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ProteomicsFalse positive glycopeptide identification through in-FAIMS glycan fragmentation.
Glycosylation is an important post-translational modification characterized by extensive heterogeneity. While mass spectrometry (MS) is the premier technique to characterize glycoproteins, the study of intact glycopeptides presents challenges often not observed in the study of unmodified species. Hi...
ORGANISM(S): Homo sapiens (Human) 
2023-09-11 | PXD041217 | Pride
Glycoproteomics Mucinomics faims Mucin-domain glycoproteomics Enrichment. Ion mobility separation 
ProteomicsGlycosite mapping and structural dynamics of TIM family immune checkpoints enabled by mucinase SmE
Mucin-domain glycoproteins are densely O-glycosylated and play key roles in a host of biological functions. In particular, the T-cell immunoglobulin and mucin-domain containing family of proteins (TIM-1, 3, 4) decorate immune cells and act as key checkpoint inhibitors in cancer. However, their dense...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2023-09-27 | PXD039583 | Pride
O-glycoprotein Tim-1 Cancer Mucinase Tim-4 Tim-3 O-glycosylation Immune checkpoint T-cell immunoglobulin and mucin-domain containing Lc-ms/ms Molecular dynamics Mucinome Mucin O-glycoproteomics Mucin domain Checkpoint inhibitor O-glycoprotease 
ProteomicsAutonomous Dissociation-type Selection for Glycoproteomics using a Real-Time Library Search
Tandem mass spectrometry (MS/MS) is the gold standard for intact glycopeptide identification, enabling peptide sequence elucidation and site-specific localization of glycan compositions. Beam-type collisional activation is generally sufficient for N-glycopeptides, while electron-driven dissociation ...
ORGANISM(S): Bos taurus (Bovine) Homo sapiens (Human) 
2024-11-15 | PXD055054 | Pride
N-glycopeptides Glycoproteomics Intelligent data acquisition Tandem mass spectrometry Beam-type collisional dissociation O-glycopeptides Product-dependent triggering Real-time library search Electron transfer dissociation 
ProteomicsOptimized mucin-selective enrichment strategy to probe the mucinome
Mucin-domain glycoproteins are densely O-glycosylated and play critical roles in a host of biological functions. Previously, we developed a mucin-selective enrichment strategy by employing a catalytically inactive mucinase (StcE) conjugated to solid support. While this method was effective, it suffe...
ORGANISM(S): Homo sapiens (Human) 
2024-04-10 | PXD046534 | Pride
Mass spectrometry Proteomics Glycoproteomics Mucins Enrichment 
ProteomicsRevealing the human cancer-associated mucinome
Mucin domains are densely O-glycosylated modular protein domains found in a wide variety of cell surface and secreted proteins. Mucin-domain glycoproteins are key players in a host of human diseases, especially cancer, but the scope of the mucinome remains poorly defined. Recently, we characterized ...
ORGANISM(S): Homo sapiens (Human) 
2022-06-29 | PXD024995 | Pride
Mucin Cancer Mucinase Proteomics Mucinome Mass spectrometry Glycoproteomics O-glycosylation 
ProteomicsGlycan shield of the ebolavirus envelope glycoprotein GP
The envelope glycoprotein GP of the ebolaviruses is essential for host cell attachment and entry. It is also the primary target of the protective and neutralizing antibody response in both natural infection and vaccination. GP is heavily glycosylated with up to 17 predicted N-linked sites, numerous ...
ORGANISM(S): Bundibugyo ebolavirus Zaire ebolavirus 
2022-08-02 | PXD031459 | Pride
Virus  ebola  glycosylation 
ProteomicsQuantification and site-specific analysis of co-occupied N- and O-glycopeptides
Protein glycosylation is a complex post-translational modification that is generally classified as N- or O-linked. Site-specific analysis of glycopeptides is accomplished with a variety of fragmentation methods, depending on the type of glycosylation being investigated and the instrumentation availa...
ORGANISM(S): Homo sapiens (Human) 
2025-04-08 | PXD062628 | Pride
Mucin Glycoproteomics O-glycosylation Glycosylation N-glycosylation 
ProteomicsTargeting host O-linked glycan biosynthesis affects Ebola virus replication efficiency and reveals differential GalNAc-T acceptor site preferences on the Ebola virus glycoprotein
Ebola virus glycoprotein is one of the most heavily O-glycosylated viral envelope glycoproteins. The glycoprotein possesses a large mucin-like domain responsible for the cytopathic effect on infected cells, yet its structure or potential role in early entry events is poorly defined. To understand th...
ORGANISM(S): Homo sapiens (Human) 
2024-04-29 | PXD036213 | Pride
Glycoproteomics O-glycosylation Virus Ebola 
ProteomicsQuantification and site-specific analysis of co-occupied N- and O-glycopeptides
Protein glycosylation is a complex post-translational modification that is generally classified as N- or O-linked. Site-specific analysis of glycopeptides is accomplished with a variety of fragmentation methods, depending on the type of glycosylation being investigated and the instrumentation availa...
ORGANISM(S): Homo sp. 
2024-10-22 | PXD053713 | Pride
Glycoproteomics Fragmentation Co-occupancy Mucins O-glycosylation N-glycosylation 
UnknownFalse-Positive Glycopeptide Identification via In-FAIMS Fragmentation.
Not available
S-EPMC10523363 | biostudies-literature
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