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ProteomicsYeast glycoproteome - pGlyco 2
Precise and large-scale characterization of glycoproteome is critical for understanding the biological functions of glycoproteins. Due to the complexity of glycosylation, the overall throughput, data quality and accessibility of site-specific glycosylation analysis are overwhelmingly lower than thos...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2017-08-15 | PXD005565 | Pride
Yeast glycoproteome 
UnknownDiscovery of a nucleocytoplasmic O-mannose glycoproteome in yeast.
Not available
S-EPMC4697373 | biostudies-literature
ProteomicsNucleocytoplasmic O-Man glycoproteome
Dynamic cycling of N-Acetylglucosamine (GlcNAc) on serine (Ser) and threonine (Thr) residues (O-GlcNAcylation) is an essential process in all eukaryotic cells except yeast, e.g Saccharomyces cerevisiae. O-GlcNAcylation modulates signaling and cellular processes in an intricate interplay with protein...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) Schizosaccharomyces pombe 
2015-12-08 | PXD002924 | Pride
O-glycoproteomics Saccharomyces cerevisiae 
ProteomicsMapping the O-mannose glycoproteome in Saccharomyces cerevisiae
O-Mannosylation is a vital protein modification conserved from fungi to humans. In an essential step towards the full understanding of O-mannosylation we mapped the O mannose glycoproteome in baker´s yeast.
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2016-01-18 | PXD003238 | Pride
Saccharomyces cerevisiae Glycoproteome O-mannose 
UnknownMapping the O-Mannose Glycoproteome in Saccharomyces cerevisiae.
Not available
S-EPMC4824858 | biostudies-literature
UnknownA universal chemical enrichment method for mapping the yeast N-glycoproteome by mass spectrometry (MS).
Not available
S-EPMC4047475 | biostudies-literature
UnknownQuantitative Data-Independent Acquisition Glycoproteomics of Sparkling Wine.
Not available
S-EPMC8724608 | biostudies-literature
ProteomicsLibrary-based virtual match-between-runs quantification scheme enabled by GlyPep-Quant dramatically enhances the identification of site-specific glycans and detection of occupancy ratio changes
Glycosylation changes are closely related to various diseases like cancer. However, the quantitative analysis of the site-specific glycans at proteomics scale remains challenging because of the extremely low interpretation rate of glycopeptide spectra. Here, we present a new software tool, GlyPep-Qu...
ORGANISM(S): Homo sapiens (Human) Saccharomyces cerevisiae (Baker's yeast) Schizosaccharomyces pombe 
2025-07-06 | PXD057799 | Pride
Proteomics  glycosylation  site-specific glycan  quantification  match-between-runs 
ProteomicsGlycoproteomic and single-protein glycomic analyses reveal zwitterionic N-glycans on natural and recombinant proteins derived from insect cells
Insect cells are a convenient cell factory to produce recombinant glycoproteins. Their glycosylation potential is believed to be simple, needing primarily addition of glycosyltransferases to humanize the recombinant products. In this study, the native glycoproteome of Spodoptera frugiperda Sf9 and T...
ORGANISM(S): Trichoplusia ni Spodoptera frugiperda 
2025-05-06 | PXD049172 | Pride
Phosphorylcholine Fucose Baculovirus expression N-glycans Insect cells 
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