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
31759178	5	81	part_of	23 N-glycosites	1266:1280	arg1	19 intact N-glycoproteins	N-glycoproteins		23 N-glycosites		Fterm	Site	N-glycoproteins		23 N-glycosites	With the criteria of quantified at least thrice out of the five technical replicates with no <1.5-fold change, p ≤ .05 and RSD ≤ 20%, 56 DEGPs were quantified from 23 N-glycosites on 19 intact N-glycoproteins.
31411531	8	23	gly	sialylated	1529:1538	arg1	the major sialylated glycan				the major sialylated glycan						The alpha 2,6-linked sialic acid on the 3-arm (the major sialylated glycan in human-derived IgG), and the alpha 2,3-linked sialic acid on the 3-arm, do not have this destabilizing effect.
30983332	5	41	gly	fucosylated	820:830	arg1	a highly fucosylated and xylosylated galactose backbone				a highly fucosylated and xylosylated galactose backbone						The mucilage contains a single heterogeneous polysaccharide composed of a highly fucosylated and xylosylated galactose backbone with arabinan and mannoglucuronan branches.
31386359	2	9	gly	glycopeptide	294:305	arg2	glycopeptide			glycopeptide						glycopeptide	Peptidoglycan is assembled from a glycopeptide precursor, Lipid II, that is polymerized by peptidoglycan glycosyltransferases into glycan strands that are subsequently cross-linked to form the mature cell wall.
29956878	6	12	gly	core-fucosylated	651:666	arg1	Three biantennary core-fucosylated N-glycan azides				Three biantennary core-fucosylated N-glycan azides						Three biantennary core-fucosylated N-glycan azides of 8 to 12 sugars were cocrystallized with PhoSL.
30673210	7	53	gly	N-glycosylation	1401:1415	arg2	270 unique N-glycosylation sites			270 unique N-glycosylation sites						sites	In addition, 270 unique N-glycosylation sites of 400 unique glycopeptides from 146 glycosylated proteins were identified from the triplicate analysis of 2 μL human serum.
30673210	7	88	gly	glycosylated	1460:1471	arg1	146 glycosylated proteins	146 glycosylated proteins				Fterm		proteins			In addition, 270 unique N-glycosylation sites of 400 unique glycopeptides from 146 glycosylated proteins were identified from the triplicate analysis of 2 μL human serum.
30673210	7	1	gly	glycopeptides	1437:1449	arg1	146 glycosylated proteins	proteins		glycopeptides		Fterm		proteins		glycopeptides	In addition, 270 unique N-glycosylation sites of 400 unique glycopeptides from 146 glycosylated proteins were identified from the triplicate analysis of 2 μL human serum.
30673210	7	53	gly	N-glycosylation	1401:1415	arg1	400 unique glycopeptides			glycopeptides						glycopeptides	In addition, 270 unique N-glycosylation sites of 400 unique glycopeptides from 146 glycosylated proteins were identified from the triplicate analysis of 2 μL human serum.
31501225	0	75	gly	N-glycopeptide	0:13	arg2	N-glycopeptide Signatures			N-glycopeptide Signatures						N-glycopeptide	N-glycopeptide Signatures of IgA2 in Serum from Patients with Hepatitis B Virus-related Liver Diseases.
29671439	0	41	gly	glycoprotein	42:53	arg1	N-linked glycoprotein	N-linked glycoprotein				Fterm		glycoprotein			MALDI-TOF-MS characterization of N-linked glycoprotein derived from ginger with ACE inhibitory activity.
29437979	2	123	gly	glycoprotein	394:405	arg1	the alphaherpesvirus pseudorabies virus (PrV) glycoprotein H	the alphaherpesvirus pseudorabies virus (PrV) glycoprotein H				Fterm		glycoprotein H			Here, we systematically analyzed the functional relevance of N-linked glycans in the alphaherpesvirus pseudorabies virus (PrV) glycoprotein H (gH), which is an essential component of the conserved core herpesvirus fusion machinery.
31987138	7	8	gly	N-glycopeptides	1242:1256	arg2	N-glycopeptides			N-glycopeptides						N-glycopeptides	Also, the great enrichment performance for N-glycopeptides were obtained in terms of sensitivity (low fmol levels), selectivity (extracting N-glycopeptides from the mixture of glycopeptides and non-glycopeptides at a 1:100 molar ratio) and reproducibility (CVs<26%).
31987138	7	36	gly	non-glycopeptides	1296:1312	arg2	non-glycopeptides			non-glycopeptides						glycopeptides and non-glycopeptides	Also, the great enrichment performance for N-glycopeptides were obtained in terms of sensitivity (low fmol levels), selectivity (extracting N-glycopeptides from the mixture of glycopeptides and non-glycopeptides at a 1:100 molar ratio) and reproducibility (CVs<26%).
31987138	7	37	gly	glycopeptides	1278:1290	arg2	glycopeptides			glycopeptides						glycopeptides and non-glycopeptides	Also, the great enrichment performance for N-glycopeptides were obtained in terms of sensitivity (low fmol levels), selectivity (extracting N-glycopeptides from the mixture of glycopeptides and non-glycopeptides at a 1:100 molar ratio) and reproducibility (CVs<26%).
31987138	7	65	gly	N-glycopeptides	1145:1159	arg2	N-glycopeptides			N-glycopeptides						N-glycopeptides	Also, the great enrichment performance for N-glycopeptides were obtained in terms of sensitivity (low fmol levels), selectivity (extracting N-glycopeptides from the mixture of glycopeptides and non-glycopeptides at a 1:100 molar ratio) and reproducibility (CVs<26%).
29675740	5	2	gly	glycopeptides	1129:1141	arg2	sample glycopeptides			sample glycopeptides						glycopeptides	To increase the number of identified peptide, fractionation of sample glycopeptides for reduction of sample complexity is required.
31311856	5	18	gly	O-mannosylated	1142:1155	arg1	an O-mannosylated protein	an O-mannosylated protein				Fterm		protein			Deletion of the cyc8 gene, which encodes for a general transcription repressor, resulted in the accumulation of excessive amounts of free O-glycans, concomitant with a severe growth defect, a reduction in the level of an O-mannosylated protein, and compromised cell wall integrity.
29642453	3	59	gly	glycosylation	439:451	arg1	NA	NA		sites		Cterm		NA	4758	sites	We monitored the potential N-linked glycosylation (NLG) sites of over 10,000 HA and NA of H1N1 subtype isolated from human, avian, and swine species over the past century.
31154130	1	23	gly	glycoproteins	224:236	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Glycosylation plays an important role in the maintenance of the structure and function of glycoproteins, while aberrant protein glycosylation is correlated with various diseases.
29299842	5	28	gly	glycosylation	661:673	arg1	defining glycan structure characteristics				defining glycan structure characteristics						Thus, a comprehensive understanding of protein glycosylation in various yeast species and defining glycan structure characteristics can provide useful information for their biotechnological and clinical implications.
30611426	5	9	gly	glycoproteins	811:823	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Furthermore, glycoproteins and in particular the glycan moieties themselves often exhibit a high degree of conformational heterogeneity.
29671439	3	9	gly	glycoproteins	399:411	arg1	the enriched glycoproteins	the enriched glycoproteins				Fterm		glycoproteins			The N-linked glycans released from the enriched glycoproteins by PNGase F are identified by MALDI-TOF-MS.
29671439	3	50	gly	released	372:379	arg1	the enriched glycoproteins AND The N-linked glycans	the enriched glycoproteins			The N-linked glycans	Fterm		glycoproteins			The N-linked glycans released from the enriched glycoproteins by PNGase F are identified by MALDI-TOF-MS.
31325506	6	11	gly	fucosylated	1385:1395	arg1	two sulfated glycans				two sulfated glycans						Of these, ten glycans (77.2%), including two sulfated glycans (8.0%), were core fucosylated, which confer unique biological functions to glycoproteins.
31325506	6	11	gly	fucosylated	1385:1395	arg1	ten glycans				ten glycans						Of these, ten glycans (77.2%), including two sulfated glycans (8.0%), were core fucosylated, which confer unique biological functions to glycoproteins.
31325506	6	11	gly	fucosylated	1385:1395	arg1	77.2%				77.2%						Of these, ten glycans (77.2%), including two sulfated glycans (8.0%), were core fucosylated, which confer unique biological functions to glycoproteins.
31325506	6	29	gly	glycoproteins	1442:1454	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Of these, ten glycans (77.2%), including two sulfated glycans (8.0%), were core fucosylated, which confer unique biological functions to glycoproteins.
30935958	0	91	gly	N-glycosylation	10:24	arg2	N-glycosylation site variants			N-glycosylation site variants						site	Impact of N-glycosylation site variants during human PrP aggregation and fibril nucleation.
29587225	1	7	gly	glycoprotein	186:197	arg1	a therapeutic glycoprotein	a therapeutic glycoprotein				Fterm		glycoprotein			Recombinant human erythropoietin (EPO) is a therapeutic glycoprotein widely used for treating anemia.
30611426	4	48	part_of	glycoprotein	772:783	arg1	glycoprotein composition	glycoprotein		glycoprotein composition		Fterm	Site	glycoprotein		position	However, the ability to study the structure of glycoproteins to high resolution was historically limited by technical barriers including a limited availability of appropriate recombinant protein expression platforms, limited methods to generate compositional homogeneity, and difficulties analyzing glycoprotein composition.
31611356	6	56	part_of	CD4	1181:1183	arg1	the CD4 binding site	CD4		the CD4 binding site		PUBTATOR	Site	CD4	920	site	Grft's ability to alter the structure of gp120, exposing the CD4 binding site, correlated with the presence of glycosylation at N295 only in clade B strains, not clade C strains.
31813565	8	70	gly	glycopeptides	1723:1735	arg2	low-abundance N-linked glycopeptides			low-abundance N-linked glycopeptides						glycopeptides	These results showed the promising application of magMOF@Au-maltose in the detection and identification of low-abundance N-linked glycopeptides in complex biological samples.
31121093	4	34	part_of	heparin	685:691	arg1	monodisperse fragments	heparin		monodisperse fragments		Fterm	Site	heparin		fragments	Our results indicate that the nanopore/SVM technique could distinguish between monodisperse fragments of heparin and chondroitin sulfate with high accuracy (>90%), allowing as low as 0.8% (w/w) of chondroitin sulfate impurities in a heparin sample to be detected.
31154130	7	2	part_of	IgG-Fc	1132:1137	arg1	83 IgG-Fc glycopeptides	83 Ig		glycopeptides		Cterm	Site	83 Ig		glycopeptides	As a result, 83 IgG-Fc glycopeptides from human serum, including 17 sialylated glycopeptides, were identified.
30988258	2	25	gly	attached	310:317	arg1	asparagine residues AND linked carbohydrate residues			asparagine residues	linked carbohydrate residues					asparagine residues	N-Glycosylation trees are complex structures of linked carbohydrate residues attached to asparagine residues.
29620509	2	96	part_of	phosphatase	355:365	arg1	the N terminus	phosphatase		the N terminus		Fterm	Site	phosphatase		terminus	Methods First, cDNA sequences encoding the extracellular domain of Necls were cloned into the modified vector pAPtag at the N terminus of alkaline phosphatase (AP) for fusion expression.
30802037	8	70	gly	O-glycopeptides	1349:1363	arg2	O-glycopeptides			O-glycopeptides						O-glycopeptides	It was found that this method had much decreased search space and had excellent sensitivity in the identification of O-glycopeptides.
31541622	4	55	gly	glycoproteins	521:533	arg1	such glycoproteins	such glycoproteins				Fterm		glycoproteins			Identifying such glycoproteins is essential to understanding the mechanisms of viral infection, as well as developing antiviral strategies.
29444271	0	42	gly	residue	157:163	arg1	plant N-glycans			residue in	plant N-glycans					residue in	Molecular characterization of second tomato α1,3/4-fucosidase (α-Fuc'ase Sl-2), a member of glycosyl hydrolase family 29 active toward the core α1,3-fucosyl residue in plant N-glycans.
31062865	3	70	gly	O-glycopeptide	919:932	arg2	O-glycopeptide profiling			O-glycopeptide profiling						O-glycopeptide	EPO-Fc, containing the Fc region of immunoglobulin G1 (IgG1) fused to EPO, was harvested at Day 5 and 8 of a batch cell culture process followed by purification and N- and O-glycopeptide profiling.
30802037	4	82	gly	O-glycopeptide	802:815	arg2	O-glycopeptide HCD spectra			O-glycopeptide HCD spectra						O-glycopeptide	In this study, we present a novel approach, termed as O-Search, for the interpretation of O-glycopeptide HCD spectra.
31733242	4	1	part_of	Araf	623:626	arg1	Xylp, and Araf residues	Araf		Xylp, and Araf residues		OGER	Site	Araf	P10398	residues	PSPC is a neutral arabinoxylan, composed of a β-(1,3)/β-(1,4)-d-xylan backbone with side chains of Xylp, and Araf residues attached in O-2 and O-3 positions.
29580922	5	48	gly	glycopeptides	823:835	arg2	glycopeptides			glycopeptides						glycopeptides	Peak area ratios of glycopeptides to corresponding normalising peptides were subjected to orthogonal projections to latent structures discriminant analysis (OPLS-DA).
30737276	10	2	gly	residues	1703:1710	arg1	the PBCV-1 MCP N-glycans			residues	the PBCV-1 MCP N-glycans					residues	Our results uncover GT activities that assemble four of the nine residues of the PBCV-1 MCP N-glycans.
30708332	0	2	part_of	protein	54:60	arg1	Thermal decomposition	protein		Thermal decomposition		Fterm	Site	protein		position	Thermal decomposition of castor oil, corn starch, soy protein, lignin, xylan, and cellulose during fast pyrolysis.
30708332	0	8	part_of	lignin	63:68	arg1	Thermal decomposition	lignin		Thermal decomposition		Fterm	Site	lignin		position	Thermal decomposition of castor oil, corn starch, soy protein, lignin, xylan, and cellulose during fast pyrolysis.
31888963	11	75	gly	sites	1905:1909	arg1	N145			N64 and N145						N64 and N145	The additional analysis of CD32a from monocytes revealed different features than observed for CD16a including the presence of a predominantly biantennary complex-type N-glycans with two sialic acids at both sites (N64 and N145).
31888963	11	78	gly	sites	1905:1909	arg1	two sialic acids			sites	two sialic acids					sites	The additional analysis of CD32a from monocytes revealed different features than observed for CD16a including the presence of a predominantly biantennary complex-type N-glycans with two sialic acids at both sites (N64 and N145).
31507595	1	49	part_of	Human	88:92	arg1	a small glycopeptide	Human CD52		a small glycopeptide		PUBTATOR	Site	Human CD52	P31358	glycopeptide	Human CD52 is a small glycopeptide (12 amino acid residues) with one N-linked glycosylation site at asparagine 3 (Asn3) and several potential O-glycosylation serine/threonine sites.
30305426	9	0	gly	sugars	1504:1509	arg1	proteins	proteins			sugars	Fterm		proteins			Moreover, because the sugars on cell-surface proteins or on proteins secreted from an XBP1s-activated cell can be molecularly distinct from those of an unactivated cell, these findings reveal a potential new mechanism for translating intracellular stress signaling into altered interactions with the extracellular environment.
31453603	7	38	gly	glycopeptides	1308:1320	arg2	the glycopeptides			the glycopeptides						glycopeptides	Glycan size and composition emerged as a decisive factor in dictating the CCS space occupied by the glycopeptides and exerted this influence in a charge state dependent fashion.
29751008	3	85	gly	glycoproteins	719:731	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Comparison of these results with recently published physicochemical stability and Fcγ receptor binding data with the same set of glycoproteins provide improved insights into correlations between glycan structure and these pharmaceutical properties.
30565163	2	77	gly	sialylated	577:586	arg1	such sialylated oligosaccharide isomers				such sialylated oligosaccharide isomers						Building on a study by Cotter and coworkers on analysis of sialylated oligosaccharides using atmospheric pressure-matrix-assisted laser-induced tandem mass spectrometry (MS/MS), we show that library search methods enable the automated differentiation of such sialylated oligosaccharide isomers using MS/MS derived from electrospray collision-induced dissociation in ion trap and beam-type fragmentation mass spectrometers.
30565163	2	91	gly	sialylated	377:386	arg1	sialylated oligosaccharides				sialylated oligosaccharides						Building on a study by Cotter and coworkers on analysis of sialylated oligosaccharides using atmospheric pressure-matrix-assisted laser-induced tandem mass spectrometry (MS/MS), we show that library search methods enable the automated differentiation of such sialylated oligosaccharide isomers using MS/MS derived from electrospray collision-induced dissociation in ion trap and beam-type fragmentation mass spectrometers.
32110292	1	31	gly	glycoproteins	174:186	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Immunoglobulin G (IgG), which contains four subclasses (IgG1-4), is one of the most important classes of glycoproteins in the immune system.
30448401	0	20	gly	Deficiency	47:56	arg1	Ocular Autoimmune Disease	Disease			Deficiency	Fterm		Disease			Inflammatory Stress Causes N-Glycan Processing Deficiency in Ocular Autoimmune Disease.
30612271	3	39	gly	glycoprotein	498:509	arg1	a type I transmembrane glycoprotein	a type I transmembrane glycoprotein				Fterm		glycoprotein			RAGE, a type I transmembrane glycoprotein, was identified as a receptor for AGEs.
30714583	6	45	gly	glycoforms	878:887	arg1	GlcNAc				GlcNAc						Then, we performed binary logistic regression to screen out three bisecting N-acetylglucosamine (GlcNAc) glycoforms for distinguishing between OA and RA.
30714583	6	45	gly	glycoforms	878:887	arg1	bisecting N-acetylglucosamine				bisecting N-acetylglucosamine						Then, we performed binary logistic regression to screen out three bisecting N-acetylglucosamine (GlcNAc) glycoforms for distinguishing between OA and RA.
31316527	6	71	part_of	CMG2	1020:1023	arg1	its CMG2 domain	CMG2		its CMG2 domain		OGER	Site	CMG2	P58335	domain	The decoy protein binds to the protective antigen (PA) of anthrax through its CMG2 domain and inhibits toxin endocytosis.
29619832	2	12	part_of	contains	348:355	arg1	This glycoprotein AND three predicted N-linked glycosylation sites	This glycoprotein		three predicted N-linked glycosylation sites		Fterm	Site	glycoprotein		sites	This glycoprotein contains three predicted N-linked glycosylation sites; one is near the protein's active site, and at least one more is known to facilitate the protein's secretion.
31606074	4	25	gly	glycosylated	379:390	arg1	glycosylated endogenous signaling peptides			glycosylated endogenous signaling peptides						peptides	Less attention has been focused on glycosylated endogenous signaling peptides due to their low abundance, structural heterogeneity and the lack of enabling analytical tools.
31514875	0	29	gly	heterogeneity	89:101	arg1	a protein	a protein				Fterm		protein			Development of Immobilized Enzyme Reactors for the characterization of the glycosylation heterogeneity of a protein.
31514875	0	75	gly	glycosylation	75:87	arg1	a protein	a protein				Fterm		protein			Development of Immobilized Enzyme Reactors for the characterization of the glycosylation heterogeneity of a protein.
30395580	4	63	gly	carries	724:730	arg1	The recombinant protein AND 13.5 kDa N-linked glycans	The recombinant protein			13.5 kDa N-linked glycans	Fterm		protein			The recombinant protein produced in A. oryzae has a molecular mass of 75 kDa, a pI of 4.2 and carries 13.5 kDa N-linked glycans.
29299842	6	16	gly	glycoproteins	984:996	arg1	recombinant glycoproteins	recombinant glycoproteins				Fterm		glycoproteins			Yeast-specific glycans are a target for glyco-engineering; implementing human-type glycosylation pathways in yeast can aid the production of recombinant glycoproteins with therapeutic potential.
31040271	5	5	gly	sialylated	990:999	arg1	an α2-3 sialylated glycoform				an α2-3 sialylated glycoform						We demonstrate distinct circulation time and organ distribution of selected glycoforms of α-galactosidase A in a Fabry disease mouse model, and find that an α2-3 sialylated glycoform designed to eliminate uptake by the mannose 6-phosphate and mannose receptors exhibits improved circulation time and targeting to hard-to-reach organs such as heart.
29343613	5	39	gly	lectin	856:861	arg1	a single glycan-binding site	lectin			a single glycan-binding site	Fterm		lectin			MVN is a monovalent lectin with a single glycan-binding site in gp120, is structurally similar to CVN and exhibits no toxicity or mitogenicity, both of which are liabilities with CVN.
30311906	6	40	gly	glycoproteins	868:880	arg1	glycoproteins	glycoproteins			high N-glycans multiplicity	Fterm		glycoproteins			Using proteomic approaches, we identified that Srd5a3 loss affects a subset of glycoproteins with high N-glycans multiplicity per protein and decreased protein abundance or N-glycosylation level.
30315106	4	87	gly	O-glycosylated	689:702	arg1	the highly O-glycosylated, mucin-like C terminus			the highly O-glycosylated, mucin-like C terminus						terminus	The monoclonal antibody mAb16D10 was previously reported to detect a glycotope in the highly O-glycosylated, mucin-like C terminus of CEL/FAPP.
29992770	9	56	gly	N-glycopeptides	1236:1250	arg2	N-glycopeptides	IgG4		N-glycopeptides		OGER		IgG4	P01861	N-glycopeptides	N-glycopeptides of IgG1, IgG4, haptoglobin, and transferrin have statistically significant different abundances between cases and controls.
29992770	9	56	gly	N-glycopeptides	1236:1250	arg1	haptoglobin	haptoglobin		N-glycopeptides		PUBTATOR		haptoglobin	3240	N-glycopeptides	N-glycopeptides of IgG1, IgG4, haptoglobin, and transferrin have statistically significant different abundances between cases and controls.
29992770	9	56	gly	N-glycopeptides	1236:1250	arg1	transferrin	transferrin		N-glycopeptides		PUBTATOR		transferrin	7018	N-glycopeptides	N-glycopeptides of IgG1, IgG4, haptoglobin, and transferrin have statistically significant different abundances between cases and controls.
29992770	9	56	gly	N-glycopeptides	1236:1250	arg1	IgG4	haptoglobin		N-glycopeptides		PUBTATOR		haptoglobin	3240	N-glycopeptides	N-glycopeptides of IgG1, IgG4, haptoglobin, and transferrin have statistically significant different abundances between cases and controls.
30136207	3	63	gly	sialylated	673:682	arg1	terminally sialylated structure				terminally sialylated structure						In this study, as the first report regarding protein O-glycosylation analysis in silkworms, we verified the O-glycan profile that a common core 1 Gal (β1-3) GalNAc disaccharide branch without terminally sialylated structure is mainly formed for a baculovirus-produced human proteoglycan 4 (PRG4) protein.
31180129	2	53	gly	glycosylated	432:443	arg1	heavily glycosylated proteins	heavily glycosylated proteins				Fterm		proteins			The ability of C. perfringens to incite NE depends upon its ability to penetrate the protective mucus barrier within the small intestine, which is largely composed of heavily glycosylated proteins called mucins.
29642453	5	63	gly	glycosylation	737:749	arg2	particular glycosylation sites			particular glycosylation sites						sites	Co-segregation of particular glycosylation sites was identified as a characteristic of zoonotic transmission from animal reservoirs, and interestingly, of "reverse zoonosis" of human viruses into swine populations as well.
30407002	2	3	gly	glycans	325:331	arg1	a certain protein	protein			glycans	Fterm		protein			However, the ubiquity of glycosylation makes probing the glycans on a certain protein as difficult as looking for a needle in a haystack.
29437979	15	142	gly	glycosylation	2390:2402	arg2	all five predicted N-linked glycosylation sites			all five predicted N-linked glycosylation sites						sites	Here, we systematically analyzed the functional relevance of all five predicted N-linked glycosylation sites in the alphaherpesvirus pseudorabies virus (PrV) gH.
29441788	1	37	gly	glycoprotein	96:107	arg1	an 87 kDa glycoprotein	an 87 kDa glycoprotein				Fterm		glycoprotein			Afamin is an 87 kDa glycoprotein with five predicted N-glycosylation sites.
29441788	1	53	gly	N-glycosylation	129:143	arg2	five predicted N-glycosylation sites			five predicted N-glycosylation sites						sites	Afamin is an 87 kDa glycoprotein with five predicted N-glycosylation sites.
31260704	3	21	gly	N-glycopeptides	516:530	arg2	N-glycopeptides	IgG1		N-glycopeptides		OGER		IgG1	P01857	N-glycopeptides	In this work, we present a high-throughput matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) method based on a microarray technology to monitor N-glycopeptides of IgG1 produced in a perfusion cell culture.
29409697	5	60	gly	N-glycosylated	1127:1140	arg1	The enzyme	The enzyme				Fterm		enzyme			The enzyme was found to be N-glycosylated by the enzymatic cleavage of glycans, while hGnTII expressed in insect cells had not been reported to be glycosylated.
30651366	6	45	gly	utilized	1037:1044	arg2	all 11 predicted N-glycosylation sites			all 11 predicted N-glycosylation sites						sites	Mass spectrometry demonstrated that all 11 predicted N-glycosylation sites were utilized in both HEK293- and Sf9-derived sE2, but that N-glycans in insect sE2 were on average smaller and less complex.
30651366	6	73	gly	N-glycosylation	1010:1024	arg2	all 11 predicted N-glycosylation sites			all 11 predicted N-glycosylation sites						sites	Mass spectrometry demonstrated that all 11 predicted N-glycosylation sites were utilized in both HEK293- and Sf9-derived sE2, but that N-glycans in insect sE2 were on average smaller and less complex.
31888963	9	84	gly	contain	1324:1330	arg1	N74 AND highly processed complex-type N-glycans	CD16a		N38 and N74	highly processed complex-type N-glycans	PUBTATOR		CD16a	2214	N38 and N74	N38 and N74 of CD16a both contain highly processed complex-type N-glycans with N-acetyllactosamine repeats and complex-type biantennary N-glycans dominate at N169.
31888963	9	84	gly	contain	1324:1330	arg1	N38 AND highly processed complex-type N-glycans	CD16a		N38 and N74	highly processed complex-type N-glycans	PUBTATOR		CD16a	2214	N38 and N74	N38 and N74 of CD16a both contain highly processed complex-type N-glycans with N-acetyllactosamine repeats and complex-type biantennary N-glycans dominate at N169.
31888963	9	84	gly	contain	1324:1330	arg1	N38 AND highly processed complex-type N-glycans	CD16a		N38 and N74	highly processed complex-type N-glycans	PUBTATOR		CD16a	2214	N38 and N74	N38 and N74 of CD16a both contain highly processed complex-type N-glycans with N-acetyllactosamine repeats and complex-type biantennary N-glycans dominate at N169.
30959980	5	13	gly	sialylated	893:902	arg1	sialylated O-glycans				sialylated O-glycans						It was worth noting that Neu5Gc-containing structures within sialylated O-glycans accounted for 91%, which were extremely different from that of other species including humans, mice, chickens, etc.
30242110	10	103	gly	glycosylation	2346:2358	arg1	single proteins	single proteins				Fterm		proteins			While the combination of methods proved to be the most beneficial for the analysis of total serum protein N-glycosylation, informed method choices can be made for the glycosylation analysis of single proteins or samples of varying complexity.
29703890	4	29	gly	glycopeptide	641:652	arg2	the glycopeptide enrichment			the glycopeptide enrichment						glycopeptide	Here, we develop a strategy using dendrimer-conjugated benzoboroxole to enhance the glycopeptide enrichment.
31384044	2	9	gly	glycopeptides	327:339	arg2	glycopeptides			glycopeptides						glycopeptides	This approach enables characterization of glycopeptides and structures of O-glycans on a proteome-wide scale with quantification of stoichiometries (though it does not allow for direct unambiguous glycosite identification).
31384044	2	52	gly	glycosite	482:490	arg2	direct unambiguous glycosite identification			direct unambiguous glycosite identification						glycosite	This approach enables characterization of glycopeptides and structures of O-glycans on a proteome-wide scale with quantification of stoichiometries (though it does not allow for direct unambiguous glycosite identification).
31126879	0	36	part_of	Silent	55:60	arg1	the Silent Face	Silent Face		the Silent Face		OGER		Silent Face	Q9HB96		Broad and Potent Neutralizing Antibodies Recognize the Silent Face of the HIV Envelope.
31790908	5	17	part_of	ICChI	747:751	arg1	the N-terminal sequence	ICChI		the N-terminal sequence		Cterm	Site	ICChI		sequence	The structure was elucidated by molecular replacement method using a mixed model of three homologous structures from the N-terminal sequence of ICChI.
30018219	6	15	part_of	EGF	1012:1014	arg1	the different EGF domains	EGF		the different EGF domains		PUBTATOR	Site	EGF	1950	domains	In contrast, recombinant Notch1 EGF repeats isolated from HEK293T cells revealed structural divergence of O-GlcNAc glycans among the different EGF domains.
31024890	14	5	gly	Glu392-Fuc	2208:2217	arg1	the Glu392-Fuc interaction			Glu392	the Glu392-Fuc interaction					Glu392	The analysis of interaction suggests that perturbing the Glu392-Fuc interaction could increase the T/H ratio, either by direct mutation of this residue or indirectly as reported experimentally in the Asn390I and Phe401S cases.
30459171	0	8	gly	glycopeptides	71:83	arg2	O-linked glycopeptides			O-linked glycopeptides						glycopeptides	Mapping the O-glycoproteome using site-specific extraction of O-linked glycopeptides (EXoO).
30315106	10	78	gly	glycoprotein	1754:1765	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			Thus, among digestive enzymes secreted by the pancreas, CEL is a glycoprotein with some unique characteristics, supporting the view that it could serve additional biological functions to its cholesteryl esterase activity in the duodenum.
29769321	7	78	gly	-sialylated	1465:1475	arg1	heterogeneously branched and predominantly α(2,3)-sialylated oligosaccharides				heterogeneously branched and predominantly α(2,3)-sialylated oligosaccharides						MS analysis revealed an N-glycan site-occupancy of >98% at Asn-303 of RpNCRD with complex-type, heterogeneously branched and predominantly α(2,3)-sialylated oligosaccharides.
29769321	7	90	gly	Asn-303	1379:1385	arg1	heterogeneously branched and predominantly α(2,3)-sialylated oligosaccharides			Asn-303	heterogeneously branched and predominantly α(2,3)-sialylated oligosaccharides					Asn-303	MS analysis revealed an N-glycan site-occupancy of >98% at Asn-303 of RpNCRD with complex-type, heterogeneously branched and predominantly α(2,3)-sialylated oligosaccharides.
31094418	6	28	gly	glycosylation	1087:1099	arg2	the four glycosylation sites			the four glycosylation sites						sites	The number per glycan varies in three of the four glycosylation sites, and in addition, for the first time, we have detected PC on the N-glycan chitobiose core in addition to terminal GlcNAc.
29931153	6	8	gly	glycosylated	1234:1245	arg1	the glycosylated Asn residue			the glycosylated Asn residue						Asn residue	We confirm that site-specific N-glycan processing is largely explained by the solvent accessibility of the glycosylated Asn residue and of the conjugated N-glycan.
30935958	9	33	gly	N-glycosylated	1111:1124	arg2	Asn197			positions Asn181 and Asn197						positions Asn181 and Asn197	In vivo PrP is N-glycosylated at positions Asn181 and Asn197.
30935958	9	33	gly	N-glycosylated	1111:1124	arg1	In vivo PrP	PrP		positions Asn181 and Asn197		PUBTATOR		PrP	5621	positions Asn181 and Asn197	In vivo PrP is N-glycosylated at positions Asn181 and Asn197.
30935958	9	33	gly	N-glycosylated	1111:1124	arg2	positions			positions Asn181 and Asn197						positions Asn181 and Asn197	In vivo PrP is N-glycosylated at positions Asn181 and Asn197.
30935958	9	33	gly	N-glycosylated	1111:1124	arg1	In vivo PrP	PrP		positions Asn181 and Asn197		PUBTATOR		PrP	5621	positions Asn181 and Asn197	In vivo PrP is N-glycosylated at positions Asn181 and Asn197.
30935958	9	33	gly	N-glycosylated	1111:1124	arg2	positions			positions Asn181 and Asn197						positions Asn181 and Asn197	In vivo PrP is N-glycosylated at positions Asn181 and Asn197.
30935958	9	33	gly	N-glycosylated	1111:1124	arg2	positions	PrP		positions Asn181 and Asn197		PUBTATOR		PrP	5621	positions Asn181 and Asn197	In vivo PrP is N-glycosylated at positions Asn181 and Asn197.
30935958	9	40	gly	positions	1129:1137	arg1	Asn197			positions Asn181 and Asn197						positions Asn181 and Asn197	In vivo PrP is N-glycosylated at positions Asn181 and Asn197.
30935958	9	40	gly	positions	1129:1137	arg1	Asn181			positions Asn181 and Asn197						positions Asn181 and Asn197	In vivo PrP is N-glycosylated at positions Asn181 and Asn197.
30935958	9	40	gly	positions	1129:1137	arg1	Asn181			positions Asn181 and Asn197						positions Asn181 and Asn197	In vivo PrP is N-glycosylated at positions Asn181 and Asn197.
30802037	2	25	part_of	mucin-type	383:392	arg1	intact mucin-type O-glycopeptides	mucin		intact mucin-type O-glycopeptides		PUBTATOR	Site	mucin	100508689	O-glycopeptides	However, this approach is often not applicable to identify intact mucin-type O-glycopeptides due to the high microheterogeneity of the glycosylation.
29981899	8	39	gly	glycoproteins	1394:1406	arg1	CLBP patients' plasma glycoproteins	CLBP patients' plasma glycoproteins				Fterm		glycoproteins			RESULTS We have found a statistically significant increase in the relative amount of high-branched (tri-antennary and tetra-antennary) N-glycan structures on CLBP patients' plasma glycoproteins compared to healthy controls.
29411222	2	47	gly	O-glycosylation	284:298	arg2	three N- and 13 O-glycosylation sites			three N- and 13 O-glycosylation sites						sites	It possesses three N- and 13 O-glycosylation sites.
29411222	2	47	gly	O-glycosylation	284:298	arg2	13			13						N- and 13	It possesses three N- and 13 O-glycosylation sites.
31501225	9	29	gly	N-glycopeptides	1350:1364	arg2	The altered N-glycopeptides			The altered N-glycopeptides						N-glycopeptides	The altered N-glycopeptides might be part of a unique glycan signature indicating an IgA-mediated mechanism and providing potential diagnostic clues in HBV-related liver diseases.
29783688	1	63	gly	attached	126:133	arg2	proteins AND Glycosaminoglycans	proteins			Glycosaminoglycans	Fterm		proteins			Glycosaminoglycans (GAGs) are found covalently attached to proteins, which create conjugates known as proteoglycans.
29936827	9	27	gly	glycosites	1555:1564	arg2	up to 8-fold more glycosites than previously reported with concomitant increased heterogeneity			up to 8-fold more glycosites than previously reported with concomitant increased heterogeneity						glycosites	We establish the method on standard glycoproteins, confirming known O-glycosites with high accuracy and confidence, and reveal up to 8-fold more glycosites than previously reported with concomitant increased heterogeneity.
29936827	9	40	gly	glycoproteins	1446:1458	arg1	standard glycoproteins	standard glycoproteins				Fterm		glycoproteins			We establish the method on standard glycoproteins, confirming known O-glycosites with high accuracy and confidence, and reveal up to 8-fold more glycosites than previously reported with concomitant increased heterogeneity.
29936827	9	43	gly	O-glycosites	1478:1489	arg2	known O-glycosites			known O-glycosites						O-glycosites	We establish the method on standard glycoproteins, confirming known O-glycosites with high accuracy and confidence, and reveal up to 8-fold more glycosites than previously reported with concomitant increased heterogeneity.
29775069	2	16	gly	glycoproteins	528:540	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Herein we report a versatile, convenient one-pot method in which O- and N-glycans are simultaneously released from glycoproteins and chromogenically labeled in situ and thus available for further characterization.
30459171	3	1	gly	glycopeptides	428:440	arg2	O-linked glycopeptides			O-linked glycopeptides						glycopeptides	Here, a chemoenzymatic method is introduced for the site-specific extraction of O-linked glycopeptides (EXoO), which enabled the mapping of over 3,000 O-linked glycosylation sites and definition of their glycans on over 1,000 proteins in human kidney tissues, T cells, and serum.
30459171	3	21	gly	glycosylation	499:511	arg2	over 3,000 O-linked glycosylation sites			over 3,000 O-linked glycosylation sites						sites	Here, a chemoenzymatic method is introduced for the site-specific extraction of O-linked glycopeptides (EXoO), which enabled the mapping of over 3,000 O-linked glycosylation sites and definition of their glycans on over 1,000 proteins in human kidney tissues, T cells, and serum.
31279935	12	23	gly	glycosylation	1459:1471	arg2	glycosylation sites			glycosylation sites						sites	We report here evidence that targeting Cel7A linker flexibility by point mutations including modification of glycosylation sites could be a promising design strategy to improve cellulase activity.
31813565	7	16	gly	glycopeptides	1381:1393	arg2	glycopeptides			glycopeptides						glycopeptides	Moreover, the nanocomposite was applied to the selective enrichment of glycopeptides from the complex biological samples and a total of 123 unique N-glycosylation sites were identified from 113 glycopeptides in 1 μL of human serum, which were assigned to 46 different glycoproteins.
31813565	7	24	gly	glycopeptides	1504:1516	arg2	113 glycopeptides			113 glycopeptides						glycopeptides	Moreover, the nanocomposite was applied to the selective enrichment of glycopeptides from the complex biological samples and a total of 123 unique N-glycosylation sites were identified from 113 glycopeptides in 1 μL of human serum, which were assigned to 46 different glycoproteins.
31813565	7	35	gly	N-glycosylation	1457:1471	arg2	123 unique N-glycosylation sites			123 unique N-glycosylation sites						sites	Moreover, the nanocomposite was applied to the selective enrichment of glycopeptides from the complex biological samples and a total of 123 unique N-glycosylation sites were identified from 113 glycopeptides in 1 μL of human serum, which were assigned to 46 different glycoproteins.
31813565	7	61	gly	glycoproteins	1578:1590	arg1	46 different glycoproteins	46 different glycoproteins				Fterm		glycoproteins			Moreover, the nanocomposite was applied to the selective enrichment of glycopeptides from the complex biological samples and a total of 123 unique N-glycosylation sites were identified from 113 glycopeptides in 1 μL of human serum, which were assigned to 46 different glycoproteins.
30136207	6	33	gly	glycoproteins	1419:1431	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Taken together, the present results clarified the functional BmPGANT2 in cultured silkworm cells, providing crucial fundamental insights for future studies dissecting the detailed silkworm O-glycosylation pathways and productions of glycoproteins with O-glycans.
30659587	4	61	gly	glycopeptide	701:712	arg2	glycopeptide mapping			glycopeptide mapping						glycopeptide	Site-specific glycosylation profiles were elucidated by glycopeptide mapping and the effect of the glycosylation variants on the FcγRIIIa receptor binding affinity and the biological activity (cell-based and surface plasmon resonance) was assessed.
29620509	2	73	gly	terminus	334:341	arg1	the modified vector pAPtag			terminus	the modified vector pAPtag					terminus	Methods First, cDNA sequences encoding the extracellular domain of Necls were cloned into the modified vector pAPtag at the N terminus of alkaline phosphatase (AP) for fusion expression.
29927116	2	72	gly	heterogeneity	338:350	arg1	glycans				glycans						The complex chemical heterogeneity of glycans found on the cell surface or the glycocalyx renders analysis of the individual contributions of glycans difficult.
31010286	5	51	part_of	D1-arm	1115:1120	arg1	the D1-arm fragment	D1-arm		the D1-arm fragment		Cterm	Site	D1-arm		fragment	Blockwise coupling of the pentasaccharide acceptor with an α-(1→2)-linked mannotriosyl trichloroacetimidate donor introduced the D1-arm fragment.
30802037	2	23	gly	O-glycopeptides	394:408	arg2	intact mucin-type O-glycopeptides			intact mucin-type O-glycopeptides						O-glycopeptides	However, this approach is often not applicable to identify intact mucin-type O-glycopeptides due to the high microheterogeneity of the glycosylation.
30904681	1	52	gly	glycosylated	150:161	arg1	a 50 kDa human plasma protein	a 50 kDa human plasma protein				Fterm		protein			The highly glycosylated ß-2-glycoprotein-1 (B2GP1), also called apolipoprotein H, is a 50 kDa human plasma protein with four or five N-glycosylation sites.
30904681	1	52	gly	glycosylated	150:161	arg1	The highly glycosylated ß-2-glycoprotein-1	The highly glycosylated ß-2-glycoprotein-1				Fterm		ß-2-glycoprotein-1	350		The highly glycosylated ß-2-glycoprotein-1 (B2GP1), also called apolipoprotein H, is a 50 kDa human plasma protein with four or five N-glycosylation sites.
30904681	1	63	gly	N-glycosylation	272:286	arg2	four or five N-glycosylation sites			four or five N-glycosylation sites						sites	The highly glycosylated ß-2-glycoprotein-1 (B2GP1), also called apolipoprotein H, is a 50 kDa human plasma protein with four or five N-glycosylation sites.
31295497	7	45	gly	sequence	1059:1066	arg1	oligosaccharides			sequence	oligosaccharides					sequence	HILIC-UPLC-ESI--HCD-MS/MS was further applied in deducing interglycosidic linkages and sequence of monosaccharide residues in oligosaccharides.
30915686	0	58	gly	N-glycoproteins	24:38	arg1	serum N-glycoproteins	serum N-glycoproteins				Fterm		N-glycoproteins			Identification of serum N-glycoproteins as a biological correlate underlying chronic stress response in mice.
30909000	2	55	part_of	GO-MAx	500:505	arg1	compositions	MAx		compositions		OGER	Site	MAx	P61244	positions	The morphologies, pore sizes, specific surface area (SSA) and compositions of GO-MAx:y composites with and different GO-to-MA mass ratios (x:y) were characterized by scanning electron microscopy (SEM), N2 adsorption-desorption isotherms, Fourier transform infrared spectroscopy (FT-IR) and X-ray photoelectron spectroscopy (XPS).
31100702	12	52	gly	glycoproteins	1526:1538	arg1	other glycoproteins	other glycoproteins				Fterm		glycoproteins			A loss of glycans of lesser complexity (oligomannose and biantennary structures) was also observed for other glycoproteins (RNase B, porcine thyroglobulin, human lactoferrin).
30295034	1	14	gly	glycoprotein	161:172	arg1	a highly glycosylated protein	a highly glycosylated protein				Fterm		protein			Alpha-1-acid glycoprotein (AGP) is a highly glycosylated protein from human plasma with five N-type glycosylation sites carrying dominantly higher antennary structures and thus represents a challenging target for characterization of glycan heterogeneity.
30295034	1	14	gly	glycoprotein	161:172	arg1	Alpha-1-acid glycoprotein	Alpha-1-acid glycoprotein				Fterm		glycoprotein			Alpha-1-acid glycoprotein (AGP) is a highly glycosylated protein from human plasma with five N-type glycosylation sites carrying dominantly higher antennary structures and thus represents a challenging target for characterization of glycan heterogeneity.
30295034	1	29	gly	glycosylation	248:260	arg2	five N-type glycosylation sites			five N-type glycosylation sites						sites	Alpha-1-acid glycoprotein (AGP) is a highly glycosylated protein from human plasma with five N-type glycosylation sites carrying dominantly higher antennary structures and thus represents a challenging target for characterization of glycan heterogeneity.
30295034	1	53	gly	glycosylated	192:203	arg1	Alpha-1-acid glycoprotein	Alpha-1-acid glycoprotein				Fterm		glycoprotein			Alpha-1-acid glycoprotein (AGP) is a highly glycosylated protein from human plasma with five N-type glycosylation sites carrying dominantly higher antennary structures and thus represents a challenging target for characterization of glycan heterogeneity.
30295034	1	53	gly	glycosylated	192:203	arg1	a highly glycosylated protein	a highly glycosylated protein				Fterm		protein			Alpha-1-acid glycoprotein (AGP) is a highly glycosylated protein from human plasma with five N-type glycosylation sites carrying dominantly higher antennary structures and thus represents a challenging target for characterization of glycan heterogeneity.
30295034	1	40	gly	carrying	268:275	arg1	five N-type glycosylation sites AND dominantly higher antennary structures			five N-type glycosylation sites	dominantly higher antennary structures					sites	Alpha-1-acid glycoprotein (AGP) is a highly glycosylated protein from human plasma with five N-type glycosylation sites carrying dominantly higher antennary structures and thus represents a challenging target for characterization of glycan heterogeneity.
30407002	4	36	gly	attached	681:688	arg2	target proteins AND glycan conversion probes	target proteins			glycan conversion probes	Fterm		proteins			The strategy relies on designing two kinds of DNA probes, glycan conversion probes and protein recognition probes, which are attached to glycans and target proteins, respectively.
30553446	4	47	part_of	IgA	507:509	arg1	the hinge region	IgA		the hinge region		PUBTATOR	Site	IgA	973	region	In IgAN, aberrant IgA1 O-glycan structure in the hinge region (HR) of serum IgA is suggested as one of the most convincing key mediators.
31190665	2	33	part_of	parasite	674:681	arg1	an immunodominant GST	GST		parasite		OGER	Site	GST		parasite	Here we have identified and characterized a σ class glycosylated GST (OoGST1), from the cattle-infective filarial nematode Onchocerca ochengi, which is homologous (99% amino acid identity) with an immunodominant GST and potential vaccine candidate from the human parasite, O. volvulus, (OvGST1b).
29441788	8	7	part_of	Fab	1249:1251	arg1	a Fab fragment	Fab		a Fab fragment		PUBTATOR	Site	Fab	2187	fragment	Because antibody fragments can work as artificial chaperones by stabilizing the structure of proteins and consequently enhance the chance for successful crystallization, we incubated a Fab fragment of the monoclonal anti-afamin antibody N14 with human afamin and obtained a stoichiometric complex.
30759204	1	44	gly	proteins	227:234	arg1	repeat regions	proteins			repeat regions	Fterm		proteins			GalNAc-type O-glycans are often added to proteins post-translationally in a clustered manner in repeat regions of proteins, such as mucins and IgA1.
31494931	7	4	gly	N-glycosylation	772:786	arg1	Glut1	Glut1			glucose transporter 1	PUBTATOR		Glut1	6513		Furthermore, MGAT1 promotes complex N-glycosylation of glucose transporter 1 (Glut1) and increases Glut1 protein levels.
29769321	4	64	part_of	SP-D	802:805	arg1	an N-glycosylated neck-CRD fragment	SP-D		an N-glycosylated neck-CRD fragment		PUBTATOR	Site	SP-D	6441	fragment	Here, to investigate both mechanisms of IAV neutralization in greater detail, we produced an N-glycosylated neck-CRD fragment of porcine SP-D (RpNCRD) in HEK293 cells.
29769321	4	93	part_of	neck-CRD	773:780	arg1	an N-glycosylated neck-CRD fragment	CRD		an N-glycosylated neck-CRD fragment		Cterm	Site	CRD		fragment	Here, to investigate both mechanisms of IAV neutralization in greater detail, we produced an N-glycosylated neck-CRD fragment of porcine SP-D (RpNCRD) in HEK293 cells.
31190665	0	66	gly	glycosylated	28:39	arg1	a novel glycosylated glutathione transferase	a novel glycosylated glutathione transferase				Fterm		transferase			Characterization of a novel glycosylated glutathione transferase of Onchocerca ochengi, closest relative of the human river blindness parasite.
29297680	10	60	gly	glycosylation	2056:2068	arg1	sugar oximes				sugar oximes						The direct glycosylation of some sensitive aglycones, such as dammarane C20-ol and sugar oximes, and the glycosylation-initiated polymerization of tetrahydrofuran were achieved for the first time.
29674057	11	7	gly	glycoproteins	1897:1909	arg1	the same glycoproteins	the same glycoproteins				Fterm		glycoproteins			Comparisons of HILIC-MS with the selectivity provided by capillary electrophoresis-MS for the same glycoproteins, revealed a remarkable complementarity of the techniques.
29703890	2	41	gly	glycoproteins	281:293	arg1	many glycoproteins	many glycoproteins				Fterm		glycoproteins			However, the heterogeneity of glycans and the low abundance of many glycoproteins complicate their global analysis.
29703890	2	53	gly	heterogeneity	226:238	arg1	many glycoproteins	glycoproteins			glycans	Fterm		glycoproteins			However, the heterogeneity of glycans and the low abundance of many glycoproteins complicate their global analysis.
30973186	1	11	gly	glycoprotein	118:129	arg1	the glycoprotein hormone erythropoietin	the glycoprotein hormone erythropoietin				Fterm		glycoprotein			The biological activity of the glycoprotein hormone erythropoietin (EPO) is dependent mainly on the structure of its N-linked glycans.
31393126	5	71	gly	glycopeptides	779:791	arg2	tryptic glycopeptides			tryptic glycopeptides						glycopeptides	Second, tryptic glycopeptides were enriched and separated by hydrophilic interaction liquid chromatography-ion trap-sequential mass spectrometry (HILIC-IT-MS).
31726038	8	14	gly	glycosylated	1480:1491	arg1	quercitrin	quercitrin				Fterm		quercitrin			In comparison to BT0986 (pdbID: 5MQN), the only known structure of an RHA-P homolog, the morphology, electrostatic potentials and amino acid composition of the substrate binding pocket are significantly different, offering insight into the substrate preference of RHA-P for glycosylated aryl compounds such as hesperidin, naringin, rutin, and quercitrin, over polysaccharides, which are preferred by BT0986.
31726038	8	14	gly	glycosylated	1480:1491	arg1	naringin	naringin				Fterm		naringin			In comparison to BT0986 (pdbID: 5MQN), the only known structure of an RHA-P homolog, the morphology, electrostatic potentials and amino acid composition of the substrate binding pocket are significantly different, offering insight into the substrate preference of RHA-P for glycosylated aryl compounds such as hesperidin, naringin, rutin, and quercitrin, over polysaccharides, which are preferred by BT0986.
31726038	8	14	gly	glycosylated	1480:1491	arg1	hesperidin	hesperidin				Fterm		hesperidin			In comparison to BT0986 (pdbID: 5MQN), the only known structure of an RHA-P homolog, the morphology, electrostatic potentials and amino acid composition of the substrate binding pocket are significantly different, offering insight into the substrate preference of RHA-P for glycosylated aryl compounds such as hesperidin, naringin, rutin, and quercitrin, over polysaccharides, which are preferred by BT0986.
29603480	3	23	gly	antenna	679:685	arg1	a sialyl-Lewisx -Lewisx (SLex -Lex ) residue			a sialyl-Lewisx -Lewisx (SLex -Lex ) residue	a sialyl-Lewisx -Lewisx (SLex -Lex ) residue		AminoAcid			residue at	We describe here the chemoenzymatic synthesis of highly complex triantennary N-glycans derived from ZP carrying SLex moieties at the C-2 and C-2' arm and a sialyl-Lewisx -Lewisx (SLex -Lex ) residue at the C-6 antenna and two closely related analogues.
30463578	7	13	gly	trisialylated	1137:1149	arg1	tetragalactosylated, trisialylated, tetrasialylated and antennary fucosylated glycoforms				tetragalactosylated, trisialylated, tetrasialylated and antennary fucosylated glycoforms						RESULTS Plasma protein N-glycome in COPD subjects exhibited significant decrease in low branched and conversely, an increase in more complex glycan structures (tetragalactosylated, trisialylated, tetrasialylated and antennary fucosylated glycoforms).
30463578	7	13	gly	trisialylated	1137:1149	arg1	more complex glycan structures				more complex glycan structures						RESULTS Plasma protein N-glycome in COPD subjects exhibited significant decrease in low branched and conversely, an increase in more complex glycan structures (tetragalactosylated, trisialylated, tetrasialylated and antennary fucosylated glycoforms).
30463578	7	45	gly	tetrasialylated	1152:1166	arg1	tetragalactosylated, trisialylated, tetrasialylated and antennary fucosylated glycoforms				tetragalactosylated, trisialylated, tetrasialylated and antennary fucosylated glycoforms						RESULTS Plasma protein N-glycome in COPD subjects exhibited significant decrease in low branched and conversely, an increase in more complex glycan structures (tetragalactosylated, trisialylated, tetrasialylated and antennary fucosylated glycoforms).
30463578	7	45	gly	tetrasialylated	1152:1166	arg1	more complex glycan structures				more complex glycan structures						RESULTS Plasma protein N-glycome in COPD subjects exhibited significant decrease in low branched and conversely, an increase in more complex glycan structures (tetragalactosylated, trisialylated, tetrasialylated and antennary fucosylated glycoforms).
30463578	7	105	gly	fucosylated	1182:1192	arg1	tetragalactosylated, trisialylated, tetrasialylated and antennary fucosylated glycoforms				tetragalactosylated, trisialylated, tetrasialylated and antennary fucosylated glycoforms						RESULTS Plasma protein N-glycome in COPD subjects exhibited significant decrease in low branched and conversely, an increase in more complex glycan structures (tetragalactosylated, trisialylated, tetrasialylated and antennary fucosylated glycoforms).
30463578	7	105	gly	fucosylated	1182:1192	arg1	more complex glycan structures				more complex glycan structures						RESULTS Plasma protein N-glycome in COPD subjects exhibited significant decrease in low branched and conversely, an increase in more complex glycan structures (tetragalactosylated, trisialylated, tetrasialylated and antennary fucosylated glycoforms).
29324282	7	77	gly	hypersialylated	1384:1398	arg1	the hypergalactosylated and hypersialylated forms	FcγRIIA			the hypergalactosylated and hypersialylated forms	PUBTATOR		FcγRIIA	2212		No significant changes were observed for the hypergalactosylated and hypersialylated forms of IgG1 with regards to binding to FcRn, FcγRIIA and FcγRIIIA, suggesting that neither half-life in circulation nor their ability to induce an immune response are likely to be affected by these modifications of the glycan chains.
29324282	7	77	gly	hypersialylated	1384:1398	arg1	the hypergalactosylated and hypersialylated forms	FcγRIIIA			the hypergalactosylated and hypersialylated forms	PUBTATOR		FcγRIIIA	2214		No significant changes were observed for the hypergalactosylated and hypersialylated forms of IgG1 with regards to binding to FcRn, FcγRIIA and FcγRIIIA, suggesting that neither half-life in circulation nor their ability to induce an immune response are likely to be affected by these modifications of the glycan chains.
29324282	7	77	gly	hypersialylated	1384:1398	arg1	the hypergalactosylated and hypersialylated forms	IgG1			the hypergalactosylated and hypersialylated forms	OGER		IgG1	P01857		No significant changes were observed for the hypergalactosylated and hypersialylated forms of IgG1 with regards to binding to FcRn, FcγRIIA and FcγRIIIA, suggesting that neither half-life in circulation nor their ability to induce an immune response are likely to be affected by these modifications of the glycan chains.
30002445	0	39	gly	glycoprotein	11:22	arg1	Single-pot glycoprotein biosynthesis	Single-pot glycoprotein biosynthesis				Fterm		glycoprotein			Single-pot glycoprotein biosynthesis using a cell-free transcription-translation system enriched with glycosylation machinery.
29959030	7	50	gly	glycosylation	1056:1068	arg1	ectosome proteins	ectosome proteins				Fterm		proteins			It is the first study to characterize the glycosylation of ectosome proteins released by CM cells.
29532326	12	49	gly	detected	1538:1545	arg1	this subunit AND these O-glycans	this subunit			these O-glycans	Fterm		subunit			Albeit low abundant, these O-glycans are the first PTMs ever detected on this subunit.
30259139	1	9	gly	glycoproteins	184:196	arg1	cerebrospinal fluid (CSF) glycoproteins	cerebrospinal fluid (CSF) glycoproteins				Fterm		glycoproteins			The subcommissural organ (SCO) is an ancient and conserved brain gland secreting into cerebrospinal fluid (CSF) glycoproteins that form the Reissner fiber (RF).
31423004	3	64	gly	core-fucosylated	540:555	arg1	core-fucosylated oligosaccharides				core-fucosylated oligosaccharides						Generally, Chinese hamster ovary (CHO) cells produce recombinant human AT (rhAT) with core-fucosylated oligosaccharides.
30624066	9	52	gly	sialylated	1774:1783	arg1	sialylated bi-				sialylated bi-						Screening the N-glycan libraries of each of the GPs against hGal-3C identified ligands corresponding to a total of 20 different saccharide compositions with sialylated bi-, tri-, and tetra-antennary structures.
29936827	5	0	gly	glycoproteins	895:907	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Although O-glycosidase can catalyze the removal of core 1 and core 3 O-linked disaccharides from glycoproteins, analysis of other types of O-glycans remains difficult, particularly when residing on glycopeptides.
29936827	5	75	gly	glycopeptides	996:1008	arg2	glycopeptides			glycopeptides						glycopeptides	Although O-glycosidase can catalyze the removal of core 1 and core 3 O-linked disaccharides from glycoproteins, analysis of other types of O-glycans remains difficult, particularly when residing on glycopeptides.
31393126	8	36	gly	sites	1269:1273	arg1	Two N-glycosylation sites			Two N-glycosylation sites						sites	Two N-glycosylation sites (N177 and N394), 3 sites (N145, N178, and N92), and 1 site of N183 were identified in MRJP1, MRJP2, and MRJP3, respectively.
31393126	8	36	gly	sites	1269:1273	arg1	N183			N183						N183	Two N-glycosylation sites (N177 and N394), 3 sites (N145, N178, and N92), and 1 site of N183 were identified in MRJP1, MRJP2, and MRJP3, respectively.
31393126	8	46	gly	sites	1294:1298	arg1	3 sites			3 sites						sites	Two N-glycosylation sites (N177 and N394), 3 sites (N145, N178, and N92), and 1 site of N183 were identified in MRJP1, MRJP2, and MRJP3, respectively.
31393126	8	46	gly	sites	1294:1298	arg1	N183			N183						N183	Two N-glycosylation sites (N177 and N394), 3 sites (N145, N178, and N92), and 1 site of N183 were identified in MRJP1, MRJP2, and MRJP3, respectively.
31393126	8	61	gly	N-glycosylation	1253:1267	arg2	Two N-glycosylation sites			Two N-glycosylation sites						sites	Two N-glycosylation sites (N177 and N394), 3 sites (N145, N178, and N92), and 1 site of N183 were identified in MRJP1, MRJP2, and MRJP3, respectively.
31393126	8	36	gly	sites	1269:1273	arg1	N177			N177 and N394						N177 and N394	Two N-glycosylation sites (N177 and N394), 3 sites (N145, N178, and N92), and 1 site of N183 were identified in MRJP1, MRJP2, and MRJP3, respectively.
31393126	8	46	gly	sites	1294:1298	arg1	N92			N145, N178, and N92						N145, N178, and N92	Two N-glycosylation sites (N177 and N394), 3 sites (N145, N178, and N92), and 1 site of N183 were identified in MRJP1, MRJP2, and MRJP3, respectively.
31393126	8	46	gly	sites	1294:1298	arg1	N145			N145, N178, and N92						N145, N178, and N92	Two N-glycosylation sites (N177 and N394), 3 sites (N145, N178, and N92), and 1 site of N183 were identified in MRJP1, MRJP2, and MRJP3, respectively.
31393126	8	46	gly	sites	1294:1298	arg1	N145			N145, N178, and N92						N145, N178, and N92	Two N-glycosylation sites (N177 and N394), 3 sites (N145, N178, and N92), and 1 site of N183 were identified in MRJP1, MRJP2, and MRJP3, respectively.
31393126	8	61	gly	N-glycosylation	1253:1267	arg2	N394			N177 and N394						N177 and N394	Two N-glycosylation sites (N177 and N394), 3 sites (N145, N178, and N92), and 1 site of N183 were identified in MRJP1, MRJP2, and MRJP3, respectively.
31393126	8	61	gly	N-glycosylation	1253:1267	arg1	N183			N183						N183	Two N-glycosylation sites (N177 and N394), 3 sites (N145, N178, and N92), and 1 site of N183 were identified in MRJP1, MRJP2, and MRJP3, respectively.
31145522	9	47	gly	LacdiNAc-glycosylated	1665:1685	arg1	LacdiNAc-glycosylated PSA				LacdiNAc-glycosylated PSA						LacdiNAc-glycosylated PSA is significantly better than the conventional PSA test in identifying patients with CSPC.
30111543	2	64	gly	glycoprotein	211:222	arg1	glycoprotein microheterogeneity	glycoprotein microheterogeneity				Fterm		glycoprotein			Elucidating glycoprotein microheterogeneity and relating subtle changes in the glycan structural repertoire to changes in protein-protein, or protein-small molecule interactions, remains a significant challenge in glycobiology.
31311856	1	26	gly	N-glycoproteins	279:293	arg1	misfolded N-glycoproteins	misfolded N-glycoproteins				Fterm		N-glycoproteins			In eukaryotic cells, unconjugated oligosaccharides that are structurally related to N-glycans (i.e. free N-glycans) are generated either from misfolded N-glycoproteins destined for the endoplasmic reticulum-associated degradation or from lipid-linked oligosaccharides, donor substrates for N-glycosylation of proteins.
31311856	1	39	gly	N-glycosylation	417:431	arg1	proteins	proteins				Fterm		proteins			In eukaryotic cells, unconjugated oligosaccharides that are structurally related to N-glycans (i.e. free N-glycans) are generated either from misfolded N-glycoproteins destined for the endoplasmic reticulum-associated degradation or from lipid-linked oligosaccharides, donor substrates for N-glycosylation of proteins.
31025190	1	9	gly	glycosylated	237:248	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			Natural hIFNγ is a glycoprotein with two N-glycosylation sites in each monomer chain, which are independently and differentially glycosylated.
31025190	1	41	gly	glycoprotein	127:138	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			Natural hIFNγ is a glycoprotein with two N-glycosylation sites in each monomer chain, which are independently and differentially glycosylated.
31025190	1	43	gly	N-glycosylation	149:163	arg2	two N-glycosylation sites			two N-glycosylation sites						sites	Natural hIFNγ is a glycoprotein with two N-glycosylation sites in each monomer chain, which are independently and differentially glycosylated.
30503907	8	21	gly	glycoproteins	1056:1068	arg1	glycan profiling	glycoproteins			glycan profiling	Fterm		glycoproteins			Our method provides a highly sensitive and simple procedure for glycan profiling of the viral glycoproteins, thereby paving way for direct glycan analyses of human- and animal-derived virions.
31325506	0	31	gly	sialylated	93:102	arg1	sialylated glycans				sialylated glycans						N-glycans of bovine submaxillary mucin contain core-fucosylated and sulfated glycans but not sialylated glycans.
31325506	0	70	gly	core-fucosylated	47:62	arg1	core-fucosylated and sulfated glycans				core-fucosylated and sulfated glycans						N-glycans of bovine submaxillary mucin contain core-fucosylated and sulfated glycans but not sialylated glycans.
30325416	6	13	gly	sialylation	1336:1346	arg1	the unlinked N-glycans				the unlinked N-glycans						Our results show that while core fucosylation and sialylation do not affect the intrinsic dynamics of the unlinked N-glycans, galactosylation of the α(1-6) arm shifts dramatically its conformational equilibrium from an outstretched to a folded conformation.
30325416	6	17	gly	fucosylation	1319:1330	arg1	the unlinked N-glycans				the unlinked N-glycans						Our results show that while core fucosylation and sialylation do not affect the intrinsic dynamics of the unlinked N-glycans, galactosylation of the α(1-6) arm shifts dramatically its conformational equilibrium from an outstretched to a folded conformation.
31349756	6	9	gly	N-glycosylation	1011:1025	arg2	one N-glycosylation site			one N-glycosylation site						site	We confirmed the presence of one N-glycosylation site, carrying 47 glycoforms covering 34 different compositions, next to two hinge region O-glycosylation sites with core 1-type glycans.
31349756	6	43	gly	sites	1133:1137	arg1	core 1-type glycans			sites	core 1-type glycans					sites	We confirmed the presence of one N-glycosylation site, carrying 47 glycoforms covering 34 different compositions, next to two hinge region O-glycosylation sites with core 1-type glycans.
31349756	6	62	gly	O-glycosylation	1117:1131	arg2	two hinge region O-glycosylation sites			two hinge region O-glycosylation sites						sites	We confirmed the presence of one N-glycosylation site, carrying 47 glycoforms covering 34 different compositions, next to two hinge region O-glycosylation sites with core 1-type glycans.
30115684	5	56	gly	glycopeptides	1026:1038	arg2	tryptic glycopeptides			tryptic glycopeptides						glycopeptides	Selective labeling of gp120 by N-azidoacetylmannosamine (ManNAz) and N-azidoacetylgalactosamine (GalNAz) incorporation into the gp120 glycan shield was characterized by mass spectrometry of tryptic glycopeptides.
29587225	5	24	gly	glycosylation	749:761	arg2	the glycosylation sites			the glycosylation sites						sites	The results revealed that desialylation enhances structural flexibility near the glycosylation sites, with greater effects observed around the O-glycosylation site relative to the N-glycosylation sites.
29587225	5	43	gly	N-glycosylation	848:862	arg2	the N-glycosylation sites			the N-glycosylation sites						sites	The results revealed that desialylation enhances structural flexibility near the glycosylation sites, with greater effects observed around the O-glycosylation site relative to the N-glycosylation sites.
29587225	5	47	gly	O-glycosylation	811:825	arg2	the O-glycosylation site			the O-glycosylation site						site	The results revealed that desialylation enhances structural flexibility near the glycosylation sites, with greater effects observed around the O-glycosylation site relative to the N-glycosylation sites.
31501225	7	56	gly	glycopeptides	1162:1174	arg1	IgA2	IgA2		glycopeptides		OGER		IgA2	P01877	glycopeptides	In contrast, the two glycopeptides of IgA2 fell back down in HBV-related HCC patients.
31174130	1	46	gly	glycopeptides	171:183	arg1	derivatized glycans			glycopeptides	derivatized glycans					glycopeptides	Enrichment and/or purification of intact glycopeptides and derivatized glycans are essential for mass spectrometry-based glycoproteomics and glycomics because of analytical challenges observed in the analysis.
30138037	9	53	gly	channel	1561:1567	arg1	a GlcNAcT1 target	channel			a GlcNAcT1 target	Fterm		channel			Data also indicate that a cardiomyocyte L-type voltage-gated Ca2+ channel (Cav) subunit (α2δ1) is a GlcNAcT1 target, and Mgat1KO Cav activity is shifted to more-depolarized membrane potentials.
31325506	7	32	part_of	BSM	1539:1541	arg1	glycopeptides	BSM		glycopeptides		Cterm	Site	BSM	281333	glycopeptides	The N-glycosylation sites were identified from the analysis of glycopeptides from BSM.
30908021	5	40	gly	sequon	1201:1206	arg1	GalNAc-GlcNAc			sequon	GalNAc-GlcNAc					sequon	We report here a mass spectrometric method that is able to identify and distinguish the isobaric structures of complex and hybrid N-glycans flanked by a terminal sulfation sequon on Gal-GlcNAc and GalNAc-GlcNAc of sulfated-3-Gal, sulfated-6-GlcNAc, and sulfated-4-GalNAc.
30908021	5	40	gly	sequon	1201:1206	arg1	Gal-GlcNAc			sequon	Gal-GlcNAc					sequon	We report here a mass spectrometric method that is able to identify and distinguish the isobaric structures of complex and hybrid N-glycans flanked by a terminal sulfation sequon on Gal-GlcNAc and GalNAc-GlcNAc of sulfated-3-Gal, sulfated-6-GlcNAc, and sulfated-4-GalNAc.
29437979	16	84	gly	N-glycosylation	2674:2688	arg2	all five N-glycosylation sites			all five N-glycosylation sites						sites	Despite the fact that mutation of specific sites affected gH transport, in vitro fusion activity, and cell-to-cell spread and resulted in delayed penetration kinetics, even simultaneous inactivation of all five N-glycosylation sites of gH did not severely inhibit formation of infectious virus particles.
29931153	2	1	gly	N-glycans	414:422	arg1	glycoproteins	glycoproteins			N-glycans	Fterm		glycoproteins			Accumulating evidence has shown that not all N-glycans on glycoproteins are uniformly processed into mature forms (hybrid and complex types in mammals) through the ER and Golgi apparatus, and a certain set of glycans remains unprocessed as an "immature" form (high-mannose type in mammals).
29931153	2	101	gly	glycoproteins	427:439	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Accumulating evidence has shown that not all N-glycans on glycoproteins are uniformly processed into mature forms (hybrid and complex types in mammals) through the ER and Golgi apparatus, and a certain set of glycans remains unprocessed as an "immature" form (high-mannose type in mammals).
31349756	5	57	gly	glycopeptide	888:899	arg2	glycopeptide analysis			glycopeptide analysis						glycopeptide	Second, a relative quantitation of the N-glycosylation site microheterogeneity was achieved by glycopeptide analysis, which was further supported by analysis of the released N-glycans.
31349756	5	63	gly	N-glycosylation	832:846	arg2	the N-glycosylation site			the N-glycosylation site						site	Second, a relative quantitation of the N-glycosylation site microheterogeneity was achieved by glycopeptide analysis, which was further supported by analysis of the released N-glycans.
29405331	8	70	gly	glycopeptide	1135:1146	arg2	glycopeptide identification			glycopeptide identification						glycopeptide	A three-step mass spectrometry fragmentation strategy was used for glycopeptide identification, facilitated by pGlyco software annotation and manual checking.
30824758	7	61	gly	glycosylation	1168:1180	arg1	prototype S. aureus Newman strain	prototype S. aureus Newman strain				Fterm		strain			Furthermore, WTA glycosylation of the prototype S. aureus Newman strain was characterized in vivo in two different animal models, namely peritonitis and deep wound infection.
31732167	3	55	gly	glycoprotein	547:558	arg1	glycoprotein (gp)41	glycoprotein (gp)41				Fterm		glycoprotein	920		The exceptions to the contiguous glycan shield include the conserved receptor CD4 binding site (CD4bs) and glycoprotein (gp)41 elements proximal to the furin cleavage site.
30115684	0	67	gly	glycoprotein	37:48	arg1	HIV-1 envelope glycoprotein gp120	HIV-1 envelope glycoprotein gp120				Fterm		glycoprotein			Metabolic labeling of HIV-1 envelope glycoprotein gp120 to elucidate the role of gp120 glycosylation on antigen uptake.
30948514	0	76	gly	O-glycosylated	36:49	arg2	an N-terminal Ser/Thr-rich domain			an N-terminal Ser/Thr-rich domain						domain	Human red and green cone opsins are O-glycosylated at an N-terminal Ser/Thr-rich domain conserved in vertebrates.
30186849	2	1	gly	glycopeptides	455:467	arg2	glycopeptides			glycopeptides						glycopeptides	Open mass spectral library search is a promising computational approach to peptide identification, but its potential in the identification of glycopeptides has not been fully explored.
29474426	6	19	gly	sialoglycopeptide	1249:1265	arg2	sialoglycopeptide			sialoglycopeptide						sialoglycopeptide	We further demonstrated that the combined use of mutants of Endo-S with Endo-M or Endo-CC, endoglycosidases from Mucor hiemalis and Coprinopsis cinerea, enables one-pot transglycosylation from sialoglycopeptide to antibodies.
29532326	10	27	part_of	C8β	1379:1381	arg1	all the thrombospondin-like (TSP) domains	C8β.		all the thrombospondin-like (TSP) domains		PUBTATOR	Site	C8β.	732	domains	Additionally, we elucidated the stoichiometry of all C-mannosylation sites in all the thrombospondin-like (TSP) domains of C8α and C8β.
29532326	10	30	part_of	C8α	1371:1373	arg1	all the thrombospondin-like (TSP) domains	C8α 		all the thrombospondin-like (TSP) domains		PUBTATOR	Site	C8α 	731	domains	Additionally, we elucidated the stoichiometry of all C-mannosylation sites in all the thrombospondin-like (TSP) domains of C8α and C8β.
30673159	10	45	gly	glycosylation	1476:1488	arg1	penetrating peptides			penetrating peptides						peptides	The results reported herein highlight the potential of the glycosylation of penetrating peptides to modulate their activity.
29775069	0	25	gly	N-glycosylation	188:202	arg1	Simultaneous Release	Simultaneous Release				Fterm		Release			Simultaneous Release and Labeling of O- and N-Glycans Allowing for Rapid Glycomic Analysis by Online LC-UV-ESI-MS/MS. Most glycoproteins and biological protein samples undergo both O- and N-glycosylation, making characterization of their structures very complicated and time-consuming.
29775069	0	47	gly	glycoproteins	123:135	arg1	Most glycoproteins	Most glycoproteins				Fterm		glycoproteins			Simultaneous Release and Labeling of O- and N-Glycans Allowing for Rapid Glycomic Analysis by Online LC-UV-ESI-MS/MS. Most glycoproteins and biological protein samples undergo both O- and N-glycosylation, making characterization of their structures very complicated and time-consuming.
31514875	3	1	gly	glycoproteins	635:647	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			In this work, two Immobilized Enzyme Reactors (IMERs) based on trypsin and pepsin protease were used for the first time to fasten and improve the reliability of the specific mapping of the N-glycosylation heterogeneity of glycoproteins.
31514875	3	4	gly	heterogeneity	618:630	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			In this work, two Immobilized Enzyme Reactors (IMERs) based on trypsin and pepsin protease were used for the first time to fasten and improve the reliability of the specific mapping of the N-glycosylation heterogeneity of glycoproteins.
31719148	2	77	gly	receptors	330:338	arg1	the C-type lectin immune receptors	receptors			receptors	Fterm		receptors			Hemocyanins also interact with glycan-recognizing innate immune receptors on antigen-presenting cells, such as the C-type lectin immune receptors mannose receptor (MR), macrophage galactose lectin (MGL), and the Toll-like receptors (TLRs), stimulating proinflammatory cytokine secretion.
29700341	3	40	gly	glycosylation	596:608	arg1	the galactose and fucose motifs			motifs						motifs	The results of binding preferences show that distinct glycosylation on the galactose and fucose motifs are key for C-type lectin receptor binding and that these interactions occur in a Ca2+-dependent fashion.
30689864	3	2	gly	N-/O-glycosylation	465:482	arg1	the target protein	protein			carbohydrate-only systems	Fterm		protein			Here, we present a computational tool, Glycan Modeler for in silico N-/O-glycosylation of the target protein and generation of carbohydrate-only systems.
30782654	10	122	gly	glycosylation	2103:2115	arg1	surface proteins	surface proteins				Fterm		proteins			It is unknown if these enzymes catalyze glycosylation of surface proteins.
30737276	7	12	gly	positions	1282:1290	arg1	the terminal α-l-rhamnose (Rha) unit			positions	the terminal α-l-rhamnose (Rha) unit					positions	According to our working model, the virus gene a064r encodes a GT with three domains: domain 1 has a β-l-rhamnosyltransferase activity, domain 2 has an α-l-rhamnosyltransferase activity, and domain 3 is a methyltransferase that decorates two positions in the terminal α-l-rhamnose (Rha) unit.
31412214	7	44	gly	glycosylation	1421:1433	arg2	N-linked glycosylation site mutant CD59			N-linked glycosylation site mutant CD59						site	Our results suggest that CD59 is retrotranslocated from the endoplasmic reticulum to the cytosol, a process mediated by recognition of trimmed N-linked oligosaccharides, supported by the partial glycosylation of non-GPI-anchored cytosolic CD59 as well as the failure of N-linked glycosylation site mutant CD59 to reach the cytosol or rescue GSIS.
30673210	7	71	part_of	proteins	1473:1480	arg1	270 unique N-glycosylation sites	proteins		270 unique N-glycosylation sites		Fterm	Site	proteins		sites	In addition, 270 unique N-glycosylation sites of 400 unique glycopeptides from 146 glycosylated proteins were identified from the triplicate analysis of 2 μL human serum.
30673210	7	71	part_of	proteins	1473:1480	arg1	400 unique glycopeptides	proteins		400 unique glycopeptides		Fterm	Site	proteins		glycopeptides	In addition, 270 unique N-glycosylation sites of 400 unique glycopeptides from 146 glycosylated proteins were identified from the triplicate analysis of 2 μL human serum.
30673210	7	83	part_of	sites	1417:1421	arg1	146 glycosylated proteins	proteins		sites		Fterm	Site	proteins		sites	In addition, 270 unique N-glycosylation sites of 400 unique glycopeptides from 146 glycosylated proteins were identified from the triplicate analysis of 2 μL human serum.
29729312	7	62	gly	His6	1149:1152	arg1	a His6 tag			His6	a His6 tag					His6	Recombinant ScGILT fused with a His6 tag was expressed and purified, and could reduce the interchain disulfide bonds of IgG at pH 4.5.
29446564	6	30	gly	sialylated	1159:1168	arg1	sialylated glycans				sialylated glycans						PMM extracts contained a wide variety of glycoproteins with different sugar residues, including abundant high-mannose and complex sialylated glycans.
29446564	6	36	gly	glycoproteins	1070:1082	arg1	glycoproteins	glycoproteins			abundant high-mannose	Fterm		glycoproteins			PMM extracts contained a wide variety of glycoproteins with different sugar residues, including abundant high-mannose and complex sialylated glycans.
29446564	6	36	gly	glycoproteins	1070:1082	arg1	glycoproteins	glycoproteins			different sugar residues	Fterm		glycoproteins			PMM extracts contained a wide variety of glycoproteins with different sugar residues, including abundant high-mannose and complex sialylated glycans.
30299005	5	3	gly	glycoproteins	907:919	arg1	therapeutic glycoproteins	therapeutic glycoproteins				Fterm		glycoproteins			When therapeutic glycoproteins containing non-Fc N-linked glycans were expressed in transient ExpiCHO-S™, the glycan pattern was unexpectedly found to have few sialylated N-glycans, in contrast to glycans produced within a stable CHO expression system.
30299005	5	40	gly	sialylated	1050:1059	arg1	few sialylated N-glycans				few sialylated N-glycans						When therapeutic glycoproteins containing non-Fc N-linked glycans were expressed in transient ExpiCHO-S™, the glycan pattern was unexpectedly found to have few sialylated N-glycans, in contrast to glycans produced within a stable CHO expression system.
30299005	5	21	gly	containing	921:930	arg1	therapeutic glycoproteins AND non-Fc N-linked glycans	therapeutic glycoproteins			non-Fc N-linked glycans	Fterm		glycoproteins			When therapeutic glycoproteins containing non-Fc N-linked glycans were expressed in transient ExpiCHO-S™, the glycan pattern was unexpectedly found to have few sialylated N-glycans, in contrast to glycans produced within a stable CHO expression system.
31838283	4	15	part_of	Fd	835:836	arg1	the Fd fragment	Fd		the Fd fragment		Cterm	Site	Fd		fragment	2-AA labelled glycan structures were annotated by CE-MS profiling in combination with exoglycosidase sequencing, revealing potential structures with terminal α-galactose and N-glycolyl-neuraminic acid (NGNA) mainly originating from the Fd fragment.
29675740	1	8	gly	glycoprotein	387:398	arg1	the glycoprotein	the glycoprotein				Fterm		glycoprotein			To elucidate the relationship between the protein function and the diversity and heterogeneity of glycans conjugated to the protein, glycosylation sites, glycan variation, and glycan proportions at each site of the glycoprotein must be analyzed.
29675740	1	29	gly	glycosylation	305:317	arg2	glycosylation sites			glycosylation sites						sites	To elucidate the relationship between the protein function and the diversity and heterogeneity of glycans conjugated to the protein, glycosylation sites, glycan variation, and glycan proportions at each site of the glycoprotein must be analyzed.
29675740	1	51	gly	heterogeneity	253:265	arg1	glycans				glycans						To elucidate the relationship between the protein function and the diversity and heterogeneity of glycans conjugated to the protein, glycosylation sites, glycan variation, and glycan proportions at each site of the glycoprotein must be analyzed.
30733536	9	34	gly	sialylated	1239:1248	arg1	several sialylated glycans				several sialylated glycans						In the process of characterisation, several sialylated glycans were subjected sequentially to two different alkylamidation reactions; this derivatisation helped to distinguish α2,3-linkage and α2,6-linkage sialyl isomers with mass spectrometry.
29976678	6	28	part_of	epitopes	805:812	arg1	E domains I and II	epitopes		E domains I and II						domains	We observed that mutants bearing FLAG epitopes in E domains I and II and the E domain I-II hinge region were all neutralized by FLAG antibody; however, the neutralization sensitivity varied highly.
29976678	6	65	part_of	region	864:869	arg1	E domains I and II	region		E domains I and II						domains	We observed that mutants bearing FLAG epitopes in E domains I and II and the E domain I-II hinge region were all neutralized by FLAG antibody; however, the neutralization sensitivity varied highly.
29931153	4	11	gly	glycoprotein	888:899	arg1	the carrier glycoprotein	the carrier glycoprotein				Fterm		glycoprotein			On the other hand, the influence of the 3D structure of the carrier glycoprotein on N-glycan maturation has been investigated mostly using individual model glycoproteins.
29931153	4	98	gly	glycoproteins	976:988	arg1	individual model glycoproteins	individual model glycoproteins				Fterm		glycoproteins			On the other hand, the influence of the 3D structure of the carrier glycoprotein on N-glycan maturation has been investigated mostly using individual model glycoproteins.
31062865	6	3	part_of	EPO	1438:1440	arg1	the three EPO N-sites	EPO		the three EPO N-sites		PUBTATOR	Site	EPO	P01588	N-sites	EPO-Fc protein generated in EX medium produced more complex tetra-antennary N-glycans at each of the three EPO N-sites while IA medium resulted in a greater fraction of bi- and tri-antennary N-glycans at these same sites.
31010286	1	20	gly	glycoprotein	364:375	arg1	the HIV-1 envelope glycoprotein spike	the HIV-1 envelope glycoprotein spike				Fterm		glycoprotein			Lipooligosaccharides (LOS) from the bacterium Rhizobium radiobacter Rv3 are structurally related to antigenic mammalian oligomannoses on the HIV-1 envelope glycoprotein spike that are targets for broadly neutralizing antibodies.
31010286	1	24	gly	oligomannoses	328:340	arg1	the HIV-1 envelope glycoprotein spike	glycoprotein			oligomannoses	Fterm		glycoprotein			Lipooligosaccharides (LOS) from the bacterium Rhizobium radiobacter Rv3 are structurally related to antigenic mammalian oligomannoses on the HIV-1 envelope glycoprotein spike that are targets for broadly neutralizing antibodies.
31364262	5	23	gly	compositional	1070:1082	arg1	42 N-glycans			position	42 N-glycans					position	Spatial distribution of 14 N-glycans is obtained by MALDI-MSI and 42 N-glycans (including structural and compositional isomers) identified and structurally characterized by LC-MS.
30389987	7	24	gly	peptide	1506:1512	arg1	the reducing-end sugar			peptide	the reducing-end sugar					peptide	Further, the carboxylate group of a conserved aspartate of PglB mediates an interaction network between the reducing-end sugar of the LLO, the asparagine side chain of the acceptor peptide, and a bound divalent metal ion.
29580922	11	47	gly	sialylated	1692:1701	arg1	Tri-antennary and sialylated N-glycans				Tri-antennary and sialylated N-glycans						CONCLUSIONS: Tri-antennary and sialylated N-glycans on haptoglobin at the Asn207 and Asn211 sites were abundant in SSCs and characteristic of extreme human longevity.
31608555	7	56	part_of	protein	1388:1394	arg1	the active site	protein		the active site		Fterm	Site	protein		site	In addition, structural data confirms the paradoxical behavior of glucose, where it replaces the high-affinity ligand(s) (disaccharide α-glycosides) from the active site of the protein.
31370181	2	70	part_of	B	371:371	arg1	the large soluble ectodomain	glycoprotein B		the large soluble ectodomain		Fterm	Site	glycoprotein B		ectodomain	The aim of this study consisted of expressing the large soluble ectodomain of glycoprotein B (gB) from Human Cytomegalovirus (HMCV) in Nicotiana tabacum Bright Yellow-2 (BY-2) suspension cells and of comparing its glycosylation profile with that of gB produced in Chinese hamster ovary (CHO) cells.
29603058	2	36	gly	glycoproteins	755:767	arg1	mammalian model glycoproteins	mammalian model glycoproteins				Fterm		glycoproteins			We used porous graphitized carbon-LC-ESI-MS/MS to separate and detect released N- and O-glycan isomers from mammalian model glycoproteins using negative mode resonance activation CID-MS/MS.
30102512	2	5	gly	composition	345:355	arg1	The mAb glycans			position	The mAb glycans					position	The mAb glycans are inherently heterogeneous in chemical structure and composition of monosaccharides.
29739851	4	45	gly	region	1349:1354	arg1	sialylation			region	sialylation					region	This strategy enabled detailed structural characterization of linkage regions, internal oligosaccharides, and nonreducing ends, revealing not only differences between xyloside-primed chondroitin/dermatan sulfate from HCC70 cells and CCD-1095Sk cells, but also sialylation of the linkage region and previously undescribed methylation and sulfation of the nonreducing ends.
29739851	4	72	gly	sialylation	1322:1332	arg1	the linkage region			the linkage region						region	This strategy enabled detailed structural characterization of linkage regions, internal oligosaccharides, and nonreducing ends, revealing not only differences between xyloside-primed chondroitin/dermatan sulfate from HCC70 cells and CCD-1095Sk cells, but also sialylation of the linkage region and previously undescribed methylation and sulfation of the nonreducing ends.
31771413	7	11	gly	glycoproteins	1173:1185	arg1	C. elegans surface glycoproteins	C. elegans surface glycoproteins				Fterm		glycoproteins			Although increased resistance to the infection might be related to lack of regular recognition of C. elegans surface glycoproteins by microbial agents, we provide genetic evidence that pmr-1 interfered nematodes mounted a stronger innate immune response to Gram-positive bacterial infection.
29231704	5	91	gly	glycopeptides	749:761	arg2	The glycopeptides			The glycopeptides						glycopeptides	The glycopeptides were separated using reversed-phase ultra high-performance liquid chromatography (UHPLC) to generate four fractions corresponding to different peptide backbones.
31737090	2	47	gly	glycoprotein	476:487	arg1	an N-linked glycoprotein	an N-linked glycoprotein				Fterm		glycoprotein			In the present study, a recombinant exo-inulinase (rKcINU1), derived from Kluyveromyces cicerisporus CBS4857, was proven as an N-linked glycoprotein, and the removal of N-linked glycan chains led to reduced activity.
31737090	2	47	gly	glycoprotein	476:487	arg1	a recombinant exo-inulinase	a recombinant exo-inulinase				Fterm		exo-inulinase			In the present study, a recombinant exo-inulinase (rKcINU1), derived from Kluyveromyces cicerisporus CBS4857, was proven as an N-linked glycoprotein, and the removal of N-linked glycan chains led to reduced activity.
30134158	4	31	gly	glycosylation	566:578	arg1	gp120 and gp41 subunits	gp120 and gp41 subunits				Fterm		subunits			Here, we compare the overall glycosylation of gp120 and gp41 subunits from BG505 (clade A) virions produced in a lymphoid cell line with those from recombinant BG505 SOSIP trimers, including CHO-derived clinical grade material.
30503907	1	29	gly	structures	122:131	arg1	hemagglutinin	hemagglutinin			structures	Fterm		hemagglutinin			Glycan structures on hemagglutinin (HA) of influenza A viruses have been analyzed previously to understand their significance.
30111774	4	28	gly	sialylated	603:612	arg1	sialylated structures				sialylated structures						Flow cytometry analysis showed that L2A5 specifically binds to sialylated structures on the cell surface of STn-expressing breast and bladder cancer cell lines.
29408873	2	71	part_of	IgG2c	501:505	arg1	the mouse IgG2c crystallizable fragment	IgG2c		the mouse IgG2c crystallizable fragment		Cterm	Site	IgG2c		fragment	Here we probe the structure and receptor-binding properties of the mouse IgG2c crystallizable fragment (Fc) to compare to mouse IgG2b and human IgG1 Fcs.
31507595	9	44	gly	di-sialylated	1660:1672	arg1	O-glycan core type-2 di-sialylated structures				O-glycan core type-2 di-sialylated structures						In addition, O-glycan core type-2 di-sialylated structures at Ser12 were more abundant in bioactive CD52 fractions.
31507595	9	98	gly	Ser12	1688:1692	arg1	O-glycan core type-2 di-sialylated structures			Ser12	O-glycan core type-2 di-sialylated structures					Ser12	In addition, O-glycan core type-2 di-sialylated structures at Ser12 were more abundant in bioactive CD52 fractions.
29648454	0	43	gly	Glycosylation	19:31	arg1	Recombinant Windmill Palm Tree Peroxidase	Recombinant Windmill Palm Tree Peroxidase				Fterm		Peroxidase			Effect of N-Linked Glycosylation of Recombinant Windmill Palm Tree Peroxidase on Its Activity and Stability.
31117584	4	58	gly	N-glycopeptide	826:839	arg2	the intact N-glycopeptide search engine			the intact N-glycopeptide search engine						N-glycopeptide	Here we report our development of the intact N-glycopeptide search engine GPSeeker and the GPSeeker-centered quantitative structural N-glycoproteomics pipeline.
31809011	6	56	part_of	Fc	936:937	arg1	the immunoglobulin G1 (IgG1) Fc fragment	Fc		the immunoglobulin G1 (IgG1) Fc fragment		Cterm	Site	Fc		fragment	As a proof of principle, the glycoproteomic N-glycan type quantitative (glyco-TQ) method was first used to determine the N-glycan type composition of the immunoglobulin G1 (IgG1) Fc fragment.
31809011	6	73	part_of	G1	926:927	arg1	the immunoglobulin G1 (IgG1) Fc fragment	G1 (IgG1		the immunoglobulin G1 (IgG1) Fc fragment		OGER	Site	G1 (IgG1	P01857	fragment	As a proof of principle, the glycoproteomic N-glycan type quantitative (glyco-TQ) method was first used to determine the N-glycan type composition of the immunoglobulin G1 (IgG1) Fc fragment.
29405331	4	94	gly	glycopeptides	691:703	arg1	similar glycan structures			glycopeptides	similar glycan structures					glycopeptides	Sialidase was used to remove the sialic acids in order to simplify the glycosylation microheterogeneity and to enhance the MS signal of glycopeptides with similar glycan structures.
29620509	11	76	gly	glycoprotein	1741:1752	arg1	glycoprotein	glycoprotein				Fterm		glycoprotein			Our method might throw a light on the expression and purification of glycoprotein for structural and functional studies.
31040211	2	43	part_of	E2	397:398	arg1	hypervariable region 1	E2		hypervariable region 1		Cterm	Site	E2		region	However, this effort has proven challenging because HCV evades neutralizing antibodies (NAbs) through molecular features of viral envelope glycoprotein E2, including hypervariable region 1 (HVR1) and N-linked glycans.
30999248	16	58	gly	glycoprotein	2390:2401	arg1	glycoprotein mAb	glycoprotein mAb				Fterm		glycoprotein			We further successfully applied our approach to profiling and subsequent structure assignment of glycans released from glycoprotein mAb, which was in perfect agreement with previous studies and CE analysis.
29579062	11	42	gly	microheterogeneity	2053:2070	arg1	N-linked glycans				N-linked glycans						Overall, our data demonstrate that HIV-1 isolates display differential sensitivity to lectins, in part due to the microheterogeneity of N-linked glycans expressed on the surface of the virus Env glycoprotein.
29725729	2	43	gly	glycoprotein	349:360	arg1	Each glycoprotein	Each glycoprotein				Fterm		glycoprotein			Each glycoprotein may have multiple glycoforms, and cancer-related ones can be only some specific glycoforms which have much higher sensitivity and specificity; for example, AFP glycoform AFP-L3 with N-glycan of 01Y(61F)41Y41M(31M41Y41L41S61M41Y41L41S is of bigger diagnostic value for hepatocellular carcinoma than total AFP (i.e., combination of all glycoforms).
30295034	9	23	gly	glycoproteins	1509:1521	arg1	desialylated glycoproteins	desialylated glycoproteins				Fterm		glycoproteins			AGP from human plasma samples of single individuals was analyzed as desialylated glycoproteins and showed variations in fucosylation and in the amount of antennary structures between individuals.
30295034	9	70	gly	desialylated	1496:1507	arg1	desialylated glycoproteins	desialylated glycoproteins				Fterm		glycoproteins			AGP from human plasma samples of single individuals was analyzed as desialylated glycoproteins and showed variations in fucosylation and in the amount of antennary structures between individuals.
31557542	8	33	part_of	CMP	1355:1357	arg1	the CMP binding positions	CMP		the CMP binding positions		OGER	Site	CMP	P21941	positions	In addition, we predicted CMP binding positions of human ST3GAL enzyme family on three-dimensional structure using molecular docking and first demonstrated the sialylmotifs relation with the CMP binding positions in ST3Gal III-VI subfamilies.
31557542	8	46	part_of	CMP	1190:1192	arg1	CMP binding positions	CMP		CMP binding positions		OGER	Site	CMP	P21941	positions	In addition, we predicted CMP binding positions of human ST3GAL enzyme family on three-dimensional structure using molecular docking and first demonstrated the sialylmotifs relation with the CMP binding positions in ST3Gal III-VI subfamilies.
31062865	3	25	part_of	G1	798:799	arg1	the Fc region	G1 (IgG1		the Fc region		OGER	Site	G1 (IgG1	P01857	region	EPO-Fc, containing the Fc region of immunoglobulin G1 (IgG1) fused to EPO, was harvested at Day 5 and 8 of a batch cell culture process followed by purification and N- and O-glycopeptide profiling.
31062865	3	98	part_of	containing	755:764	arg1	EPO-Fc AND the Fc region	EPO-Fc		the Fc region		PUBTATOR	Site	EPO	P01588	region	EPO-Fc, containing the Fc region of immunoglobulin G1 (IgG1) fused to EPO, was harvested at Day 5 and 8 of a batch cell culture process followed by purification and N- and O-glycopeptide profiling.
30242110	1	9	gly	glycoprotein	222:233	arg1	glycoprotein characteristics	glycoprotein characteristics				Fterm		glycoprotein			N-Glycosylation is a fundamentally important protein modification with a major impact on glycoprotein characteristics such as serum half-life and receptor interaction.
30943309	3	45	gly	de-sialylated	502:514	arg1	de-sialylated N-glycans				de-sialylated N-glycans						All melanoma variants and EVs have nearly identical profiles of de-sialylated N-glycans.
30902814	10	12	gly	glycosylation	1514:1526	arg2	four glycosylation sites			four glycosylation sites						sites	In silico docking experiments with the recently published cryo-EM structure of the M41 IBV spike protein and our glycosylation results revealed a potential ligand receptor site that is ringed by four glycosylation sites that dramatically impact ligand binding.
30782654	4	114	part_of	LCP	734:736	arg1	the conserved LCP domain	LCP		the conserved LCP domain		Cterm	Site	LCP	Q6NYC1	domain	Here we show by X-ray crystallography that LcpA adopts an α-β-α structural fold, akin to the conserved LCP domain, which harbors characteristic catalytic arginine residues.
30348313	4	26	gly	modified	477:484	arg3	this nuclease AND high-mannose type N-glycosylation	this nuclease			high-mannose type N-glycosylation	Fterm		nuclease			In this work, it was found that this nuclease is modified by high-mannose type N-glycosylation with a certain degree of macro- and microheterogeneity.
30295034	1	89	part_of	protein	205:211	arg1	five N-type glycosylation sites	protein		five N-type glycosylation sites		Fterm	Site	protein		sites	Alpha-1-acid glycoprotein (AGP) is a highly glycosylated protein from human plasma with five N-type glycosylation sites carrying dominantly higher antennary structures and thus represents a challenging target for characterization of glycan heterogeneity.
31349756	4	26	gly	O-glycosylation	719:733	arg2	N- and O-glycosylation sites			N- and O-glycosylation sites						sites	First, N- and O-glycosylation sites and their corresponding glycoforms were identified.
31719148	4	73	gly	glycoproteins	812:824	arg1	complex dodecameric quaternary structures	glycoproteins			complex dodecameric quaternary structures	Fterm		glycoproteins			Mollusk hemocyanins, such as Concholepas concholepas (CCH), Fissurella latimarginata (FLH), and Megathura crenulata (KLH), are oligomeric glycoproteins with complex dodecameric quaternary structures and heterogeneous glycosylation patterns, primarily consisting of mannose-rich N-glycans.
31611356	4	59	gly	N448	810:813	arg1	glycan absence			N448	glycan absence					N448	In addition to a significant loss of Grft activity by the removal of glycosylation at N295, glycan absence at N332 or N448 was found to have moderate effects on Grft potency.
31611356	4	72	gly	N332	802:805	arg1	glycan absence			N332	glycan absence					N332	In addition to a significant loss of Grft activity by the removal of glycosylation at N295, glycan absence at N332 or N448 was found to have moderate effects on Grft potency.
30144627	2	8	gly	glycosylation	525:537	arg2	8 glycosylation sites			8 glycosylation sites						sites	This heterodimeric protein is specific to human pregnancy, consists in an α and a β subunit, so-called hCGα and hCGβ, respectively, and has 8 glycosylation sites leading to a high number of isoforms.
29411222	10	16	gly	O-glycopeptide	1514:1527	arg2	O-glycopeptide analysis			O-glycopeptide analysis						O-glycopeptide	For both, N- and O-glycopeptide analysis, determination was achieved without prior cleavage of the sialic acid residues for the first time.
31819007	5	45	gly	glycoproteins	825:837	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Using immunoblotting, flow cytometry, and LC-MS-based glycolipid and glycan profiling, we found that CRISPR/Cas9-mediated GALE deletion in human cells triggers major imbalances in NSs and dramatic changes in glycolipids and glycoproteins, including a subset of integrins and the cell-surface death receptor FS-7-associated surface antigen.
31751705	1	22	gly	N-glycopeptides	274:288	arg2	N-glycopeptides			N-glycopeptides						N-glycopeptides	In the present study, for the discovery of uncharacterized glycan-binding receptors or lectin-like receptors in plants, we developed neoglycopolymers to which three types of N-glycopeptides are conjugated; the first with plant complex type N-glycan (M3FX), the second with high-mannose type N-glycan (M8), and the third with animal complex type N-glycan (NeuAc2Gal2GN2M3).
31591262	6	74	gly	glycopeptides	1018:1030	arg2	glycopeptides			glycopeptides						fragments, glycopeptides	Protein glycosylation was determined in various ways, including at the level of intact mAb, protein fragments, glycopeptides, or released glycans, using a wide variety of methods for derivatization, separation, identification, and quantification.
31375533	3	7	gly	epitopes	367:374	arg1	N-glycans			epitopes	N-glycans					epitopes	Here we found that bisecting GlcNAc, a branching sugar residue in N-glycan, suppresses the biosynthesis of various types of terminal epitopes in N-glycans, including fucose, sialic acid and human natural killer-1.
31375533	3	22	gly	epitopes	367:374	arg1	sialic acid			epitopes	sialic acid					epitopes	Here we found that bisecting GlcNAc, a branching sugar residue in N-glycan, suppresses the biosynthesis of various types of terminal epitopes in N-glycans, including fucose, sialic acid and human natural killer-1.
31375533	3	22	gly	epitopes	367:374	arg1	fucose			epitopes	fucose					epitopes	Here we found that bisecting GlcNAc, a branching sugar residue in N-glycan, suppresses the biosynthesis of various types of terminal epitopes in N-glycans, including fucose, sialic acid and human natural killer-1.
31375533	3	45	gly	residue	289:295	arg1	N-glycan			residue in	N-glycan					residue in	Here we found that bisecting GlcNAc, a branching sugar residue in N-glycan, suppresses the biosynthesis of various types of terminal epitopes in N-glycans, including fucose, sialic acid and human natural killer-1.
31541622	9	53	gly	O-glycoproteins	1423:1437	arg1	O-glycoproteins	O-glycoproteins				Fterm		O-glycoproteins			We predicted O-glycoproteins and O-glycan compositions for the first time for this organism.
30213862	8	7	gly	N-glycosylation	1269:1283	arg2	the four other N-glycosylation sites			the four other N-glycosylation sites						sites	This remarkable sensitivity could only be eliminated by preventing glycosylation at N162 with an Asn to Gln mutation; mutations at the four other N-glycosylation sites preserved tighter binding in the Man5 glycoform.
30213862	8	29	gly	glycoform	1329:1337	arg1	the Man5 glycoform				the Man5 glycoform						This remarkable sensitivity could only be eliminated by preventing glycosylation at N162 with an Asn to Gln mutation; mutations at the four other N-glycosylation sites preserved tighter binding in the Man5 glycoform.
30213862	8	37	gly	glycosylation	1190:1202	arg1	N162			Asn						Asn	This remarkable sensitivity could only be eliminated by preventing glycosylation at N162 with an Asn to Gln mutation; mutations at the four other N-glycosylation sites preserved tighter binding in the Man5 glycoform.
30673210	5	80	gly	glycopeptide	1180:1191	arg2	glycopeptide			glycopeptide						glycopeptide	The biomimetic membrane could identify as many as 32 N-glycopeptides from the IgG digest, exhibiting high sensitivity (about 50 fmol) and a wide scope for glycopeptide enrichment.
30673210	5	106	gly	N-glycopeptides	1078:1092	arg2	32 N-glycopeptides			32 N-glycopeptides						N-glycopeptides	The biomimetic membrane could identify as many as 32 N-glycopeptides from the IgG digest, exhibiting high sensitivity (about 50 fmol) and a wide scope for glycopeptide enrichment.
30111543	1	56	gly	glycosylation	79:91	arg1	plasma proteins	plasma proteins				Fterm		proteins			Altered glycosylation patterns of plasma proteins are associated with autoimmune disorders and pathogenesis of various cancers.
29562594	1	78	gly	residues	253:260	arg1	glycoproteins	glycoproteins			residues	Fterm		glycoproteins			Kifunensine, a potent and selective inhibitor of class I α-mannosidases, prevents α-mannosidases I from trimming mannose residues on glycoproteins, thus resulting in oligomannose-type glycans.
29562594	1	86	gly	glycoproteins	265:277	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Kifunensine, a potent and selective inhibitor of class I α-mannosidases, prevents α-mannosidases I from trimming mannose residues on glycoproteins, thus resulting in oligomannose-type glycans.
31301102	7	47	part_of	Fc	1412:1413	arg1	the Fc region	Fc		the Fc region		Cterm	Site	Fc		region	However, this was independent of plant glycosylation, but related to the oxidation status of two methionine residues in the Fc region.
30990348	7	100	part_of	region	1502:1507	arg1	the CH2 domain	region		the CH2 domain						domain	Considering that mAbs interact with FcγR and C1q via their hinge proximal region in the CH2 domain, the structural stabilization of the CH2 domain by the terminal Gal residue on the Man α1-6 arm of Fc-glycans may be important for the effector functions of mAbs.
29333671	2	57	gly	glycopeptides	464:476	arg2	glycopeptides			glycopeptides						glycopeptides	In this study, a customized dextran-bonded silica-based stationary phase was introduced for selective enrichment of glycopeptides and glycans from complex biological samples.
30649348	5	53	gly	sialylated	759:768	arg1	sialylated O-glycans				sialylated O-glycans						Furthermore, sialylated O-glycans have been proposed to play a central role in tumour immune escape by modulating the production of immunoregulatory cytokines and growth factors through interactions with sialic acid-binding immunoglobulin-like lectins.
29600528	5	38	gly	asialoglycoprotein	1095:1112	arg1	asialoglycoprotein (ASGP) receptor-rich HepG2 cells	asialoglycoprotein (ASGP) receptor-rich HepG2 cells				Fterm		asialoglycoprotein			More importantly, comparing with the galactose-free fluorescent hyperbranched polymers h-P(OEGMA-co-VBPT-co-BYMA), hPEVB FNPs can be selectively internalized by asialoglycoprotein (ASGP) receptor-rich HepG2 cells, indicating their potential application in the bioimaging fields.
30733536	2	36	gly	glycosylation	220:232	arg2	Asn residues			Asn residues						Asn residues	N-linked glycosylation is involved in stability and function of these proteins and occurs at Asn residues.
31154130	4	54	part_of	IgG-Fc	683:688	arg1	IgG-Fc glycopeptides	IgG		IgG-Fc glycopeptides		Cterm	Site	IgG		glycopeptides	We herein report an integrated approach for comprehensive profiling and quantitation of IgG-Fc glycopeptides.
30144627	2	34	part_of	has	519:521	arg1	This heterodimeric protein AND 8 glycosylation sites	This heterodimeric protein		8 glycosylation sites		Fterm	Site	protein		sites	This heterodimeric protein is specific to human pregnancy, consists in an α and a β subunit, so-called hCGα and hCGβ, respectively, and has 8 glycosylation sites leading to a high number of isoforms.
30186849	4	21	gly	glycopeptides	809:821	arg2	glycopeptides			glycopeptides						glycopeptides	In pMatchGlyco, (1) MS/MS spectra of deglycopeptides are used to create spectral library, (2) MS/MS spectra of glycopeptides are matched to the spectra in library in an open (precursor tolerant) manner and the glycans are inferred, and (3) a false discovery rate is estimated for top-scored matches above a threshold.
30186849	4	40	gly	deglycopeptides	735:749	arg2	deglycopeptides			deglycopeptides						deglycopeptides	In pMatchGlyco, (1) MS/MS spectra of deglycopeptides are used to create spectral library, (2) MS/MS spectra of glycopeptides are matched to the spectra in library in an open (precursor tolerant) manner and the glycans are inferred, and (3) a false discovery rate is estimated for top-scored matches above a threshold.
31216452	1	59	gly	glycoprotein	173:184	arg1	a glycoprotein growth factor	a glycoprotein growth factor				Fterm		glycoprotein			Recombinant human erythropoietin (rHuEPO) as a glycoprotein growth factor has been considered a biological drug for treatment of anemic patients with chronic renal failure or who receive cancer chemotherapy.
31669586	13	74	gly	N-glycosylation	1699:1713	arg1	serum proteins	serum proteins				Fterm		proteins			The obtained results complete our previous IgG N-glycosylation analysis in autoimmune thyroid patients and show that the altered N-glycosylation of serum proteins is characteristic for autoimmunity process in HT.
29936827	2	7	gly	glycosylated	272:283	arg1	mammalian cellular proteins	mammalian cellular proteins				Fterm		proteins			Over 50% of mammalian cellular proteins are typically glycosylated; this modification is involved in a wide range of biological functions such as barrier formation against intestinal microbes and serves as signaling molecules for selectins and galectins in the innate immune system.
31393126	3	12	gly	heterogeneity	582:594	arg1	RJ glycoproteins	RJ glycoproteins				Fterm		glycoproteins			Here, a combined glycomics and glycoproteomics strategy was developed for the site-specific analysis of N-linked glycosylation heterogeneity of RJ glycoproteins.
31393126	3	54	gly	glycoproteins	602:614	arg1	RJ glycoproteins	RJ glycoproteins				Fterm		glycoproteins			Here, a combined glycomics and glycoproteomics strategy was developed for the site-specific analysis of N-linked glycosylation heterogeneity of RJ glycoproteins.
31393126	3	65	gly	glycosylation	568:580	arg1	RJ glycoproteins	RJ glycoproteins				Fterm		glycoproteins			Here, a combined glycomics and glycoproteomics strategy was developed for the site-specific analysis of N-linked glycosylation heterogeneity of RJ glycoproteins.
30503329	3	24	gly	glycoproteins	517:529	arg1	cell wall glycoproteins	cell wall glycoproteins				Fterm		glycoproteins			In this report we demonstrate that Neurospora crassa GH72 glucan transferases function to crosslink cell wall glycoproteins into the cell wall.
30659587	3	11	gly	sialylated	627:636	arg1	high mannose				high mannose						By adding media supplements at specific concentrations in cell culture and applying enzymatic glycoengineering, a diverse N-glycan variant population was generated, including high mannose, afucosylated, fucosylated, agalactosylated, galactosylated, asialylated, and sialylated forms.
30659587	3	78	gly	asialylated	610:620	arg1	high mannose				high mannose						By adding media supplements at specific concentrations in cell culture and applying enzymatic glycoengineering, a diverse N-glycan variant population was generated, including high mannose, afucosylated, fucosylated, agalactosylated, galactosylated, asialylated, and sialylated forms.
30659587	3	83	gly	fucosylated	564:574	arg1	high mannose				high mannose						By adding media supplements at specific concentrations in cell culture and applying enzymatic glycoengineering, a diverse N-glycan variant population was generated, including high mannose, afucosylated, fucosylated, agalactosylated, galactosylated, asialylated, and sialylated forms.
30659587	3	86	gly	afucosylated	550:561	arg1	high mannose				high mannose						By adding media supplements at specific concentrations in cell culture and applying enzymatic glycoengineering, a diverse N-glycan variant population was generated, including high mannose, afucosylated, fucosylated, agalactosylated, galactosylated, asialylated, and sialylated forms.
29709182	3	57	gly	glycans	729:735	arg1	the α-Neu5Ac-(2→3)-β-d-Gal-(1→4)-β-d-GlcNAc motif			the α-Neu5Ac-(2→3)-β-d-Gal-(1→4)-β-d-GlcNAc motif	the α-Neu5Ac-(2→3)-β-d-Gal-(1→4)-β-d-GlcNAc motif						This work also revealed that the α-Neu5Ac-(2→3)-β-d-Gal-(1→4)-β-d-GlcNAc motif, which is common in natural glycans, had a low reactivity as glycosyl donors, so it was rather difficult to directly couple this trisaccharide with sterically hindered acceptors.
31381874	7	3	gly	glycopeptide	1301:1312	arg2	glycopeptide			glycopeptide						glycopeptide	Quantitation of the azide incorporation showed an azide antibody ratio of 8 (glycan data) and 6-10 (glycopeptide data) which translates to a high drug antibody ratio based on IgG-ADC standards.
29675740	7	64	gly	glycopeptides	1391:1403	arg2	many glycopeptides			many glycopeptides						glycopeptides	As a result, many glycopeptides having long glycans were enriched in the highest hydrophilic fraction.
29675740	7	60	gly	having	1405:1410	arg1	many glycopeptides AND long glycans			many glycopeptides	long glycans					glycopeptides	As a result, many glycopeptides having long glycans were enriched in the highest hydrophilic fraction.
29671439	6	51	gly	glycoproteins	975:987	arg1	the glycan structure	glycoproteins			the glycan structure	Fterm		glycoproteins			The results of this study are expected to provide a reference for the glycan structure of ginger glycoproteins with ACE-inhibitory activity.
31108197	6	16	gly	sialylated	1227:1236	arg1	sialylated N-linked glycans				sialylated N-linked glycans						Man6GlcNAc2 was identified as the main high mannose N-linked structure that was decreased in adult while higher expression of sialylated N-linked glycans and lower core fucosylation for complex structures were associated with ageing.
30280442	5	40	gly	glycosylated	901:912	arg1	a "hyperbranched" fucose residue			a "hyperbranched" fucose residue						residue in	The target molecule includes a glucosyl-asparagine linkage and a "hyperbranched" fucose residue in which all of the hydroxyl groups are glycosylated.
30389987	5	15	gly	peptide	977:983	arg1	the GlcNAc moiety			peptide	the GlcNAc moiety					peptide	We found that the atoms forming the N-glycosidic bond (C-1 of the GlcNAc moiety of LLO and the -NH2 group of the peptide) are closer than in the previous structure, suggesting that we have captured a conformation closer to the transition state of the reaction.
30782654	13	94	gly	glycosylation	2685:2697	arg1	a cell wall-anchored protein	a cell wall-anchored protein				Fterm		protein			Our studies provide the first experimental evidence of an archetypal LCP enzyme that promotes glycosylation of a cell wall-anchored protein in Gram-positive bacteria.
29343613	3	66	part_of	sites	561:565	arg1	gp120	gp120		sites		PUBTATOR	Site	gp120	3700	sites	However, the promiscuity of CVN to associate with multiple glycosylation sites in gp120 and its multivalency limit current understanding of the molecular arrangement of the DAVEI molecules on trimeric spike.
31809011	5	50	gly	glycopeptide	639:650	arg2	each glycopeptide			each glycopeptide						glycopeptide	Taking advantage of the specificity of different endoglycosidases and isotope dimethyl labeling, six N-glycan types of structures linked on each glycopeptide, including high-mannose/hybrid, biantennary, and triantennary with/without core fucose, were quantified.
29949660	6	4	part_of	lignin	1255:1260	arg1	lignin composition	lignin		lignin composition		Fterm	Site	lignin		position	Alteration of lignin composition affects interactions with plant cell wall matrix polysaccharides to alter the sequestration of multiple latent defense signal molecules with an impact on biotic stress responses.
31884067	5	80	gly	glycoproteins	829:841	arg1	HNK-1 carrier glycoproteins				HNK-1 carrier glycoproteins						We also analyzed the expression levels of glycosyltransferases responsible for HNK-1 and of HNK-1 carrier glycoproteins by quantitative RT-PCR and western blotting.
29619832	4	19	gly	glycosylation	755:767	arg2	All three glycosylation sites			All three glycosylation sites						sites	All three glycosylation sites on the protein, expressed in human embryonic kidney (HEK) cells, were characterized individually using a mass spectrometry-based glycopeptide analysis workflow.
29619832	4	24	gly	glycopeptide	904:915	arg2	a mass spectrometry-based glycopeptide analysis workflow			a mass spectrometry-based glycopeptide analysis workflow						glycopeptide	All three glycosylation sites on the protein, expressed in human embryonic kidney (HEK) cells, were characterized individually using a mass spectrometry-based glycopeptide analysis workflow.
31100702	14	62	gly	glycoproteins	1867:1879	arg1	all mammalian glycoproteins	all mammalian glycoproteins				Fterm		glycoproteins			The polystyrene resin detergent removal step conserved the full N-glycan profile and could be applied to all mammalian glycoproteins tested.
30578591	3	58	gly	glycopeptide	426:437	arg2	intact glycopeptide analysis			intact glycopeptide analysis						glycopeptide	In this study, intact glycopeptide analysis is performed on an influenza NA (A/H1N1/California/2009) that is expressed in human 293T and insect Hi-5 cells.
31531180	0	5	part_of	Composition	9:19	arg1	Yingshan Cloud Mist Tea	Mist Tea		Composition		OGER	Site	Mist Tea	Q7Z7G1	position	Chemical Composition and Antioxidant Activities of Polysaccharides from Yingshan Cloud Mist Tea.
31531180	0	33	part_of	Tea	92:94	arg1	Chemical Composition	Mist Tea		Chemical Composition		OGER	Site	Mist Tea	Q7Z7G1	position	Chemical Composition and Antioxidant Activities of Polysaccharides from Yingshan Cloud Mist Tea.
29596681	1	53	gly	glycoproteins	220:232	arg1	therapeutic glycoproteins	glycoproteins			different glycan structures	Fterm		glycoproteins			Precise gene editing technologies are providing new opportunities to stably engineer host cells for recombinant production of therapeutic glycoproteins with different glycan structures.
29043680	4	18	gly	glycoproteins	490:502	arg1	Properly folded glycoproteins	Properly folded glycoproteins				Fterm		glycoproteins			Properly folded glycoproteins are released from these processes and allowed to continue their transit to the Golgi where further processing and maturation of N-glycans leads to the formation of more complex structures with different functions.
29992770	6	37	gly	N-glycopeptide	873:886	arg2	detailed N-glycopeptide information			detailed N-glycopeptide information						N-glycopeptide	RESULTS: Combined with a database search using web-based software (GlycopeptideID), MS/MS provided detailed N-glycopeptide information, including glycosylation site, glycan composition, and proposed structures.
30074304	1	35	gly	Glycosylation	117:129	arg1	circulating proteins	circulating proteins				Fterm		proteins			Glycosylation of cell surface, secreted, and circulating proteins is one of the most common types of post-translational modification.
29299842	4	56	gly	glycoproteins	552:564	arg1	cell-surface glycoproteins	cell-surface glycoproteins				Fterm		glycoproteins			Moreover, in pathogenic yeasts, glycans assembled on cell-surface glycoproteins can mediate their interactions with host cells.
29433940	1	10	gly	glycoproteins	168:180	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			A silkworm-baculovirus system is particularly effective for producing recombinant proteins, including glycoproteins.
30299005	0	25	gly	glycoproteins	118:130	arg1	therapeutic glycoproteins	therapeutic glycoproteins				Fterm		glycoproteins			Transient CHO expression platform for robust antibody production and its enhanced N-glycan sialylation on therapeutic glycoproteins.
30299005	0	80	gly	sialylation	91:101	arg1	therapeutic glycoproteins	glycoproteins			sialylation	Fterm		glycoproteins			Transient CHO expression platform for robust antibody production and its enhanced N-glycan sialylation on therapeutic glycoproteins.
29767770	8	2	part_of	PGM	1448:1450	arg1	another PGM motifs	PGM		another PGM motifs		OGER	Site	PGM	P13611	motifs	Chemical removal of O-linked oligosaccharides from PGM led to a significant increase of TNF-α cytokine levels, suggesting that their removal could exposure another PGM motifs able to induce a higher secretion of TNF-α levels.
29446564	5	21	part_of	proteins	871:878	arg1	composition	proteins		composition		Fterm	Site	proteins		position	We observed that the amount and composition of proteins and glycoproteins associated with different glycans structures changed over time in the intestines and PMM under different physiological conditions.
29446564	5	45	part_of	glycoproteins	884:896	arg1	composition	glycoproteins		composition		Fterm	Site	glycoproteins		position	We observed that the amount and composition of proteins and glycoproteins associated with different glycans structures changed over time in the intestines and PMM under different physiological conditions.
29931153	10	100	gly	N-glycosylated	1721:1734	arg1	the N-glycosylated site			the N-glycosylated site						site	Structural features of the protein surface around the N-glycosylated site do seem to affect N-glycan processing and maturation.
29775069	6	19	gly	glycoproteins	1350:1362	arg1	model glycoproteins	model glycoproteins				Fterm		glycoproteins			Using this technique, O- and N-glycans were simultaneously prepared from some model glycoproteins and complex biological samples, without significant peeling, desialylation, deacetylation, desulfation or other side-reactions, and then comprehensively analyzed by online HILIC-UV-ESI-MS/MS and RP-HPLC-UV-ESI-MS/MS, with which some novel O- and N-glycan structures were first found.
29437979	12	117	gly	N-glycosylation	1775:1789	arg2	all five N-glycosylation sites			all five N-glycosylation sites						sites	However, even simultaneous inactivation of all five N-glycosylation sites of gH did not severely inhibit formation of infectious virus particles.IMPORTANCE Herpesvirus infection requires fusion of the viral envelope with cellular membranes, which involves the conserved fusion machinery consisting of gB and the heterodimeric gH/gL complex.
29949660	0	70	part_of	lignin	60:65	arg1	altered lignin compositions	lignin		altered lignin compositions		Fterm	Site	lignin		positions	Elicitors and defense gene induction in plants with altered lignin compositions.
29921663	5	125	gly	glycopeptides	1012:1024	arg2	tryptic IgG glycopeptides			tryptic IgG glycopeptides						glycopeptides	Because of this, the differences in IgG Fc glycosylation between 60 pediatric meningococcal sepsis patients admitted to the pediatric intensive care unit and 46 age-matched healthy controls were investigated, employing liquid chromatography with mass spectrometric detection of tryptic IgG glycopeptides.
29408166	1	59	gly	fucosylation	227:238	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Recently, site-specific fucosylation of glycoproteins has attracted attention as it can be associated with several types of cancers including prostate cancer.
29408166	1	110	gly	glycoproteins	243:255	arg1	site-specific fucosylation	glycoproteins			site-specific fucosylation	Fterm		glycoproteins			Recently, site-specific fucosylation of glycoproteins has attracted attention as it can be associated with several types of cancers including prostate cancer.
29858715	6	22	gly	fucosylated	757:767	arg1	unusual highly fucosylated N-linked glycans				unusual highly fucosylated N-linked glycans						PIP carries unusual highly fucosylated N-linked glycans with multiple Lewisy (Ley) epitopes on bi-, tri- and tetraantennary structures resulting in up to nine fucosyl residues on a tetraantennary glycan.
29858715	6	25	gly	epitopes	813:820	arg1	tri-				tri-						PIP carries unusual highly fucosylated N-linked glycans with multiple Lewisy (Ley) epitopes on bi-, tri- and tetraantennary structures resulting in up to nine fucosyl residues on a tetraantennary glycan.
29858715	6	25	gly	epitopes	813:820	arg1	tetraantennary structures				tetraantennary structures						PIP carries unusual highly fucosylated N-linked glycans with multiple Lewisy (Ley) epitopes on bi-, tri- and tetraantennary structures resulting in up to nine fucosyl residues on a tetraantennary glycan.
29858715	6	25	gly	epitopes	813:820	arg1	bi-				bi-						PIP carries unusual highly fucosylated N-linked glycans with multiple Lewisy (Ley) epitopes on bi-, tri- and tetraantennary structures resulting in up to nine fucosyl residues on a tetraantennary glycan.
29858715	6	84	gly	residues	897:904	arg1	a tetraantennary glycan			residues	a tetraantennary glycan					residues	PIP carries unusual highly fucosylated N-linked glycans with multiple Lewisy (Ley) epitopes on bi-, tri- and tetraantennary structures resulting in up to nine fucosyl residues on a tetraantennary glycan.
30782654	3	22	gly	glycoprotein	525:536	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			In the actinobacterium Actinomyces oris, an LCP homolog here named LcpA is genetically linked to GspA, a glycoprotein that is covalently attached to the bacterial peptidoglycan by the housekeeping sortase SrtA.
31606074	3	29	gly	glycopeptide	230:241	arg2	the glycopeptide level			the glycopeptide level						glycopeptide	Studies at the glycopeptide level are typically considered as a downstream work resulting from enzymatic digested glycoproteins.
31606074	3	48	gly	glycoproteins	329:341	arg1	enzymatic digested glycoproteins	enzymatic digested glycoproteins				Fterm		glycoproteins			Studies at the glycopeptide level are typically considered as a downstream work resulting from enzymatic digested glycoproteins.
31501225	7	24	part_of	IgA2	1179:1182	arg1	the two glycopeptides	IgA2		the two glycopeptides		OGER	Site	IgA2	P01877	glycopeptides	In contrast, the two glycopeptides of IgA2 fell back down in HBV-related HCC patients.
31602612	3	22	gly	glycoproteins	466:478	arg1	yeast cell wall glycoproteins	glycoproteins			N-glycans	Fterm		glycoproteins			Here, we describe methods for data-independent acquisition (SWATH) mass spectrometry analysis of structure and occupancy of N-glycans from yeast cell wall glycoproteins.
30074767	5	76	gly	glycoprotein	530:541	arg1	glycoprotein	glycoprotein				Fterm		glycoprotein			Dane particles are covered with an envelope of glycoprotein called HBV surface antigen (HBsAg).
30935958	10	41	gly	positions	1204:1212	arg1	their glycans			positions	their glycans					positions	Little is known about the importance of these positions and their glycans for PrP stability, aggregation and fibril formation.
29535710	4	85	part_of	IgG	703:705	arg1	liquid chromatography electrospray mass spectrometry (LC-ESI-MS)-measured IgG glycopeptides	IgG		liquid chromatography electrospray mass spectrometry (LC-ESI-MS)-measured IgG glycopeptides		Cterm	Site	IgG		glycopeptides	To identify genetic loci involved in IgG glycosylation, we performed a genome-wide association study (GWAS) on liquid chromatography electrospray mass spectrometry (LC-ESI-MS)-measured IgG glycopeptides of 1,823 individuals in the Cooperative Health Research in the Augsburg Region (KORA F4) study cohort.
30063822	2	28	part_of	present	344:350	arg1	proteins AND single N-glycosylation sites	proteins		single N-glycosylation sites		Fterm	Site	proteins		sites	The procedure relies on the presence of single N-glycosylation sites that are present natively in proteins or that can be engineered into glycoproteins by mutational elimination of all but one glycosylation site.
29333671	4	1	gly	glycoprotein	724:735	arg1	α1 -acid glycoprotein	α1 -acid glycoprotein				Fterm		glycoprotein			Additionally, the glycomic analysis of fetuin, α1 -acid glycoprotein, and human serum N-glycome also indicated the relatively higher sensitivity, selectivity, and glycoform coverage of dextran-bonded silica than that of Sepharose and porous graphitized carbon.
29620509	5	71	gly	protein	722:728	arg1	The residual glycan	protein			The residual glycan	Fterm		protein			The residual glycan of purified protein was removed by endoglycosidase H. Finally, AP protein was removed by using human rhinovirus protease and size exclusion chromatography.
30899004	4	5	gly	N-glycosites	780:791	arg2	1,545 N-glycosites			1,545 N-glycosites						N-glycosites	Here we show that N-glycoproteome site-specific microheterogeneity can be captured via large-scale glycopeptide profiling methods enabled by activated ion electron transfer dissociation (AI-ETD), ultimately characterizing 1,545 N-glycosites (>5,600 unique N-glycopeptides) from mouse brain tissue.
30899004	4	5	gly	N-glycosites	780:791	arg2	>5,600 unique N-glycopeptides			>5,600 unique N-glycopeptides						N-glycopeptides	Here we show that N-glycoproteome site-specific microheterogeneity can be captured via large-scale glycopeptide profiling methods enabled by activated ion electron transfer dissociation (AI-ETD), ultimately characterizing 1,545 N-glycosites (>5,600 unique N-glycopeptides) from mouse brain tissue.
30899004	4	40	gly	glycopeptide	651:662	arg2	large-scale glycopeptide profiling methods			large-scale glycopeptide profiling methods						glycopeptide	Here we show that N-glycoproteome site-specific microheterogeneity can be captured via large-scale glycopeptide profiling methods enabled by activated ion electron transfer dissociation (AI-ETD), ultimately characterizing 1,545 N-glycosites (>5,600 unique N-glycopeptides) from mouse brain tissue.
30899004	4	45	gly	N-glycopeptides	808:822	arg2	1,545 N-glycosites			1,545 N-glycosites						N-glycosites	Here we show that N-glycoproteome site-specific microheterogeneity can be captured via large-scale glycopeptide profiling methods enabled by activated ion electron transfer dissociation (AI-ETD), ultimately characterizing 1,545 N-glycosites (>5,600 unique N-glycopeptides) from mouse brain tissue.
30899004	4	45	gly	N-glycopeptides	808:822	arg2	>5,600 unique N-glycopeptides			>5,600 unique N-glycopeptides						N-glycopeptides	Here we show that N-glycoproteome site-specific microheterogeneity can be captured via large-scale glycopeptide profiling methods enabled by activated ion electron transfer dissociation (AI-ETD), ultimately characterizing 1,545 N-glycosites (>5,600 unique N-glycopeptides) from mouse brain tissue.
30528732	7	55	gly	glycosylation	1240:1252	arg2	several glycosylation sites			several glycosylation sites						sites	With structural analysis, we found several glycosylation sites (such as T383, S8, and S46) are located at the openings of the substrate-binding tunnel, and potentially involve in the binding of cellulose.
29674057	4	6	gly	glycoforms	589:598	arg1	protein glycoforms	protein glycoforms				Fterm		protein			Yet, resolving protein glycoforms at the intact level is challenging.
30904681	8	30	gly	glycosylation	1242:1254	arg2	an unreported partially occupied fifth glycosylation site			an unreported partially occupied fifth glycosylation site						site	Two of our samples showed an unreported partially occupied fifth glycosylation site presumably arising from the presence of SNP variant S88N.
30659587	5	3	gly	glycosylation	914:926	arg2	The two fusion body glycosylation sites			The two fusion body glycosylation sites						sites	The two fusion body glycosylation sites were characterized by a high degree of sialic acid, more complex N-glycan structures, a higher degree of antennarity, and a site-specific behavior in the presence of a media supplement.
31316527	3	49	gly	N-glycosylation	713:727	arg2	the N-glycosylation site			the N-glycosylation site						site	Three variants were produced by targeting protein to plant apoplast (APO), endoplasmic reticulum (ER) or removing the N-glycosylation site by a point mutation (Agly).
30528732	0	56	gly	glycosylation	17:29	arg1	cellobiohydrolase I	cellobiohydrolase I				Fterm		cellobiohydrolase I			The diversity of glycosylation of cellobiohydrolase I from Trichoderma reesei determined with mass spectrometry.
30484241	2	15	gly	glycoproteins	384:396	arg1	homogeneous misfolded glycoproteins	homogeneous misfolded glycoproteins				Fterm		glycoproteins			To evaluate the role of oligosaccharides in protein folding, we synthesized small glycoprotein models, homogeneous misfolded glycoproteins, and erythropoietins.
30484241	2	31	gly	glycoprotein	341:352	arg1	small glycoprotein models	small glycoprotein models				Fterm		glycoprotein			To evaluate the role of oligosaccharides in protein folding, we synthesized small glycoprotein models, homogeneous misfolded glycoproteins, and erythropoietins.
31174130	7	19	gly	glycoproteins	1280:1292	arg1	human plasma glycoproteins	human plasma glycoproteins				Fterm		glycoproteins			The enrichment performance of the titania glyco-purification tip was tested using human plasma digest as a real-world complex sample and, 112 N-glycopeptides from human plasma glycoproteins were detected by the analysis of enriched samples by nLC-QTOF-MS/MS.
31174130	7	66	gly	N-glycopeptides	1246:1260	arg1	human plasma glycoproteins	glycoproteins		N-glycopeptides		Fterm		glycoproteins		N-glycopeptides	The enrichment performance of the titania glyco-purification tip was tested using human plasma digest as a real-world complex sample and, 112 N-glycopeptides from human plasma glycoproteins were detected by the analysis of enriched samples by nLC-QTOF-MS/MS.
31034685	9	53	part_of	β-casein	1361:1368	arg1	specific phosphorylation sites	β-casein		specific phosphorylation sites		Fterm	Site	β-casein		sites	RESULTS PGC/MS/MS enabled accurate quantitation of the stoichiometry of specific phosphorylation sites from β-casein by efficient separation of the phosphopeptide and its non-phosphorylated counterpart, which cannot be achieved by reversed-phase chromatography.
31362136	8	16	gly	modified	1045:1052	arg1	Hemicellulose domain AND increased xylose contents			Hemicellulose domain	increased xylose contents					domain	Hemicellulose domain was also modified under salt stress, with increased xylose contents.
30348313	9	1	gly	occupied	1231:1238	arg2	sites			sites						sites	The results show two facts: 1) which sites must be occupied by a glycan for the proper folding and stability and 2) how N. benthamiana glycosylates the foreign nuclease.
30348313	9	62	gly	glycosylates	1315:1326	arg1	the foreign nuclease	the foreign nuclease				Fterm		nuclease			The results show two facts: 1) which sites must be occupied by a glycan for the proper folding and stability and 2) how N. benthamiana glycosylates the foreign nuclease.
29976678	14	80	part_of	protein	2256:2262	arg1	different regions	protein		different regions		Fterm	Site	protein		regions	To test this, we created a panel of ZIKV mutants with epitope insertions in different regions of the envelope protein.
29760474	0	52	part_of	IgG	324:326	arg1	IgG Fc regions	IgG		IgG Fc regions		Cterm	Site	IgG		regions	Structural basis for the recognition of complex-type N-glycans by Endoglycosidase S. Endoglycosidase S (EndoS) is a bacterial endo-β-N-acetylglucosaminidase that specifically catalyzes the hydrolysis of the β-1,4 linkage between the first two N-acetylglucosamine residues of the biantennary complex-type N-linked glycans of IgG Fc regions.
31759178	10	70	gly	N-glycoproteins	2507:2521	arg1	21 intact N-glycoproteins	21 intact N-glycoproteins				Fterm		N-glycoproteins			With the criteria of quantified at least thrice out of the five technical replicates with no < 1.5-fold change and p ≤ .05, 56 DEGPs were quantified from 21 intact N-glycoproteins; 13 and 5 intact N-glycoproteins (each with one or more DEGPs) were observed with uniform down and up regulation; whereas one were observed with simultaneous up and down regulation.
31759178	10	130	gly	N-glycoproteins	2540:2554	arg1	13 and 5 intact N-glycoproteins	13 and 5 intact N-glycoproteins				Fterm		N-glycoproteins			With the criteria of quantified at least thrice out of the five technical replicates with no < 1.5-fold change and p ≤ .05, 56 DEGPs were quantified from 21 intact N-glycoproteins; 13 and 5 intact N-glycoproteins (each with one or more DEGPs) were observed with uniform down and up regulation; whereas one were observed with simultaneous up and down regulation.
30611426	7	14	gly	glycoproteins	1189:1201	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Methods to express glycoproteins, incorporate stable isotope labels, and analyze glycoproteins have recently opened new avenues to prepare and investigate glycoproteins.
30611426	7	31	gly	glycoproteins	1263:1275	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Methods to express glycoproteins, incorporate stable isotope labels, and analyze glycoproteins have recently opened new avenues to prepare and investigate glycoproteins.
30611426	7	52	gly	glycoproteins	1127:1139	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Methods to express glycoproteins, incorporate stable isotope labels, and analyze glycoproteins have recently opened new avenues to prepare and investigate glycoproteins.
31126879	4	8	part_of	Env	554:556	arg1	Env protein residues	Env		Env protein residues		PUBTATOR	Site	Env	100616444	residues	A 3.3Å cryo-EM structure of a SF12-Env trimer complex showed additional contacts to Env protein residues by SF12 compared with VRC-PG05, the only other known donor-derived silentface antibody, explaining SF12's increased neutralization breadth, potency, and resistance to Env mutation routes.
31430160	12	32	gly	sialylated	1912:1921	arg1	highly sialylated glycan isomers				highly sialylated glycan isomers						Meanwhile, the upregulation of highly sialylated glycan isomers with α2,6-linked sialic acids were found to be associated with breast cancer metastasis.
31141660	7	80	gly	fucosylation	1220:1231	arg1	glycans				glycans						Since diagnostic useful cleavages produce peaks with significant intensities, this approach is also beneficial for rapid recognition of antenna from core fucosylation in glycans detected with low abundances.
31548313	3	63	gly	core-fucosylated	454:469	arg1	core-fucosylated glycans				core-fucosylated glycans						The ability of ENGases to act on core-fucosylated glycans is a key factor determining their therapeutic utility because mammalian N-glycans are frequently α-1,6-fucosylated.
31548313	3	69	gly	α-1,6-fucosylated	576:592	arg1	mammalian N-glycans				mammalian N-glycans						The ability of ENGases to act on core-fucosylated glycans is a key factor determining their therapeutic utility because mammalian N-glycans are frequently α-1,6-fucosylated.
31174130	7	53	part_of	glycoproteins	1280:1292	arg1	112 N-glycopeptides	glycoproteins		112 N-glycopeptides		Fterm	Site	glycoproteins		N-glycopeptides	The enrichment performance of the titania glyco-purification tip was tested using human plasma digest as a real-world complex sample and, 112 N-glycopeptides from human plasma glycoproteins were detected by the analysis of enriched samples by nLC-QTOF-MS/MS.
29548671	0	52	part_of	Silent	74:79	arg1	the Silent Face	Silent Face		the Silent Face		OGER		Silent Face	Q9HB96		A Neutralizing Antibody Recognizing Primarily N-Linked Glycan Targets the Silent Face of the HIV Envelope.
29615747	0	6	part_of	Glycoprotein	41:52	arg1	A Critical Domain	Glycoprotein		A Critical Domain		Fterm		Glycoprotein			A Critical Domain of Ebolavirus Envelope Glycoprotein Determines Glycoform and Infectivity.
29615747	0	9	part_of	Critical	2:9	arg1	A Critical Domain	Critical		A Critical Domain		Cterm		Critical			A Critical Domain of Ebolavirus Envelope Glycoprotein Determines Glycoform and Infectivity.
30315106	0	55	part_of	lipase	49:54	arg1	The mucinous domain	carboxyl-ester lipase		The mucinous domain		PUBTATOR	Site	carboxyl-ester lipase	P19835	domain	The mucinous domain of pancreatic carboxyl-ester lipase (CEL) contains core 1/core 2 O-glycans that can be modified by ABO blood group determinants.
30293150	3	40	gly	glycoproteins	476:488	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			The major structural proteins (archaellins) of the archaellum are glycoproteins, modified with N-linked tetrasaccharides that are essential for the proper assembly and function of archaella.
30293150	3	40	gly	glycoproteins	476:488	arg1	The major structural proteins	The major structural proteins				Fterm		proteins			The major structural proteins (archaellins) of the archaellum are glycoproteins, modified with N-linked tetrasaccharides that are essential for the proper assembly and function of archaella.
29931153	5	40	gly	N-glycoprotein	1020:1033	arg1	N-glycoprotein maturation	N-glycoprotein maturation				Fterm		N-glycoprotein			To obtain more insights into N-glycoprotein maturation, we herein analyze glycoprotein structures extracted from the Protein Data Bank.
29931153	5	49	gly	glycoprotein	1065:1076	arg1	glycoprotein structures	glycoprotein structures				Fterm		glycoprotein			To obtain more insights into N-glycoprotein maturation, we herein analyze glycoprotein structures extracted from the Protein Data Bank.
30169672	3	30	gly	O-glycans	643:651	arg1	the proteins	proteins			O-glycans	Fterm		proteins			In our study, the use of PGC chromatography-ESI mass spectrometry in negative ion mode enabled the identification of 138 N-glycans and 6 O-glycans on the proteins of Streptozotocin-induced (STZ) diabetic mouse ovarian tissues (n = 3).
30169672	3	67	gly	N-glycans	627:635	arg1	the proteins	proteins			N-glycans	Fterm		proteins			In our study, the use of PGC chromatography-ESI mass spectrometry in negative ion mode enabled the identification of 138 N-glycans and 6 O-glycans on the proteins of Streptozotocin-induced (STZ) diabetic mouse ovarian tissues (n = 3).
30612270	8	60	gly	glycosite	1489:1497	arg2	glycosite 137N			glycosite 137N						glycosite	We observed a relative increase of triantennary glycans of up to a factor of three and, even more, MS peaks corresponding to tetraantennary compositions on ceruloplasmin at glycosite 137N in all 17 samples, which we did not detect using a bottom up approach.
31362986	8	44	gly	occupied	1664:1671	arg2	both binding sites			both binding sites						sites	We also noted that full-length IgA and FcαRI form a mixture of 1:1 and 1:2 complexes tending toward a 1:1 stoichiometry due to different IgA tailpiece conformations that make it less likely that both binding sites are simultaneously occupied.
31311856	4	22	gly	glycoproteins	906:918	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			A structural analysis of these glycans revealed that their structures are identical to those of O-mannosyl glycans that are attached to glycoproteins.
31311856	4	56	gly	attached	894:901	arg2	glycoproteins AND O-mannosyl glycans	glycoproteins			O-mannosyl glycans	Fterm		glycoproteins			A structural analysis of these glycans revealed that their structures are identical to those of O-mannosyl glycans that are attached to glycoproteins.
29909447	6	12	gly	glycoproteins	877:889	arg1	purified glycoproteins	purified glycoproteins				Fterm		glycoproteins			We recently demonstrated the successful application of an automated high-throughput (HT), glycan permethylation protocol based on 96-well microplates, in the analysis of purified glycoproteins.
29405331	6	65	gly	glycopeptides	911:923	arg1	low abundance glycan modification			glycopeptides	low abundance glycan modification					glycopeptides	In-source dissociation was found to severely affect the identification and quantification of glycopeptides with low abundance glycan modification.
29976678	9	64	part_of	protein	1331:1337	arg1	E protein domain III	protein		E protein domain III		Fterm	Site	protein		domain	Although we could not generate infectious viruses with FLAG epitope insertions in a buried region of E protein domain III, we found that the V5 epitope could be inserted at this site without greatly impacting fitness.
29674057	3	56	gly	glycopeptides	373:385	arg2	glycopeptides			glycopeptides						glycopeptides	Whereas analysis of released glycans and glycopeptides provides information about the composition and/or position of the glycan, intact glycoprotein analysis allows assignment of individual proteoforms and co-occurring modifications.
29674057	3	79	gly	glycoprotein	468:479	arg1	intact glycoprotein analysis	intact glycoprotein analysis				Fterm		glycoprotein			Whereas analysis of released glycans and glycopeptides provides information about the composition and/or position of the glycan, intact glycoprotein analysis allows assignment of individual proteoforms and co-occurring modifications.
31329418	5	5	gly	α-2,6-sialylated	1290:1305	arg1	α-2,6-sialylated fucosylated N-glycans				α-2,6-sialylated fucosylated N-glycans						The method was successfully applied to isomer-specific, quantitative comparison of sialylated N-glycans between bovine and rabbit immunoglobulin G (IgG) and the search for serum sialylated N-glycan biomarker candidates of hepatocellular carcinoma, during which a 55% increase of α-2,6-sialylated fucosylated N-glycans was revealed, demonstrating the great applicability and potential clinical usage of the method.
31329418	5	6	gly	fucosylated	1307:1317	arg1	α-2,6-sialylated fucosylated N-glycans				α-2,6-sialylated fucosylated N-glycans						The method was successfully applied to isomer-specific, quantitative comparison of sialylated N-glycans between bovine and rabbit immunoglobulin G (IgG) and the search for serum sialylated N-glycan biomarker candidates of hepatocellular carcinoma, during which a 55% increase of α-2,6-sialylated fucosylated N-glycans was revealed, demonstrating the great applicability and potential clinical usage of the method.
31329418	5	16	gly	sialylated	1189:1198	arg1	serum sialylated N-glycan biomarker candidates				serum sialylated N-glycan biomarker candidates						The method was successfully applied to isomer-specific, quantitative comparison of sialylated N-glycans between bovine and rabbit immunoglobulin G (IgG) and the search for serum sialylated N-glycan biomarker candidates of hepatocellular carcinoma, during which a 55% increase of α-2,6-sialylated fucosylated N-glycans was revealed, demonstrating the great applicability and potential clinical usage of the method.
31329418	5	22	gly	sialylated	1094:1103	arg1	sialylated N-glycans				sialylated N-glycans						The method was successfully applied to isomer-specific, quantitative comparison of sialylated N-glycans between bovine and rabbit immunoglobulin G (IgG) and the search for serum sialylated N-glycan biomarker candidates of hepatocellular carcinoma, during which a 55% increase of α-2,6-sialylated fucosylated N-glycans was revealed, demonstrating the great applicability and potential clinical usage of the method.
31160824	2	41	gly	N-glycosylated	224:237	arg1	Numerous N-glycosylated proteins	Numerous N-glycosylated proteins				Fterm		proteins			Numerous N-glycosylated proteins are found in the human gut, from both dietary and host sources, including immunoglobulins such as IgA that are secreted into the intestine at high levels.
30397756	2	62	gly	glycoproteins	311:323	arg1	glycoproteins	glycoproteins			Glycan structures	Fterm		glycoproteins			Glycan structures from glycoproteins are usually altered in cancer.
30466347	1	67	part_of	IgG	219:221	arg1	the CH2 domain	IgG		the CH2 domain		Cterm	Site	IgG		domain	Glycosylation of the conserved asparagine residue in each heavy chain of IgG in the CH2 domain is known as N-glycosylation.
31669586	0	50	gly	proteins	47:54	arg1	Altered N-glycan profile	proteins			Altered N-glycan profile	Fterm		proteins			Altered N-glycan profile of IgG-depleted serum proteins in Hashimoto's thyroiditis.
30621113	5	25	gly	glycoforms	1138:1147	arg1	oligomannose glycoforms				oligomannose glycoforms						We determined the optimal concentration of kifunensine used in the infiltration solution, 0.375 µM, which was sufficient to produce exclusively oligomannose glycoforms, at a concentration 14 times lower than previously published levels.
29949660	5	67	part_of	lignin	1062:1067	arg1	the different lignin compositions	lignin		the different lignin compositions		Fterm	Site	lignin		positions	Glycome profiling, fractionation and enzymatic digestion studies indicated that the different lignin compositions led to differential extractability of a range of heterogeneous oligosaccharide epitopes, with elicitor activity originating from different cell wall polymers.
29408166	10	35	gly	core-fucosylation	1945:1961	arg1	other low-concentrated glycoproteins	other low-concentrated glycoproteins				Fterm		glycoproteins			Furthermore, the described strategy could be used to monitor potential changes in site-specific core-fucosylation of other low-concentrated glycoproteins, which could serve as more specific markers ("marker refinement") in cancer research.
29408166	10	18	gly	glycoproteins	1989:2001	arg1	other low-concentrated glycoproteins	glycoproteins			site-specific core-fucosylation	Fterm		glycoproteins			Furthermore, the described strategy could be used to monitor potential changes in site-specific core-fucosylation of other low-concentrated glycoproteins, which could serve as more specific markers ("marker refinement") in cancer research.
31754374	3	40	gly	N-glycosylated	374:387	arg1	Most fungal enzymes	Most fungal enzymes				Fterm		enzymes			Most fungal enzymes are N-glycosylated, which influences their secretion, stability, activity, signalization, and protease protection.
31719144	6	28	gly	glycoprotein	693:704	arg1	a homodimeric glycoprotein	a homodimeric glycoprotein				Fterm		glycoprotein			MPO is a homodimeric glycoprotein, posttranslationally modified with complex sugars at specific sites.
29299842	2	11	gly	attached	243:250	arg2	proteins AND glycans	proteins			glycans	Fterm		proteins			The structures of glycans attached to proteins are quite diverse among different organisms and even within yeast species.
29659495	4	56	gly	glycosylation	562:574	arg1	a therapeutic protein	a therapeutic protein				Fterm		protein			Since glycosylation can affect the efficacy, safety and stability of a therapeutic protein, methods to control glycan structures and distributions in plant-based systems would be beneficial.
30899004	5	25	part_of	glycosites	1065:1074	arg1	the same protein	protein		glycosites		Fterm	Site	protein		glycosites	Our data reveal that N-glycosylation profiles can differ between subcellular regions and structural domains and that N-glycosite heterogeneity manifests in several different forms, including dramatic differences in glycosites on the same protein.
31569500	8	63	part_of	ER-retrieval	1298:1309	arg1	a C-terminal dilysine ER-retrieval motif	ER		a C-terminal dilysine ER-retrieval motif		PUBTATOR	Site	ER	2069	motif	In contrast, PIGM, ALG3, ALG6, and ALG8 have 12 or 14 TMDs and display a C-terminal dilysine ER-retrieval motif oriented towards the cytoplasm.
31034685	11	38	gly	glycosylation	1876:1888	arg1	peptides			peptides						peptides	CONCLUSIONS PGC has demonstrated superior separation of peptides with phosphorylation and glycosylation and can be used as an alternative in the proteomic characterization of post-translational modifications (PTMs) by polar groups.
29878199	12	42	gly	glycoproteins	1745:1757	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Cell biology studies in fibroblasts of affected individuals showed intracellular mislocalization of glycoproteins and a defect in post-Golgi transport of glycoproteins to the cell membrane.
29878199	12	60	gly	glycoproteins	1691:1703	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Cell biology studies in fibroblasts of affected individuals showed intracellular mislocalization of glycoproteins and a defect in post-Golgi transport of glycoproteins to the cell membrane.
31809011	6	51	gly	fragment	939:946	arg1	the N-glycan type composition			fragment	the N-glycan type composition					fragment	As a proof of principle, the glycoproteomic N-glycan type quantitative (glyco-TQ) method was first used to determine the N-glycan type composition of the immunoglobulin G1 (IgG1) Fc fragment.
31446948	7	52	gly	glycoprotein	1360:1371	arg1	model glycoprotein	model glycoprotein				Fterm		glycoprotein			Through the investigation of single glycan standard and complex glycans released from model glycoprotein and serum, the results demonstrate that the method has good quantitative accuracy and high reproducibility.
31446948	7	89	gly	released	1340:1347	arg2	model glycoprotein AND single glycan standard and complex glycans	model glycoprotein			single glycan standard and complex glycans	Fterm		glycoprotein			Through the investigation of single glycan standard and complex glycans released from model glycoprotein and serum, the results demonstrate that the method has good quantitative accuracy and high reproducibility.
29992770	7	18	gly	N-glycopeptides	997:1011	arg2	Thirty-eight tryptic N-glycopeptides			Thirty-eight tryptic N-glycopeptides						N-glycopeptides	Thirty-eight tryptic N-glycopeptides are identified, having 19 unique N-glycosylation sites representing 14 glycoproteins.
29992770	7	28	gly	N-glycosylation	1046:1060	arg2	19 unique N-glycosylation sites			19 unique N-glycosylation sites						sites	Thirty-eight tryptic N-glycopeptides are identified, having 19 unique N-glycosylation sites representing 14 glycoproteins.
31776339	2	31	gly	structures	292:301	arg1	proteins	proteins			structures	Fterm		proteins			However, constructing biosynthetic pathways to study and engineer precise glycan structures on proteins remains a bottleneck.
30407002	1	32	gly	glycosylation	144:156	arg1	specific proteins	specific proteins				Fterm		proteins			The visualization of glycosylation states of specific proteins in vivo is of great importance for uncovering their roles in disease development.
29437979	14	65	gly	glycoproteins	2172:2184	arg1	Viral envelope glycoproteins	Viral envelope glycoproteins				Fterm		glycoproteins			Viral envelope glycoproteins, such as gH, usually contain N-glycans, which can have a strong impact on their folding, transport, and functions.
29437979	14	68	gly	contain	2207:2213	arg1	Viral envelope glycoproteins AND N-glycans	Viral envelope glycoproteins			N-glycans	Fterm		glycoproteins			Viral envelope glycoproteins, such as gH, usually contain N-glycans, which can have a strong impact on their folding, transport, and functions.
29671439	4	28	gly	glycoproteins	499:511	arg1	the crude ginger glycoproteins	the crude ginger glycoproteins				Fterm		glycoproteins			The results suggest that the crude ginger glycoproteins are active against ACE with an IC50 value of 0.83 ± 0.09 mg mL-1.
29596681	7	78	gly	disialylated	1197:1208	arg1	substantial disialylated glycoforms				substantial disialylated glycoforms						We were unable to introduce substantial disialylated glycoforms.
30513306	0	36	gly	glycoprotein	11:22	arg1	Structural glycoprotein LmAbd-9	Structural glycoprotein LmAbd-9				Fterm		glycoprotein			Structural glycoprotein LmAbd-9 is required for the formation of the endocuticle during locust molting.
29730764	5	59	gly	glycopeptides	747:759	arg2	O-linked glycopeptides			O-linked glycopeptides						glycopeptides	Focusing on O-linked glycopeptides, we noticed that in EThcD, larger glycan oxonium ions better survive the activation than those in HCD.
30295034	2	9	gly	glycoprotein	537:548	arg1	the intact glycoprotein	the intact glycoprotein				Fterm		glycoprotein			Here, we show that glycan composition over all five glycosylation sites can be determined quantitatively by ESI-qTOF-MS of the intact glycoprotein in negative ion mode.
30295034	2	94	gly	glycosylation	455:467	arg2	all five glycosylation sites			all five glycosylation sites						sites	Here, we show that glycan composition over all five glycosylation sites can be determined quantitatively by ESI-qTOF-MS of the intact glycoprotein in negative ion mode.
29773674	6	40	gly	leucine-rich	1023:1034	arg1	small leucine-rich proteoglycan decorin			leucine	small leucine-rich proteoglycan decorin					leucine	We applied this workflow to the small leucine-rich proteoglycan decorin and three hyalectan proteoglycans: neurocan, brevican, and aggrecan.We characterized glycosylation of these proteoglycans using LC-MS methods easily implemented on instruments widely used in proteomics laboratories.
29773674	6	62	gly	glycosylation	1142:1154	arg1	these proteoglycans				these proteoglycans						We applied this workflow to the small leucine-rich proteoglycan decorin and three hyalectan proteoglycans: neurocan, brevican, and aggrecan.We characterized glycosylation of these proteoglycans using LC-MS methods easily implemented on instruments widely used in proteomics laboratories.
30276752	1	6	gly	glycosylation	256:268	arg2	the same glycosylation site			the same glycosylation site						site	N-Glycans are posttranslational modifications of proteins attached to the amide side chains of asparagine residues, with possible heterogeneity due to different structures being possible at the same glycosylation site.
30276752	1	11	gly	proteins	106:113	arg1	N-Glycans	proteins			N-Glycans	Fterm		proteins			N-Glycans are posttranslational modifications of proteins attached to the amide side chains of asparagine residues, with possible heterogeneity due to different structures being possible at the same glycosylation site.
30513306	3	4	gly	glycoprotein	406:417	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			LmAbd-9 encodes a glycoprotein with a chitin binding domain 4, belonging to RR-1 subclass of the CPR family, which has two potential O-linked glycosylation sites (S115 and T137) at which glycosylation modification may occur.
30513306	3	54	gly	glycosylation	530:542	arg2	two potential O-linked glycosylation sites			two potential O-linked glycosylation sites						sites	LmAbd-9 encodes a glycoprotein with a chitin binding domain 4, belonging to RR-1 subclass of the CPR family, which has two potential O-linked glycosylation sites (S115 and T137) at which glycosylation modification may occur.
30513306	3	63	gly	sites	544:548	arg1	two potential O-linked glycosylation sites			two potential O-linked glycosylation sites						sites	LmAbd-9 encodes a glycoprotein with a chitin binding domain 4, belonging to RR-1 subclass of the CPR family, which has two potential O-linked glycosylation sites (S115 and T137) at which glycosylation modification may occur.
29632092	8	33	part_of	sites	2240:2244	arg1	LTA	LTA		sites		OGER	Site	LTA	P01374	sites	As the dlt and glycosylation pathways compete for the same sites on LTA and induction of glycosylation results in decreased d-alanylation, the interplay between the two modification systems holds implications for resistance to antibiotics and antimicrobial peptides.
29562594	2	33	gly	glycosylation	437:449	arg1	a recombinant protein	a recombinant protein				Fterm		protein			We report for the first time that through one-time vacuum infiltration of kifunensine in plant tissue, N-linked glycosylation of a recombinant protein transiently produced in whole-plants shifted completely from complex-type to oligomannose-type.
31813565	6	79	part_of	magMOF	1189:1194	arg1	The magMOF@Au-maltose nanocomposite	MOF		The magMOF@Au-maltose nanocomposite		OGER	Site	MOF		nanocomposite	The magMOF@Au-maltose nanocomposite can enrich 24 and 32 glycopeptides from tryptic HRP and human IgG digests, respectively.
31094418	3	5	gly	ES-62	563:567	arg1	four potential N-glycosylation sites			four potential N-glycosylation sites						sites	However, it was unknown at this time which of ES-62's four potential N-glycosylation sites carries the PC-modified glycans.
31094418	3	50	gly	N-glycosylation	586:600	arg2	four potential N-glycosylation sites			four potential N-glycosylation sites						sites	However, it was unknown at this time which of ES-62's four potential N-glycosylation sites carries the PC-modified glycans.
31572782	3	34	gly	glycoproteins	360:372	arg1	intact glycoproteins	intact glycoproteins				Fterm		glycoproteins			Here, we present an NMR-based strategy to delineate the N-glycan composition in intact glycoproteins and under physiological conditions.
31572782	3	44	gly	composition	338:348	arg1	intact glycoproteins	glycoproteins			composition	Fterm		glycoproteins			Here, we present an NMR-based strategy to delineate the N-glycan composition in intact glycoproteins and under physiological conditions.
29555702	7	18	gly	glycoprotein	1418:1429	arg1	a given glycoprotein	a given glycoprotein				Fterm		glycoprotein			There was also a high degree of glycan microheterogeneity, in which different variants of glycan structures were found at a given glycoprotein.
31737090	7	58	gly	position	1708:1715	arg1	the N-linked glycan chains			Asn-362 position	the N-linked glycan chains					Asn-362 position	CONCLUSION The increased enzyme activity in N362Q, combined with thermostability testing, 3D modeling, kinetics data and secondary structure analysis, implied that the N-linked glycan chains at the Asn-362 position functioned negatively, mainly as a type of steric hindrance toward its adjacent N-glycans to bring rigidity.
30898558	2	27	gly	glycosylated	478:489	arg1	the glycosylated catalytic domain	endoglucanase		domain		Fterm		endoglucanase		domain	Here, we report the X-ray structure of the glycosylated catalytic domain (CD) of Trichoderma harzianum endoglucanase, ThCel7B, solved and refined at 2.9 Å resolution.
29603480	1	65	gly	glycoproteins	161:173	arg1	Complex N-glycans	glycoproteins			Complex N-glycans	Fterm		glycoproteins			Complex N-glycans of glycoproteins of the zona pellucida (ZP) of human oocytes have been implicated in the binding of spermatozoa.
30621113	3	38	gly	N-glycosylation	661:675	arg1	the Fc region			the Fc region						region	In particular, attention has focused on engineering processes in vivo or in vitro to alter the structure of the N-glycosylation of the Fc region of anti-cancer monoclonal antibodies in order to increase antibody-dependent cell-mediated cytotoxicity (ADCC).
29931153	3	28	gly	N-glycoprotein	725:738	arg1	N-glycoprotein maturation	N-glycoprotein maturation				Fterm		N-glycoprotein			Much attention has been paid to environmental factors regulating N-glycoprotein maturation, such as the expression levels of glycosyltransferases/glycosidases.
29675740	1	68	part_of	glycoprotein	387:398	arg1	each site	glycoprotein		each site		Fterm	Site	glycoprotein		site	To elucidate the relationship between the protein function and the diversity and heterogeneity of glycans conjugated to the protein, glycosylation sites, glycan variation, and glycan proportions at each site of the glycoprotein must be analyzed.
29681470	3	17	part_of	residues	476:483	arg1	the core proteins	proteins		residues		Fterm	AminoAcid	proteins	38288	serine residues	GAG biosynthesis is initiated by peptide O-xylosyltransferases, which transfer xylose onto selected serine residues in the core proteins.
30315106	7	49	gly	linked	1203:1208	arg2	Ser/Thr AND GalNAc residues			Ser/Thr	GalNAc residues					Ser/Thr	Testing of the mAb16D10 antibody in glycan microarrays then demonstrated that it recognized structures containing terminal GalNAc-α1,3(Fuc-α1,2)Gal (blood group A antigen) and also repeated protein sequences containing GalNAc residues linked to Ser/Thr (Tn antigen), findings that were supported by immunostainings of human pancreatic tissue.
30315106	7	94	gly	containing	1176:1185	arg1	repeated protein sequences AND GalNAc residues			repeated protein sequences	GalNAc residues					sequences	Testing of the mAb16D10 antibody in glycan microarrays then demonstrated that it recognized structures containing terminal GalNAc-α1,3(Fuc-α1,2)Gal (blood group A antigen) and also repeated protein sequences containing GalNAc residues linked to Ser/Thr (Tn antigen), findings that were supported by immunostainings of human pancreatic tissue.
31529350	6	3	gly	N-glycosylation	1218:1232	arg2	N-glycosylation sites			N-glycosylation sites						sites	We analyzed serum native transferrin, as first line test for CDG and we profiled serum IgG and total serum N-glycans by a combination of consolidated (N-glycan analysis by MALDI MS) and innovative mass spectrometry-based protocols, such as GlycoWorks RapiFluor N-glycan analysis coupled with LC-ESI MS. Intact serum transferrin showed, as expected for a CDG type I defect, underoccupancy of N-glycosylation sites.
29595997	3	28	gly	glycoproteins	536:548	arg1	host glycoproteins	host glycoproteins				Fterm		glycoproteins			Because Env is heavily glycosylated compared to host glycoproteins, the glycans have become targets for the antibody response.
30528732	5	15	gly	glycosylation	597:609	arg2	the four potential glycosylation sites			the four potential glycosylation sites						sites	However, investigations have been focused on N-glycosylation of three of the four potential glycosylation sites, as well as O-glycosylation on the linker region, while a full picture of glycosylation of T. reesei CBHI is still needed.
30528732	5	54	gly	N-glycosylation	550:564	arg1	the four potential glycosylation sites			the four potential glycosylation sites						sites	However, investigations have been focused on N-glycosylation of three of the four potential glycosylation sites, as well as O-glycosylation on the linker region, while a full picture of glycosylation of T. reesei CBHI is still needed.
31586542	1	16	gly	glycosylated	198:209	arg1	HIV- and SIV-envelope (Env) trimers	HIV- and SIV-envelope (Env) trimers				Fterm		trimers			HIV- and SIV-envelope (Env) trimers are both extensively glycosylated, and antibodies identified to date have been unable to fully neutralize SIVmac239.
30427586	1	9	gly	glycopeptides	201:213	arg2	glycopeptides			glycopeptides						glycopeptides	The unambiguous mass spectrometric identification and characterization of glycopeptides is crucial to elucidate the micro- and macroheterogeneity of glycoproteins.
30427586	1	15	gly	macroheterogeneity	254:271	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			The unambiguous mass spectrometric identification and characterization of glycopeptides is crucial to elucidate the micro- and macroheterogeneity of glycoproteins.
30427586	1	26	gly	glycoproteins	276:288	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			The unambiguous mass spectrometric identification and characterization of glycopeptides is crucial to elucidate the micro- and macroheterogeneity of glycoproteins.
30063822	2	5	gly	N-glycosylation	313:327	arg2	single N-glycosylation sites			single N-glycosylation sites						sites	The procedure relies on the presence of single N-glycosylation sites that are present natively in proteins or that can be engineered into glycoproteins by mutational elimination of all but one glycosylation site.
30063822	2	22	gly	glycoproteins	404:416	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			The procedure relies on the presence of single N-glycosylation sites that are present natively in proteins or that can be engineered into glycoproteins by mutational elimination of all but one glycosylation site.
30063822	2	72	gly	glycosylation	459:471	arg2	one glycosylation site			one glycosylation site						site	The procedure relies on the presence of single N-glycosylation sites that are present natively in proteins or that can be engineered into glycoproteins by mutational elimination of all but one glycosylation site.
29931153	0	20	gly	N-glycoprotein	126:139	arg1	N-glycoprotein processing	N-glycoprotein processing				Fterm		N-glycoprotein			Analysis of protein landscapes around N-glycosylation sites from the PDB repository for understanding the structural basis of N-glycoprotein processing and maturation.
29931153	0	51	gly	N-glycosylation	38:52	arg2	N-glycosylation sites			N-glycosylation sites						sites	Analysis of protein landscapes around N-glycosylation sites from the PDB repository for understanding the structural basis of N-glycoprotein processing and maturation.
31554601	1	6	gly	glycoproteins	219:231	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Glycosylation is one of the most common post-translational modifications which diversifies the structure and function of glycoproteins like immunoglobulin G (IgG).
31514875	9	5	gly	glycosylation	1798:1810	arg2	the 4 glycosylation site			the 4 glycosylation site						site	For the first time, the complementarity of trypsin and pepsin was illustrated for the glycosylation mapping as trypsin led to identifications on 2 out of 4 glycosylation site while pepsin was informative on the 4 glycosylation site.
31514875	9	24	gly	glycosylation	1741:1753	arg2	2 out of 4 glycosylation site			2 out of 4 glycosylation site						site	For the first time, the complementarity of trypsin and pepsin was illustrated for the glycosylation mapping as trypsin led to identifications on 2 out of 4 glycosylation site while pepsin was informative on the 4 glycosylation site.
31122132	4	74	gly	glycosylation	999:1011	arg2	all N-linked glycosylation sites			all N-linked glycosylation sites						sites	We further explore two strategies to overcome the rapid serum clearance of polymeric IgA: removal of all N-linked glycosylation sites creating an aglycosylated polymeric IgA and engineering in FcRn binding with the generation of a polymeric IgG-IgA Fc fusion.
30033944	5	21	gly	sialylated	700:709	arg1	branched sialylated N-glycans				branched sialylated N-glycans						Its expression in the mouse brain increases during development, suggesting that branched sialylated N-glycans play essential roles during brain development.
29885470	3	114	gly	glycoproteins	497:509	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Here a novel method is developed for dissociation of N-linked glycans from glycoproteins for analysis by MS and online LC/MS.
30898558	2	3	part_of	endoglucanase	538:550	arg1	the glycosylated catalytic domain	endoglucanase		the glycosylated catalytic domain		Fterm	Site	endoglucanase		domain	Here, we report the X-ray structure of the glycosylated catalytic domain (CD) of Trichoderma harzianum endoglucanase, ThCel7B, solved and refined at 2.9 Å resolution.
30898876	7	15	gly	glycoproteins	1558:1570	arg1	extracellular glycoproteins	extracellular glycoproteins				Fterm		glycoproteins			Whereas B4GALNT3 and B4GALNT4 synthesized LDN on extracellular glycoproteins, B3GALNT2 primarily transferred LDN to intracellular glycoproteins, thereby clearly delineating proteins that carry type-I or type-II LDNs.
30898876	7	56	gly	glycoproteins	1625:1637	arg1	intracellular glycoproteins	intracellular glycoproteins				Fterm		glycoproteins			Whereas B4GALNT3 and B4GALNT4 synthesized LDN on extracellular glycoproteins, B3GALNT2 primarily transferred LDN to intracellular glycoproteins, thereby clearly delineating proteins that carry type-I or type-II LDNs.
30898876	7	89	gly	LDN	1537:1539	arg1	extracellular glycoproteins	glycoproteins			LDN	Fterm		glycoproteins			Whereas B4GALNT3 and B4GALNT4 synthesized LDN on extracellular glycoproteins, B3GALNT2 primarily transferred LDN to intracellular glycoproteins, thereby clearly delineating proteins that carry type-I or type-II LDNs.
30484241	1	6	gly	glycosylation	207:219	arg2	glycosylation sites			glycosylation sites						sites	This chapter describes the folding of synthetic homogeneous glycosylpolypeptides into glycoproteins depending on the position and number of glycosylation sites and oligosaccharide structures.
30484241	1	23	gly	glycoproteins	153:165	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			This chapter describes the folding of synthetic homogeneous glycosylpolypeptides into glycoproteins depending on the position and number of glycosylation sites and oligosaccharide structures.
30177739	0	54	gly	fucosylated	49:59	arg1	fucosylated glycans				fucosylated glycans						YesU from Bacillus subtilis preferentially binds fucosylated glycans.
30335821	1	36	gly	glycoprotein	206:217	arg1	the glycoprotein	the glycoprotein				Fterm		glycoprotein			As a step toward the development of variant forms of Env with enhanced immunogenic properties, we have expressed the glycoprotein in the yeast surface display system in a form that can be subjected to random mutagenesis followed by screening for forms with enhanced binding to germline antibodies.
31393126	11	39	gly	glycoproteins	1768:1780	arg1	the RJ glycoproteins	the RJ glycoproteins				Fterm		glycoproteins			Understanding the properties of the site-specific glycosylation heterogeneity of the RJ glycoproteins can be potentially useful for producing a glycoprotein with desirable pharmacokinetic and biological activity.
31393126	11	43	gly	heterogeneity	1744:1756	arg1	the RJ glycoproteins	the RJ glycoproteins				Fterm		glycoproteins			Understanding the properties of the site-specific glycosylation heterogeneity of the RJ glycoproteins can be potentially useful for producing a glycoprotein with desirable pharmacokinetic and biological activity.
31393126	11	58	gly	glycoprotein	1824:1835	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			Understanding the properties of the site-specific glycosylation heterogeneity of the RJ glycoproteins can be potentially useful for producing a glycoprotein with desirable pharmacokinetic and biological activity.
31393126	11	95	gly	glycosylation	1730:1742	arg1	the RJ glycoproteins	the RJ glycoproteins				Fterm		glycoproteins			Understanding the properties of the site-specific glycosylation heterogeneity of the RJ glycoproteins can be potentially useful for producing a glycoprotein with desirable pharmacokinetic and biological activity.
30612271	0	38	gly	N-glycosylation	29:43	arg1	the VC1 domain	receptor for advanced glycation end products		domain		PUBTATOR		receptor for advanced glycation end products	177	domain	Insights into the effects of N-glycosylation on the characteristics of the VC1 domain of the human receptor for advanced glycation end products (RAGE) secreted by Pichia pastoris.
30637588	3	42	part_of	ECM-like	765:772	arg1	the native ECM-like composition	ECM		the native ECM-like composition		OGER	Site	ECM	Q13201	position	Recently, in vitro fabricated cell-derived ECM have emerged as promising materials for regenerative medicine due to their ability of better recapitulate the native ECM-like composition and structure, without the limitations of availability and pathogen transfer risks of tissue-derived ECM scaffolds.
30080931	1	66	gly	glycosylation	295:307	arg2	additional N-linked glycosylation motifs			additional N-linked glycosylation motifs						motifs	Refocusing of B cell responses can be achieved by preserving the overall fold of the antigen structure but selectively mutating the undesired antigenic sites with additional N-linked glycosylation motifs for glycan-masking the vaccine antigen.
31260704	3	3	part_of	IgG1	535:538	arg1	N-glycopeptides	IgG1		N-glycopeptides		OGER	Site	IgG1	P01857	N-glycopeptides	In this work, we present a high-throughput matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) method based on a microarray technology to monitor N-glycopeptides of IgG1 produced in a perfusion cell culture.
29675740	3	81	gly	glycopeptide	746:757	arg2	a liquid chromatography/mass spectrometry (MS)-based glycopeptide analysis method			a liquid chromatography/mass spectrometry (MS)-based glycopeptide analysis method						glycopeptide	Therefore, we developed a liquid chromatography/mass spectrometry (MS)-based glycopeptide analysis method to reveal the site-specific glycome (Glycan heterogeneity-based Relational IDentification of Glycopeptide signals on Elution profile, Glyco-RIDGE).
29446564	5	49	gly	glycoproteins	884:896	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			We observed that the amount and composition of proteins and glycoproteins associated with different glycans structures changed over time in the intestines and PMM under different physiological conditions.
30624066	1	2	gly	glycoproteins	277:289	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			A multipronged electrospray ionization mass spectrometry (ESI-MS) approach for investigating glycan-mediated interactions between water-soluble glycan-binding proteins (GBPs) and glycoproteins (GPs) is described.
31141660	5	64	gly	fucosylated	664:674	arg1	core fucosylated N-glycans				core fucosylated N-glycans						All types of core fucosylated N-glycans have produced two abundant ions consistent with B- and C-glycosidic cleavages corresponding to the loss of the FucGlcNAcPHN residue with a mass 457 and 441 Da from the parent ions.
30908021	1	21	gly	glycoproteins	199:211	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Sulfated N-glycans are biologically important structures derived from enzymatically post-glycosylational modifications of glycoproteins in many therapeutic biologics.
29444271	4	33	gly	N-glycans	1050:1058	arg1	Lea epitopes			Lea epitopes	Lea epitopes						Similarly to rFuc'ase Sl-1, rFuc'ase Sl-2 hydrolyzed the non-reducing terminal α1, 3-fucose residue on LNFP III and α1, 4-fucose residues of Lea epitopes on plant complex type N-glycans, but not the core α1, 3-fucose residue on Manβ1-4GlcNAcβ1-4(Fucα1-3)GlcNAc or Fucα1-3GlcNAc.
29444271	4	35	gly	epitopes	1019:1026	arg1	plant complex type N-glycans				plant complex type N-glycans						Similarly to rFuc'ase Sl-1, rFuc'ase Sl-2 hydrolyzed the non-reducing terminal α1, 3-fucose residue on LNFP III and α1, 4-fucose residues of Lea epitopes on plant complex type N-glycans, but not the core α1, 3-fucose residue on Manβ1-4GlcNAcβ1-4(Fucα1-3)GlcNAc or Fucα1-3GlcNAc.
29444271	4	64	gly	epitopes	1019:1026	arg1	4-fucose residues				4-fucose residues						Similarly to rFuc'ase Sl-1, rFuc'ase Sl-2 hydrolyzed the non-reducing terminal α1, 3-fucose residue on LNFP III and α1, 4-fucose residues of Lea epitopes on plant complex type N-glycans, but not the core α1, 3-fucose residue on Manβ1-4GlcNAcβ1-4(Fucα1-3)GlcNAc or Fucα1-3GlcNAc.
29444271	4	64	gly	epitopes	1019:1026	arg1	Lea epitopes				Lea epitopes						Similarly to rFuc'ase Sl-1, rFuc'ase Sl-2 hydrolyzed the non-reducing terminal α1, 3-fucose residue on LNFP III and α1, 4-fucose residues of Lea epitopes on plant complex type N-glycans, but not the core α1, 3-fucose residue on Manβ1-4GlcNAcβ1-4(Fucα1-3)GlcNAc or Fucα1-3GlcNAc.
30542567	8	58	gly	glycopeptide	1319:1330	arg2	a glycopeptide			a glycopeptide						glycopeptide	This is the first time that a glycopeptide bearing a bisecting N-acetyl glucosamine (GlcNAc), the rare N-glycan branch, and two LewisX trisaccharide antennae was synthesized, enabling access to this class of complex glycopeptide structures.
31884067	9	57	gly	glycoproteins	1316:1328	arg1	L1	L1 and AMPA receptor subunit			HNK-1 carrier glycoproteins	PUBTATOR		L1 and AMPA receptor subunit	3897		We also showed that the expression of HNK-1 carrier glycoproteins such as neural cell adhesion molecule (NCAM), L1 and AMPA receptor subunit GluA2 were also increased in the PRMT1-deficient cerebellum.
31884067	9	57	gly	glycoproteins	1316:1328	arg1	neural cell adhesion molecule	neural cell adhesion molecule			HNK-1 carrier glycoproteins	PUBTATOR		neural cell adhesion molecule	4684		We also showed that the expression of HNK-1 carrier glycoproteins such as neural cell adhesion molecule (NCAM), L1 and AMPA receptor subunit GluA2 were also increased in the PRMT1-deficient cerebellum.
31884067	9	57	gly	glycoproteins	1316:1328	arg1	AMPA receptor subunit	L1 and AMPA receptor subunit			HNK-1 carrier glycoproteins	PUBTATOR		L1 and AMPA receptor subunit	3897		We also showed that the expression of HNK-1 carrier glycoproteins such as neural cell adhesion molecule (NCAM), L1 and AMPA receptor subunit GluA2 were also increased in the PRMT1-deficient cerebellum.
30033600	6	4	gly	peptide	1000:1006	arg1	185 O-GalNAc modified peptide sequences				185 O-GalNAc modified peptide sequences						This method is further applied to analyze the human serum sample, where 185 O-GalNAc modified peptide sequences corresponding to 94 proteins with high confidence (FDR (false detection rate) <1%) are identified.
30560888	7	54	gly	afucosylated	1114:1125	arg1	Bisected and afucosylated Fc-glycans				Bisected and afucosylated Fc-glycans						Bisected and afucosylated Fc-glycans were significantly lower in Jo1+ compared to Jo1- patients.
31647243	3	37	gly	glycoprotein	173:184	arg1	glycoprotein	glycoprotein				Fterm		glycoprotein			glycoprotein, 30CYGP, exhibits strong immunomodulatory activities.
31737090	8	111	gly	N-glycosylation	1841:1855	arg1	the other four sites			sites						sites	Meanwhile, the N-glycosylation at the other four sites positively regulated enzyme activity caused by altered substrate affinity by means of fine-tuning the β-sandwich domain configuration.
29596681	3	32	gly	glycoproteins	502:514	arg1	therapeutic glycoproteins	therapeutic glycoproteins				Fterm		glycoproteins			Structures of glycans on therapeutic glycoproteins are important for circulation, biodistribution and bioactivity.
31154130	7	9	gly	sialylated	1184:1193	arg1	17 sialylated glycopeptides			17 sialylated glycopeptides						glycopeptides	As a result, 83 IgG-Fc glycopeptides from human serum, including 17 sialylated glycopeptides, were identified.
31154130	7	56	gly	glycopeptides	1195:1207	arg2	17 sialylated glycopeptides			17 sialylated glycopeptides						glycopeptides	As a result, 83 IgG-Fc glycopeptides from human serum, including 17 sialylated glycopeptides, were identified.
31154130	7	36	gly	glycopeptides	1139:1151	arg2	17 sialylated glycopeptides			glycopeptides						glycopeptides	As a result, 83 IgG-Fc glycopeptides from human serum, including 17 sialylated glycopeptides, were identified.
31514875	4	39	gly	glycoprotein	764:775	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			The performance of the supports was evaluated with the digestion of human Chorionic Gonadotropin hormone (hCG), a glycoprotein characterized by four N- and four O-glycosylation sites, prior to the analysis of the digests by nanoliquid chromatography coupled to tandem mass spectrometry (nanoLC-MS/MS).
31514875	4	60	gly	O-glycosylation	811:825	arg2	four N- and four O-glycosylation sites			four N- and four O-glycosylation sites						sites	The performance of the supports was evaluated with the digestion of human Chorionic Gonadotropin hormone (hCG), a glycoprotein characterized by four N- and four O-glycosylation sites, prior to the analysis of the digests by nanoliquid chromatography coupled to tandem mass spectrometry (nanoLC-MS/MS).
30640124	5	39	gly	unglycosylated	956:969	arg1	the unglycosylated protein	the unglycosylated protein				Fterm		protein			Interestingly, an electrochemical sensor with a sandwich format employing the identified aptamer as a signaling receptor, provides a tool of discriminating human PSA from the unglycosylated protein, with a limit of detection of 0.66 ng/mL.
31888963	8	41	gly	sites	1251:1255	arg1	>75% hybrid and oligomannose forms			sites	>75% hybrid and oligomannose forms					sites	The CD16a N45-glycans contain markedly less processing than other sites with >75% hybrid and oligomannose forms.
30327321	2	67	part_of	contain	279:285	arg1	The medium and long isoforms AND a unique N-terminal domain	The medium and long isoforms		a unique N-terminal domain		Fterm	Site	isoforms		domain	The medium and long isoforms contain a unique N-terminal domain of unknown function, DUF959, and our sequence-based secondary structure predictions indicated that DUF959 could be an intrinsically disordered domain.
31776333	7	48	gly	glycoprotein	1218:1229	arg1	glycoprotein structures	glycoprotein structures				Fterm		glycoprotein			This work establishes cytoplasmic glycoengineering as a powerful platform for producing glycoprotein structures with diverse future biomedical applications.
30385505	7	22	gly	glycoprotein	1278:1289	arg1	a reporter glycoprotein	a reporter glycoprotein				Fterm		glycoprotein			Moreover, we used fluorescence anisotropy to determine the galectin affinities to recombinant erythropoietin used as a reporter glycoprotein produced by the glycoengineered cells and to synthetic N-glycans with defined branch structures.
32110292	10	58	gly	more	1839:1842	arg1	intact glycopeptides			intact glycopeptides						glycopeptides	Moreover, this method identifies 5 times more intact glycopeptides from human serum than the native-ETD method, implying that the approach can also accommodate large-scale site-specific profiling of glycoproteomes.
32110292	10	63	gly	glycopeptides	1851:1863	arg2	intact glycopeptides			intact glycopeptides						glycopeptides	Moreover, this method identifies 5 times more intact glycopeptides from human serum than the native-ETD method, implying that the approach can also accommodate large-scale site-specific profiling of glycoproteomes.
30335377	8	51	gly	glycoproteins	1214:1226	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Therefore, we hypothesize an important role of glycoproteins in the structuring of anammox granules, comparable to the importance of glycans in the extracellular matrix of multicellular organisms.
30500162	8	52	gly	glycoproteins	1196:1208	arg1	serum glycoproteins	serum glycoproteins				Fterm		glycoproteins			First, Neu5Gc-positive or Neu5Gc-deficient mouse strains were used to generate glycopeptides from serum glycoproteins.
30500162	8	39	gly	glycopeptides	1171:1183	arg1	serum glycoproteins	glycoproteins		glycopeptides		Fterm		glycoproteins		glycopeptides	First, Neu5Gc-positive or Neu5Gc-deficient mouse strains were used to generate glycopeptides from serum glycoproteins.
31541622	8	25	gly	glycoproteins	1258:1270	arg1	some glycoproteins	some glycoproteins				Fterm		glycoproteins			We mapped some glycoproteins only to the BmNPV susceptible or resistant strain, underlining the potential relationship between glycosylation and viral susceptibility.
29408166	0	40	gly	core-fucosylation	86:102	arg1	low-concentrated glycoproteins	low-concentrated glycoproteins				Fterm		glycoproteins			An endoglycosidase-assisted LC-MS/MS-based strategy for the analysis of site-specific core-fucosylation of low-concentrated glycoproteins in human serum using prostate-specific antigen (PSA) as example.
29408166	0	105	gly	glycoproteins	124:136	arg1	low-concentrated glycoproteins	glycoproteins			site-specific core-fucosylation	Fterm		glycoproteins			An endoglycosidase-assisted LC-MS/MS-based strategy for the analysis of site-specific core-fucosylation of low-concentrated glycoproteins in human serum using prostate-specific antigen (PSA) as example.
29528515	3	32	part_of	terminus	755:762	arg1	caps	caps		terminus		OGER	Site	caps	Q13938	terminus	The target oligosaccharides had a free amino group at the reducing terminus and varied caps at the non-reducing terminus to enable further modification and structure-activity relationship studies.
31776333	2	55	gly	glycoprotein	209:220	arg1	novel glycoprotein structures	novel glycoprotein structures				Fterm		glycoprotein			Yet our ability to engineer novel glycoprotein structures remains limited.
29927116	1	43	gly	glycoprotein	134:145	arg1	synthetic glycoprotein	synthetic glycoprotein				Fterm		glycoprotein			This article describes a protocol for remodeling cells with synthetic glycoprotein and glycolipid mimetics that are functionalized with lipid anchors, allowing for cell surface display of specific glycan structures in predefined nanoscale arrangements.
30553446	4	1	gly	structure	463:471	arg1	the hinge region			the hinge region	the hinge region		Site			region	In IgAN, aberrant IgA1 O-glycan structure in the hinge region (HR) of serum IgA is suggested as one of the most convincing key mediators.
30169672	4	64	gly	structures	924:933	arg1	their proteins	proteins			structures	Fterm		proteins			Diabetic mouse ovaries exhibited a relative decrease in sialylation, fucosylation and, to a lesser extent, branched N-linked glycan structures, as well as an increase in oligomannose structures on their proteins, compared with nondiabetic mouse ovaries.
31062865	4	77	gly	glycopeptides	1038:1050	arg2	N-linked glycopeptides			N-linked glycopeptides						glycopeptides	A mixed anion exchange chromatographic column was implemented to capture and enrich N-linked glycopeptides.
31111416	1	48	gly	glycosylation	146:158	arg2	28 glycosylation sites			28 glycosylation sites						sites	Characterization of HIV Env glycoprotein with 28 glycosylation sites is the essential step of structure-based vaccine design programs.
30909000	7	59	gly	used	1651:1654	arg2	GO-MAx:y composites			GO-MAx:y composites						composites	Consequently, GO-MAx:y composites could be used as reusable adsorbents for removal/enrichment inorganic/organic substances in aqueous solutions.
30136207	1	45	gly	serine	272:277	arg1	residue			residue						threonine residue	Mucin-type O-glycosylation is initiated by UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases (ppGalNAc-Ts or PGANTs), attaching GalNAc to serine or threonine residue of a protein substrate.
31529350	8	85	gly	glycosylation	1519:1531	arg1	total serum and IgG N-glycans				total serum and IgG N-glycans						As a whole, ALG12-CDG behaves as a dual CDG (CDG-I and II defects) and it is associated with distinct, abnormal glycosylation of total serum and IgG N-glycans.
31669471	4	1	gly	glycosylation	687:699	arg1	receptors	receptors				Fterm		receptors			Therefore, we developed a lectin-based reverse-phase protein microarray method for screening the glycosylation pattern of receptors in picomolar (pM) concentrations.
30104209	5	63	gly	fucosylated	1341:1351	arg1	fucosylated or paucimannosidic glycans				fucosylated or paucimannosidic glycans						Indicative of tissue-specific remodelling of glycans in the Golgi apparatus of hypopharyngeal gland cells, only a low amount of fucosylated or paucimannosidic glycans were detected as compared with other insect samples or even bee venom.
30151520	0	103	gly	N-glycopeptides	46:60	arg2	protonated N-glycopeptides			protonated N-glycopeptides						N-glycopeptides	Precursor ion survival energies of protonated N-glycopeptides and their weak dependencies on high mannose N-glycan composition in collision-induced dissociation.
29578688	1	63	gly	glycoproteins	289:301	arg1	gp120 and gp 41 envelope glycoproteins	gp120 and gp 41 envelope glycoproteins				Fterm		glycoproteins			The development of an HIV vaccine has been hampered by the extraordinary mutability and genetic diversity of the virus, particularly the substantial sequence diversity of gp120 and gp 41 envelope glycoproteins existing in more than 2000 HIV variants.
30135430	7	34	gly	glycoprotein	1018:1029	arg1	two representative glycoprotein families	two representative glycoprotein families				Fterm		glycoprotein	2651		More focused analyses revealed reduced signaling responses of two representative glycoprotein families modified by GCNT2, insulin-like growth factor receptor and integrins.
31558607	2	4	gly	N-glycosylation	397:411	arg2	a single N-glycosylation sequon			a single N-glycosylation sequon						sequon	ProBDNF carries a single N-glycosylation sequon (Asn-127) that remains virtually unstudied despite being located in a highly conserved region proximal to the proteolytic site.
31558607	2	4	gly	N-glycosylation	397:411	arg2	Asn-127			Asn-127						Asn-127	ProBDNF carries a single N-glycosylation sequon (Asn-127) that remains virtually unstudied despite being located in a highly conserved region proximal to the proteolytic site.
31998308	1	4	gly	attached	154:161	arg2	the fragment crystallizable AND the biantennary sugar moiety			the fragment crystallizable	the biantennary sugar moiety					fragment	Select residues in the biantennary sugar moiety attached to the fragment crystallizable of immunoglobulin G (IgG) antibodies can modulate IgG effector functions.
31998308	1	76	gly	residues	113:120	arg1	the biantennary sugar moiety			residues in	the biantennary sugar moiety					residues in	Select residues in the biantennary sugar moiety attached to the fragment crystallizable of immunoglobulin G (IgG) antibodies can modulate IgG effector functions.
31141660	8	29	gly	multifucosylated	1287:1302	arg1	multifucosylated glycans				multifucosylated glycans						Moreover, in multifucosylated glycans, this type of labeling allows to distinguish how many fucose residues are on the specific antenna and provides additional information on the topology of N-glycans, such as type of antennarity or identification of bisecting moiety.
31247951	1	20	gly	glycosylated	92:103	arg1	Most human proteins	Most human proteins				Fterm		proteins			Most human proteins are glycosylated.
30224661	5	9	gly	N-glycopeptide	827:840	arg2	N-glycopeptide			N-glycopeptide						N-glycopeptide	Instead, the N-glycopeptide population from these alleles exhibited high-mannose structures, representing structures prior to the addition of the first GlcNAc in the Golgi.
30111543	3	32	gly	glycoprotein	570:581	arg1	α1-acid glycoprotein	α1-acid glycoprotein				Fterm		glycoprotein			Here, we apply mass spectrometry-based approaches to elucidate the global and site-specific microheterogeneity of two plasma proteins: α1-acid glycoprotein (AGP) and haptoglobin (Hp).
30111543	3	32	gly	glycoprotein	570:581	arg1	two plasma proteins	two plasma proteins				Fterm		proteins			Here, we apply mass spectrometry-based approaches to elucidate the global and site-specific microheterogeneity of two plasma proteins: α1-acid glycoprotein (AGP) and haptoglobin (Hp).
30111543	3	50	gly	microheterogeneity	519:536	arg1	α1-acid glycoprotein	α1-acid glycoprotein				Fterm		glycoprotein			Here, we apply mass spectrometry-based approaches to elucidate the global and site-specific microheterogeneity of two plasma proteins: α1-acid glycoprotein (AGP) and haptoglobin (Hp).
30111543	3	50	gly	microheterogeneity	519:536	arg1	two plasma proteins	two plasma proteins				Fterm		proteins			Here, we apply mass spectrometry-based approaches to elucidate the global and site-specific microheterogeneity of two plasma proteins: α1-acid glycoprotein (AGP) and haptoglobin (Hp).
29043680	5	24	gly	glycoproteins	738:750	arg1	Incompletely folded glycoproteins	Incompletely folded glycoproteins				Fterm		glycoproteins			Incompletely folded glycoproteins are removed from the ER by a highly conserved degradation process to prevent the accumulation or secretion of misfolded proteins and maintain ER homeostasis.
31291761	3	32	gly	epitopes	672:679	arg1	glycan epitopes				glycan epitopes						Glycome profiling uses mAb groupings that recognize 19 groups of glycan epitopes present in most major classes of cell wall glycans and was used to determine cell wall composition.
31611356	6	67	gly	glycosylation	1231:1243	arg1	N295			N295						N295	Grft's ability to alter the structure of gp120, exposing the CD4 binding site, correlated with the presence of glycosylation at N295 only in clade B strains, not clade C strains.
29301962	1	12	gly	glycosylation	294:306	arg1	secretory proteins	proteins		sites		Fterm		proteins		sites	Oligosaccharyltransferase (OST) is an essential membrane protein complex in the endoplasmic reticulum, where it transfers an oligosaccharide from a dolichol-pyrophosphate-activated donor to glycosylation sites of secretory proteins.
30578591	6	51	gly	glycosites	978:987	arg2	different glycosites	NA		glycosites		Cterm		NA	4758	glycosites	Different types of glycans are identified from different glycosites of NA expressed in human cells, which implies the site-dependence of glycosylation on NA.
31719144	12	64	gly	glycoproteins	1521:1533	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			In particular, we detected glycosylation phenotypes uncommon for glycoproteins in the extracellular space, such as a high abundance of phosphorylated high-mannose species and severely truncated small glycans having the size of paucimannose or smaller.
31507595	6	13	gly	sialylated	1206:1215	arg1	tetra-antennary α-2,3/6 sialylated N-glycans				tetra-antennary α-2,3/6 sialylated N-glycans						Glycomic (porous graphitized carbon-ESI-MS/MS) and glycopeptide (C8-LC-ESI-MS) analysis of recombinant soluble human CD52-immunoglobulin Fc fusion proteins revealed that CD52 bioactivity was correlated with a high abundance of tetra-antennary α-2,3/6 sialylated N-glycans.
31507595	6	70	gly	glycopeptide	1006:1017	arg2	glycopeptide			glycopeptide						glycopeptide	Glycomic (porous graphitized carbon-ESI-MS/MS) and glycopeptide (C8-LC-ESI-MS) analysis of recombinant soluble human CD52-immunoglobulin Fc fusion proteins revealed that CD52 bioactivity was correlated with a high abundance of tetra-antennary α-2,3/6 sialylated N-glycans.
30444974	5	21	gly	ubiquitin	929:937	arg1	The glycan profile	ubiquitin			The glycan profile	Fterm		ubiquitin			The glycan profile of E. histolytica ubiquitin has high mannose N-glycan structures.
31719144	8	67	gly	N-glycosylation	968:982	arg2	5 putative N-glycosylation sites			5 putative N-glycosylation sites						sites	MPO potentially can be heavily modified as it harbors 5 putative N-glycosylation sites (10 in the mature dimer).
29716988	10	9	gly	found	1935:1939	arg2	glycoproteins AND N-glycan moieties	glycoproteins			N-glycan moieties	Fterm		glycoproteins			Considering the complexity of N-glycan moieties generally found in glycoproteins, characterized by different degrees of branching, isomer structures, and variable abundances, our findings point to these factors as another level of complexity in Bothrops venoms, features that could dramatically contribute to their distinct biological activities.
29716988	10	60	gly	glycoproteins	1944:1956	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Considering the complexity of N-glycan moieties generally found in glycoproteins, characterized by different degrees of branching, isomer structures, and variable abundances, our findings point to these factors as another level of complexity in Bothrops venoms, features that could dramatically contribute to their distinct biological activities.
31331074	4	59	gly	glycoproteins	668:680	arg1	the glycan structures	glycoproteins			the glycan structures	Fterm		glycoproteins			Dynamic cellular differentiation can be monitored and quantitatively characterized by profiling the glycan structures of total cellular glycoproteins.
31316527	15	60	part_of	CMG2	2554:2557	arg1	the CMG2 and Fc domains	CMG2		the CMG2 and Fc domains		OGER	Site	CMG2	P58335	domains	In MD simulations, the MAN8 glycoform exhibits quantitatively higher distance between the CMG2 and Fc domains, as well as higher hydrophobic solvent accessible surface areas (SASA), indicating a possibly higher aggregation tendency of the ER variant.
30307368	5	47	part_of	GEM	1129:1131	arg1	GEM epitopes	GEM		GEM epitopes		OGER	Site	GEM	P55040	epitopes	Furthermore, we show that potent inhibition of MICA shedding can be achieved by antibodies that bind GEM epitopes adjacent to previously reported cleavage sites, and that these anti-MICA/B antibodies can prevent tumor growth in vivo.
31421168	3	26	gly	Leu	373:375	arg1	The monosaccharide composition			Leu	The monosaccharide composition					Leu	The monosaccharide composition of Leu.
30908021	7	53	gly	glycoproteins	1795:1807	arg1	influenza glycoproteins	glycoproteins			N-glycan sulfation	Fterm		glycoproteins			The novel findings highlight the tremendous structural diversity of sulfated N-glycans and strongly suggest potential functional importance of N-glycan sulfation of influenza glycoproteins.
30302011	1	7	gly	glycoprotein	134:145	arg1	The HIV-1 envelope (Env) glycoprotein	The HIV-1 envelope (Env) glycoprotein				Fterm		glycoprotein			The HIV-1 envelope (Env) glycoprotein is the primary target of the humoral immune response and a critical vaccine candidate.
31807707	5	17	gly	glycoprotein	934:945	arg1	the glycoprotein processing machinery	the glycoprotein processing machinery				Fterm		glycoprotein			This approach refines and further extends the current knowledge on N-glycans biosynthesis and provides a basis to quantify alterations in the glycoprotein processing machinery.
30033944	1	31	gly	N-glycosylation	103:117	arg1	proteins	proteins				Fterm		proteins			Proper N-glycosylation of proteins is important for normal brain development and nervous system function.
31398379	5	61	gly	glycoproteins	1675:1687	arg1	specific venom glycoproteins	specific venom glycoproteins				Fterm		glycoproteins			CONCLUSIONS Combining the current data on venom and larvae with that we previously published on royal jelly, a total honeybee N-glycomic repertoire of some 150 compositions can be proposed in addition to the 20 previously identified on specific venom glycoproteins.
30295034	6	57	gly	nonsialylated	1026:1038	arg1	nonsialylated oligosaccharides				nonsialylated oligosaccharides						The pattern of nonsialylated oligosaccharides was used for interpretation of the fully sialylated species using bioinformatics tools.
29888905	8	10	gly	fucosylated	1481:1491	arg1	the predominant N-glycan				the predominant N-glycan						In HEK-293 and H4 EVs, the predominant N-glycan was tetraantennary proximally fucosylated with α2,3-linked N-acetylneuraminic acid; HEK-293 EVs also contained the LacdiNAc structure.
30542567	0	31	gly	glycopeptides	28:40	arg2	glycopeptides			glycopeptides						glycopeptides	Chemoenzymatic synthesis of glycopeptides bearing rare N-glycan sequences with or without bisecting GlcNAc.
30990348	1	5	gly	core-fucosylated	256:271	arg1	Typical crystallizable fragment (Fc) glycans				Typical crystallizable fragment (Fc) glycans						Typical crystallizable fragment (Fc) glycans attached to the CH2 domain in therapeutic monoclonal antibodies (mAbs) are core-fucosylated and asialo-biantennary complex-type glycans, e.g., G2F (full galactosylation), G1aF (terminal galactosylation on the Man α1-6 arm), G1bF (terminal galactosylation on the Man α1-3 arm), and G0F (non-galactosylation).
30990348	1	5	gly	core-fucosylated	256:271	arg1	core-fucosylated and asialo-biantennary complex-type glycans				core-fucosylated and asialo-biantennary complex-type glycans						Typical crystallizable fragment (Fc) glycans attached to the CH2 domain in therapeutic monoclonal antibodies (mAbs) are core-fucosylated and asialo-biantennary complex-type glycans, e.g., G2F (full galactosylation), G1aF (terminal galactosylation on the Man α1-6 arm), G1bF (terminal galactosylation on the Man α1-3 arm), and G0F (non-galactosylation).
30990348	1	114	gly	fragment	159:166	arg1	Typical crystallizable fragment (Fc) glycans				Typical crystallizable fragment (Fc) glycans						Typical crystallizable fragment (Fc) glycans attached to the CH2 domain in therapeutic monoclonal antibodies (mAbs) are core-fucosylated and asialo-biantennary complex-type glycans, e.g., G2F (full galactosylation), G1aF (terminal galactosylation on the Man α1-6 arm), G1bF (terminal galactosylation on the Man α1-3 arm), and G0F (non-galactosylation).
30990348	1	114	gly	fragment	159:166	arg1	core-fucosylated and asialo-biantennary complex-type glycans				core-fucosylated and asialo-biantennary complex-type glycans						Typical crystallizable fragment (Fc) glycans attached to the CH2 domain in therapeutic monoclonal antibodies (mAbs) are core-fucosylated and asialo-biantennary complex-type glycans, e.g., G2F (full galactosylation), G1aF (terminal galactosylation on the Man α1-6 arm), G1bF (terminal galactosylation on the Man α1-3 arm), and G0F (non-galactosylation).
30990348	1	137	gly	attached	181:188	arg2	the CH2 domain AND core-fucosylated and asialo-biantennary complex-type glycans			the CH2 domain	core-fucosylated and asialo-biantennary complex-type glycans					domain	Typical crystallizable fragment (Fc) glycans attached to the CH2 domain in therapeutic monoclonal antibodies (mAbs) are core-fucosylated and asialo-biantennary complex-type glycans, e.g., G2F (full galactosylation), G1aF (terminal galactosylation on the Man α1-6 arm), G1bF (terminal galactosylation on the Man α1-3 arm), and G0F (non-galactosylation).
30990348	1	137	gly	attached	181:188	arg2	the CH2 domain AND Typical crystallizable fragment (Fc) glycans			the CH2 domain	Typical crystallizable fragment (Fc) glycans					domain	Typical crystallizable fragment (Fc) glycans attached to the CH2 domain in therapeutic monoclonal antibodies (mAbs) are core-fucosylated and asialo-biantennary complex-type glycans, e.g., G2F (full galactosylation), G1aF (terminal galactosylation on the Man α1-6 arm), G1bF (terminal galactosylation on the Man α1-3 arm), and G0F (non-galactosylation).
30078634	7	23	gly	glycoproteins	1038:1050	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Together this work demonstrates that subsets of glycoproteins can be regulated through pharmacologic inhibition of N-linked glycosylation.
31499077	11	24	gly	sialylation	1883:1893	arg1	complex structures				complex structures						We hypothesize, that intensified mannose trimming at the initial steps of N-glycosylation pathway during differentiation, together with the remodeling of the expression of key glycosyltransferases leads to increased diversity of N-glycans and enhanced fucosylation and sialylation of complex structures.
31499077	11	24	gly	sialylation	1883:1893	arg1	N-glycans				N-glycans						We hypothesize, that intensified mannose trimming at the initial steps of N-glycosylation pathway during differentiation, together with the remodeling of the expression of key glycosyltransferases leads to increased diversity of N-glycans and enhanced fucosylation and sialylation of complex structures.
31499077	11	35	gly	fucosylation	1866:1877	arg1	complex structures				complex structures						We hypothesize, that intensified mannose trimming at the initial steps of N-glycosylation pathway during differentiation, together with the remodeling of the expression of key glycosyltransferases leads to increased diversity of N-glycans and enhanced fucosylation and sialylation of complex structures.
31499077	11	35	gly	fucosylation	1866:1877	arg1	N-glycans				N-glycans						We hypothesize, that intensified mannose trimming at the initial steps of N-glycosylation pathway during differentiation, together with the remodeling of the expression of key glycosyltransferases leads to increased diversity of N-glycans and enhanced fucosylation and sialylation of complex structures.
29632412	3	38	part_of	IgG	394:396	arg1	the IgG glycome composition	IgG		the IgG glycome composition		PUBTATOR	Site	IgG	668542	position	By analyzing the IgG glycome composition of 95 CC strains, we made several important observations: (i) glycome variation between mouse strains was higher than between individual humans, despite all mice having the same environmental influences; (ii) five genetic loci were found to be associated with murine IgG glycosylation; (iii) variants outside traditional glycosylation site motifs affected glycome variation; (iv) bisecting N-acetylglucosamine (GlcNAc) was produced by several strains although most previous studies have reported the absence of glycans containing the bisecting GlcNAc on murine IgGs; and (v) common laboratory mouse strains are not optimal animal models for studying effects of glycosylation on IgG function.
30899004	3	51	gly	glycopeptides	371:383	arg2	intact glycopeptides			intact glycopeptides						glycopeptides	A lack of suitable analytical methods for large-scale analyses of intact glycopeptides has limited our abilities both to address the degree of heterogeneity across the glycoproteome and to understand how this contributes biologically to complex systems.
29593217	4	3	part_of	gp120	792:796	arg1	the gp120 GDIR peptide motif	gp120		the gp120 GDIR peptide motif		PUBTATOR	Site	gp120	3700	motif	Our structures show conserved contacts mediated by common D gene-encoded residues with the N332gp120 glycan and the gp120 GDIR peptide motif, but a distinct Env-binding orientation relative to PGT121/10-1074 bNAbs.
29367749	4	9	part_of	enzyme	766:771	arg1	the active site	enzyme		the active site		Fterm	Site	enzyme		site	Docking of RebA in the active site of the enzyme revealed that only the steviol C-19 β-D-glucosyl moiety is available for glucosylation.
30612270	4	36	gly	glycoprotein	831:842	arg1	the intact glycoprotein	the intact glycoprotein				Fterm		glycoprotein			However, ionization properties of glycopeptides can strongly depend on their composition and can therefore lead to intensities that do not reflect the actual proportions present in the intact glycoprotein.
30612270	4	37	gly	glycopeptides	673:685	arg2	glycopeptides			glycopeptides						glycopeptides	However, ionization properties of glycopeptides can strongly depend on their composition and can therefore lead to intensities that do not reflect the actual proportions present in the intact glycoprotein.
30385505	9	59	gly	2,3-sialylated	1575:1588	arg1	2,3-sialylated N-acetyllactosamine (LacNAc) structures				2,3-sialylated N-acetyllactosamine (LacNAc) structures						Galectin-8N targeted both N- and O-linked glycans with high affinity, preferring 2,3-sialylated N-acetyllactosamine (LacNAc) structures.
29931153	9	4	gly	glycoproteins	1652:1664	arg1	immature glycoproteins	immature glycoproteins				Fterm		glycoproteins			Most notably, γ-branched amino acid residues (Asn+Asp+Leu) occur more frequently on unstructured loop regions of immature glycoproteins.
30427586	2	32	gly	O-glycopeptides	412:426	arg2	O-glycopeptides			O-glycopeptides						O-glycopeptides	Here, combining lower and stepped collisional energy fragmentation for the in-depth and site-specific analysis of N- and O-glycopeptides is proposed.
31669606	1	38	gly	N-glycosylated	106:119	arg1	well-defined N-glycosylated IgG4-Fc variants	well-defined N-glycosylated IgG4-Fc variants				Fterm		variants			A series of well-defined N-glycosylated IgG4-Fc variants were utilized to investigate the effect of glycan structure on their physicochemical properties (conformational stability and photostability) and interactions with an Fc γ receptor IIIA (FcγRIIIA).
29603480	9	18	gly	glycosylation	1571:1583	arg2	the various glycosylation sites			the various glycosylation sites						sites	It is not the multivalent display of SLex on a multi-antennary glycan but the presentation of multiple SLex -Lex on the various glycosylation sites of ZP that accounts for high avidity binding.
29446564	3	1	gly	glycoproteins	400:412	arg1	several glycoproteins	several glycoproteins				Fterm		glycoproteins			We identified several glycoproteins expressed in the intestine and perimicrovillar membrane (PMM) of Triatoma (Meccus) pallidipennis under different feeding conditions.
30409628	1	15	gly	glycoprotein	204:215	arg1	glycoprotein	glycoprotein				Fterm		glycoprotein			Tropomyosin (TM) from Exopalaemon modestus was glycoprotein, the effects of deglycosylation (enzyme and chemical regents) and Maillard reaction on the conformation, allergenicity and human cell sensitization of TM were investigated.
31031563	5	21	gly	found	923:927	arg2	necrotic regions AND the glycans			necrotic regions	the glycans					regions	While the structural glycan classes detected in the tumor and stromal regions are typically classified as high mannose or branched glycans, the glycans found in necrotic regions displayed limited branching, contained sialic acid modifications and lack fucose modifications.
31031563	5	67	gly	detected	807:814	arg2	the tumor and stromal regions AND high mannose			the tumor and stromal regions	high mannose					regions	While the structural glycan classes detected in the tumor and stromal regions are typically classified as high mannose or branched glycans, the glycans found in necrotic regions displayed limited branching, contained sialic acid modifications and lack fucose modifications.
31031563	5	67	gly	detected	807:814	arg2	the tumor and stromal regions AND branched glycans			the tumor and stromal regions	branched glycans					regions	While the structural glycan classes detected in the tumor and stromal regions are typically classified as high mannose or branched glycans, the glycans found in necrotic regions displayed limited branching, contained sialic acid modifications and lack fucose modifications.
31031563	5	67	gly	detected	807:814	arg2	the tumor and stromal regions AND the structural glycan classes			the tumor and stromal regions	the structural glycan classes					regions	While the structural glycan classes detected in the tumor and stromal regions are typically classified as high mannose or branched glycans, the glycans found in necrotic regions displayed limited branching, contained sialic acid modifications and lack fucose modifications.
31453603	5	12	gly	glycopeptide	934:945	arg2	model protonated glycopeptide ions			model protonated glycopeptide ions						glycopeptide	This report presents an IMS study of model protonated glycopeptide ions with systematically varied oligosaccharide topologies, polypeptide sequences, and charge states.
29370305	2	55	part_of	contains	256:263	arg1	HIV-1 Env AND a signal peptide	HIV-1 Env		peptide		PUBTATOR	Site	HIV-1 Env	155971	peptide	Like other membrane-bound and secreted proteins, HIV-1 Env contains at its N terminus a signal peptide (SP) that directs the nascent Env to the endoplasmic reticulum (ER) where Env synthesis and post-translational modifications take place.
31362986	1	14	part_of	sites	177:181	arg1	Human immunoglobulin A	Human immunoglobulin A		sites		PUBTATOR	Site	Human immunoglobulin A	973	sites	Human immunoglobulin A (IgA) is the most prevalent antibody class at mucosal sites with an important role in mucosal defense.
29346724	6	48	gly	N-glycosylation	779:793	arg1	their attached N-glycans			sites	their attached N-glycans					sites	Various biophysical and biochemical approaches were then employed to elucidate the N-glycosylation sites and the function of their attached N-glycans.
29619832	6	0	gly	glycosylation	1113:1125	arg1	this important protein	this important protein				Fterm		protein			We found that the producer cell type imparts a substantial influence on the glycosylation of this important protein.
30335377	6	9	gly	glycosylation	926:938	arg2	The potential glycosylation sequence motif			The potential glycosylation sequence motif						motif	The potential glycosylation sequence motif was identical to that proposed for the surface layer protein of " Candidatus Kuenenia stuttgartiensis".
31809011	2	49	gly	glycopeptides	274:286	arg2	intact glycopeptides			intact glycopeptides						glycopeptides	Current glycoproteome methods mainly focus on qualitative identification of glycosylation sites or intact glycopeptides.
31809011	2	66	gly	glycosylation	244:256	arg2	glycosylation sites			glycosylation sites						sites	Current glycoproteome methods mainly focus on qualitative identification of glycosylation sites or intact glycopeptides.
31453603	8	50	gly	glycopeptide	1471:1482	arg2	glycopeptide CCSs			glycopeptide CCSs						glycopeptide	Furthermore, elongation of the glycan group was found to either increase or decrease glycopeptide CCSs depending on the ion charge state and the size of the glycan.
29703890	8	21	gly	glycosylation	1245:1257	arg2	glycosylation sites			glycosylation sites						sites	Importantly, the enriched glycopeptides remain intact, making the current method compatible with mass-spectrometry-based approaches to identify glycosylation sites and glycan structures.
29703890	8	38	gly	glycopeptides	1127:1139	arg2	the enriched glycopeptides			the enriched glycopeptides						glycopeptides	Importantly, the enriched glycopeptides remain intact, making the current method compatible with mass-spectrometry-based approaches to identify glycosylation sites and glycan structures.
30528732	1	32	gly	glycosylated	128:139	arg1	glycosylated enzymes	glycosylated enzymes				Fterm		enzymes			Cellulases are glycosylated enzymes that have wide applications in fields like biofuels.
29596458	10	6	gly	N-glycopeptides	1322:1336	arg2	Twenty four N-glycopeptides			Twenty four N-glycopeptides						N-glycopeptides	Twenty four N-glycopeptides were identified with high confidence together with elucidation of the peptide sequence, N-glycosylation site, glycan composition and proposed glycan structures.
29596458	10	57	gly	N-glycosylation	1426:1440	arg2	N-glycosylation site			N-glycosylation site						site	Twenty four N-glycopeptides were identified with high confidence together with elucidation of the peptide sequence, N-glycosylation site, glycan composition and proposed glycan structures.
29443078	4	49	gly	2,6-di-sialylated	966:982	arg1	SCT	SCT			2,6-di-sialylated bi-antennary complex type N-glycan	OGER		SCT	P09683		In particular, the binding behavior of a newly isolated HIV-1 broadly neutralizing antibody (bNAb), PG9, to the mixture of closely spaced Man5GlcNAc2 (Man5) and 2,6-di-sialylated bi-antennary complex type N-glycan (SCT) on an ACG array, opens a new avenue to guide the effective immunogen design for HIV vaccine development.
29508223	1	49	part_of	CID-derived	135:145	arg1	negative ion CID-derived fragments	CID-derived		negative ion CID-derived fragments		Cterm	Site	CID-derived		fragments	Extracted arrival time distributions of negative ion CID-derived fragments produced prior to traveling-wave ion mobility separation were evaluated for their ability to provide structural information on N-linked glycans.
31501225	6	65	part_of	IgA2	990:993	arg1	the glycopeptides	IgA2		the glycopeptides		OGER	Site	IgA2	P01877	glycopeptides	TPLTAN205ITK (H5N5S1F1) and (H5N4S2F1) corresponding to the glycopeptides of IgA2 were significantly elevated in serum from patients with HBV infection and even higher in HBV-related LC patients, as compared with healthy donor.
31557542	7	58	gly	positions	1024:1032	arg1	ST3Gal IV			positions	ST3Gal IV					positions	We found for the first time N-glycosylation positions in ST3Gal IV and VI, mucin type glycosylation in ST3Gal III and O-GlcNAcylation in ST3Gal V and their relation with sialylmotifs.
31557542	7	61	gly	glycosylation	1066:1078	arg1	ST3Gal III				ST3Gal III						We found for the first time N-glycosylation positions in ST3Gal IV and VI, mucin type glycosylation in ST3Gal III and O-GlcNAcylation in ST3Gal V and their relation with sialylmotifs.
31557542	7	61	gly	glycosylation	1066:1078	arg1	ST3Gal V				ST3Gal V						We found for the first time N-glycosylation positions in ST3Gal IV and VI, mucin type glycosylation in ST3Gal III and O-GlcNAcylation in ST3Gal V and their relation with sialylmotifs.
31987138	3	53	gly	N-glycopeptides	465:479	arg2	N-glycopeptides enrichment			N-glycopeptides enrichment						N-glycopeptides	However, most of current covalent coupling reactions for N-glycopeptides enrichment are still limited by long coupling time and harsh coupling conditions.
29773674	7	68	gly	linker-glycosite	1302:1317	arg2	the linker-glycosite and three N-glycosylation sites			the linker-glycosite and three N-glycosylation sites						linker-glycosite	For decorin, we assigned the linker-glycosite and three N-glycosylation sites.
29773674	7	76	gly	N-glycosylation	1329:1343	arg2	the linker-glycosite and three N-glycosylation sites			the linker-glycosite and three N-glycosylation sites						sites	For decorin, we assigned the linker-glycosite and three N-glycosylation sites.
31384044	3	16	gly	glycopeptide	722:733	arg2	11,452 unique glycopeptide sequences			11,452 unique glycopeptide sequences						glycopeptide sequences	The method relies on a spectral library of O-glycopeptides; the Glyco-DIA library contains sublibraries obtained from human cell lines and human serum, and it currently covers 2,076 O-glycoproteins (11,452 unique glycopeptide sequences) and the 5 most common core1 O-glycan structures.
31384044	3	28	gly	O-glycopeptides	552:566	arg2	O-glycopeptides			O-glycopeptides						O-glycopeptides	The method relies on a spectral library of O-glycopeptides; the Glyco-DIA library contains sublibraries obtained from human cell lines and human serum, and it currently covers 2,076 O-glycoproteins (11,452 unique glycopeptide sequences) and the 5 most common core1 O-glycan structures.
31384044	3	6	gly	O-glycoproteins	691:705	arg1	11,452 unique glycopeptide sequences	O-glycoproteins		glycopeptide sequences		Fterm		O-glycoproteins		glycopeptide sequences	The method relies on a spectral library of O-glycopeptides; the Glyco-DIA library contains sublibraries obtained from human cell lines and human serum, and it currently covers 2,076 O-glycoproteins (11,452 unique glycopeptide sequences) and the 5 most common core1 O-glycan structures.
29773674	8	74	part_of	mucin-like	1414:1423	arg1	densely glycosylated mucin-like regions	mucin		densely glycosylated mucin-like regions		PUBTATOR	Site	mucin	100508689	regions	For neurocan and brevican, we identified densely glycosylated mucin-like regions in the extended domains.
30280442	1	27	gly	glycoproteins	125:137	arg1	N-linked glycoproteins	glycoproteins			carbohydrate moieties	Fterm		glycoproteins			Chlorella viruses produce N-linked glycoproteins with carbohydrate moieties that differ in structure from all other N-linked glycans.
29675740	4	23	gly	glycopeptides	979:991	arg2	glycopeptides			glycopeptides						glycopeptides	This method used accurate masses and retention times of glycopeptides, without requiring MS2, and could be applied to complex mixtures.
30315106	7	27	part_of	protein	1158:1164	arg1	repeated protein sequences	protein		repeated protein sequences		Fterm	Site	protein		sequences	Testing of the mAb16D10 antibody in glycan microarrays then demonstrated that it recognized structures containing terminal GalNAc-α1,3(Fuc-α1,2)Gal (blood group A antigen) and also repeated protein sequences containing GalNAc residues linked to Ser/Thr (Tn antigen), findings that were supported by immunostainings of human pancreatic tissue.
31362986	2	82	gly	glycosylated	364:375	arg1	FcαRI	FcαRI		domain		PUBTATOR		FcαRI	2204	domain	Little is known about the impact of N-glycan modifications of IgA1 and IgA2 on binding to the Fcα receptor (FcαRI), which is also heavily glycosylated at its extracellular domain.
31362986	2	82	gly	glycosylated	364:375	arg1	the Fcα receptor	Fcα receptor		domain		PUBTATOR		Fcα receptor	2204	domain	Little is known about the impact of N-glycan modifications of IgA1 and IgA2 on binding to the Fcα receptor (FcαRI), which is also heavily glycosylated at its extracellular domain.
30151520	2	87	gly	glycopeptide	443:454	arg2	a given glycopeptide ion			a given glycopeptide ion						glycopeptide	In this context, the overall composition of a given glycopeptide ion is a key characteristic; however, the extent to which the carbohydrate moiety influences the preferred dissociation channels has received relatively little study.
30990348	7	148	gly	residue	1595:1601	arg1	the Man α1-6 arm			the Man α1-6 arm	the Man α1-6 arm						Considering that mAbs interact with FcγR and C1q via their hinge proximal region in the CH2 domain, the structural stabilization of the CH2 domain by the terminal Gal residue on the Man α1-6 arm of Fc-glycans may be important for the effector functions of mAbs.
30542567	6	3	gly	glycopeptide	1034:1045	arg2	a glycopeptide acceptor			a glycopeptide acceptor						glycopeptide	The N-glycans were then transformed to oxazoline donors and ligated with a glycopeptide acceptor from haptoglobin promoted by the wild type Arthrobacter endo-β-N-acetylglucosaminidase (Endo-A).
29475941	10	48	gly	structures	1471:1480	arg1	recombinant proteins	proteins			structures	Fterm		proteins			The N-glycan structures on recombinant proteins expressed in triple KO cells were simplified and changed from complex types to high-mannose types at the protein level.
30612271	5	66	part_of	VC1	678:680	arg1	the VC1 domain	VC1		the VC1 domain		Cterm	Site	VC1		domain	The majority of RAGE ligands bind to the VC1 domain.
30466347	1	13	gly	Glycosylation	146:158	arg1	the conserved asparagine residue			the conserved asparagine residue						asparagine residue	Glycosylation of the conserved asparagine residue in each heavy chain of IgG in the CH2 domain is known as N-glycosylation.
31108197	0	49	gly	glycosylation	9:21	arg1	membrane proteins	membrane proteins				Fterm		proteins			Distinct glycosylation in membrane proteins within neonatal versus adult myocardial tissue.
29703890	0	28	gly	glycoproteins	107:119	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			An enrichment method based on synergistic and reversible covalent interactions for large-scale analysis of glycoproteins.
31111416	9	12	part_of	Env	1545:1547	arg1	Env sequence	Env		Env sequence		PUBTATOR	Site	Env	100616444	sequence	The exact glycan profiles were provided for 20 individual sites, whereas only the glycosylation type could be deduced for 5 sites, dictated by their location within Env sequence.
31751705	2	35	gly	glycopeptide	713:724	arg2	glycopeptide			glycopeptide						glycopeptide	Three types of Asn-oligosaccharide (Asn-M3FX, Asn-M8, or Asn-NeuAc2Gal2GN2M3) were prepared from storage glycoproteins of Ginkgo biloba seeds, Vigna angularis seeds, and egg yolk glycopeptides from actinase digests of each glycoproteins or glycopeptide.
31751705	2	40	gly	glycoproteins	578:590	arg1	storage glycoproteins	storage glycoproteins				Fterm		glycoproteins			Three types of Asn-oligosaccharide (Asn-M3FX, Asn-M8, or Asn-NeuAc2Gal2GN2M3) were prepared from storage glycoproteins of Ginkgo biloba seeds, Vigna angularis seeds, and egg yolk glycopeptides from actinase digests of each glycoproteins or glycopeptide.
31751705	2	46	gly	glycoproteins	696:708	arg1	each glycoproteins	each glycoproteins				Fterm		glycoproteins			Three types of Asn-oligosaccharide (Asn-M3FX, Asn-M8, or Asn-NeuAc2Gal2GN2M3) were prepared from storage glycoproteins of Ginkgo biloba seeds, Vigna angularis seeds, and egg yolk glycopeptides from actinase digests of each glycoproteins or glycopeptide.
31751705	2	68	gly	glycopeptides	652:664	arg2	egg yolk glycopeptides			egg yolk glycopeptides						glycopeptides	Three types of Asn-oligosaccharide (Asn-M3FX, Asn-M8, or Asn-NeuAc2Gal2GN2M3) were prepared from storage glycoproteins of Ginkgo biloba seeds, Vigna angularis seeds, and egg yolk glycopeptides from actinase digests of each glycoproteins or glycopeptide.
30899004	5	11	gly	N-glycosite	967:977	arg2	N-glycosite heterogeneity			N-glycosite heterogeneity						N-glycosite	Our data reveal that N-glycosylation profiles can differ between subcellular regions and structural domains and that N-glycosite heterogeneity manifests in several different forms, including dramatic differences in glycosites on the same protein.
30899004	5	24	gly	glycosites	1065:1074	arg2	glycosites			glycosites						glycosites	Our data reveal that N-glycosylation profiles can differ between subcellular regions and structural domains and that N-glycosite heterogeneity manifests in several different forms, including dramatic differences in glycosites on the same protein.
30033600	4	46	gly	removed	637:643	arg1	bovine fetuin AND the sialic acid residues	bovine fetuin			the sialic acid residues	Fterm		fetuin			It is found that more than 90% of the sialic acid residues can be removed from bovine fetuin by the acid-assisted de-sialylation method, which significantly simplifies the glycan structure and improves identification sensitivity.
31525900	5	12	gly	laminarioligosaccharide	942:964	arg1	one glucosyl residue			one glucosyl residue	one glucosyl residue		Site			residue	BGL1 transferred one glucosyl residue from substrate laminarioligosaccharide to another laminarioligosaccharide as an acceptor in a β(1 → 3) or β(1 → 6) fashion to produce higher laminarioligosaccharides or 3-O-β-d-gentiobiosyl-d-laminarioligosaccharides.
29433940	8	31	gly	di-sialylated	945:957	arg1	additional di-sialylated N-glycan structures				additional di-sialylated N-glycan structures						Furthermore, the co-expression of N-acetylglucosaminyltransferase II facilitated the formation of additional di-sialylated N-glycan structures.
29405331	10	42	part_of	A1AT	1474:1477	arg1	A1AT glycopeptides	A1AT		A1AT glycopeptides		PUBTATOR	Site	A1AT	5265	glycopeptides	Structural assignments revealed that all three glycosylation sites of A1AT glycopeptides contain complex N-glycan structures: site Asn70 contains biantennary glycans without fucosylation; site Asn107 contains bi-, tri- and tetra-antennary glycans with both core- and antennary-fucosylation; site Asn271 contains bi- and tri-antennary glycans with both core- and antennary-fucosylation.
30385505	3	29	gly	glycans	521:527	arg1	glycoproteins	glycoproteins			glycans	Fterm		glycoproteins			However, in cells, galectins bind glycans on glycoproteins and glycolipids in the context of other cellular components, such as at the cell surface.
30385505	3	30	gly	glycoproteins	532:544	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			However, in cells, galectins bind glycans on glycoproteins and glycolipids in the context of other cellular components, such as at the cell surface.
31100702	13	2	gly	glycoproteins	1733:1745	arg1	all target glycoproteins	all target glycoproteins				Fterm		glycoproteins			These results indicate that acetone precipitation, a commonly used step for small-scale glycan purification, is not suitable for all target glycoproteins.
29619832	5	31	gly	glycosylation	968:980	arg1	the same protein	the same protein				Fterm		protein			These data were compared to the glycosylation profile of the same protein expressed in insect cells.
29502191	9	5	gly	glycoproteins	1241:1253	arg1	cellular glycoproteins	cellular glycoproteins				Fterm		glycoproteins			The presence of these unusual complex N-glycans resulted in stronger interactions of cellular glycoproteins with the PHA-L.
31384044	0	15	gly	glycopeptide	78:89	arg2	silico-boosted glycopeptide libraries			silico-boosted glycopeptide libraries						glycopeptide	Glyco-DIA: a method for quantitative O-glycoproteomics with in silico-boosted glycopeptide libraries.
30611426	4	35	gly	glycoprotein	772:783	arg1	glycoprotein composition	glycoprotein composition				Fterm		glycoprotein			However, the ability to study the structure of glycoproteins to high resolution was historically limited by technical barriers including a limited availability of appropriate recombinant protein expression platforms, limited methods to generate compositional homogeneity, and difficulties analyzing glycoprotein composition.
30611426	4	51	gly	glycoproteins	520:532	arg1	glycoproteins	glycoproteins				Fterm		structure of glycoproteins			However, the ability to study the structure of glycoproteins to high resolution was historically limited by technical barriers including a limited availability of appropriate recombinant protein expression platforms, limited methods to generate compositional homogeneity, and difficulties analyzing glycoprotein composition.
31338503	6	59	gly	neoglycoprotein	1046:1060	arg1	the CFG and neoglycoprotein array platforms	the CFG and neoglycoprotein array platforms				Fterm		neoglycoprotein			In this study, we performed a systematic comparison of microarray data from 8 lectins across a range of concentrations on the CFG and neoglycoprotein array platforms.
30899004	6	1	gly	glycopeptides	1232:1244	arg2	intact glycopeptides			intact glycopeptides						glycopeptides	Moreover, we use this large-scale glycoproteomic dataset to develop several visualizations that will prove useful for analyzing intact glycopeptides in future studies.
29330305	7	64	gly	glycoprotein	1675:1686	arg1	the glycoprotein's	the glycoprotein's				Fterm		glycoprotein			The changes in binding activity mirrored changes in NMR spectra of the two CD16a glycoforms, indicating that CD16a glycan composition also affects the glycoprotein's structure.
31593866	1	1	gly	N-glycosylation	339:353	arg1	therapeutic glycoproteins	therapeutic glycoproteins				Fterm		glycoproteins			As glycomics research is gaining momentum in the biopharmaceutical industry, there is an increasing need for reproducible high throughput glycoanalytical methods to monitor and characterize the N-glycosylation of therapeutic glycoproteins.
31593866	1	9	gly	glycoproteins	370:382	arg1	therapeutic glycoproteins	therapeutic glycoproteins				Fterm		glycoproteins			As glycomics research is gaining momentum in the biopharmaceutical industry, there is an increasing need for reproducible high throughput glycoanalytical methods to monitor and characterize the N-glycosylation of therapeutic glycoproteins.
29976678	3	83	part_of	glycoprotein	501:512	arg1	the premembrane (prM) and envelope (E) glycoprotein regions	glycoprotein		the premembrane (prM) and envelope (E) glycoprotein regions		Fterm	Site	glycoprotein		regions	We first created a panel of ZIKV mutants with the FLAG epitope inserted in the premembrane (prM) and envelope (E) glycoprotein regions.
29858715	1	5	gly	glycoprotein	187:198	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			Prolactin-inducible protein (PIP) is a glycoprotein found in body secretions from exocrine glands like saliva and seminal plasma.
30902814	5	79	part_of	M41-RBD	737:743	arg1	the predicted N-glycosylation sites	M41		the predicted N-glycosylation sites		PUBTATOR	Site	M41		sites	Ten single Asn-to-Ala substitutions at the predicted N-glycosylation sites of the M41-RBD were evaluated along with two control Val-to-Ala substitutions.
29931153	7	59	gly	glycoproteins	1435:1447	arg1	fully folded glycoproteins	fully folded glycoproteins				Fterm		glycoproteins			Potential bias of protein structural features toward immature or mature forms was explored within a range of concentric circles of fully folded glycoproteins.
31370181	2	44	gly	glycoprotein	358:369	arg1	glycoprotein B	glycoprotein B				Fterm		glycoprotein B			The aim of this study consisted of expressing the large soluble ectodomain of glycoprotein B (gB) from Human Cytomegalovirus (HMCV) in Nicotiana tabacum Bright Yellow-2 (BY-2) suspension cells and of comparing its glycosylation profile with that of gB produced in Chinese hamster ovary (CHO) cells.
29725729	1	20	gly	glycoproteins	234:246	arg1	quite a few glycoproteins	quite a few glycoproteins				Fterm		glycoproteins			Aberrant glycosylation has been commonly observed in various physiological and pathological disorders (including cancers), and quite a few glycoproteins have been approved by the US Food and Drug Administration (FDA) as markers for early diagnosis.
29878199	3	84	gly	glycoproteins	593:605	arg1	total plasma glycoproteins	total plasma glycoproteins				Fterm		glycoproteins			In a cohort of 99 individuals with abnormal Golgi glycosylation, 47 of which being unsolved, glycomics profiling was performed of total plasma glycoproteins.
30361439	7	1	gly	asparagine-linked	1002:1018	arg1	N-glycans			asparagine	N-glycans					asparagine	The interaction of IgG1 Fc with CD16a, but not with CD16b, is known to be sensitive to the composition of the asparagine-linked carbohydrates (N-glycans) attached to the receptor.
30361439	7	1	gly	asparagine-linked	1002:1018	arg1	the asparagine-linked carbohydrates			asparagine	the asparagine-linked carbohydrates					asparagine	The interaction of IgG1 Fc with CD16a, but not with CD16b, is known to be sensitive to the composition of the asparagine-linked carbohydrates (N-glycans) attached to the receptor.
30361439	7	6	gly	attached	1046:1053	arg1	the receptor AND the asparagine-linked carbohydrates	the receptor			the asparagine-linked carbohydrates	Fterm		receptor			The interaction of IgG1 Fc with CD16a, but not with CD16b, is known to be sensitive to the composition of the asparagine-linked carbohydrates (N-glycans) attached to the receptor.
30361439	7	6	gly	attached	1046:1053	arg2	the receptor AND N-glycans	the receptor			N-glycans	Fterm		receptor			The interaction of IgG1 Fc with CD16a, but not with CD16b, is known to be sensitive to the composition of the asparagine-linked carbohydrates (N-glycans) attached to the receptor.
30444974	6	63	gly	Hex3HexNAc2	1027:1037	arg1	fragments			fragments	fragments		Site			fragments	The N-linked glycan profile showed fragments from Hex3HexNAc2 to Hex9HexNAc2.
30325416	5	21	part_of	IgGs	1280:1283	arg1	the Fc region	IgGs		the Fc region		Cterm	Site	IgGs		region	Here we report the results of a systematic study, based on extensive molecular dynamics simulations in excess of 62 μs of cumulative simulation time, on the effect of sequence on the structure and dynamics of increasingly larger, complex biantennary N-glycoforms isolated from the protein, i.e. from chitobiose to the larger N-glycan species commonly found in the Fc region of human IgGs.
31031563	4	15	gly	regions	717:723	arg1	the glycan structures			regions	the glycan structures					regions	Using a recently developed mass spectrometry imaging approach to evaluate N-linked glycan distributions in human formalin-fixed clinical cancer tissues, differences in the glycan structures of regions of tumor, stroma and necrosis were evaluated.
30063822	1	34	gly	glycoproteins	220:232	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			An enzyme- and click chemistry-mediated methodology for the site-specific nitroxide spin labeling of glycoproteins has been developed and applied.
29949660	2	2	part_of	lignin	346:351	arg1	different lignin compositions	lignin		different lignin compositions		Fterm	Site	lignin		positions,	Two Arabidopsis lines with similar lignin contents, but strikingly different lignin compositions, exhibited different quantitative and qualitative transcriptional responses.
30513306	3	14	part_of	glycoprotein	406:417	arg1	a chitin binding domain 4	glycoprotein		a chitin binding domain 4		Fterm	Site	glycoprotein		domain	LmAbd-9 encodes a glycoprotein with a chitin binding domain 4, belonging to RR-1 subclass of the CPR family, which has two potential O-linked glycosylation sites (S115 and T137) at which glycosylation modification may occur.
30513306	3	38	part_of	has	503:505	arg1	a glycoprotein AND two potential O-linked glycosylation sites	a glycoprotein		two potential O-linked glycosylation sites		Fterm	Site	glycoprotein		sites	LmAbd-9 encodes a glycoprotein with a chitin binding domain 4, belonging to RR-1 subclass of the CPR family, which has two potential O-linked glycosylation sites (S115 and T137) at which glycosylation modification may occur.
31362986	7	74	gly	N-glycans	1334:1342	arg1	the receptor	receptor			N-glycans	Fterm		receptor			Our results suggest that different N-glycans on the receptor significantly contribute to binding affinities for its cognate ligand.
31145522	2	5	gly	LacdiNAc-glycosylated	285:305	arg1	LDN-PSA				LDN-PSA						To identify clinically significant prostate cancer (CSPC) we determined the performance of LacdiNAc-glycosylated prostate-specific antigen (LDN-PSA) and LDN-PSA normalized by prostate volume (LDN-PSAD).
31145522	2	5	gly	LacdiNAc-glycosylated	285:305	arg1	LacdiNAc-glycosylated prostate-specific antigen				LacdiNAc-glycosylated prostate-specific antigen						To identify clinically significant prostate cancer (CSPC) we determined the performance of LacdiNAc-glycosylated prostate-specific antigen (LDN-PSA) and LDN-PSA normalized by prostate volume (LDN-PSAD).
30673210	6	38	gly	glycopeptide	1352:1363	arg2	glycopeptide enrichment			glycopeptide enrichment						glycopeptide	A molar ratio of IgG trypsin digest to bovine serum albumin trypsin digest as low as 1/500 verified the outstanding specificity and efficiency for glycopeptide enrichment.
29976678	2	13	gly	glycoproteins	244:256	arg1	these glycoproteins	these glycoproteins				Fterm		glycoproteins			In this study, we explored the capacity of these glycoproteins to tolerate insertion of linear epitope sequences and the potential of antibodies that bind these epitopes to inhibit infection.
31154130	0	15	gly	glycopeptides	78:90	arg2	IgG-Fc glycopeptides			IgG-Fc glycopeptides						glycopeptides	An integrated approach for comprehensive profiling and quantitation of IgG-Fc glycopeptides with application to rheumatoid arthritis.
30898876	8	14	gly	glycoproteins	1775:1787	arg1	mammalian glycoproteins	mammalian glycoproteins				Fterm		glycoproteins			Taken together, our results indicate the presence of mammalian glycoproteins carrying type-I LDN on N-glycans and suggest that type-I and type-II LDNs have different roles in vivo.
30898876	8	85	gly	carrying	1789:1796	arg1	mammalian glycoproteins AND type-I LDN	mammalian glycoproteins			type-I LDN	Fterm		glycoproteins			Taken together, our results indicate the presence of mammalian glycoproteins carrying type-I LDN on N-glycans and suggest that type-I and type-II LDNs have different roles in vivo.
30513259	1	82	part_of	Fc	280:281	arg1	the crystallizable fragment (Fc) region	Fc		the crystallizable fragment (Fc) region		Cterm	Site	Fc		region	The N-linked glycan in immunoglobulin G is critical for the stability and function of the crystallizable fragment (Fc) region.
31256374	1	34	gly	glycoproteins	45:57	arg1	Most glycoproteins	Most glycoproteins				Fterm		glycoproteins			Most glycoproteins carry a very heterogeneous mixture of oligosaccharides and even a single glycosylation site of a pure glycoprotein is often heterogeneously glycosylated.
31256374	1	37	gly	glycoprotein	161:172	arg1	a pure glycoprotein	a pure glycoprotein				Fterm		glycoprotein			Most glycoproteins carry a very heterogeneous mixture of oligosaccharides and even a single glycosylation site of a pure glycoprotein is often heterogeneously glycosylated.
31256374	1	6	gly	glycosylated	199:210	arg1	a pure glycoprotein	glycoprotein		site		Fterm		glycoprotein		site	Most glycoproteins carry a very heterogeneous mixture of oligosaccharides and even a single glycosylation site of a pure glycoprotein is often heterogeneously glycosylated.
31256374	1	28	gly	glycosylation	132:144	arg1	a pure glycoprotein	glycoprotein		site		Fterm		glycoprotein		site	Most glycoproteins carry a very heterogeneous mixture of oligosaccharides and even a single glycosylation site of a pure glycoprotein is often heterogeneously glycosylated.
31289257	4	12	gly	glycoproteins	762:774	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Altered glycosylation was detected using biotinylated agaracus bisporus lectin, which specifically binds exposed Gal-(β-1,3)-GalNAc linked to glycoproteins.
31815459	6	72	gly	glycosylation	1218:1230	arg1	a rare l-fucosamine- and d-fucosamine-containing 1,2-cis-linked disaccharide motif			a rare l-fucosamine- and d-fucosamine-containing 1,2-cis-linked disaccharide motif							Here, we report the first total synthesis of the conjugation-ready trisaccharide repeating unit of Pseudomonas aeruginosa O11 via a highly stereoselective and efficient assembly of a rare l-fucosamine- and d-fucosamine-containing 1,2-cis-linked disaccharide motif and its regioselective glycosylation at O3.
30943309	4	28	gly	de-sialylated	537:549	arg1	The major de-sialylated N-glycan structures				The major de-sialylated N-glycan structures						The major de-sialylated N-glycan structures of cells and EVs are core-fucosylated, tetra-antennary N-glycans with β1,6-N-acetylglucosamine branches.
30943309	4	28	gly	de-sialylated	537:549	arg1	core-fucosylated, tetra-antennary N-glycans				core-fucosylated, tetra-antennary N-glycans						The major de-sialylated N-glycan structures of cells and EVs are core-fucosylated, tetra-antennary N-glycans with β1,6-N-acetylglucosamine branches.
30943309	4	55	gly	core-fucosylated	592:607	arg1	The major de-sialylated N-glycan structures				The major de-sialylated N-glycan structures						The major de-sialylated N-glycan structures of cells and EVs are core-fucosylated, tetra-antennary N-glycans with β1,6-N-acetylglucosamine branches.
30943309	4	55	gly	core-fucosylated	592:607	arg1	core-fucosylated, tetra-antennary N-glycans				core-fucosylated, tetra-antennary N-glycans						The major de-sialylated N-glycan structures of cells and EVs are core-fucosylated, tetra-antennary N-glycans with β1,6-N-acetylglucosamine branches.
30087829	7	19	gly	glycosylation	719:731	arg2	one highly conserved glycosylation site			one highly conserved glycosylation site						site	Unlike highly glycosylated fungal laccases, the less-glycosylated DLac contains one highly conserved glycosylation site at N432 and an unique glycosylation site at N468.
30087829	7	19	gly	glycosylation	719:731	arg2	N468			N468						N468	Unlike highly glycosylated fungal laccases, the less-glycosylated DLac contains one highly conserved glycosylation site at N432 and an unique glycosylation site at N468.
30087829	7	19	gly	glycosylation	719:731	arg2	N432			N432						N432	Unlike highly glycosylated fungal laccases, the less-glycosylated DLac contains one highly conserved glycosylation site at N432 and an unique glycosylation site at N468.
30087829	7	28	gly	glycosylation	760:772	arg2	N468			N468						N468	Unlike highly glycosylated fungal laccases, the less-glycosylated DLac contains one highly conserved glycosylation site at N432 and an unique glycosylation site at N468.
30087829	7	28	gly	glycosylation	760:772	arg2	an unique glycosylation site			an unique glycosylation site						site	Unlike highly glycosylated fungal laccases, the less-glycosylated DLac contains one highly conserved glycosylation site at N432 and an unique glycosylation site at N468.
30087829	7	28	gly	glycosylation	760:772	arg2	N432			N432						N432	Unlike highly glycosylated fungal laccases, the less-glycosylated DLac contains one highly conserved glycosylation site at N432 and an unique glycosylation site at N468.
31409668	9	19	gly	fucosylated	1431:1441	arg1	fucosylated glycans				fucosylated glycans						Lactating participants who had given birth by vaginal delivery presented an increased proportion of high mannose and fucosylated glycans in salivary SIgA, and selected high mannose, fucosylated, sialylated, and both fucosylated and sialylated glycans in plasma IgA, indicating that the hormonal changes during vaginal delivery could affect plasma and saliva IgA.
31409668	9	92	gly	fucosylated	1530:1540	arg1	both fucosylated and sialylated glycans				both fucosylated and sialylated glycans						Lactating participants who had given birth by vaginal delivery presented an increased proportion of high mannose and fucosylated glycans in salivary SIgA, and selected high mannose, fucosylated, sialylated, and both fucosylated and sialylated glycans in plasma IgA, indicating that the hormonal changes during vaginal delivery could affect plasma and saliva IgA.
31409668	9	94	gly	sialylated	1546:1555	arg1	both fucosylated and sialylated glycans				both fucosylated and sialylated glycans						Lactating participants who had given birth by vaginal delivery presented an increased proportion of high mannose and fucosylated glycans in salivary SIgA, and selected high mannose, fucosylated, sialylated, and both fucosylated and sialylated glycans in plasma IgA, indicating that the hormonal changes during vaginal delivery could affect plasma and saliva IgA.
30612270	6	34	gly	glycopeptides	1089:1101	arg2	glycopeptides			glycopeptides						glycopeptides	The four glycosylation sites of human serum ceruloplasmin from 17 different individuals were analyzed using glycopeptides of varying peptide lengths, obtained by action of different proteases and by limited digestion.
30612270	6	54	gly	glycosylation	990:1002	arg1	human serum ceruloplasmin	ceruloplasmin		sites		PUBTATOR		ceruloplasmin	1356	sites	The four glycosylation sites of human serum ceruloplasmin from 17 different individuals were analyzed using glycopeptides of varying peptide lengths, obtained by action of different proteases and by limited digestion.
31841688	5	16	gly	afucosylated	1086:1097	arg1	afucosylated glycans				afucosylated glycans						Notably, we confirmed that the biosimilar had a higher level of afucosylated glycans, resulting in a stronger FcγIIIa binding affinity and increased ADCC activity.
30902814	8	32	gly	glycosylation	1123:1135	arg2	glycosylation sites			glycosylation sites						sites	LC/MSE glycomics analysis revealed that glycosylation sites have specific proportions of N-glycan subtypes.
30152690	4	39	gly	glycosylation	899:911	arg2	the site			the site						site	Investigations involving mass spectrometry, molecular modeling, and mutagenesis revealed that the glycan shedding was site-specific, dependent on structural elements, and required a glycine residue immediately following the site of glycosylation.
31888963	6	69	gly	glycosylation	905:917	arg2	glycosylation site			glycosylation site						site	The composition of CD16a N-glycans varied by glycosylation site and donor.
31545132	0	17	part_of	PEKK-HAp-CS	35:45	arg1	PEKK-HAp-CS composites	HAp		PEKK-HAp-CS composites		OGER	Site	HAp	O95197	composites	Thermomechanical investigations of PEKK-HAp-CS composites.
30669833	8	83	gly	glycoproteins	1462:1474	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Lectin histochemical staining analysis also showed that PCa cells overexpressed glycoproteins containing LacdiNAc and sialic acids moieties.
30669833	8	16	gly	containing	1476:1485	arg1	glycoproteins AND LacdiNAc and sialic acids moieties	glycoproteins			LacdiNAc and sialic acids moieties	Fterm		glycoproteins			Lectin histochemical staining analysis also showed that PCa cells overexpressed glycoproteins containing LacdiNAc and sialic acids moieties.
31174130	0	31	gly	glycopeptides	87:99	arg2	glycopeptides			glycopeptides						glycopeptides	A New titania glyco-purification tip for the fast enrichment and efficient analysis of glycopeptides and glycans by MALDI-TOF-MS.
29437979	4	35	gly	glycosylation	707:719	arg2	positions 77, 162, 542, 604, and 627			positions 77, 162, 542, 604, and 627						positions 77, 162, 542, 604, and 627,	gH contains five potential N-linked glycosylation sites at positions 77, 162, 542, 604, and 627, which were inactivated by conservative mutations (asparagine to glutamine) singly or in combination.
29437979	4	35	gly	glycosylation	707:719	arg2	five potential N-linked glycosylation sites			five potential N-linked glycosylation sites						sites	gH contains five potential N-linked glycosylation sites at positions 77, 162, 542, 604, and 627, which were inactivated by conservative mutations (asparagine to glutamine) singly or in combination.
29437979	4	63	gly	mutations	807:815	arg1	asparagine			asparagine						asparagine	gH contains five potential N-linked glycosylation sites at positions 77, 162, 542, 604, and 627, which were inactivated by conservative mutations (asparagine to glutamine) singly or in combination.
31311856	0	12	gly	derived	13:19	arg2	O-mannosylated glycoproteins AND Free glycans	O-mannosylated glycoproteins			Free glycans	Fterm		glycoproteins			Free glycans derived from O-mannosylated glycoproteins suggest the presence of an O-glycoprotein degradation pathway in yeast.
31311856	0	17	gly	O-glycoprotein	82:95	arg1	an O-glycoprotein degradation pathway	an O-glycoprotein degradation pathway				Fterm		O-glycoprotein			Free glycans derived from O-mannosylated glycoproteins suggest the presence of an O-glycoprotein degradation pathway in yeast.
31311856	0	59	gly	O-mannosylated	26:39	arg1	O-mannosylated glycoproteins	O-mannosylated glycoproteins				Fterm		glycoproteins			Free glycans derived from O-mannosylated glycoproteins suggest the presence of an O-glycoprotein degradation pathway in yeast.
31311856	0	62	gly	glycoproteins	41:53	arg1	O-mannosylated glycoproteins	O-mannosylated glycoproteins				Fterm		glycoproteins			Free glycans derived from O-mannosylated glycoproteins suggest the presence of an O-glycoprotein degradation pathway in yeast.
30685086	1	12	part_of	proteins	324:331	arg1	Ser or Thr residues	proteins		Ser or Thr residues		Fterm	AminoAcid	proteins		Thr residues	The UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases (GalNAc-Ts) catalyze mucin-type O-glycosylation by transferring α-N-acetylgalactosamine (GalNAc) from UDP- GalNAc to Ser or Thr residues of target proteins.
30500162	7	31	gly	glycopeptides	1054:1066	arg2	glycopeptides			glycopeptides						glycopeptides	Here, we compare serum IgG recognition of Neu5Gc-containing glycoproteins, glycopeptides, and synthetic glycans.
30500162	7	45	gly	glycoproteins	1039:1051	arg1	Neu5Gc-containing glycoproteins				Neu5Gc-containing glycoproteins						Here, we compare serum IgG recognition of Neu5Gc-containing glycoproteins, glycopeptides, and synthetic glycans.
28921428	2	8	part_of	Galα1,3-Gal	338:348	arg1	Galα1,3-Gal (alpha-Gal) and N-glycolylneuraminic acid (Neu5Gc) residues	Gal		Galα1,3-Gal (alpha-Gal) and N-glycolylneuraminic acid (Neu5Gc) residues		OGER	Site	Gal	Q8N6F7	residues	Recombinant proteins produced in nonhuman cells can have in its structure glycan epitopes, such as Galα1,3-Gal (alpha-Gal) and N-glycolylneuraminic acid (Neu5Gc) residues, that are antigenic to humans and can potentially affect the efficacy of the recombinant product.
30848132	2	33	gly	glycosylated	347:358	arg1	highly glycosylated proteins	highly glycosylated proteins				Fterm		proteins			The intestinal tract is covered by a mucus layer mainly comprised by highly glycosylated proteins called mucins.
31485742	4	47	gly	glycosylated	572:583	arg1	a potent antibacterial glycosylated peptide			peptide	[βGlc-T9					peptide	Our study led to the design of a potent antibacterial glycosylated peptide, [βGlc-T9,K7]indolicidin, which showed decreased toxicity against erythrocytes and macrophage cells and thus a higher therapeutic selectivity.
31485742	4	47	gly	glycosylated	572:583	arg1	K7]indolicidin	indolicidin			[βGlc-T9	Fterm		indolicidin			Our study led to the design of a potent antibacterial glycosylated peptide, [βGlc-T9,K7]indolicidin, which showed decreased toxicity against erythrocytes and macrophage cells and thus a higher therapeutic selectivity.
31485742	4	47	gly	glycosylated	572:583	arg1	K7]indolicidin	indolicidin		peptide		Fterm		indolicidin		peptide	Our study led to the design of a potent antibacterial glycosylated peptide, [βGlc-T9,K7]indolicidin, which showed decreased toxicity against erythrocytes and macrophage cells and thus a higher therapeutic selectivity.
30892132	5	7	gly	observed	1021:1028	arg2	three potential N-linked glycosylation sites AND The glycan modifications			three potential N-linked glycosylation sites	The glycan modifications					sites	The glycan modifications of PD-1 could be observed in three potential N-linked glycosylation sites, while no substantial influences were detected to the binding of toripalimab.
30892132	5	24	gly	glycosylation	1058:1070	arg2	three potential N-linked glycosylation sites			three potential N-linked glycosylation sites						sites	The glycan modifications of PD-1 could be observed in three potential N-linked glycosylation sites, while no substantial influences were detected to the binding of toripalimab.
29593217	4	23	gly	residues	749:756	arg1	the N332gp120 glycan			residues	the N332gp120 glycan					residues	Our structures show conserved contacts mediated by common D gene-encoded residues with the N332gp120 glycan and the gp120 GDIR peptide motif, but a distinct Env-binding orientation relative to PGT121/10-1074 bNAbs.
30673159	9	44	gly	glycopeptide	1360:1371	arg2	the resulting glycopeptide hybrids			the resulting glycopeptide hybrids						glycopeptide	The incorporation of these glycan residues into the peptide structure influenced the internalization efficiency and cellular toxicity of the resulting glycopeptide hybrids in the different cell lines tested.
31208374	9	74	gly	sialylated	1463:1472	arg1	sialylated structures				sialylated structures						Most of these glycans were core-fucosylated, multiply branched and sialylated structures, whose abundance has been strongly associated with greater invasive and metastatic potential of cancer.
31208374	9	116	gly	core-fucosylated	1423:1438	arg1	these glycans				these glycans						Most of these glycans were core-fucosylated, multiply branched and sialylated structures, whose abundance has been strongly associated with greater invasive and metastatic potential of cancer.
31737090	4	60	gly	glycosylation	733:745	arg2	the C-terminus β-sandwich domain			the C-terminus β-sandwich domain						domain	The structural modeling showed that all five glycosylation sites (Asn-362, Asn-370, Asn-399, Asn-467 and Asn-526) were located at the C-terminus β-sandwich domain, which has been proven to be more conducive to the occurrence of glycosylation modification than the N-terminus domain.
31737090	4	60	gly	glycosylation	733:745	arg2	all five glycosylation sites			all five glycosylation sites						sites	The structural modeling showed that all five glycosylation sites (Asn-362, Asn-370, Asn-399, Asn-467 and Asn-526) were located at the C-terminus β-sandwich domain, which has been proven to be more conducive to the occurrence of glycosylation modification than the N-terminus domain.
31737090	4	95	gly	sites	747:751	arg1	all five glycosylation sites			all five glycosylation sites						sites	The structural modeling showed that all five glycosylation sites (Asn-362, Asn-370, Asn-399, Asn-467 and Asn-526) were located at the C-terminus β-sandwich domain, which has been proven to be more conducive to the occurrence of glycosylation modification than the N-terminus domain.
31737090	4	60	gly	glycosylation	733:745	arg2	Asn-526			Asn-362, Asn-370, Asn-399, Asn-467 and Asn-526						Asn-362, Asn-370, Asn-399, Asn-467 and Asn-526	The structural modeling showed that all five glycosylation sites (Asn-362, Asn-370, Asn-399, Asn-467 and Asn-526) were located at the C-terminus β-sandwich domain, which has been proven to be more conducive to the occurrence of glycosylation modification than the N-terminus domain.
31737090	4	95	gly	sites	747:751	arg1	Asn-526			Asn-362, Asn-370, Asn-399, Asn-467 and Asn-526						Asn-362, Asn-370, Asn-399, Asn-467 and Asn-526	The structural modeling showed that all five glycosylation sites (Asn-362, Asn-370, Asn-399, Asn-467 and Asn-526) were located at the C-terminus β-sandwich domain, which has been proven to be more conducive to the occurrence of glycosylation modification than the N-terminus domain.
29593217	2	24	part_of	epitopes	426:433	arg1	Env	Env		epitopes		PUBTATOR	Site	Env	155971	epitopes	Developing bNAbs with increased efficacy requires understanding how antibodies interact with the native oligomannose and complex-type N-glycan shield that hides most protein epitopes on HIV-1 envelope (Env).
29593217	2	24	part_of	epitopes	426:433	arg1	HIV-1 envelope	HIV-1 envelope		epitopes		PUBTATOR	Site	HIV-1 envelope	155971	epitopes	Developing bNAbs with increased efficacy requires understanding how antibodies interact with the native oligomannose and complex-type N-glycan shield that hides most protein epitopes on HIV-1 envelope (Env).
29405331	9	49	gly	glycopeptide	1265:1276	arg2	initial glycopeptide fragmentation			initial glycopeptide fragmentation						glycopeptide	The collision energy used for initial glycopeptide fragmentation was found to be crucial for improved detection of oxonium ions and better selection of Y1 ion (peptide+GlcNAc).
29502007	1	5	gly	glycoprotein	173:184	arg1	a glycoprotein hormone	a glycoprotein hormone				Fterm		glycoprotein			Recombinant, human, erythropoietin (rhEPO) is a glycoprotein hormone which is prescribed throughout the world to treat anaemia caused by chronic kidney disease or chemotherapy.
31737090	5	35	part_of	Mut	1058:1060	arg1	all five N-glycosylation sites	Mut		all five N-glycosylation sites		OGER	Site	Mut	P22033	sites	Single-site N-glycosylation mutants with Asn substituted by Gln were obtained, and the Mut with all five N-glycosylation sites removed was constructed, which resulted in the loss of all enzyme activity.
31245822	8	60	gly	di-sialylated	1225:1237	arg1	di-sialylated structures				di-sialylated structures						The main structures present in saliva were neutral oligosaccharides consisting of high mannose, hybrid and complex structures, followed by smaller fractions of mono and di-sialylated structures.
30782654	0	111	gly	Glycosylation	68:80	arg1	a Gram-Positive Bacterial Cell Wall-Anchored Protein				a Gram-Positive Bacterial Cell Wall-Anchored Protein						Structure and Mechanism of LcpA, a Phosphotransferase That Mediates Glycosylation of a Gram-Positive Bacterial Cell Wall-Anchored Protein.
29441788	1	23	part_of	glycoprotein	96:107	arg1	five predicted N-glycosylation sites	glycoprotein		five predicted N-glycosylation sites		Fterm	Site	glycoprotein		sites	Afamin is an 87 kDa glycoprotein with five predicted N-glycosylation sites.
31256376	3	79	gly	C-mannosylation	400:414	arg2	Trp residues			Trp residues						Trp residues	C-mannosylation occurs on Trp residues within a relatively loosely defined consensus motif.
30186849	3	73	gly	glycopeptide	582:593	arg2	intact N-linked glycopeptide identification			intact N-linked glycopeptide identification						glycopeptide	Here we present pMatchGlyco, a new spectral library search tool for intact N-linked glycopeptide identification using high-energy collisional dissociation (HCD) tandem mass spectrometry (MS/MS) data.
31592495	1	19	gly	glycoprotein	138:149	arg1	a cell-surface N-linked glycoprotein	a cell-surface N-linked glycoprotein				Fterm		glycoprotein			CD73, a cell-surface N-linked glycoprotein that produces extracellular adenosine, is a novel target for cancer immunotherapy.
29408873	3	8	gly	asparagine-linked	707:723	arg1	GlcNAc asparagine-linked (N)-glycan			asparagine	GlcNAc asparagine-linked (N)-glycan					asparagine	Models of mIgG2c Fc determined by x-ray crystallography with a complex-type biantennary (to 2.05 Å) or a truncated (1)GlcNAc asparagine-linked (N)-glycan attached (to 2.04 Å) show differences in key regions related to mouse Fc γ receptor IV (mFcγRIV) binding.
29466327	1	0	gly	glycoproteins	183:195	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			N-glycosylation is a ubiquitous modification of eukaryotic secretory and membrane-bound proteins; about 90% of glycoproteins are N-glycosylated.
29466327	1	4	gly	N-glycosylated	201:214	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			N-glycosylation is a ubiquitous modification of eukaryotic secretory and membrane-bound proteins; about 90% of glycoproteins are N-glycosylated.
31608555	4	82	gly	protein	649:655	arg1	glucose	protein			glucose	Fterm		protein			This study reports crystal structures of an α-glycoside-binding protein (αGlyBP, ORF ID: TTHA0356 from Thermus thermophilus HB8) in complex with disaccharide α-glycosides namely trehalose (α-1,1), sucrose (α-1,2), maltose (α-1,4), palatinose (α-1,6) and glucose within a resolution range of 1.6-2.0 Å.
31669586	8	60	gly	disialylated	960:971	arg1	disialylated diantennary N-glycan				disialylated diantennary N-glycan						RESULTS The results showed an increase of monosialylated tri-antennary structure (A3G3S1) and disialylated diantennary N-glycan with antennary fucose (FA2G2S2).
31669586	8	100	gly	monosialylated	908:921	arg1	monosialylated tri-antennary structure				monosialylated tri-antennary structure						RESULTS The results showed an increase of monosialylated tri-antennary structure (A3G3S1) and disialylated diantennary N-glycan with antennary fucose (FA2G2S2).
29888865	1	20	gly	heterogeneity	177:189	arg1	recombinant proteins	recombinant proteins				Fterm		proteins			Essentials Glycosylation heterogeneity of recombinant proteins affects pharmacokinetics and immunogenicity.
30016589	8	74	gly	Asn162-glycan	1748:1760	arg1	the CD16a Asn162-glycan conformational heterogeneity			Asn162	the CD16a Asn162-glycan conformational heterogeneity					Asn162	Thus, antibody engineering to enhance intermolecular glycan-glycan contacts will likely provide limited improvement, and future designs should maximize the affinity by maintaining the CD16a Asn162-glycan conformational heterogeneity.
32110292	8	47	gly	N-glycopeptides	1557:1571	arg2	IgG3 and IgG4 intact N-glycopeptides			IgG3 and IgG4 intact N-glycopeptides						N-glycopeptides	This comprehensive glycosylation analysis strategy for the first time allows the discrimination of IgG3 and IgG4 intact N-glycopeptides with high similarity in sequence without the antibody-based pre-separation.
30557003	9	19	gly	fucosylation	1731:1742	arg1	Fifteen N-glycan compositions				Fifteen N-glycan compositions						Fifteen N-glycan compositions with bisecting GlcNAc, sialic acid, and core fucosylation showed significant differences in HCC serum.
29675740	6	9	gly	glycopeptides	1217:1229	arg2	glycopeptides			glycopeptides						glycopeptides	Therefore, in this study, glycopeptides were fractionated into four fractions by hydrophilic interaction chromatography, and each fraction was analyzed using the Glyco-RIDGE method.
30136532	10	6	gly	sialylated	1165:1174	arg1	sialylated glycans				sialylated glycans						In combination with the sialic acid derivatization, SiH-NPC presented a significant advantage in the analysis of sialylated glycans as well as isomeric oligosaccharides by liquid chromatography-mass spectrometry.
29769321	4	34	gly	N-glycosylated	758:771	arg1	an N-glycosylated neck-CRD fragment			an N-glycosylated neck-CRD fragment						fragment	Here, to investigate both mechanisms of IAV neutralization in greater detail, we produced an N-glycosylated neck-CRD fragment of porcine SP-D (RpNCRD) in HEK293 cells.
31084922	1	56	part_of	IgA1	134:137	arg1	BACKGROUND Glomerular deposition	IgA1		BACKGROUND Glomerular deposition		PUBTATOR	Site	IgA1	P01876	position	BACKGROUND Glomerular deposition of IgA1 is a common feature of Henoch-Schönlein purpura nephritis (HSPN) and is indistinguishable from that seen in IgA nephropathy (IgAN).
30959459	4	17	gly	residues	859:866	arg1	ST6Gal-I			cysteine residues	ST6Gal-I					cysteine residues	Mutagenesis of selected cysteine residues in ST6Gal-I mimicked these effects, and also rendered the enzyme inactive.
31501225	8	22	gly	glycopeptides	1279:1291	arg2	two glycopeptides			two glycopeptides						glycopeptides	In addition, the variation in the abundance of two glycopeptides was not caused by its protein concentration.
30144627	9	10	gly	glycosylation	1515:1527	arg2	6 glycosylation sites			6 glycosylation sites						sites	This may be due to its dramatic higher heterogeneity induced by its 6 glycosylation sites and a lack of ionization in the MS source.
30484241	3	0	gly	glycoproteins	531:543	arg1	synthetic glycoproteins	synthetic glycoproteins				Fterm		glycoproteins			In addition to these chemical syntheses, this chapter introduces a unique method for 15N-labeling of synthetic glycoproteins to enable structural analysis.
29936827	8	21	gly	O-glycopeptides	1327:1341	arg2	intact O-glycopeptides			intact O-glycopeptides						O-glycopeptides	For the first time, we can analyze intact O-glycopeptides generated by O-protease and enriched using a solid-phase platform.
30578591	5	43	gly	glycoproteins	906:918	arg1	functional glycoproteins	functional glycoproteins				Fterm		glycoproteins			The NA expressed in human cells has more complex glycans than that of insect cells, suggesting the importance of selecting an appropriate expression system for the production of functional glycoproteins.
29858715	0	43	gly	highly-fucosylated	110:127	arg1	highly-fucosylated glycan structures				highly-fucosylated glycan structures						Unusual N-type glycosylation of salivary prolactin-inducible protein (PIP): multiple LewisY epitopes generate highly-fucosylated glycan structures.
30302011	7	21	gly	epitope	1275:1281	arg1	the integrity				the integrity						These data provide detailed insight into the glycan shield's ability to compensate for the loss of a glycan, as well as the cascade of glycan movements on a protomer, starting at the point mutation, that affects the integrity of an antibody epitope located at the edge of the diminishing effect.
30063822	0	6	gly	Tag	13:15	arg1	Glycoproteins	Glycoproteins			Tag	Fterm		Glycoproteins			Paramagnetic Tag for Glycosylation Sites in Glycoproteins: Structural Constraints on Heparan Sulfate Binding to Robo1.
31246420	10	7	part_of	290.1	1902:1906	arg1	the m/z 290.1 fragment	290.1		the m/z 290.1 fragment		Cterm	Site	290.1		fragment	This approach was also effective for purchased Neu5Acα2-3Galβ1-4Glc and Neu5Acα2-6Galβ1-4Glc and for Neu5Acα2-3Galβ1-4GlcNAc and Neu5Acα2-6Galβ1-4GlcNAc linkage isomers with the Neu5Acα2-6 consistently requiring more energy for optimal generation of the m/z 290.1 fragment.
30427586	6	4	gly	N-glycopeptides	1201:1215	arg2	all N-glycopeptides			all N-glycopeptides						N-glycopeptides	It is shown for the first time that this fragmentation signature can consistently be found across all N-glycopeptides, but not on O-glycopeptides.
30427586	6	36	gly	O-glycopeptides	1229:1243	arg2	O-glycopeptides			O-glycopeptides						O-glycopeptides	It is shown for the first time that this fragmentation signature can consistently be found across all N-glycopeptides, but not on O-glycopeptides.
30259139	2	16	gly	glycoproteins	341:353	arg1	RF glycoproteins	RF glycoproteins				Fterm		glycoproteins			The present investigation was designed to further investigate the dynamic of the biosynthetic process of RF glycoproteins prior and after their release into the CSF, to identify the RF proteome and N-glycome and to clarify the mechanism of assembly of RF glycoproteins.
30259139	2	54	gly	glycoproteins	488:500	arg1	RF glycoproteins	RF glycoproteins				Fterm		glycoproteins			The present investigation was designed to further investigate the dynamic of the biosynthetic process of RF glycoproteins prior and after their release into the CSF, to identify the RF proteome and N-glycome and to clarify the mechanism of assembly of RF glycoproteins.
29760474	0	59	gly	regions	331:337	arg1	the biantennary complex-type N-linked glycans			regions	the biantennary complex-type N-linked glycans					regions	Structural basis for the recognition of complex-type N-glycans by Endoglycosidase S. Endoglycosidase S (EndoS) is a bacterial endo-β-N-acetylglucosaminidase that specifically catalyzes the hydrolysis of the β-1,4 linkage between the first two N-acetylglucosamine residues of the biantennary complex-type N-linked glycans of IgG Fc regions.
30959857	0	18	gly	Thunb.-Composition	47:64	arg1	Polysaccharide-Rich Fractions			position	Polysaccharide-Rich Fractions					position	Polysaccharide-Rich Fractions from Rosa rugosa Thunb.-Composition and Chemopreventive Potential.
31884067	10	22	gly	glycoproteins	1660:1672	arg1	carrier glycoproteins	carrier glycoproteins				Fterm		glycoproteins			CONCLUSIONS Loss of arginine methylation leads to an increase in HNK-1 glycan in the developing cerebellum but not in the cerebral cortex via upregulation of the biosynthetic enzyme and carrier glycoproteins.
29949660	1	76	part_of	lignin	215:220	arg1	altered lignin composition	lignin		altered lignin composition		Fterm	Site	lignin		position	A reduction in the lignin content in transgenic plants induces the ectopic expression of defense genes, but the importance of altered lignin composition in such phenomena remains unclear.
30152909	2	69	gly	glycoforms	589:598	arg1	GlcNAc2 Mann				GlcNAc2 Mann						METHODS RNase B solution was electrosprayed and its intact glycoforms of GlcNAc2 Mann (n = 5-9) with the highest abundance (charge state z = 16) were isolated individually and fragmented using CID, ETD, HCD, ETciD, and EThcD on the Orbitrap Fusion Lumos Tribrid mass spectrometer; the dissociation parameters were optimized for selective fragmentation of the N-glycan moiety and protein backbone as well as high sequence coverage.
30624066	6	53	part_of	galectin-3	1077:1086	arg1	a C-terminal domain fragment	galectin-3		a C-terminal domain fragment		PUBTATOR	Site	galectin-3	3958	fragment	Implementation of the approach is illustrated using the known interactions between a C-terminal domain fragment of human galectin-3 (hGal-3C) and three human serum GPs, α-1-acid glycoprotein (AGP), haptoglobin phenotype 1-1 (Hp1-1) and α-2-macroglobulin (α2M).
30014879	3	59	part_of	origin	445:450	arg1	chemical composition	origin		chemical composition		Fterm	Site	origin		position	Here we determined for the first time the chemical composition and structure of serotype 3 capsular polysaccharide (CPS), a major bacterial virulence factor and the antigen at the origin of S. suis classification into serotypes.
31094418	4	12	gly	found	829:833	arg1	all four potential N-glycosylation sites AND PC-modified glycans			all four potential N-glycosylation sites	PC-modified glycans					sites	In the present study, we now employ more advanced analytical tools-nano-flow liquid chromatography with high-definition electrospray mass spectrometry-to show that PC-modified glycans are found at all four potential N-glycosylation sites.
31094418	4	80	gly	N-glycosylation	857:871	arg2	all four potential N-glycosylation sites			all four potential N-glycosylation sites						sites	In the present study, we now employ more advanced analytical tools-nano-flow liquid chromatography with high-definition electrospray mass spectrometry-to show that PC-modified glycans are found at all four potential N-glycosylation sites.
29941589	2	23	gly	glycoprotein	238:249	arg1	the envelope glycoprotein complex	the envelope glycoprotein complex				Fterm		glycoprotein			Vaccine development has focused on the envelope glycoprotein complex (GPC) that extends from the virion envelope.
30451447	6	28	part_of	NSP	964:966	arg1	composition	NSP		composition		OGER	Site	NSP	Q9NQC3	position,	The results obtained by differentiating composition, viscosity and concentration of oats NSP in fermentation medium showed that Bacillus licheniformis pre-digests oat NSP, degrades high viscosity of oat β-glucan and makes hemicellulose easier to access for other bacteria.
30902814	10	82	part_of	receptor	1477:1484	arg1	a potential ligand receptor site	receptor		a potential ligand receptor site		Fterm	Site	receptor		site	In silico docking experiments with the recently published cryo-EM structure of the M41 IBV spike protein and our glycosylation results revealed a potential ligand receptor site that is ringed by four glycosylation sites that dramatically impact ligand binding.
30336974	4	46	part_of	glycoproteins	799:811	arg1	Ser/Thr	glycoproteins		Ser/Thr		Fterm	Site	glycoproteins		Ser/Thr	MTOG is initiated by the addition of N-acetyl-α-d-galactosamine (GalNAc) to Ser/Thr of glycoproteins.
31734359	4	84	part_of	position	1009:1016	arg1	the form	form of the SeH		position		PUBTATOR	Site	form of the SeH	2053	position	Structural investigations including FT-IR, Raman spectra and 1D, 2D NMR analysis revealed that selenium in CSe-tps1 replaced the hydroxyl group at the C-6 position in the polysaccharide with the form of selenyl ester, while most of the selenium in ASe-tps1 replaced the hydroxyl group at the C-1 and C-6 position in the form of the SeH bond on the branch of the polysaccharide.
31751705	0	10	gly	N-glycopeptide	78:91	arg2	multivalent N-glycopeptide units			multivalent N-glycopeptide units						N-glycopeptide	Synthesis and preliminary evaluation of neoglycopolymers carrying multivalent N-glycopeptide units.
30669833	0	91	gly	Multisialylated	18:32	arg1	Multisialylated LacdiNAc Structures				Multisialylated LacdiNAc Structures						Identification of Multisialylated LacdiNAc Structures as Highly Prostate Cancer Specific Glycan Signatures on PSA.
31411531	6	6	part_of	domain	1049:1054	arg1	human-derived IgG	IgG		domain		Cterm	Site	IgG		domain	When human-derived and CHO-expressed IgG1 were analyzed by HDX, sialic acid-containing glycans were found to destabilize the CH2 domain in CHO-expressed IgG, but not human-derived IgG.
31411531	6	6	part_of	domain	1049:1054	arg1	CHO-expressed IgG	CHO-expressed Ig		domain		Cterm	Site	CHO-expressed Ig		domain	When human-derived and CHO-expressed IgG1 were analyzed by HDX, sialic acid-containing glycans were found to destabilize the CH2 domain in CHO-expressed IgG, but not human-derived IgG.
31098625	6	79	gly	N-glycosylation	1084:1098	arg1	individual proteins	individual proteins				Fterm		proteins			Dynamic changes in the absolute abundances of milk proteins, as well as variation in site-specific N-glycosylation of individual proteins, were quantified.
30151520	4	51	gly	glycosylation	901:913	arg2	glycosylation site			glycosylation site						site	Groups of analytes which shared a common charge state, polypeptide sequence, and glycosylation site exhibited 50% precursor ion survival energies that varied only slightly as the size and composition of the oligosaccharide was varied.
30033944	6	56	gly	sialylated	849:858	arg1	branched sialylated N-glycans				branched sialylated N-glycans						However, the carrier proteins, interacting partners and localization of branched sialylated N-glycans remain unknown.
30389790	7	28	gly	glycoproteins	1455:1467	arg1	misfolded glycoproteins	misfolded glycoproteins				Fterm		glycoproteins			Further studies disclosed that the defects could not be ascribed to disruption of glycoprotein entrance into calnexin-folding cycles, inhibition of the oligosaccharyltransferase by transfer reaction products, or reduced proteasomal degradation of misfolded glycoproteins.
30389790	7	30	gly	glycoprotein	1280:1291	arg1	glycoprotein entrance	glycoprotein entrance				Fterm		glycoprotein			Further studies disclosed that the defects could not be ascribed to disruption of glycoprotein entrance into calnexin-folding cycles, inhibition of the oligosaccharyltransferase by transfer reaction products, or reduced proteasomal degradation of misfolded glycoproteins.
29632412	3	24	gly	glycosylation	739:751	arg2	traditional glycosylation site motifs			site motifs						site motifs	By analyzing the IgG glycome composition of 95 CC strains, we made several important observations: (i) glycome variation between mouse strains was higher than between individual humans, despite all mice having the same environmental influences; (ii) five genetic loci were found to be associated with murine IgG glycosylation; (iii) variants outside traditional glycosylation site motifs affected glycome variation; (iv) bisecting N-acetylglucosamine (GlcNAc) was produced by several strains although most previous studies have reported the absence of glycans containing the bisecting GlcNAc on murine IgGs; and (v) common laboratory mouse strains are not optimal animal models for studying effects of glycosylation on IgG function.
31437391	7	49	gly	fucosylated	1173:1183	arg1	fucosylated and bisecting GlcNAc structures				fucosylated and bisecting GlcNAc structures						Preliminary data suggest that fucosylated and bisecting GlcNAc structures were higher in abundances in females with AD, while both females and males exhibited lower abundances of high-mannose structures.
29231704	8	16	gly	glycosylation	1221:1233	arg2	eight different glycosylation sites			eight different glycosylation sites						sites	A total of 268 site-specific N-glycopeptides were detected, representing eight different glycosylation sites from two isomers of AGP.
29231704	8	52	gly	N-glycopeptides	1161:1175	arg2	268 site-specific N-glycopeptides			268 site-specific N-glycopeptides						N-glycopeptides	A total of 268 site-specific N-glycopeptides were detected, representing eight different glycosylation sites from two isomers of AGP.
31453603	3	49	gly	non-glycosylated	650:665	arg1	glycosylated and non-glycosylated peptides			glycosylated and non-glycosylated peptides						peptides	This capability has potential to greatly simplify glycoproteomic analyses, as glycosylated and non-glycosylated peptides can be rapidly partitioned in the gas phase.
31453603	3	52	gly	glycosylated	633:644	arg1	glycosylated and non-glycosylated peptides			glycosylated and non-glycosylated peptides						peptides	This capability has potential to greatly simplify glycoproteomic analyses, as glycosylated and non-glycosylated peptides can be rapidly partitioned in the gas phase.
30553446	2	51	part_of	IgA	267:269	arg1	Asymptomatic IgA deposition	IgA		Asymptomatic IgA deposition		PUBTATOR	Site	IgA	973	position	On the other hands, Asymptomatic IgA deposition (IgAD) is occasionally observed in donated kidney.
32110292	8	100	part_of	IgG3	1536:1539	arg1	IgG3 and IgG4 intact N-glycopeptides	IgG3		IgG3 and IgG4 intact N-glycopeptides		OGER	Site	IgG3	P01860	N-glycopeptides	This comprehensive glycosylation analysis strategy for the first time allows the discrimination of IgG3 and IgG4 intact N-glycopeptides with high similarity in sequence without the antibody-based pre-separation.
32110292	8	102	part_of	IgG4	1545:1548	arg1	IgG3 and IgG4 intact N-glycopeptides	IgG4		IgG3 and IgG4 intact N-glycopeptides		OGER	Site	IgG4	P01861	N-glycopeptides	This comprehensive glycosylation analysis strategy for the first time allows the discrimination of IgG3 and IgG4 intact N-glycopeptides with high similarity in sequence without the antibody-based pre-separation.
30003921	9	5	gly	glycosylated	1270:1281	arg1	diverse and structurally different glycosylated proteins	diverse and structurally different glycosylated proteins				Fterm		proteins			This study for the first time provides direct evidence that BinA is competent to bind diverse and structurally different glycosylated proteins.
29562594	3	77	gly	N-glycosylation	640:654	arg2	one N-glycosylation site			one N-glycosylation site						site	Fc-fused capillary morphogenesis protein 2 (CMG2-Fc) containing one N-glycosylation site on the Fc domain, produced in Nicotiana benthamiana whole plants, served as a model protein.
29775069	3	17	gly	glycoproteins	646:658	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			In this procedure, glycoproteins are incubated with 1-phenyl-3-methyl-5-pyrazolone (PMP) in aqueous ammonium hydroxide, making O-glycans released from protein backbones by β-elimination and N-glycans liberated by alkaline hydrolysis.
30813247	2	11	gly	glycoprotein	274:285	arg1	glycoprotein E	glycoprotein E				Fterm		glycoprotein E			This vaccine is based on glycoprotein E (gE) of varicella zoster virus (VZV), the most abundantly expressed protein of VZV, harboring sites for N- and O-linked glycosylation.
29992770	9	25	part_of	IgG1	1255:1258	arg1	N-glycopeptides	IgG4		N-glycopeptides		OGER	Site	IgG4	P01861	N-glycopeptides	N-glycopeptides of IgG1, IgG4, haptoglobin, and transferrin have statistically significant different abundances between cases and controls.
29992770	9	31	part_of	haptoglobin	1267:1277	arg1	N-glycopeptides	haptoglobin		N-glycopeptides		PUBTATOR	Site	haptoglobin	3240	N-glycopeptides	N-glycopeptides of IgG1, IgG4, haptoglobin, and transferrin have statistically significant different abundances between cases and controls.
29992770	9	57	part_of	IgG4	1261:1264	arg1	N-glycopeptides	haptoglobin		N-glycopeptides		PUBTATOR	Site	haptoglobin	3240	N-glycopeptides	N-glycopeptides of IgG1, IgG4, haptoglobin, and transferrin have statistically significant different abundances between cases and controls.
29992770	9	59	part_of	transferrin	1284:1294	arg1	N-glycopeptides	transferrin		N-glycopeptides		PUBTATOR	Site	transferrin	7018	N-glycopeptides	N-glycopeptides of IgG1, IgG4, haptoglobin, and transferrin have statistically significant different abundances between cases and controls.
30578591	4	2	gly	glycosylated	640:651	arg1	four potential N-linked glycosylation sites			four potential N-linked glycosylation sites						sites	The data indicate that three of four potential N-linked glycosylation sites are glycosylated, including one partial glycosylation site from both cell lines.
30578591	4	19	gly	glycosylation	616:628	arg2	four potential N-linked glycosylation sites			four potential N-linked glycosylation sites						sites	The data indicate that three of four potential N-linked glycosylation sites are glycosylated, including one partial glycosylation site from both cell lines.
30578591	4	50	gly	glycosylation	676:688	arg2	one partial glycosylation site			one partial glycosylation site						site	The data indicate that three of four potential N-linked glycosylation sites are glycosylated, including one partial glycosylation site from both cell lines.
30935958	17	72	gly	glycosylation	2227:2239	arg1	position 181			position 181						position 181	We hypothesize that glycosylation of position 181 is a key site for prion strain differentiation in vivo.
31411531	2	13	gly	sialylation	276:286	arg1	complex N-glycans				complex N-glycans						Although terminal sialylation on complex N-glycans can happen via either an alpha 2,3-linkage or an alpha 2,6-linkage, sialic acids on human serum IgG Fc are almost exclusively alpha 2,6-linked.
30063822	3	12	gly	glycoproteins	504:516	arg1	Recombinantly expressing glycoproteins	Recombinantly expressing glycoproteins				Fterm		glycoproteins			Recombinantly expressing glycoproteins in HEK293S (GnT1-) cells results in N-glycans with high-mannose structures that can be processed to leave a single GlcNAc residue.
29408166	2	116	gly	glycoproteins	382:394	arg1	individual glycoproteins	individual glycoproteins				Fterm		glycoproteins			However, individual glycoproteins, which might serve as potential cancer markers, often are very low-concentrated in complex serum matrices and distinct glycan structures are hard to detect by immunoassays.
29529546	1	0	gly	linked	144:149	arg1	glycoproteins AND saccharides	glycoproteins			saccharides	Fterm		glycoproteins			BACKGROUND Glycans are short chains of saccharides linked to glycoproteins that are known to be involved in a wide range of inflammatory processes.
29529546	1	70	gly	glycoproteins	154:166	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			BACKGROUND Glycans are short chains of saccharides linked to glycoproteins that are known to be involved in a wide range of inflammatory processes.
31350337	5	39	gly	glycoproteins	1159:1171	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			We demonstrate that the ogc cluster is conserved in the Burkholderia genus, and we confirm the production of glycoproteins with similar glycans in the Burkholderia species: B. thailandensis, B. gladioli, and B. pseudomallei Furthermore, we show that absence of protein O-glycosylation severely affects bacterial fitness and accelerates bacterial clearance in a Galleria mellonella larva infection model.
30622255	3	31	gly	fucosylated	437:447	arg1	long fucosylated HexNAc-based repeats				long fucosylated HexNAc-based repeats						We detect N-glycans of up to 7000 Da, which contain long fucosylated HexNAc-based repeats, as well as glucuronylated structures.
30539483	1	19	part_of	IgG	178:180	arg1	the fragment crystallizable	IgG		the fragment crystallizable		Cterm	Site	IgG		fragment	Engineering the fragment crystallizable (Fc) of human IgG can bring improved effector functions to monoclonal antibodies and Fc-fusion-based medicines and vaccines.
31754374	12	89	gly	N-glycosylation	1879:1893	arg2	N-glycosylation site			N-glycosylation site						site	The N-glycosylation site N5 is important for improved BxlB catalytic efficiency, but needs to be complemented by N1 and/or N7.
29773674	8	0	gly	glycosylated	1401:1412	arg1	densely glycosylated mucin-like regions			densely glycosylated mucin-like regions						regions	For neurocan and brevican, we identified densely glycosylated mucin-like regions in the extended domains.
30553311	9	81	part_of	contained	1123:1131	arg1	PHP AND uronic acid residue	PHP		uronic acid residue	total carbohydrates	OGER	Site	PHP	Q9DAK9	residue	Analysis of chemical characterization showed that PHP contained 75.36 ± 1.48% of total carbohydrates, 24.63 ± 1.69% of uronic acid residue and no proteins with monosaccharides such as rhamnose, arabinose, xylose, mannose, glucose, and galactose in a molar ratio of 10.25:9.38:1:12.45:9.9:11.55.
30353291	7	21	part_of	ESI	1009:1011	arg1	spray solvent composition	ESI		spray solvent composition		OGER	Site	ESI	P19957	position,	We also systematically examine the effects of ESI parameters, including spray solvent composition, auxiliary gas flow rate, sheath gas flow rate, sample infusion rate, sample concentration, and spray voltage, and discuss their effects on in-ESI HDX.
31244828	1	64	gly	glycoprotein	172:183	arg1	myelin oligodendrocytes glycoprotein	myelin oligodendrocytes glycoprotein				Fterm		glycoprotein			Autoantibodies to myelin oligodendrocytes glycoprotein (MOG) are found in a fraction of patients with inflammatory demyelination and are detected with MOG-transfected cells.
31611356	2	61	gly	glycosylation	332:344	arg2	N295			N295						N295	A key factor for Grft potency is glycosylation at N295 of gp120, which is directly adjacent to N332, a target glycan for an entire class of broadly neutralizing antibodies (bNAbs).
30503285	4	2	part_of	hormone	863:869	arg1	one engineered site	growth hormone		one engineered site		PUBTATOR	Site	growth hormone	2688	site	The effectiveness of this two-plasmid synthetic operon system has been tested on three proteins with therapeutic potential: the native and an engineered version of the naturally O-glycosylated human interferon α-2b, as well as human growth hormone with one engineered site of glycosylation.
30503285	4	3	part_of	α-2b	833:836	arg1	one engineered site	interferon α-2b		one engineered site		PUBTATOR	Site	interferon α-2b	3440	site	The effectiveness of this two-plasmid synthetic operon system has been tested on three proteins with therapeutic potential: the native and an engineered version of the naturally O-glycosylated human interferon α-2b, as well as human growth hormone with one engineered site of glycosylation.
31145522	0	86	gly	LacdiNAc-glycosylated	29:49	arg1	the LacdiNAc-glycosylated prostate-specific antigen				the LacdiNAc-glycosylated prostate-specific antigen						Clinical significance of the LacdiNAc-glycosylated prostate-specific antigen assay for prostate cancer detection.
30186849	1	14	gly	microheterogeneity	204:221	arg1	insufficient fragmentation	insufficient fragmentation				Fterm		fragmentation			Confident characterization of intact glycopeptides is a challenging task in mass spectrometry-based glycoproteomics due to microheterogeneity of glycosylation, complexity of glycans, and insufficient fragmentation of peptide bones.
30186849	1	17	gly	glycopeptides	118:130	arg2	intact glycopeptides			intact glycopeptides						glycopeptides	Confident characterization of intact glycopeptides is a challenging task in mass spectrometry-based glycoproteomics due to microheterogeneity of glycosylation, complexity of glycans, and insufficient fragmentation of peptide bones.
30186849	1	23	gly	glycosylation	226:238	arg1	glycans				glycans						Confident characterization of intact glycopeptides is a challenging task in mass spectrometry-based glycoproteomics due to microheterogeneity of glycosylation, complexity of glycans, and insufficient fragmentation of peptide bones.
30948514	7	54	gly	O-glycan	1364:1371	arg1	Ser			Ser	Ser		AminoAcid			Ser	Finally, the analysis of bovine OPSR by MS identified an O-glycan on Ser22, a residue that is semi-conserved (Ser or Thr) among vertebrate OPSR and OPSG.
30948514	7	54	gly	O-glycan	1364:1371	arg1	Thr			Thr	Thr		AminoAcid			Thr	Finally, the analysis of bovine OPSR by MS identified an O-glycan on Ser22, a residue that is semi-conserved (Ser or Thr) among vertebrate OPSR and OPSG.
30948514	7	54	gly	O-glycan	1364:1371	arg1	a residue			a residue	a residue		Site			residue	Finally, the analysis of bovine OPSR by MS identified an O-glycan on Ser22, a residue that is semi-conserved (Ser or Thr) among vertebrate OPSR and OPSG.
30948514	7	60	gly	semi-conserved	1401:1414	arg1	Ser22			Ser22						Ser22	Finally, the analysis of bovine OPSR by MS identified an O-glycan on Ser22, a residue that is semi-conserved (Ser or Thr) among vertebrate OPSR and OPSG.
30948514	7	60	gly	semi-conserved	1401:1414	arg1	Thr			Thr						Thr	Finally, the analysis of bovine OPSR by MS identified an O-glycan on Ser22, a residue that is semi-conserved (Ser or Thr) among vertebrate OPSR and OPSG.
30948514	7	60	gly	semi-conserved	1401:1414	arg1	Ser			Ser						Ser	Finally, the analysis of bovine OPSR by MS identified an O-glycan on Ser22, a residue that is semi-conserved (Ser or Thr) among vertebrate OPSR and OPSG.
30948514	7	60	gly	semi-conserved	1401:1414	arg1	a residue			a residue						residue	Finally, the analysis of bovine OPSR by MS identified an O-glycan on Ser22, a residue that is semi-conserved (Ser or Thr) among vertebrate OPSR and OPSG.
31738061	5	23	gly	glycosylation	859:871	arg1	a trisaccharide lactone donor				a trisaccharide lactone donor						The successful strategy relies on both chemical glycosylation of a trisaccharide lactone donor for the introduction of sulfated HNK-1 branch and substrate promiscuities of bacterial glycosyltransferases that can tolerate sulfated substrates for enzymatic diversification.
31541622	3	50	gly	glycoproteins	489:501	arg1	many cases glycoproteins	many cases glycoproteins				Fterm		glycoproteins			During the initial stage of viral replication, viruses interact with cell membrane receptors, which are in many cases glycoproteins.
31754374	0	42	gly	N-glycosylation	12:26	arg2	N-glycosylation sites			N-glycosylation sites						sites	Redesigning N-glycosylation sites in a GH3 β-xylosidase improves the enzymatic efficiency.
30908021	4	11	gly	glycopeptide	945:956	arg2	de novo glycopeptide sequencing			de novo glycopeptide sequencing						glycopeptide	With the aid of database for data mining, 1380 unique N-glycopeptides were identified and manually validated by de novo glycopeptide sequencing, of which 514 were sulfated at the site-specific locations.
30908021	4	85	gly	N-glycopeptides	879:893	arg2	1380 unique N-glycopeptides			1380 unique N-glycopeptides						N-glycopeptides	With the aid of database for data mining, 1380 unique N-glycopeptides were identified and manually validated by de novo glycopeptide sequencing, of which 514 were sulfated at the site-specific locations.
31062865	5	56	part_of	EPO	1199:1201	arg1	the EPO region	EPO		the EPO region		PUBTATOR	Site	EPO	P01588	region	Using intact glycopeptide characterization, the EPO-Fc was observed to maintain their individual EPO and Fc N-glycan characteristics in which the EPO region presented bi-, tri-, and tetra-branched N-glycan structures, while the Fc N-glycan displayed mostly biantennary glycans.
31289257	7	59	gly	glycoprotein	1243:1254	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			This is the first study to described MAP6 as a glycoprotein containing Gal-(β-1,3)-GalNAc oligosaccharides and to show that hyperglycosylation of MAP6 is strongly associated with the pathogenesis of PD.
29532326	9	12	part_of	detected	1232:1239	arg1	C8 AND two more N-glycosylation sites	C8		two more N-glycosylation sites		PUBTATOR	Site	C8	3224	sites	In addition to the known N-glycosylation sites, two more N-glycosylation sites were detected on C8.
29370305	12	15	part_of	Env	1955:1957	arg1	The HIV-1 Env SP sequences	HIV-1 Env		The HIV-1 Env SP sequences		PUBTATOR	Site	HIV-1 Env	100616444	sequences	The HIV-1 Env SP sequences thus may be under selective pressure to balance virus infectiousness with virus resistance to the host antibody responses.
29370305	12	67	part_of	HIV-1	1949:1953	arg1	The HIV-1 Env SP sequences	HIV-1 Env		The HIV-1 Env SP sequences		PUBTATOR	Site	HIV-1 Env	100616444	sequences	The HIV-1 Env SP sequences thus may be under selective pressure to balance virus infectiousness with virus resistance to the host antibody responses.
29370305	8	45	part_of	Env	1403:1405	arg1	the Env V1V2 region	Env		the Env V1V2 region		PUBTATOR	Site	Env	100616444	region	Mutations at positions 8, 12, and 15 also rendered the virus more resistant to neutralization by monoclonal antibodies against the Env V1V2 region.
31809011	7	28	gly	proteins	1014:1021	arg1	the glycan type profile	proteins			the glycan type profile	Fterm		proteins			Then we applied the method to analyze the glycan type profile of proteins from the breast cancer cell line MCF7, and we quantitatively revealed the N-glycan type microheterogeneity at the glycopeptide and glycoprotein level.
31809011	7	31	gly	glycoprotein	1154:1165	arg1	the glycopeptide and glycoprotein level	the glycopeptide and glycoprotein level				Fterm		glycoprotein			Then we applied the method to analyze the glycan type profile of proteins from the breast cancer cell line MCF7, and we quantitatively revealed the N-glycan type microheterogeneity at the glycopeptide and glycoprotein level.
31809011	7	79	gly	glycopeptide	1137:1148	arg2	the glycopeptide and glycoprotein level			the glycopeptide and glycoprotein level						glycopeptide	Then we applied the method to analyze the glycan type profile of proteins from the breast cancer cell line MCF7, and we quantitatively revealed the N-glycan type microheterogeneity at the glycopeptide and glycoprotein level.
30737276	8	4	gly	region	1490:1495	arg1	the l-fucose				the l-fucose						The a075l gene encodes a β-xylosyltransferase that attaches the distal d-xylose (Xyl) unit to the l-fucose (Fuc) that is part of the conserved N-glycan core region.
30578646	3	62	gly	enzyme	461:466	arg1	the sialylation pathway	enzyme			the sialylation pathway	Fterm		enzyme			Here, we report that CRISPR/Cas9-mediated knock out of the CMAS gene, encoding a key enzyme in the sialylation pathway, in the mouse colorectal cancer MC38 cell line completely abrogated cell surface expression of sialic acids (MC38-Sianull ) and, unexpectedly, significantly increased in vivo tumor growth compared to the control MC38-MOCK cells.
30294837	3	49	gly	has	476:478	arg1	The enzyme 6-O-α-rhamnosyl-β-glucosidase AND the capacity to transfer the rutinosyl moiety (6-O-α-l-rhamnopyranosyl-β-d-glucopyranose) from 7-O-rutinosylated flavonoids to hydroxylated organic compounds	The enzyme 6-O-α-rhamnosyl-β-glucosidase			the capacity to transfer the rutinosyl moiety (6-O-α-l-rhamnopyranosyl-β-d-glucopyranose) from 7-O-rutinosylated flavonoids to hydroxylated organic compounds	Fterm		6-O-α-rhamnosyl-β-glucosidase			The enzyme 6-O-α-rhamnosyl-β-glucosidase (EC 3.2.1.168) has the capacity to transfer the rutinosyl moiety (6-O-α-l-rhamnopyranosyl-β-d-glucopyranose) from 7-O-rutinosylated flavonoids to hydroxylated organic compounds.
29475941	9	19	gly	glycans	1386:1392	arg1	these enzymes	enzymes			glycans	Fterm		enzymes			Therefore, we expressed two lysosomal enzymes, α-galactosidase-A and lysosomal acid lipase, in the triple KO cells and found that the glycans on these enzymes were sensitive to endoglycosidase H treatment.
30403372	1	51	gly	glycoprotein	254:265	arg1	envelope glycoprotein	envelope glycoprotein				Fterm		glycoprotein			VRC01 broadly neutralizing antibodies (bnAbs) target the CD4-binding site (CD4BS) of the human immunodeficiency virus-1 (HIV-1) envelope glycoprotein (Env).
29475941	11	21	gly	enzymes	1748:1754	arg1	high-mannose-type N-glycans	enzymes			high-mannose-type N-glycans	Fterm		enzymes			Our results indicate that the triple KO HEK293 cells are suitable for producing recombinant proteins, including lysosomal enzymes with high-mannose-type N-glycans.
30513349	9	56	gly	glycoproteins	1636:1648	arg1	fully humanized N-glycan profiles	glycoproteins			fully humanized N-glycan profiles	Fterm		glycoproteins			The work presented here shows the potential of expanding the glyco-engineering toolbox for CHO cells to produce a wider variety of glycoproteins with fully humanized N-glycan profiles.
31301102	2	35	gly	structures	272:281	arg1	the antibody Fc region			the antibody Fc region	the antibody Fc region		Site			region	Glycan structures in the antibody Fc region influence binding properties to Fc receptors, which opens opportunities for modulation of antibody effector functions.
31332757	4	24	gly	glycosites	647:656	arg2	Fc glycosites			Fc glycosites						glycosites	First, an azido-tagged unnatural N-glycan substrate is transferred onto Fc glycosites of a therapeutic antibody through Endo-S-catalyzed glycoremodeling, followed by click reaction with an alkyne-tagged payload drug to give a well-defined gsADC.
31111416	2	11	part_of	Env	377:379	arg1	the primary sequence	Env		the primary sequence		PUBTATOR	Site	Env	100616444	sequence	A comprehensive LC-MS/MS peptide mapping analysis was applied to assess the primary sequence, glycosylation profiles, and glycosite occupancy of Env to ensure the adequate mimicking of the native immunogen.
31411531	7	12	gly	sialylated	1132:1141	arg1	sialylated glycans				sialylated glycans						When structural isomers of sialylated glycans were chromatographically resolved and identified in the limited proteolysis experiment, we found that only alpha 2,3-linked sialic acid on the 6-arm (the major sialylated glycans in CHO-expressed IgG1) destabilizes the CH2 domain, presumably because of the steric effect that decreases the glycan-CH2 domain interaction.
31411531	7	24	gly	sialylated	1311:1320	arg1	the major sialylated glycans				the major sialylated glycans						When structural isomers of sialylated glycans were chromatographically resolved and identified in the limited proteolysis experiment, we found that only alpha 2,3-linked sialic acid on the 6-arm (the major sialylated glycans in CHO-expressed IgG1) destabilizes the CH2 domain, presumably because of the steric effect that decreases the glycan-CH2 domain interaction.
31411531	7	60	gly	domain	1452:1457	arg1	the glycan-CH2 domain interaction				the glycan-CH2 domain interaction						When structural isomers of sialylated glycans were chromatographically resolved and identified in the limited proteolysis experiment, we found that only alpha 2,3-linked sialic acid on the 6-arm (the major sialylated glycans in CHO-expressed IgG1) destabilizes the CH2 domain, presumably because of the steric effect that decreases the glycan-CH2 domain interaction.
31364262	6	78	gly	sialylated	1219:1228	arg1	complex neutral, bisecting, and sialylated N-glycan families				complex neutral, bisecting, and sialylated N-glycan families						The spatial distribution of oligomannose, complex neutral, bisecting, and sialylated N-glycan families are localized to the tumor regions of late-stage ovarian cancer patients relative to early-stage patients.
30902814	0	96	gly	Glycosylation	0:12	arg1	the viral attachment protein	the viral attachment protein				Fterm		protein			Glycosylation of the viral attachment protein of avian coronavirus is essential for host cell and receptor binding.
29671439	2	5	gly	glycoproteins	273:285	arg1	then the crude glycoproteins	then the crude glycoproteins				Fterm		glycoproteins			The activity is monitored via HPLC, and then the crude glycoproteins are enriched with lectin microarrays and magnetic microspheres.
31611356	2	28	part_of	N295	349:352	arg1	A key factor	factor		N295		Fterm	SpecificSite	factor		N295	A key factor for Grft potency is glycosylation at N295 of gp120, which is directly adjacent to N332, a target glycan for an entire class of broadly neutralizing antibodies (bNAbs).
30307368	0	37	part_of	MICA	65:68	arg1	MICA epitope	MICA		MICA epitope		PUBTATOR	Site	MICA	100507436	epitope	High-resolution glycosylation site-engineering method identifies MICA epitope critical for shedding inhibition activity of anti-MICA antibodies.
30848132	5	35	gly	sialylated	794:803	arg1	core-5-type and sialylated O-glycans				core-5-type and sialylated O-glycans						In total, 56 glycans were identified on Arctic charr intestinal mucins, with a high prevalence of core-5-type and sialylated O-glycans.
31809011	8	1	gly	glycoproteins	1356:1368	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			The novel quantitative strategy to evaluate the relative intensity of the six states of N-glycan type glycosylation on each site provides a new avenue to investigate the function of glycoproteins in broad areas, such as cancer biomarker research, pharmaceuticals characterization, and antiglycan vaccine development.
31759178	7	9	gly	N-glycopeptide	1886:1899	arg2	intact N-glycopeptide search engine			intact N-glycopeptide search engine						N-glycopeptide	SIGNIFICANCE: Differential N-glycosylation in breast MCF-7 cancer cells (relative to MCF-10A epithelial cells) were qualitatively and quantitatively characterized with site- and structure-specific N-glycoproteomics using RPLC-nanoESI-MS/MS (HCD with stepped NCEs) and intact N-glycopeptide search engine GPSeeker.
31325506	1	60	gly	heavily-glycosylated	150:169	arg1	a heavily-glycosylated macromolecular (approximately 4 MDa) protein	a heavily-glycosylated macromolecular (approximately 4 MDa) protein				Fterm		protein			Bovine submaxillary mucin (BSM) is a heavily-glycosylated macromolecular (approximately 4 MDa) protein and is used in various biomaterial applications in light of its high viscosity and biocompatibility, in addition to use as a biochemical substrate or inhibitor as a result of its abundant O-glycans.
31256376	6	70	gly	proteins	822:829	arg1	the common N-linked carbohydrates	proteins			the common N-linked carbohydrates	Fterm		proteins			In addition, an enzyme, peptide N-glycosidase F (PNGase F), removes most of the common N-linked carbohydrates unaltered from proteins while hydrolyzing the originally glycosylated Asn residue to Asp.
31256376	6	76	gly	glycosylated	864:875	arg1	the originally glycosylated Asn residue			the originally glycosylated Asn residue						Asn residue	In addition, an enzyme, peptide N-glycosidase F (PNGase F), removes most of the common N-linked carbohydrates unaltered from proteins while hydrolyzing the originally glycosylated Asn residue to Asp.
30016589	2	65	gly	carbohydrate	367:378	arg1	the IgG1 crystallizable fragment			the IgG1 crystallizable fragment	the IgG1 crystallizable fragment		Site			fragment	Core fucosylation, a prevalent modification to the asparagine (N)-linked carbohydrate on the IgG1 crystallizable fragment (Fc), decreases the Fc γ receptor IIIa (CD16a) binding affinity and mAb efficacy.
29727657	1	16	part_of	C	185:185	arg1	The recombinant C-terminal domain	chitinase C		The recombinant C-terminal domain		Cterm	Site	chitinase C		domain	The recombinant C-terminal domain of chitinase C of Chitinophaga pinensis (CpChiC-GH18C) exhibits the highest activity at pH 6.0 and 35 °C, with a Km of 76.13 (mg-1 ml), a kcat of 10.16 (s-1), and a kcat/Km of 0.133 (mg-1 ml s-1) on colloidal chitin.
30459171	4	10	gly	glycosylation	661:673	arg2	O-linked glycosylation sites			O-linked glycosylation sites						sites	This large-scale localization of O-linked glycosylation sites demonstrated that EXoO is an effective method for defining the site-specific O-linked glycoproteome in different types of sample.
30898876	0	50	gly	glycoproteins	28:40	arg1	mammalian glycoproteins	mammalian glycoproteins				Fterm		glycoproteins			Identification of mammalian glycoproteins with type-I LacdiNAc structures synthesized by the glycosyltransferase B3GALNT2.
29441788	5	9	part_of	afamin	695:700	arg1	all N-glycosylation sites	afamin		all N-glycosylation sites		PUBTATOR	Site	afamin	173	sites	Fully nonglycosylated rhAFM was obtained by transfection of point-mutated cDNA to delete all N-glycosylation sites of afamin.
31905645	13	69	part_of	MCC	1880:1882	arg1	MCC composites	MCC		MCC composites		OGER	Site	MCC		composites	MCC chemical modification induced the enhancement of the thermal stability of MCC composites.
29304471	2	0	gly	glycosylation	285:297	arg2	the single N-linked glycosylation site			the single N-linked glycosylation site						site	Compared to dengue virus (DENV), the loop containing the single N-linked glycosylation site on Zika virus (ZIKV) envelope (E) proteins extends further towards the DII fusion loop (DII-FL) on neighboring E proteins within E dimers on mature viruses.
31838284	1	28	gly	glycoproteins	122:134	arg1	therapeutic glycoproteins	therapeutic glycoproteins				Fterm		glycoproteins			Erythropoiesis stimulating agents (ESAs) are a group of therapeutic glycoproteins used to treat anaemia caused by chronic kidney disease or chemotherapy.
30990348	6	49	gly	residue	1353:1359	arg1	the Man α1-6 arm			the Man α1-6 arm	the Man α1-6 arm						Hydrogen-deuterium exchange/mass spectrometry analysis of dynamic structures of mAbs revealed the greater involvement of the terminal Gal residue on the Man α1-6 arm in the structural stability of the CH2 domain.
29110612	0	67	part_of	Composition	22:32	arg1	Melatonin Release	Release		Composition		Fterm	Site	Release		position	Influence of Implants Composition on Melatonin Release from Ethylcellulose Matrix.
31244828	10	42	part_of	MOG	1468:1470	arg1	the extracellular domain	MOG		the extracellular domain		PUBTATOR	Site	MOG	4340	domain	The folding of the extracellular domain of MOG with the formation of beta-sheets did not depend on its glycosylation as seen by circular dichroism.
30612270	7	5	gly	sialylated	1221:1230	arg1	highly sialylated compositions			highly sialylated compositions						positions	In most cases, highly sialylated compositions showed an increased relative abundance with increasing peptide length.
31108197	8	19	gly	sialylated	1641:1650	arg1	all sialylated N-linked glycans				all sialylated N-linked glycans						Interestingly, O-linked glycans from mature tissue contained both N-acetylneuraminic acid (Neu5Ac) and N-glycolylneuraminic acid (Neu5Gc), while all sialylated N-linked glycans detected contained only Neu5Ac.
29730764	9	46	gly	glycopeptides	1650:1662	arg2	O-linked glycopeptides			O-linked glycopeptides						glycopeptides	The limited overlap of results delivered by the two search engines draws attention to the fact that automated data interpretation of O-linked glycopeptides is not even close to being solved.
29444271	2	30	gly	epitope	630:636	arg1	Lea epitope(s)				Lea epitope(s)						In this study, we have characterized another tomato gene (Solyc11g069010) encoding α1, 3/4-fucosidase (α-Fuc'ase Sl-2), which is also active toward the complex type N-glycans containing Lea epitope(s).
30983324	8	9	gly	glycoproteins	1611:1623	arg1	therapeutic glycoproteins	therapeutic glycoproteins				Fterm		glycoproteins			These results suggest that stepwise PGC-SPE and LC/MS/MS pairwise assays can be used as an efficient tool to detect glycosylation changes of therapeutic glycoproteins including abundant acidic species in biologics or biosimilar development.
31393126	10	40	part_of	glycoproteins	1565:1577	arg1	each single glycosylation site	glycoproteins		each single glycosylation site		Fterm	Site	glycoproteins		site	The diversity of N-glycans attached to each single glycosylation site of these glycoproteins confirmed that MRJP1 and MRJP2 heterogeneity was mostly associated with their glycoform populations.
31558607	9	63	gly	glycoforms	1666:1675	arg1	these protein glycoforms	these protein glycoforms				Fterm		protein			Our results open new opportunities for functional studies of these protein glycoforms in different cells and tissues.
31548313	0	36	gly	core-fucosylated	46:61	arg1	core-fucosylated N-glycans				core-fucosylated N-glycans						Structural basis for the specific cleavage of core-fucosylated N-glycans by endo-β-N-acetylglucosaminidase from the fungus Cordyceps militaris.
29921663	5	61	part_of	IgG	1008:1010	arg1	tryptic IgG glycopeptides	IgG		tryptic IgG glycopeptides		Cterm	Site	IgG		glycopeptides	Because of this, the differences in IgG Fc glycosylation between 60 pediatric meningococcal sepsis patients admitted to the pediatric intensive care unit and 46 age-matched healthy controls were investigated, employing liquid chromatography with mass spectrometric detection of tryptic IgG glycopeptides.
30576150	8	0	gly	mannosylated	1479:1490	arg1	GlcNAc2-Man6				GlcNAc2-Man6						The relative abundances of fucosylated PNO3 (GlcNAc4-Man3-Fuc) and sialylated PNO18 (GlcNAc4-Man3-Gal2-NeuAc) increased during lactation, and Meishan sows demonstrated a higher ( P < 0.05) abundance of mannosylated PNO10 (GlcNAc2-Man6) and sialylated PNO17 (GlcNAc5-Man3-Gal-NeuAc) than Yorkshire sows.
30576150	8	9	gly	sialylated	1517:1526	arg1	GlcNAc5-Man3-Gal-NeuAc				GlcNAc5-Man3-Gal-NeuAc						The relative abundances of fucosylated PNO3 (GlcNAc4-Man3-Fuc) and sialylated PNO18 (GlcNAc4-Man3-Gal2-NeuAc) increased during lactation, and Meishan sows demonstrated a higher ( P < 0.05) abundance of mannosylated PNO10 (GlcNAc2-Man6) and sialylated PNO17 (GlcNAc5-Man3-Gal-NeuAc) than Yorkshire sows.
30576150	8	65	gly	fucosylated	1304:1314	arg1	GlcNAc4-Man3-Fuc				GlcNAc4-Man3-Fuc						The relative abundances of fucosylated PNO3 (GlcNAc4-Man3-Fuc) and sialylated PNO18 (GlcNAc4-Man3-Gal2-NeuAc) increased during lactation, and Meishan sows demonstrated a higher ( P < 0.05) abundance of mannosylated PNO10 (GlcNAc2-Man6) and sialylated PNO17 (GlcNAc5-Man3-Gal-NeuAc) than Yorkshire sows.
30576150	8	75	gly	sialylated	1344:1353	arg1	GlcNAc4-Man3-Gal2-NeuAc				GlcNAc4-Man3-Gal2-NeuAc						The relative abundances of fucosylated PNO3 (GlcNAc4-Man3-Fuc) and sialylated PNO18 (GlcNAc4-Man3-Gal2-NeuAc) increased during lactation, and Meishan sows demonstrated a higher ( P < 0.05) abundance of mannosylated PNO10 (GlcNAc2-Man6) and sialylated PNO17 (GlcNAc5-Man3-Gal-NeuAc) than Yorkshire sows.
30063822	5	1	gly	N-glycosylation	953:967	arg2	a single N-glycosylation site			a single N-glycosylation site						site	To illustrate the procedure, we have made an application to a two-domain construct of Robo1, a protein that carries a single N-glycosylation site in its N-terminal domains.
31174130	3	33	gly	N-glycopeptides	588:602	arg2	IgG N-glycopeptides			IgG N-glycopeptides						N-glycopeptides	The glycopeptide enrichment efficacy of the titania-based sol-gel material was evaluated by the enrichment of IgG N-glycopeptides from their proteolytic products.
31174130	3	59	gly	glycopeptide	478:489	arg2	glycopeptide			glycopeptide						glycopeptide	The glycopeptide enrichment efficacy of the titania-based sol-gel material was evaluated by the enrichment of IgG N-glycopeptides from their proteolytic products.
30578591	6	7	part_of	NA	992:993	arg1	different glycosites	NA		different glycosites		Cterm	Site	NA	4758	glycosites	Different types of glycans are identified from different glycosites of NA expressed in human cells, which implies the site-dependence of glycosylation on NA.
30578591	6	27	part_of	site-dependence	1039:1053	arg1	NA	NA		site-dependence		Cterm	Site	NA	4758	site-dependence	Different types of glycans are identified from different glycosites of NA expressed in human cells, which implies the site-dependence of glycosylation on NA.
31247951	6	4	gly	fucosylated	1083:1093	arg1	core fucosylated structures				core fucosylated structures						We report protein-specific N-glycosylation patterns, including a correlation of core fucosylated structures with immunoglobulin G (IgG) levels, and of trisialylated, trigalactosylated, and triantennary structures with heparin cofactor 2 (SERPIND2).
31247951	6	64	gly	trisialylated	1149:1161	arg1	trisialylated, trigalactosylated, and triantennary structures				trisialylated, trigalactosylated, and triantennary structures						We report protein-specific N-glycosylation patterns, including a correlation of core fucosylated structures with immunoglobulin G (IgG) levels, and of trisialylated, trigalactosylated, and triantennary structures with heparin cofactor 2 (SERPIND2).
31557542	6	72	part_of	CMP	911:913	arg1	CMP binding site	CMP		CMP binding site		OGER	Site	CMP	P21941	site	Herein, we investigated the structure, glycosylation and CMP binding site of human ST3GAL family using computational methods.
29941589	4	51	gly	glycosylation	641:653	arg2	the N-linked glycosylation sites			the N-linked glycosylation sites						sites	Here, using a virus-like-particle system that presents Lassa virus GPC in a native-like context, we determine the composite population of each of the N-linked glycosylation sites presented on the trimeric GPC spike.
29231704	10	5	gly	N-glycopeptides	1459:1473	arg2	∼35% more N-glycopeptides			∼35% more N-glycopeptides						N-glycopeptides	Reversed-phase UHPLC coupled with CZE generated ∼35% more N-glycopeptides than direct reversed-phase UHPLC-ESI-MS/MS analysis and ∼70% more N-glycopeptides than direct CZE-ESI-MS/MS analysis.
29231704	10	13	gly	N-glycopeptides	1541:1555	arg2	∼70% more N-glycopeptides			∼70% more N-glycopeptides						N-glycopeptides	Reversed-phase UHPLC coupled with CZE generated ∼35% more N-glycopeptides than direct reversed-phase UHPLC-ESI-MS/MS analysis and ∼70% more N-glycopeptides than direct CZE-ESI-MS/MS analysis.
29703890	7	2	gly	glycopeptides	1086:1098	arg2	low-abundance glycopeptides			low-abundance glycopeptides						glycopeptides	This robust and simple method is highly effective for sensitive glycoproteomics analysis, especially capturing low-abundance glycopeptides.
31256374	1	3	part_of	glycoprotein	161:172	arg1	a single glycosylation site	glycoprotein		a single glycosylation site		Fterm	Site	glycoprotein		site	Most glycoproteins carry a very heterogeneous mixture of oligosaccharides and even a single glycosylation site of a pure glycoprotein is often heterogeneously glycosylated.
31776333	1	25	gly	Glycosylation	88:100	arg1	proteins	proteins				Fterm		proteins			Glycosylation of proteins profoundly impacts their physical and biological properties.
31393126	2	90	gly	glycoproteins	440:452	arg1	these glycoproteins	these glycoproteins				Fterm		glycoproteins			Although there have been analyses on the glycosylation modification of RJ proteins, none of these methods have been conducted on a site-specific analysis of glycosylation from these glycoproteins.
31040271	4	22	gly	enzymes	718:724	arg1	N-glycans	enzymes			N-glycans	Fterm		enzymes			Here we present a comprehensive gene engineering screen in Chinese hamster ovary cells that enables production of lysosomal enzymes with N-glycans custom designed to affect key glycan features guiding cellular uptake and circulation.
30528732	6	23	gly	domain	1139:1144	arg1	the mannosylation				the mannosylation						In this work, with extensive mass spectrometric investigations on CBHI from two T. reesei strains grown under three conditions, several new discoveries were made: 1) N45 and N64 are N-glycosylated with high mannose type glycans; 2) the catalytic domain of CBHI is extensively O-glycosylated with hexoses and N-acetylhexosamines; 3) experimental evidence on the mannosylation of carbohydrate binding domain (other than the linker adjacent region) was found.
30528732	6	38	gly	O-glycosylated	1016:1029	arg1	the catalytic domain			the catalytic domain						domain	In this work, with extensive mass spectrometric investigations on CBHI from two T. reesei strains grown under three conditions, several new discoveries were made: 1) N45 and N64 are N-glycosylated with high mannose type glycans; 2) the catalytic domain of CBHI is extensively O-glycosylated with hexoses and N-acetylhexosamines; 3) experimental evidence on the mannosylation of carbohydrate binding domain (other than the linker adjacent region) was found.
30528732	6	48	gly	made	897:900	arg1	the catalytic domain			the catalytic domain						domain	In this work, with extensive mass spectrometric investigations on CBHI from two T. reesei strains grown under three conditions, several new discoveries were made: 1) N45 and N64 are N-glycosylated with high mannose type glycans; 2) the catalytic domain of CBHI is extensively O-glycosylated with hexoses and N-acetylhexosamines; 3) experimental evidence on the mannosylation of carbohydrate binding domain (other than the linker adjacent region) was found.
30528732	6	71	gly	mannosylation	1101:1113	arg1	carbohydrate binding domain			carbohydrate binding domain							In this work, with extensive mass spectrometric investigations on CBHI from two T. reesei strains grown under three conditions, several new discoveries were made: 1) N45 and N64 are N-glycosylated with high mannose type glycans; 2) the catalytic domain of CBHI is extensively O-glycosylated with hexoses and N-acetylhexosamines; 3) experimental evidence on the mannosylation of carbohydrate binding domain (other than the linker adjacent region) was found.
30528732	6	11	gly	N-glycosylated	922:935	arg1	N45			N45 and N64						N45 and N64	In this work, with extensive mass spectrometric investigations on CBHI from two T. reesei strains grown under three conditions, several new discoveries were made: 1) N45 and N64 are N-glycosylated with high mannose type glycans; 2) the catalytic domain of CBHI is extensively O-glycosylated with hexoses and N-acetylhexosamines; 3) experimental evidence on the mannosylation of carbohydrate binding domain (other than the linker adjacent region) was found.
29411222	7	12	gly	sialylated	1236:1245	arg1	TNFR-specific highly sialylated glycans				TNFR-specific highly sialylated glycans						N-Glycopeptide analysis with UHPLC-QTOF-MSE confirmed the N-glycosylation sites (N149, N171 and N317) as well as Fc-specific glycosylation on N317, and TNFR-specific highly sialylated glycans on N149 and N171 on both investigated products.
29411222	7	58	gly	N-glycosylation	1121:1135	arg2	the N-glycosylation sites			the N-glycosylation sites						sites	N-Glycopeptide analysis with UHPLC-QTOF-MSE confirmed the N-glycosylation sites (N149, N171 and N317) as well as Fc-specific glycosylation on N317, and TNFR-specific highly sialylated glycans on N149 and N171 on both investigated products.
29411222	7	45	gly	sites	1137:1141	arg1	TNFR-specific highly sialylated glycans			sites	TNFR-specific highly sialylated glycans					sites	N-Glycopeptide analysis with UHPLC-QTOF-MSE confirmed the N-glycosylation sites (N149, N171 and N317) as well as Fc-specific glycosylation on N317, and TNFR-specific highly sialylated glycans on N149 and N171 on both investigated products.
29411222	7	20	gly	sites	1137:1141	arg1	N171			N149, N171 and N317						N149, N171 and N317	N-Glycopeptide analysis with UHPLC-QTOF-MSE confirmed the N-glycosylation sites (N149, N171 and N317) as well as Fc-specific glycosylation on N317, and TNFR-specific highly sialylated glycans on N149 and N171 on both investigated products.
29411222	7	44	gly	glycosylation	1188:1200	arg1	N317			N317						N317	N-Glycopeptide analysis with UHPLC-QTOF-MSE confirmed the N-glycosylation sites (N149, N171 and N317) as well as Fc-specific glycosylation on N317, and TNFR-specific highly sialylated glycans on N149 and N171 on both investigated products.
29411222	7	44	gly	glycosylation	1188:1200	arg1	TNFR-specific highly sialylated glycans			N317	TNFR-specific highly sialylated glycans					N317	N-Glycopeptide analysis with UHPLC-QTOF-MSE confirmed the N-glycosylation sites (N149, N171 and N317) as well as Fc-specific glycosylation on N317, and TNFR-specific highly sialylated glycans on N149 and N171 on both investigated products.
29411222	7	44	gly	glycosylation	1188:1200	arg1	TNFR-specific highly sialylated glycans			N317	TNFR-specific highly sialylated glycans					N317	N-Glycopeptide analysis with UHPLC-QTOF-MSE confirmed the N-glycosylation sites (N149, N171 and N317) as well as Fc-specific glycosylation on N317, and TNFR-specific highly sialylated glycans on N149 and N171 on both investigated products.
29411222	7	58	gly	N-glycosylation	1121:1135	arg2	N317			N149, N171 and N317						N149, N171 and N317	N-Glycopeptide analysis with UHPLC-QTOF-MSE confirmed the N-glycosylation sites (N149, N171 and N317) as well as Fc-specific glycosylation on N317, and TNFR-specific highly sialylated glycans on N149 and N171 on both investigated products.
32110292	3	91	part_of	region	649:654	arg1	a highly similar amino acid sequence	region		a highly similar amino acid sequence						sequence	N-Glycosylation of IgG is crucial for its effector function and makes IgG highly heterogeneous both in structure and function, although all four subclasses of IgG contain only a single N-glycosylation site in the Fc region with a highly similar amino acid sequence.
29562594	3	41	part_of	containing	625:634	arg1	CMG2-Fc AND one N-glycosylation site	CMG2-Fc		one N-glycosylation site		PUBTATOR	Site	2 (CMG2	118429	site	Fc-fused capillary morphogenesis protein 2 (CMG2-Fc) containing one N-glycosylation site on the Fc domain, produced in Nicotiana benthamiana whole plants, served as a model protein.
29562594	3	41	part_of	containing	625:634	arg1	a model protein AND one N-glycosylation site	a model protein		one N-glycosylation site		Fterm	Site	protein		site	Fc-fused capillary morphogenesis protein 2 (CMG2-Fc) containing one N-glycosylation site on the Fc domain, produced in Nicotiana benthamiana whole plants, served as a model protein.
29562594	3	41	part_of	containing	625:634	arg1	Fc-fused capillary morphogenesis protein 2 AND one N-glycosylation site	Fc-fused capillary morphogenesis protein 2		one N-glycosylation site		Fterm	Site	protein 2		site	Fc-fused capillary morphogenesis protein 2 (CMG2-Fc) containing one N-glycosylation site on the Fc domain, produced in Nicotiana benthamiana whole plants, served as a model protein.
31606074	8	16	gly	glycosylated	975:986	arg1	glycosylated neuropeptides			glycosylated neuropeptides						neuropeptides	We also include recommendations for data analysis to identify glycosylated neuropeptides in crustaceans where a complete neuropeptide database is still lacking.
30343578	3	14	gly	N-glycopeptides	629:643	arg2	N-glycopeptides			N-glycopeptides						N-glycopeptides	With sequential trypsin digestion of proteins, C18 depletion of peptides without glycosylation, PNGase F digestion of N-glycopeptides, PGC enrichment of N-glycans, CH3I permethylation of the enriched N-glycans, cell-surface N-glycomes of the HepG2 and LO2 cells were analyzed using C18-RPLC-MS/MS (HCD).
31062865	0	55	gly	glycopeptides	27:39	arg2	intact glycopeptides			intact glycopeptides						glycopeptides	Characterization of intact glycopeptides reveals the impact of culture media on site-specific glycosylation of EPO-Fc fusion protein generated by CHO-GS cells.
31062865	0	106	gly	glycosylation	94:106	arg1	EPO-Fc fusion protein	EPO-Fc fusion protein				Fterm		protein			Characterization of intact glycopeptides reveals the impact of culture media on site-specific glycosylation of EPO-Fc fusion protein generated by CHO-GS cells.
29956878	8	24	part_of	protein	917:923	arg1	a protein consensus motif	protein		a protein consensus motif		Fterm	Site	protein		motif	This work also provided a protein consensus motif for the observed specificity as well as a glimpse into N-glycan flexibility upon binding.
31244828	4	47	part_of	has	720:722	arg1	MOG AND one known N-glycosylation site	MOG		one known N-glycosylation site		PUBTATOR	Site	MOG	4340	site	MOG has one known N-glycosylation site at N31 located in the BC loop linking two beta-sheets.
30708139	8	55	gly	glycosylation	1184:1196	arg2	one additional glycosylation site			one additional glycosylation site						site	Finally, two analogs with one additional glycosylation site were suggested as the qualified analogs for hyper-glycosylation of the LH, which can be considered for further experimental investigations.
30532014	4	37	gly	glycopeptide	651:662	arg2	a readily available bi-antennary glycopeptide			a readily available bi-antennary glycopeptide						glycopeptide	Here we describe a biomimetic approach in which a readily available bi-antennary glycopeptide can be converted in ten or fewer chemical and enzymatic steps into multi-antennary N-glycans that at each arm can be uniquely extended by glycosyltransferases to give access to highly complex asymmetrically branched N-glycans.
30037551	10	97	gly	mannosylated	1611:1622	arg1	mannosylated glycans				mannosylated glycans						Also the specific deglycosylation of a F. hepatica lysate demonstrated the relevance of mannosylated glycans in the induction of Th2/Treg immune responses during the infection.
29730471	4	21	gly	glycoproteins	846:858	arg1	neutral glycoproteins	neutral glycoproteins				Fterm		glycoproteins			The secretory cells of the Brunner's glands from No-Pro pigs primarily produced neutral glycoproteins and a small amount of acidic non-sulphated mucins.
31514875	10	63	gly	glycosylation	1862:1874	arg1	a protein	a protein				Fterm		protein			The potential of IMERs for the study of the glycosylation of a protein was illustrated with the comparison of two hCG-based drugs, Ovitrelle® and Pregnyl®.
29411222	1	8	part_of	receptor	187:194	arg1	the tumor necrosis factor receptor (TNFR) extracellular domain	tumor necrosis factor receptor		the tumor necrosis factor receptor (TNFR) extracellular domain		PUBTATOR	Site	tumor necrosis factor receptor	7132	domain	Etanercept is a soluble fusion protein of the tumor necrosis factor receptor (TNFR) extracellular domain, linked to an Fc part of IgG1.
29579062	1	52	gly	glycoprotein	179:190	arg1	HIV-1 envelope (Env) glycoprotein	HIV-1 envelope (Env) glycoprotein				Fterm		glycoprotein			Lectins that target N-glycans on the surface of HIV-1 envelope (Env) glycoprotein have the potential for use as antiviral agents.
29921663	3	109	gly	attached	546:553	arg1	the fragment crystallizable (Fc) region AND the glycan structure			the fragment crystallizable (Fc) region	the glycan structure					region	Immunoglobulin G (IgG) is involved in the adaptive immune response against meningococcal infections, and its effector functions are highly influenced by the glycan structure attached to the fragment crystallizable (Fc) region.
30563843	2	26	part_of	terminus	244:251	arg1	the angiotensin I peptide	terminus		the angiotensin I peptide						peptide	Renin-mediated cleavage of the angiotensin I peptide from the N terminus of angiotensinogen (AGT) is the rate-limiting step of this cascade; however, the detailed molecular mechanism underlying this step is unclear.
30563843	2	66	part_of	I	223:223	arg1	the angiotensin I peptide	angiotensin I		the angiotensin I peptide		PUBTATOR	Site	angiotensin I	183	peptide	Renin-mediated cleavage of the angiotensin I peptide from the N terminus of angiotensinogen (AGT) is the rate-limiting step of this cascade; however, the detailed molecular mechanism underlying this step is unclear.
30563843	2	72	part_of	angiotensin	211:221	arg1	the angiotensin I peptide	angiotensin I		the angiotensin I peptide		PUBTATOR	Site	angiotensin I	183	peptide	Renin-mediated cleavage of the angiotensin I peptide from the N terminus of angiotensinogen (AGT) is the rate-limiting step of this cascade; however, the detailed molecular mechanism underlying this step is unclear.
30563843	2	79	part_of	angiotensinogen	256:270	arg1	the N terminus	angiotensinogen		the N terminus		PUBTATOR	Site	angiotensinogen	183	terminus	Renin-mediated cleavage of the angiotensin I peptide from the N terminus of angiotensinogen (AGT) is the rate-limiting step of this cascade; however, the detailed molecular mechanism underlying this step is unclear.
31381874	2	42	gly	glycosylation	449:461	arg2	glycosylation sites			glycosylation sites						sites	However, this potential has not been explored thoroughly due to its high molecular weight, polymeric structure and large number of glycosylation sites.
31905645	3	85	part_of	PBS/MCC	407:413	arg1	The PBS/MCC composites	MCC		The PBS/MCC composites		OGER	Site	MCC		composites	The PBS/MCC composites were prepared by using a melt blending of 70 wt% of MCC processed from bleached softwood.
29580922	8	9	gly	sialylated	1351:1360	arg1	tri-antennary and sialylated N-glycans				tri-antennary and sialylated N-glycans						Peak area ratios of ECA-enriched glycopeptides were successfully discriminated between SSCs and controls using OPLS-DA, and indicated that tri-antennary and sialylated N-glycans of haptoglobin at Asn207 and Asn211 sites were characterized in SSCs.
29580922	8	20	gly	glycopeptides	1227:1239	arg2	ECA-enriched glycopeptides			ECA-enriched glycopeptides						glycopeptides	Peak area ratios of ECA-enriched glycopeptides were successfully discriminated between SSCs and controls using OPLS-DA, and indicated that tri-antennary and sialylated N-glycans of haptoglobin at Asn207 and Asn211 sites were characterized in SSCs.
29580922	8	38	gly	N-glycans	1362:1370	arg1	Asn207 and Asn211 sites			Asn207 and Asn211 sites	Asn207 and Asn211 sites		Site			sites	Peak area ratios of ECA-enriched glycopeptides were successfully discriminated between SSCs and controls using OPLS-DA, and indicated that tri-antennary and sialylated N-glycans of haptoglobin at Asn207 and Asn211 sites were characterized in SSCs.
29580922	8	63	gly	sites	1408:1412	arg1	tri-antennary and sialylated N-glycans			sites	tri-antennary and sialylated N-glycans					sites	Peak area ratios of ECA-enriched glycopeptides were successfully discriminated between SSCs and controls using OPLS-DA, and indicated that tri-antennary and sialylated N-glycans of haptoglobin at Asn207 and Asn211 sites were characterized in SSCs.
31754374	11	21	gly	N-glycosylation	1717:1731	arg2	only two N-glycosylation sites			only two N-glycosylation sites						sites	Among them, the two glycomutants which maintained only two N-glycosylation sites each (BxlBN1;5 and BxlBN5;7) showed improved catalytic efficiency, whereas the other four mutants' catalytic efficiencies were reduced.
30708139	2	17	gly	hyper-glycosylated	390:407	arg1	hyper-glycosylated protein	hyper-glycosylated protein				Fterm		protein			One aspect of glycoengineering is to introduce new N-glycosylation site (Asn-X-Thr/Ser, where X ≠ Pro) into desirable positions in the peptide backbone, resulting in the generation of hyper-glycosylated protein.
30708139	2	38	gly	N-glycosylation	257:271	arg2	new N-glycosylation site			new N-glycosylation site						site	One aspect of glycoengineering is to introduce new N-glycosylation site (Asn-X-Thr/Ser, where X ≠ Pro) into desirable positions in the peptide backbone, resulting in the generation of hyper-glycosylated protein.
30708139	2	46	gly	site	273:276	arg1	Asn-X-Thr/Ser			Asn-X-Thr/Ser						Asn	One aspect of glycoengineering is to introduce new N-glycosylation site (Asn-X-Thr/Ser, where X ≠ Pro) into desirable positions in the peptide backbone, resulting in the generation of hyper-glycosylated protein.
31813565	2	81	gly	glycopeptides	486:498	arg2	N-linked glycopeptides			N-linked glycopeptides						glycopeptides	In this work, a facile strategy to prepare hydrophilic maltose-functionalized magnetic metal-organic framework loaded with Au nanoparticles (denoted as magMOF@Au-maltose) for highly efficient enrichment of N-linked glycopeptides.
31987138	5	44	gly	moieties	797:804	arg1	glycopeptides			glycopeptides	glycopeptides		Site			glycopeptides	With the use of facile synthesis of Cys-terminated magnetic nanoparticles, the oxidized glycan moieties on glycopeptides could be selectively captured by the β-amino thiols groups on the surface of magnetic nanoparticles through thiazolidine formation.
31987138	5	67	gly	glycopeptides	809:821	arg2	glycopeptides			glycopeptides						glycopeptides	With the use of facile synthesis of Cys-terminated magnetic nanoparticles, the oxidized glycan moieties on glycopeptides could be selectively captured by the β-amino thiols groups on the surface of magnetic nanoparticles through thiazolidine formation.
31117584	7	82	gly	quantified N-glycosites	1710:1732	arg2	the 231 quantified N-glycosites			the 231 quantified N-glycosites						quantified N-glycosites	Besides double isomers of sialic acid linkages and fucose sequences, quadruple isomers from combination of two linages and two sequences were chromatographically separated and confidently identified; microheterogeneity with different differentially expressions were observed on 183 out of the 231 quantified N-glycosites.
31548313	4	6	gly	asparagine-linked	756:772	arg1	the asparagine-linked GlcNAc			asparagine	the asparagine-linked GlcNAc					asparagine	Although the biochemistries and structures of various ENGases have been studied extensively, the structural basis for the recognition of the core fucose and the asparagine-linked GlcNAc is unclear.
30592377	5	95	gly	fucosylated	1037:1047	arg1	high-mannose, branched and fucosylated glycans				high-mannose, branched and fucosylated glycans						A series of high-mannose, branched and fucosylated glycans are detected predominantly within tumor regions.
29340583	9	47	part_of	proteins	1597:1604	arg1	six glycosites	proteins		six glycosites		Fterm	Site	proteins		glycosites	Glycopeptide purification by zwitterionic-hydrophilic interaction liquid chromatography coupled with tandem mass spectrometry identified six glycosites from five H. pullorum proteins, which was consistent with proteins reactive with a polyclonal antiserum generated against glycosylated HgpA.
29956878	3	37	gly	N-glycoproteins	333:347	arg1	mammalian N-glycoproteins	mammalian N-glycoproteins				Fterm		N-glycoproteins			Core fucosylation influences the intrinsic properties and bioactivities of mammalian N-glycoproteins and its level is linked to various cancers.
29740059	7	24	gly	glycoproteins	1428:1440	arg1	other therapeutic glycoproteins	other therapeutic glycoproteins				Fterm		glycoproteins			These results validate our new approach for glycosylation engineering, and we expect this approach will be useful in future efforts to enhance the efficacy of other therapeutic glycoproteins.
30311906	7	11	gly	N-glycosylated	1059:1072	arg1	IgSF-CAM adhesion proteins	IgSF-CAM adhesion proteins				Fterm		proteins			As IgSF-CAM adhesion proteins are critical for neuron adhesion and highly N-glycosylated, we observed impaired IgSF-CAM-mediated neurite outgrowth and axon guidance in Srd5a3 mutant cerebellum.
30902814	2	58	gly	glycosylated	242:253	arg1	The heavily glycosylated IBV spike protein	The heavily glycosylated IBV spike protein				Fterm		protein			The heavily glycosylated IBV spike protein is responsible for binding to host tissues.
29648454	6	20	gly	glycosylation	775:787	arg1	this site			this site						site	Glycosylation site N256 was under-glycosylated in the wild-type (1.5%) compared to the native enzyme (55%); therefore, we mutated WPTP to promote glycosylation at this site (WPTP E254G).
29648454	6	10	gly	under-glycosylated	657:674	arg2	Glycosylation site N256			N256						N256	Glycosylation site N256 was under-glycosylated in the wild-type (1.5%) compared to the native enzyme (55%); therefore, we mutated WPTP to promote glycosylation at this site (WPTP E254G).
29642453	4	9	gly	glycosylation	603:615	arg2	glycosylation sites			glycosylation sites						sites	The results show a shift in glycosylation sites as a hallmark of 1918 and 2009 pandemics, and also for the 1976 "abortive pandemic".
32110292	5	66	gly	glycosylation	1025:1037	arg1	the protein sequence			the protein sequence						sequence	However, site-specific and comprehensive N-glycosylation analysis of IgG subclasses still cannot be achieved by MS alone due to the partial sequence coverage and loss of connections among glycosylation of the protein sequence.
29415413	4	1	gly	contains	668:675	arg1	The chemical composition AND a neutral polysaccharide			The chemical composition	a neutral polysaccharide					position	The chemical composition of the extracted polysaccharide contains a neutral polysaccharide with a high total sugar content and low protein, phenol and flavonoid content.
31262188	5	56	gly	glycoproteins	798:810	arg1	N-linked glycans	glycoproteins			N-linked glycans	Fterm		glycoproteins			Furthermore, N-linked glycans from human salivary glycoproteins, when released and purified, were potent inhibitors of M1, M3, and M12 GAS colonization ex vivo.
31062865	6	91	gly	sites	1546:1550	arg1	bi-			sites	bi-					sites	EPO-Fc protein generated in EX medium produced more complex tetra-antennary N-glycans at each of the three EPO N-sites while IA medium resulted in a greater fraction of bi- and tri-antennary N-glycans at these same sites.
31062865	6	91	gly	sites	1546:1550	arg1	tri-antennary N-glycans			sites	tri-antennary N-glycans					sites	EPO-Fc protein generated in EX medium produced more complex tetra-antennary N-glycans at each of the three EPO N-sites while IA medium resulted in a greater fraction of bi- and tri-antennary N-glycans at these same sites.
30602567	2	20	gly	transglycosylation	312:329	arg1	high glucose or cellobiose concentrations				high glucose or cellobiose concentrations						However, the susceptibility of these enzymes to inhibition and transglycosylation at high glucose or cellobiose concentrations severely limits their activity and, consequently, the overall efficiency of enzyme mixtures.
29729312	3	30	gly	glycosylation	613:625	arg2	two potential N-linked glycosylation sites			two potential N-linked glycosylation sites						sites	Its open reading frame covers 771 base pairs, encoding a protein of 256 amino acids that possesses GILT signature sequence CQHGX2ECX2NX4C, active-site CXXC motif, and two potential N-linked glycosylation sites.
30170051	3	58	gly	containing	527:536	arg1	2.98% protein AND a high molecular weight polysaccharide	2.98% protein			a high molecular weight polysaccharide	Fterm		protein			Lallemantia ibrica seed gum (LISG) is a high molecular weight polysaccharide (5.74 × 106 g/mol) containing, on average, 89.60% carbohydrate, 2.98% protein, 8.95% ash, 0.2% fat and 6.52% moisture.
31062865	10	97	gly	glycopeptide	2026:2037	arg2	This intact glycopeptide method			This intact glycopeptide method						glycopeptide	This intact glycopeptide method can decipher site-specific glycosylation profile and provide a more detailed characterization of N- and O-glycans present for enhanced understanding of the key product quality attributes such as media on recombinant proteins of biotechnology interest.
31807707	0	41	gly	glycoprotein	30:41	arg1	glycoprotein secretion	glycoprotein secretion				Fterm		glycoprotein			Mechanistic reconstruction of glycoprotein secretion through monitoring of intracellular N-glycan processing.
31759178	4	44	gly	moieties	964:971	arg1	sequence			sequence						sequence	With spectrum-level FDR ≤ 1%, 581 intact N-glycopeptides with comprehensive structural information of both the peptide backbones (amino acid sequences, N-glycosites) and the N-glycan moieties (monosaccharide composition, sequence and linkages) were identified from five technical replicates (TR1, TR2, TR3, TR4 and TR5).
31759178	4	86	gly	N-glycopeptides	822:836	arg2	581 intact N-glycopeptides			581 intact N-glycopeptides						N-glycopeptides	With spectrum-level FDR ≤ 1%, 581 intact N-glycopeptides with comprehensive structural information of both the peptide backbones (amino acid sequences, N-glycosites) and the N-glycan moieties (monosaccharide composition, sequence and linkages) were identified from five technical replicates (TR1, TR2, TR3, TR4 and TR5).
31759178	4	75	gly	N-glycosites	933:944	arg2	amino acid sequences			sequences, N-glycosites						sequences, N-glycosites	With spectrum-level FDR ≤ 1%, 581 intact N-glycopeptides with comprehensive structural information of both the peptide backbones (amino acid sequences, N-glycosites) and the N-glycan moieties (monosaccharide composition, sequence and linkages) were identified from five technical replicates (TR1, TR2, TR3, TR4 and TR5).
31759178	4	102	gly	backbones	900:908	arg1	amino acid sequences			sequences, N-glycosites						sequences, N-glycosites	With spectrum-level FDR ≤ 1%, 581 intact N-glycopeptides with comprehensive structural information of both the peptide backbones (amino acid sequences, N-glycosites) and the N-glycan moieties (monosaccharide composition, sequence and linkages) were identified from five technical replicates (TR1, TR2, TR3, TR4 and TR5).
30403372	1	29	part_of	CD4-binding	174:184	arg1	the CD4-binding site	CD4		the CD4-binding site		PUBTATOR	Site	CD4	920	site	VRC01 broadly neutralizing antibodies (bnAbs) target the CD4-binding site (CD4BS) of the human immunodeficiency virus-1 (HIV-1) envelope glycoprotein (Env).
31639407	5	5	part_of	TLC	852:854	arg1	TLC, and acylation sites	TLC		TLC, and acylation sites		OGER	Site	TLC	P31025	sites	Monosaccharide residues were identified from selective 1D TOCSY spectra and TLC, and acylation sites from 2D HMBC spectra.
29773674	9	19	gly	linker-glycosites	1489:1505	arg2	50 linker-glycosites			50 linker-glycosites						linker-glycosites	For aggrecan, we identified 50 linker-glycosites and mucin-type O-glycosites in the extended region and N-glycosites in the globular domains, many of which are novel and have not been observed previously.
29773674	9	55	gly	N-glycosites	1562:1573	arg2	N-glycosites			N-glycosites						region and N-glycosites	For aggrecan, we identified 50 linker-glycosites and mucin-type O-glycosites in the extended region and N-glycosites in the globular domains, many of which are novel and have not been observed previously.
29773674	9	61	gly	O-glycosites	1522:1533	arg2	mucin-type O-glycosites			mucin-type O-glycosites						O-glycosites	For aggrecan, we identified 50 linker-glycosites and mucin-type O-glycosites in the extended region and N-glycosites in the globular domains, many of which are novel and have not been observed previously.
30389790	4	73	gly	had	737:739	arg1	the healthier strain AND both G3M9 and Man9GlcNAc2 The lipid-linked oligosaccharide patterns	the healthier strain			both G3M9 and Man9GlcNAc2 The lipid-linked oligosaccharide patterns	Fterm		strain			The sick strain displayed only G3M9 as an ER protein-linked oligosaccharide, whereas the healthier strain had both G3M9 and Man9GlcNAc2 The lipid-linked oligosaccharide patterns of the two strains revealed that the most abundantly formed glycans were G3M9 in Δgls1-S and Glc2Man9GlcNAc2 in Δgls1-H, suggesting reduced Alg10p glucosyltransferase activity in the Δgls1-H strain.
31592495	5	37	gly	glycoproteins	778:790	arg1	other N-linked glycoproteins	other N-linked glycoproteins				Fterm		glycoproteins			We analyzed CD73 glycan signatures and global alterations in transcripts encoding other N-linked glycoproteins by using mass spectrometry glycomics and RNA sequencing (RNAseq), respectively.
29340583	9	68	gly	glycosites	1564:1573	arg2	six glycosites			six glycosites						glycosites	Glycopeptide purification by zwitterionic-hydrophilic interaction liquid chromatography coupled with tandem mass spectrometry identified six glycosites from five H. pullorum proteins, which was consistent with proteins reactive with a polyclonal antiserum generated against glycosylated HgpA.
31888963	5	86	part_of	CD16a	809:813	arg1	the composition	CD16a		the composition		PUBTATOR	Site	CD16a	2214	position	Here we isolated monocytes from individual donors and characterized the composition of CD16a and CD32a N-glycans from all modified sites.
29931153	1	60	gly	glycoproteins	232:244	arg1	nascent glycoproteins	nascent glycoproteins				Fterm		glycoproteins			Asparagine-linked glycans (N-glycans) are attached onto nascent glycoproteins in the endoplasmic reticulum (ER) and subsequently processed by a set of processing enzymes in the ER and Golgi apparatus.
29931153	1	78	gly	Asparagine-linked	168:184	arg1	N-glycans			Asparagine	N-glycans					Asparagine	Asparagine-linked glycans (N-glycans) are attached onto nascent glycoproteins in the endoplasmic reticulum (ER) and subsequently processed by a set of processing enzymes in the ER and Golgi apparatus.
29931153	1	78	gly	Asparagine-linked	168:184	arg1	Asparagine-linked glycans			Asparagine	Asparagine-linked glycans					Asparagine	Asparagine-linked glycans (N-glycans) are attached onto nascent glycoproteins in the endoplasmic reticulum (ER) and subsequently processed by a set of processing enzymes in the ER and Golgi apparatus.
29333671	3	34	gly	glycosylation	584:596	arg2	broader glycosylation site coverage			broader glycosylation site coverage						site	This material has exhibited superior selectivity and broader glycosylation site coverage over commercial Sepharose in glycoproteomic evaluation.
30336974	12	50	gly	glycoproteins	1961:1973	arg1	specific glycoproteins	specific glycoproteins				Fterm		glycoproteins			Consequences of MGE using GalNAc analogues depend on the expression and activity of various glycosyl transferases which determine global glycosylation on cell surface as well as on specific glycoproteins.
30336974	12	69	gly	glycosylation	1908:1920	arg1	specific glycoproteins	specific glycoproteins				Fterm		glycoproteins			Consequences of MGE using GalNAc analogues depend on the expression and activity of various glycosyl transferases which determine global glycosylation on cell surface as well as on specific glycoproteins.
29618644	5	104	part_of	epitopes	1063:1070	arg1	HIV-1 Env	HIV-1 Env		epitopes		PUBTATOR	Site	HIV-1 Env	100616444	epitopes	Mutations in the 253-11 MPER, which were previously reported to increase the lifetime of the prefusion Env conformation, affected the resistance of 253-11 to antibodies targeting various epitopes on HIV-1 Env, presumably destabilizing its otherwise stable, closed trimer structure.
30427586	3	53	gly	glycoproteins	509:521	arg1	four representative and biopharmaceutically relevant glycoproteins	four representative and biopharmaceutically relevant glycoproteins				Fterm		glycoproteins			Using a set of four representative and biopharmaceutically relevant glycoproteins (IgG, fibrinogen, lactotransferrin, and ribonuclease B), the benefits and limitations of the developed workflow are highlighted and a state-of-the-art blueprint for conducting high-quality in-depth N- and O-glycoproteomic analyses is provided.
29370305	4	53	part_of	Env	548:550	arg1	The Env SP sequences	Env		The Env SP sequences		PUBTATOR	Site	Env	155971	sequences	The Env SP sequences of HIV-1 isolates display high sequence variability, and the significance of such variability is unclear.
29411222	9	91	gly	O-glycopeptides	1438:1452	arg2	Four different O-glycopeptides			Four different O-glycopeptides						O-glycopeptides	Four different O-glycopeptides bearing core 1-type glycans were detected.
30539483	0	15	part_of	IgG1	98:101	arg1	Hyper-Glycosylated Fragment Crystallizable (Fc) Region	Human IgG1		Hyper-Glycosylated Fragment Crystallizable (Fc) Region		OGER		Human IgG1	P01857		A Method to Detect the Binding of Hyper-Glycosylated Fragment Crystallizable (Fc) Region of Human IgG1 to Glycan Receptors.
29405331	3	38	gly	antennary-fucosylated	498:518	arg1	antennary-fucosylated glycosites			antennary-fucosylated glycosites						glycosites	The serum glycoprotein alpha-1-antitrypsin (A1AT) which contains both core- and antennary-fucosylated glycosites was used in this study.
29405331	3	78	gly	glycoprotein	428:439	arg1	The serum glycoprotein alpha-1-antitrypsin	The serum glycoprotein alpha-1-antitrypsin				Fterm		glycoprotein			The serum glycoprotein alpha-1-antitrypsin (A1AT) which contains both core- and antennary-fucosylated glycosites was used in this study.
29405331	3	99	gly	glycosites	520:529	arg2	antennary-fucosylated glycosites			antennary-fucosylated glycosites						glycosites	The serum glycoprotein alpha-1-antitrypsin (A1AT) which contains both core- and antennary-fucosylated glycosites was used in this study.
29405497	8	60	part_of	endolysin	1255:1263	arg1	a corresponding domain	endolysin		a corresponding domain		Fterm	Site	endolysin		domain	Replacement of CBDP40 with a corresponding domain from a different Listeria phage endolysin yielded an enzyme with a significant shift in pH optimum.
29976678	5	54	part_of	protein	752:758	arg1	numerous surface-exposed E protein sites	protein		numerous surface-exposed E protein sites		Fterm	Site	protein		sites	Although FLAG insertions in prM greatly impaired viral fitness, this sequence was tolerated in numerous surface-exposed E protein sites.
30980844	7	57	part_of	GLUT1-containing	1075:1090	arg1	the GLUT1-containing membrane microdomains	GLUT1		the GLUT1-containing membrane microdomains		PUBTATOR	Site	GLUT1	20525	microdomains	Our data indicate that the GLUT1-containing membrane microdomains in L929 cells, as well as GLUT1's basal activity, are instead sphingolipid-dependent, being sensitive to both myriocin and sphingomyelinase treatment.
29405331	2	19	gly	glycosylation	259:271	arg2	each site			each site						site	Both the glycosylation sites (heterogeneity) and multiple possible glycan occupancy at each site (microheterogeneity) can be resolved via intact glycopeptide analysis.
29405331	2	19	gly	glycosylation	259:271	arg2	the glycosylation sites			the glycosylation sites						sites	Both the glycosylation sites (heterogeneity) and multiple possible glycan occupancy at each site (microheterogeneity) can be resolved via intact glycopeptide analysis.
29405331	2	23	gly	site	342:345	arg1	multiple possible glycan occupancy			site	multiple possible glycan occupancy					site	Both the glycosylation sites (heterogeneity) and multiple possible glycan occupancy at each site (microheterogeneity) can be resolved via intact glycopeptide analysis.
29405331	2	31	gly	glycopeptide	395:406	arg2	intact glycopeptide analysis			intact glycopeptide analysis						glycopeptide	Both the glycosylation sites (heterogeneity) and multiple possible glycan occupancy at each site (microheterogeneity) can be resolved via intact glycopeptide analysis.
31316527	16	113	gly	glycosylation	2831:2843	arg1	protein molecular dynamics	protein molecular dynamics				Fterm		protein			This study highlights the impacts of N-glycosylation on protein properties and provides insight into the effects of glycosylation on protein molecular dynamics.
29343613	3	15	gly	glycosylation	547:559	arg2	multiple glycosylation sites			multiple glycosylation sites						sites	However, the promiscuity of CVN to associate with multiple glycosylation sites in gp120 and its multivalency limit current understanding of the molecular arrangement of the DAVEI molecules on trimeric spike.
29231704	2	92	gly	glycopeptides	429:441	arg2	glycopeptides			glycopeptides						glycopeptides	In contrast, capillary zone electrophoresis separation of glycopeptides is particularly sensitive to the sialic acid composition of the glycan.
30152909	6	62	gly	N-glycoproteins	1649:1663	arg1	intact N-glycoproteins	intact N-glycoproteins				Fterm		N-glycoproteins			CONCLUSIONS For comprehensive structural characterization of intact N-glycoproteins using tandem mass spectrometry, the composition and topology of the N-glycan moiety can be identified using HCD and EThcD complementarily at low and high energies; while the amino acid sequence and glycosite can be identified using CID, ETD, HCD, ETciD, and EThcD with their optimal dissociation parameters.
30152909	6	77	gly	glycosite	1863:1871	arg2	glycosite			glycosite						sequence and glycosite	CONCLUSIONS For comprehensive structural characterization of intact N-glycoproteins using tandem mass spectrometry, the composition and topology of the N-glycan moiety can be identified using HCD and EThcD complementarily at low and high energies; while the amino acid sequence and glycosite can be identified using CID, ETD, HCD, ETciD, and EThcD with their optimal dissociation parameters.
30003921	12	2	gly	polypeptide	1834:1844	arg1	glycan core			polypeptide	glycan core					polypeptide	As BinA displays only mild affinity with receptor polypeptide, we hypothesize that toxin-receptor specificity of BinA in Culex may be mediated by dual interaction of BinA with glycan core of GPI anchor and receptor polypeptide.
31062865	2	116	gly	glycosylation	702:714	arg1	the target protein	the target protein				Fterm		protein			Here, we performed an intact glycopeptide analysis method to simultaneously analyze the site-specific N- and O-glycan profiles of the recombinant erythropoietin Fc (EPO-Fc) protein secreted from a Chinese hamster ovary glutamine synthetase stable cell line and compared the effects of two commercial culture media, EX-CELL (EX) and immediate advantage (IA) media, on the glycosylation profile of the target protein.
31062865	2	118	gly	glycopeptide	360:371	arg2	an intact glycopeptide analysis method			an intact glycopeptide analysis method						glycopeptide	Here, we performed an intact glycopeptide analysis method to simultaneously analyze the site-specific N- and O-glycan profiles of the recombinant erythropoietin Fc (EPO-Fc) protein secreted from a Chinese hamster ovary glutamine synthetase stable cell line and compared the effects of two commercial culture media, EX-CELL (EX) and immediate advantage (IA) media, on the glycosylation profile of the target protein.
31062865	2	39	gly	protein	504:510	arg1	the site-specific N- and O-glycan profiles	protein			the site-specific N- and O-glycan profiles	Fterm		protein			Here, we performed an intact glycopeptide analysis method to simultaneously analyze the site-specific N- and O-glycan profiles of the recombinant erythropoietin Fc (EPO-Fc) protein secreted from a Chinese hamster ovary glutamine synthetase stable cell line and compared the effects of two commercial culture media, EX-CELL (EX) and immediate advantage (IA) media, on the glycosylation profile of the target protein.
31117584	1	1	gly	presence	334:341	arg1	a single specific glycosite AND different N-glycan structures			a single specific glycosite	different N-glycan structures					glycosite	N-Glycosylation, being one of the most common and complex protein post-translational modifications (PTMs), is known to have microheterogeneity with the presence of different N-glycan structures at a single specific glycosite.
31117584	1	2	gly	glycosite	397:405	arg2	a single specific glycosite			a single specific glycosite						glycosite	N-Glycosylation, being one of the most common and complex protein post-translational modifications (PTMs), is known to have microheterogeneity with the presence of different N-glycan structures at a single specific glycosite.
30513259	3	37	part_of	Fc	604:605	arg1	aglycosylated Fc region	Fc		aglycosylated Fc region		Cterm	Site	Fc		region	To confirm this hypothesis, we examined the small-angle X-ray scattering (SAXS) profile of the glycosylated Fc region (gFc) and aglycosylated Fc region (aFc) in solution.
30513259	3	69	part_of	Fc	570:571	arg1	the glycosylated Fc region	Fc		the glycosylated Fc region		Cterm	Site	Fc		region	To confirm this hypothesis, we examined the small-angle X-ray scattering (SAXS) profile of the glycosylated Fc region (gFc) and aglycosylated Fc region (aFc) in solution.
30612270	9	2	gly	glycosylation	1745:1757	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			The data presented here leads to the conclusion that a middle down - or when possible a top down - approach is favorable for qualitative and quantitative analysis of the glycosylation of glycoproteins.
30612270	9	75	gly	glycoproteins	1762:1774	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			The data presented here leads to the conclusion that a middle down - or when possible a top down - approach is favorable for qualitative and quantitative analysis of the glycosylation of glycoproteins.
31813565	6	23	gly	glycopeptides	1242:1254	arg2	24 and 32 glycopeptides			24 and 32 glycopeptides						glycopeptides	The magMOF@Au-maltose nanocomposite can enrich 24 and 32 glycopeptides from tryptic HRP and human IgG digests, respectively.
30513259	0	13	part_of	Fc	118:119	arg1	aglycosylated Fc regions	Fc		aglycosylated Fc regions		Cterm	Site	Fc		regions	CH2 domain orientation of human immunoglobulin G in solution: Structural comparison of glycosylated and aglycosylated Fc regions using small-angle X-ray scattering.
29703890	5	49	gly	glycopeptide	773:784	arg2	glycopeptide coverage			glycopeptide coverage						glycopeptide	We test the performance of several boronic acid derivatives, showing that benzoboroxole markedly increases glycopeptide coverage from human cell lysates.
31548313	2	47	gly	transglycosylate	283:298	arg1	N-glycans				N-glycans						Endo-β-N-acetylglucosaminidase (ENGase) can release or transglycosylate N-glycans and is a promising tool for the chemoenzymatic synthesis of glycoproteins with homogeneously modified glycans.
31548313	2	79	gly	glycoproteins	370:382	arg1	homogeneously modified glycans	glycoproteins			homogeneously modified glycans	Fterm		glycoproteins			Endo-β-N-acetylglucosaminidase (ENGase) can release or transglycosylate N-glycans and is a promising tool for the chemoenzymatic synthesis of glycoproteins with homogeneously modified glycans.
31102532	3	10	gly	heterogeneity	404:416	arg1	glycan structures				glycan structures						The heterogeneity of glycan structures is one of the most challenging issues in the production of therapeutic proteins.
29878199	14	22	gly	glycoproteins	1938:1950	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Our combined data indicate an important role for SLC10A7 in bone mineralization and transport of glycoproteins to the extracellular matrix.
29619832	4	52	part_of	sites	769:773	arg1	the protein	protein		sites		Fterm	Site	protein		sites	All three glycosylation sites on the protein, expressed in human embryonic kidney (HEK) cells, were characterized individually using a mass spectrometry-based glycopeptide analysis workflow.
30389790	8	69	gly	glycoprotein	1494:1505	arg1	triglucosylated glycoprotein	triglucosylated glycoprotein				Fterm		glycoprotein			Lack of triglucosylated glycoprotein deglucosylation neither significantly prevented glycan elongation in the Golgi nor modified the overall cell wall monosaccharide composition.
31751750	2	7	part_of	chitin/PLA/nHAP	503:517	arg1	chitin/PLA/nHAP composites	chitin		chitin/PLA/nHAP composites		Fterm	Site	chitin		composites	The ionic liquid 1-ethyl-3-methylimidazolium acetate ([C2mim][OAc]) was used as a solvent to prepare chitin/PLA/nHAP composites.
30033944	11	82	gly	sialylated	1441:1450	arg1	Synthesized branched sialylated glycan clusters				Synthesized branched sialylated glycan clusters						Synthesized branched sialylated glycan clusters interacted with sialic acid-binding immunoglobulin-like lectin H (Siglec-H), which is known to be a microglia-specific molecule.
29446564	4	7	gly	glycoprotein	648:659	arg1	glycoprotein extracts	glycoprotein extracts				Fterm		glycoprotein			In order to assess changes in protein-linked glycans, we performed lectin and immunoblot analyses on glycoprotein extracts from these intestinal tissues using well-characterized lectins, and an antibody, which collectively recognize a wide range of different glycans epitopes.
30403372	5	22	gly	Asn276	957:962	arg1	a glycan			position Asn276	a glycan					position Asn276	Our results show VRC01 germline antibodies interacted with a wild-type 426c core lacking variable loops 1-3 in the presence and absence of a glycan at position Asn276, with the latter form binding with higher affinity than the former.
30335377	5	5	gly	glycoprotein	837:848	arg1	a high abundant glycoprotein	a high abundant glycoprotein				Fterm		glycoprotein			By further analysis with mass spectrometry, a high abundant glycoprotein, carrying a heterogeneous O-glycan structure, was identified.
30335377	5	1	gly	carrying	851:858	arg1	a high abundant glycoprotein AND a heterogeneous O-glycan structure	a high abundant glycoprotein			a heterogeneous O-glycan structure	Fterm		glycoprotein			By further analysis with mass spectrometry, a high abundant glycoprotein, carrying a heterogeneous O-glycan structure, was identified.
29619832	1	6	gly	glycoprotein	200:211	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			Human lysyl oxidase-like 2 (hLOXL2), a glycoprotein implicated in tumor progression and organ fibrosis, is a molecular target for anticancer and antifibrosis treatment.
30503329	13	50	gly	glycoproteins	1774:1786	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			The pathway effectively crosslinks glycoproteins into the fungal cell wall.
31776339	6	10	gly	regions	1031:1037	arg1	minimal sialic acid motifs			regions	minimal sialic acid motifs					regions	We use selected pathways to synthesize a protein vaccine candidate with an α-galactose adjuvant motif in a one-pot cell-free system and human antibody constant regions with minimal sialic acid motifs in glycoengineered Escherichia coli.
31776339	6	35	gly	motif	967:971	arg1	human antibody constant regions			human antibody constant regions	human antibody constant regions		Site			regions	We use selected pathways to synthesize a protein vaccine candidate with an α-galactose adjuvant motif in a one-pot cell-free system and human antibody constant regions with minimal sialic acid motifs in glycoengineered Escherichia coli.
31737090	0	41	gly	N-glycosylation	7:21	arg1	a recombinant exo-inulinase	a recombinant exo-inulinase				Fterm		exo-inulinase			Unique N-glycosylation of a recombinant exo-inulinase from Kluyveromyces cicerisporus and its effect on enzymatic activity and thermostability.
30463578	0	91	gly	N-glycosylation	0:14	arg1	plasma proteins	plasma proteins				Fterm		proteins			N-glycosylation patterns of plasma proteins and immunoglobulin G in chronic obstructive pulmonary disease.
30698702	6	70	gly	bifucosylated	989:1001	arg1	bifucosylated N-glycan				bifucosylated N-glycan						Specifically, seven bisecting structures (M/Z 9732+, 10602+, 10752+, 11622+, 11772+, 12642+, 13522+) decreased, M/Z 10552+ (two-antennae complex N-glycan) and M/Z 12792+ (three-antennae complex N-glycan) decreased, M/Z 10132+ and M/Z 11162+ (high-mannose N-glycan) increased, and M/Z 12282+ (bifucosylated N-glycan) increased.
29885470	6	96	gly	α-1,3-fucosylated	949:965	arg1	the core α-1,3-fucosylated structure				the core α-1,3-fucosylated structure						Using the method, the neutral and acidic N-glycans were successfully released without peeling degradation of the core α-1,3-fucosylated structure or detectable de-N-acetylation, revealing its general applicability to various types of N-glycans.
31887339	8	47	gly	fucosylation	1017:1028	arg1	sialylated glycans				sialylated glycans						Statistical analysis showed that CRC associates with increase in IgG agalactosylation, decrease in IgG sialylation and fucosylation of sialylated glycans.
31887339	8	55	gly	sialylated	1033:1042	arg1	sialylated glycans				sialylated glycans						Statistical analysis showed that CRC associates with increase in IgG agalactosylation, decrease in IgG sialylation and fucosylation of sialylated glycans.
31887339	8	75	gly	sialylation	1001:1011	arg1	sialylated glycans				sialylated glycans						Statistical analysis showed that CRC associates with increase in IgG agalactosylation, decrease in IgG sialylation and fucosylation of sialylated glycans.
30909000	6	26	part_of	GO-MAx	1524:1529	arg1	GO-MAx:y composites	MAx		GO-MAx:y composites		OGER	Site	MAx	P61244	composites	In addition, GO-MAx:y composites also exhibited high mechanical properties and good reusability.
29500371	8	44	gly	heterogeneity	1446:1458	arg1	the N-glycan				the N-glycan						In addition, we discuss the benefits of the FcγRIIIa chromatography column to assess the heterogeneity of the N-glycan.
29730764	2	6	gly	glycopeptides	486:498	arg2	O-linked glycopeptides			O-linked glycopeptides						glycopeptides	Two search engines, Byonic and Protein Prospector, were used for the interpretation of the data, and N- and O-linked glycopeptides were assigned from separate searches.
30395580	11	24	gly	Asn88	1623:1627	arg1	the glycans			Asn88 and Asn210	the glycans					Asn88 and Asn210	In particular, the glycans at Asn88 and Asn210 appear to have evolved as an integral part of the asco-laccase structure.
30395580	11	28	gly	Asn210	1633:1638	arg1	the glycans			Asn88 and Asn210	the glycans					Asn88 and Asn210	In particular, the glycans at Asn88 and Asn210 appear to have evolved as an integral part of the asco-laccase structure.
30503329	4	71	gly	glycoproteins	743:755	arg1	cell wall glycoproteins	cell wall glycoproteins				Fterm		glycoproteins			With an in vitro assay, we show that the glucan transferases are able to attach lichenin, a cell wall glucan with a repeating β-1,4-glucose-β-1,4-glucose-β-1,3-glucose structure, to cell wall glycoproteins.
29301962	1	20	part_of	proteins	327:334	arg1	glycosylation sites	proteins		glycosylation sites		Fterm	Site	proteins		sites	Oligosaccharyltransferase (OST) is an essential membrane protein complex in the endoplasmic reticulum, where it transfers an oligosaccharide from a dolichol-pyrophosphate-activated donor to glycosylation sites of secretory proteins.
30959980	3	9	part_of	mucin-type	512:521	arg1	a major mucin-type glycopeptide	mucin		a major mucin-type glycopeptide		PUBTATOR	Site	mucin	100508689	glycopeptide	In the present study, a major mucin-type glycopeptide (RIF6) of hyla rabbit intestine was isolated and the O-glycans were extensively characterized based on liquid chromatography-tandem mass spectrometry (LC-MS/MS) combined with bioinformatics approaches.
29475941	3	7	gly	heterogeneity	493:505	arg1	glycans				glycans						However, protein production in mammalian cells has several drawbacks, including heterogeneity of glycans attached to the produced protein.
29475941	3	36	gly	attached	518:525	arg1	the produced protein AND glycans	the produced protein			glycans	Fterm		protein			However, protein production in mammalian cells has several drawbacks, including heterogeneity of glycans attached to the produced protein.
29405331	10	32	gly	antennary-fucosylation	1766:1787	arg1	bi-				bi-						Structural assignments revealed that all three glycosylation sites of A1AT glycopeptides contain complex N-glycan structures: site Asn70 contains biantennary glycans without fucosylation; site Asn107 contains bi-, tri- and tetra-antennary glycans with both core- and antennary-fucosylation; site Asn271 contains bi- and tri-antennary glycans with both core- and antennary-fucosylation.
29405331	10	32	gly	antennary-fucosylation	1766:1787	arg1	tri-antennary glycans				tri-antennary glycans						Structural assignments revealed that all three glycosylation sites of A1AT glycopeptides contain complex N-glycan structures: site Asn70 contains biantennary glycans without fucosylation; site Asn107 contains bi-, tri- and tetra-antennary glycans with both core- and antennary-fucosylation; site Asn271 contains bi- and tri-antennary glycans with both core- and antennary-fucosylation.
29405331	10	62	gly	antennary-fucosylation	1671:1692	arg1	bi-				bi-						Structural assignments revealed that all three glycosylation sites of A1AT glycopeptides contain complex N-glycan structures: site Asn70 contains biantennary glycans without fucosylation; site Asn107 contains bi-, tri- and tetra-antennary glycans with both core- and antennary-fucosylation; site Asn271 contains bi- and tri-antennary glycans with both core- and antennary-fucosylation.
29405331	10	62	gly	antennary-fucosylation	1671:1692	arg1	tri-				tri-						Structural assignments revealed that all three glycosylation sites of A1AT glycopeptides contain complex N-glycan structures: site Asn70 contains biantennary glycans without fucosylation; site Asn107 contains bi-, tri- and tetra-antennary glycans with both core- and antennary-fucosylation; site Asn271 contains bi- and tri-antennary glycans with both core- and antennary-fucosylation.
29405331	10	62	gly	antennary-fucosylation	1671:1692	arg1	tetra-antennary glycans				tetra-antennary glycans						Structural assignments revealed that all three glycosylation sites of A1AT glycopeptides contain complex N-glycan structures: site Asn70 contains biantennary glycans without fucosylation; site Asn107 contains bi-, tri- and tetra-antennary glycans with both core- and antennary-fucosylation; site Asn271 contains bi- and tri-antennary glycans with both core- and antennary-fucosylation.
29405331	10	69	gly	glycosylation	1451:1463	arg2	all three glycosylation sites			all three glycosylation sites						sites	Structural assignments revealed that all three glycosylation sites of A1AT glycopeptides contain complex N-glycan structures: site Asn70 contains biantennary glycans without fucosylation; site Asn107 contains bi-, tri- and tetra-antennary glycans with both core- and antennary-fucosylation; site Asn271 contains bi- and tri-antennary glycans with both core- and antennary-fucosylation.
29405331	10	80	gly	glycopeptides	1479:1491	arg2	A1AT glycopeptides			A1AT glycopeptides						glycopeptides	Structural assignments revealed that all three glycosylation sites of A1AT glycopeptides contain complex N-glycan structures: site Asn70 contains biantennary glycans without fucosylation; site Asn107 contains bi-, tri- and tetra-antennary glycans with both core- and antennary-fucosylation; site Asn271 contains bi- and tri-antennary glycans with both core- and antennary-fucosylation.
29405331	10	33	gly	contain	1493:1499	arg1	all three glycosylation sites AND complex N-glycan structures			all three glycosylation sites	complex N-glycan structures					sites	Structural assignments revealed that all three glycosylation sites of A1AT glycopeptides contain complex N-glycan structures: site Asn70 contains biantennary glycans without fucosylation; site Asn107 contains bi-, tri- and tetra-antennary glycans with both core- and antennary-fucosylation; site Asn271 contains bi- and tri-antennary glycans with both core- and antennary-fucosylation.
29405331	10	33	gly	contain	1493:1499	arg1	A1AT glycopeptides AND complex N-glycan structures			A1AT glycopeptides	complex N-glycan structures					glycopeptides	Structural assignments revealed that all three glycosylation sites of A1AT glycopeptides contain complex N-glycan structures: site Asn70 contains biantennary glycans without fucosylation; site Asn107 contains bi-, tri- and tetra-antennary glycans with both core- and antennary-fucosylation; site Asn271 contains bi- and tri-antennary glycans with both core- and antennary-fucosylation.
29405331	10	98	gly	contains	1541:1548	arg1	site Asn70 AND biantennary glycans			site Asn70	biantennary glycans					site Asn70	Structural assignments revealed that all three glycosylation sites of A1AT glycopeptides contain complex N-glycan structures: site Asn70 contains biantennary glycans without fucosylation; site Asn107 contains bi-, tri- and tetra-antennary glycans with both core- and antennary-fucosylation; site Asn271 contains bi- and tri-antennary glycans with both core- and antennary-fucosylation.
29405331	10	77	gly	contains	1707:1714	arg1	site Asn271 AND tri-antennary glycans			site Asn271	tri-antennary glycans					site Asn271	Structural assignments revealed that all three glycosylation sites of A1AT glycopeptides contain complex N-glycan structures: site Asn70 contains biantennary glycans without fucosylation; site Asn107 contains bi-, tri- and tetra-antennary glycans with both core- and antennary-fucosylation; site Asn271 contains bi- and tri-antennary glycans with both core- and antennary-fucosylation.
29405331	10	77	gly	contains	1707:1714	arg1	site Asn271 AND bi-			site Asn271	bi-					site Asn271	Structural assignments revealed that all three glycosylation sites of A1AT glycopeptides contain complex N-glycan structures: site Asn70 contains biantennary glycans without fucosylation; site Asn107 contains bi-, tri- and tetra-antennary glycans with both core- and antennary-fucosylation; site Asn271 contains bi- and tri-antennary glycans with both core- and antennary-fucosylation.
29405331	10	8	gly	contains	1604:1611	arg1	site Asn107 AND tetra-antennary glycans			site Asn107	tetra-antennary glycans					site Asn107	Structural assignments revealed that all three glycosylation sites of A1AT glycopeptides contain complex N-glycan structures: site Asn70 contains biantennary glycans without fucosylation; site Asn107 contains bi-, tri- and tetra-antennary glycans with both core- and antennary-fucosylation; site Asn271 contains bi- and tri-antennary glycans with both core- and antennary-fucosylation.
29405331	10	8	gly	contains	1604:1611	arg1	site Asn107 AND bi-			site Asn107	bi-					site Asn107	Structural assignments revealed that all three glycosylation sites of A1AT glycopeptides contain complex N-glycan structures: site Asn70 contains biantennary glycans without fucosylation; site Asn107 contains bi-, tri- and tetra-antennary glycans with both core- and antennary-fucosylation; site Asn271 contains bi- and tri-antennary glycans with both core- and antennary-fucosylation.
29405331	10	8	gly	contains	1604:1611	arg1	site Asn107 AND tri-			site Asn107	tri-					site Asn107	Structural assignments revealed that all three glycosylation sites of A1AT glycopeptides contain complex N-glycan structures: site Asn70 contains biantennary glycans without fucosylation; site Asn107 contains bi-, tri- and tetra-antennary glycans with both core- and antennary-fucosylation; site Asn271 contains bi- and tri-antennary glycans with both core- and antennary-fucosylation.
29405331	10	69	gly	glycosylation	1451:1463	arg2	A1AT glycopeptides			glycopeptides						glycopeptides	Structural assignments revealed that all three glycosylation sites of A1AT glycopeptides contain complex N-glycan structures: site Asn70 contains biantennary glycans without fucosylation; site Asn107 contains bi-, tri- and tetra-antennary glycans with both core- and antennary-fucosylation; site Asn271 contains bi- and tri-antennary glycans with both core- and antennary-fucosylation.
29433940	6	27	gly	N-glycans	530:538	arg1	proteins	proteins			N-glycans	Fterm		proteins			Sialylated N-glycans on proteins were successfully produced in silkworm by co-expressing galactosyltransferase and sialyltransferase and providing an external supply of a sialylation-related substrate.
30033944	4	51	gly	sialylated	553:562	arg1	a major N-glycan				a major N-glycan						A2G'2F has a branched sialic acid structural feature, and branched sialylated A2G'2F is a major N-glycan in the mouse brain.
30002445	2	6	gly	glycoproteins	340:352	arg1	homogeneous glycoproteins	homogeneous glycoproteins				Fterm		glycoproteins			Unfortunately, cell-based production of homogeneous glycoproteins remains a significant challenge due to cell viability constraints and the inability to control glycosylation components at precise ratios in vivo.
31141660	9	47	gly	multifucosylated	1622:1637	arg1	multifucosylated N-glycans				multifucosylated N-glycans						The practical applicability of the approach is demonstrated on the analysis of multifucosylated N-glycans detected with lower abundances in lung cancer samples.
30673210	4	22	gly	N-glycopeptides	810:824	arg2	The N-glycopeptides			The N-glycopeptides						N-glycopeptides	The N-glycopeptides from trypsin digests of immunoglobulin G (IgG), mixture of IgG and bovine serum albumin (BSA), and serum proteins were enriched using this material and compared with a commercial material ZIC-HILIC.
30013106	4	17	gly	glycoproteins	764:776	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Solid-state NMR spectroscopy, assisted by dynamic nuclear polarization and glycosyl linkage analysis, reveals that chitin and α-1,3-glucan build a hydrophobic scaffold that is surrounded by a hydrated matrix of diversely linked β-glucans and capped by a dynamic layer of glycoproteins and α-1,3-glucan.
29730764	1	32	gly	glycopeptide	341:352	arg2	glycopeptide			glycopeptide						glycopeptide	A very complex mixture of intact, human N- and O-glycopeptides, enriched from the tryptic digest of urinary proteins of three healthy donors using a two-step lectin affinity enrichment, was analyzed by LC-MS/MS, leading to approximately 45,000 glycopeptide EThcD spectra.
29730764	1	61	gly	O-glycopeptides	144:158	arg2	O-glycopeptides			O-glycopeptides						O-glycopeptides	A very complex mixture of intact, human N- and O-glycopeptides, enriched from the tryptic digest of urinary proteins of three healthy donors using a two-step lectin affinity enrichment, was analyzed by LC-MS/MS, leading to approximately 45,000 glycopeptide EThcD spectra.
30016589	2	47	part_of	IgG1	387:390	arg1	the IgG1 crystallizable fragment	IgG1		the IgG1 crystallizable fragment		OGER	Site	IgG1	P01857	fragment	Core fucosylation, a prevalent modification to the asparagine (N)-linked carbohydrate on the IgG1 crystallizable fragment (Fc), decreases the Fc γ receptor IIIa (CD16a) binding affinity and mAb efficacy.
29769533	0	12	gly	glycoprotein	62:73	arg1	the glycoprotein architecture	the glycoprotein architecture				Fterm		glycoprotein			Structure of a cleavage-independent HIV Env recapitulates the glycoprotein architecture of the native cleaved trimer.
30336974	6	68	gly	glycoproteins	1106:1118	arg1	cell surface glycoproteins	cell surface glycoproteins				Fterm		glycoproteins			Ac5GalNTGc was metabolized and incorporated as N-thioglycolyl-d-galactosamine (GalNTGc) in cell surface glycoproteins in both the cell lines with varying degrees of efficiency.
29976678	1	24	gly	glycoproteins	126:138	arg1	Zika virus (ZIKV) glycoproteins	Zika virus (ZIKV) glycoproteins				Fterm		glycoproteins			Zika virus (ZIKV) glycoproteins are the primary target of the humoral immune response.
29740059	1	22	gly	glycoproteins	193:205	arg1	Sialylation	glycoproteins			Sialylation	Fterm		glycoproteins			Sialylation of recombinant therapeutic glycoproteins modulates their pharmacokinetic properties by affecting their in vivo half-life.
29596681	6	16	gly	glycoform	1146:1154	arg1	rather homogenous biantennary N-glycans				rather homogenous biantennary N-glycans						We demonstrate stable precise gene engineering of rather homogenous biantennary N-glycans with and without galactose (G0F, G2F) as well as the α2,6-linked monosialylated (G2FS1) glycoform.
29596681	6	34	gly	monosialylated	1123:1136	arg1	the α2,6-linked monosialylated (G2FS1) glycoform				the α2,6-linked monosialylated (G2FS1) glycoform						We demonstrate stable precise gene engineering of rather homogenous biantennary N-glycans with and without galactose (G0F, G2F) as well as the α2,6-linked monosialylated (G2FS1) glycoform.
29596681	6	34	gly	monosialylated	1123:1136	arg1	rather homogenous biantennary N-glycans				rather homogenous biantennary N-glycans						We demonstrate stable precise gene engineering of rather homogenous biantennary N-glycans with and without galactose (G0F, G2F) as well as the α2,6-linked monosialylated (G2FS1) glycoform.
30669833	4	7	gly	multisialylated	804:818	arg1	multisialylated LacdiNAc (GalNAcβ1-4GlcNAc) structures				multisialylated LacdiNAc (GalNAcβ1-4GlcNAc) structures						We found that abundance of multisialylated LacdiNAc (GalNAcβ1-4GlcNAc) structures were significantly upregulated in the PCa group compared to the BPH group.
30902814	3	30	part_of	sites	331:335	arg1	the spike protein	protein		sites		Fterm	Site	protein		sites	Glycosylation sites in the spike protein are highly conserved across viral genotypes, suggesting an important role for this modification in the virus life cycle.
29231704	7	20	gly	glycoprotein	1112:1123	arg1	alpha-1-acid glycoprotein	alpha-1-acid glycoprotein				Fterm		glycoprotein			We applied this method for the analysis of alpha-1-acid glycoprotein (AGP).
30325416	7	82	gly	arm	1803:1805	arg1	both isolated, and Fc-bound N-glycans				both isolated, and Fc-bound N-glycans						These findings are in agreement with and can help rationalize recent experimental evidence showing a differential recognition of positional isomers in glycan array data and also the preference of sialyltransferase for the more accessible, outstretched α(1-3) arm in both isolated, and Fc-bound N-glycans.
31216452	4	47	gly	presence	694:701	arg2	their terminus AND sialic acids			their terminus	sialic acids					terminus	Evidences cleared that EPO's activity increased by numbers of N-glycan moieties with presence of sialic acids at their terminus.
29580922	0	54	gly	glycopeptides	15:27	arg2	Characteristic glycopeptides			Characteristic glycopeptides						glycopeptides	Characteristic glycopeptides associated with extreme human longevity identified through plasma glycoproteomics.
30673210	8	45	gly	O-glycopeptides	1607:1621	arg2	278 unique O-glycopeptides			278 unique O-glycopeptides						O-glycopeptides	Furthermore, 48 unique O-glycosylation sites of 278 unique O-glycopeptides were identified from the triplicate analysis of 30 μg deglycosylated fetuin digest.
30673210	8	92	gly	O-glycosylation	1571:1585	arg2	48 unique O-glycosylation sites			48 unique O-glycosylation sites						sites	Furthermore, 48 unique O-glycosylation sites of 278 unique O-glycopeptides were identified from the triplicate analysis of 30 μg deglycosylated fetuin digest.
30673210	8	92	gly	O-glycosylation	1571:1585	arg2	278 unique O-glycopeptides			O-glycopeptides						O-glycopeptides	Furthermore, 48 unique O-glycosylation sites of 278 unique O-glycopeptides were identified from the triplicate analysis of 30 μg deglycosylated fetuin digest.
30315106	4	29	part_of	CEL/FAPP	730:737	arg1	the highly O-glycosylated, mucin-like C terminus	CEL		the highly O-glycosylated, mucin-like C terminus		PUBTATOR	Site	CEL	P19835	terminus	The monoclonal antibody mAb16D10 was previously reported to detect a glycotope in the highly O-glycosylated, mucin-like C terminus of CEL/FAPP.
30574787	1	5	gly	glycoproteins	83:95	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Knowledge of glycoproteins, their site-specific glycosylation patterns, and the glycan structures that they present to their recognition partners in health and disease is gradually being built on using a range of experimental approaches.
29580922	8	63	part_of	sites	1408:1412	arg1	haptoglobin	haptoglobin		sites		PUBTATOR	Site	haptoglobin	3240	sites	Peak area ratios of ECA-enriched glycopeptides were successfully discriminated between SSCs and controls using OPLS-DA, and indicated that tri-antennary and sialylated N-glycans of haptoglobin at Asn207 and Asn211 sites were characterized in SSCs.
30111543	6	21	gly	glycoprotein	1069:1080	arg1	glycoprotein microheterogeneity	glycoprotein microheterogeneity				Fterm		glycoprotein			Taken together, our results not only elucidate how glycoprotein microheterogeneity regulates protein-drug/protein interactions but also inform the pharmacokinetics of plasma proteins, many of which are drug targets, and whose glycosylation status changes in various disease states.
31759178	6	108	gly	N-glycoproteins	1330:1344	arg1	the 19 intact N-glycoproteins	the 19 intact N-glycoproteins				Fterm		N-glycoproteins			For the 19 intact N-glycoproteins observed with differential N-glycosylation expression, 14 (each with one or more DEGPs) were observed with uniform down regulation; 6 (each with one or more DEGPs) were observed with uniform up regulation; whereas one was observed with both up and down regulation.
29579191	1	41	gly	Glycosylation	163:175	arg1	proteoglycans	proteins			proteoglycans	Fterm		proteins			Glycosylation of proteins, lipids and proteoglycans in human cells involves at least 167 identified glycosyltransferases (GTfs), and these orchestrate the biosynthesis of diverse types of glycoconjugates and glycan structures.
30503285	1	10	gly	O-glycosylated	186:199	arg1	O-glycosylated proteins	O-glycosylated proteins				Fterm		proteins			We have developed an Escherichia coli strain for the in vivo production of O-glycosylated proteins.
30500162	9	48	gly	glycopeptides	1295:1307	arg2	Neu5Gc-positive glycopeptides			Neu5Gc-positive glycopeptides						glycopeptides	Then we developed a reproducible ELISA to screen human sera against Neu5Gc-positive glycopeptides for detection of human serum anti-Neu5Gc IgGs.
31174130	2	1	gly	glycopeptides	447:459	arg2	glycopeptides			glycopeptides						glycopeptides	Here, a titania-based material was synthesized using a facile sol-gel method for the efficient analysis of glycopeptides and glycans.
29757379	0	58	gly	glycosite	38:46	arg2	Quiescin sulfhydryl oxidase 1 (QSOX1) glycosite mutation			Quiescin sulfhydryl oxidase 1 (QSOX1) glycosite mutation						glycosite	Quiescin sulfhydryl oxidase 1 (QSOX1) glycosite mutation perturbs secretion but not Golgi localization.
30037551	6	6	gly	glycoproteins	1068:1080	arg1	model glycoproteins	model glycoproteins				Fterm		glycoproteins			Immobilized glycosidases were effective in the selective deglycosylation of model glycoproteins and a Fasciola hepatica lysate, evidenced by a decrease in specific lectin recognition of 40-50% after enzymatic deglycosylation.
30037551	6	58	gly	deglycosylation	1043:1057	arg1	model glycoproteins	model glycoproteins				Fterm		glycoproteins			Immobilized glycosidases were effective in the selective deglycosylation of model glycoproteins and a Fasciola hepatica lysate, evidenced by a decrease in specific lectin recognition of 40-50% after enzymatic deglycosylation.
29888905	9	105	gly	fucosylated	1683:1693	arg1	tetraantennary proximally fucosylated glycans				tetraantennary proximally fucosylated glycans						Mouse Tu-2449 EV profiles were very heterogeneous, with di-, tri-, and tetraantennary proximally fucosylated glycans and the presence of peripheral Galα3Gal structure.
31541622	7	62	gly	glycoproteins	1125:1137	arg1	More than 400 silkworm N- and O- glycoproteins	More than 400 silkworm N- and O- glycoproteins				Fterm		glycoproteins			More than 400 silkworm N- and O- glycoproteins were identified with high confidence, demonstrating that this organism employs extensive glycosylation.
32110292	3	42	gly	N-glycosylation	618:632	arg2	only a single N-glycosylation site			only a single N-glycosylation site						site	N-Glycosylation of IgG is crucial for its effector function and makes IgG highly heterogeneous both in structure and function, although all four subclasses of IgG contain only a single N-glycosylation site in the Fc region with a highly similar amino acid sequence.
30973186	3	31	part_of	sites	415:419	arg1	Plk	Plk		sites		PUBTATOR	Site	Plk	5347	sites	EPO variants with an alkyne-bearing non-natural amino acid (Plk) at the N-glycosylation sites 24, 38, and 83 were obtained by amber suppression followed by protein purification and refolding.
30651366	2	60	gly	glycoprotein	336:347	arg1	the HCV E2 envelope glycoprotein	the HCV E2 envelope glycoprotein				Fterm		glycoprotein			Cumulative evidence supports the importance of antibodies targeting the HCV E2 envelope glycoprotein to facilitate viral clearance.
29932998	7	42	part_of	1:1	1135:1137	arg1	DMP (1:1) composites	NF/GG: DMP (1		DMP (1:1) composites		OGER	Site	NF/GG: DMP (1	Q9Y222	composites	The optimized oil-entrapped Florite R NF/GG: DMP (1:1) composites eluted MFM via case-II transport mechanism and its drug release data was best fitted in zero-order kinetic model.
29932998	7	70	part_of	DMP	1130:1132	arg1	DMP (1:1) composites	NF/GG: DMP (1		DMP (1:1) composites		OGER	Site	NF/GG: DMP (1	Q9Y222	composites	The optimized oil-entrapped Florite R NF/GG: DMP (1:1) composites eluted MFM via case-II transport mechanism and its drug release data was best fitted in zero-order kinetic model.
29981899	9	47	gly	disialylated	1471:1482	arg1	disialylated and trisialylated glycan structures				disialylated and trisialylated glycan structures						Furthermore, relative amounts of disialylated and trisialylated glycan structures were increased, while high-mannose and glycans containing bisecting N-acetylglucosamine decreased in CLBP.
29981899	9	66	gly	trisialylated	1488:1500	arg1	disialylated and trisialylated glycan structures				disialylated and trisialylated glycan structures						Furthermore, relative amounts of disialylated and trisialylated glycan structures were increased, while high-mannose and glycans containing bisecting N-acetylglucosamine decreased in CLBP.
29451981	11	92	gly	glycopeptide	2129:2140	arg2	site specific glycopeptide analyses			site specific glycopeptide analyses						glycopeptide	After analyzing the glycome by both approaches and determining the glycans present, a glycan library was created for site specific glycopeptide analyses.
29882469	1	9	gly	glycoproteins	254:266	arg1	therapeutic glycoproteins	therapeutic glycoproteins				Fterm		glycoproteins			Glycoengineered yeast cells, which express human-compatible glycan structures, are particularly attractive host cells to produce therapeutic glycoproteins.
30663306	4	19	gly	glycoproteins	913:925	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Integration of label-free quantitative proteomic analysis and lectin array profiles confirmed that BCF exposure results in changes in the levels of glycoproteins present at the cell surface and also changes to their glycosylation pattern.
29615747	3	21	gly	receptors	493:501	arg1	macrophage galactose-type calcium-type lectin	receptors			macrophage galactose-type calcium-type lectin	Fterm		receptors			Here, we report that the structural features of ebolavirus envelope glycoproteins (GPs) and one of their counter receptors, macrophage galactose-type calcium-type lectin (MGL/CD301), play crucial roles in determining viral infectivity.
29615747	3	36	gly	glycoproteins	448:460	arg1	ebolavirus envelope glycoproteins	ebolavirus envelope glycoproteins				Fterm		glycoproteins			Here, we report that the structural features of ebolavirus envelope glycoproteins (GPs) and one of their counter receptors, macrophage galactose-type calcium-type lectin (MGL/CD301), play crucial roles in determining viral infectivity.
31739015	6	53	part_of	Ara	1031:1033	arg1	some Gal and Ara residues	Ara		some Gal and Ara residues		OGER	Site	Ara	O95255	residues	LJP-A-2 ~ LJP-A-4 were similar to each other, mainly composed of GalA (>50%) with some Gal and Ara residues, while LJP-A-1 mainly composed of Gal and Ara (>70%).
31739015	6	59	part_of	Gal	1023:1025	arg1	some Gal and Ara residues	Gal		some Gal and Ara residues		OGER	Site	Gal	Q8N6F7	residues	LJP-A-2 ~ LJP-A-4 were similar to each other, mainly composed of GalA (>50%) with some Gal and Ara residues, while LJP-A-1 mainly composed of Gal and Ara (>70%).
29642453	6	67	gly	glycosylation	980:992	arg1	canonical sites			canonical sites						sites	After the 2009 pandemic, recent isolates accrued glycosylation at canonical sites in HA, reflecting gradual seasonal adaptation, and a novel glycosylation in NA as an independent signature for adaptation among humans.
29443078	2	43	gly	glycosylations	471:484	arg2	the 3-O and 6-O positions			the 3-O and 6-O positions						positions	To achieve the desired structural diversity, the strategy began with the chemo-enzymatic synthesis of three kinds of oligosaccharyl fluoride modules, followed by their stepwise α-selective glycosylations at the 3-O and 6-O positions of the mannose residue of the common core trisaccharide having a crucial β-mannoside linkage.
29858715	8	6	gly	glycoprotein	1117:1128	arg1	a specific glycoprotein Ley antigens				a specific glycoprotein Ley antigens						Here, for the first time on a specific glycoprotein Ley antigens are unambiguously characterized on an N-type glycan by NMR spectroscopy.
30637588	4	72	part_of	ECM	1008:1010	arg1	GAG composition	ECM		GAG composition		OGER	Site	ECM	Q13201	position	However, little is known about the molecular and more specifically, GAG composition of these cell-derived ECM.
30640124	1	13	gly	glycosylation	202:214	arg1	proteins	proteins				Fterm		proteins			The development of chemical sensors capable of detecting the specific glycosylation patterns of proteins offers a powerful mean for the early detection of cancer.
29885470	7	37	gly	derived	1107:1113	arg2	chicken ovalbumin AND The Fmoc-derivatized N-glycans	chicken ovalbumin			The Fmoc-derivatized N-glycans	Fterm		ovalbumin			The Fmoc-derivatized N-glycans derived from chicken ovalbumin, Fagopyrum esculentum Moench Pollen and FBS were successfully analyzed by online LC/MS to distinguish isomers.
31734359	4	7	gly	position	860:867	arg1	the polysaccharide			position	the polysaccharide					position	Structural investigations including FT-IR, Raman spectra and 1D, 2D NMR analysis revealed that selenium in CSe-tps1 replaced the hydroxyl group at the C-6 position in the polysaccharide with the form of selenyl ester, while most of the selenium in ASe-tps1 replaced the hydroxyl group at the C-1 and C-6 position in the form of the SeH bond on the branch of the polysaccharide.
30612270	8	79	part_of	compositions	1456:1467	arg1	ceruloplasmin	ceruloplasmin		compositions		PUBTATOR	Site	ceruloplasmin	1356	positions	We observed a relative increase of triantennary glycans of up to a factor of three and, even more, MS peaks corresponding to tetraantennary compositions on ceruloplasmin at glycosite 137N in all 17 samples, which we did not detect using a bottom up approach.
30673210	2	93	gly	glycosylated	427:438	arg1	glycosylated peptides			glycosylated peptides						peptides	Although hydrophilic interaction chromatography (HILIC) has been developed for enrichment of glycosylated peptides, a plethora of hydrophilic materials always suffered from large steric hindrance, great cost, and difficulty with modifications of high-density hydrophilic groups.
31453603	9	69	gly	glycopeptides	1636:1648	arg2	selected glycopeptides			selected glycopeptides						glycopeptides	Molecular dynamics (MD) simulations of the gas phase structures and CCSs of selected glycopeptides revealed that the experimental observations were consistent with a glycan size and charge state dependent interplay between destabilizing coulombic repulsion effects (tending to result in more extended structures) and stabilizing charge solvation effects in which the glycan plays a major role (tending to result in more compact structures).
29405331	1	56	gly	glycosylation	218:230	arg1	glycopeptides			glycopeptides						glycopeptides	A liquid chromatography-tandem mass spectrometry (LC-MS/MS)-based methodology has been developed to differentiate core- and antennary-fucosylated glycosylation of glycopeptides.
29405331	1	59	gly	glycopeptides	235:247	arg2	glycopeptides			glycopeptides						glycopeptides	A liquid chromatography-tandem mass spectrometry (LC-MS/MS)-based methodology has been developed to differentiate core- and antennary-fucosylated glycosylation of glycopeptides.
31062865	7	27	part_of	IgG	1706:1708	arg1	the final IgG Fc site	IgG		the final IgG Fc site		Cterm	Site	IgG		site	Interestingly, the sialylation content decreased from sites 1-4 in both media while the fucosylation progressively increased with a maximum at the final IgG Fc site.
29757379	6	52	gly	glycosylation	871:883	arg2	a highly conserved N-linked glycosylation site			a highly conserved N-linked glycosylation site						site	We found a highly conserved N-linked glycosylation site to be required for QSOX1 secretion from fibroblasts and other cell types.
31325506	4	24	gly	sialylated	1197:1206	arg1	no hybrid-type or sialylated N-glycans				no hybrid-type or sialylated N-glycans						Seventeen N-glycans comprising ten complex-type [Fucose0~2Hexose3~4N-acetylhexosamine1~6Sulfate0~1; 61.1% (the sum of the relative quantities of each N-glycan out of the total N-glycans)], two high-mannose-type (Hexose5~6N-acetylhexosamine2; 12.0%), and five paucimannose type (Fucose0~1Hexose3~4N-acetylhexosamine2~3; 26.9%) were identified, but no hybrid-type or sialylated N-glycans were found.
31264852	2	78	part_of	lipoxygenase	363:374	arg1	the lipoxygenase catalytic domains	lipoxygenase		the lipoxygenase catalytic domains		Fterm	Site	lipoxygenase		domains	While the lipoxygenase catalytic domains are structurally and functionally similar, these fungal enzymes are decorated with N-linked glycans.
31529350	1	25	gly	linked	246:251	arg1	protein AND glycan moieties	protein			glycan moieties	Fterm		protein			Congenital disorders of glycosylation (CDG) are genetic diseases characterized by deficient synthesis (CDG type I) and/or abnormal processing (CDG type II) of glycan moieties linked to protein and lipids.
30503329	0	69	gly	glycoprotein	85:96	arg1	cell wall glycoprotein N-linked galactomannan	cell wall glycoprotein N-linked galactomannan				Fterm		glycoprotein			Neurospora crassa family GH72 glucanosyltransferases function to crosslink cell wall glycoprotein N-linked galactomannan to cell wall lichenin.
29578688	5	1	gly	glycoproteins	1284:1296	arg1	HIV surface glycoproteins	HIV surface glycoproteins				Fterm		glycoproteins			To verify this proposition, we first designed and chemo-enzymatically synthesized a series of unusual hybrid-type N-glycan structures, which may exist on HIV surface glycoproteins through the host-guided N-glycosylation pathway.
29888865	13	65	gly	fucosylated	2269:2279	arg1	fucosylated LacdiNAc				fucosylated LacdiNAc						Although the proportion of biologically important epitopes common to all samples (i.e. sialylation and high-mannose) varied between samples, some recombinant products expressed distinct and immunologically relevant epitopes, such as LacdiNAc (LDN), fucosylated LacdiNAc (FucLDN), NeuGc, LewisX/Y and Galα1,3 Gal epitopes.
29888865	13	65	gly	fucosylated	2269:2279	arg1	FucLDN				FucLDN						Although the proportion of biologically important epitopes common to all samples (i.e. sialylation and high-mannose) varied between samples, some recombinant products expressed distinct and immunologically relevant epitopes, such as LacdiNAc (LDN), fucosylated LacdiNAc (FucLDN), NeuGc, LewisX/Y and Galα1,3 Gal epitopes.
30772453	4	57	gly	glycoprotein	1156:1167	arg1	higher glycoprotein titers	higher glycoprotein titers				Fterm		glycoprotein			Compared to E. coli cells carrying the same glycosylation machinery on extrachromosomal plasmids, glyco-recoded strains attached glycans to acceptor protein targets with equal or greater efficiency while exhibiting markedly better growth phenotypes and higher glycoprotein titers.
30503285	4	56	gly	glycosylation	899:911	arg2	one engineered site			one engineered site						site	The effectiveness of this two-plasmid synthetic operon system has been tested on three proteins with therapeutic potential: the native and an engineered version of the naturally O-glycosylated human interferon α-2b, as well as human growth hormone with one engineered site of glycosylation.
29880818	4	47	gly	proteins	491:498	arg1	the N-glycan profiles	proteins			the N-glycan profiles	Fterm		proteins			In the present study, the N-glycan profiles of membrane proteins were analyzed from adriamycin (ADR)-resistant U937/ADR cells and sensitive line U937 cells using mass spectrometry (MS).
30641224	0	97	gly	Glycosylation	0:12	arg1	human plasma lipoproteins	human plasma lipoproteins				Fterm		lipoproteins			Glycosylation of human plasma lipoproteins reveals a high level of diversity, which directly impacts their functional properties.
31572782	4	37	gly	receptor	498:505	arg1	the glycan pattern	receptor			the glycan pattern	Fterm		receptor			The employed methodology allowed dissecting the glycan pattern of the IgE high-affinity receptor (FcεRIα) expressed in human HEK 293 cells, identifying the presence and relative abundance of specific glycan epitopes.
31098625	12	56	gly	carried	1978:1984	arg1	Individual milk proteins AND unique glycan modifications	Individual milk proteins			unique glycan modifications	Fterm		proteins			Individual milk proteins carried unique glycan modifications that varied systematically in structure even with site specificity.
31033942	4	1	gly	fucosylated	739:749	arg1	the fucosylated HMO structures				the fucosylated HMO structures						We demonstrate here, a genetically encoded bacterial biosensor for the high-throughput, linkage-specific detection and quantification of the fucosylated HMO structures, 2'-fucosyllactose and 3-fucosyllactose, which we achieved via heterologous expression of fucosidases.
30560888	8	34	gly	afucosylated	1300:1311	arg1	bisected, afucosylated and galactosylated forms				bisected, afucosylated and galactosylated forms						Anti-Jo1-IgG enriched from eleven patients contained even significantly lower abundances of bisected, afucosylated and galactosylated forms compared to matched total-IgG.
31809011	3	12	gly	glycoproteins	329:341	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			However, the systematic quantitation of glycoproteins has remained largely unexplored.
30959459	2	62	gly	sialylation	447:457	arg1	N- and O-linked glycans				N- and O-linked glycans						By utilizing lectin microarray glycan profiling, Golgi pH and redox screens, we show here that hypoxia inhibits terminal sialylation of N- and O-linked glycans in a HIF- independent manner by lowering Golgi oxidative potential.
31881468	3	57	gly	glycosylation	628:640	arg1	the protein	the protein				Fterm		protein			Here we present molecular dynamics simulation studies of unfolding and folding of the protein MOG in both the absence and presence of N-glycan in order to understand the role of glycosylation in the stability and flexibility of the protein.
30003921	7	74	gly	glycoproteins	914:926	arg1	asialofetuin	asialofetuin				Fterm		asialofetuin			Surface plasmon resonance revealed differential binding of BinA with glycoproteins (fetuin, asialofetuin and thyroglobulin) and affinity for simple sugars, l-fucose and l-arabinose.
30003921	7	74	gly	glycoproteins	914:926	arg1	fetuin	fetuin				Fterm		fetuin			Surface plasmon resonance revealed differential binding of BinA with glycoproteins (fetuin, asialofetuin and thyroglobulin) and affinity for simple sugars, l-fucose and l-arabinose.
30003921	7	74	gly	glycoproteins	914:926	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Surface plasmon resonance revealed differential binding of BinA with glycoproteins (fetuin, asialofetuin and thyroglobulin) and affinity for simple sugars, l-fucose and l-arabinose.
30513259	3	11	gly	glycosylated	557:568	arg1	gFc	Fc		region		Cterm		Fc		region	To confirm this hypothesis, we examined the small-angle X-ray scattering (SAXS) profile of the glycosylated Fc region (gFc) and aglycosylated Fc region (aFc) in solution.
30513259	3	53	gly	aglycosylated	590:602	arg1	aglycosylated Fc region	Fc		region		Cterm		Fc		region	To confirm this hypothesis, we examined the small-angle X-ray scattering (SAXS) profile of the glycosylated Fc region (gFc) and aglycosylated Fc region (aFc) in solution.
31776339	5	34	gly	motifs	808:813	arg1	23 unique glycan motifs				23 unique glycan motifs						We demonstrate GlycoPRIME by constructing 37 putative protein glycosylation pathways, creating 23 unique glycan motifs, 18 of which have not yet been synthesized on proteins.
31122132	2	87	gly	sialylated	695:704	arg1	incompletely sialylated N-linked glycans				incompletely sialylated N-linked glycans						However, the transition of IgA into clinical development has been challenged by complex expression and characterization, as well as rapid serum clearance that is thought to be mediated by glycan receptor scavenging of recombinantly produced IgA monomer bearing incompletely sialylated N-linked glycans.
30737276	0	39	gly	variants	41:48	arg1	The N-glycan structures	variants			The N-glycan structures	Fterm		variants			The N-glycan structures of the antigenic variants of chlorovirus PBCV-1 major capsid protein help to identify the virus-encoded glycosyltransferases.
29572115	9	16	part_of	IgG	1319:1321	arg1	IgG glycome composition	IgG		IgG glycome composition		Cterm	Site	IgG		position	This indicates that long-acting factors affecting IgG glycome composition are among the underlying mechanisms of RA and that decreased galactosylation is a pre-existing risk factor involved in the disease development.
30275012	4	78	gly	has	554:556	arg1	a C. difficile strain AND a complex glycan	a C. difficile strain			a complex glycan	Fterm		strain			Here, we show that a C. difficile strain of S-layer cassette type 11, Ox247, has a complex glycan attached via an O-linkage to Thr-38 of the S-layer low-molecular-weight subunit.
30275012	4	65	gly	attached	575:582	arg1	Thr-38 AND a complex glycan	subunit		Thr-38	a complex glycan	Fterm		subunit		Thr-38	Here, we show that a C. difficile strain of S-layer cassette type 11, Ox247, has a complex glycan attached via an O-linkage to Thr-38 of the S-layer low-molecular-weight subunit.
30074304	2	16	gly	polymers	465:472	arg1	serine			serine	serine		AminoAcid			serine	These modifications occur most commonly as one of three major classes: N-linked glycosylation on asparagine residues, O-linked glycosylation on serine or threonine residues, or as glycosaminoglycan oligosaccharide polymers on serine.
30074304	2	67	gly	serine	395:400	arg1	residues			residues						threonine residues	These modifications occur most commonly as one of three major classes: N-linked glycosylation on asparagine residues, O-linked glycosylation on serine or threonine residues, or as glycosaminoglycan oligosaccharide polymers on serine.
30074304	2	55	gly	glycosylation	331:343	arg1	asparagine residues			asparagine residues						asparagine residues	These modifications occur most commonly as one of three major classes: N-linked glycosylation on asparagine residues, O-linked glycosylation on serine or threonine residues, or as glycosaminoglycan oligosaccharide polymers on serine.
30074304	2	51	gly	glycosylation	378:390	arg1	threonine			threonine residues						threonine residues	These modifications occur most commonly as one of three major classes: N-linked glycosylation on asparagine residues, O-linked glycosylation on serine or threonine residues, or as glycosaminoglycan oligosaccharide polymers on serine.
30074304	2	51	gly	glycosylation	378:390	arg1	serine			serine						serine	These modifications occur most commonly as one of three major classes: N-linked glycosylation on asparagine residues, O-linked glycosylation on serine or threonine residues, or as glycosaminoglycan oligosaccharide polymers on serine.
30503329	6	13	gly	glycoproteins	897:909	arg1	the glycoproteins	the glycoproteins				Fterm		glycoproteins			First, N-linked oligosaccharides present on the glycoproteins are modified by the addition of a galactomannan.
30503329	6	30	gly	present	882:888	arg1	the glycoproteins AND N-linked oligosaccharides	the glycoproteins			N-linked oligosaccharides	Fterm		glycoproteins			First, N-linked oligosaccharides present on the glycoproteins are modified by the addition of a galactomannan.
29885470	4	89	gly	glycoproteins	663:675	arg1	glycans	glycoproteins			glycans	Fterm		glycoproteins			This new method employs aqueous ammonia solution containing NaBH3CN as the reaction medium to release glycans from glycoproteins as 1-amino-alditol forms.
30315110	0	32	gly	glycosylation	87:99	arg1	a bacterial lipopolysaccharide				a bacterial lipopolysaccharide						Structural and functional characterization of a modified legionaminic acid involved in glycosylation of a bacterial lipopolysaccharide.
31040211	2	29	gly	glycoprotein	384:395	arg1	viral envelope glycoprotein	viral envelope glycoprotein				Fterm		glycoprotein			However, this effort has proven challenging because HCV evades neutralizing antibodies (NAbs) through molecular features of viral envelope glycoprotein E2, including hypervariable region 1 (HVR1) and N-linked glycans.
31914594	9	36	gly	3-fucosylated	1488:1500	arg1	3-fucosylated glycans				3-fucosylated glycans						In conclusion, this study unveils biochemical, topological, and functional features of a hypoxia-regulated galectin in AT, which modulates endothelial cell function through recognition of 3-fucosylated glycans.
29703890	3	54	gly	glycopeptides	452:464	arg2	glycopeptides			glycopeptides						glycopeptides	Chemical methods based on reversible covalent interactions between boronic acid and glycans have great potential to enrich glycopeptides, but the binding affinity is typically not strong enough to capture low-abundance species.
31062865	9	22	gly	O-glycopeptides	1864:1878	arg2	O-glycopeptides			O-glycopeptides						O-glycopeptides	For O-glycopeptides, both media produced predominantly three structures, N1F1F0SOG0, N1H1F0S1G0, and N1H1F0S2G0, with lesser amounts of other structures.
29924315	8	43	gly	sialylated	1499:1508	arg1	sialylated KS chains				sialylated KS chains						Treating human tracheal extracts with sialidase or keratanase eliminated Siglec-8 binding, indicating sialylated KS chains as Siglec-8-binding determinants.
29924315	8	43	gly	sialylated	1499:1508	arg1	Siglec-8-binding determinants				Siglec-8-binding determinants						Treating human tracheal extracts with sialidase or keratanase eliminated Siglec-8 binding, indicating sialylated KS chains as Siglec-8-binding determinants.
29321476	6	48	gly	released	771:778	arg1	extracted glycoproteins AND Glycans	extracted glycoproteins			Glycans	Fterm		glycoproteins			Glycans were released from extracted glycoproteins and analyzed by LC-MS/MS.
29321476	6	66	gly	glycoproteins	795:807	arg1	extracted glycoproteins	extracted glycoproteins				Fterm		glycoproteins			Glycans were released from extracted glycoproteins and analyzed by LC-MS/MS.
30318233	2	27	gly	protein	324:330	arg1	total sugar	protein			total sugar	Fterm		protein			The chemical composition of SP composed of 57 ± 0.29% of total sugar, 1.14 ± 0.28% of protein and 25.6 ± 0.45% of sulfate.
29333671	1	11	gly	glycopeptides	267:279	arg1	glycans			glycopeptides	glycans					glycopeptides	Glycosylation analysis of proteins from biological sources utilizing mass spectrometry based approaches is challenging due to the relatively low abundance of glycopeptides, the structural diversity of glycans, and the coexisting matrices.
30104209	4	37	gly	β-mannosylation	1001:1015	arg1	the N-glycans				the N-glycans						Similarly to recent in-depth studies on other insect species, previously overlooked glucuronic acid termini, sulfation of mannose residues and core β-mannosylation of the N-glycans were found; additionally, a relatively rare zwitterionic modification with phosphoethanolamine is present, in contrast to the phosphorylcholine occurring in lepidopteran species.
30104209	4	37	gly	β-mannosylation	1001:1015	arg1	mannose residues				mannose residues						Similarly to recent in-depth studies on other insect species, previously overlooked glucuronic acid termini, sulfation of mannose residues and core β-mannosylation of the N-glycans were found; additionally, a relatively rare zwitterionic modification with phosphoethanolamine is present, in contrast to the phosphorylcholine occurring in lepidopteran species.
31246420	9	81	gly	sialylated	1383:1392	arg1	labile sialylated structures				labile sialylated structures						This strategy was not as effective with labile sialylated structures; instead, it was observed that the optimal collision energy for the m/z 290.1 sialic acid B-fragment differed consistently between sialic acid isomers, allowing differentiation between isomers when fragmentation spectra were insufficient.
30336974	4	52	gly	glycoproteins	799:811	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			MTOG is initiated by the addition of N-acetyl-α-d-galactosamine (GalNAc) to Ser/Thr of glycoproteins.
30385505	0	69	gly	glycoproteins	30:42	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Galectin binding to cells and glycoproteins with genetically modified glycosylation reveals galectin-glycan specificities in a natural context.
30500162	10	54	gly	glycopeptides	1400:1412	arg2	glycopeptides			glycopeptides						glycopeptides	Finally, we evaluated ELISA screens against glycopeptides in comparison with glycoproteins, as well as against elaborated arrays displaying synthetic Neu5Gc-glycans.
30500162	10	62	gly	glycoproteins	1433:1445	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Finally, we evaluated ELISA screens against glycopeptides in comparison with glycoproteins, as well as against elaborated arrays displaying synthetic Neu5Gc-glycans.
30500162	8	6	part_of	glycoproteins	1196:1208	arg1	glycopeptides	glycoproteins		glycopeptides		Fterm	Site	glycoproteins		glycopeptides	First, Neu5Gc-positive or Neu5Gc-deficient mouse strains were used to generate glycopeptides from serum glycoproteins.
31130941	14	91	gly	Asn459	2698:2703	arg1	the Asn459 N-glycan			Asn459	the Asn459 N-glycan					Asn459	Here we have identified and characterized a novel protease from B. bacteriovorus, facilitating the study of plasma IgA by cleaving the Fc-tail, including the Asn459 N-glycan.
29408873	0	35	part_of	Fc	12:13	arg1	Mouse IgG2c Fc loop residues	Fc		Mouse IgG2c Fc loop residues		Cterm	Site	Fc		residues	Mouse IgG2c Fc loop residues promote greater receptor-binding affinity than mouse IgG2b or human IgG1.
29408873	0	81	part_of	IgG2c	6:10	arg1	Mouse IgG2c Fc loop residues	IgG2c		Mouse IgG2c Fc loop residues		Cterm	Site	IgG2c		residues	Mouse IgG2c Fc loop residues promote greater receptor-binding affinity than mouse IgG2b or human IgG1.
29931153	9	54	part_of	glycoproteins	1652:1664	arg1	unstructured loop regions	glycoproteins		unstructured loop regions		Fterm	Site	glycoproteins		regions	Most notably, γ-branched amino acid residues (Asn+Asp+Leu) occur more frequently on unstructured loop regions of immature glycoproteins.
31751705	3	65	gly	Asn-oligosaccharide	793:811	arg1	Asn-oligosaccharide			Asn	Asn-oligosaccharide					Asn	Neoglycopolymers were synthesized such that the α-amino groups of Asn-oligosaccharide were coupled to the carboxyl groups of poly-γ-L-glutamic acid (γ-L-PGA) with 4-(4,6-Dimethoxy-1,3,5-triazin-2-yl)-4-methylmorpholinium chloride n-hydrate (DMT-MM).
31654087	7	22	gly	sialylated	946:955	arg1	their sialylated forms				their sialylated forms						Rosmarinic acid inhibited the expression of Tn, T antigens and their sialylated forms, fucosylated antigens, di NAclactosamine, and mannose antigens.
30513259	4	7	part_of	Fc	807:808	arg1	the Fc region	Fc		the Fc region		Cterm	Site	Fc		region	Conformational characteristics of the CH2 domain orientation were validated by comparison with SAXS profiles theoretically calculated from multiple crystal structures of the Fc region with different CH2 domain orientations.
30412755	1	28	part_of	PPy/C-MWCNT	290:300	arg1	various binary composition	PPy		various binary composition		OGER	Site	PPy	P01298	position	A highly competent material, based on poly lactic acid (PLLA) grafted hydroxypropyl guar gum (HPG-g-PLLA) and polypyrrole/carboxylated multiwalled carbon nanotube (PPy/C-MWCNT) composite of various binary composition and copolymer of one of these nanocomposites have been synthesized successfully by in-situ polymerization.
30412755	1	28	part_of	PPy/C-MWCNT	290:300	arg1	polypyrrole/carboxylated multiwalled carbon nanotube (PPy/C-MWCNT) composite	PPy		polypyrrole/carboxylated multiwalled carbon nanotube (PPy/C-MWCNT) composite		OGER	Site	PPy	P01298	composite	A highly competent material, based on poly lactic acid (PLLA) grafted hydroxypropyl guar gum (HPG-g-PLLA) and polypyrrole/carboxylated multiwalled carbon nanotube (PPy/C-MWCNT) composite of various binary composition and copolymer of one of these nanocomposites have been synthesized successfully by in-situ polymerization.
31384044	4	11	gly	glycoproteins	1001:1013	arg1	159 glycoproteins	159 glycoproteins				Fterm		glycoproteins			Applying the Glyco-DIA library to human serum without enrichment for glycopeptides enabled us to identify and quantify 269 distinct glycopeptide sequences bearing up to 5 different core1 O-glycans from 159 glycoproteins in a SingleShot analysis.
31384044	4	18	gly	glycopeptide	927:938	arg2	269 distinct glycopeptide sequences			269 distinct glycopeptide sequences						glycopeptide sequences	Applying the Glyco-DIA library to human serum without enrichment for glycopeptides enabled us to identify and quantify 269 distinct glycopeptide sequences bearing up to 5 different core1 O-glycans from 159 glycoproteins in a SingleShot analysis.
31384044	4	19	gly	glycopeptides	864:876	arg2	glycopeptides			glycopeptides						glycopeptides	Applying the Glyco-DIA library to human serum without enrichment for glycopeptides enabled us to identify and quantify 269 distinct glycopeptide sequences bearing up to 5 different core1 O-glycans from 159 glycoproteins in a SingleShot analysis.
30565163	4	37	part_of	2,4A3-H2O	1316:1324	arg1	(2,4A3-H2O) fragment	2,4A3-H2O		(2,4A3-H2O) fragment		Cterm	Site	2,4A3-H2O		fragment	We found that 2,4A3 cross-ring fragment at the terminal monosaccharide in sialyllactoses, sialyllactosamines, and sialyl pentasaccharides is highly abundant in the MS/MS spectra of [M+2X-H]+ species of α2,6-NeuAc glycans, while (2,4A3-H2O) fragment is highly abundant in α2,3-NeuAc moiety.
30342133	9	40	part_of	protein	1399:1405	arg1	Ardeh residue	protein		Ardeh residue		Fterm	Site	protein		residue	The results showed that Ardeh residue could be a potential alternative renewable plant protein source to be used as a food ingredient for the enhancement of food nutritional value and quality especially after conjugation with maltodextrin.
30904681	0	13	part_of	β-2-glycoprotein-1	96:113	arg1	multiple glycosylation sites	-2-glycoprotein-1		multiple glycosylation sites		PUBTATOR	Site	-2-glycoprotein-1	350	sites	Simultaneous characterization of SNPs and N-glycans from multiple glycosylation sites of intact β-2-glycoprotein-1 (B2GP1) by ESI-qTOF-MS.
30484241	4	4	gly	glycoproteins	669:681	arg1	glycoproteins	glycoproteins				Fterm		structure of glycoproteins			Based on experimental results, it can be suggested that N-glycans stabilize the structure of glycoproteins.
29620509	8	28	gly	deglycosylation	1224:1238	arg1	native N-glycan protein				native N-glycan protein						The soluble and active form of purified Necl-4 protein was obtained after deglycosylation of native N-glycan protein with an expression level of 4 mg/L culture and purity of 95%.
30813247	4	27	gly	glycoprotein	802:813	arg1	only one single viral glycoprotein	only one single viral glycoprotein				Fterm		glycoprotein			This situation is at variance with the current notion since a live vaccine, causing an active virus infection, should be far more efficient than a subunit vaccine based on only one single viral glycoprotein.
31244828	4	12	gly	N-glycosylation	734:748	arg2	one known N-glycosylation site			one known N-glycosylation site						site	MOG has one known N-glycosylation site at N31 located in the BC loop linking two beta-sheets.
31244828	4	12	gly	N-glycosylation	734:748	arg2	N31			N31						N31	MOG has one known N-glycosylation site at N31 located in the BC loop linking two beta-sheets.
30146545	2	1	gly	glycoproteins	279:291	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Due to the complex nature of glycan structures on glycoproteins, assessing the configuration and positions of the glycosidic linkages of a glycan is a subject of considerable interest.
29740059	2	13	gly	glycoproteins	310:322	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			N-glycan branching on glycoproteins increases the number of potential attachment sites for sialic acid.
29740059	2	45	gly	branching	297:305	arg1	glycoproteins	glycoproteins			branching	Fterm		glycoproteins			N-glycan branching on glycoproteins increases the number of potential attachment sites for sialic acid.
30737276	6	15	gly	having	1004:1009	arg1	antigenic variants AND truncated glycan structures	antigenic variants			truncated glycan structures	Fterm		variants			We determined the GT functions by comparing the WT glycan structures from PBCV-1 with those from a set of PBCV-1 spontaneous GT gene mutants resulting in antigenic variants having truncated glycan structures.
31539564	11	56	gly	glycoprotein	1798:1809	arg1	glycoprotein cultivation processes	glycoprotein cultivation processes				Fterm		glycoprotein			The GReBA can be used as a guidance for development of glycoprotein cultivation processes.
29992770	3	77	gly	N-glycopeptides	395:409	arg2	specific N-glycopeptides			specific N-glycopeptides						N-glycopeptides	The authors aimed to use mass-spectrometry (MS) technology to find specific N-glycopeptides potentially serving as serum biomarkers for preclinical OSCC screening.
29297680	13	22	gly	glycosylations	2562:2575	arg1	β-mannosylation/rhamnosylation				β-mannosylation/rhamnosylation						Exploiting the former glycosyloxypyrylium intermediate, SN2-type glycosylations were realized in specific cases, such as β-mannosylation/rhamnosylation.
30621113	1	60	gly	N-glycosylation	150:164	arg1	blood factors	blood factors				Fterm		factors			N-glycosylation has been shown to affect the pharmacokinetic properties of several classes of biologics, including monoclonal antibodies, blood factors, and lysosomal enzymes.
30621113	1	60	gly	N-glycosylation	150:164	arg1	lysosomal enzymes	lysosomal enzymes				Fterm		enzymes			N-glycosylation has been shown to affect the pharmacokinetic properties of several classes of biologics, including monoclonal antibodies, blood factors, and lysosomal enzymes.
30389790	11	21	gly	glycoproteins	1898:1910	arg1	G3M9-bearing glycoproteins	G3M9-bearing glycoproteins				Fterm		glycoproteins			We propose that accumulation of G3M9-bearing glycoproteins is toxic and at least partially responsible for defects observed in MOGS-CDG.
31034685	10	8	gly	glycopeptides	1611:1623	arg2	isomeric glycopeptides			isomeric glycopeptides						glycopeptides	PGC/MS/MS also enabled comprehensive characterization of protein sialoglycosylation as isomeric glycopeptides with different combinations of α2-3- and α2-6-linked sialic acids can be separated and the ratios of each combination were verified by exoglycosidase digestion.
30325416	5	50	gly	found	1248:1252	arg2	the Fc region AND the larger N-glycan species			the Fc region	the larger N-glycan species					region	Here we report the results of a systematic study, based on extensive molecular dynamics simulations in excess of 62 μs of cumulative simulation time, on the effect of sequence on the structure and dynamics of increasingly larger, complex biantennary N-glycoforms isolated from the protein, i.e. from chitobiose to the larger N-glycan species commonly found in the Fc region of human IgGs.
30325416	5	63	gly	N-glycoforms	1147:1158	arg1	increasingly larger, complex biantennary N-glycoforms				increasingly larger, complex biantennary N-glycoforms						Here we report the results of a systematic study, based on extensive molecular dynamics simulations in excess of 62 μs of cumulative simulation time, on the effect of sequence on the structure and dynamics of increasingly larger, complex biantennary N-glycoforms isolated from the protein, i.e. from chitobiose to the larger N-glycan species commonly found in the Fc region of human IgGs.
31141660	3	59	gly	fucosylated	426:436	arg1	fucosylated N-glycans				fucosylated N-glycans						In this work, we propose utility of phenylhydrazine (PHN) labeling for structural studies of fucosylated N-glycans by tandem MALDI mass spectrometry (MS) in the positive ion mode.
31869330	2	93	gly	glycosylate	456:466	arg1	proteins	proteins				Fterm		proteins			In an effort to better understand the evolution and function of protein glycosylation operating there, we aimed to determine if other human-restricted, Neisseria species similarly glycosylate proteins and if so, to assess the levels of glycoform diversity.
30444974	8	74	part_of	ubiquitin	1384:1392	arg1	the ubiquitin biochemical composition	ubiquitin		the ubiquitin biochemical composition		Fterm	Site	ubiquitin		position	Finally, we propose a set of possible high mannose N-glycan structures that will help to elucidate the ubiquitin biochemical composition and may well represent good targets for anti-amoebic drugs.
31914594	0	24	gly	3-fucosylated	94:106	arg1	3-fucosylated glycans				3-fucosylated glycans						An adipose tissue galectin controls endothelial cell function via preferential recognition of 3-fucosylated glycans.
29858715	9	30	gly	glycoproteins	1237:1249	arg1	specific glycoproteins	specific glycoproteins				Fterm		glycoproteins			So far, for specific glycoproteins Ley epitopes had only been reported on O-glycans.
29792883	6	70	gly	glycoforms	919:928	arg1	met			met						met	Sixty-three glycoforms met our criteria for relative quantification and were extracted from the raw data with the software MassyTools.
29976678	3	94	gly	glycoprotein	501:512	arg1	the premembrane (prM) and envelope (E) glycoprotein regions	the premembrane (prM) and envelope (E) glycoprotein regions				Fterm		glycoprotein			We first created a panel of ZIKV mutants with the FLAG epitope inserted in the premembrane (prM) and envelope (E) glycoprotein regions.
30327321	0	1	part_of	domain	15:20	arg1	collagen XVIII	collagen XVIII		domain		PUBTATOR	Site	collagen XVIII	80781	domain	The N-terminal domain of unknown function (DUF959) in collagen XVIII is intrinsically disordered and highly O-glycosylated.
30395580	10	56	gly	N-glycosylation	1445:1459	arg2	The N-glycosylation sites			The N-glycosylation sites						sites	The N-glycosylation sites are surprisingly conserved among asco-laccases and in most cases the glycan displays extensive interactions with the protein.
31111416	2	73	gly	glycosite	354:362	arg2	glycosite occupancy			glycosite occupancy						glycosite	A comprehensive LC-MS/MS peptide mapping analysis was applied to assess the primary sequence, glycosylation profiles, and glycosite occupancy of Env to ensure the adequate mimicking of the native immunogen.
30513306	2	20	gly	glycoprotein	295:306	arg1	an endocuticle structural glycoprotein gene	an endocuticle structural glycoprotein gene				Fterm		glycoprotein			In the present study, an endocuticle structural glycoprotein gene, LmAbd-9, was characterized based on the Locusta migratoria transcriptome.
31640540	10	103	gly	glycosylated	1775:1786	arg1	glycosylated protein	glycosylated protein				Fterm		protein			CONCLUSIONS Glycosylator was used to generate models of glycosylated protein without steric clashes.
31759178	2	5	gly	N-glycopeptide	298:311	arg2	intact N-glycopeptide search engine			intact N-glycopeptide search engine						N-glycopeptide	Our recent development of intact N-glycopeptide search engine GPSeeker has enabled relatively quantitative structure-specific characterization of differentially expressed intact N-glycopeptides (DEGPs) with isotopic labeling of the peptide backbones and structure-specific fragment ions of the N-glycan moieties.
31759178	2	123	gly	N-glycopeptides	443:457	arg2	differentially expressed intact N-glycopeptides (DEGPs)			differentially expressed intact N-glycopeptides (DEGPs)						N-glycopeptides	Our recent development of intact N-glycopeptide search engine GPSeeker has enabled relatively quantitative structure-specific characterization of differentially expressed intact N-glycopeptides (DEGPs) with isotopic labeling of the peptide backbones and structure-specific fragment ions of the N-glycan moieties.
29730764	8	64	gly	glycosylated	1408:1419	arg1	highly glycosylated peptides			highly glycosylated peptides						peptides	We found that ETD efficiency is still a limiting factor, and for highly glycosylated peptides, the only information revealed in EThcD was related to the glycan structures.
29927116	3	75	gly	regions	557:563	arg1	individual glycans			regions	individual glycans					regions	This technique allows for the precise study of individual glycans at different regions of the glycocalyx, and may be useful for interrogating glycan interactions in infection or immunity or in stem cell differentiation.
30640124	2	48	gly	linked	387:392	arg1	proteins AND the glycans	proteins			the glycans	Fterm		proteins			Unfortunately, this strategy is scarcely explored because receptors recognizing the glycans linked to proteins are challenging to discover.
29580922	11	10	part_of	sites	1753:1757	arg1	haptoglobin	haptoglobin		sites		PUBTATOR	Site	haptoglobin	3240	sites	CONCLUSIONS: Tri-antennary and sialylated N-glycans on haptoglobin at the Asn207 and Asn211 sites were abundant in SSCs and characteristic of extreme human longevity.
31669606	7	43	gly	glycoforms	1024:1033	arg1	Man5				Man5						The HM and Man5 glycoforms display increased affinity for FcγRIIIA by at least 14.7-fold compared with GlcNAc1 IgG4-Fc.
31669606	7	43	gly	glycoforms	1024:1033	arg1	HM				HM						The HM and Man5 glycoforms display increased affinity for FcγRIIIA by at least 14.7-fold compared with GlcNAc1 IgG4-Fc.
29532326	9	45	gly	N-glycosylation	1205:1219	arg2	two more N-glycosylation sites			two more N-glycosylation sites						sites	In addition to the known N-glycosylation sites, two more N-glycosylation sites were detected on C8.
29532326	9	83	gly	N-glycosylation	1173:1187	arg2	the known N-glycosylation sites			the known N-glycosylation sites						sites	In addition to the known N-glycosylation sites, two more N-glycosylation sites were detected on C8.
31601857	2	35	gly	glycoprotein	387:398	arg1	serum α1-acid glycoprotein	glycoprotein			glycan structures	Fterm		glycoprotein			Recently, we demonstrated that glycan structures of serum α1-acid glycoprotein (AGP) changed dramatically in cancer patients and that α1,3fucosylated AGP (fAGP) levels increased along with disease progression and decreased responding to chemotherapy treatments.
29463753	0	42	part_of	protein	31:37	arg1	Signal peptide	protein		Signal peptide		Fterm	Site	protein		peptide	Signal peptide of HIV envelope protein impacts glycosylation and antigenicity of gp120.
30151520	1	89	gly	glycosylated	247:258	arg1	glycosylated peptides			glycosylated peptides						peptides	Fully realizing the capabilities of tandem mass spectrometry (MS/MS) for analysis of glycosylated peptides will require further understanding of the unimolecular dissociation chemistry that dictates their fragmentation pathways.
30030954	6	42	gly	sialylated	1071:1080	arg1	sialylated glycans				sialylated glycans						These results suggest that sialylated glycans play important role in the antimicrobial function of lactoferrin.
29603480	8	66	gly	epitope	1286:1292	arg1	the context of a complex N-glycan results in a loss of inhibitory potential				the context of a complex N-glycan results in a loss of inhibitory potential						Our studies show that although SLex can inhibit the binding of spermatozoa, presenting this epitope in the context of a complex N-glycan results in a loss of inhibitory potential, and in this context only SLex -Lex can make productive interactions.
31098625	10	18	gly	fucosylated + sialylated	1686:1709	arg1	high-mannose, undecorated, fucosylated, sialylated, and combined fucosylated + sialylated glycans				high-mannose, undecorated, fucosylated, sialylated, and combined fucosylated + sialylated glycans						Fucosylated glycans of lactoferrin and high-mannose, undecorated, fucosylated, sialylated, and combined fucosylated + sialylated glycans of secretory immunoglobulin A increased during lactation even when the concentrations of the parent proteins decreased.
31098625	10	23	gly	sialylated	1661:1670	arg1	high-mannose, undecorated, fucosylated, sialylated, and combined fucosylated + sialylated glycans				high-mannose, undecorated, fucosylated, sialylated, and combined fucosylated + sialylated glycans						Fucosylated glycans of lactoferrin and high-mannose, undecorated, fucosylated, sialylated, and combined fucosylated + sialylated glycans of secretory immunoglobulin A increased during lactation even when the concentrations of the parent proteins decreased.
31098625	10	26	gly	fucosylated	1648:1658	arg1	high-mannose, undecorated, fucosylated, sialylated, and combined fucosylated + sialylated glycans				high-mannose, undecorated, fucosylated, sialylated, and combined fucosylated + sialylated glycans						Fucosylated glycans of lactoferrin and high-mannose, undecorated, fucosylated, sialylated, and combined fucosylated + sialylated glycans of secretory immunoglobulin A increased during lactation even when the concentrations of the parent proteins decreased.
29408873	5	69	gly	glycosylation	1102:1114	arg2	the Asn297 site			the Asn297 site						Asn297 site	Secondary structural elements surrounding the Asn297 site of glycosylation form longer beta strands in the truncated mIgG2c Fc glycoform when compared to mIgG2c with the complex-type N-glycan.
30904681	0	47	gly	sites	80:84	arg1	N-glycans			sites	N-glycans					sites	Simultaneous characterization of SNPs and N-glycans from multiple glycosylation sites of intact β-2-glycoprotein-1 (B2GP1) by ESI-qTOF-MS.
30904681	0	11	gly	glycosylation	66:78	arg2	multiple glycosylation sites	B2GP1		sites		PUBTATOR		B2GP1	350	sites	Simultaneous characterization of SNPs and N-glycans from multiple glycosylation sites of intact β-2-glycoprotein-1 (B2GP1) by ESI-qTOF-MS.
30904681	0	11	gly	glycosylation	66:78	arg2	multiple glycosylation sites	-2-glycoprotein-1		sites		PUBTATOR		-2-glycoprotein-1	350	sites	Simultaneous characterization of SNPs and N-glycans from multiple glycosylation sites of intact β-2-glycoprotein-1 (B2GP1) by ESI-qTOF-MS.
31776333	5	23	gly	origin	843:848	arg1	defined glycans	origin			defined glycans	Fterm		origin			The Glycoli platform leverages a recently discovered site-specific polypeptide glycosyltransferase together with variable glycosyltransferase modules to synthesize defined glycans, of bacterial or mammalian origin, directly onto recombinant proteins in the E. coli cytoplasm.
30611426	3	8	gly	attached	333:340	arg2	proteins AND The carbohydrates	proteins			The carbohydrates	Fterm		proteins			The carbohydrates covalently attached to proteins during maturation in the cell directly impact protein structure and function as integral and indispensable components.
31381874	6	17	gly	glycopeptides	1186:1198	arg2	glycopeptides			glycopeptides						glycopeptides	The number of azide groups incorporated onto the IgM glycans were characterized by mass spectrometry of the enzymatically released glycans and glycopeptides.
30898876	4	64	gly	glycoproteins	1065:1077	arg1	the glycoproteins	the glycoproteins				Fterm		glycoproteins			Using isotope-coded glycosylation site-specific tagging (IGOT)-LC/MS analysis of Lec8 Chinese hamster cells lacking galactosylation and of cells transfected with the B3GALNT2 gene, we identified the glycoproteins that carry B3GALNT2-generated type-I LDN in their N-glycans.
30898876	4	35	gly	carry	1084:1088	arg1	the glycoproteins AND B3GALNT2-generated type-I LDN	the glycoproteins			B3GALNT2-generated type-I LDN	Fterm		glycoproteins			Using isotope-coded glycosylation site-specific tagging (IGOT)-LC/MS analysis of Lec8 Chinese hamster cells lacking galactosylation and of cells transfected with the B3GALNT2 gene, we identified the glycoproteins that carry B3GALNT2-generated type-I LDN in their N-glycans.
30315106	0	91	gly	contains	62:69	arg1	pancreatic carboxyl-ester lipase AND core 1/core 2 O-glycans	carboxyl-ester lipase		domain	core 1/core 2 O-glycans	PUBTATOR		carboxyl-ester lipase	P19835	domain	The mucinous domain of pancreatic carboxyl-ester lipase (CEL) contains core 1/core 2 O-glycans that can be modified by ABO blood group determinants.
31501225	6	46	gly	glycopeptides	973:985	arg1	IgA2	IgA2		glycopeptides		OGER		IgA2	P01877	glycopeptides	TPLTAN205ITK (H5N5S1F1) and (H5N4S2F1) corresponding to the glycopeptides of IgA2 were significantly elevated in serum from patients with HBV infection and even higher in HBV-related LC patients, as compared with healthy donor.
30994122	0	51	gly	asparagine	59:68	arg1	an N-GlcNAz asparagine building block			asparagine	an N-GlcNAz asparagine building block					asparagine	Efficient synthesis and enzymatic extension of an N-GlcNAz asparagine building block.
31151515	5	30	part_of	contained	836:844	arg1	CSF AND abundant rhamnogalacturonan regions	CSF		abundant rhamnogalacturonan regions		OGER	Site	CSF		regions	CSF and SSF, rich in neutral sugars side chains, contained abundant rhamnogalacturonan regions.
29343613	9	14	part_of	lectin	1479:1484	arg1	the lectin domain	lectin		the lectin domain		Fterm	Site	lectin		domain	That the lectin domain in DAVEIs can utilize MVN without loss of virolytic function argues that restricted HIV-1 Env (envelope glycoprotein) glycan engagement is sufficient for virolysis.
30915686	9	22	gly	sialylated	1355:1364	arg1	sialylated N-glycan				sialylated N-glycan						Our results indicated that sialylated N-glycan was identified as a biomarker associated with depressive symptoms, which may have utility as a candidate biomarker for the clinical diagnosis and monitoring of depression.
31154130	6	3	gly	glycopeptides	953:965	arg2	subclass-specific glycopeptides			subclass-specific glycopeptides						glycopeptides	Secondly, subclass-specific glycopeptides were identified on the basis of high-resolution MS and MS/MS data by using ultra high performance liquid chromatography (UHPLC) coupled to Q-TOF-MS.
31208374	13	1	gly	glycoproteins	2390:2402	arg1	the intact glycoproteins	the intact glycoproteins				Fterm		glycoproteins			Further studies on direct identification of the intact glycoproteins using a glycoprteomics approach will provide a deeper understanding of specific biomarkers towards their clinical utility.
31370181	5	32	gly	occupied	973:980	arg2	some sites			some sites						sites	The glycosylation profile differed at each N-site, some sites being occupied exclusively by oligomannosidic type N-glycans and others by complex N-glycans processed in some cases with additional Lewis A structures (BY-2) or with beta-1,4-galactose and sialic acid (CHO).
31914594	4	29	gly	3-fucosylated	665:677	arg1	3-fucosylated structures				3-fucosylated structures						Here, we reveal biochemical and biophysical determinants of Gal-12 structure, including its preferential recognition of 3-fucosylated structures, a unique feature among members of the galectin family.
29617676	3	10	gly	found	643:647	arg1	position 459 AND sialic acid			position 459	sialic acid					position 459	This antiviral activity is mediated by sialic acid found in the complex N-linked glycans at position 459.
31743713	9	21	part_of	Araf	1135:1138	arg1	some Araf and Rhap residues	Araf		some Araf and Rhap residues		OGER	Site	Araf	P10398	residues	Structural and linkage analysis by GC-MS and NMR spectroscopy suggested that PZMP3-2 was a homogalacturonan (HG)-like pectic polysaccharide branched at C-2 with some Araf and Rhap residues.
31000718	4	10	gly	mannosylation	644:656	arg1	phytanyl pyrophosphate GlcNAc2				phytanyl pyrophosphate GlcNAc2						Endoplasmic reticulum mannosyltransferases (MTases) are expressed in E. coli and used for mannosylation of the dolichol mimic, phytanyl pyrophosphate GlcNAc2.
30115684	1	6	gly	glycoprotein	154:165	arg1	the envelope glycoprotein gp120	the envelope glycoprotein gp120				Fterm		glycoprotein			The glycan shield on the envelope glycoprotein gp120 of human immunodeficiency virus 1 (HIV-1) has drawn immense attention as a vulnerable site for broadly neutralizing antibodies (bNAbs) and for its significant impact on host adaptive immune response to HIV-1.
30138037	5	90	gly	-glycoprotein	596:608	arg1	mannosyl (α-1,3-)-glycoprotein β-1,2- N-acetylglucosaminyltransferase	mannosyl (α-1,3-)-glycoprotein β-1,2- N-acetylglucosaminyltransferase				Fterm		-glycoprotein			The glycosyltransferase gene, mannosyl (α-1,3-)-glycoprotein β-1,2- N-acetylglucosaminyltransferase (Mgat1), whose product, N-acetylglucosaminyltransferase 1 (GlcNAcT1) is necessary for the formation of hybrid and complex N-glycan structures in the medial Golgi, was shown to be at reduced levels in human end-stage cardiomyopathy, thus making Mgat1 an attractive target for investigating the role of hybrid/complex N-glycosylation in cardiac pathogenesis.
30959459	6	48	gly	sialylation	1387:1397	arg1	O-linked glycans				O-linked glycans						Structure comparisons revealed similar disulfide bonds also in ST3Gal-I, suggesting that this O-glycan and glycolipid modifying sialyltransferase is also sensitive to hypoxia and thereby contribute to attenuated sialylation of O-linked glycans in hypoxic cells.
30513259	2	36	part_of	Fc	451:452	arg1	the Fc region	Fc		the Fc region		Cterm	Site	Fc		region	Alteration of these protein properties upon the removal of the N-linked glycan has often been explained by the alteration of the CH2 domain orientation in the Fc region.
31208374	10	84	gly	core-fucosylated	1674:1689	arg1	two core-fucosylated and agalactosylated glycans				two core-fucosylated and agalactosylated glycans						N-glycans quantified form IgG confirmed their abundance in BC patients, of which two core-fucosylated and agalactosylated glycans (m/z 1591, 1794) could specifically distinguish (AUC = 0.944 and 0.921, p ≤ 0.001) stage II patients from NC.
30990348	0	44	gly	residues	30:37	arg1	Fc-glycan			residues in	Fc-glycan					residues in	Effects of terminal galactose residues in mannose α1-6 arm of Fc-glycan on the effector functions of therapeutic monoclonal antibodies.
30990348	0	44	gly	residues	30:37	arg1	mannose α1-6 arm			residues in	mannose α1-6 arm					residues in	Effects of terminal galactose residues in mannose α1-6 arm of Fc-glycan on the effector functions of therapeutic monoclonal antibodies.
31558607	1	36	part_of	precursor	255:263	arg1	a prodomain	proBDNF precursor		a prodomain		PUBTATOR	Site	proBDNF precursor	627	prodomain	Brain-derived neurotrophic factor (BDNF) is generated by proteolytic cleavage of a prodomain from the proBDNF precursor either intracellularly by furin-like proteases or extracellularly by plasmin or matrix metalloproteinases.
31117584	5	5	gly	N-glycopeptides	1102:1116	arg2	5 405 and 1 081 intact N-glycopeptides			5 405 and 1 081 intact N-glycopeptides						N-glycopeptides	In benchmark characterization of differentially expressed N-glycosylation in hepatocellular carcinoma HepG2 cells relative to LO2 cells, 5 405 and 1 081 intact N-glycopeptides with putative linkage structures were identified and quantified with isotopic dimethyl labeling and 2D liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis.
29603058	4	11	gly	position	1186:1193	arg1	N-glycan structures			position	N-glycan structures					position	Using the Skyline software, at least two diagnostic fragment ions of high specificity were validated for automated discrimination of sialylation and arm position in N-glycan structures, and sialylation in O-glycan structures, complementing existing structural diagnostic ions.
29603058	4	39	gly	position	1186:1193	arg1	sialylation			position	sialylation					position	Using the Skyline software, at least two diagnostic fragment ions of high specificity were validated for automated discrimination of sialylation and arm position in N-glycan structures, and sialylation in O-glycan structures, complementing existing structural diagnostic ions.
29603058	4	80	gly	sialylation	1166:1176	arg1	N-glycan structures				N-glycan structures						Using the Skyline software, at least two diagnostic fragment ions of high specificity were validated for automated discrimination of sialylation and arm position in N-glycan structures, and sialylation in O-glycan structures, complementing existing structural diagnostic ions.
29603058	4	44	gly	sialylation	1223:1233	arg1	arm position			position	sialylation					position	Using the Skyline software, at least two diagnostic fragment ions of high specificity were validated for automated discrimination of sialylation and arm position in N-glycan structures, and sialylation in O-glycan structures, complementing existing structural diagnostic ions.
29699572	3	36	part_of	IgG	563:565	arg1	IgG glycome composition	IgG		IgG glycome composition		Cterm	Site	IgG		position	IgG glycome composition in patients with IS (n = 78) and cerebral arterial stenosis (CAS) (n = 75) and controls (n = 77) were analyzed by ultra-performance liquid chromatography.
29441788	5	43	gly	N-glycosylation	670:684	arg2	all N-glycosylation sites	afamin		sites		PUBTATOR		afamin	173	sites	Fully nonglycosylated rhAFM was obtained by transfection of point-mutated cDNA to delete all N-glycosylation sites of afamin.
31790908	1	12	gly	glycosylated	134:145	arg1	a 35-kDa, glycosylated protein	a 35-kDa, glycosylated protein				Fterm		protein			The ICChI is a 35-kDa, glycosylated protein isolated from the latex of the weed Ipomoea carnea.
31569500	6	55	part_of	motifs	967:972	arg1	all enzymes	enzymes		motifs		Fterm	Site	enzymes		motifs	Multiple alignments of other eukaryotic GT-C families underlined the presence of similar conserved motifs in luminal loops, in all enzymes of the superfamily.
30937380	2	8	gly	Asn297	356:361	arg1	the conserved N-linked glycan			Asn297	the conserved N-linked glycan					Asn297	Streptococcus pyogenes secretes a unique endo-β-N-acetylglucosaminidase, EndoS2, which deglycosylates the conserved N-linked glycan at Asn297 on IgG Fc to eliminate its effector functions and evade the immune system.
30937380	2	13	gly	deglycosylates	308:321	arg1	the conserved N-linked glycan				the conserved N-linked glycan						Streptococcus pyogenes secretes a unique endo-β-N-acetylglucosaminidase, EndoS2, which deglycosylates the conserved N-linked glycan at Asn297 on IgG Fc to eliminate its effector functions and evade the immune system.
31541622	0	64	gly	O-glycoproteins	28:42	arg1	O-glycoproteins	O-glycoproteins				Fterm		O-glycoproteins			Precision mapping of N- and O-glycoproteins in viral resistant and susceptible strains of Bombyx mori.
31467031	2	45	part_of	proteins	268:275	arg1	The composition	proteins		The composition		Fterm	Site	proteins		position	The composition of serum proteins such as immunoglobulin G (IgG) strongly associates with disease including forms lacking a fucose modification of the crystallizable fragment (Fc) asparagine(N)-linked glycan that show increased effector function, however, virtually nothing is known about the composition of cell surface receptors or their bound ligands in situ because of low abundance in the circulating blood.
31467031	2	69	part_of	receptors	564:572	arg1	the composition	receptors		the composition		Fterm	Site	receptors		position	The composition of serum proteins such as immunoglobulin G (IgG) strongly associates with disease including forms lacking a fucose modification of the crystallizable fragment (Fc) asparagine(N)-linked glycan that show increased effector function, however, virtually nothing is known about the composition of cell surface receptors or their bound ligands in situ because of low abundance in the circulating blood.
29596458	9	96	gly	N-glycopeptides	1207:1221	arg2	Three hundred and sixty eight potential N-glycopeptides			Three hundred and sixty eight potential N-glycopeptides						N-glycopeptides	Three hundred and sixty eight potential N-glycopeptides were quantified by mass spectrometry and 149 were further selected for identification.
30983324	6	64	gly	sialylated	1301:1310	arg1	both phosphorylated and sialylated glycans				both phosphorylated and sialylated glycans						Indeed, we have successfully performed glycomic characterization of agalsidase-beta, a representative therapeutic enzyme containing both phosphorylated and sialylated glycans.
30983324	6	22	gly	containing	1266:1275	arg1	a representative therapeutic enzyme AND both phosphorylated and sialylated glycans	a representative therapeutic enzyme			both phosphorylated and sialylated glycans	Fterm		enzyme			Indeed, we have successfully performed glycomic characterization of agalsidase-beta, a representative therapeutic enzyme containing both phosphorylated and sialylated glycans.
30612270	6	68	part_of	ceruloplasmin	1025:1037	arg1	The four glycosylation sites	ceruloplasmin		The four glycosylation sites		PUBTATOR	Site	ceruloplasmin	1356	sites	The four glycosylation sites of human serum ceruloplasmin from 17 different individuals were analyzed using glycopeptides of varying peptide lengths, obtained by action of different proteases and by limited digestion.
30403372	6	52	gly	Asn276	1067:1072	arg1	an Asn276 oligosaccharide			Asn276	an Asn276 oligosaccharide					Asn276	Interactions in the presence of an Asn276 oligosaccharide could be enhanced upon carbohydrate shortening, which should be considered for immunogen design.
29671439	1	26	gly	glycoproteins	135:147	arg1	ginger glycoproteins	ginger glycoproteins				Fterm		glycoproteins			Herein, the ability of ginger glycoproteins to inhibit the angiotensin-converting enzyme (ACE) is characterized.
30802037	3	14	gly	tags	648:651	arg1	the Ser/Thr residues			the Ser/Thr residues	the Ser/Thr residues		Site			residues	Because there is virtually no carbohydrate-related tag on the peptide fragments after the O-glycopeptides are dissociated in HCD, we find it is unnecessary to set the variable mass tags on the Ser/Thr residues to identify the peptide sequences.
30802037	3	39	gly	tag	518:520	arg1	the peptide fragments			the peptide fragments	the peptide fragments		Site			fragments	Because there is virtually no carbohydrate-related tag on the peptide fragments after the O-glycopeptides are dissociated in HCD, we find it is unnecessary to set the variable mass tags on the Ser/Thr residues to identify the peptide sequences.
30802037	3	83	gly	O-glycopeptides	557:571	arg2	the O-glycopeptides			the O-glycopeptides						O-glycopeptides	Because there is virtually no carbohydrate-related tag on the peptide fragments after the O-glycopeptides are dissociated in HCD, we find it is unnecessary to set the variable mass tags on the Ser/Thr residues to identify the peptide sequences.
30513259	0	35	gly	aglycosylated	104:116	arg1	aglycosylated Fc regions			aglycosylated Fc regions						regions	CH2 domain orientation of human immunoglobulin G in solution: Structural comparison of glycosylated and aglycosylated Fc regions using small-angle X-ray scattering.
31256372	5	3	gly	isolated	625:632	arg2	peptides AND N-glycans			peptides	N-glycans					peptides	Thereafter, N-glycans are isolated from peptides using reverse-phase cartridges and are desalted with carbograph cartridges before finally being derivatized with the fluorescent label 2AB.
30637588	8	65	part_of	ECM	1595:1597	arg1	the GAG composition	ECM		the GAG composition		OGER	Site	ECM	Q13201	position	In summary, the method presented here offers a novel approach to determine the GAG composition of cell-derived ECM, which we believe is critical for a better understanding of ECM role in directing cellular responses and has the potential for generating important knowledge to use in the development of novel ECM-like biomaterials for tissue engineering applications.
30592755	11	14	gly	sialylated	1722:1731	arg1	the branched and sialylated structures				the branched and sialylated structures						Glycotyping analysis further revealed ethnic-based disparities mainly in the branched and sialylated structures.
29698801	11	40	gly	glycoprotein	1790:1801	arg1	specific serum glycoprotein	specific serum glycoprotein				Fterm		glycoprotein			Differing from serum comprehensive glycomes, profiling of specific serum glycoprotein contributes to more detailed understanding of biological relevance of glycosylation alterations in disease prognosis.
31776333	0	51	gly	glycoprotein	63:74	arg1	nanoscale glycoprotein assemblies	nanoscale glycoprotein assemblies				Fterm		glycoprotein			Cytoplasmic glycoengineering enables biosynthesis of nanoscale glycoprotein assemblies.
31325506	7	71	gly	N-glycosylation	1461:1475	arg2	The N-glycosylation sites			The N-glycosylation sites						sites	The N-glycosylation sites were identified from the analysis of glycopeptides from BSM.
31325506	7	38	gly	glycopeptides	1520:1532	arg2	glycopeptides	BSM		glycopeptides		Cterm		BSM	281333	glycopeptides	The N-glycosylation sites were identified from the analysis of glycopeptides from BSM.
31726038	7	49	gly	rhamnose-	1105:1113	arg1	a shallow active site			a shallow active site	a shallow active site		Site			site	The structure shows highly conserved rhamnose- and calcium-binding residues in a shallow active site that is housed in the (β/α)8 domain.
30643095	2	9	gly	glycoproteins	151:163	arg1	The glycans	glycoproteins			The glycans	Fterm		glycoproteins			The glycans of glycoproteins are classified into two groups, namely, N-glycans and O-glycans, according to their glycan-peptide linkage regions.
29642453	3	45	part_of	NA	487:488	arg1	the potential N-linked glycosylation (NLG) sites	NA		the potential N-linked glycosylation (NLG) sites		Cterm	Site	NA	4758	sites	We monitored the potential N-linked glycosylation (NLG) sites of over 10,000 HA and NA of H1N1 subtype isolated from human, avian, and swine species over the past century.
31025190	1	7	part_of	glycoprotein	127:138	arg1	two N-glycosylation sites	glycoprotein		two N-glycosylation sites		Fterm	Site	glycoprotein		sites	Natural hIFNγ is a glycoprotein with two N-glycosylation sites in each monomer chain, which are independently and differentially glycosylated.
29299842	1	0	gly	glycosylation	77:89	arg1	protein secretion	protein secretion				Fterm		protein			Protein glycosylation, the most universal and diverse post-translational modification, can affect protein secretion, stability, and immunogenicity.
30018219	7	30	gly	O-GlcNAc	1128:1135	arg1	many other domains			many other domains	many other domains		Site			domains	Although the majority of Notch1 EGF2 and EGF20 domains contained the extended forms of the glycan, the O-GlcNAc in many other domains mostly existed as a monosaccharide irrespective of the exogenous EOGT expression.
30030954	5	9	gly	sialylated	843:852	arg1	native and sialylated glycans				native and sialylated glycans						The results showed that native and sialylated glycans enriched lactoferrin have similar minimum inhibitory concentration (MIC) values against E.coli DH5a (1 mg/ml), whereas the MIC value for fully deglycosylated lactoferrin was 6mg/ml.
30802037	9	22	gly	glycopeptide	1467:1478	arg2	glycopeptide spectra matching			glycopeptide spectra matching						glycopeptide	Compared with the conventional searching approach, O-Search yielded 96%, 86%, and 79% improvement in glycopeptide spectra matching, glycopeptide identification, and peptide sequence identification, respectively.
30802037	9	44	gly	glycopeptide	1498:1509	arg2	glycopeptide identification			glycopeptide identification						glycopeptide	Compared with the conventional searching approach, O-Search yielded 96%, 86%, and 79% improvement in glycopeptide spectra matching, glycopeptide identification, and peptide sequence identification, respectively.
31529350	9	99	gly	glycoproteins	1594:1606	arg1	Glycan profiling	glycoproteins			Glycan profiling	Fterm		glycoproteins			Glycan profiling of target glycoproteins may endorse the molecular defect unraveling the complex clinical phenotype of CDG patients.
31813565	0	38	gly	glycopeptides	106:118	arg2	N-linked glycopeptides			N-linked glycopeptides						glycopeptides	Hydrophilic maltose-modified magnetic metal-organic framework for highly efficient enrichment of N-linked glycopeptides.
29500371	0	36	gly	Heterogeneity	14:26	arg1	the Fc-Glycan				the Fc-Glycan						Assessing the Heterogeneity of the Fc-Glycan of a Therapeutic Antibody Using an engineered FcγReceptor IIIa-Immobilized Column.
30444974	7	38	part_of	Asn-Asp-Ser	1140:1150	arg1	the same ubiquitin Asn-Asp-Ser sequon	Asn-Asp-Ser		the same ubiquitin Asn-Asp-Ser sequon		Cterm	Site	Asn-Asp-Ser		sequon	Based in our findings and ubiquitin function, we hypothesize that the same ubiquitin Asn-Asp-Ser sequon carries heterogenic glycosylations, at different metabolic pathway stages according to ubiquitin functional requirements.
30444974	7	58	part_of	ubiquitin	1130:1138	arg1	the same ubiquitin Asn-Asp-Ser sequon	ubiquitin		the same ubiquitin Asn-Asp-Ser sequon		Fterm	Site	ubiquitin		sequon	Based in our findings and ubiquitin function, we hypothesize that the same ubiquitin Asn-Asp-Ser sequon carries heterogenic glycosylations, at different metabolic pathway stages according to ubiquitin functional requirements.
30385505	2	10	gly	sites	366:370	arg1	glycan interactions			sites	glycan interactions					sites	Moreover, galectins gain higher affinity and fine-tune specificity by glycan interactions at sites adjacent to their β-galactoside-binding site, as revealed by extensive testing against panels of purified glycans.
29936827	4	87	gly	heterogeneity	770:782	arg1	O-glycans	enzymes			O-glycans	Fterm		enzymes			However, system-wide analysis on O-linked glycosylation remains a challenge due to the lack of equivalent enzymes and the inherent structural heterogeneity of O-glycans.
30111774	5	34	gly	O-glycosylated	778:791	arg1	tumour-associated O-glycosylated proteins	tumour-associated O-glycosylated proteins				Fterm		proteins			Moreover, immunoblotting assays demonstrated reactivity to tumour-associated O-glycosylated proteins, such as MUC1.
31569500	2	0	gly	O-mannosylation	298:312	arg1	proteins	proteins				Fterm		proteins			In eukaryotes, they act in the endoplasmic reticulum (ER) lumen and are involved in N-glycosylation, glypiation, O-mannosylation, and C-mannosylation of proteins.
31569500	2	15	gly	N-glycosylation	269:283	arg1	proteins	proteins				Fterm		proteins			In eukaryotes, they act in the endoplasmic reticulum (ER) lumen and are involved in N-glycosylation, glypiation, O-mannosylation, and C-mannosylation of proteins.
31569500	2	48	gly	C-mannosylation	319:333	arg1	proteins	proteins				Fterm		proteins			In eukaryotes, they act in the endoplasmic reticulum (ER) lumen and are involved in N-glycosylation, glypiation, O-mannosylation, and C-mannosylation of proteins.
31569500	2	58	gly	proteins	338:345	arg1	O-mannosylation	proteins			O-mannosylation	Fterm		proteins			In eukaryotes, they act in the endoplasmic reticulum (ER) lumen and are involved in N-glycosylation, glypiation, O-mannosylation, and C-mannosylation of proteins.
31569500	2	58	gly	proteins	338:345	arg1	C-mannosylation	proteins			C-mannosylation	Fterm		proteins			In eukaryotes, they act in the endoplasmic reticulum (ER) lumen and are involved in N-glycosylation, glypiation, O-mannosylation, and C-mannosylation of proteins.
30651366	14	17	gly	glycosylation	2502:2514	arg2	the predicted glycosylation sites			the predicted glycosylation sites						sites	Mass spectrometry demonstrated that the predicted glycosylation sites were utilized in both mammalian and insect cell E2, although the glycan types in insect cell E2 were smaller and less complex.
30651366	14	78	gly	utilized	2527:2534	arg2	the predicted glycosylation sites			the predicted glycosylation sites						sites	Mass spectrometry demonstrated that the predicted glycosylation sites were utilized in both mammalian and insect cell E2, although the glycan types in insect cell E2 were smaller and less complex.
31289257	1	39	gly	glycosylation	111:123	arg1	proteins	proteins				Fterm		proteins			Aberrant glycosylation of proteins has major implications for human diseases.
30276752	3	5	gly	glycoproteins	555:567	arg1	specific glycoproteins	specific glycoproteins				Fterm		glycoproteins			A simple analytical approach to analyze N-glycans on specific glycoproteins is presented, which involves a combination of tryptic peptide mass spectrometry and "off-line" RP-HPLC MALDI-TOF MS/MS complemented by blotting to recognize specific epitopes.
30276752	3	19	gly	N-glycans	533:541	arg1	specific glycoproteins	glycoproteins			N-glycans	Fterm		glycoproteins			A simple analytical approach to analyze N-glycans on specific glycoproteins is presented, which involves a combination of tryptic peptide mass spectrometry and "off-line" RP-HPLC MALDI-TOF MS/MS complemented by blotting to recognize specific epitopes.
29370305	1	82	gly	glycoprotein	121:132	arg1	HIV-1 envelope glycoprotein	HIV-1 envelope glycoprotein				Fterm		glycoprotein	155971		HIV-1 envelope glycoprotein (Env) mediates virus attachment and entry into the host cells.
30959980	3	17	gly	glycopeptide	523:534	arg2	a major mucin-type glycopeptide			a major mucin-type glycopeptide						glycopeptide	In the present study, a major mucin-type glycopeptide (RIF6) of hyla rabbit intestine was isolated and the O-glycans were extensively characterized based on liquid chromatography-tandem mass spectrometry (LC-MS/MS) combined with bioinformatics approaches.
29878199	7	12	part_of	domain	1098:1103	arg1	a splice acceptor site	domain		a splice acceptor site						site	These included a missense mutation that disrupted transmembrane domain 4 and a mutation in a splice acceptor site resulting in skipping of exon 9.
29897488	1	48	gly	glycoproteins	272:284	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Summary GlycoStore is a curated chromatographic, electrophoretic and mass-spectrometry composition database of N-, O-, glycosphingolipid (GSL) glycans and free oligosaccharides associated with a range of glycoproteins, glycolipids and biotherapeutics.
29885470	11	119	gly	glycoproteins	1984:1996	arg1	glycoproteins	glycoproteins			the N-glycans	Fterm		glycoproteins			As a type of informational molecule, the N-glycans of glycoproteins participate directly in the molecular interactions between glycan epitopes and their corresponding protein receptors.
31316527	10	106	gly	glycosylated	1760:1771	arg1	glycosylated variants	glycosylated variants				Fterm		variants			Glycosylation showed strong stabilizing effects on rCMG2-Fc during in planta accumulation, evidenced by the over 2-fold higher expression and less protein degradation observed for glycosylated variants compared to the Agly variant.
30030954	3	21	gly	sialylated	685:694	arg1	native, fully deglycosylated and sialylated glycan				native, fully deglycosylated and sialylated glycan						Three lactoferrin forms with different glycan profile were obtained by treatment with these fusion tagged enzymes; native, fully deglycosylated and sialylated glycan enriched lactoferrin.
29773674	5	6	gly	peptides	958:965	arg1	sequence coverage				sequence coverage						Here, we developed a workflow to improve sequence coverage and identification of glycosylated peptides in proteoglycans.
29773674	5	6	gly	peptides	958:965	arg1	identification				identification						Here, we developed a workflow to improve sequence coverage and identification of glycosylated peptides in proteoglycans.
29773674	5	15	gly	sequence	905:912	arg1	sequence coverage				sequence coverage						Here, we developed a workflow to improve sequence coverage and identification of glycosylated peptides in proteoglycans.
29773674	5	37	gly	peptides	958:965	arg1	proteoglycans				proteoglycans						Here, we developed a workflow to improve sequence coverage and identification of glycosylated peptides in proteoglycans.
29773674	5	56	gly	glycosylated	945:956	arg1	glycosylated peptides			glycosylated peptides							Here, we developed a workflow to improve sequence coverage and identification of glycosylated peptides in proteoglycans.
30802037	5	17	gly	tags	867:870	arg1	the Ser/Thr residues			the Ser/Thr residues	the Ser/Thr residues		Site			residues	Instead of setting the variable mass tags on the Ser/Thr residues, we set variable mass tags on the peptide level.
30576150	9	36	gly	mannosylated	1690:1701	arg1	GlcNAc2-Man9				GlcNAc2-Man9						Apparent correlations between milk N-glycans and offspring gut microbial populations were found; for example, mannosylated PNO21 (GlcNAc2-Man9) was positively correlated with OTU706 ( Lactobacillus amylovorus) and OTU1380 ( Bacteroides uniformis).
31501225	2	20	gly	N-glycopeptides	183:197	arg2	N-glycopeptides			N-glycopeptides						N-glycopeptides	Characterizing N-glycopeptides that correspond to N-glycan structure with specific site information enables better understanding of the molecular pathogenesis of liver damage and cancer.
31987138	1	15	gly	N-glycopeptides	194:208	arg2	N-glycopeptides			N-glycopeptides						N-glycopeptides	For mass spectrometry (MS)-based N-glycoproteomics, selective enrichment of N-glycopeptides prior to MS analysis is a crucial step to reduce sample complexity.
30322851	5	52	gly	glycoform	617:625	arg1	a unique tetrasaccharide glycoform				a unique tetrasaccharide glycoform						glycolytica, a unique tetrasaccharide glycoform consisting of di-N-acetylbacillosamine and glucose as the first two sugars followed by a rare sugar whose mass spectrometric fragmentation profile was most consistent with di-N-acetyl hexuronic acid and a N-acetylhexosamine at the nonreducing end has been identified.
30327321	8	53	gly	O-glycosylated	1381:1394	arg1	a disordered, elongated and highly O-glycosylated mucin-like domain			a disordered, elongated and highly O-glycosylated mucin-like domain						domain	Thus, the medium and long ColXVIII isoforms contain at their extreme N-terminus a disordered, elongated and highly O-glycosylated mucin-like domain that is not found in other collagens, and we suggest naming it the Mucin-like domain in ColXVIII (MUCL-C18).
30327321	8	59	gly	it	1474:1475	arg1	the Mucin-like domain			the Mucin-like domain						domain	Thus, the medium and long ColXVIII isoforms contain at their extreme N-terminus a disordered, elongated and highly O-glycosylated mucin-like domain that is not found in other collagens, and we suggest naming it the Mucin-like domain in ColXVIII (MUCL-C18).
29729312	3	82	part_of	GILT	522:525	arg1	GILT signature sequence CQHGX2ECX2NX4C	GILT		GILT signature sequence CQHGX2ECX2NX4C		OGER	Site	GILT	P13284	sequence	Its open reading frame covers 771 base pairs, encoding a protein of 256 amino acids that possesses GILT signature sequence CQHGX2ECX2NX4C, active-site CXXC motif, and two potential N-linked glycosylation sites.
29729312	3	6	part_of	possesses	512:520	arg1	a protein AND active-site CXXC motif	a protein		active-site CXXC motif		Fterm	Site	protein		motif	Its open reading frame covers 771 base pairs, encoding a protein of 256 amino acids that possesses GILT signature sequence CQHGX2ECX2NX4C, active-site CXXC motif, and two potential N-linked glycosylation sites.
29729312	3	6	part_of	possesses	512:520	arg1	a protein AND two potential N-linked glycosylation sites	a protein		two potential N-linked glycosylation sites		Fterm	Site	protein		sites	Its open reading frame covers 771 base pairs, encoding a protein of 256 amino acids that possesses GILT signature sequence CQHGX2ECX2NX4C, active-site CXXC motif, and two potential N-linked glycosylation sites.
29729312	3	6	part_of	possesses	512:520	arg1	a protein AND GILT signature sequence CQHGX2ECX2NX4C	a protein		GILT signature sequence CQHGX2ECX2NX4C		Fterm	Site	protein		sequence	Its open reading frame covers 771 base pairs, encoding a protein of 256 amino acids that possesses GILT signature sequence CQHGX2ECX2NX4C, active-site CXXC motif, and two potential N-linked glycosylation sites.
29956878	7	4	gly	α1,6-fucosylated	832:847	arg1	α1,6-fucosylated N-glycans				α1,6-fucosylated N-glycans						The resulting highly resolved structures gave a detailed view on how the exclusive recognition of α1,6-fucosylated N-glycans by such a small protein occurs.
29437979	7	146	gly	glycosylated	1112:1123	arg1	all five sites			all five sites						sites	Our results demonstrate that all five sites are glycosylated.
29888865	5	84	gly	glycoprotein	590:601	arg1	a plasma glycoprotein	a plasma glycoprotein				Fterm		glycoprotein			SUMMARY: Background/Objective Human factor VIII (FVIII) is a plasma glycoprotein, defects of which result in hemophilia A. Current substitution therapy uses FVIII products purified from human plasma or from various cell lines (recombinant FVIII) with different levels of B-domain deletion.
30003921	5	8	gly	glycoproteins	684:696	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			A total of 34 saccharides (mono-, di- and polysaccharides, and glycoproteins) were used for initial high-throughput screening.
31611356	3	36	gly	glycosylation	663:675	arg2	nearly every glycosylation site			nearly every glycosylation site						site	Here, we unify previous work on the importance of other glycans to Grft potency against HIV-1 and Grft's role in mediating the conformational change of gp120 by mutating nearly every glycosylation site in gp120.
29508223	2	27	gly	released	340:347	arg1	several glycoproteins AND high-mannose glycans	several glycoproteins			high-mannose glycans	Fterm		glycoproteins			Fragmentation of high-mannose glycans released from several glycoproteins, including those from viral sources, provided over 50 fragments, many of which gave unique collisional cross-sections and provided additional information used to assign structural isomers.
29508223	2	41	gly	glycoproteins	362:374	arg1	several glycoproteins	several glycoproteins				Fterm		glycoproteins			Fragmentation of high-mannose glycans released from several glycoproteins, including those from viral sources, provided over 50 fragments, many of which gave unique collisional cross-sections and provided additional information used to assign structural isomers.
31370181	7	68	gly	glycoproteins	1304:1316	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			These results suggest a similar gB conformation when glycoproteins are expressed in plant cells as site accessibility influences the glycosylation profile at each site.
30466347	6	62	gly	fucosylation	1355:1366	arg1	IgG1 mAb N-glycans impact				IgG1 mAb N-glycans impact						We demonstrated that the core fucosylation, non-reducing terminal galactosylation, sialylation, and mannosylation of IgG1 mAb N-glycans impact not only on FcγRIIIa binding, antibody-dependent cell-mediated cytotoxicity, and C1q binding, but also FcRn binding, thermal stability and propensity for protein aggregation.
30074304	5	30	gly	N-glycans	888:896	arg1	a given region			a given region	a given region		Site			region	The PNGase F is applied by solvent sprayer as a molecular layer on frozen or formalin-fixed tissues and all released N-glycans in a given region of tissue are detected using matrix-assisted laser desorption/ionization (MALDI) imaging mass spectrometry (MALDI-IMS).
30612271	0	67	part_of	VC1	75:77	arg1	the VC1 domain	VC1		the VC1 domain		Cterm	Site	VC1		domain	Insights into the effects of N-glycosylation on the characteristics of the VC1 domain of the human receptor for advanced glycation end products (RAGE) secreted by Pichia pastoris.
30612271	0	70	part_of	receptor	99:106	arg1	the VC1 domain	receptor for advanced glycation end products		the VC1 domain		PUBTATOR	Site	receptor for advanced glycation end products	177	domain	Insights into the effects of N-glycosylation on the characteristics of the VC1 domain of the human receptor for advanced glycation end products (RAGE) secreted by Pichia pastoris.
30693728	6	15	gly	detected	1233:1240	arg1	the compositions AND galacturonic acid			the compositions	galacturonic acid					positions	Eight monosaccharides (mannose, glucosamine, ribose, glucuronic acid, galacturonic acid, aminogalactose, glucose and galactose) were detected in the compositions of water-soluble polysaccharides in the antler velvet by using different processing methods.
30693728	6	15	gly	detected	1233:1240	arg1	the compositions AND galactose			the compositions	galactose					positions	Eight monosaccharides (mannose, glucosamine, ribose, glucuronic acid, galacturonic acid, aminogalactose, glucose and galactose) were detected in the compositions of water-soluble polysaccharides in the antler velvet by using different processing methods.
30693728	6	15	gly	detected	1233:1240	arg1	the compositions AND Eight monosaccharides			the compositions	Eight monosaccharides					positions	Eight monosaccharides (mannose, glucosamine, ribose, glucuronic acid, galacturonic acid, aminogalactose, glucose and galactose) were detected in the compositions of water-soluble polysaccharides in the antler velvet by using different processing methods.
30693728	6	15	gly	detected	1233:1240	arg1	the compositions AND ribose			the compositions	ribose					positions	Eight monosaccharides (mannose, glucosamine, ribose, glucuronic acid, galacturonic acid, aminogalactose, glucose and galactose) were detected in the compositions of water-soluble polysaccharides in the antler velvet by using different processing methods.
30693728	6	15	gly	detected	1233:1240	arg1	the compositions AND mannose			the compositions	mannose					positions	Eight monosaccharides (mannose, glucosamine, ribose, glucuronic acid, galacturonic acid, aminogalactose, glucose and galactose) were detected in the compositions of water-soluble polysaccharides in the antler velvet by using different processing methods.
30693728	6	15	gly	detected	1233:1240	arg2	the compositions AND glucosamine			the compositions	glucosamine					positions	Eight monosaccharides (mannose, glucosamine, ribose, glucuronic acid, galacturonic acid, aminogalactose, glucose and galactose) were detected in the compositions of water-soluble polysaccharides in the antler velvet by using different processing methods.
30693728	6	15	gly	detected	1233:1240	arg2	the compositions AND glucose			the compositions	glucose					positions	Eight monosaccharides (mannose, glucosamine, ribose, glucuronic acid, galacturonic acid, aminogalactose, glucose and galactose) were detected in the compositions of water-soluble polysaccharides in the antler velvet by using different processing methods.
30693728	6	15	gly	detected	1233:1240	arg2	the compositions AND glucuronic acid			the compositions	glucuronic acid					positions	Eight monosaccharides (mannose, glucosamine, ribose, glucuronic acid, galacturonic acid, aminogalactose, glucose and galactose) were detected in the compositions of water-soluble polysaccharides in the antler velvet by using different processing methods.
31291761	0	58	gly	wall	36:39	arg1	glycan epitopes			glycan epitopes						epitopes	Identification and analysis of cell wall glycan epitopes and polyphenol oxidase in pawpaw (Asimina triloba [L.] Dunal) fruit pulp as affected by high pressure processing and refrigerated storage.
29512066	2	5	gly	glycoproteins	277:289	arg1	denatured carboxymethylated glycoproteins	denatured carboxymethylated glycoproteins				Fterm		glycoproteins			N-glycans are released from denatured carboxymethylated glycoproteins by digestion with peptide-N-glycosidase F (PNGase F) and purified using both C18 Sep-Pak® and porous graphitized carbon (PGC) HyperSep™ Hypercarb™ solid-phase extraction (SPE) cartridges.
29512066	2	45	gly	released	235:242	arg1	denatured carboxymethylated glycoproteins AND N-glycans	denatured carboxymethylated glycoproteins			N-glycans	Fterm		glycoproteins			N-glycans are released from denatured carboxymethylated glycoproteins by digestion with peptide-N-glycosidase F (PNGase F) and purified using both C18 Sep-Pak® and porous graphitized carbon (PGC) HyperSep™ Hypercarb™ solid-phase extraction (SPE) cartridges.
29924315	11	16	gly	sialylated	1826:1835	arg1	sialylated KS proteoglycans				sialylated KS proteoglycans						We conclude that sialylated KS proteoglycans are endogenous human airway ligands that bind Siglec-8 and may regulate allergic inflammation.
30335821	6	51	gly	glycosylation	1595:1607	arg1	certain regions			regions						regions	However, yeast-displayed Env is not recognized by some anti-Env antibodies sensitive to quaternary structure, suggesting either that the displayed protein exists in a monomeric state or that for these antibodies, yeast glycosylation in certain regions hinders recognition or access.
31640540	7	6	gly	glycoprotein	1336:1347	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			The GUI provides a straightforward two-dimensional (2D) rendering of a glycoprotein that allows for a quick visual inspection of the glycosylation state of all the sequons on a protein structure.
31640540	7	32	gly	glycosylation	1398:1410	arg1	all the sequons			all the sequons							The GUI provides a straightforward two-dimensional (2D) rendering of a glycoprotein that allows for a quick visual inspection of the glycosylation state of all the sequons on a protein structure.
30904681	1	65	part_of	protein	246:252	arg1	four or five N-glycosylation sites	protein		four or five N-glycosylation sites		Fterm	Site	protein		sites	The highly glycosylated ß-2-glycoprotein-1 (B2GP1), also called apolipoprotein H, is a 50 kDa human plasma protein with four or five N-glycosylation sites.
29443078	1	58	gly	glycoproteins	267:279	arg1	human glycoproteins	human glycoproteins				Fterm		glycoproteins			We present a highly efficient way for the rapid preparation of a wide range of N-linked oligosaccharides (estimated to exceed 20,000 structures) that are commonly found on human glycoproteins.
29443078	1	64	gly	found	252:256	arg2	human glycoproteins AND N-linked oligosaccharides	human glycoproteins			N-linked oligosaccharides	Fterm		glycoproteins			We present a highly efficient way for the rapid preparation of a wide range of N-linked oligosaccharides (estimated to exceed 20,000 structures) that are commonly found on human glycoproteins.
31154130	0	66	part_of	IgG-Fc	71:76	arg1	IgG-Fc glycopeptides	IgG		IgG-Fc glycopeptides		Cterm	Site	IgG		glycopeptides	An integrated approach for comprehensive profiling and quantitation of IgG-Fc glycopeptides with application to rheumatoid arthritis.
31507595	5	5	gly	sialylated	829:838	arg1	N-glycosylation and multi-antennary sialylated N-glycans				N-glycosylation and multi-antennary sialylated N-glycans						Analysis of native CD52 purified from human spleen revealed extensive heterogeneity in N-glycosylation and multi-antennary sialylated N-glycans with abundant polyLacNAc extensions, together with mainly di-sialylated O-glycosylation type structures.
31507595	5	28	gly	di-sialylated	908:920	arg1	mainly di-sialylated O-glycosylation type structures				mainly di-sialylated O-glycosylation type structures						Analysis of native CD52 purified from human spleen revealed extensive heterogeneity in N-glycosylation and multi-antennary sialylated N-glycans with abundant polyLacNAc extensions, together with mainly di-sialylated O-glycosylation type structures.
31453603	0	88	gly	glycopeptides	106:118	arg2	protonated N-linked glycopeptides			protonated N-linked glycopeptides						glycopeptides	Composition and charge state influence on the ion-neutral collision cross sections of protonated N-linked glycopeptides: an experimental and theoretical deconstruction of coulombic repulsion vs. charge solvation effects.
29548671	1	14	gly	glycosylated	227:238	arg1	a highly glycosylated region			a highly glycosylated region						region	Virtually the entire surface of the HIV-1-envelope trimer is recognized by neutralizing antibodies, except for a highly glycosylated region at the center of the "silent face" on the gp120 subunit.
31712146	5	82	part_of	SCP	734:736	arg1	compositions	SCP		compositions		PUBTATOR	Site	SCP	64827	positions	The results revealed that there were obvious differences in extraction yield, molecular weight, compositions of monosaccharide and organic element, molecular morphology, rheological properties and the contents of total sugar, protein, uronic acid and sulfate of SCP, MAP and SFP.
31501225	4	53	gly	N-glycopeptide	565:578	arg2	N-glycopeptide			N-glycopeptide						N-glycopeptide	We used an N-glycopeptide method based on 18O/16O C-terminal labeling to obtain 82 comparisons of serum from patients with HBV-related hepatocellular carcinoma (HCC) and liver cirrhosis (LC).
31737090	5	48	gly	N-glycosylation	1076:1090	arg2	all five N-glycosylation sites			all five N-glycosylation sites						sites	Single-site N-glycosylation mutants with Asn substituted by Gln were obtained, and the Mut with all five N-glycosylation sites removed was constructed, which resulted in the loss of all enzyme activity.
30525457	1	79	gly	fucosylated	126:136	arg1	fucosylated biantennary N-glycans				fucosylated biantennary N-glycans						Glycosylated human IgG contains fucosylated biantennary N-glycans with different modifications including N-acetylglucosamine, which bisects the mannose core.
31507595	8	115	gly	sialylated	1496:1505	arg1	sialylated N-glycan structures				sialylated N-glycan structures						When glycoforms of CD52-Fc were fractionated by anion exchange MonoQ-GL chromatography, bioactive fractions displayed mainly tetra-antennary, α-2,3 sialylated N-glycan structures and a lower relative abundance of bisecting GlcNAc structures compared to non-bioactive fractions.
30033944	2	90	gly	glycoproteins	337:349	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Identification of the localization, carrier proteins and interacting partners of N-glycans is essential for understanding the roles of glycoproteins.
30948514	3	21	gly	N-glycosylated	561:574	arg2	Asn34			Asn34						Asn34	Human rhodopsin is N-glycosylated on Asn2 and Asn15, whereas human (h) red and green cone opsins (hOPSR and hOPSG, respectively) are N-glycosylated at Asn34 Here, utilizing a monoclonal antibody (7G8 mAB), we demonstrate that hOPSR and hOPSG from human retina also are O-glycosylated with full occupancy.
30948514	3	51	gly	N-glycosylated	447:460	arg1	Human rhodopsin	Human rhodopsin		Asn2 and Asn15		PUBTATOR		Human rhodopsin	6010	Asn2 and Asn15	Human rhodopsin is N-glycosylated on Asn2 and Asn15, whereas human (h) red and green cone opsins (hOPSR and hOPSG, respectively) are N-glycosylated at Asn34 Here, utilizing a monoclonal antibody (7G8 mAB), we demonstrate that hOPSR and hOPSG from human retina also are O-glycosylated with full occupancy.
30948514	3	51	gly	N-glycosylated	447:460	arg1	Asn15			Asn2 and Asn15						Asn2 and Asn15	Human rhodopsin is N-glycosylated on Asn2 and Asn15, whereas human (h) red and green cone opsins (hOPSR and hOPSG, respectively) are N-glycosylated at Asn34 Here, utilizing a monoclonal antibody (7G8 mAB), we demonstrate that hOPSR and hOPSG from human retina also are O-glycosylated with full occupancy.
30948514	3	51	gly	N-glycosylated	447:460	arg2	Asn15			Asn2 and Asn15						Asn2 and Asn15	Human rhodopsin is N-glycosylated on Asn2 and Asn15, whereas human (h) red and green cone opsins (hOPSR and hOPSG, respectively) are N-glycosylated at Asn34 Here, utilizing a monoclonal antibody (7G8 mAB), we demonstrate that hOPSR and hOPSG from human retina also are O-glycosylated with full occupancy.
30948514	3	51	gly	N-glycosylated	447:460	arg1	Asn2			Asn2 and Asn15						Asn2 and Asn15	Human rhodopsin is N-glycosylated on Asn2 and Asn15, whereas human (h) red and green cone opsins (hOPSR and hOPSG, respectively) are N-glycosylated at Asn34 Here, utilizing a monoclonal antibody (7G8 mAB), we demonstrate that hOPSR and hOPSG from human retina also are O-glycosylated with full occupancy.
30948514	3	51	gly	N-glycosylated	447:460	arg1	Asn15	Human rhodopsin		Asn2 and Asn15		PUBTATOR		Human rhodopsin	6010	Asn2 and Asn15	Human rhodopsin is N-glycosylated on Asn2 and Asn15, whereas human (h) red and green cone opsins (hOPSR and hOPSG, respectively) are N-glycosylated at Asn34 Here, utilizing a monoclonal antibody (7G8 mAB), we demonstrate that hOPSR and hOPSG from human retina also are O-glycosylated with full occupancy.
30948514	3	51	gly	N-glycosylated	447:460	arg2	Asn15	Human rhodopsin		Asn2 and Asn15		PUBTATOR		Human rhodopsin	6010	Asn2 and Asn15	Human rhodopsin is N-glycosylated on Asn2 and Asn15, whereas human (h) red and green cone opsins (hOPSR and hOPSG, respectively) are N-glycosylated at Asn34 Here, utilizing a monoclonal antibody (7G8 mAB), we demonstrate that hOPSR and hOPSG from human retina also are O-glycosylated with full occupancy.
30948514	3	51	gly	N-glycosylated	447:460	arg1	Asn2	Human rhodopsin		Asn2 and Asn15		PUBTATOR		Human rhodopsin	6010	Asn2 and Asn15	Human rhodopsin is N-glycosylated on Asn2 and Asn15, whereas human (h) red and green cone opsins (hOPSR and hOPSG, respectively) are N-glycosylated at Asn34 Here, utilizing a monoclonal antibody (7G8 mAB), we demonstrate that hOPSR and hOPSG from human retina also are O-glycosylated with full occupancy.
30948514	3	51	gly	N-glycosylated	447:460	arg2	Asn15			Asn2 and Asn15						Asn2 and Asn15	Human rhodopsin is N-glycosylated on Asn2 and Asn15, whereas human (h) red and green cone opsins (hOPSR and hOPSG, respectively) are N-glycosylated at Asn34 Here, utilizing a monoclonal antibody (7G8 mAB), we demonstrate that hOPSR and hOPSG from human retina also are O-glycosylated with full occupancy.
30948514	3	51	gly	N-glycosylated	447:460	arg1	Asn2			Asn2 and Asn15						Asn2 and Asn15	Human rhodopsin is N-glycosylated on Asn2 and Asn15, whereas human (h) red and green cone opsins (hOPSR and hOPSG, respectively) are N-glycosylated at Asn34 Here, utilizing a monoclonal antibody (7G8 mAB), we demonstrate that hOPSR and hOPSG from human retina also are O-glycosylated with full occupancy.
30948514	3	51	gly	N-glycosylated	447:460	arg1	Asn2			Asn2 and Asn15						Asn2 and Asn15	Human rhodopsin is N-glycosylated on Asn2 and Asn15, whereas human (h) red and green cone opsins (hOPSR and hOPSG, respectively) are N-glycosylated at Asn34 Here, utilizing a monoclonal antibody (7G8 mAB), we demonstrate that hOPSR and hOPSG from human retina also are O-glycosylated with full occupancy.
31256376	16	18	gly	glycopeptide	2343:2354	arg2	glycopeptide identification			glycopeptide identification						glycopeptide	In addition, ESI-compatible alternative MS/MS techniques, electron-capture and electron-transfer dissociation, aid glycopeptide identification as well as modification site assignments.
30335821	4	6	part_of	CD4	1060:1062	arg1	CD4 binding site	CD4		CD4 binding site		PUBTATOR	Site	CD4	920	site	Multiple yeast-displayed gp120 and gp140 proteins are capable of binding to antibodies directed against the V3-variable loop, CD4 binding site, and gp41 membrane-proximal regions, including some antibodies whose binding is known to depend on Env conformation and N-linked glycan.
31654087	0	41	gly	Glycosylation	0:12	arg1	proteins	proteins				Fterm		proteins			Glycosylation of proteins of human skin fibroblasts is changed by rosmarinic acid.
30898876	6	53	gly	glycoproteins	1400:1412	arg1	the identified glycoproteins	the identified glycoproteins				Fterm		glycoproteins			Our analysis also uncovered that most of the identified glycoproteins localize to intracellular organelles, particularly to the endoplasmic reticulum.
29406618	9	41	part_of	HAp/glucan	1518:1527	arg1	HAp/glucan composite	HAp		HAp/glucan composite		OGER	Site	HAp	O95197	composite	Therefore, this suggests the lack of volume change-related side effects of HAp/glucan composite in bone defects treatment if postoperative inflammation is prevented.
30348313	8	37	gly	demannosylation	1052:1066	arg1	the nuclease activity	the nuclease activity				Fterm		nuclease			The partial demannosylation of R-TBN1 did not affect the nuclease activity; moreover, a little shift in substrate specificity was observed.
30389987	4	57	part_of	PglB	736:739	arg1	an inhibitory peptide	X-ray structure of PglB		an inhibitory peptide		OGER	Site	X-ray structure of PglB	Q99645	peptide	Here we present the X-ray structure of PglB bound to a reactive LLO analog and an inhibitory peptide, revealing previously unobserved interactions in the active site.
30002445	3	10	gly	glycoprotein	560:571	arg1	a novel cell-free glycoprotein synthesis (CFGpS) technology	a novel cell-free glycoprotein synthesis (CFGpS) technology				Fterm		glycoprotein			To address these challenges, we describe a novel cell-free glycoprotein synthesis (CFGpS) technology that seamlessly integrates protein biosynthesis with asparagine-linked protein glycosylation.
30739313	2	57	gly	O-Glycans	184:192	arg1	the cell surface proteins	proteins			O-Glycans	Fterm		proteins			O-Glycans on the cell surface proteins also modulate the cell's interactions with the surrounding environments and other cells.
30612271	7	19	gly	N-glycosylation	773:787	arg2	two N-glycosylation sites			two N-glycosylation sites						sites	Out of two N-glycosylation sites, one (Asn25) was fully occupied while the other (Asn81) was under-glycosylated, generating two VC1 variants, named p36 and p34.
30612271	7	41	gly	occupied	818:825	arg2	Asn25			Asn25						Asn25	Out of two N-glycosylation sites, one (Asn25) was fully occupied while the other (Asn81) was under-glycosylated, generating two VC1 variants, named p36 and p34.
30612271	7	84	gly	under-glycosylated	855:872	arg1	Asn81			Asn81						Asn81	Out of two N-glycosylation sites, one (Asn25) was fully occupied while the other (Asn81) was under-glycosylated, generating two VC1 variants, named p36 and p34.
29231704	1	51	gly	glycopeptides	307:319	arg2	glycopeptides			glycopeptides						glycopeptides	Reversed-phase chromatographic separation of glycopeptides tends to be dominated by the peptide composition.
30335377	7	20	gly	glycosylated	1071:1082	arg1	The heavily glycosylated protein	The heavily glycosylated protein				Fterm		protein			The heavily glycosylated protein forms a large fraction of the EPS and was also located by lectin staining.
31316527	4	32	gly	had	791:793	arg1	Both the APO and ER variants AND a complex-type N-glycan	Both the APO and ER variants			a complex-type N-glycan	Fterm		variants			Both the APO and ER variants had a complex-type N-glycan (GnGnXF) as their predominant glycans.
31316527	4	32	gly	had	791:793	arg1	Both the APO and ER variants AND their predominant glycans	Both the APO and ER variants			their predominant glycans	Fterm		variants			Both the APO and ER variants had a complex-type N-glycan (GnGnXF) as their predominant glycans.
30427586	5	14	gly	N-glycopeptides	973:987	arg2	N-glycopeptides			N-glycopeptides						N-glycopeptides	For the unambiguous identification of N-glycopeptides, the use of a conserved yet, rarely employed-fragmentation signature [Mpeptide +H+0,2 X GlcNAc]+ is proposed.
29738687	1	48	gly	isolated	274:281	arg1	Escherichia coli type strain O81 AND lipopolysaccharides	strain			lipopolysaccharides	Fterm		strain			Glycerophosphate-containing O-specific polysaccharides (OPSs) were obtained by mild acidic degradation of lipopolysaccharides isolated from Escherichia coli type strain O81 and E. coli strain HS3-104 from horse feces.
30902814	4	76	gly	N-glycosylation	501:515	arg1	IBV strain M41 spike protein	protein		domain		Fterm		protein		domain	Here, we analyzed the N-glycosylation of the receptor-binding domain (RBD) of IBV strain M41 spike protein and assessed the role of this modification in host receptor binding.
32110292	6	18	gly	N-glycopeptides	1246:1260	arg2	N-glycopeptides			N-glycopeptides						N-glycopeptides	We report here a chemical labeling strategy to improve the electron transfer dissociation efficiency in mass spectrometry analysis, which enables a 100% peptide sequence coverage of N-glycopeptides in all subclasses of IgG.
29437979	4	81	part_of	contains	674:681	arg1	gH AND five potential N-linked glycosylation sites	gH		five potential N-linked glycosylation sites		PUBTATOR	Site	gH	8836	sites	gH contains five potential N-linked glycosylation sites at positions 77, 162, 542, 604, and 627, which were inactivated by conservative mutations (asparagine to glutamine) singly or in combination.
29546786	7	45	gly	glycoproteins	1150:1162	arg1	typical glycans	glycoproteins			typical glycans	Fterm		glycoproteins			Interestingly, the priming with polysaccharide Ags (in a composition of the bacterial cell envelope), that is, dominant Ags of bacteria, led to the induction of Abs against typical glycans of mammalian glycoproteins and glycolipids (e.g. Abs of the ABH blood group system) that do not have a structural similarity to the polysaccharides.
30275012	4	2	part_of	subunit	647:653	arg1	Thr-38	subunit		Thr-38		Fterm	SpecificSite	subunit		Thr-38	Here, we show that a C. difficile strain of S-layer cassette type 11, Ox247, has a complex glycan attached via an O-linkage to Thr-38 of the S-layer low-molecular-weight subunit.
30737276	9	52	gly	l-Fuc	1612:1616	arg1	the core region			the core region	the core region		Site			region	Last, gene a071r encodes a GT that is involved in the attachment of a semiconserved element, α-d-Rha, to the same l-Fuc in the core region.
29769533	1	26	gly	glycosylated	253:264	arg1	well-folded, native-like glycosylated trimers	well-folded, native-like glycosylated trimers				Fterm		trimers			Furin cleavage of the HIV envelope glycoprotein is an essential step for cell entry that enables formation of well-folded, native-like glycosylated trimers, releases constraints on the fusion peptide, and limits enzymatic processing of the N-glycan shield.
29333671	0	50	gly	glycopeptides	33:45	arg2	N-linked glycopeptides			N-linked glycopeptides						glycopeptides	Selective enrichment of N-linked glycopeptides and glycans by using a dextran-modified hydrophilic material.
31010286	2	52	gly	epitopes	497:504	arg1	a hybrid structure			epitopes	a hybrid structure					epitopes	Here, we prepared a hybrid structure of viral and bacterial epitopes as part of a vaccine design strategy to elicit oligomannose-specific HIV-neutralizing antibodies using glycoconjugates based on the Rv3 LOS structure.
31098625	2	61	gly	modified	261:268	arg3	These proteins AND glycans	These proteins			glycans	Fterm		proteins			These proteins are highly modified by glycans that are currently being recognized as vital to protein structure, stability, function, and health of the intestinal mucosa.
29773674	9	70	part_of	mucin-type	1511:1520	arg1	mucin-type O-glycosites	mucin		mucin-type O-glycosites		PUBTATOR	Site	mucin	100508689	O-glycosites	For aggrecan, we identified 50 linker-glycosites and mucin-type O-glycosites in the extended region and N-glycosites in the globular domains, many of which are novel and have not been observed previously.
30565163	4	65	gly	monosaccharide	1143:1156	arg1	2,4A3 cross-ring fragment			2,4A3 cross-ring fragment	2,4A3 cross-ring fragment		Site			fragment	We found that 2,4A3 cross-ring fragment at the terminal monosaccharide in sialyllactoses, sialyllactosamines, and sialyl pentasaccharides is highly abundant in the MS/MS spectra of [M+2X-H]+ species of α2,6-NeuAc glycans, while (2,4A3-H2O) fragment is highly abundant in α2,3-NeuAc moiety.
31669471	1	59	gly	Glycosylation	169:181	arg1	cell receptors	cell receptors				Fterm		receptors			Glycosylation of cell receptors influences their function and development of tumour induces changes in glycosylation.
31737090	3	21	gly	N-glycosylation	570:584	arg2	Five N-glycosylation sites			Five N-glycosylation sites						sites	RESULTS Five N-glycosylation sites with variable high mannose-type oligosaccharides (Man3-9GlcNAc2) were confirmed in the rKcINU1.
31737090	3	94	gly	sites	586:590	arg1	Man3-9GlcNAc2			sites	Man3-9GlcNAc2					sites	RESULTS Five N-glycosylation sites with variable high mannose-type oligosaccharides (Man3-9GlcNAc2) were confirmed in the rKcINU1.
31737090	3	94	gly	sites	586:590	arg1	variable high mannose-type oligosaccharides			sites	variable high mannose-type oligosaccharides					sites	RESULTS Five N-glycosylation sites with variable high mannose-type oligosaccharides (Man3-9GlcNAc2) were confirmed in the rKcINU1.
30673159	8	52	gly	glycopeptides	1073:1085	arg2	these glycopeptides			these glycopeptides						glycopeptides	The uptake efficiency and intracellular distribution of these glycopeptides have been systematically characterized by means of flow cytometry and confocal microscopy and in zebrafish animal models.
31102532	4	4	gly	protein	703:709	arg1	mainly high-mannose-type N-glycans	protein			mainly high-mannose-type N-glycans	Fterm		protein			Previously, we knocked out genes encoding α1,2-mannosidase-Is, MAN1A1, MAN1A2 and MAN1B1, in HEK293 cells, establishing a triple-knockout (T-KO) cell line, which produced recombinant protein with mainly high-mannose-type N-glycans.
29301962	3	21	part_of	subunit	509:515	arg1	The active site	STT3 subunit		The active site		PUBTATOR	Site	STT3 subunit	852862	site	The active site of the catalytic STT3 subunit points away from the center of the complex, allowing unhindered access to substrates.
30503329	1	18	gly	glucan/chitin/glycoprotein	163:188	arg1	a glucan/chitin/glycoprotein cell wall matrix	a glucan/chitin/glycoprotein cell wall matrix				Fterm		glucan/chitin/glycoprotein			The formation of a glucan/chitin/glycoprotein cell wall matrix is vital for fungal survival, growth, and morphogenesis.
29716988	1	10	gly	used	262:265	arg2	peptides			peptides						peptides	The complexity of snake venoms has long been investigated to explore a myriad of biologically active proteins and peptides that are used for immobilizing or killing prey, and are responsible for the pathological effects observed on envenomation.
30407002	6	31	gly	tyrosine-protein	990:1005	arg1	tyrosine-protein kinase 7-specific sialic acid			tyrosine	tyrosine-protein kinase 7-specific sialic acid					tyrosine	This strategy has been used to visualize tyrosine-protein kinase 7-specific sialic acid in living CEM cells and zebrafish and to monitor its variation during drug treatment.
30427586	4	8	gly	glycopeptide	897:908	arg2	glycopeptide enrichment			glycopeptide enrichment						glycopeptide	Further, a modified and improved version of cotton hydrophilic interaction liquid chromatography-based solid phase extraction for glycopeptide enrichment is described.
30565163	3	40	gly	sialylated	789:798	arg1	native sialylated oligosaccharide isomers				native sialylated oligosaccharide isomers						We compare MS/MS spectra of five sets of native sialylated oligosaccharide isomers and show a spectral library search method that can distinguish between these isomers using the precursor ion [M+2X-H]+, where X=Li, Na, or K. Sialic acid linkage (α2,3 vs. α2,6) is known to have a dramatic effect on the fragmentation of the sialylated compounds.
31062865	5	74	gly	glycopeptide	1066:1077	arg2	intact glycopeptide characterization			intact glycopeptide characterization						glycopeptide	Using intact glycopeptide characterization, the EPO-Fc was observed to maintain their individual EPO and Fc N-glycan characteristics in which the EPO region presented bi-, tri-, and tetra-branched N-glycan structures, while the Fc N-glycan displayed mostly biantennary glycans.
29548671	6	10	part_of	trimer	1143:1148	arg1	all major exposed regions	trimer		all major exposed regions		Fterm	Site	trimer		regions	HIV-1 neutralization can thus be achieved at the silent face center by glycan-recognizing antibody; along with other known epitopes, the VRC-PG05 epitope completes coverage by neutralizing antibody of all major exposed regions of the prefusion closed trimer.
31393126	10	67	gly	glycoproteins	1565:1577	arg1	these glycoproteins	these glycoproteins				Fterm		glycoproteins			The diversity of N-glycans attached to each single glycosylation site of these glycoproteins confirmed that MRJP1 and MRJP2 heterogeneity was mostly associated with their glycoform populations.
31393126	10	19	gly	attached	1513:1520	arg2	these glycoproteins AND N-glycans	glycoproteins		site	N-glycans	Fterm		glycoproteins		site	The diversity of N-glycans attached to each single glycosylation site of these glycoproteins confirmed that MRJP1 and MRJP2 heterogeneity was mostly associated with their glycoform populations.
31393126	10	73	gly	glycosylation	1537:1549	arg2	each single glycosylation site	glycoproteins		site		Fterm		glycoproteins		site	The diversity of N-glycans attached to each single glycosylation site of these glycoproteins confirmed that MRJP1 and MRJP2 heterogeneity was mostly associated with their glycoform populations.
31332757	5	43	gly	sialylated	885:894	arg1	a natural sialylated N-glycan				a natural sialylated N-glycan						In an alternative way, glycoengineering of antibody with a natural sialylated N-glycan and successive selective oxidation of sialic acid moieties using sodium periodate provided an aldehyde handle on the glycans for conjugation with an aminooxy-assembled payload.
31817903	13	39	gly	glycosylation	1903:1915	arg1	an N-acetylmuramic acid derivative				an N-acetylmuramic acid derivative						To our knowledge, this is the first example of enzymatic glycosylation of an N-acetylmuramic acid derivative.
31669586	3	98	gly	Glycosylation	319:331	arg1	serum proteins	serum proteins				Fterm		proteins			Glycosylation of serum proteins was examined in HT only to a limited extent.
30908021	3	49	gly	hemagglutinin	602:614	arg1	the N-glycans	hemagglutinin			the N-glycans	Fterm		hemagglutinin			Using liquid chromatography-mass spectrometry, we have analyzed the N-glycans of influenza viral hemagglutinin and neuraminidase from several subtypes of influenza vaccines, and utilized the existing resource to establish an N-glycan library consisting of 927 N-glycan structures and 387 sulfated N-glycan compositions.
31025190	3	12	gly	glycosylated	499:510	arg1	glycosylated full-length native hIFNγ homodimers	glycosylated full-length native hIFNγ homodimers				Fterm		homodimers			Here, we report the development of model structures of glycosylated full-length native hIFNγ homodimers.
29343613	9	51	gly	glycoprotein	1597:1608	arg1	restricted HIV-1 Env				restricted HIV-1 Env						That the lectin domain in DAVEIs can utilize MVN without loss of virolytic function argues that restricted HIV-1 Env (envelope glycoprotein) glycan engagement is sufficient for virolysis.
29343613	9	51	gly	glycoprotein	1597:1608	arg1	envelope glycoprotein				envelope glycoprotein						That the lectin domain in DAVEIs can utilize MVN without loss of virolytic function argues that restricted HIV-1 Env (envelope glycoprotein) glycan engagement is sufficient for virolysis.
31423004	1	25	gly	glycosylation	240:252	arg2	all four possible glycosylation sites			all four possible glycosylation sites						sites	Human antithrombin (AT) has two isoforms of which the predominant α-form is glycosylated on all four possible glycosylation sites and the lower abundant β-isoform lacks the oligosaccharide on Asn135.
31423004	1	24	gly	glycosylated	206:217	arg1	all four possible glycosylation sites			sites						sites	Human antithrombin (AT) has two isoforms of which the predominant α-form is glycosylated on all four possible glycosylation sites and the lower abundant β-isoform lacks the oligosaccharide on Asn135.
31256376	15	5	gly	glycopeptides	2213:2225	arg2	glycopeptides			glycopeptides						glycopeptides	Using a mass spectrometer as online detector not only assures the analysis of every component eluting (mass mapping), but also at the same time diagnostic carbohydrate ions can be generated by collisional activation that permits the selective and specific detection of glycopeptides.
29405331	3	73	part_of	contains	474:481	arg1	A1AT AND antennary-fucosylated glycosites	A1AT		antennary-fucosylated glycosites		PUBTATOR	Site	A1AT	5265	glycosites	The serum glycoprotein alpha-1-antitrypsin (A1AT) which contains both core- and antennary-fucosylated glycosites was used in this study.
29405331	3	73	part_of	contains	474:481	arg1	The serum glycoprotein alpha-1-antitrypsin AND antennary-fucosylated glycosites	The serum glycoprotein alpha-1-antitrypsin		antennary-fucosylated glycosites		Fterm	Site	glycoprotein		glycosites	The serum glycoprotein alpha-1-antitrypsin (A1AT) which contains both core- and antennary-fucosylated glycosites was used in this study.
30592755	6	13	gly	glycoproteins	1014:1026	arg1	whole serum glycoproteins	whole serum glycoproteins				Fterm		glycoproteins			RESULTS Total of 51 N-glycans released from whole serum glycoproteins could be reproducibly quantified within which 33 glycoforms were detected in all ethnicities.
30592755	6	40	gly	released	988:995	arg2	whole serum glycoproteins AND 51 N-glycans	whole serum glycoproteins			51 N-glycans	Fterm		glycoproteins			RESULTS Total of 51 N-glycans released from whole serum glycoproteins could be reproducibly quantified within which 33 glycoforms were detected in all ethnicities.
29751008	7	81	gly	glycopeptide	1264:1275	arg2	C'E glycopeptide loop flexibility			C'E glycopeptide loop flexibility						glycopeptide	Finally, a trend of increasing C'E glycopeptide loop flexibility with decreasing glycan size was observed that correlates with their FcγRIIIa receptor binding properties.
29992770	11	55	gly	N-glycopeptides	1559:1573	arg2	These N-glycopeptides			These N-glycopeptides						N-glycopeptides	These N-glycopeptides are the lead candidates for validation as future diagnostic modalities of OSCC as early as stage I.
30959459	3	58	part_of	α-2,6-sialyltransferase	672:694	arg1	the catalytic domain	sialyltransferase		the catalytic domain		PUBTATOR	Site	sialyltransferase	84620	domain	This redox state change was accompanied by loss of two surface-exposed disulfide bonds in the catalytic domain of the α-2,6-sialyltransferase (ST6Gal-I) and its ability to functionally interact with B4GalT-I, an enzyme adding the preceding galactose to complex N-glycans.
29642453	0	48	gly	Glycosylation	0:12	arg1	Hemagglutinin	Hemagglutinin				Fterm		Hemagglutinin			Glycosylation of Hemagglutinin and Neuraminidase of Influenza A Virus as Signature for Ecological Spillover and Adaptation among Influenza Reservoirs.
29529546	2	86	gly	N-glycosylation	406:420	arg1	serum proteins	serum proteins				Fterm		proteins			As depression has been consistently associated with chronic low-grade inflammation, we asked whether patients with Major Depressive Disorder show alterations in the N-glycosylation pattern of serum proteins that might be linked to associated changes in inflammatory processes.
30063822	5	31	part_of	carries	936:942	arg1	a protein AND a single N-glycosylation site	a protein		a single N-glycosylation site		Fterm	Site	protein		site	To illustrate the procedure, we have made an application to a two-domain construct of Robo1, a protein that carries a single N-glycosylation site in its N-terminal domains.
30063822	5	31	part_of	carries	936:942	arg1	Robo1 AND a single N-glycosylation site	Robo1		a single N-glycosylation site		PUBTATOR	Site	Robo1	Q9Y6N7	site	To illustrate the procedure, we have made an application to a two-domain construct of Robo1, a protein that carries a single N-glycosylation site in its N-terminal domains.
31606074	5	17	gly	glycosylated	576:587	arg1	glycosylated neuropeptides			glycosylated neuropeptides						neuropeptides	Here, protocols are presented to isolate and characterize glycosylated neuropeptides utilizing nanoflow liquid chromatography coupled with mass spectrometry (LC-MS).
29535710	1	9	gly	glycoprotein	100:111	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			Immunoglobulin G (IgG), a glycoprotein secreted by plasma B-cells, plays a major role in the human adaptive immune response and are associated with a wide range of diseases.
30990348	9	97	gly	sialylglycopeptides	2604:2622	arg2	hen egg yolk sialylglycopeptides			hen egg yolk sialylglycopeptides						sialylglycopeptides	Abbreviations: ABC, ammonium bicarbonate solution; ACN, acetonitrile; ADCC, antibody-dependent cell-mediated cytotoxicity; C1q, complement component 1q; CDC, complement-dependent cytotoxicity; CQA, critical quality attribute; Endo, endo-β-N-acetylglucosaminidase; FA, formic acid; Fc, crystallizable fragment; FcγR, Fcγ receptors; Fuc, fucose; Gal, galactose; GlcNAc, N-acetylglucosamine; GST, glutathione S-transferase; HER2, human epidermal growth factor receptor 2; HDX, hydrogen-deuterium exchange; HILIC, hydrophilic interaction liquid chromatography; HLB-SPE, hydrophilic-lipophilic balance-solid-phase extraction; HPLC, high-performance liquid chromatography; mAb, monoclonal antibody; Man, mannose; MS, mass spectrometry; PBS, phosphate-buffered saline; SGP, hen egg yolk sialylglycopeptides.
29936827	10	72	gly	O-glycosites	1746:1757	arg2	their dominant O-glycosites			their dominant O-glycosites						O-glycosites	This technique is further applied for analysis of Zika virus recombinant glycoproteins, revealing their dominant O-glycosites and setting a basis set of O-glycosylation tracts in these important viral antigens.
29936827	10	83	gly	glycoproteins	1706:1718	arg1	Zika virus recombinant glycoproteins	Zika virus recombinant glycoproteins				Fterm		glycoproteins			This technique is further applied for analysis of Zika virus recombinant glycoproteins, revealing their dominant O-glycosites and setting a basis set of O-glycosylation tracts in these important viral antigens.
30242110	2	42	gly	glycoforms	404:413	arg1	protein glycoforms	protein glycoforms				Fterm		protein			More than half of the proteins in human serum are glycosylated, and the relative abundances of protein glycoforms often reflect alterations in health and disease.
30909000	7	10	part_of	GO-MAx	1622:1627	arg1	GO-MAx:y composites	MAx		GO-MAx:y composites		OGER	Site	MAx	P61244	composites	Consequently, GO-MAx:y composites could be used as reusable adsorbents for removal/enrichment inorganic/organic substances in aqueous solutions.
29596681	4	47	gly	Asn297	715:720	arg1	the conserved N-glycan			Asn297	the conserved N-glycan					Asn297	In particular, the latter has been demonstrated for therapeutic IgG1 antibodies where the core α1,6Fucose on the conserved N-glycan at Asn297 have remarkable dampening effects on antibody effector functions.
30302011	3	49	part_of	CD4	373:375	arg1	CD4 binding site epitopes	CD4		CD4 binding site epitopes		PUBTATOR	Site	CD4	920	epitopes	Importantly, glycan N301 shields V3 loop and CD4 binding site epitopes from neutralising antibodies.
30959980	6	26	gly	sulfated-sialylated	1087:1105	arg1	sulfated-sialylated glycans				sulfated-sialylated glycans						Sulfated glycans accounted for 58%, unique disufated and sulfated-sialylated glycans were also detected in rabbit intestinal mucin.
30295034	3	60	gly	glycoprotein	636:647	arg1	the glycoprotein species	the glycoprotein species				Fterm		glycoprotein			We find numerous glycan species extending the mass range of the glycoprotein species from 35.0 to 38.5 kDa.
31892825	5	19	gly	α1,3-fucosylated	1396:1411	arg1	plant-specific α1,3-fucosylated and/or β1,2-xylosylated N-glycans				plant-specific α1,3-fucosylated and/or β1,2-xylosylated N-glycans						Our N-glycan structural analysis using purified miraculin, followed by hydrazynolysis, 2-pyridylamine (PA)-labeling, high-performance liquid chromatography, and a liquid chromatography tandem-mass spectrometry analysis revealed that both the native and recombinant miraculins carried an M3 structure as a predominant structure and that most of the N-glycan structures on the miraculins were pauci-mannosidic structures with a smaller amount of plant-specific α1,3-fucosylated and/or β1,2-xylosylated N-glycans and without a Lewis a epitope.
29231704	11	53	gly	glycoproteins	1700:1712	arg1	highly heterogeneous glycoproteins	highly heterogeneous glycoproteins				Fterm		glycoproteins			This approach is a promising tool for global, site-specific glycosylation analysis of highly heterogeneous glycoproteins with mass-limited samples.
29231704	11	72	gly	glycosylation	1653:1665	arg1	highly heterogeneous glycoproteins	highly heterogeneous glycoproteins				Fterm		glycoproteins			This approach is a promising tool for global, site-specific glycosylation analysis of highly heterogeneous glycoproteins with mass-limited samples.
31877766	1	80	gly	glycoprotein	101:112	arg1	a matrix glycoprotein	a matrix glycoprotein				Fterm		glycoprotein			Osteopontin (OPN) is a matrix glycoprotein of urinary calculi.
31154130	9	30	gly	glycopeptide	1480:1491	arg2	36 potential glycopeptide biomarkers			36 potential glycopeptide biomarkers						glycopeptide	Finally, 36 potential glycopeptide biomarkers, including 13 species from IgG1, 12 species from IgG2/3 and 11 species from IgG4 were identified.
30892132	4	65	part_of	epitopes	925:932	arg1	an unconventionally long complementarity-determining region	epitopes		an unconventionally long complementarity-determining region						region	Our analysis reveals that toripalimab mainly binds to the FG loop of PD-1 with an unconventionally long complementarity-determining region 3 loop of the heavy chain, which is distinct from the known binding epitopes of anti-PD-1 mAbs with structural evidences.
29674057	5	17	gly	glycosylation	746:758	arg1	intact pharmaceutical proteins	intact pharmaceutical proteins				Fterm		proteins			We have explored the capacity of hydrophilic liquid chromatography-mass spectrometry (HILIC-MS) for assessing glycosylation patterns of intact pharmaceutical proteins by analyzing the complex glycoproteins interferon-beta-1a (rhIFN-β - 1a) and recombinant human erythropoietin (rhEPO).
29674057	5	20	gly	glycoproteins	828:840	arg1	the complex glycoproteins	the complex glycoproteins				Fterm		glycoproteins			We have explored the capacity of hydrophilic liquid chromatography-mass spectrometry (HILIC-MS) for assessing glycosylation patterns of intact pharmaceutical proteins by analyzing the complex glycoproteins interferon-beta-1a (rhIFN-β - 1a) and recombinant human erythropoietin (rhEPO).
30003921	11	12	gly	glycoproteins	1460:1472	arg1	The glycoproteins	The glycoproteins				Fterm		glycoproteins			The glycoproteins do not form stable complexes with BinA, however, as observed in the pull-down assay using affinity immobilized BinA and in native-PAGE analysis.
30673210	1	15	gly	glycopeptides	309:321	arg2	glycopeptides detection			glycopeptides detection						glycopeptides	In the study of glycoproteomics with mass spectrometry, certain pretreatments of samples are required for eliminating the interference of nonglycopeptides and improving the efficiency of glycopeptides detection.
30673210	1	31	gly	nonglycopeptides	260:275	arg2	nonglycopeptides			nonglycopeptides						nonglycopeptides	In the study of glycoproteomics with mass spectrometry, certain pretreatments of samples are required for eliminating the interference of nonglycopeptides and improving the efficiency of glycopeptides detection.
31430121	5	77	gly	site	1167:1170	arg1	glucosamine (GlcN) located +2			site	glucosamine (GlcN) located +2					site	These analogs served as effective DspB substrates, and the rate of hydrolysis was dependent on the specific substrate de-N-acetylation pattern, with glucosamine (GlcN) located +2 from the site of cleavage being preferentially hydrolyzed.
31000718	7	38	gly	glycoprotein	1192:1203	arg1	N-linked glycoprotein biosynthesis	N-linked glycoprotein biosynthesis				Fterm		glycoprotein			Reconstitution of the LLO pathway to synthesize Man9GlcNAc2 in vitro provides an important tool for functional studies of the N-linked glycoprotein biosynthesis pathway.
30295034	4	11	gly	glycosylation	763:775	arg2	all glycosylation sites			all glycosylation sites						sites	The dominant glycan compositions contain tri- and tetraantennary structures on all glycosylation sites.
30295034	4	0	gly	contain	713:719	arg1	all glycosylation sites AND The dominant glycan compositions			all glycosylation sites	The dominant glycan compositions					sites	The dominant glycan compositions contain tri- and tetraantennary structures on all glycosylation sites.
30295034	4	0	gly	contain	713:719	arg1	all glycosylation sites AND tri- and tetraantennary structures			all glycosylation sites	tri- and tetraantennary structures					sites	The dominant glycan compositions contain tri- and tetraantennary structures on all glycosylation sites.
29888905	3	91	gly	glycoproteins	566:578	arg1	N-glycans	glycoproteins			N-glycans	Fterm		glycoproteins			Here, we describe a strategy for high-resolution quantitative profiling and structure elucidation of N-glycans from EV glycoproteins of three cell lines: human HEK-293, human glioma H4 and mouse glioma Tu-2449.
30063822	6	36	gly	used	1119:1122	arg2	sites			sites						sites	The construct has also been labeled with 15N at amide nitrogens of lysine residues to provide a set of sites that are used to derive an effective location of the paramagnetic nitroxide moiety of the TEMPO group.
31373757	3	9	gly	fucosylation	497:508	arg1	O-glycans				O-glycans						These aberrant modifications affect different aspects of glycosylation, including an increase in core fucosylation and GlcNAc branching on N-glycans, alteration of O-glycans, upregulated sialylation, and O-GlcNAcylation.
31373757	3	9	gly	fucosylation	497:508	arg1	N-glycans				N-glycans						These aberrant modifications affect different aspects of glycosylation, including an increase in core fucosylation and GlcNAc branching on N-glycans, alteration of O-glycans, upregulated sialylation, and O-GlcNAcylation.
31373757	3	33	gly	sialylation	582:592	arg1	O-glycans				O-glycans						These aberrant modifications affect different aspects of glycosylation, including an increase in core fucosylation and GlcNAc branching on N-glycans, alteration of O-glycans, upregulated sialylation, and O-GlcNAcylation.
31373757	3	33	gly	sialylation	582:592	arg1	N-glycans				N-glycans						These aberrant modifications affect different aspects of glycosylation, including an increase in core fucosylation and GlcNAc branching on N-glycans, alteration of O-glycans, upregulated sialylation, and O-GlcNAcylation.
31738061	1	71	gly	glycoproteins	224:236	arg1	O-	glycoproteins			O-	Fterm		glycoproteins			The human natural killer-1 (HNK-1) epitope is a unique sulfated trisaccharide sequence presented on O- and N-glycans of various glycoproteins and on glycolipids.
30002445	5	7	gly	glycosylation	1023:1035	arg1	target proteins	target proteins				Fterm		proteins			The resulting extracts enable a one-pot reaction scheme for efficient and site-specific glycosylation of target proteins.
31174130	3	22	part_of	IgG	584:586	arg1	IgG N-glycopeptides	IgG		IgG N-glycopeptides		Cterm	Site	IgG		N-glycopeptides	The glycopeptide enrichment efficacy of the titania-based sol-gel material was evaluated by the enrichment of IgG N-glycopeptides from their proteolytic products.
30612270	3	39	gly	glycoprotein	613:624	arg1	the glycoprotein	the glycoprotein				Fterm		glycoprotein			Mass spectrometry is most commonly used to characterize and quantify glycopeptides and glycans liberated from the glycoprotein of interest.
30612270	3	62	gly	glycopeptides	568:580	arg2	glycopeptides			glycopeptides						glycopeptides	Mass spectrometry is most commonly used to characterize and quantify glycopeptides and glycans liberated from the glycoprotein of interest.
30375138	4	20	gly	peptide	814:820	arg1	a commercially available peptide synthesizer				a commercially available peptide synthesizer						This study represents a proof-of-concept demonstration that the enzymatic synthesis of oligosaccharides can be achieved in an automated manner using a commercially available peptide synthesizer.
31507595	1	6	gly	glycosylation	166:178	arg2	asparagine 3			asparagine 3						asparagine 3	Human CD52 is a small glycopeptide (12 amino acid residues) with one N-linked glycosylation site at asparagine 3 (Asn3) and several potential O-glycosylation serine/threonine sites.
31507595	1	6	gly	glycosylation	166:178	arg2	one N-linked glycosylation site			one N-linked glycosylation site						site	Human CD52 is a small glycopeptide (12 amino acid residues) with one N-linked glycosylation site at asparagine 3 (Asn3) and several potential O-glycosylation serine/threonine sites.
31507595	1	6	gly	glycosylation	166:178	arg2	Asn3			Asn3						Asn3	Human CD52 is a small glycopeptide (12 amino acid residues) with one N-linked glycosylation site at asparagine 3 (Asn3) and several potential O-glycosylation serine/threonine sites.
31507595	1	6	gly	glycosylation	166:178	arg2	several potential O-glycosylation serine/threonine sites			several potential O-glycosylation serine/threonine sites						sites	Human CD52 is a small glycopeptide (12 amino acid residues) with one N-linked glycosylation site at asparagine 3 (Asn3) and several potential O-glycosylation serine/threonine sites.
31507595	1	20	gly	glycopeptide	110:121	arg2	12 amino acid residues			12 amino acid residues						residues	Human CD52 is a small glycopeptide (12 amino acid residues) with one N-linked glycosylation site at asparagine 3 (Asn3) and several potential O-glycosylation serine/threonine sites.
31507595	1	20	gly	glycopeptide	110:121	arg2	a small glycopeptide			a small glycopeptide						glycopeptide	Human CD52 is a small glycopeptide (12 amino acid residues) with one N-linked glycosylation site at asparagine 3 (Asn3) and several potential O-glycosylation serine/threonine sites.
31507595	1	48	gly	O-glycosylation	230:244	arg2	several potential O-glycosylation serine/threonine sites			several potential O-glycosylation serine/threonine sites						sites	Human CD52 is a small glycopeptide (12 amino acid residues) with one N-linked glycosylation site at asparagine 3 (Asn3) and several potential O-glycosylation serine/threonine sites.
31558607	2	10	part_of	carries	380:386	arg1	ProBDNF AND a single N-glycosylation sequon	ProBDNF		a single N-glycosylation sequon		PUBTATOR	Site	ProBDNF	627	sequon	ProBDNF carries a single N-glycosylation sequon (Asn-127) that remains virtually unstudied despite being located in a highly conserved region proximal to the proteolytic site.
29888865	13	53	part_of	Galα1,3	2320:2326	arg1	Galα1,3 Gal epitopes	Gal		Galα1,3 Gal epitopes		OGER	Site	Gal	Q8N6F7	epitopes	Although the proportion of biologically important epitopes common to all samples (i.e. sialylation and high-mannose) varied between samples, some recombinant products expressed distinct and immunologically relevant epitopes, such as LacdiNAc (LDN), fucosylated LacdiNAc (FucLDN), NeuGc, LewisX/Y and Galα1,3 Gal epitopes.
29888865	13	111	part_of	Gal	2328:2330	arg1	Galα1,3 Gal epitopes	Gal		Galα1,3 Gal epitopes		OGER	Site	Gal	Q8N6F7	epitopes	Although the proportion of biologically important epitopes common to all samples (i.e. sialylation and high-mannose) varied between samples, some recombinant products expressed distinct and immunologically relevant epitopes, such as LacdiNAc (LDN), fucosylated LacdiNAc (FucLDN), NeuGc, LewisX/Y and Galα1,3 Gal epitopes.
29340583	7	65	gly	glycoprotein	1121:1132	arg1	the first H. pullorum N-linked glycoprotein	the first H. pullorum N-linked glycoprotein				Fterm		glycoprotein			In this study, we identified the first H. pullorum N-linked glycoprotein, termed HgpA.
31098956	1	40	gly	structure	177:185	arg1	sequence			sequence						sequence	N-linked glycosylation is one of the most common protein PTMs, and the topological structure (monosaccharide composition and sequence as well as glycosidic linkages) of N-glycans is vital information to understand their biological functions and roles.
29596458	13	42	gly	N-glycopeptides	1801:1815	arg2	high-confidence N-glycopeptides			high-confidence N-glycopeptides						N-glycopeptides	We propose high-confidence N-glycopeptides which have the power to separate the bloodstream infections from blood culture negative febrile patients and shed light on host response during bacteremia.
29535710	4	28	gly	glycopeptides	707:719	arg2	liquid chromatography electrospray mass spectrometry (LC-ESI-MS)-measured IgG glycopeptides			liquid chromatography electrospray mass spectrometry (LC-ESI-MS)-measured IgG glycopeptides						glycopeptides	To identify genetic loci involved in IgG glycosylation, we performed a genome-wide association study (GWAS) on liquid chromatography electrospray mass spectrometry (LC-ESI-MS)-measured IgG glycopeptides of 1,823 individuals in the Cooperative Health Research in the Augsburg Region (KORA F4) study cohort.
30973186	3	9	gly	N-glycosylation	399:413	arg2	the N-glycosylation sites 24, 38, and 83			the N-glycosylation sites 24, 38, and 83						sites	EPO variants with an alkyne-bearing non-natural amino acid (Plk) at the N-glycosylation sites 24, 38, and 83 were obtained by amber suppression followed by protein purification and refolding.
31370181	1	6	gly	glycosylation	161:173	arg1	recombinant viral glycoproteins	recombinant viral glycoproteins				Fterm		glycoproteins			The ability to control the glycosylation pattern of recombinant viral glycoproteins represents a major prerequisite before their use as vaccines.
31370181	1	16	gly	glycoproteins	204:216	arg1	recombinant viral glycoproteins	recombinant viral glycoproteins				Fterm		glycoproteins			The ability to control the glycosylation pattern of recombinant viral glycoproteins represents a major prerequisite before their use as vaccines.
31732167	3	47	part_of	furin	592:596	arg1	the furin cleavage site	furin		the furin cleavage site		PUBTATOR	Site	furin	5045	site	The exceptions to the contiguous glycan shield include the conserved receptor CD4 binding site (CD4bs) and glycoprotein (gp)41 elements proximal to the furin cleavage site.
31732167	3	53	part_of	CD4	518:520	arg1	receptor CD4 binding site	CD4		receptor CD4 binding site		PUBTATOR	Site	CD4	920	site	The exceptions to the contiguous glycan shield include the conserved receptor CD4 binding site (CD4bs) and glycoprotein (gp)41 elements proximal to the furin cleavage site.
31468229	4	21	gly	glycoprotein	893:904	arg1	relative carbohydrate mass	glycoprotein			relative carbohydrate mass	Fterm		glycoprotein			N-Glycoprofiling analysis of G-hPRL provided: (i) identification of each N-glycan structure and relative intensity; (ii) average N-glycan mass; (iii) molecular mass of the whole glycoprotein and relative carbohydrate mass fraction; (iv) mass fraction of each monosaccharide.
31468229	4	21	gly	glycoprotein	893:904	arg1	average N-glycan mass	glycoprotein			average N-glycan mass	Fterm		glycoprotein			N-Glycoprofiling analysis of G-hPRL provided: (i) identification of each N-glycan structure and relative intensity; (ii) average N-glycan mass; (iii) molecular mass of the whole glycoprotein and relative carbohydrate mass fraction; (iv) mass fraction of each monosaccharide.
31759178	8	69	gly	N-glycopeptides	1966:1980	arg2	581 intact N-glycopeptides			581 intact N-glycopeptides						N-glycopeptides	With spectrum-level FDR ≤ 1%, 581 intact N-glycopeptides with comprehensive structural information of both the peptide backbones and the N-glycan moieties were identified; For the 248 putative N-glycosites, 248 were confirmed where 125 have not been annotated in UniProt as of July 25, 2019.
31759178	8	120	gly	N-glycosites	2118:2129	arg2	the 248 putative N-glycosites			the 248 putative N-glycosites						N-glycosites	With spectrum-level FDR ≤ 1%, 581 intact N-glycopeptides with comprehensive structural information of both the peptide backbones and the N-glycan moieties were identified; For the 248 putative N-glycosites, 248 were confirmed where 125 have not been annotated in UniProt as of July 25, 2019.
29740059	6	29	gly	di-sialylated	1216:1228	arg1	di-sialylated N-glycan structures				di-sialylated N-glycan structures						Furthermore, a detailed analysis of the resulting N-glycan structures using LC/MS revealed increased tri- and tetra- sialylated N-glycan structures accompanied by a reduction of di-sialylated N-glycan structures.
29740059	6	57	gly	sialylated	1155:1164	arg1	sialylated N-glycan structures				sialylated N-glycan structures						Furthermore, a detailed analysis of the resulting N-glycan structures using LC/MS revealed increased tri- and tetra- sialylated N-glycan structures accompanied by a reduction of di-sialylated N-glycan structures.
31747749	1	28	gly	N-glycosylation	44:58	arg1	total human plasma proteins	total human plasma proteins				Fterm		proteins			The N-glycosylation profile of total human plasma proteins could be a useful biomarker for various pathological states.
31349756	2	37	gly	glycoprotein	379:390	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			Like typical recombinant IgG-based therapeutics, atacicept is a glycoprotein whose glycosylation-related heterogeneity arises from the glycosylation-site localization, site-specific occupation and structural diversity of the attached glycans.
30542567	1	14	gly	glycopeptides	117:129	arg2	N-Linked glycopeptides			N-Linked glycopeptides						glycopeptides	N-Linked glycopeptides have highly diverse structures in nature.
31031563	3	80	gly	glycosylation	436:448	arg1	cell surface proteins	cell surface proteins				Fterm		proteins			Changes in the glycosylation of cell surface proteins is another common feature of cancer progression.
31398379	4	7	gly	fucosylated	1301:1311	arg1	more fucosylated and fewer Man4/5-based hybrid glycans				more fucosylated and fewer Man4/5-based hybrid glycans						In comparison to honeybee royal jelly, there were more fucosylated and fewer Man4/5-based hybrid glycans in the larvae and venom samples as well as contrasting antennal lengths.
31256376	7	20	gly	O-glycosylation	897:911	arg2	Thr			Ser, Thr, and Tyr residues						Ser, Thr, and Tyr residues	O-glycosylation occurs at Ser, Thr, and Tyr residues, usually in sequence stretches rich in hydroxy-amino acids.
31256376	7	20	gly	O-glycosylation	897:911	arg2	Ser			Ser, Thr, and Tyr residues						Ser, Thr, and Tyr residues	O-glycosylation occurs at Ser, Thr, and Tyr residues, usually in sequence stretches rich in hydroxy-amino acids.
31256376	7	20	gly	O-glycosylation	897:911	arg2	Ser			Ser, Thr, and Tyr residues						Ser, Thr, and Tyr residues	O-glycosylation occurs at Ser, Thr, and Tyr residues, usually in sequence stretches rich in hydroxy-amino acids.
29529546	8	22	gly	N-glycosylation	1720:1734	arg1	serum proteins	serum proteins				Fterm		proteins			CONCLUSION The results offer the first evidence that specific differences in the N-glycosylation pattern of serum proteins constitute a so far unrecognized level of biological alterations that might be involved in the immune changes associated with MDD.
31301102	2	9	part_of	Fc	299:300	arg1	the antibody Fc region	Fc		the antibody Fc region		Cterm	Site	Fc		region	Glycan structures in the antibody Fc region influence binding properties to Fc receptors, which opens opportunities for modulation of antibody effector functions.
29231704	3	79	gly	N-glycopeptide	580:593	arg2	superior N-glycopeptide analysis			superior N-glycopeptide analysis						N-glycopeptide	In this paper, we combine the two techniques to achieve superior N-glycopeptide analysis.
29535710	2	46	part_of	IgGs	290:293	arg1	the Fc binding region	IgGs		the Fc binding region		Cterm	Site	IgGs		region	Glycosylation of the Fc binding region of IgGs, responsible for the antibody's effector function, is essential for prompting a proper immune response.
29936827	7	10	gly	O-glycosylated	1164:1177	arg1	O-glycosylated peptides			O-glycosylated peptides						peptides	This method enables the assignment of O-glycosylated peptides, N-glycan profile, sialyl O-glycopeptides linkage, and mapping of heterogeneous O-glycosylation.
29936827	7	96	gly	peptides	1179:1186	arg1	N-glycan profile			peptides	N-glycan profile					peptides	This method enables the assignment of O-glycosylated peptides, N-glycan profile, sialyl O-glycopeptides linkage, and mapping of heterogeneous O-glycosylation.
29936827	7	100	gly	O-glycopeptides	1214:1228	arg2	sialyl O-glycopeptides linkage			sialyl O-glycopeptides linkage						O-glycopeptides	This method enables the assignment of O-glycosylated peptides, N-glycan profile, sialyl O-glycopeptides linkage, and mapping of heterogeneous O-glycosylation.
31384044	1	21	gly	O-glycoproteins	268:282	arg1	O-glycoproteins	O-glycoproteins				Fterm		O-glycoproteins			We report a liquid chromatography coupled to tandem mass spectrometry O-glycoproteomics strategy using data-independent acquisition (DIA) mode for direct analysis of O-glycoproteins.
31754374	13	36	gly	N5 N-glycosylation	2179:2196	arg2	N5 N-glycosylation sites			N5 N-glycosylation sites						sites	Molecular dynamics simulations of BxlBnon-glyc and BxlBN1;5 reveals that the mobility pattern of structural elements in the vicinity of the catalytic pocket changes upon N1 and N5 N-glycosylation sites, enhancing substrate binding properties which may underlie the observed differences in catalytic efficiency between BxlBnon-glyc and BxlBN1;5.
30708139	5	61	gly	N-glycosylation	856:870	arg2	new N-glycosylation sites			new N-glycosylation sites						sites	As the first step, we explored the amino acid sequence of LH to find out desirable positions for introducing Asn or/and Thr to create new N-glycosylation sites.
29618644	3	68	gly	glycosylation	496:508	arg2	N-linked glycosylation sites			N-linked glycosylation sites						sites	We found that sequence polymorphisms in the V3 loop and N-linked glycosylation sites contribute only minimally to the high neutralization resistance of 253-11.
29330305	2	21	gly	asparagine-linked	571:587	arg1	N-glycans			asparagine	N-glycans					asparagine	Therapeutic monoclonal antibodies (mAbs) with greater Fc-mediated affinity for CD16a show superior therapeutic outcome; however, one significant factor that promotes antibody-CD16a interactions, the asparagine-linked carbohydrates (N-glycans), remains undefined.
29330305	2	21	gly	asparagine-linked	571:587	arg1	the asparagine-linked carbohydrates			asparagine	the asparagine-linked carbohydrates					asparagine	Therapeutic monoclonal antibodies (mAbs) with greater Fc-mediated affinity for CD16a show superior therapeutic outcome; however, one significant factor that promotes antibody-CD16a interactions, the asparagine-linked carbohydrates (N-glycans), remains undefined.
31311856	6	19	gly	O-glycosylated	1398:1411	arg1	O-glycosylated proteins	O-glycosylated proteins				Fterm		proteins			Our findings provide evidence in support of a regulated pathway for the degradation of O-glycoproteins in yeast and offer critical insights into the catabolic mechanisms that control the fate of O-glycosylated proteins.
31311856	6	66	gly	O-glycoproteins	1290:1304	arg1	O-glycoproteins	O-glycoproteins				Fterm		O-glycoproteins			Our findings provide evidence in support of a regulated pathway for the degradation of O-glycoproteins in yeast and offer critical insights into the catabolic mechanisms that control the fate of O-glycosylated proteins.
29548671	3	13	gly	N448	581:584	arg1	N-linked glycans			N262, N295, and N448	N-linked glycans					N262, N295, and N448	The crystal structure of the antigen-binding fragment of VRC-PG05 in complex with gp120 revealed an epitope comprised primarily of N-linked glycans from N262, N295, and N448 at the silent face center.
29548671	3	16	gly	N262	565:568	arg1	N-linked glycans			N262, N295, and N448	N-linked glycans					N262, N295, and N448	The crystal structure of the antigen-binding fragment of VRC-PG05 in complex with gp120 revealed an epitope comprised primarily of N-linked glycans from N262, N295, and N448 at the silent face center.
29548671	3	23	gly	N295	571:574	arg1	N-linked glycans			N262, N295, and N448	N-linked glycans					N262, N295, and N448	The crystal structure of the antigen-binding fragment of VRC-PG05 in complex with gp120 revealed an epitope comprised primarily of N-linked glycans from N262, N295, and N448 at the silent face center.
29941589	5	46	gly	glycoprotein	886:897	arg1	GP2 fusion glycoprotein	GP2 fusion glycoprotein				Fterm		glycoprotein			Our analysis reveals the presence of underprocessed oligomannose-type glycans, which form punctuated clusters that obscure the proteinous surface of both the GP1 attachment and GP2 fusion glycoprotein subunits of the Lassa virus GPC.
29976678	15	19	part_of	protein	2474:2480	arg1	even a buried region	protein can		even a buried region		OGER	Site	protein can	P35658	region	In characterizing these viruses, we found that the strength of antibody binding to an epitope is the major determinant of the neutralization potential of an antibody, that even a buried region of the envelope protein can be efficiently targeted, and that the sole potential envelope glycan does not impact nearby epitope antibody binding and neutralization.
31040211	11	46	gly	glycoproteins	1925:1937	arg1	HCV envelope glycoproteins	HCV envelope glycoproteins				Fterm		glycoproteins			This importance of structural dynamics of HCV envelope glycoproteins has critical implications for vaccine development and suggests that similar phenomena could contribute to immune evasion of other viruses.
31759178	5	39	gly	N-glycoproteins	1295:1309	arg1	19 intact N-glycoproteins	19 intact N-glycoproteins				Fterm		N-glycoproteins			With the criteria of quantified at least thrice out of the five technical replicates with no <1.5-fold change, p ≤ .05 and RSD ≤ 20%, 56 DEGPs were quantified from 23 N-glycosites on 19 intact N-glycoproteins.
31759178	5	49	gly	23 N-glycosites	1266:1280	arg2	23 N-glycosites			23 N-glycosites						23 N-glycosites	With the criteria of quantified at least thrice out of the five technical replicates with no <1.5-fold change, p ≤ .05 and RSD ≤ 20%, 56 DEGPs were quantified from 23 N-glycosites on 19 intact N-glycoproteins.
31453603	4	96	gly	glycopeptides	780:792	arg2	glycopeptides			glycopeptides						glycopeptides	Nevertheless, the physical and chemical characteristics of glycopeptides that dictate their mass vs. mobility loci have yet to be systematically investigated.
30224661	4	14	gly	N-glycopeptides	680:694	arg2	N-glycopeptides			N-glycopeptides						N-glycopeptides	Profiles of N-glycopeptides revealed that plants carrying the ugnt1 loss-of-function allele are virtually devoid of complex and hybrid N-glycans.
30177739	7	1	gly	non-fucosylated	1317:1331	arg1	not non-fucosylated glycans				not non-fucosylated glycans						Moreover the adherence of B. subtilis to intestinal cells was significantly inhibited by Lex and Ley but by not non-fucosylated glycans, suggesting the interaction of YesU to fucosylated glycans may be involved in the adhesion of B. subtilis to the gastrointestinal tract of mammals.
30177739	7	22	gly	fucosylated	1380:1390	arg1	fucosylated glycans				fucosylated glycans						Moreover the adherence of B. subtilis to intestinal cells was significantly inhibited by Lex and Ley but by not non-fucosylated glycans, suggesting the interaction of YesU to fucosylated glycans may be involved in the adhesion of B. subtilis to the gastrointestinal tract of mammals.
31838284	6	54	gly	sulphated/penta-sialylated	1164:1189	arg1	sulphated/penta-sialylated N-glycans				sulphated/penta-sialylated N-glycans						The products exhibit notable differences in N- and O-glycosylation, including attributes such as sialic acid occupation, O-acetylation, N-acetyllactosamine extended antennae and sulphated/penta-sialylated N-glycans, which have the potential to cause divergence of therapeutic potencies.
30739313	1	2	gly	glycoproteins	169:181	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Mucin-type O-glycans have profound effects on the structure and stability of glycoproteins.
29595997	4	38	gly	glycoprotein	758:769	arg1	the complex structure	glycoprotein			the complex structure	Fterm		glycoprotein			Therefore, considerable efforts have been made in developing and validating biophysical methods to elucidate the complex structure of the Env-spike glycoprotein, with its combination of glycan and protein epitopes.
30325416	3	84	gly	core-fucosylation	366:382	arg1	IgG Fc-glycans				IgG Fc-glycans						Indeed, while core-fucosylation of IgG Fc-glycans greatly affects the antibody-dependent cell-mediated cytotoxicity function, with obvious repercussions in the design of therapeutic antibodies, sialylation can reverse the antibody inflammatory response, and galactosylation levels have been linked to aging, to the onset of inflammation, and to the predisposition to rheumatoid arthritis.
31154130	4	4	gly	glycopeptides	690:702	arg2	IgG-Fc glycopeptides			IgG-Fc glycopeptides						glycopeptides	We herein report an integrated approach for comprehensive profiling and quantitation of IgG-Fc glycopeptides.
30674035	6	82	gly	α2,6-sialylated	1062:1076	arg1	agalacto-, mono-, and digalactosylated as well as α2,6-sialylated structures				agalacto-, mono-, and digalactosylated as well as α2,6-sialylated structures						The N-glycosylation profile of ALS CSF IgG consisted of diantennary N-glycans predominantly with proximal fucose and some bisecting GlcNAc; agalacto-, mono-, and digalactosylated as well as α2,6-sialylated structures were detected.
31606074	0	43	gly	glycosylated	34:45	arg1	glycosylated neuropeptides			glycosylated neuropeptides						neuropeptides	Isolation and characterization of glycosylated neuropeptides.
29642453	1	58	gly	Glycosylation	151:163	arg1	the hemagglutinin	the hemagglutinin				Fterm		hemagglutinin			Glycosylation of the hemagglutinin (HA) and neuraminidase (NA) of the influenza provides crucial means for immune evasion and viral fitness in a host population.
30186849	5	47	gly	glycoprotein	1156:1167	arg1	a complex glycoprotein data set	a complex glycoprotein data set				Fterm		glycoprotein			The efficiency and reliability of pMatchGlyco were demonstrated on a data set of mixture sample of six standard glycoproteins and a complex glycoprotein data set generated from human cancer cell line OVCAR3.
30186849	5	56	gly	glycoproteins	1128:1140	arg1	six standard glycoproteins	six standard glycoproteins				Fterm		glycoproteins			The efficiency and reliability of pMatchGlyco were demonstrated on a data set of mixture sample of six standard glycoproteins and a complex glycoprotein data set generated from human cancer cell line OVCAR3.
29463753	2	30	gly	glycosylation	267:279	arg2	potential N-linked glycosylation sites			potential N-linked glycosylation sites						sites	One such signature involves a reduced number of potential N-linked glycosylation sites (PNGs).
31754374	8	45	gly	N-glycosylation	1331:1345	arg2	four new N-glycosylation sites			four new N-glycosylation sites						sites	Additionally, there was no enzyme secretion in the mutant in which the N-glycosylation context was changed by the introduction of four new N-glycosylation sites (BxlBCC), despite the high transcript levels.
31501225	5	80	gly	N-glycopeptide	813:826	arg2	N-glycopeptide			N-glycopeptide						N-glycopeptide	Then, multiple reaction monitoring (MRM) was performed to quantify N-glycopeptide relative to the protein content, especially in the healthy donor-HBV-LC-HCC cascade.
31905645	11	12	part_of	PBS/MCC	1647:1653	arg1	the PBS/MCC composites	MCC		the PBS/MCC composites		OGER	Site	MCC		composites	Scanning electron microscopy analysis evidenced the agglomeration of the MCC in the PBS/MCC composites.
31531180	1	13	part_of	composition	148:158	arg1	Yingshan Cloud Mist Tea	Mist Tea		composition		OGER	Site	Mist Tea	Q7Z7G1	position	The study was designed to investigate the chemical composition and antioxidant activities of polysaccharides from Yingshan Cloud Mist Tea.
31531180	1	45	part_of	Tea	231:233	arg1	chemical composition	Mist Tea		chemical composition		OGER	Site	Mist Tea	Q7Z7G1	position	The study was designed to investigate the chemical composition and antioxidant activities of polysaccharides from Yingshan Cloud Mist Tea.
31130941	3	60	part_of	IgA	722:724	arg1	a single proteolytic cleavage site	IgA		a single proteolytic cleavage site		PUBTATOR	Site	IgA	973	site	Mapping preferential sites of proteolytic activity showed a single proteolytic cleavage site of native plasma IgA (pIgA) in the Fc-tail; as well as in the secretory component (SC) of secretory IgA (SIgA).
29976678	12	112	gly	glycoprotein	1946:1957	arg1	the envelope glycoprotein	the envelope glycoprotein				Fterm		glycoprotein			The structure of the mature ZIKV particle reveals a virion surface covered by the envelope glycoprotein, which is the dominant target of the humoral immune response.
30553311	9	9	gly	residue	1200:1206	arg1	total carbohydrates			residue	total carbohydrates					residue	Analysis of chemical characterization showed that PHP contained 75.36 ± 1.48% of total carbohydrates, 24.63 ± 1.69% of uronic acid residue and no proteins with monosaccharides such as rhamnose, arabinose, xylose, mannose, glucose, and galactose in a molar ratio of 10.25:9.38:1:12.45:9.9:11.55.
30553311	9	28	gly	proteins	1215:1222	arg1	rhamnose	proteins			rhamnose	Fterm		proteins			Analysis of chemical characterization showed that PHP contained 75.36 ± 1.48% of total carbohydrates, 24.63 ± 1.69% of uronic acid residue and no proteins with monosaccharides such as rhamnose, arabinose, xylose, mannose, glucose, and galactose in a molar ratio of 10.25:9.38:1:12.45:9.9:11.55.
30553311	9	28	gly	proteins	1215:1222	arg1	monosaccharides	proteins			monosaccharides	Fterm		proteins			Analysis of chemical characterization showed that PHP contained 75.36 ± 1.48% of total carbohydrates, 24.63 ± 1.69% of uronic acid residue and no proteins with monosaccharides such as rhamnose, arabinose, xylose, mannose, glucose, and galactose in a molar ratio of 10.25:9.38:1:12.45:9.9:11.55.
30902814	4	31	part_of	receptor-binding	524:539	arg1	the receptor-binding domain	receptor		the receptor-binding domain		Fterm	Site	receptor		domain	Here, we analyzed the N-glycosylation of the receptor-binding domain (RBD) of IBV strain M41 spike protein and assessed the role of this modification in host receptor binding.
30902814	4	48	part_of	protein	578:584	arg1	the receptor-binding domain	protein		the receptor-binding domain		Fterm	Site	protein		domain	Here, we analyzed the N-glycosylation of the receptor-binding domain (RBD) of IBV strain M41 spike protein and assessed the role of this modification in host receptor binding.
30651366	11	54	part_of	protein	2205:2211	arg1	conserved regions	protein		conserved regions		Fterm	Site	protein		regions	A major challenge for vaccine development is focusing the immune response on conserved regions of the HCV envelope protein, E2, capable of eliciting neutralizing antibodies.
29535710	2	54	gly	Glycosylation	248:260	arg1	the Fc binding region			the Fc binding region						region	Glycosylation of the Fc binding region of IgGs, responsible for the antibody's effector function, is essential for prompting a proper immune response.
31500407	6	12	part_of	motifs	1003:1008	arg1	the mucin cytoplasmic tail	motifs		the mucin cytoplasmic tail						tail	Glycosylation could also be influenced through recycling motifs on the mucin cytoplasmic tail.
31500407	6	43	part_of	mucin	1017:1021	arg1	the mucin cytoplasmic tail	mucin		the mucin cytoplasmic tail		PUBTATOR	Site	mucin	100508689	tail	Glycosylation could also be influenced through recycling motifs on the mucin cytoplasmic tail.
31526239	3	94	gly	N-glycosylation	477:491	arg1	proteins	proteins				Fterm		proteins			N-glycosylation of proteins is one of the most frequently observed co- and post-translational modifications, reflecting, importantly, the real-time status of the interplay between the genomic and postgenomic factors.
29642453	2	26	gly	glycosylation	358:370	arg2	each glycosylation sites			each glycosylation sites						sites	However, the time-dependent dynamics of each glycosylation sites have not been addressed.
30898876	1	11	gly	glycoproteins	365:377	arg1	many mammalian glycoproteins	many mammalian glycoproteins				Fterm		glycoproteins			The type-I LacdiNAc (LDN; GalNAcβ1-3GlcNAc) has rarely been observed in mammalian cells except in the O-glycan of α-dystroglycan, in contrast to type-II LDN structures (GalNAcβ1-4GlcNAc) in N- and O-glycans that are present in many mammalian glycoproteins, such as pituitary and hypothalamic hormones.
30898876	1	69	gly	present	339:345	arg1	many mammalian glycoproteins AND O-glycans	glycoproteins			O-glycans	Fterm		glycoproteins			The type-I LacdiNAc (LDN; GalNAcβ1-3GlcNAc) has rarely been observed in mammalian cells except in the O-glycan of α-dystroglycan, in contrast to type-II LDN structures (GalNAcβ1-4GlcNAc) in N- and O-glycans that are present in many mammalian glycoproteins, such as pituitary and hypothalamic hormones.
30898876	1	69	gly	present	339:345	arg1	many mammalian glycoproteins AND N-	glycoproteins			N-	Fterm		glycoproteins			The type-I LacdiNAc (LDN; GalNAcβ1-3GlcNAc) has rarely been observed in mammalian cells except in the O-glycan of α-dystroglycan, in contrast to type-II LDN structures (GalNAcβ1-4GlcNAc) in N- and O-glycans that are present in many mammalian glycoproteins, such as pituitary and hypothalamic hormones.
30537828	1	11	gly	glycoproteins	183:195	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			The glycan part of glycoproteins is known to be involved in the structure and modulatory functions of glycoproteins, serving as ligands for cell-to-cell interactions, and as specific ligands for cell-to-microbe interactions.
30537828	1	43	gly	glycoproteins	100:112	arg1	The glycan part	glycoproteins			The glycan part	Fterm		glycoproteins			The glycan part of glycoproteins is known to be involved in the structure and modulatory functions of glycoproteins, serving as ligands for cell-to-cell interactions, and as specific ligands for cell-to-microbe interactions.
31000718	1	46	gly	glycoprotein	153:164	arg1	glycoprotein folding	glycoprotein folding				Fterm		glycoprotein			The asparagine (N)-linked Man9GlcNAc2 is required for glycoprotein folding and secretion.
29725729	3	13	gly	information	946:956	arg1	sequence			sequence						sequence	Mass spectrometry-based glycomics is currently the state-of-the-art instrumental analytical pipeline for high-throughput characterization of various glycoforms, where not only monosaccharide composition but also comprehensive structural information (sequence and linkage) of N-glycans are now reported thanks to our recently developed N-glycan database search engine GlySeeker.
29231704	9	49	gly	pentasialylated	1362:1376	arg1	unusual pentasialylated terminal sialic acids				unusual pentasialylated terminal sialic acids						Glycans included tetra-sialic acids with multi N-acetyllactosamine (LacNAc) repeats and unusual pentasialylated terminal sialic acids.
30152909	1	9	gly	glycoprotein	201:212	arg1	an intact glycoprotein	an intact glycoprotein				Fterm		glycoprotein			RATIONALE The functional study and application of an intact glycoprotein require the structural characterization of both the protein backbone and the glycan moiety; the former has been successfully demonstrated with selective fragmentation of the protein backbone in CID and ExD; whether the latter can be achieved with selective fragmentation of the glycan moiety remains to be explored.
30624066	6	49	gly	glycoprotein	1134:1145	arg1	α-1-acid glycoprotein	α-1-acid glycoprotein				Fterm		glycoprotein			Implementation of the approach is illustrated using the known interactions between a C-terminal domain fragment of human galectin-3 (hGal-3C) and three human serum GPs, α-1-acid glycoprotein (AGP), haptoglobin phenotype 1-1 (Hp1-1) and α-2-macroglobulin (α2M).
29411222	6	80	gly	glycoprotein	876:887	arg1	Similar glycoprotein species	Similar glycoprotein species				Fterm		glycoprotein			Similar glycoprotein species for the complete monomer and the Fc domain of originator and follow-on product were observed, however, small differences in lysine variants and oxidation were found.
29888905	6	22	gly	released	933:940	arg1	membrane-derived tryptic glycopeptides AND N-Glycans			membrane-derived tryptic glycopeptides	N-Glycans					glycopeptides	N-Glycans were released from membrane-derived tryptic glycopeptides with peptide N-glycosidase F, labeled with 2-aminobenzamide and analyzed by normal phase-high-pressure liquid chromatography (NP-HPLC) and matrix-assisted laser desorption ionization-time-of-flight (MALDI-TOF) mass spectrometry.
29888905	6	47	gly	glycopeptides	972:984	arg2	membrane-derived tryptic glycopeptides			membrane-derived tryptic glycopeptides						glycopeptides	N-Glycans were released from membrane-derived tryptic glycopeptides with peptide N-glycosidase F, labeled with 2-aminobenzamide and analyzed by normal phase-high-pressure liquid chromatography (NP-HPLC) and matrix-assisted laser desorption ionization-time-of-flight (MALDI-TOF) mass spectrometry.
30902814	5	94	gly	N-glycosylation	708:722	arg2	the predicted N-glycosylation sites	M41		sites		PUBTATOR		M41		sites	Ten single Asn-to-Ala substitutions at the predicted N-glycosylation sites of the M41-RBD were evaluated along with two control Val-to-Ala substitutions.
29671439	5	16	gly	released	724:731	arg1	the ginger glycoproteins AND the N-glycans	the ginger glycoproteins			the N-glycans	Fterm		glycoproteins			The ginger glycoproteins are enriched by concanavalin A (Con A) and solanum tuberosum (Potato) lectin (STL), and the structures of the N-glycans released from the ginger glycoproteins include high-mannose type glycans, fucosylated-type glycans, and hybrid-type glycans, as analyzed by MALDI-TOF-MS.
29671439	5	32	gly	glycoproteins	749:761	arg1	the ginger glycoproteins	the ginger glycoproteins				Fterm		glycoproteins			The ginger glycoproteins are enriched by concanavalin A (Con A) and solanum tuberosum (Potato) lectin (STL), and the structures of the N-glycans released from the ginger glycoproteins include high-mannose type glycans, fucosylated-type glycans, and hybrid-type glycans, as analyzed by MALDI-TOF-MS.
29671439	5	43	gly	glycoproteins	590:602	arg1	The ginger glycoproteins	The ginger glycoproteins				Fterm		glycoproteins			The ginger glycoproteins are enriched by concanavalin A (Con A) and solanum tuberosum (Potato) lectin (STL), and the structures of the N-glycans released from the ginger glycoproteins include high-mannose type glycans, fucosylated-type glycans, and hybrid-type glycans, as analyzed by MALDI-TOF-MS.
31813565	4	62	gly	glycopeptides	839:851	arg2	glycopeptides			glycopeptides						glycopeptides	The physical property and adsorption of magMOF@Au-maltose to glycopeptides were investigated.
30737276	3	45	gly	found	544:548	arg1	the three domains AND similar glycans			the three domains	similar glycans					domains	The structures of the four N-linked glycans from the PBCV-1 MCP consist of nonasaccharides, and similar glycans are not found elsewhere in the three domains of life.
29420040	5	70	gly	quantitative	1034:1045	arg1	site-specific			site-specific						site-specific	We sought to determine the impact of the removal of 15 potential N-glycan sites (5 per protomer) from the germline-targeting soluble trimer, BG505 SOSIP.v4.1-GT1, using quantitative, site-specific N-glycan mass spectrometry analysis.
30397756	9	40	gly	γ-subunits	1513:1522	arg1	fucosylation	γ-subunits			fucosylation	Fterm		γ-subunits			In terms of glycosylation, the amount of O-glycans in the Aα-subunit is decreased in LC patients, while sialylation and fucosylation of N-type glycans of Bβ- and γ-subunits are increased in LC and HCC.
30397756	9	40	gly	γ-subunits	1513:1522	arg1	sialylation	γ-subunits			sialylation	Fterm		γ-subunits			In terms of glycosylation, the amount of O-glycans in the Aα-subunit is decreased in LC patients, while sialylation and fucosylation of N-type glycans of Bβ- and γ-subunits are increased in LC and HCC.
30397756	9	21	gly	sialylation	1455:1465	arg1	N-type glycans	γ-subunits			N-type glycans	Fterm		γ-subunits			In terms of glycosylation, the amount of O-glycans in the Aα-subunit is decreased in LC patients, while sialylation and fucosylation of N-type glycans of Bβ- and γ-subunits are increased in LC and HCC.
30397756	9	28	gly	fucosylation	1471:1482	arg1	N-type glycans	γ-subunits			N-type glycans	Fterm		γ-subunits			In terms of glycosylation, the amount of O-glycans in the Aα-subunit is decreased in LC patients, while sialylation and fucosylation of N-type glycans of Bβ- and γ-subunits are increased in LC and HCC.
29941589	7	9	gly	glycoprotein	1282:1293	arg1	the glycoprotein spikes	the glycoprotein spikes				Fterm		glycoprotein			Combined, our data provide a structure-based blueprint for understanding how glycans render the glycoprotein spikes of Lassa virus and other Old World arenaviruses immunologically resistant targets.
30708139	3	69	gly	glycosylation	557:569	arg2	new N-linked glycosylation sites			new N-linked glycosylation sites						sites	In this study, human luteinizing hormone (LH) was considered for identification of the suitable positions for the addition of new N-linked glycosylation sites.
29304471	2	62	part_of	site	299:302	arg1	Zika virus (ZIKV) envelope (E) proteins	proteins		site		Fterm	Site	proteins		site	Compared to dengue virus (DENV), the loop containing the single N-linked glycosylation site on Zika virus (ZIKV) envelope (E) proteins extends further towards the DII fusion loop (DII-FL) on neighboring E proteins within E dimers on mature viruses.
30151520	7	40	gly	glycopeptide	1540:1551	arg2	glycopeptide			glycopeptide						glycopeptide	This lack of sensitivity to oligosaccharide composition stands in contrast to other physicochemical properties of glycopeptide ions (e.g., polypeptide composition, charge state, charge carrier) which sharply influence their energy-resolved CID characteristics.
31905645	6	84	part_of	MCC	1004:1006	arg1	the unmodified MCC composite	MCC		the unmodified MCC composite		OGER	Site	MCC		composite	The 1.6-fold increase of E was obtained for CDI modified composition in comparison to the unmodified MCC composite.
31154130	2	25	gly	glycoprotein	453:464	arg1	the most dominant and significant glycoprotein	the most dominant and significant glycoprotein				Fterm		glycoprotein			Human immunoglobulin G (IgG), which is composed of four subclasses (IgG1, IgG2, IgG3 and IgG4), is one of the most dominant and significant glycoprotein in human serum.
31514875	5	16	gly	glycopeptides	1145:1157	arg2	glycopeptides			glycopeptides						glycopeptides	Firstly, the repeatability of the nanoLC-MS/MS was evaluated and a method to control the identification of the identified glycans was developed to validate them regarding the retention time of glycopeptides in reversed phase nanoLC separation.
30563843	7	14	gly	residues	1350:1357	arg1	glycan components			residues	glycan components					residues	Mutagenesis and kinetic analyses confirmed that renin-mediated production of angiotensin I is controlled by interactions of amino acid residues and glycan components outside renin's active-site cleft.
29466327	6	16	part_of	OST	928:930	arg1	the OST catalytic site	OST		the OST catalytic site		OGER	Site	OST		site	Ost3 was found to mediate the OST-Sec61 translocon interface, funnelling the acceptor peptide towards the OST catalytic site as the nascent peptide emerges from the translocon.
29992770	10	23	gly	N-glycopeptides	1458:1472	arg2	specific N-glycopeptides			specific N-glycopeptides						N-glycopeptides	CONCLUSIONS AND CLINICAL RELEVANCE: The authors are the first to suggest specific N-glycopeptides to serve as potential serum biomarkers to detect preclinical OSCC in patients.
29981898	5	46	gly	gly-12	1008:1013	arg1	the N-glycans			gly-12-gly-13	the N-glycans					gly-12-gly-13	Using an off-line HPLC-MALDI-TOF-MS approach combined with exoglycosidase digestions and MS/MS, we reveal that the multiple hexose residues of the N-glycans of the gly-12;gly-13;gly-14 triple mutant are not just mannose, but include galactoses in three different positions (β-intersecting, β-bisecting and α-terminal) on isomeric forms of Hex4-8HexNAc2 structures; some of these structures are fucosylated and/or methylated.
30651366	3	143	part_of	E2	485:486	arg1	conserved E2 epitopes	E2		conserved E2 epitopes		Cterm	Site	E2		epitopes	However, a significant challenge for a B cell-based vaccine is focusing the immune response on conserved E2 epitopes capable of eliciting neutralizing antibodies not associated with viral escape.
31104946	1	26	gly	glycoproteins	116:128	arg1	Viral glycoproteins	Viral glycoproteins				Fterm		glycoproteins			Viral glycoproteins are under constant immune surveillance by a host's adaptive immune responses.
30659587	2	47	gly	N-glycosylation	338:352	arg2	three different N-glycosylation sites			three different N-glycosylation sites						sites	Chinese hamster ovary fed-batch cell culture batches yielded consistent glycoprofiles of a Fc-fusion antibody comprizing three different N-glycosylation sites.
31905645	5	70	part_of	MCC	861:863	arg1	the MCC composite	MCC		the MCC composite		OGER	Site	MCC		composite	The addition of filler into PBS led to a 4.5-fold improvement of Young's modulus E for the MCC composite, in comparison to neat PBS.
29619832	2	22	gly	glycoprotein	335:346	arg1	This glycoprotein	This glycoprotein				Fterm		glycoprotein			This glycoprotein contains three predicted N-linked glycosylation sites; one is near the protein's active site, and at least one more is known to facilitate the protein's secretion.
29619832	2	23	gly	glycosylation	382:394	arg2	three predicted N-linked glycosylation sites			three predicted N-linked glycosylation sites						sites	This glycoprotein contains three predicted N-linked glycosylation sites; one is near the protein's active site, and at least one more is known to facilitate the protein's secretion.
30002445	7	47	gly	glycoproteins	1320:1332	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			As such, we anticipate CFGpS will facilitate fundamental understanding in glycoscience and make possible applications in on demand biomanufacturing of glycoproteins.
30157878	4	54	part_of	IgG	618:620	arg1	The IgG glycome composition	IgG		The IgG glycome composition		Cterm	Site	IgG		position	The IgG glycome composition was analysed by ultra-performance liquid chromatography.
30503329	5	38	gly	glycoprotein	820:831	arg1	the glycoprotein	the glycoprotein				Fterm		glycoprotein			We propose that the pathway for attachment of lichenin to the glycoprotein has four steps.
30030954	1	31	gly	glycosylated	143:154	arg1	a highly glycosylated antimicrobial protein	a highly glycosylated antimicrobial protein				Fterm		protein			Lactoferrin is a highly glycosylated antimicrobial protein that contains multiple glycan types.
30030954	1	8	gly	contains	183:190	arg1	a highly glycosylated antimicrobial protein AND multiple glycan types	a highly glycosylated antimicrobial protein			multiple glycan types	Fterm		protein			Lactoferrin is a highly glycosylated antimicrobial protein that contains multiple glycan types.
30576150	5	66	gly	fucosylated	830:840	arg1	Twenty-two N-glycan structures				Twenty-two N-glycan structures						Twenty-two N-glycan structures were identified in sow milk, among which 36% (8 out of 22) were fucosylated, 41% (9 out of 22) were sialylated, and 14% (3 out of 22) were high mannosylated.
30576150	5	102	gly	mannosylated	910:921	arg1	Twenty-two N-glycan structures				Twenty-two N-glycan structures						Twenty-two N-glycan structures were identified in sow milk, among which 36% (8 out of 22) were fucosylated, 41% (9 out of 22) were sialylated, and 14% (3 out of 22) were high mannosylated.
30397756	3	57	gly	glycoprotein	523:534	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			Blood plasma from 111 healthy and sick donors was analyzed to determine the post-translational modifications (PTM) of intact Aα-, Bβ-, and γ-subunits of fibrinogen, a glycoprotein predominantly produced in liver cells.
31813565	5	58	gly	glycopeptides	951:963	arg2	glycopeptides			glycopeptides						glycopeptides	The results showed magMOF@Au-maltose possessing the outstanding performance in glycopeptides enrichment with high selectivity (1:200, mass ratio of horseradish peroxidase to bovine serum albumin digest), a low limit of detection (10 fmol), a high recovery (over 83.3%), and a large binding capacity (83 μg•mg-1).
31501225	3	67	gly	glycoproteins	426:438	arg1	serum glycoproteins	serum glycoproteins				Fterm		glycoproteins			Here, unbiased quantification of N-glycopeptides of a cluster of serum glycoproteins with 40-55 kDa molecular weight (40-kDa band) was investigated in hepatitis B virus (HBV)-related liver diseases.
31501225	3	73	gly	N-glycopeptides	388:402	arg2	N-glycopeptides			N-glycopeptides						N-glycopeptides	Here, unbiased quantification of N-glycopeptides of a cluster of serum glycoproteins with 40-55 kDa molecular weight (40-kDa band) was investigated in hepatitis B virus (HBV)-related liver diseases.
29299842	9	70	gly	glycoproteins	1461:1473	arg1	glycoproteins				glycoproteins						Here, we present the protocols employed in our laboratory to investigate the N-and O-glycan chains released from purified glycoproteins or cell wall mannoproteins in several yeast species.