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ProteomicsOptimization of O-GIG for O-glycopeptide Characterization with Sialic Acid Linkage Determination-Fig6
O-glycoprotein analysis has been historically challenging due, in part, to a dearth of available enzymes active in release of O-glycans. Moreover, chemical releasing methods, such as β-elimination/Michael addition are not specific to O-glycan release and can also eliminate phosphoryl substitutions....
ORGANISM(S): Bos taurus (Bovine) 
2020-07-28 | PXD020034 | Pride
Mucin O-glycopeptide immobilization Operator Lactoferrin O-glycosylation Sialic acid 
ProteomicsOptimization of O-GIG for O-glycopeptide Characterization with Sialic Acid Linkage Determination-Fig3
O-glycoprotein analysis has been historically challenging due, in part, to a dearth of available enzymes active in release of O-glycans. Moreover, chemical releasing methods, such as β-elimination/Michael addition are not specific to O-glycan release and can also eliminate phosphoryl substitutions....
ORGANISM(S): Bos taurus (Bovine) 
2020-07-28 | PXD020048 | Pride
Mucin O-glycopeptide immobilization Operator Lactoferrin O-glycosylation Sialic acid 
ProteomicsOptimization of O-GIG for O-glycopeptide Characterization with Sialic Acid Linkage Determination-figure 5
O-glycoprotein analysis has been historically challenging due, in part, to a dearth of available enzymes active in release of O-glycans. Moreover, chemical releasing methods, such as β-elimination/Michael addition are not specific to O-glycan release and can also eliminate phosphoryl substitutions....
ORGANISM(S): Bos taurus (Bovine) 
2020-07-28 | PXD020032 | Pride
Mucin O-glycopeptide immobilization Operator Lactoferrin O-glycosylation Sialic acid 
ProteomicsOptimization of O-GIG for O-glycopeptide Characterization with Sialic Acid Linkage Determination-Figure 4
O-glycoprotein analysis has been historically challenging due, in part, to a dearth of available enzymes active in release of O-glycans. Moreover, chemical releasing methods, such as β-elimination/Michael addition are not specific to O-glycan release and can also eliminate phosphoryl substitutions....
ORGANISM(S): Bos taurus (Bovine) 
2020-07-28 | PXD020053 | Pride
Mucin O-glycopeptide immobilization Operator Lactoferrin O-glycosylation Sialic acid 
ProteomicsOptimization of O-GIG for O-glycopeptide Characterization with Sialic Acid Linkage Determination -Figure 2
O-glycoprotein analysis has been historically challenging due, in part, to a dearth of available enzymes active in release of O-glycans. Moreover, chemical releasing methods, such as β-elimination/Michael addition are not specific to O-glycan release and can also eliminate phosphoryl substitutions....
ORGANISM(S): Bos taurus (Bovine) 
2020-07-28 | PXD020039 | Pride
Mucin O-glycopeptide immobilization Operator Lactoferrin O-glycosylation Sialic acid 
ProteomicspGlyco3: Intact N- and O-glycopeptide search engine
Analyses of N- and O-glycopeptide using pGlyco3 as well as Byonic, MSFragger and MetaMorpheus. N-glycopeptides and O-Man glycopeptides of fission yeast and budding yeast are also analyzed using pGlyco3.
ORGANISM(S): Saccharomyces Cerevisiae (ncbitaxon:4932) Homo Sapiens (ncbitaxon:9606) Schizosaccharomyces Pombe (ncbitaxon:4896) 
2021-01-27 | MSV000086771 | MassIVE
ProteomicsIMPROVED N- AND O-GLYCOPEPTIDE IDENTIFICATION USING HIGH-FIELD ASYMMETRIC WAVEFORM ION MOBILITY SPECTROMETRY (FAIMS)
Mass spectrometry is the premier tool for identifying and quantifying site-specific protein glycosylation globally. Analysis of intact glycopeptides often requires an enrichment step, after which the samples remain highly complex and exhibit a broad dynamic range of abundance. Here, we evaluated th...
ORGANISM(S): Homo sapiens (Human) 
2023-10-24 | PXD038673 | Pride
Faims N-glycopeptides Mass spectrometry O-glycopeptides Glycoproteomics 
ProteomicsGlyco-DIA: a method for quantitative O-glycoproteomics with in silico-boosted glycopeptide libraries
We report a LC-MS/MS O-glycoproteomics strategy using Data Independent Acquisition (DIA) mode that holds the potential for enabling direct analysis of O-glycoproteins with characterization of sites and structures of O-glycans on a proteome-wide scale with quantification of stoichiometries. To explor...
ORGANISM(S): Homo sapiens (Human) 
2019-11-19 | PXD011063 | Pride
Glycoproteomics Mass spectrometry O-glycosylation Data independent acquisition Human serum 
ProteomicsSerum O-glycoproteome using O-glycopeptide truncation strategy
Here, we report an O-glycopeptide truncation strategy for the characterization of protein O-GalNAcylation in biological samples. The O-glycopeptide truncation strategy utilizes another protease or O-glycopeptidase for targeted cleavage of tryptic and enriched O-glycopeptides, which increases the ana...
ORGANISM(S): Homo Sapiens (human) 
2023-05-13 | PXD041041 | JPOST Repository
ProteomicsLarge scale intact glycopeptide identification by Mascot database search
We present the adaptability of Mascot search engine for automated identification of intact glycopeptide mass spectra. The steps involved in adopting Mascot for intact glycopeptide analysis include: i) assigning unique one letter codes for monosaccharides, ii) linearizing glycan sequences and iii) pr...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2018-07-02 | MSV000082567 | MassIVE
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