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We developed an automated glycopeptide enrichment method for the analysis of serum site-specific N-glycoproteome. This automated method allowed for processing one sample within 20 min. It showed higher enrichment specificity, more intact glycopeptide identifications, and better quantitative reproduc...
ORGANISM(S): Homo Sapiens (human) 
Protein glycosylation is one of the most common protein modifications and plays essential roles in biology and therapeutics. However, the analysis of in vivo O-linked glycosylation, a major type of protein glycosylation, has been severely impeded by the scarcity of technology. Here, a chemoenzymatic...
ORGANISM(S): Homo sapiens (Human) 
2018-12-05 | PXD009476 | Pride
Glycosylation is a critical determinant of the efficacy, stability, and pharmacological behavior of therapeutic proteins. R27T, an engineered variant of interferon-β1a, contains two N-glycosylation sites (Asn25 and Asn80), increasing its structural complexity and analytical requirements. In this stu...
ORGANISM(S): Homo sapiens (Human) 
2026-09-21 | PXD077477 | Pride
Protein kinases are prime targets for drug development due to their involvement in various cancers. However, selective inhibition of kinases, while avoiding off-target effects remains a significant challenge for the development of protein kinase inhibitors. Activity-based protein profiling (ABPP), i...
ORGANISM(S): Homo sapiens (Human) 
2025-05-07 | PXD058749 | Pride
Comparative, dose-dependent analysis of interactions between small molecule drugs and their targets, as well as off-targets, in complex proteomes is crucial for selecting optimal drug candidates. The affinity of small molecules for targeted proteins is largely dictated by interactions between amino ...
ORGANISM(S): Homo sapiens (Human) 
2024-10-17 | PXD045864 | Pride
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
1. Systematic survey of PTM site and stoichiometry on histone proteins has been lagged behind due to the lack of efficient quantitative peptide comparison methodology on histone proteins. Our quantitative mass spectrometry-based proteomics approach, Site-Profiling, used SILAC-based peptide ratio ana...
ORGANISM(S): Homo sapiens (Human) 
2023-03-06 | PXD029508 | Pride
Many protein subunit vaccines and biologics contain glycosylated antigens and antibodies, yet quantitative frameworks for comparing glycosylation across lots, manufacturers, and production platforms remain limited. We performed site specific glycosylation LC-MS/MS analysis for intact N-linked glycop...
ORGANISM(S): Influenza A virus (A/Panama/2007/1999(H3N2)) Influenza A virus (A/Philippines/2/1982(H3N2)) Human alphaherpesvirus 3 Influenza A virus (A/New Caledonia/20/1999(H1N1)) Severe acute respiratory syndrome coronavirus 2 Influenza A virus (A/Shandong/9/1993(H3N2)) 
2026-07-21 | PXD074672 | Pride
HeLa cell line is frequently used in biomedical research, however little is known about N-glycan structures expressed on individual glycoproteins of this complex sample. We characterized site-specific N-glycosylation of HeLa N-glycoproteins using a complex workflow based on high and low energy tande...
ORGANISM(S): Bos taurus (Bovine) Homo sapiens (Human) 
2019-10-21 | PXD013930 | Pride
Site-specific incorporation of two noncanonical amino acids for two-color bioorthogonal labeling and chemical-controlled crosslinking of proteins on live mammalian cells
ORGANISM(S): Mus Musculus (mouse) 
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