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ProteomicsMapping and quantification of over 2,000 O-linked glycopeptides in activated human T cells with isotope-targeted glycoproteomics
Post-translational modifications (PTMs) on proteins often function to regulate signaling cascades, with the activation of T cells during an adaptive immune response being a classic example. Mounting evidence indicates that the modification of proteins by O-linked Nacetylglucosamine (O-GlcNAc), the o...
ORGANISM(S): Homo sapiens (Human) 
2018-01-25 | PXD004559 | Pride
Glycoproteomics Mass spectrometry O-glcnac T cells O-linked n-acetylglucosamine 
ProteomicsGlobal view of domain-specific O-linked mannose glycosylation in glycoengineered cells
Protein O-linked mannose (O-Man) glycosylation is an evolutionary conserved post-translational modification, whose biosynthesis is initiated by three non-redundant enzyme families, POMT1/POMT2, TMTC1-4 and TMEM260. In this study, we applied a targeted workflow for membrane glycoproteomics to five hu...
ORGANISM(S): Homo sapiens (Human) 
2024-06-10 | PXD045597 | Pride
Lc-msms O-man Glycoproteomics Ptm Glycobiology O-mannose 
ProteomicsComparison of Intact Glycopeptide Enrichment Methods Using Strong Anion Exchange and Hydrophilic Interaction Liquid Chromatography
Heterogeneity of protein glycosylation poses great challenge for analysis that is key to un-puzzle systems glycobiology in diseases. Resolving this conundrum requires global enrichment of glycopeptides for identification and quantitation. To this aim, hydrophilic interaction chromatography (HILIC) h...
ORGANISM(S): Homo sapiens (Human) 
2017-10-19 | PXD005145 | Pride
Glycoproteomics Hilic Sax Quantitation O-linked 
ProteomicsComparison of Intact Glycopeptide Enrichment Methods Using Strong Anion Exchange and Hydrophilic Interaction Liquid Chromatography
Heterogeneity of protein glycosylation poses great challenge for analysis that is key to un-puzzle systems glycobiology in diseases. Resolving this conundrum requires global enrichment of glycopeptides for identification and quantitation. To this aim, hydrophilic interaction chromatography (HILIC) h...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2018-07-02 | MSV000082566 | MassIVE
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
UnknownDeciphering fucosylated protein-linked O-glycans in oral Tannerella serpentiformis: Insights from NMR spectroscopy and glycoproteomics.
Not available
S-EPMC11632369 | biostudies-literature
ProteomicsSite-specific Analysis of O-linked Glycoproteome Using Chemoenzymatic Strategy, part 2
Protein glycosylation is ubiquitous and plays critical roles in biology. However, study of O-linked glycoproteome (O-glycoproteome), a major type of protein glycosylation, has been severely impeded due to paucity of technology. We presented a chemoenzymatic strategy for extraction of site-specific O...
ORGANISM(S): Homo sapiens (Human) 
2022-02-28 | PXD007895 | Pride
Site specific O-linked glycoproteomics Hiv Solid phase 
ProteomicsRe-analysis of glycoproteomics data with MSFragger-Glyco
Reanalysis of submissions PXD011533 and PXD009476 using MSFragger-Glyco mode. Processed MSFragger results files (pepXML) and PSM tables (psm.tsv) supporting MSFragger-Glyco manuscript (Fast and Comprehensive N- and O-glycoproteomics analysis with MSFragger-Glyco. Recent advances in methods for enric...
ORGANISM(S): Mus musculus (Mouse) Homo sapiens (Human) 
2020-10-06 | PXD021196 | Pride
Glycosylation Glycoproteomics Msfragger Reanalysis O-glycosylation Glycan Glycopeptide N-glycosylation 
UnknownMapping and Quantification of Over 2000 O-linked Glycopeptides in Activated Human T Cells with Isotope-Targeted Glycoproteomics (Isotag).
Not available
S-EPMC5880114 | biostudies-literature
ProteomicsGlycoproteomics analysis of triple wild-type lung adenocarcinoma tissue samples
Glycoproteomics analysis of triple wild-type lung adenocarcinoma tissue samples for the publication of the same name.
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2024-11-18 | MSV000096450 | MassIVE
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