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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
We presented a user-friendly proteomic database search platform, MS-Decipher, for the identification of peptides from MS data. Two scoring schemes, rank score and hyperscore, could be used for peptide spectra matching. FDR controlling strategies could be used after searching, and it was found that M...
ORGANISM(S): Homo Sapiens (human) 
A large family of GalNAc transferases (GalNAc-Ts) catalyzes the covalent attachment of N-Acetylgalactosamine (GalNAc) to serine and threonine residues on proteins that pass through the secretory pathway in the first committed step of mucin-type O-glycosylation. Abnormalities in the activity of indi...
ORGANISM(S): Mus musculus (Mouse) 
2024-05-24 | PXD040196 | Pride
We adopted the method used in the O-Pair article to validate the FDR calculations of O-glycopeptide search in O-Search-Pattern, O-Pair Search, MSFragger-Glyco, and pGlyco. The detailed description of the method was provided in the ‘Methods’ and ‘Evaluating O-Pair Search performance’ parts of O-Pair ...
ORGANISM(S): Homo Sapiens (human) 
Glycosylation is one of the most important, but also most complex, post-translational modifications of proteins. Mass spectrometry-based glycoproteomics analysis offers a powerful approach to explore the fundamental roles of glycosylation, but achieving sufficient fragmentation for glycopeptide assi...
ORGANISM(S): Candida albicans (Yeast) Mus musculus (Mouse) Homo sapiens (Human) 
2026-09-01 | PXD074575 | Pride
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