doc_id	sent_index	relation_id	relation	trigger	trigger_offset	arg_num	arg_base_np	arg_protein	arg_domain	arg_site	arg_sugar	PSource	SiteSource	NProtein	NID	SiteName	sent_text
PMC7124471-1-10	5	85	gly	glycosites	476:485	arg1	serotransferrin	serotransferrin				OGER		serotransferrin	P02787		There were four N-linked glycosites of serotransferrin identified, i.e. N432, N630, N637, and N523 (Fig. 6B, supplemental Table S26).
PMC6934601-1-fig6	11	43	gly	SPN	1298:1300	arg1	sialic acid	SPN			sialic acid	OGER		SPN	P16150		(F) The sialic acid and O-glycan content of SPN in MV-4-11 and THP-1 cells was assessed following treatment with neuraminidase, to remove sialic acids, and O-glycosidase, to cleave core 1 O-glycans.
PMC5643531-1-9	0	372	gly	Glycosylation	0:12	arg1	Fz8	Fz8				OGER		Fz8	Q9H461		Glycosylation of Fz8 is required for Wnt/β-catenin signaling.
PMC5795011-1-fig2	2	26	gly	glycoprotein	325:336	arg1	Standard bovine alpha-1-acid glycoprotein 1	Standard bovine alpha-1-acid glycoprotein 1				OGER		alpha-1-acid glycoprotein 1	P02763		Standard bovine alpha-1-acid glycoprotein 1 was digested with trypsin, the glycopeptides were analyzed by LC-MS and the data were searched against the custom glycoprotein database using the Mascot search engine.
PMC6243375-1-4	28	174	gly	glycoproteins	5221:5233	arg1	heavily O‐linked glycoproteins	heavily O‐linked glycoproteins				Cterm		O‐linked			Analysis of the site distribution on glycoproteins demonstrated advantage of EXoO to study heavily O‐linked glycoproteins that is difficult to be analyzed by current analytical approach due to structural complexity and resistance to enzymatic digestion.
PMC5643531-1-9	45	179	gly	Glycosylation	5802:5814	arg1	Fz8	Fz8				OGER		Fz8	Q9H461		Glycosylation of Fz8 is critical for the onset of Wnt signaling by facilitating cell surface localization of Fz8.
PMC5643531-1-8	0	60	gly	glycosylation	19:31	arg1	Fz8	Fz8				OGER		Fz8	Q9H461		OTG is involved in glycosylation of Fz8.
PMC5098438-1-5	68	534	gly	glycoforms	12620:12629	arg1	IgG1 Fc glycoforms	IgG1 Fc glycoforms				Cterm		IgG1			We can rationalize these properties by the analysis of known crystal structures of IgG1 Fc glycoforms.
PMC5098438-1-5	68	534	gly	glycoforms	12620:12629	arg1	IgG1 Fc glycoforms	IgG1 Fc glycoforms				Cterm		Fc			We can rationalize these properties by the analysis of known crystal structures of IgG1 Fc glycoforms.
PMC5643531-1-9	10	102	gly	glycosylation	1318:1330	arg1	Fz8	Fz8				OGER		Fz8	Q9H461		Taken together, these results suggest that N-linked glycosylation of Fz8 may be critical for its cell surface localization and subsequently for Wnt/β-catenin signaling during early embryogenesis.
PMC7124471-1-11	21	58	part_of	N-linked	2530:2537	arg1	all other N-linked intact glycopeptide carrying N630	N-linked		all other N-linked intact glycopeptide carrying N630		Cterm	SpecificSite	N-linked		N630	For all other N-linked intact glycopeptide carrying N630, a spectrum sequence list (.
PMC5098438-1-5	52	116	gly	glycoforms	9179:9188	arg1	homogeneous IgG-Fc glycoforms	homogeneous IgG-Fc glycoforms				Cterm		IgG			SPR binding studies with homogeneous IgG-Fc glycoforms with defined core N-linked glycan transferred to the GlcNAc moiety by the transglycosylation activity of an Arthrobacter endoglycosidase (EndoA) showed that the presence of a bisecting GlcNAc or even a bisecting mannose residue could significantly enhance the binding of the Fc to FcγRIIIA.
PMC7124471-1-6	9	96	gly	glycoproteins	1309:1321	arg1	QSOX1	QSOX1				OGER		QSOX1	O00391		The plant glycoprotein HRP and the four chicken glycoproteins including IOVO, OVAL, Ogchi and QSOX1 were used to validate the setting of database search parameters.
PMC6243375-1-4	26	151	gly	glycoproteins	4772:4784	arg1	these heavily O‐linked glycoproteins	these heavily O‐linked glycoproteins				Cterm		O‐linked			Among these heavily O‐linked glycoproteins, VCAN contained the highest number of sites reaching 165 sites with distinct peptide sequences surrounding the sites, whereas MUC1 contained 161 sites, the second highest, but composited from only six distinct sequence repeats.
PMC7124471-1-11	4	352	part_of	serotransferrin	684:698	arg1	the glycosite N630	serotransferrin		the glycosite N630		OGER	SpecificSite	serotransferrin	P02787	glycosite N630	To obtain the quantitative information of these glycans identified on the glycosite N630 of serotransferrin, the peak area of each precursor ion was integrated by Skyline (35).
PMC3942810-2-1	7	218	gly	RJ	1124:1125	arg1	all	RJ			all	Cterm		RJ			This method suggested that all of the 13 novel proteins predicted to be secretory proteins are real protein components of RJ.
PMC5098438-1-5	11	256	gly	glycoproteins	1964:1976	arg1	CD152	CD152				OGER		CD152	P16410		Furthermore, this series of ions is prominent in the corresponding spectrum of Glc3Man7GlcNAc2 obtained from recombinant glycoproteins, such as CD152 expressed in CHO cells in the presence of the glucosidase inhibitor NB-DNJ, further confirming the structure of the 3-antenna.
PMC5643531-1-8	13	72	gly	glycosylation	1737:1749	arg1	Fz8	Fz8				OGER		Fz8	Q9H461		These results suggest the possibility that OTG inhibits cell surface localization of Fz8 by interfering with N-linked glycosylation of Fz8.
PMC7124471-1-fig5	2	30	gly	glycosites	281:290	arg1	serotransferrin	serotransferrin				OGER		serotransferrin	P02787		C, D, The overlap of N-glycan masses identified on the four glycosites N432, N630 and N637 of serotransferrin and on the four glycosites N529, N822, N882 and N1029 of complement factor H in different samples including commercial transferrin, serum spiked with HRP and ovalbumin, UGP and FGP data set.
PMC7124471-1-fig5	2	47	gly	glycosites	347:356	arg1	complement factor H	complement factor H				OGER		complement factor H	P08603		C, D, The overlap of N-glycan masses identified on the four glycosites N432, N630 and N637 of serotransferrin and on the four glycosites N529, N822, N882 and N1029 of complement factor H in different samples including commercial transferrin, serum spiked with HRP and ovalbumin, UGP and FGP data set.
PMC7124471-1-11	66	281	part_of	albumin	9333:9339	arg1	N68	albumin		N68		Cterm	SpecificSite	albumin		N68	They included the previously reported glycosite N63 of alpha-1B-glycoprotein and N68 of albumin (7), suggesting that our method was reliable.
PMC5976746-1-5	38	201	gly	glycosylation	6114:6126	arg1	BG505 NFL trimers	BG505 NFL trimers				OGER		BG505 NFL trimers	P07196		The minor increase in thermo stability may be due to less variation in the glycosylation profiles of BG505 NFL trimers produced in CHO-M cells.
PMC7124471-1-11	23	437	part_of	serotransferrin	2934:2948	arg1	N630	serotransferrin		N630		OGER	SpecificSite	serotransferrin	P02787	N630	For quantitative study of site-specific glycosylation in human serum using peak areas on LC-MS/MS, it needs to consider the numerous variants of N-linked intact glycopeptides containing the same N-glycosite, such as N630 of serotransferrin.
PMC7143757-1-1	8	67	gly	glycosylated	1129:1140	arg1	rCTB	rCTB				OGER		CTB			The MW of rCTB increased when PglL was co-expressed, indicating that rCTB might have been glycosylated.
PMC4595782-1-7	56	83	gly	SAC	11186:11188	arg1	Par-4	SAC			Par-4	OGER		SAC	Q96PN6		The cytotoxic effect of this protein on both human (PC3) and rat prostate cancer cell lines (MAT-LyLu) further suggests its efficacy on cancer cells of different origin, and this might be due to the highly conserved SAC domain of Par-4 (El-Guendy and Rangnekar, 2003).
PMC7124471-1-10	8	18	gly	glycosites	935:944	arg1	serotransferrin	serotransferrin				OGER		serotransferrin	P02787		Among the mentioned glycosites of serotransferrin, N523 and N637 are not reported in Uniprot.
PMC3938046-1-3	22	165	gly	glycoprotein	3816:3827	arg1	lysosome-associated membrane glycoprotein 1	lysosome-associated membrane glycoprotein 1				OGER		lysosome-associated membrane glycoprotein 1	P11279		Other glycoproteins with 10 or more N-glycosites included receptor-type tyrosine-protein phosphatase eta isoform 1, plexin B2, nicastrin, toll-like receptor 13, and lysosome-associated membrane glycoprotein 1.
PMC7124471-1-11	7	443	part_of	serotransferrin	1032:1046	arg1	N630	serotransferrin		N630		OGER	SpecificSite	serotransferrin	P02787	N630	In total, 363 N-glycan masses were identified on N630 of serotransferrin from UGP and FGP data sets.
PMC5098438-1-1	13	38	gly	aglycosylated	2067:2079	arg1	aglycosylated HCs	aglycosylated HCs				OGER		HCs	O75390		Treatment with PNGase F (peptide N-glycosidase F) led to aglycosylated HCs with similar apparent molecular weights for the commercial MabThera® and for Tt/C2B8.
PMC7124471-1-10	23	89	gly	N-glycosites	2439:2450	arg1	transferrin receptor 1	transferrin receptor 1				OGER		transferrin receptor 1	P02787		S4, the two N-glycosites of serotransferrin and the two N-glycosites of transferrin receptor 1 identified in our work don't approach to each other in their protein complex's structure.
PMC7124471-1-10	23	89	gly	N-glycosites	2439:2450	arg1	serotransferrin	serotransferrin				OGER		serotransferrin	P02787		S4, the two N-glycosites of serotransferrin and the two N-glycosites of transferrin receptor 1 identified in our work don't approach to each other in their protein complex's structure.
PMC7124471-1-10	23	96	gly	N-glycosites	2483:2494	arg1	transferrin receptor 1	transferrin receptor 1				OGER		transferrin receptor 1	P02787		S4, the two N-glycosites of serotransferrin and the two N-glycosites of transferrin receptor 1 identified in our work don't approach to each other in their protein complex's structure.
PMC7124471-1-10	23	96	gly	N-glycosites	2483:2494	arg1	serotransferrin	serotransferrin				OGER		serotransferrin	P02787		S4, the two N-glycosites of serotransferrin and the two N-glycosites of transferrin receptor 1 identified in our work don't approach to each other in their protein complex's structure.
PMC7124471-1-8	4	56	part_of	CD44	618:621	arg1	The N-glycosite N25	CD44		The N-glycosite N25		OGER	SpecificSite	CD44	P16070	N-glycosite N25	The N-glycosite N25 of CD44 locates at its extracellular part.
PMC5795011-1-fig1	0	22	gly	glycoprotein	113:124	arg1	bovine alpha-1-acid glycoprotein 1	bovine alpha-1-acid glycoprotein 1				OGER		alpha-1-acid glycoprotein 1	P02763		HCD-MS2 spectrum of a di-sialylated bi-antennary glycopeptide (m/z 1177.81373+) derived from bovine alpha-1-acid glycoprotein 1.
PMC5643531-1-9	13	191	gly	glycosylation	1935:1947	arg1	Fz8	Fz8				OGER		Fz8	Q9H461		OTG interacted with Wnt receptor Fz8 and inhibited its cell surface targeting possibly by preventing N-linked glycosylation of Fz8.
PMC5098438-1-3	7	9	gly	glycosylated	1127:1138	arg1	fully glycosylated full IgG	fully glycosylated full IgG				Cterm		IgG			As mentioned above, T. thermophila produces a population of aglycosylated HCs (Fig. 1D) leading to the formation of a-, hemi- and fully glycosylated full IgG.
PMC5098438-1-3	7	48	gly	aglycosylated	1051:1063	arg1	aglycosylated HCs	aglycosylated HCs				OGER		HCs	O75390		As mentioned above, T. thermophila produces a population of aglycosylated HCs (Fig. 1D) leading to the formation of a-, hemi- and fully glycosylated full IgG.
PMC7124471-1-11	73	505	gly	glycoform	10395:10403	arg1	serotransferrin glycoform	serotransferrin glycoform				OGER		serotransferrin	P02787		Compared with the established methods based on immuno-capture and MS, our method avoids immuno-capture and provides more details of serotransferrin glycoform in a site-specific manner.
PMC5795011-1-4	64	407	part_of	glycoprotein	11184:11195	arg1	Asn 93	alpha-1-acid glycoprotein 1		Asn 93		OGER	SpecificSite	alpha-1-acid glycoprotein 1	P02763	Asn 93	For example, Mascot annotated a total of nine different mono-, di-, tri- and tetra-sialylated N-glycan structures on a single glycosylation site (Asn 93) of serum alpha-1-acid glycoprotein 1 (Fig. 5).
PMC7124471-1-fig5	2	46	part_of	glycosites	347:356	arg1	commercial transferrin	transferrin		glycosites		OGER	SpecificSite	transferrin	P02787	glycosites N529, N822, N882 and N1029	C, D, The overlap of N-glycan masses identified on the four glycosites N432, N630 and N637 of serotransferrin and on the four glycosites N529, N822, N882 and N1029 of complement factor H in different samples including commercial transferrin, serum spiked with HRP and ovalbumin, UGP and FGP data set.
PMC7124471-1-fig5	2	13	part_of	H	406:406	arg1	N529	complement factor H		glycosites N529, N822, N882 and N1029		OGER	SpecificSite	complement factor H	P08603	glycosites N529, N822, N882 and N1029	C, D, The overlap of N-glycan masses identified on the four glycosites N432, N630 and N637 of serotransferrin and on the four glycosites N529, N822, N882 and N1029 of complement factor H in different samples including commercial transferrin, serum spiked with HRP and ovalbumin, UGP and FGP data set.
PMC7124471-1-fig5	2	13	part_of	H	406:406	arg1	N1029	complement factor H		glycosites N529, N822, N882 and N1029		OGER	SpecificSite	complement factor H	P08603	glycosites N529, N822, N882 and N1029	C, D, The overlap of N-glycan masses identified on the four glycosites N432, N630 and N637 of serotransferrin and on the four glycosites N529, N822, N882 and N1029 of complement factor H in different samples including commercial transferrin, serum spiked with HRP and ovalbumin, UGP and FGP data set.
PMC7124471-1-fig5	2	13	part_of	H	406:406	arg1	N822	complement factor H		glycosites N529, N822, N882 and N1029		OGER	SpecificSite	complement factor H	P08603	glycosites N529, N822, N882 and N1029	C, D, The overlap of N-glycan masses identified on the four glycosites N432, N630 and N637 of serotransferrin and on the four glycosites N529, N822, N882 and N1029 of complement factor H in different samples including commercial transferrin, serum spiked with HRP and ovalbumin, UGP and FGP data set.
PMC7124471-1-fig5	2	13	part_of	H	406:406	arg1	N882	complement factor H		glycosites N529, N822, N882 and N1029		OGER	SpecificSite	complement factor H	P08603	glycosites N529, N822, N882 and N1029	C, D, The overlap of N-glycan masses identified on the four glycosites N432, N630 and N637 of serotransferrin and on the four glycosites N529, N822, N882 and N1029 of complement factor H in different samples including commercial transferrin, serum spiked with HRP and ovalbumin, UGP and FGP data set.
PMC7124471-1-fig5	2	13	part_of	H	406:406	arg1	N1029	complement factor H		glycosites N529, N822, N882 and N1029		OGER	SpecificSite	complement factor H	P08603	glycosites N529, N822, N882 and N1029	C, D, The overlap of N-glycan masses identified on the four glycosites N432, N630 and N637 of serotransferrin and on the four glycosites N529, N822, N882 and N1029 of complement factor H in different samples including commercial transferrin, serum spiked with HRP and ovalbumin, UGP and FGP data set.
PMC7124471-1-fig5	2	13	part_of	H	406:406	arg1	N822	complement factor H		glycosites N529, N822, N882 and N1029		OGER	SpecificSite	complement factor H	P08603	glycosites N529, N822, N882 and N1029	C, D, The overlap of N-glycan masses identified on the four glycosites N432, N630 and N637 of serotransferrin and on the four glycosites N529, N822, N882 and N1029 of complement factor H in different samples including commercial transferrin, serum spiked with HRP and ovalbumin, UGP and FGP data set.
PMC7124471-1-fig5	2	13	part_of	H	406:406	arg1	N882	complement factor H		glycosites N529, N822, N882 and N1029		OGER	SpecificSite	complement factor H	P08603	glycosites N529, N822, N882 and N1029	C, D, The overlap of N-glycan masses identified on the four glycosites N432, N630 and N637 of serotransferrin and on the four glycosites N529, N822, N882 and N1029 of complement factor H in different samples including commercial transferrin, serum spiked with HRP and ovalbumin, UGP and FGP data set.
PMC7124471-1-fig5	2	13	part_of	H	406:406	arg1	N822	complement factor H		glycosites N529, N822, N882 and N1029		OGER	SpecificSite	complement factor H	P08603	glycosites N529, N822, N882 and N1029	C, D, The overlap of N-glycan masses identified on the four glycosites N432, N630 and N637 of serotransferrin and on the four glycosites N529, N822, N882 and N1029 of complement factor H in different samples including commercial transferrin, serum spiked with HRP and ovalbumin, UGP and FGP data set.
PMC7124471-1-fig5	2	13	part_of	H	406:406	arg1	N882	complement factor H		glycosites N529, N822, N882 and N1029		OGER	SpecificSite	complement factor H	P08603	glycosites N529, N822, N882 and N1029	C, D, The overlap of N-glycan masses identified on the four glycosites N432, N630 and N637 of serotransferrin and on the four glycosites N529, N822, N882 and N1029 of complement factor H in different samples including commercial transferrin, serum spiked with HRP and ovalbumin, UGP and FGP data set.
PMC7124471-1-fig5	2	13	part_of	H	406:406	arg1	N882	complement factor H		glycosites N529, N822, N882 and N1029		OGER	SpecificSite	complement factor H	P08603	glycosites N529, N822, N882 and N1029	C, D, The overlap of N-glycan masses identified on the four glycosites N432, N630 and N637 of serotransferrin and on the four glycosites N529, N822, N882 and N1029 of complement factor H in different samples including commercial transferrin, serum spiked with HRP and ovalbumin, UGP and FGP data set.
PMC7124471-1-fig5	2	33	part_of	serotransferrin	315:329	arg1	the four glycosites	serotransferrin		glycosites N432, N630 and N637		OGER	SpecificSite	serotransferrin	P02787	glycosites N432, N630 and N637	C, D, The overlap of N-glycan masses identified on the four glycosites N432, N630 and N637 of serotransferrin and on the four glycosites N529, N822, N882 and N1029 of complement factor H in different samples including commercial transferrin, serum spiked with HRP and ovalbumin, UGP and FGP data set.
PMC7124471-1-fig5	2	33	part_of	serotransferrin	315:329	arg1	N630	serotransferrin		glycosites N432, N630 and N637		OGER	SpecificSite	serotransferrin	P02787	glycosites N432, N630 and N637	C, D, The overlap of N-glycan masses identified on the four glycosites N432, N630 and N637 of serotransferrin and on the four glycosites N529, N822, N882 and N1029 of complement factor H in different samples including commercial transferrin, serum spiked with HRP and ovalbumin, UGP and FGP data set.
PMC7124471-1-fig5	2	33	part_of	serotransferrin	315:329	arg1	N432	serotransferrin		glycosites N432, N630 and N637		OGER	SpecificSite	serotransferrin	P02787	glycosites N432, N630 and N637	C, D, The overlap of N-glycan masses identified on the four glycosites N432, N630 and N637 of serotransferrin and on the four glycosites N529, N822, N882 and N1029 of complement factor H in different samples including commercial transferrin, serum spiked with HRP and ovalbumin, UGP and FGP data set.
PMC7124471-1-fig5	2	33	part_of	serotransferrin	315:329	arg1	N630	serotransferrin		glycosites N432, N630 and N637		OGER	SpecificSite	serotransferrin	P02787	glycosites N432, N630 and N637	C, D, The overlap of N-glycan masses identified on the four glycosites N432, N630 and N637 of serotransferrin and on the four glycosites N529, N822, N882 and N1029 of complement factor H in different samples including commercial transferrin, serum spiked with HRP and ovalbumin, UGP and FGP data set.
PMC7124471-1-fig5	2	33	part_of	serotransferrin	315:329	arg1	N432	serotransferrin		glycosites N432, N630 and N637		OGER	SpecificSite	serotransferrin	P02787	glycosites N432, N630 and N637	C, D, The overlap of N-glycan masses identified on the four glycosites N432, N630 and N637 of serotransferrin and on the four glycosites N529, N822, N882 and N1029 of complement factor H in different samples including commercial transferrin, serum spiked with HRP and ovalbumin, UGP and FGP data set.
PMC7124471-1-fig5	2	33	part_of	serotransferrin	315:329	arg1	N432	serotransferrin		glycosites N432, N630 and N637		OGER	SpecificSite	serotransferrin	P02787	glycosites N432, N630 and N637	C, D, The overlap of N-glycan masses identified on the four glycosites N432, N630 and N637 of serotransferrin and on the four glycosites N529, N822, N882 and N1029 of complement factor H in different samples including commercial transferrin, serum spiked with HRP and ovalbumin, UGP and FGP data set.
PMC6243375-1-4	27	60	gly	glycosylated	5056:5067	arg1	LPA	LPA				OGER		LPA	P08519		ACAN, LPA, and TNXB were heavily O‐linked glycosylated to have 82, 73, and 44 sites, respectively.
PMC6243375-1-4	27	60	gly	glycosylated	5056:5067	arg1	TNXB	TNXB				OGER		TNXB	P22105		ACAN, LPA, and TNXB were heavily O‐linked glycosylated to have 82, 73, and 44 sites, respectively.
PMC6243375-1-4	27	60	gly	glycosylated	5056:5067	arg1	ACAN	ACAN				OGER		ACAN	P16112		ACAN, LPA, and TNXB were heavily O‐linked glycosylated to have 82, 73, and 44 sites, respectively.
PMC7124471-1-fig5	1	17	gly	glycosites	176:185	arg1	B	B				Cterm		B	P02787		The number of identified N-glycan masses on each of the eight glycosites of complement factor H (A) and on each of the four glycosites of serotransferrin (B) are shown.
PMC7124471-1-fig5	1	17	gly	glycosites	176:185	arg1	serotransferrin	serotransferrin				OGER		serotransferrin	P02787		The number of identified N-glycan masses on each of the eight glycosites of complement factor H (A) and on each of the four glycosites of serotransferrin (B) are shown.
PMC7124471-1-fig5	1	22	gly	glycosites	114:123	arg1	complement factor H	complement factor H				OGER		complement factor H	P08603		The number of identified N-glycan masses on each of the eight glycosites of complement factor H (A) and on each of the four glycosites of serotransferrin (B) are shown.
PMC7124471-1-fig5	1	22	gly	glycosites	114:123	arg1	A	A				Cterm		A	P08603		The number of identified N-glycan masses on each of the eight glycosites of complement factor H (A) and on each of the four glycosites of serotransferrin (B) are shown.
PMC6243375-1-4	8	154	gly	glycosylation	1731:1743	arg1	VCAN	VCAN				OGER		VCAN	P13611		Interestingly, immunoglobulin heavy constant alpha 1 (IGHA1) has the highest PSM number in the normal tissue and serum but had the second highest PSM number in the tumor tissue where versican core protein (VCAN) scored the highest PSM number suggesting their relatively high abundance for detection and aberrant O‐linked glycosylation of VCAN in tumor tissue.
PMC7081908-1-1	1	34	gly	glycoproteins	95:107	arg1	The four gp120 glycoproteins	The four gp120 glycoproteins				OGER		gp120 glycoproteins	Q14624		The four gp120 glycoproteins included in the current study were selected on the basis of the immunogenicity analysis of a large panel of HIV-1 Env variants (16) and were included in a polyvalent DNA prime-protein boost HIV vaccine formulation currently going through a phase I clinical study at HVTN (HVTN124).
PMC5643531-1-9	5	109	gly	glycosylation	744:756	arg1	Fz8	Fz8				OGER		Fz8	Q9H461		These results demonstrate that glycosylation of Fz8 could be an essential factor in its membrane targeting.
PMC5643531-1-fig7	0	35	gly	N-glycosylation	9:23	arg1	Fz8 receptor	Fz8 receptor				OGER		Fz8 receptor	Q9H461		Putative N-glycosylation sites of Fz8 receptor are important for Wnt8 signaling.
PMC5457524-1-1	3	207	gly	SNAP	417:420	arg1	the SNAP tag	SNAP			the SNAP tag	OGER		SNAP	P60880		The human Fbs1 sugar-binding domain (residues 92–296, hereafter referred as Fbs1) was expressed as a fusion to the C-terminus of the SNAP tag to facilitate its immobilization to beads35.
PMC5643531-1-8	3	62	gly	glycosylation	465:477	arg1	Fz8	Fz8				OGER		Fz8	Q9H461		Since OTG interacts and co-localizes with Fz8 in the ER, we speculated that OTG may influence glycosylation and maturation of Fz8.
PMC5457524-1-3	7	5	gly	Fbs1–glycoprotein	1340:1356	arg1	high- and low-affinity Fbs1–glycoprotein interactions	high- and low-affinity Fbs1–glycoprotein interactions				OGER		Fbs1	Q9HAH7		Much higher levels of plasmid were captured with RNase B beads, indicating that the plasmid display system can differentiate between high- and low-affinity Fbs1–glycoprotein interactions.
PMC5795011-1-4	64	181	gly	glycosylation	11134:11146	arg1	serum alpha-1-acid glycoprotein 1	serum alpha-1-acid glycoprotein 1				OGER		alpha-1-acid glycoprotein 1	P02763		For example, Mascot annotated a total of nine different mono-, di-, tri- and tetra-sialylated N-glycan structures on a single glycosylation site (Asn 93) of serum alpha-1-acid glycoprotein 1 (Fig. 5).
PMC5795011-1-4	64	295	gly	glycoprotein	11184:11195	arg1	serum alpha-1-acid glycoprotein 1	serum alpha-1-acid glycoprotein 1				OGER		alpha-1-acid glycoprotein 1	P02763		For example, Mascot annotated a total of nine different mono-, di-, tri- and tetra-sialylated N-glycan structures on a single glycosylation site (Asn 93) of serum alpha-1-acid glycoprotein 1 (Fig. 5).
PMC5643531-1-8	8	2	gly	glycosylation	987:999	arg1	Fz8	Fz8				OGER		Fz8	Q9H461		We also tested whether OTG affected glycosylation of Fz8.
PMC7124471-1-11	72	22	gly	serotransferrin	10121:10135	arg1	Hex5HexNAc4NANA2	serotransferrin			Hex5HexNAc4NANA2	OGER		serotransferrin	P02787		In the serum of patient with CDG-1a, the loss of an entire oligosaccharide moiety, i.e. Hex5HexNAc4NANA2 from serotransferrin was identified by MS. In our result, this glycan is identified on all the five glycosites of serotransferrin.
PMC7124471-1-11	72	236	gly	glycosites	10216:10225	arg1	serotransferrin	serotransferrin				OGER		serotransferrin	P02787		In the serum of patient with CDG-1a, the loss of an entire oligosaccharide moiety, i.e. Hex5HexNAc4NANA2 from serotransferrin was identified by MS. In our result, this glycan is identified on all the five glycosites of serotransferrin.
PMC6243375-1-5	9	75	gly	glycoprotein	1740:1751	arg1	fibulin‐2	fibulin‐2				OGER		fibulin‐2	P98095		In addition to VCAN and ACAN, an average of 4.3‐fold increase was detected in 14 sites across fibulin‐2 (FBLN2), a glycoprotein known to be involved in stabilizing the VCAN and ACAN network for growth and metastasis of tumor (Olin et al, 2001; Baird et al, 2013; Fig 3D and Appendix Table S1).
PMC5457524-1-3	19	64	gly	B	3217:3217	arg1	IV	RNase B			IV	OGER		RNase B	P07998		Mizushima et al.3738 previously reported that Man(IV) of RNase B forms a hydrogen bond with the sidechain Nδ atom of Asn-159 of mouse Fbs1.
PMC5457524-1-3	19	64	gly	B	3217:3217	arg1	Man	RNase B			Man	OGER		RNase B	P07998		Mizushima et al.3738 previously reported that Man(IV) of RNase B forms a hydrogen bond with the sidechain Nδ atom of Asn-159 of mouse Fbs1.
PMC5795011-1-fig5	0	6	part_of	glycoprotein	162:173	arg1	Asn 93	alpha-1-acid glycoprotein 1		Asn 93		OGER	SpecificSite	alpha-1-acid glycoprotein 1	P02763	Asn 93	Annotation of nine different glycan structures with varied degree of complexity and sialylation by Mascot on a single glycosylation site (Asn 93) of alpha-1-acid glycoprotein 1 in serum.
PMC5643531-1-fig6	0	2	gly	glycosylation	14:26	arg1	Fz8 receptor	Fz8 receptor				OGER		Fz8 receptor	Q9H461		OTG regulates glycosylation of Fz8 receptor.
PMC7124471-1-10	7	49	part_of	H	830:830	arg1	N882	complement factor H		N529, N822, N882, and N1029		OGER	SpecificSite	complement factor H	P08603	N529, N822, N882, and N1029	The number of N-glycans on N529, N822, N882, and N1029 of complement factor H also varied among serum spiked with glycoproteins, UGP and FGP data set (Fig. 6D).
PMC7124471-1-10	7	49	part_of	H	830:830	arg1	N1029	complement factor H		N529, N822, N882, and N1029		OGER	SpecificSite	complement factor H	P08603	N529, N822, N882, and N1029	The number of N-glycans on N529, N822, N882, and N1029 of complement factor H also varied among serum spiked with glycoproteins, UGP and FGP data set (Fig. 6D).
PMC7124471-1-10	7	49	part_of	H	830:830	arg1	N822	complement factor H		N529, N822, N882, and N1029		OGER	SpecificSite	complement factor H	P08603	N529, N822, N882, and N1029	The number of N-glycans on N529, N822, N882, and N1029 of complement factor H also varied among serum spiked with glycoproteins, UGP and FGP data set (Fig. 6D).
PMC7124471-1-10	7	49	part_of	H	830:830	arg1	N1029	complement factor H		N529, N822, N882, and N1029		OGER	SpecificSite	complement factor H	P08603	N529, N822, N882, and N1029	The number of N-glycans on N529, N822, N882, and N1029 of complement factor H also varied among serum spiked with glycoproteins, UGP and FGP data set (Fig. 6D).
PMC7124471-1-10	7	49	part_of	H	830:830	arg1	N822	complement factor H		N529, N822, N882, and N1029		OGER	SpecificSite	complement factor H	P08603	N529, N822, N882, and N1029	The number of N-glycans on N529, N822, N882, and N1029 of complement factor H also varied among serum spiked with glycoproteins, UGP and FGP data set (Fig. 6D).
PMC7124471-1-10	7	49	part_of	H	830:830	arg1	N822	complement factor H		N529, N822, N882, and N1029		OGER	SpecificSite	complement factor H	P08603	N529, N822, N882, and N1029	The number of N-glycans on N529, N822, N882, and N1029 of complement factor H also varied among serum spiked with glycoproteins, UGP and FGP data set (Fig. 6D).
PMC7143757-1-1	17	59	gly	glycosylated	1907:1918	arg1	glycosylated CTB4573H	CTB4573H (CTB				OGER		CTB4573H (CTB	Q01459		The higher MW band of glycosylated CTB4573H (CTB-OPSBa) was detected by both antibodies, while the lower band was not observed because of the poor immunogenicity of short-chain OPS (Figure 1B).
PMC5976746-1-5	41	215	gly	glycosylation	6491:6503	arg1	BG505 NFL	BG505 NFL				OGER		BG505 NFL	P07196		A comparison of glycosylation profiles of BG505 NFL and BG505 SOSIP both expressed from CHO cells, but purified differently, was also performed (35).
PMC5976746-1-5	41	215	gly	glycosylation	6491:6503	arg1	BG505 SOSIP	BG505 SOSIP				Cterm		BG505 SOSIP			A comparison of glycosylation profiles of BG505 NFL and BG505 SOSIP both expressed from CHO cells, but purified differently, was also performed (35).
PMC3938046-1-9	3	8	gly	N-glycosylated	478:491	arg1	Prkar1a/b	Prkar1a/b				OGER		Prkar1a	P10644		Further, several membrane proteins and N-glycosylated proteins (Ctnnb1, Abcc8, Stat3, Basp1, Acadvl, Prkar1a/b, and Flnb) were detected in the crude membrane-enriched fractions.
PMC3938046-1-9	3	8	gly	N-glycosylated	478:491	arg1	Stat3	Stat3				OGER		Stat3	P40763		Further, several membrane proteins and N-glycosylated proteins (Ctnnb1, Abcc8, Stat3, Basp1, Acadvl, Prkar1a/b, and Flnb) were detected in the crude membrane-enriched fractions.
PMC3938046-1-9	3	8	gly	N-glycosylated	478:491	arg1	Basp1	Basp1				OGER		Basp1	P80723		Further, several membrane proteins and N-glycosylated proteins (Ctnnb1, Abcc8, Stat3, Basp1, Acadvl, Prkar1a/b, and Flnb) were detected in the crude membrane-enriched fractions.
PMC3938046-1-9	3	8	gly	N-glycosylated	478:491	arg1	Flnb	Flnb				OGER		Flnb	O75369		Further, several membrane proteins and N-glycosylated proteins (Ctnnb1, Abcc8, Stat3, Basp1, Acadvl, Prkar1a/b, and Flnb) were detected in the crude membrane-enriched fractions.
PMC3938046-1-9	3	8	gly	N-glycosylated	478:491	arg1	Ctnnb1	Ctnnb1				OGER		Ctnnb1	P35222		Further, several membrane proteins and N-glycosylated proteins (Ctnnb1, Abcc8, Stat3, Basp1, Acadvl, Prkar1a/b, and Flnb) were detected in the crude membrane-enriched fractions.
PMC3938046-1-9	3	8	gly	N-glycosylated	478:491	arg1	Abcc8	Abcc8				OGER		Abcc8	Q09428		Further, several membrane proteins and N-glycosylated proteins (Ctnnb1, Abcc8, Stat3, Basp1, Acadvl, Prkar1a/b, and Flnb) were detected in the crude membrane-enriched fractions.
PMC3938046-1-9	3	8	gly	N-glycosylated	478:491	arg1	Acadvl	Acadvl				OGER		Acadvl	P49748		Further, several membrane proteins and N-glycosylated proteins (Ctnnb1, Abcc8, Stat3, Basp1, Acadvl, Prkar1a/b, and Flnb) were detected in the crude membrane-enriched fractions.
PMC7124471-1-7	13	20	gly	N-glycosylation	1603:1617	arg1	CFH	CFH				OGER		CFH	P08603		This suggested that N-glycosylation of CFH was site-specific.
PMC3942810-2-2	3	57	gly	N-glycosylated	460:473	arg1	RJ	RJ				Cterm		RJ			To the best of our knowledge, this is the most comprehensive assignment of the N-glycosylated sites of RJ.
PMC7124471-1-10	6	59	gly	glycosites	618:627	arg1	serotransferrin	serotransferrin				OGER		serotransferrin	P02787		The number of N-glycans on those glycosites of serotransferrin varied among commercial serotransferrin, serum spiked with glycoproteins, UGP and FGP data set (Fig. 6C).
PMC7107550-1-4	19	241	gly	SMs	4138:4140	arg1	all	SMs			all	OGER		SMs	P52788		Because all of the sequences obtained from the database were the result of one or several accidental transmissions from SMs to RMs of a single SIVsm subtype (8) only recently described (Apetrei et al. 2005, 2006), we cannot rule out the alternative hypotheses that this site is not polymorphic in the SIVsm subtype-8 envelope or that this polymorphism was fixed in RMs due to an extreme bottleneck upon transmission.
PMC2762462-1-1	2	73	gly	glycoprotein	406:417	arg1	ST6	ST6				OGER		ST6	P27701		Like other sialyltransferases, ST6 is a type II transmembrane glycoprotein, comprised of a short N-terminal cytosolic tail, a hydrophobic signal-anchor sequence that is embedded in the membrane, a so-called "stem" region, and a long C-terminal catalytic domain that is exposed to the lumen of the Golgi apparatus.
PMC7124471-1-10	20	27	gly	N-glycosylation	2237:2251	arg1	serotransferrin	serotransferrin				OGER		serotransferrin	P02787		From the site-specific glycoform result of serotransferrin, it is easy to obtain a structure-function perspective of N-glycosylation of serotransferrin in pathogen-host interaction.
PMC7124471-1-6	7	18	gly	glycoproteins	1016:1028	arg1	QSOX1	QSOX1				OGER		QSOX1	O00391		Among the 16 proteins, there are four glycoproteins including IOVO, Ogchi, OVAL and QSOX1, and most of the GPSMs identified from this sample were from IOVO instead of OVAL (supplemental Table S19).
PMC5795011-1-4	4	303	gly	glycoprotein	927:938	arg1	serum alpha-1-acid glycoprotein 1	serum alpha-1-acid glycoprotein 1				OGER		alpha-1-acid glycoprotein 1	P02763		The result of the described strategy for large scale automated glycopeptide analysis of LC-MS datasets was demonstrated by serum alpha-1-acid glycoprotein 1 (A1AG1) as an example.
PMC5795011-1-4	4	303	gly	glycoprotein	927:938	arg1	A1AG1	A1AG1				Cterm		A1AG1	P02763		The result of the described strategy for large scale automated glycopeptide analysis of LC-MS datasets was demonstrated by serum alpha-1-acid glycoprotein 1 (A1AG1) as an example.
PMC5457524-1-3	19	124	part_of	Fbs1	3288:3291	arg1	Asn-159	Fbs1		Asn-159		OGER	SpecificSite	Fbs1	Q9HAH7	Asn-159	Mizushima et al.3738 previously reported that Man(IV) of RNase B forms a hydrogen bond with the sidechain Nδ atom of Asn-159 of mouse Fbs1.
PMC7081908-1-5	7	101	gly	glycosylation	1555:1567	arg1	recombinant gp120 proteins	recombinant gp120 proteins				OGER		gp120 proteins	Q14624		This report presents the first extensive comparison of glycosylation patterns of recombinant gp120 proteins from four clades of HIV-1 in two different cell lines, grown either at laboratory scale or under 50-liter GMP conditions, purified using different methods, and in two GMP lots prepared under identical conditions.
PMC6934601-1-7	12	104	gly	highly-glycosylated	1816:1834	arg1	SPN	SPN				OGER		SPN	P16150		In particular, our findings uncover a role for highly-glycosylated cell surface molecules (SPN and MUC1) in hindering CD3 bsAb-induced T cell-tumor cell clustering and consequent tumor cell lysis.
PMC7124471-1-11	81	111	gly	glycoform	11348:11356	arg1	serotransferrin glycoform	serotransferrin glycoform				OGER		serotransferrin	P02787		This can be achieved by in-depth analysis of serotransferrin glycoform and the binding affinity of each glycan to TbpA.
PMC5976746-1-5	80	53	gly	homogeneity	13916:13926	arg1	the CHO-M-derived BG505 NFL	the CHO-M-derived BG505 NFL				OGER		BG505 NFL trimers	P07196		High homogeneity, low V3 exposure, and low F105 binding of the CHO-M-derived BG505 NFL trimers contributed to elicitation of robust tier 2 and low tier 1 neutralization when formulated in ISCOMATRIX and inoculated into rabbits.
PMC5795011-1-fig5	0	8	gly	glycoprotein	162:173	arg1	alpha-1-acid glycoprotein 1	alpha-1-acid glycoprotein 1				OGER		alpha-1-acid glycoprotein 1	P02763		Annotation of nine different glycan structures with varied degree of complexity and sialylation by Mascot on a single glycosylation site (Asn 93) of alpha-1-acid glycoprotein 1 in serum.
PMC5795011-1-fig5	0	26	gly	glycosylation	118:130	arg1	alpha-1-acid glycoprotein 1	alpha-1-acid glycoprotein 1				OGER		alpha-1-acid glycoprotein 1	P02763		Annotation of nine different glycan structures with varied degree of complexity and sialylation by Mascot on a single glycosylation site (Asn 93) of alpha-1-acid glycoprotein 1 in serum.
PMC5795011-1-fig5	0	34	gly	varied	52:57	arg1	alpha-1-acid glycoprotein 1	alpha-1-acid glycoprotein 1				OGER		alpha-1-acid glycoprotein 1	P02763		Annotation of nine different glycan structures with varied degree of complexity and sialylation by Mascot on a single glycosylation site (Asn 93) of alpha-1-acid glycoprotein 1 in serum.
PMC7124471-1-10	19	60	gly	N-glycosites	2001:2012	arg1	serotransferrin	serotransferrin				OGER		serotransferrin	P02787		In this regard, the number of N-glycan mass identified on the four N-glycosites of serotransferrin might indicate the accessibility of each site to OSTs and their functional importance.
PMC5795011-1-4	19	760	gly	glycopeptide	3264:3275	arg1	alpha-2-macroglobulin	alpha-2-macroglobulin				OGER		alpha-2-macroglobulin	P01023		As opposed to the above examples, Mascot annotated the fucose residue to the core HexNAc of a di-sialylated bi-antennary glycopeptide of alpha-2-macroglobulin.
