg1	accuracy					1189:1196	an overall training accuracy	1169:1196	an overall training accuracy of 0.8033 with all 315 features	1169:1228	RESULT: Nglyc method achieved an overall training accuracy of 0.8033 with all 315 features.
31577193	9	27	theme	Nglyc	1074:1078	arg1	performance					1059:1069	the performance	1055:1069	the performance of Nglyc	1055:1078	Further, the performance of Nglyc was evaluated using human and mouse N-glycosylation sites.
31577193	1	28	theme	post-translational	159:176	arg1	mechanisms					178:187	the most important post-translational mechanisms	140:187	the most important post-translational mechanisms in eukaryotes	140:201	BACKGROUND: N-Glycosylation is one of the most important post-translational mechanisms in eukaryotes.
31577193	14	29	theme	method	1619:1624	arg1	success					1604:1610	success	1604:1610	success	1604:1610	Applicability and success of our method was further evaluated using human and mouse N-glycosylation sites.
31577193	14	29	theme	method	1619:1624	arg1	Applicability					1586:1598	Applicability	1586:1598	Applicability	1586:1598	Applicability and success of our method was further evaluated using human and mouse N-glycosylation sites.
31577193	3	30	gly	glycosylated	358:369	arg1	sequons					334:340	not all N-X-[S/T] sequons	316:340	not all N-X-[S/T] sequons in proteins	316:352	However, not all N-X-[S/T] sequons in proteins are glycosylated.
31577193	5	31	theme	Nglycosylation	572:585	arg1	sites					587:591	Nglycosylation sites	572:591	Nglycosylation sites	572:591	OBJECTIVE: In this article, our motivation is to develop a computational method to predict Nglycosylation sites in eukaryotic protein sequences.
31577193	13	32	theme	other	1571:1575	arg1	methods					1577:1583	the other methods	1567:1583	the other methods	1567:1583	Comparison study shows that our method performs better than the other methods.
31577193	7	33	theme	N-glycosylation	823:837	arg1	sites					839:843	600 N-glycosylation sites	819:843	600 N-glycosylation sites	819:843	The method was trained using a dataset of 600 N-glycosylation sites and 600 non-glycosylation sites and tested on the dataset containing 295 Nglycosylation sites and 253 non-glycosylation sites.
31577193	1	34	theme	mechanisms	178:187	arg1	mechanisms					178:187	the most important post-translational mechanisms	140:187	the most important post-translational mechanisms in eukaryotes	140:201	BACKGROUND: N-Glycosylation is one of the most important post-translational mechanisms in eukaryotes.
31577193	1	34	theme	mechanisms	178:187	arg1	BACKGROUND					102:111	BACKGROUND	102:111	BACKGROUND: N-Glycosylation is one of the most important post-translational mechanisms in eukaryotes.	102:202	BACKGROUND: N-Glycosylation is one of the most important post-translational mechanisms in eukaryotes.
31577193	1	34	theme	mechanisms	178:187	arg1	one					133:135	one	133:135	one	133:135	BACKGROUND: N-Glycosylation is one of the most important post-translational mechanisms in eukaryotes.
31577193	7	35	contain	containing	903:912	arg2	sites					965:969	253 non-glycosylation sites	943:969	253 non-glycosylation sites	943:969	The method was trained using a dataset of 600 N-glycosylation sites and 600 non-glycosylation sites and tested on the dataset containing 295 Nglycosylation sites and 253 non-glycosylation sites.
31577193	7	35	contain	containing	903:912	arg2	sites					933:937	295 Nglycosylation sites	914:937	295 Nglycosylation sites	914:937	The method was trained using a dataset of 600 N-glycosylation sites and 600 non-glycosylation sites and tested on the dataset containing 295 Nglycosylation sites and 253 non-glycosylation sites.
31577193	7	35	contain	containing	903:912	arg1	dataset					895:901	the dataset	891:901	the dataset containing 295 Nglycosylation sites and 253 non-glycosylation sites	891:969	The method was trained using a dataset of 600 N-glycosylation sites and 600 non-glycosylation sites and tested on the dataset containing 295 Nglycosylation sites and 253 non-glycosylation sites.
31577193	6	36	theme	sequence	758:765	arg1	features					767:774	315 sequence features	754:774	315 sequence features	754:774	METHODS: In this article, we report a random forest method, Nglyc, to predict N-glycosylation site from protein sequence, using 315 sequence features.
31577193	10	37	with	accuracy	1189:1196	arg1	features					1221:1228	all 315 features	1213:1228	all 315 features	1213:1228	RESULT: Nglyc method achieved an overall training accuracy of 0.8033 with all 315 features.
31577193	12	38	theme	overall	1432:1438	arg1	accuracy					1440:1447	an overall accuracy	1429:1447	an overall accuracy of 0.8248 with 0.8305 sensitivity and 0.8182 specificity	1429:1504	CONCLUSION: Our method achieved an overall accuracy of 0.8248 with 0.8305 sensitivity and 0.8182 specificity.
31577193	0	39	theme	Random	9:14	arg1	Method					23:28	A Random Forest Method	7:28	Nglyc: A Random Forest Method for Prediction of N-Glycosylation Sites in Eukaryotic Protein Sequence.	0:100	Nglyc: A Random Forest Method for Prediction of N-Glycosylation Sites in Eukaryotic Protein Sequence.
31577193	5	40	theme	eukaryotic	596:605	arg1	sequences					615:623	eukaryotic protein sequences	596:623	eukaryotic protein sequences	596:623	OBJECTIVE: In this article, our motivation is to develop a computational method to predict Nglycosylation sites in eukaryotic protein sequences.
31577193	12	41	with	accuracy	1440:1447	arg1	sensitivity					1471:1481	0.8305 sensitivity	1464:1481	0.8305 sensitivity	1464:1481	CONCLUSION: Our method achieved an overall accuracy of 0.8248 with 0.8305 sensitivity and 0.8182 specificity.
31577193	12	41	with	accuracy	1440:1447	arg1	specificity					1494:1504	0.8182 specificity	1487:1504	0.8182 specificity	1487:1504	CONCLUSION: Our method achieved an overall accuracy of 0.8248 with 0.8305 sensitivity and 0.8182 specificity.
31577193	11	42	theme	specificity	1379:1389	arg1	rate					1391:1394	specificity rate	1379:1394	specificity rate	1379:1394	Performance comparison with NetNGlyc, EnsembleGly and GPP methods shows that Nglyc performs better than the other methods with high sensitivity and specificity rate.
31577193	6	43	theme	random	664:669	arg1	Nglyc					686:690	Nglyc	686:690	Nglyc	686:690	METHODS: In this article, we report a random forest method, Nglyc, to predict N-glycosylation site from protein sequence, using 315 sequence features.
31577193	6	43	theme	random	664:669	arg1	method					678:683	a random forest method	662:683	a random forest method	662:683	METHODS: In this article, we report a random forest method, Nglyc, to predict N-glycosylation site from protein sequence, using 315 sequence features.
31577193	8	44	theme	Nglyc	972:976	arg1	prediction					978:987	Nglyc prediction	972:987	Nglyc prediction	972:987	Nglyc prediction was compared with NetNGlyc, EnsembleGly and GPP methods.
31577193	3	45	from	sequons	334:340	arg1	proteins					345:352	proteins	345:352	proteins	345:352	However, not all N-X-[S/T] sequons in proteins are glycosylated.
31577193	0	46	theme	Forest	16:21	arg1	Method					23:28	A Random Forest Method	7:28	Nglyc: A Random Forest Method for Prediction of N-Glycosylation Sites in Eukaryotic Protein Sequence.	0:100	Nglyc: A Random Forest Method for Prediction of N-Glycosylation Sites in Eukaryotic Protein Sequence.
31577193	10	47	theme	0.8033	1201:1206	arg1	accuracy					1189:1196	an overall training accuracy	1169:1196	an overall training accuracy of 0.8033 with all 315 features	1169:1228	RESULT: Nglyc method achieved an overall training accuracy of 0.8033 with all 315 features.
31577193	7	48	gly	non-glycosylation	853:869	arg2	600					849:851	600	849:851	600	849:851	The method was trained using a dataset of 600 N-glycosylation sites and 600 non-glycosylation sites and tested on the dataset containing 295 Nglycosylation sites and 253 non-glycosylation sites.
31577193	7	48	gly	non-glycosylation	853:869	arg2	sites					871:875	600 non-glycosylation sites	849:875	600 non-glycosylation sites	849:875	The method was trained using a dataset of 600 N-glycosylation sites and 600 non-glycosylation sites and tested on the dataset containing 295 Nglycosylation sites and 253 non-glycosylation sites.
31577193	2	49	theme	N-X-[S/T	244:251	arg1	sequon					254:259	N-X-[S/T] sequon	244:259	N-X-[S/T] sequon where X is any amino acid other than proline	244:304	N-glycosylation predominantly occurs in N-X-[S/T] sequon where X is any amino acid other than proline.
31577193	9	50	theme	mouse	1110:1114	arg1	sites					1132:1136	human and mouse N-glycosylation sites	1100:1136	human and mouse N-glycosylation sites	1100:1136	Further, the performance of Nglyc was evaluated using human and mouse N-glycosylation sites.
31577193	15	51	from	Ngly	1766:1769	arg1	available					1716:1724	available	1716:1724	available	1716:1724	Nglyc method is freely available at https://github.com/bioinformaticsML/ Ngly.
31577193	11	52	theme	other	1339:1343	arg1	methods					1345:1351	the other methods	1335:1351	the other methods	1335:1351	Performance comparison with NetNGlyc, EnsembleGly and GPP methods shows that Nglyc performs better than the other methods with high sensitivity and specificity rate.
31577193	10	53	theme	Nglyc	1147:1151	arg1	method					1153:1158	Nglyc method	1147:1158	RESULT: Nglyc method	1139:1158	RESULT: Nglyc method achieved an overall training accuracy of 0.8033 with all 315 features.
31577193	4	54	theme	Nglycosylation	455:468	arg1	mechanism					470:478	Nglycosylation mechanism	455:478	Nglycosylation mechanism	455:478	Therefore, accurate prediction of N-glycosylation sites is essential to understand Nglycosylation mechanism.
31577193	5	55	theme	computational	540:552	arg1	method					554:559	a computational method	538:559	a computational method to predict Nglycosylation sites in eukaryotic protein sequences	538:623	OBJECTIVE: In this article, our motivation is to develop a computational method to predict Nglycosylation sites in eukaryotic protein sequences.
31577193	6	56	from	sequence	738:745	arg1	site					720:723	N-glycosylation site	704:723	N-glycosylation site from protein sequence	704:745	METHODS: In this article, we report a random forest method, Nglyc, to predict N-glycosylation site from protein sequence, using 315 sequence features.
31577193	14	57	theme	mouse	1664:1668	arg1	sites					1686:1690	human and mouse N-glycosylation sites	1654:1690	human and mouse N-glycosylation sites	1654:1690	Applicability and success of our method was further evaluated using human and mouse N-glycosylation sites.
31577193	4	58	theme	sites	422:426	arg1	prediction					392:401	accurate prediction	383:401	accurate prediction of N-glycosylation sites	383:426	Therefore, accurate prediction of N-glycosylation sites is essential to understand Nglycosylation mechanism.
31577193	12	59	theme	0.8305	1464:1469	arg1	sensitivity					1471:1481	0.8305 sensitivity	1464:1481	0.8305 sensitivity	1464:1481	CONCLUSION: Our method achieved an overall accuracy of 0.8248 with 0.8305 sensitivity and 0.8182 specificity.
31577193	11	60	dep	EnsembleGly	1269:1279	arg1	methods					1289:1295	methods	1289:1295	methods	1289:1295	Performance comparison with NetNGlyc, EnsembleGly and GPP methods shows that Nglyc performs better than the other methods with high sensitivity and specificity rate.
31577193	2	61	gly	N-glycosylation	204:218	arg2	sequon					254:259	N-X-[S/T] sequon	244:259	N-X-[S/T] sequon where X is any amino acid other than proline	244:304	N-glycosylation predominantly occurs in N-X-[S/T] sequon where X is any amino acid other than proline.
31577193	11	62	theme	Performance	1231:1241	arg1	comparison					1243:1252	Performance comparison	1231:1252	Performance comparison with NetNGlyc, EnsembleGly and GPP methods	1231:1295	Performance comparison with NetNGlyc, EnsembleGly and GPP methods shows that Nglyc performs better than the other methods with high sensitivity and specificity rate.
31577193	4	63	theme	N-glycosylation	406:420	arg1	sites					422:426	N-glycosylation sites	406:426	N-glycosylation sites	406:426	Therefore, accurate prediction of N-glycosylation sites is essential to understand Nglycosylation mechanism.
31577193	6	64	theme	protein	730:736	arg1	sequence					738:745	protein sequence	730:745	protein sequence	730:745	METHODS: In this article, we report a random forest method, Nglyc, to predict N-glycosylation site from protein sequence, using 315 sequence features.
31577193	10	65	theme	training	1180:1187	arg1	accuracy					1189:1196	an overall training accuracy	1169:1196	an overall training accuracy of 0.8033 with all 315 features	1169:1228	RESULT: Nglyc method achieved an overall training accuracy of 0.8033 with all 315 features.
31577193	12	66	theme	0.8182	1487:1492	arg1	specificity					1494:1504	0.8182 specificity	1487:1504	0.8182 specificity	1487:1504	CONCLUSION: Our method achieved an overall accuracy of 0.8248 with 0.8305 sensitivity and 0.8182 specificity.
31577193	1	67	from	mechanisms	178:187	arg1	eukaryotes					192:201	eukaryotes	192:201	eukaryotes	192:201	BACKGROUND: N-Glycosylation is one of the most important post-translational mechanisms in eukaryotes.
31577193	6	68	theme	forest	671:676	arg1	Nglyc					686:690	Nglyc	686:690	Nglyc	686:690	METHODS: In this article, we report a random forest method, Nglyc, to predict N-glycosylation site from protein sequence, using 315 sequence features.
31577193	6	68	theme	forest	671:676	arg1	method					678:683	a random forest method	662:683	a random forest method	662:683	METHODS: In this article, we report a random forest method, Nglyc, to predict N-glycosylation site from protein sequence, using 315 sequence features.
31577193	7	69	gly	Nglycosylation	918:931	arg2	sites					933:937	295 Nglycosylation sites	914:937	295 Nglycosylation sites	914:937	The method was trained using a dataset of 600 N-glycosylation sites and 600 non-glycosylation sites and tested on the dataset containing 295 Nglycosylation sites and 253 non-glycosylation sites.
31577193	7	69	gly	Nglycosylation	918:931	arg2	295					914:916	295	914:916	295	914:916	The method was trained using a dataset of 600 N-glycosylation sites and 600 non-glycosylation sites and tested on the dataset containing 295 Nglycosylation sites and 253 non-glycosylation sites.
31577193	0	70	theme	N-Glycosylation	48:62	arg1	Sites					64:68	N-Glycosylation Sites	48:68	N-Glycosylation Sites	48:68	Nglyc: A Random Forest Method for Prediction of N-Glycosylation Sites in Eukaryotic Protein Sequence.
31577193	14	71	theme	N-glycosylation	1670:1684	arg1	sites					1686:1690	human and mouse N-glycosylation sites	1654:1690	human and mouse N-glycosylation sites	1654:1690	Applicability and success of our method was further evaluated using human and mouse N-glycosylation sites.
31577193	7	72	theme	sites	871:875	arg1	dataset					808:814	a dataset	806:814	a dataset of 600 N-glycosylation sites and 600 non-glycosylation sites	806:875	The method was trained using a dataset of 600 N-glycosylation sites and 600 non-glycosylation sites and tested on the dataset containing 295 Nglycosylation sites and 253 non-glycosylation sites.
31577193	7	73	theme	non-glycosylation	947:963	arg1	sites					965:969	253 non-glycosylation sites	943:969	253 non-glycosylation sites	943:969	The method was trained using a dataset of 600 N-glycosylation sites and 600 non-glycosylation sites and tested on the dataset containing 295 Nglycosylation sites and 253 non-glycosylation sites.
31577193	11	74	with	comparison	1243:1252	arg1	GPP					1285:1287	GPP	1285:1287	GPP	1285:1287	Performance comparison with NetNGlyc, EnsembleGly and GPP methods shows that Nglyc performs better than the other methods with high sensitivity and specificity rate.
31577193	11	74	with	comparison	1243:1252	arg1	EnsembleGly					1269:1279	EnsembleGly	1269:1279	EnsembleGly	1269:1279	Performance comparison with NetNGlyc, EnsembleGly and GPP methods shows that Nglyc performs better than the other methods with high sensitivity and specificity rate.
31577193	15	75	theme	https	1729:1733	arg1	Ngly					1766:1769	https://github.com/bioinformaticsML/ Ngly	1729:1769	https://github.com/bioinformaticsML/ Ngly	1729:1769	Nglyc method is freely available at https://github.com/bioinformaticsML/ Ngly.
31577193	3	76	theme	N-X-[S/T	324:331	arg1	sequons					334:340	not all N-X-[S/T] sequons	316:340	not all N-X-[S/T] sequons in proteins	316:352	However, not all N-X-[S/T] sequons in proteins are glycosylated.
31577193	11	77	theme	high	1358:1361	arg1	sensitivity					1363:1373	high sensitivity	1358:1373	high sensitivity	1358:1373	Performance comparison with NetNGlyc, EnsembleGly and GPP methods shows that Nglyc performs better than the other methods with high sensitivity and specificity rate.
31577193	0	78	dep	Nglyc	0:4	arg1	Method					23:28	A Random Forest Method	7:28	Nglyc: A Random Forest Method for Prediction of N-Glycosylation Sites in Eukaryotic Protein Sequence.	0:100	Nglyc: A Random Forest Method for Prediction of N-Glycosylation Sites in Eukaryotic Protein Sequence.
31577193	6	79	theme	N-glycosylation	704:718	arg1	site					720:723	N-glycosylation site	704:723	N-glycosylation site from protein sequence	704:745	METHODS: In this article, we report a random forest method, Nglyc, to predict N-glycosylation site from protein sequence, using 315 sequence features.
31577193	4	80	gly	N-glycosylation	406:420	arg2	sites					422:426	N-glycosylation sites	406:426	N-glycosylation sites	406:426	Therefore, accurate prediction of N-glycosylation sites is essential to understand Nglycosylation mechanism.
31577193	6	81	gly	N-glycosylation	704:718	arg2	site					720:723	N-glycosylation site	704:723	N-glycosylation site from protein sequence	704:745	METHODS: In this article, we report a random forest method, Nglyc, to predict N-glycosylation site from protein sequence, using 315 sequence features.
31958346	10	0	theme	N401	1550:1553	arg1	occupancy					1555:1563	N401 occupancy	1550:1563	N401 occupancy	1550:1563	To examine the involvement of Bip in N401-glycosylation, the effect of Bip over-expression on N401 occupancy was evaluated in HEK293T cells, and the results demonstrated Bip increases the N401 glycan-free form by mediating selective prolongation of its protein half-life.
31958346	2	1	theme	GluA1	415:419	arg1	analysis					397:404	a comprehensive N-glycosylation analysis	365:404	a comprehensive N-glycosylation analysis of mouse GluA1, one of the major subunits of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor, which possesses six potential N-glycosylation sites in the N-terminal domain	365:601	In this study, we performed a comprehensive N-glycosylation analysis of mouse GluA1, one of the major subunits of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor, which possesses six potential N-glycosylation sites in the N-terminal domain.
31958346	1	2	theme	neuronal	316:323	arg1	physiology					325:334	neuronal physiology	316:334	neuronal physiology	316:334	In the mammalian nervous system, protein N-glycosylation plays an important role in neuronal physiology.
31958346	9	3	theme	molecular	1360:1368	arg1	chaperone					1370:1378	a molecular chaperone	1358:1378	a molecular chaperone that plays a key role in protein folding in the ER (endoplasmic reticulum)	1358:1453	Bip has been known as a molecular chaperone that plays a key role in protein folding in the ER (endoplasmic reticulum).
31958346	9	3	theme	molecular	1360:1368	arg1	Bip					1336:1338	Bip	1336:1338	Bip	1336:1338	Bip has been known as a molecular chaperone that plays a key role in protein folding in the ER (endoplasmic reticulum).
31958346	10	4	theme	half-life	1717:1725	arg1	prolongation					1689:1700	selective prolongation	1679:1700	selective prolongation of its protein half-life	1679:1725	To examine the involvement of Bip in N401-glycosylation, the effect of Bip over-expression on N401 occupancy was evaluated in HEK293T cells, and the results demonstrated Bip increases the N401 glycan-free form by mediating selective prolongation of its protein half-life.
31958346	11	5	from	function	2003:2010	arg1	brain					2019:2023	the brain	2015:2023	the brain	2015:2023	Taken together, we propose that the N401-glycosite of GluA1 receives a unique control of modification, and we also propose a novel N-glycosylation occupancy regulatory mechanism by Bip that might be associated with α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate receptors function in the brain.
31958346	4	6	theme	incomplete	819:828	arg1	occupancy					846:854	incomplete N-glycosylation occupancy	819:854	incomplete N-glycosylation occupancy	819:854	In addition, only the N401-glycosylation site demonstrated incomplete N-glycosylation occupancy.
31958346	1	7	theme	nervous	249:255	arg1	system					257:262	the mammalian nervous system	235:262	the mammalian nervous system	235:262	In the mammalian nervous system, protein N-glycosylation plays an important role in neuronal physiology.
31958346	3	8	gly	occupancy	740:748	arg2	GluA1					753:757	GluA1	753:757	GluA1	753:757	By mass spectrometry-based analysis, we identified the N-glycoforms and semiquantitatively determined the site-specific N-glycosylation occupancy of GluA1.
31958346	11	9	theme	α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate	1943:1991	arg1	function					2003:2010	α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate receptors function	1943:2010	α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate receptors function in the brain	1943:2023	Taken together, we propose that the N401-glycosite of GluA1 receives a unique control of modification, and we also propose a novel N-glycosylation occupancy regulatory mechanism by Bip that might be associated with α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate receptors function in the brain.
31958346	0	10	theme	N-glycosylation	173:187	arg1	occupancy					189:197	N-glycosylation occupancy	173:197	N-glycosylation occupancy by molecular chaperones in mice	173:229	Monitoring the glycosylation of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate-type glutamate receptors using specific antibodies reveals a novel regulatory mechanism of N-glycosylation occupancy by molecular chaperones in mice.
31958346	3	11	theme	mass	607:610	arg1	analysis					631:638	mass spectrometry-based analysis	607:638	mass spectrometry-based analysis	607:638	By mass spectrometry-based analysis, we identified the N-glycoforms and semiquantitatively determined the site-specific N-glycosylation occupancy of GluA1.
31958346	9	12	theme	protein	1405:1411	arg1	folding					1413:1419	protein folding	1405:1419	protein folding in the ER (endoplasmic reticulum)	1405:1453	Bip has been known as a molecular chaperone that plays a key role in protein folding in the ER (endoplasmic reticulum).
31958346	6	13	theme	mouse	1128:1132	arg1	forebrains					1134:1143	mouse forebrains	1128:1143	mouse forebrains	1128:1143	Using this antibody, we clarified that N401 occupancy varies between cell types and increases in an age-dependent manner in mouse forebrains.
31958346	7	14	theme	N401	1242:1245	arg1	site					1247:1250	the N401 site	1238:1250	the N401 site	1238:1250	To address the regulatory mechanism of N401-glycosylation, binding proteins of GluA1 around the N401 site were screened.
31958346	3	15	theme	site-specific	710:722	arg1	occupancy					740:748	the site-specific N-glycosylation occupancy	706:748	the site-specific N-glycosylation occupancy of GluA1	706:757	By mass spectrometry-based analysis, we identified the N-glycoforms and semiquantitatively determined the site-specific N-glycosylation occupancy of GluA1.
31958346	10	16	from	involvement	1471:1481	arg1	N401-glycosylation					1493:1510	N401-glycosylation	1493:1510	N401-glycosylation	1493:1510	To examine the involvement of Bip in N401-glycosylation, the effect of Bip over-expression on N401 occupancy was evaluated in HEK293T cells, and the results demonstrated Bip increases the N401 glycan-free form by mediating selective prolongation of its protein half-life.
31958346	0	17	theme	specific	113:120	arg1	antibodies					122:131	specific antibodies	113:131	specific antibodies	113:131	Monitoring the glycosylation of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate-type glutamate receptors using specific antibodies reveals a novel regulatory mechanism of N-glycosylation occupancy by molecular chaperones in mice.
31958346	9	18	theme	endoplasmic	1432:1442	arg1	ER					1428:1429	the ER	1424:1429	the ER (endoplasmic reticulum)	1424:1453	Bip has been known as a molecular chaperone that plays a key role in protein folding in the ER (endoplasmic reticulum).
31958346	9	18	theme	endoplasmic	1432:1442	arg1	reticulum					1444:1452	endoplasmic reticulum	1432:1452	endoplasmic reticulum	1432:1452	Bip has been known as a molecular chaperone that plays a key role in protein folding in the ER (endoplasmic reticulum).
31958346	3	19	theme	GluA1	753:757	arg1	occupancy					740:748	the site-specific N-glycosylation occupancy	706:748	the site-specific N-glycosylation occupancy of GluA1	706:757	By mass spectrometry-based analysis, we identified the N-glycoforms and semiquantitatively determined the site-specific N-glycosylation occupancy of GluA1.
31958346	7	20	theme	regulatory	1161:1170	arg1	mechanism					1172:1180	the regulatory mechanism	1157:1180	the regulatory mechanism of N401-glycosylation	1157:1202	To address the regulatory mechanism of N401-glycosylation, binding proteins of GluA1 around the N401 site were screened.
31958346	2	21	theme	N-terminal	585:594	arg1	domain					596:601	the N-terminal domain	581:601	the N-terminal domain	581:601	In this study, we performed a comprehensive N-glycosylation analysis of mouse GluA1, one of the major subunits of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor, which possesses six potential N-glycosylation sites in the N-terminal domain.
31958346	2	22	contain	possesses	532:540	arg2	sites					572:576	six potential N-glycosylation sites	542:576	six potential N-glycosylation sites in the N-terminal domain	542:601	In this study, we performed a comprehensive N-glycosylation analysis of mouse GluA1, one of the major subunits of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor, which possesses six potential N-glycosylation sites in the N-terminal domain.
31958346	2	22	contain	possesses	532:540	arg1	receptor					516:523	α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor	451:523	α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor	451:523	In this study, we performed a comprehensive N-glycosylation analysis of mouse GluA1, one of the major subunits of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor, which possesses six potential N-glycosylation sites in the N-terminal domain.
31958346	0	23	theme	novel	143:147	arg1	mechanism					160:168	a novel regulatory mechanism	141:168	a novel regulatory mechanism of N-glycosylation occupancy by molecular chaperones in mice	141:229	Monitoring the glycosylation of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate-type glutamate receptors using specific antibodies reveals a novel regulatory mechanism of N-glycosylation occupancy by molecular chaperones in mice.
31958346	2	24	from	sites	572:576	arg1	domain					596:601	the N-terminal domain	581:601	the N-terminal domain	581:601	In this study, we performed a comprehensive N-glycosylation analysis of mouse GluA1, one of the major subunits of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor, which possesses six potential N-glycosylation sites in the N-terminal domain.
31958346	2	25	theme	major	433:437	arg1	subunits					439:446	the major subunits	429:446	the major subunits of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor, which possesses six potential N-glycosylation sites in the N-terminal domain	429:601	In this study, we performed a comprehensive N-glycosylation analysis of mouse GluA1, one of the major subunits of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor, which possesses six potential N-glycosylation sites in the N-terminal domain.
31958346	10	26	theme	glycan-free	1649:1659	arg1	form					1661:1664	the N401 glycan-free form	1640:1664	the N401 glycan-free form	1640:1664	To examine the involvement of Bip in N401-glycosylation, the effect of Bip over-expression on N401 occupancy was evaluated in HEK293T cells, and the results demonstrated Bip increases the N401 glycan-free form by mediating selective prolongation of its protein half-life.
31958346	2	27	theme	receptor	516:523	arg1	subunits					439:446	the major subunits	429:446	the major subunits of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor, which possesses six potential N-glycosylation sites in the N-terminal domain	429:601	In this study, we performed a comprehensive N-glycosylation analysis of mouse GluA1, one of the major subunits of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor, which possesses six potential N-glycosylation sites in the N-terminal domain.
31958346	8	28	theme	HSP70	1267:1271	arg1	proteins					1280:1287	HSP70 family proteins	1267:1287	HSP70 family proteins	1267:1287	HSP70 family proteins, including Bip, were identified as candidates.
31958346	8	28	theme	HSP70	1267:1271	arg1	candidates					1324:1333	candidates	1324:1333	candidates	1324:1333	HSP70 family proteins, including Bip, were identified as candidates.
31958346	8	28	theme	HSP70	1267:1271	arg1	Bip					1300:1302	Bip	1300:1302	Bip	1300:1302	HSP70 family proteins, including Bip, were identified as candidates.
31958346	2	29	theme	type	501:504	arg1	receptor					516:523	α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor	451:523	α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor	451:523	In this study, we performed a comprehensive N-glycosylation analysis of mouse GluA1, one of the major subunits of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor, which possesses six potential N-glycosylation sites in the N-terminal domain.
31958346	0	30	theme	α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate-type	32:85	arg1	receptors					97:105	α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate-type glutamate receptors	32:105	α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate-type glutamate receptors using specific antibodies	32:131	Monitoring the glycosylation of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate-type glutamate receptors using specific antibodies reveals a novel regulatory mechanism of N-glycosylation occupancy by molecular chaperones in mice.
31958346	6	31	theme	N401	1043:1046	arg1	occupancy					1048:1056	N401 occupancy	1043:1056	N401 occupancy	1043:1056	Using this antibody, we clarified that N401 occupancy varies between cell types and increases in an age-dependent manner in mouse forebrains.
31958346	10	32	from	effect	1517:1522	arg1	occupancy					1555:1563	N401 occupancy	1550:1563	N401 occupancy	1550:1563	To examine the involvement of Bip in N401-glycosylation, the effect of Bip over-expression on N401 occupancy was evaluated in HEK293T cells, and the results demonstrated Bip increases the N401 glycan-free form by mediating selective prolongation of its protein half-life.
31958346	2	33	theme	N-glycosylation	556:570	arg1	sites					572:576	six potential N-glycosylation sites	542:576	six potential N-glycosylation sites in the N-terminal domain	542:601	In this study, we performed a comprehensive N-glycosylation analysis of mouse GluA1, one of the major subunits of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor, which possesses six potential N-glycosylation sites in the N-terminal domain.
31958346	10	34	theme	selective	1679:1687	arg1	prolongation					1689:1700	selective prolongation	1679:1700	selective prolongation of its protein half-life	1679:1725	To examine the involvement of Bip in N401-glycosylation, the effect of Bip over-expression on N401 occupancy was evaluated in HEK293T cells, and the results demonstrated Bip increases the N401 glycan-free form by mediating selective prolongation of its protein half-life.
31958346	2	35	theme	mouse	409:413	arg1	subunits					439:446	the major subunits	429:446	the major subunits of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor, which possesses six potential N-glycosylation sites in the N-terminal domain	429:601	In this study, we performed a comprehensive N-glycosylation analysis of mouse GluA1, one of the major subunits of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor, which possesses six potential N-glycosylation sites in the N-terminal domain.
31958346	2	35	theme	mouse	409:413	arg1	one					422:424	one	422:424	one	422:424	In this study, we performed a comprehensive N-glycosylation analysis of mouse GluA1, one of the major subunits of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor, which possesses six potential N-glycosylation sites in the N-terminal domain.
31958346	2	35	theme	mouse	409:413	arg1	GluA1					415:419	mouse GluA1	409:419	mouse GluA1	409:419	In this study, we performed a comprehensive N-glycosylation analysis of mouse GluA1, one of the major subunits of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor, which possesses six potential N-glycosylation sites in the N-terminal domain.
31958346	5	36	theme	N401-glycosylation	974:991	arg1	occupancy					993:1001	N401-glycosylation occupancy	974:1001	N401-glycosylation occupancy	974:1001	Therefore, we generated a peptide antibody that specifically detects the N401-glycan-free form to precisely quantify N401-glycosylation occupancy.
31958346	2	37	gly	N-glycosylation	556:570	arg2	sites					572:576	six potential N-glycosylation sites	542:576	six potential N-glycosylation sites in the N-terminal domain	542:601	In this study, we performed a comprehensive N-glycosylation analysis of mouse GluA1, one of the major subunits of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor, which possesses six potential N-glycosylation sites in the N-terminal domain.
31958346	2	37	gly	N-glycosylation	556:570	arg2	six					542:544	six	542:544	six	542:544	In this study, we performed a comprehensive N-glycosylation analysis of mouse GluA1, one of the major subunits of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor, which possesses six potential N-glycosylation sites in the N-terminal domain.
31958346	2	38	gly	N-glycosylation	381:395	arg1	subunits					439:446	the major subunits	429:446	the major subunits of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor, which possesses six potential N-glycosylation sites in the N-terminal domain	429:601	In this study, we performed a comprehensive N-glycosylation analysis of mouse GluA1, one of the major subunits of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor, which possesses six potential N-glycosylation sites in the N-terminal domain.
31958346	2	38	gly	N-glycosylation	381:395	arg1	one					422:424	one	422:424	one	422:424	In this study, we performed a comprehensive N-glycosylation analysis of mouse GluA1, one of the major subunits of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor, which possesses six potential N-glycosylation sites in the N-terminal domain.
31958346	2	38	gly	N-glycosylation	381:395	arg1	GluA1					415:419	mouse GluA1	409:419	mouse GluA1	409:419	In this study, we performed a comprehensive N-glycosylation analysis of mouse GluA1, one of the major subunits of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor, which possesses six potential N-glycosylation sites in the N-terminal domain.
31958346	11	39	theme	regulatory	1885:1894	arg1	mechanism					1896:1904	a novel N-glycosylation occupancy regulatory mechanism	1851:1904	a novel N-glycosylation occupancy regulatory mechanism by Bip that might be associated with α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate receptors function in the brain	1851:2023	Taken together, we propose that the N401-glycosite of GluA1 receives a unique control of modification, and we also propose a novel N-glycosylation occupancy regulatory mechanism by Bip that might be associated with α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate receptors function in the brain.
31958346	10	40	theme	protein	1709:1715	arg1	half-life					1717:1725	its protein half-life	1705:1725	its protein half-life	1705:1725	To examine the involvement of Bip in N401-glycosylation, the effect of Bip over-expression on N401 occupancy was evaluated in HEK293T cells, and the results demonstrated Bip increases the N401 glycan-free form by mediating selective prolongation of its protein half-life.
31958346	11	41	theme	N-glycosylation	1859:1873	arg1	mechanism					1896:1904	a novel N-glycosylation occupancy regulatory mechanism	1851:1904	a novel N-glycosylation occupancy regulatory mechanism by Bip that might be associated with α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate receptors function in the brain	1851:2023	Taken together, we propose that the N401-glycosite of GluA1 receives a unique control of modification, and we also propose a novel N-glycosylation occupancy regulatory mechanism by Bip that might be associated with α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate receptors function in the brain.
31958346	11	42	theme	GluA1	1782:1786	arg1	N401-glycosite					1764:1777	the N401-glycosite	1760:1777	the N401-glycosite of GluA1	1760:1786	Taken together, we propose that the N401-glycosite of GluA1 receives a unique control of modification, and we also propose a novel N-glycosylation occupancy regulatory mechanism by Bip that might be associated with α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate receptors function in the brain.
31958346	11	42	theme	GluA1	1782:1786	arg1	GluA1					1782:1786	GluA1	1782:1786	GluA1	1782:1786	Taken together, we propose that the N401-glycosite of GluA1 receives a unique control of modification, and we also propose a novel N-glycosylation occupancy regulatory mechanism by Bip that might be associated with α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate receptors function in the brain.
31958346	3	43	theme	spectrometry-based	612:629	arg1	analysis					631:638	mass spectrometry-based analysis	607:638	mass spectrometry-based analysis	607:638	By mass spectrometry-based analysis, we identified the N-glycoforms and semiquantitatively determined the site-specific N-glycosylation occupancy of GluA1.
31958346	1	44	theme	important	298:306	arg1	role					308:311	an important role	295:311	an important role	295:311	In the mammalian nervous system, protein N-glycosylation plays an important role in neuronal physiology.
31958346	6	45	theme	age-dependent	1104:1116	arg1	manner					1118:1123	an age-dependent manner	1101:1123	an age-dependent manner in mouse forebrains	1101:1143	Using this antibody, we clarified that N401 occupancy varies between cell types and increases in an age-dependent manner in mouse forebrains.
31958346	4	46	gly	N401-glycosylation	782:799	arg2	site					801:804	only the N401-glycosylation site	773:804	only the N401-glycosylation site	773:804	In addition, only the N401-glycosylation site demonstrated incomplete N-glycosylation occupancy.
31958346	9	47	from	folding	1413:1419	arg1	ER					1428:1429	the ER	1424:1429	the ER (endoplasmic reticulum)	1424:1453	Bip has been known as a molecular chaperone that plays a key role in protein folding in the ER (endoplasmic reticulum).
31958346	9	47	from	folding	1413:1419	arg1	reticulum					1444:1452	endoplasmic reticulum	1432:1452	endoplasmic reticulum	1432:1452	Bip has been known as a molecular chaperone that plays a key role in protein folding in the ER (endoplasmic reticulum).
31958346	0	48	from	chaperones	212:221	arg1	mice					226:229	mice	226:229	mice	226:229	Monitoring the glycosylation of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate-type glutamate receptors using specific antibodies reveals a novel regulatory mechanism of N-glycosylation occupancy by molecular chaperones in mice.
31958346	10	49	theme	Bip	1527:1529	arg1	over-expression					1531:1545	Bip over-expression	1527:1545	Bip over-expression	1527:1545	To examine the involvement of Bip in N401-glycosylation, the effect of Bip over-expression on N401 occupancy was evaluated in HEK293T cells, and the results demonstrated Bip increases the N401 glycan-free form by mediating selective prolongation of its protein half-life.
31958346	0	50	theme	receptors	97:105	arg1	glycosylation					15:27	the glycosylation	11:27	the glycosylation of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate-type glutamate receptors using specific antibodies	11:131	Monitoring the glycosylation of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate-type glutamate receptors using specific antibodies reveals a novel regulatory mechanism of N-glycosylation occupancy by molecular chaperones in mice.
31958346	6	51	theme	cell	1073:1076	arg1	types					1078:1082	cell types	1073:1082	cell types	1073:1082	Using this antibody, we clarified that N401 occupancy varies between cell types and increases in an age-dependent manner in mouse forebrains.
31958346	4	52	theme	N401-glycosylation	782:799	arg1	site					801:804	only the N401-glycosylation site	773:804	only the N401-glycosylation site	773:804	In addition, only the N401-glycosylation site demonstrated incomplete N-glycosylation occupancy.
31958346	11	53	theme	modification	1817:1828	arg1	control					1806:1812	a unique control	1797:1812	a unique control of modification	1797:1828	Taken together, we propose that the N401-glycosite of GluA1 receives a unique control of modification, and we also propose a novel N-glycosylation occupancy regulatory mechanism by Bip that might be associated with α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate receptors function in the brain.
31958346	2	54	theme	comprehensive	367:379	arg1	analysis					397:404	a comprehensive N-glycosylation analysis	365:404	a comprehensive N-glycosylation analysis of mouse GluA1, one of the major subunits of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor, which possesses six potential N-glycosylation sites in the N-terminal domain	365:601	In this study, we performed a comprehensive N-glycosylation analysis of mouse GluA1, one of the major subunits of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor, which possesses six potential N-glycosylation sites in the N-terminal domain.
31958346	1	55	theme	mammalian	239:247	arg1	system					257:262	the mammalian nervous system	235:262	the mammalian nervous system	235:262	In the mammalian nervous system, protein N-glycosylation plays an important role in neuronal physiology.
31958346	0	56	theme	occupancy	189:197	arg1	mechanism					160:168	a novel regulatory mechanism	141:168	a novel regulatory mechanism of N-glycosylation occupancy by molecular chaperones in mice	141:229	Monitoring the glycosylation of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate-type glutamate receptors using specific antibodies reveals a novel regulatory mechanism of N-glycosylation occupancy by molecular chaperones in mice.
31958346	9	57	theme	key	1393:1395	arg1	role					1397:1400	a key role	1391:1400	a key role	1391:1400	Bip has been known as a molecular chaperone that plays a key role in protein folding in the ER (endoplasmic reticulum).
31958346	11	58	theme	receptors	1993:2001	arg1	function					2003:2010	α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate receptors function	1943:2010	α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate receptors function in the brain	1943:2023	Taken together, we propose that the N401-glycosite of GluA1 receives a unique control of modification, and we also propose a novel N-glycosylation occupancy regulatory mechanism by Bip that might be associated with α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate receptors function in the brain.
31958346	0	59	theme	molecular	202:210	arg1	chaperones					212:221	molecular chaperones	202:221	molecular chaperones in mice	202:229	Monitoring the glycosylation of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate-type glutamate receptors using specific antibodies reveals a novel regulatory mechanism of N-glycosylation occupancy by molecular chaperones in mice.
31958346	3	60	theme	N-glycosylation	724:738	arg1	occupancy					740:748	the site-specific N-glycosylation occupancy	706:748	the site-specific N-glycosylation occupancy of GluA1	706:757	By mass spectrometry-based analysis, we identified the N-glycoforms and semiquantitatively determined the site-specific N-glycosylation occupancy of GluA1.
31958346	1	61	theme	protein	265:271	arg1	N-glycosylation					273:287	protein N-glycosylation	265:287	protein N-glycosylation	265:287	In the mammalian nervous system, protein N-glycosylation plays an important role in neuronal physiology.
31958346	5	62	theme	peptide	883:889	arg1	antibody					891:898	a peptide antibody	881:898	a peptide antibody that specifically detects the N401-glycan-free form to precisely quantify N401-glycosylation occupancy	881:1001	Therefore, we generated a peptide antibody that specifically detects the N401-glycan-free form to precisely quantify N401-glycosylation occupancy.
31958346	7	63	theme	GluA1	1225:1229	arg1	proteins					1213:1220	binding proteins	1205:1220	binding proteins of GluA1 around the N401 site	1205:1250	To address the regulatory mechanism of N401-glycosylation, binding proteins of GluA1 around the N401 site were screened.
31958346	7	64	theme	binding	1205:1211	arg1	proteins					1213:1220	binding proteins	1205:1220	binding proteins of GluA1 around the N401 site	1205:1250	To address the regulatory mechanism of N401-glycosylation, binding proteins of GluA1 around the N401 site were screened.
31958346	7	65	theme	N401-glycosylation	1185:1202	arg1	mechanism					1172:1180	the regulatory mechanism	1157:1180	the regulatory mechanism of N401-glycosylation	1157:1202	To address the regulatory mechanism of N401-glycosylation, binding proteins of GluA1 around the N401 site were screened.
31958346	4	66	theme	N-glycosylation	830:844	arg1	occupancy					846:854	incomplete N-glycosylation occupancy	819:854	incomplete N-glycosylation occupancy	819:854	In addition, only the N401-glycosylation site demonstrated incomplete N-glycosylation occupancy.
31958346	5	67	theme	N401-glycan-free	930:945	arg1	form					947:950	the N401-glycan-free form	926:950	the N401-glycan-free form to precisely quantify N401-glycosylation occupancy	926:1001	Therefore, we generated a peptide antibody that specifically detects the N401-glycan-free form to precisely quantify N401-glycosylation occupancy.
31958346	0	68	theme	regulatory	149:158	arg1	mechanism					160:168	a novel regulatory mechanism	141:168	a novel regulatory mechanism of N-glycosylation occupancy by molecular chaperones in mice	141:229	Monitoring the glycosylation of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate-type glutamate receptors using specific antibodies reveals a novel regulatory mechanism of N-glycosylation occupancy by molecular chaperones in mice.
31958346	10	69	theme	HEK293T	1582:1588	arg1	cells					1590:1594	HEK293T cells	1582:1594	HEK293T cells	1582:1594	To examine the involvement of Bip in N401-glycosylation, the effect of Bip over-expression on N401 occupancy was evaluated in HEK293T cells, and the results demonstrated Bip increases the N401 glycan-free form by mediating selective prolongation of its protein half-life.
31958346	2	70	theme	subunits	439:446	arg1	subunits					439:446	the major subunits	429:446	the major subunits of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor, which possesses six potential N-glycosylation sites in the N-terminal domain	429:601	In this study, we performed a comprehensive N-glycosylation analysis of mouse GluA1, one of the major subunits of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor, which possesses six potential N-glycosylation sites in the N-terminal domain.
31958346	2	70	theme	subunits	439:446	arg1	one					422:424	one	422:424	one	422:424	In this study, we performed a comprehensive N-glycosylation analysis of mouse GluA1, one of the major subunits of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor, which possesses six potential N-glycosylation sites in the N-terminal domain.
31958346	2	70	theme	subunits	439:446	arg1	GluA1					415:419	mouse GluA1	409:419	mouse GluA1	409:419	In this study, we performed a comprehensive N-glycosylation analysis of mouse GluA1, one of the major subunits of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor, which possesses six potential N-glycosylation sites in the N-terminal domain.
31958346	11	71	gly	N401-glycosite	1764:1777	arg2	GluA1					1782:1786	GluA1	1782:1786	GluA1	1782:1786	Taken together, we propose that the N401-glycosite of GluA1 receives a unique control of modification, and we also propose a novel N-glycosylation occupancy regulatory mechanism by Bip that might be associated with α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate receptors function in the brain.
31958346	11	71	gly	N401-glycosite	1764:1777	arg2	N401-glycosite					1764:1777	the N401-glycosite	1760:1777	the N401-glycosite of GluA1	1760:1786	Taken together, we propose that the N401-glycosite of GluA1 receives a unique control of modification, and we also propose a novel N-glycosylation occupancy regulatory mechanism by Bip that might be associated with α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate receptors function in the brain.
31958346	11	71	gly	N401-glycosite	1764:1777	arg1	GluA1					1782:1786	GluA1	1782:1786	GluA1	1782:1786	Taken together, we propose that the N401-glycosite of GluA1 receives a unique control of modification, and we also propose a novel N-glycosylation occupancy regulatory mechanism by Bip that might be associated with α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate receptors function in the brain.
31958346	8	72	theme	family	1273:1278	arg1	proteins					1280:1287	HSP70 family proteins	1267:1287	HSP70 family proteins	1267:1287	HSP70 family proteins, including Bip, were identified as candidates.
31958346	8	72	theme	family	1273:1278	arg1	candidates					1324:1333	candidates	1324:1333	candidates	1324:1333	HSP70 family proteins, including Bip, were identified as candidates.
31958346	8	72	theme	family	1273:1278	arg1	Bip					1300:1302	Bip	1300:1302	Bip	1300:1302	HSP70 family proteins, including Bip, were identified as candidates.
31958346	10	73	theme	N401	1644:1647	arg1	form					1661:1664	the N401 glycan-free form	1640:1664	the N401 glycan-free form	1640:1664	To examine the involvement of Bip in N401-glycosylation, the effect of Bip over-expression on N401 occupancy was evaluated in HEK293T cells, and the results demonstrated Bip increases the N401 glycan-free form by mediating selective prolongation of its protein half-life.
31958346	2	74	theme	glutamate	506:514	arg1	receptor					516:523	α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor	451:523	α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor	451:523	In this study, we performed a comprehensive N-glycosylation analysis of mouse GluA1, one of the major subunits of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor, which possesses six potential N-glycosylation sites in the N-terminal domain.
31958346	0	75	theme	glutamate	87:95	arg1	receptors					97:105	α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate-type glutamate receptors	32:105	α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate-type glutamate receptors using specific antibodies	32:131	Monitoring the glycosylation of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate-type glutamate receptors using specific antibodies reveals a novel regulatory mechanism of N-glycosylation occupancy by molecular chaperones in mice.
31958346	2	76	theme	α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate	451:499	arg1	receptor					516:523	α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor	451:523	α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor	451:523	In this study, we performed a comprehensive N-glycosylation analysis of mouse GluA1, one of the major subunits of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor, which possesses six potential N-glycosylation sites in the N-terminal domain.
31958346	0	77	gly	glycosylation	15:27	arg1	receptors					97:105	α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate-type glutamate receptors	32:105	α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate-type glutamate receptors using specific antibodies	32:131	Monitoring the glycosylation of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate-type glutamate receptors using specific antibodies reveals a novel regulatory mechanism of N-glycosylation occupancy by molecular chaperones in mice.
31958346	2	78	theme	potential	546:554	arg1	sites					572:576	six potential N-glycosylation sites	542:576	six potential N-glycosylation sites in the N-terminal domain	542:601	In this study, we performed a comprehensive N-glycosylation analysis of mouse GluA1, one of the major subunits of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor, which possesses six potential N-glycosylation sites in the N-terminal domain.
31958346	6	79	from	manner	1118:1123	arg1	forebrains					1134:1143	mouse forebrains	1128:1143	mouse forebrains	1128:1143	Using this antibody, we clarified that N401 occupancy varies between cell types and increases in an age-dependent manner in mouse forebrains.
31958346	11	80	theme	occupancy	1875:1883	arg1	mechanism					1896:1904	a novel N-glycosylation occupancy regulatory mechanism	1851:1904	a novel N-glycosylation occupancy regulatory mechanism by Bip that might be associated with α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate receptors function in the brain	1851:2023	Taken together, we propose that the N401-glycosite of GluA1 receives a unique control of modification, and we also propose a novel N-glycosylation occupancy regulatory mechanism by Bip that might be associated with α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate receptors function in the brain.
31958346	10	81	theme	Bip	1486:1488	arg1	involvement					1471:1481	the involvement	1467:1481	the involvement of Bip in N401-glycosylation	1467:1510	To examine the involvement of Bip in N401-glycosylation, the effect of Bip over-expression on N401 occupancy was evaluated in HEK293T cells, and the results demonstrated Bip increases the N401 glycan-free form by mediating selective prolongation of its protein half-life.
31958346	11	82	theme	novel	1853:1857	arg1	mechanism					1896:1904	a novel N-glycosylation occupancy regulatory mechanism	1851:1904	a novel N-glycosylation occupancy regulatory mechanism by Bip that might be associated with α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate receptors function in the brain	1851:2023	Taken together, we propose that the N401-glycosite of GluA1 receives a unique control of modification, and we also propose a novel N-glycosylation occupancy regulatory mechanism by Bip that might be associated with α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate receptors function in the brain.
31958346	2	83	theme	N-glycosylation	381:395	arg1	analysis					397:404	a comprehensive N-glycosylation analysis	365:404	a comprehensive N-glycosylation analysis of mouse GluA1, one of the major subunits of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor, which possesses six potential N-glycosylation sites in the N-terminal domain	365:601	In this study, we performed a comprehensive N-glycosylation analysis of mouse GluA1, one of the major subunits of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor, which possesses six potential N-glycosylation sites in the N-terminal domain.
31958346	10	84	theme	over-expression	1531:1545	arg1	effect					1517:1522	the effect	1513:1522	the effect of Bip over-expression on N401 occupancy	1513:1563	To examine the involvement of Bip in N401-glycosylation, the effect of Bip over-expression on N401 occupancy was evaluated in HEK293T cells, and the results demonstrated Bip increases the N401 glycan-free form by mediating selective prolongation of its protein half-life.
31958346	11	85	theme	unique	1799:1804	arg1	control					1806:1812	a unique control	1797:1812	a unique control of modification	1797:1828	Taken together, we propose that the N401-glycosite of GluA1 receives a unique control of modification, and we also propose a novel N-glycosylation occupancy regulatory mechanism by Bip that might be associated with α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate receptors function in the brain.
21389326	0	0	theme	complex	88:94	arg1	assembly					43:50	the extracellular assembly	25:50	the extracellular assembly of the hematopoietic Flt3 signaling complex	25:94	Structural insights into the extracellular assembly of the hematopoietic Flt3 signaling complex.
21389326	1	1	theme	signaling	292:300	arg1	cascades					302:309	signaling cascades	292:309	signaling cascades crucial for the development and homeostasis of hematopoietic progenitors and antigen-presenting dendritic cells	292:421	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3) and its cytokine ligand (FL) play central roles in hematopoiesis and the immune system, by establishing signaling cascades crucial for the development and homeostasis of hematopoietic progenitors and antigen-presenting dendritic cells.
21389326	2	2	theme	acute	586:590	arg1	leukemia					600:607	acute myeloid leukemia	586:607	acute myeloid leukemia	586:607	However, Flt3 is also one of the most frequently mutated receptors in hematologic malignancies and is currently a major prognostic factor and clinical target for acute myeloid leukemia.
21389326	4	3	theme	extracellular	889:901	arg1	domain					903:908	extracellular domain 3	889:910	extracellular domain 3 of Flt3	889:918	FL induces dimerization of Flt3 via a remarkably compact binding epitope localized at the tip of extracellular domain 3 of Flt3, and it invokes a ternary complex devoid of homotypic receptor interactions.
21389326	4	3	theme	extracellular	889:901	arg1	Flt3					915:918	Flt3	915:918	Flt3	915:918	FL induces dimerization of Flt3 via a remarkably compact binding epitope localized at the tip of extracellular domain 3 of Flt3, and it invokes a ternary complex devoid of homotypic receptor interactions.
21389326	1	4	theme	Fms-like	145:152	arg1	receptor					170:177	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3	97:179	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3)	97:186	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3) and its cytokine ligand (FL) play central roles in hematopoiesis and the immune system, by establishing signaling cascades crucial for the development and homeostasis of hematopoietic progenitors and antigen-presenting dendritic cells.
21389326	1	4	theme	Fms-like	145:152	arg1	Flt3					182:185	Flt3	182:185	Flt3	182:185	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3) and its cytokine ligand (FL) play central roles in hematopoiesis and the immune system, by establishing signaling cascades crucial for the development and homeostasis of hematopoietic progenitors and antigen-presenting dendritic cells.
21389326	7	5	theme	FL	1442:1443	arg1	reminiscent					1445:1455	FL reminiscent	1442:1455	FL reminiscent of a "lock-and-key" binding mode	1442:1488	Together, our data suggest that the high-affinity Flt3:FL complex is driven in part by a single preformed binding epitope on FL reminiscent of a "lock-and-key" binding mode, thereby setting the stage for antagonist design.
21389326	0	6	theme	signaling	78:86	arg1	complex					88:94	the hematopoietic Flt3 signaling complex	55:94	the hematopoietic Flt3 signaling complex	55:94	Structural insights into the extracellular assembly of the hematopoietic Flt3 signaling complex.
21389326	3	7	theme	Flt3	655:658	arg1	complex					676:682	the Flt3 ligand-receptor complex	651:682	the Flt3 ligand-receptor complex	651:682	Here, we report the structural basis for the Flt3 ligand-receptor complex and unveil an unanticipated extracellular assembly unlike any other RTKIII/V complex characterized to date.
21389326	3	8	theme	structural	630:639	arg1	basis					641:645	the structural basis	626:645	the structural basis for the Flt3 ligand-receptor complex	626:682	Here, we report the structural basis for the Flt3 ligand-receptor complex and unveil an unanticipated extracellular assembly unlike any other RTKIII/V complex characterized to date.
21389326	1	9	theme	tyrosine	154:161	arg1	receptor					170:177	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3	97:179	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3)	97:186	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3) and its cytokine ligand (FL) play central roles in hematopoiesis and the immune system, by establishing signaling cascades crucial for the development and homeostasis of hematopoietic progenitors and antigen-presenting dendritic cells.
21389326	1	9	theme	tyrosine	154:161	arg1	Flt3					182:185	Flt3	182:185	Flt3	182:185	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3) and its cytokine ligand (FL) play central roles in hematopoiesis and the immune system, by establishing signaling cascades crucial for the development and homeostasis of hematopoietic progenitors and antigen-presenting dendritic cells.
21389326	1	10	theme	crucial	311:317	arg1	cascades					302:309	signaling cascades	292:309	signaling cascades crucial for the development and homeostasis of hematopoietic progenitors and antigen-presenting dendritic cells	292:421	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3) and its cytokine ligand (FL) play central roles in hematopoiesis and the immune system, by establishing signaling cascades crucial for the development and homeostasis of hematopoietic progenitors and antigen-presenting dendritic cells.
21389326	6	11	theme	points	1227:1232	arg1	dissection					1195:1204	thermodynamic dissection	1181:1204	thermodynamic dissection of complex formation points to a pronounced enthalpically driven binding event	1181:1283	Furthermore, thermodynamic dissection of complex formation points to a pronounced enthalpically driven binding event coupled to an entropic penalty.
21389326	7	12	theme	preformed	1413:1421	arg1	epitope					1431:1437	a single preformed binding epitope	1404:1437	a single preformed binding epitope on FL reminiscent of a "lock-and-key" binding mode	1404:1488	Together, our data suggest that the high-affinity Flt3:FL complex is driven in part by a single preformed binding epitope on FL reminiscent of a "lock-and-key" binding mode, thereby setting the stage for antagonist design.
21389326	1	13	theme	central	222:228	arg1	roles					230:234	central roles	222:234	central roles	222:234	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3) and its cytokine ligand (FL) play central roles in hematopoiesis and the immune system, by establishing signaling cascades crucial for the development and homeostasis of hematopoietic progenitors and antigen-presenting dendritic cells.
21389326	2	14	theme	hematologic	494:504	arg1	malignancies					506:517	hematologic malignancies	494:517	hematologic malignancies	494:517	However, Flt3 is also one of the most frequently mutated receptors in hematologic malignancies and is currently a major prognostic factor and clinical target for acute myeloid leukemia.
21389326	3	15	theme	unanticipated	698:710	arg1	assembly					726:733	an unanticipated extracellular assembly	695:733	an unanticipated extracellular assembly unlike any other RTKIII/V complex characterized to date	695:789	Here, we report the structural basis for the Flt3 ligand-receptor complex and unveil an unanticipated extracellular assembly unlike any other RTKIII/V complex characterized to date.
21389326	2	16	theme	clinical	566:573	arg1	target					575:580	clinical target	566:580	clinical target for acute myeloid leukemia	566:607	However, Flt3 is also one of the most frequently mutated receptors in hematologic malignancies and is currently a major prognostic factor and clinical target for acute myeloid leukemia.
21389326	7	17	theme	binding	1423:1429	arg1	epitope					1431:1437	a single preformed binding epitope	1404:1437	a single preformed binding epitope on FL reminiscent of a "lock-and-key" binding mode	1404:1488	Together, our data suggest that the high-affinity Flt3:FL complex is driven in part by a single preformed binding epitope on FL reminiscent of a "lock-and-key" binding mode, thereby setting the stage for antagonist design.
21389326	4	18	theme	homotypic	964:972	arg1	interactions					983:994	homotypic receptor interactions	964:994	homotypic receptor interactions	964:994	FL induces dimerization of Flt3 via a remarkably compact binding epitope localized at the tip of extracellular domain 3 of Flt3, and it invokes a ternary complex devoid of homotypic receptor interactions.
21389326	4	19	theme	interactions	983:994	arg1	devoid					954:959	devoid	954:959	devoid	954:959	FL induces dimerization of Flt3 via a remarkably compact binding epitope localized at the tip of extracellular domain 3 of Flt3, and it invokes a ternary complex devoid of homotypic receptor interactions.
21389326	5	20	with	Comparisons	997:1007	arg1	receptors					1033:1041	homologous receptors	1022:1041	homologous receptors	1022:1041	Comparisons of Flt3 with homologous receptors and available mutagenesis data for FL have allowed us to rationalize the unique features of the Flt3 extracellular assembly.
21389326	3	21	theme	extracellular	712:724	arg1	assembly					726:733	an unanticipated extracellular assembly	695:733	an unanticipated extracellular assembly unlike any other RTKIII/V complex characterized to date	695:789	Here, we report the structural basis for the Flt3 ligand-receptor complex and unveil an unanticipated extracellular assembly unlike any other RTKIII/V complex characterized to date.
21389326	6	22	theme	binding	1271:1277	arg1	event					1279:1283	a pronounced enthalpically driven binding event	1237:1283	a pronounced enthalpically driven binding event	1237:1283	Furthermore, thermodynamic dissection of complex formation points to a pronounced enthalpically driven binding event coupled to an entropic penalty.
21389326	7	23	theme	FL	1372:1373	arg1	complex					1375:1381	the high-affinity Flt3:FL complex	1349:1381	the high-affinity Flt3:FL complex	1349:1381	Together, our data suggest that the high-affinity Flt3:FL complex is driven in part by a single preformed binding epitope on FL reminiscent of a "lock-and-key" binding mode, thereby setting the stage for antagonist design.
21389326	1	24	theme	kinase	163:168	arg1	receptor					170:177	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3	97:179	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3)	97:186	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3) and its cytokine ligand (FL) play central roles in hematopoiesis and the immune system, by establishing signaling cascades crucial for the development and homeostasis of hematopoietic progenitors and antigen-presenting dendritic cells.
21389326	1	24	theme	kinase	163:168	arg1	Flt3					182:185	Flt3	182:185	Flt3	182:185	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3) and its cytokine ligand (FL) play central roles in hematopoiesis and the immune system, by establishing signaling cascades crucial for the development and homeostasis of hematopoietic progenitors and antigen-presenting dendritic cells.
21389326	2	25	theme	receptors	481:489	arg1	one					446:448	one	446:448	one	446:448	However, Flt3 is also one of the most frequently mutated receptors in hematologic malignancies and is currently a major prognostic factor and clinical target for acute myeloid leukemia.
21389326	2	25	theme	receptors	481:489	arg1	receptors					481:489	the most frequently mutated receptors	453:489	the most frequently mutated receptors in hematologic malignancies	453:517	However, Flt3 is also one of the most frequently mutated receptors in hematologic malignancies and is currently a major prognostic factor and clinical target for acute myeloid leukemia.
21389326	6	26	theme	driven	1264:1269	arg1	event					1279:1283	a pronounced enthalpically driven binding event	1237:1283	a pronounced enthalpically driven binding event	1237:1283	Furthermore, thermodynamic dissection of complex formation points to a pronounced enthalpically driven binding event coupled to an entropic penalty.
21389326	7	27	theme	single	1406:1411	arg1	epitope					1431:1437	a single preformed binding epitope	1404:1437	a single preformed binding epitope on FL reminiscent of a "lock-and-key" binding mode	1404:1488	Together, our data suggest that the high-affinity Flt3:FL complex is driven in part by a single preformed binding epitope on FL reminiscent of a "lock-and-key" binding mode, thereby setting the stage for antagonist design.
21389326	7	28	theme	"	1475:1475	arg1	mode					1485:1488	a "lock-and-key" binding mode	1460:1488	a "lock-and-key" binding mode	1460:1488	Together, our data suggest that the high-affinity Flt3:FL complex is driven in part by a single preformed binding epitope on FL reminiscent of a "lock-and-key" binding mode, thereby setting the stage for antagonist design.
21389326	4	29	theme	ternary	938:944	arg1	complex					946:952	a ternary complex	936:952	a ternary complex devoid of homotypic receptor interactions	936:994	FL induces dimerization of Flt3 via a remarkably compact binding epitope localized at the tip of extracellular domain 3 of Flt3, and it invokes a ternary complex devoid of homotypic receptor interactions.
21389326	7	30	from	epitope	1431:1437	arg1	reminiscent					1445:1455	FL reminiscent	1442:1455	FL reminiscent of a "lock-and-key" binding mode	1442:1488	Together, our data suggest that the high-affinity Flt3:FL complex is driven in part by a single preformed binding epitope on FL reminiscent of a "lock-and-key" binding mode, thereby setting the stage for antagonist design.
21389326	4	31	theme	devoid	954:959	arg1	complex					946:952	a ternary complex	936:952	a ternary complex devoid of homotypic receptor interactions	936:994	FL induces dimerization of Flt3 via a remarkably compact binding epitope localized at the tip of extracellular domain 3 of Flt3, and it invokes a ternary complex devoid of homotypic receptor interactions.
21389326	4	32	theme	binding	849:855	arg1	epitope					857:863	a remarkably compact binding epitope	828:863	a remarkably compact binding epitope localized at the tip of extracellular domain 3 of Flt3	828:918	FL induces dimerization of Flt3 via a remarkably compact binding epitope localized at the tip of extracellular domain 3 of Flt3, and it invokes a ternary complex devoid of homotypic receptor interactions.
21389326	2	33	theme	mutated	473:479	arg1	receptors					481:489	the most frequently mutated receptors	453:489	the most frequently mutated receptors in hematologic malignancies	453:517	However, Flt3 is also one of the most frequently mutated receptors in hematologic malignancies and is currently a major prognostic factor and clinical target for acute myeloid leukemia.
21389326	6	34	theme	pronounced	1239:1248	arg1	event					1279:1283	a pronounced enthalpically driven binding event	1237:1283	a pronounced enthalpically driven binding event	1237:1283	Furthermore, thermodynamic dissection of complex formation points to a pronounced enthalpically driven binding event coupled to an entropic penalty.
21389326	0	35	theme	Structural	0:9	arg1	insights					11:18	Structural insights	0:18	Structural insights into the extracellular assembly of the hematopoietic Flt3 signaling complex	0:94	Structural insights into the extracellular assembly of the hematopoietic Flt3 signaling complex.
21389326	5	36	theme	assembly	1158:1165	arg1	features					1123:1130	the unique features	1112:1130	the unique features of the Flt3 extracellular assembly	1112:1165	Comparisons of Flt3 with homologous receptors and available mutagenesis data for FL have allowed us to rationalize the unique features of the Flt3 extracellular assembly.
21389326	2	37	theme	myeloid	592:598	arg1	leukemia					600:607	acute myeloid leukemia	586:607	acute myeloid leukemia	586:607	However, Flt3 is also one of the most frequently mutated receptors in hematologic malignancies and is currently a major prognostic factor and clinical target for acute myeloid leukemia.
21389326	7	38	theme	lock-and-key	1463:1474	arg1	mode					1485:1488	a "lock-and-key" binding mode	1460:1488	a "lock-and-key" binding mode	1460:1488	Together, our data suggest that the high-affinity Flt3:FL complex is driven in part by a single preformed binding epitope on FL reminiscent of a "lock-and-key" binding mode, thereby setting the stage for antagonist design.
21389326	7	39	theme	mode	1485:1488	arg1	reminiscent					1445:1455	FL reminiscent	1442:1455	FL reminiscent of a "lock-and-key" binding mode	1442:1488	Together, our data suggest that the high-affinity Flt3:FL complex is driven in part by a single preformed binding epitope on FL reminiscent of a "lock-and-key" binding mode, thereby setting the stage for antagonist design.
21389326	5	40	theme	unique	1116:1121	arg1	features					1123:1130	the unique features	1112:1130	the unique features of the Flt3 extracellular assembly	1112:1165	Comparisons of Flt3 with homologous receptors and available mutagenesis data for FL have allowed us to rationalize the unique features of the Flt3 extracellular assembly.
21389326	3	41	theme	other	746:750	arg1	complex					761:767	any other RTKIII/V complex	742:767	any other RTKIII/V complex characterized to date	742:789	Here, we report the structural basis for the Flt3 ligand-receptor complex and unveil an unanticipated extracellular assembly unlike any other RTKIII/V complex characterized to date.
21389326	4	42	theme	Flt3	819:822	arg1	dimerization					803:814	dimerization	803:814	dimerization of Flt3	803:822	FL induces dimerization of Flt3 via a remarkably compact binding epitope localized at the tip of extracellular domain 3 of Flt3, and it invokes a ternary complex devoid of homotypic receptor interactions.
21389326	1	43	theme	class	101:105	arg1	receptor					170:177	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3	97:179	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3)	97:186	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3) and its cytokine ligand (FL) play central roles in hematopoiesis and the immune system, by establishing signaling cascades crucial for the development and homeostasis of hematopoietic progenitors and antigen-presenting dendritic cells.
21389326	1	43	theme	class	101:105	arg1	Flt3					182:185	Flt3	182:185	Flt3	182:185	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3) and its cytokine ligand (FL) play central roles in hematopoiesis and the immune system, by establishing signaling cascades crucial for the development and homeostasis of hematopoietic progenitors and antigen-presenting dendritic cells.
21389326	5	44	theme	available	1047:1055	arg1	data					1069:1072	available mutagenesis data	1047:1072	available mutagenesis data for FL	1047:1079	Comparisons of Flt3 with homologous receptors and available mutagenesis data for FL have allowed us to rationalize the unique features of the Flt3 extracellular assembly.
21389326	5	45	theme	mutagenesis	1057:1067	arg1	data					1069:1072	available mutagenesis data	1047:1072	available mutagenesis data for FL	1047:1079	Comparisons of Flt3 with homologous receptors and available mutagenesis data for FL have allowed us to rationalize the unique features of the Flt3 extracellular assembly.
21389326	4	46	theme	receptor	974:981	arg1	interactions					983:994	homotypic receptor interactions	964:994	homotypic receptor interactions	964:994	FL induces dimerization of Flt3 via a remarkably compact binding epitope localized at the tip of extracellular domain 3 of Flt3, and it invokes a ternary complex devoid of homotypic receptor interactions.
21389326	5	47	with	data	1069:1072	arg1	receptors					1033:1041	homologous receptors	1022:1041	homologous receptors	1022:1041	Comparisons of Flt3 with homologous receptors and available mutagenesis data for FL have allowed us to rationalize the unique features of the Flt3 extracellular assembly.
21389326	0	48	theme	extracellular	29:41	arg1	assembly					43:50	the extracellular assembly	25:50	the extracellular assembly of the hematopoietic Flt3 signaling complex	25:94	Structural insights into the extracellular assembly of the hematopoietic Flt3 signaling complex.
21389326	1	49	theme	immune	261:266	arg1	system					268:273	the immune system	257:273	the immune system	257:273	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3) and its cytokine ligand (FL) play central roles in hematopoiesis and the immune system, by establishing signaling cascades crucial for the development and homeostasis of hematopoietic progenitors and antigen-presenting dendritic cells.
21389326	4	50	theme	Flt3	915:918	arg1	domain					903:908	extracellular domain 3	889:910	extracellular domain 3 of Flt3	889:918	FL induces dimerization of Flt3 via a remarkably compact binding epitope localized at the tip of extracellular domain 3 of Flt3, and it invokes a ternary complex devoid of homotypic receptor interactions.
21389326	4	50	theme	Flt3	915:918	arg1	Flt3					915:918	Flt3	915:918	Flt3	915:918	FL induces dimerization of Flt3 via a remarkably compact binding epitope localized at the tip of extracellular domain 3 of Flt3, and it invokes a ternary complex devoid of homotypic receptor interactions.
21389326	1	51	theme	hematopoietic	358:370	arg1	progenitors					372:382	hematopoietic progenitors	358:382	hematopoietic progenitors	358:382	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3) and its cytokine ligand (FL) play central roles in hematopoiesis and the immune system, by establishing signaling cascades crucial for the development and homeostasis of hematopoietic progenitors and antigen-presenting dendritic cells.
21389326	5	52	theme	Flt3	1139:1142	arg1	assembly					1158:1165	the Flt3 extracellular assembly	1135:1165	the Flt3 extracellular assembly	1135:1165	Comparisons of Flt3 with homologous receptors and available mutagenesis data for FL have allowed us to rationalize the unique features of the Flt3 extracellular assembly.
21389326	6	53	theme	entropic	1299:1306	arg1	penalty					1308:1314	an entropic penalty	1296:1314	an entropic penalty	1296:1314	Furthermore, thermodynamic dissection of complex formation points to a pronounced enthalpically driven binding event coupled to an entropic penalty.
21389326	1	54	theme	progenitors	372:382	arg1	homeostasis					343:353	homeostasis	343:353	homeostasis	343:353	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3) and its cytokine ligand (FL) play central roles in hematopoiesis and the immune system, by establishing signaling cascades crucial for the development and homeostasis of hematopoietic progenitors and antigen-presenting dendritic cells.
21389326	1	54	theme	progenitors	372:382	arg1	development					327:337	the development	323:337	the development	323:337	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3) and its cytokine ligand (FL) play central roles in hematopoiesis and the immune system, by establishing signaling cascades crucial for the development and homeostasis of hematopoietic progenitors and antigen-presenting dendritic cells.
21389326	5	55	theme	Flt3	1012:1015	arg1	data					1069:1072	available mutagenesis data	1047:1072	available mutagenesis data for FL	1047:1079	Comparisons of Flt3 with homologous receptors and available mutagenesis data for FL have allowed us to rationalize the unique features of the Flt3 extracellular assembly.
21389326	5	55	theme	Flt3	1012:1015	arg1	Comparisons					997:1007	Comparisons	997:1007	Comparisons of Flt3 with homologous receptors	997:1041	Comparisons of Flt3 with homologous receptors and available mutagenesis data for FL have allowed us to rationalize the unique features of the Flt3 extracellular assembly.
21389326	4	56	theme	domain	903:908	arg1	tip					882:884	the tip	878:884	the tip of extracellular domain 3 of Flt3	878:918	FL induces dimerization of Flt3 via a remarkably compact binding epitope localized at the tip of extracellular domain 3 of Flt3, and it invokes a ternary complex devoid of homotypic receptor interactions.
21389326	1	57	theme	receptor	111:118	arg1	receptor					170:177	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3	97:179	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3)	97:186	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3) and its cytokine ligand (FL) play central roles in hematopoiesis and the immune system, by establishing signaling cascades crucial for the development and homeostasis of hematopoietic progenitors and antigen-presenting dendritic cells.
21389326	1	57	theme	receptor	111:118	arg1	Flt3					182:185	Flt3	182:185	Flt3	182:185	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3) and its cytokine ligand (FL) play central roles in hematopoiesis and the immune system, by establishing signaling cascades crucial for the development and homeostasis of hematopoietic progenitors and antigen-presenting dendritic cells.
21389326	3	58	theme	ligand-receptor	660:674	arg1	complex					676:682	the Flt3 ligand-receptor complex	651:682	the Flt3 ligand-receptor complex	651:682	Here, we report the structural basis for the Flt3 ligand-receptor complex and unveil an unanticipated extracellular assembly unlike any other RTKIII/V complex characterized to date.
21389326	3	59	theme	RTKIII/V	752:759	arg1	complex					761:767	any other RTKIII/V complex	742:767	any other RTKIII/V complex characterized to date	742:789	Here, we report the structural basis for the Flt3 ligand-receptor complex and unveil an unanticipated extracellular assembly unlike any other RTKIII/V complex characterized to date.
21389326	5	60	theme	homologous	1022:1031	arg1	receptors					1033:1041	homologous receptors	1022:1041	homologous receptors	1022:1041	Comparisons of Flt3 with homologous receptors and available mutagenesis data for FL have allowed us to rationalize the unique features of the Flt3 extracellular assembly.
21389326	2	61	from	receptors	481:489	arg1	malignancies					506:517	hematologic malignancies	494:517	hematologic malignancies	494:517	However, Flt3 is also one of the most frequently mutated receptors in hematologic malignancies and is currently a major prognostic factor and clinical target for acute myeloid leukemia.
21389326	1	62	theme	tyrosine	120:127	arg1	receptor					170:177	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3	97:179	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3)	97:186	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3) and its cytokine ligand (FL) play central roles in hematopoiesis and the immune system, by establishing signaling cascades crucial for the development and homeostasis of hematopoietic progenitors and antigen-presenting dendritic cells.
21389326	1	62	theme	tyrosine	120:127	arg1	Flt3					182:185	Flt3	182:185	Flt3	182:185	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3) and its cytokine ligand (FL) play central roles in hematopoiesis and the immune system, by establishing signaling cascades crucial for the development and homeostasis of hematopoietic progenitors and antigen-presenting dendritic cells.
21389326	6	63	theme	formation	1217:1225	arg1	points					1227:1232	complex formation points	1209:1232	complex formation points	1209:1232	Furthermore, thermodynamic dissection of complex formation points to a pronounced enthalpically driven binding event coupled to an entropic penalty.
21389326	5	64	theme	extracellular	1144:1156	arg1	assembly					1158:1165	the Flt3 extracellular assembly	1135:1165	the Flt3 extracellular assembly	1135:1165	Comparisons of Flt3 with homologous receptors and available mutagenesis data for FL have allowed us to rationalize the unique features of the Flt3 extracellular assembly.
21389326	2	65	theme	prognostic	544:553	arg1	factor					555:560	a major prognostic factor	536:560	a major prognostic factor	536:560	However, Flt3 is also one of the most frequently mutated receptors in hematologic malignancies and is currently a major prognostic factor and clinical target for acute myeloid leukemia.
21389326	1	66	theme	antigen-presenting	388:405	arg1	cells					417:421	antigen-presenting dendritic cells	388:421	antigen-presenting dendritic cells	388:421	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3) and its cytokine ligand (FL) play central roles in hematopoiesis and the immune system, by establishing signaling cascades crucial for the development and homeostasis of hematopoietic progenitors and antigen-presenting dendritic cells.
21389326	6	67	theme	complex	1209:1215	arg1	points					1227:1232	complex formation points	1209:1232	complex formation points	1209:1232	Furthermore, thermodynamic dissection of complex formation points to a pronounced enthalpically driven binding event coupled to an entropic penalty.
21389326	1	68	theme	kinase	129:134	arg1	receptor					170:177	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3	97:179	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3)	97:186	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3) and its cytokine ligand (FL) play central roles in hematopoiesis and the immune system, by establishing signaling cascades crucial for the development and homeostasis of hematopoietic progenitors and antigen-presenting dendritic cells.
21389326	1	68	theme	kinase	129:134	arg1	Flt3					182:185	Flt3	182:185	Flt3	182:185	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3) and its cytokine ligand (FL) play central roles in hematopoiesis and the immune system, by establishing signaling cascades crucial for the development and homeostasis of hematopoietic progenitors and antigen-presenting dendritic cells.
21389326	4	69	located	localized	865:873	arg1	tip					882:884	the tip	878:884	the tip of extracellular domain 3 of Flt3	878:918	FL induces dimerization of Flt3 via a remarkably compact binding epitope localized at the tip of extracellular domain 3 of Flt3, and it invokes a ternary complex devoid of homotypic receptor interactions.
21389326	4	69	located	localized	865:873	arg2	epitope					857:863	a remarkably compact binding epitope	828:863	a remarkably compact binding epitope localized at the tip of extracellular domain 3 of Flt3	828:918	FL induces dimerization of Flt3 via a remarkably compact binding epitope localized at the tip of extracellular domain 3 of Flt3, and it invokes a ternary complex devoid of homotypic receptor interactions.
21389326	1	70	theme	cytokine	196:203	arg1	FL					213:214	FL	213:214	FL	213:214	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3) and its cytokine ligand (FL) play central roles in hematopoiesis and the immune system, by establishing signaling cascades crucial for the development and homeostasis of hematopoietic progenitors and antigen-presenting dendritic cells.
21389326	1	70	theme	cytokine	196:203	arg1	ligand					205:210	its cytokine ligand	192:210	its cytokine ligand (FL)	192:215	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3) and its cytokine ligand (FL) play central roles in hematopoiesis and the immune system, by establishing signaling cascades crucial for the development and homeostasis of hematopoietic progenitors and antigen-presenting dendritic cells.
21389326	2	71	theme	major	538:542	arg1	factor					555:560	a major prognostic factor	536:560	a major prognostic factor	536:560	However, Flt3 is also one of the most frequently mutated receptors in hematologic malignancies and is currently a major prognostic factor and clinical target for acute myeloid leukemia.
21389326	1	72	theme	dendritic	407:415	arg1	cells					417:421	antigen-presenting dendritic cells	388:421	antigen-presenting dendritic cells	388:421	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3) and its cytokine ligand (FL) play central roles in hematopoiesis and the immune system, by establishing signaling cascades crucial for the development and homeostasis of hematopoietic progenitors and antigen-presenting dendritic cells.
21389326	7	73	theme	Flt3	1367:1370	arg1	complex					1375:1381	the high-affinity Flt3:FL complex	1349:1381	the high-affinity Flt3:FL complex	1349:1381	Together, our data suggest that the high-affinity Flt3:FL complex is driven in part by a single preformed binding epitope on FL reminiscent of a "lock-and-key" binding mode, thereby setting the stage for antagonist design.
21389326	0	74	theme	Flt3	73:76	arg1	complex					88:94	the hematopoietic Flt3 signaling complex	55:94	the hematopoietic Flt3 signaling complex	55:94	Structural insights into the extracellular assembly of the hematopoietic Flt3 signaling complex.
21389326	1	75	theme	cells	417:421	arg1	homeostasis					343:353	homeostasis	343:353	homeostasis	343:353	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3) and its cytokine ligand (FL) play central roles in hematopoiesis and the immune system, by establishing signaling cascades crucial for the development and homeostasis of hematopoietic progenitors and antigen-presenting dendritic cells.
21389326	1	75	theme	cells	417:421	arg1	development					327:337	the development	323:337	the development	323:337	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3) and its cytokine ligand (FL) play central roles in hematopoiesis and the immune system, by establishing signaling cascades crucial for the development and homeostasis of hematopoietic progenitors and antigen-presenting dendritic cells.
21389326	7	76	theme	antagonist	1521:1530	arg1	design					1532:1537	antagonist design	1521:1537	antagonist design	1521:1537	Together, our data suggest that the high-affinity Flt3:FL complex is driven in part by a single preformed binding epitope on FL reminiscent of a "lock-and-key" binding mode, thereby setting the stage for antagonist design.
21389326	1	77	theme	RTKIII	137:142	arg1	receptor					170:177	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3	97:179	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3)	97:186	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3) and its cytokine ligand (FL) play central roles in hematopoiesis and the immune system, by establishing signaling cascades crucial for the development and homeostasis of hematopoietic progenitors and antigen-presenting dendritic cells.
21389326	1	77	theme	RTKIII	137:142	arg1	Flt3					182:185	Flt3	182:185	Flt3	182:185	The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3) and its cytokine ligand (FL) play central roles in hematopoiesis and the immune system, by establishing signaling cascades crucial for the development and homeostasis of hematopoietic progenitors and antigen-presenting dendritic cells.
21389326	0	78	theme	hematopoietic	59:71	arg1	complex					88:94	the hematopoietic Flt3 signaling complex	55:94	the hematopoietic Flt3 signaling complex	55:94	Structural insights into the extracellular assembly of the hematopoietic Flt3 signaling complex.
21389326	7	79	theme	high-affinity	1353:1365	arg1	complex					1375:1381	the high-affinity Flt3:FL complex	1349:1381	the high-affinity Flt3:FL complex	1349:1381	Together, our data suggest that the high-affinity Flt3:FL complex is driven in part by a single preformed binding epitope on FL reminiscent of a "lock-and-key" binding mode, thereby setting the stage for antagonist design.
21389326	6	80	theme	thermodynamic	1181:1193	arg1	dissection					1195:1204	thermodynamic dissection	1181:1204	thermodynamic dissection of complex formation points to a pronounced enthalpically driven binding event	1181:1283	Furthermore, thermodynamic dissection of complex formation points to a pronounced enthalpically driven binding event coupled to an entropic penalty.
21389326	4	81	theme	compact	841:847	arg1	epitope					857:863	a remarkably compact binding epitope	828:863	a remarkably compact binding epitope localized at the tip of extracellular domain 3 of Flt3	828:918	FL induces dimerization of Flt3 via a remarkably compact binding epitope localized at the tip of extracellular domain 3 of Flt3, and it invokes a ternary complex devoid of homotypic receptor interactions.
21389326	7	82	theme	binding	1477:1483	arg1	mode					1485:1488	a "lock-and-key" binding mode	1460:1488	a "lock-and-key" binding mode	1460:1488	Together, our data suggest that the high-affinity Flt3:FL complex is driven in part by a single preformed binding epitope on FL reminiscent of a "lock-and-key" binding mode, thereby setting the stage for antagonist design.