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Site-specific characterization of glycosylation requires intact glycopeptide analysis, and recent efforts have focused on how to best interrogate glycopeptides using tandem mass spectrometry (MS/MS). Beam-type collisional activation, i.e., higher-energy collisional dissociation (HCD), has been a val...
ORGANISM(S): Bos taurus (Bovine) Homo sapiens (Human) 
2020-07-20 | PXD017646 | Pride
Proteins glycosylation is primarily characterized as N-glycosylation or O-glycosylation. Recognition of the consensus N-glycosylation sequon (N-X-S/T/C) has enabled the mapping of the glycosite occupancy of intact glycopeptides, whereas O-glycosylation consensus sequons do not exit, making the chara...
ORGANISM(S): Homo sapiens (Human) 
2024-04-25 | PXD042701 | Pride
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
The recently described O-glycoprotease OpeRATOR presents exciting opportunities for O-glycoproteomics. This bacterial enzyme purified from A. muciniphila cleaves N-terminally to serine and threonine residues that are modified with (preferably asialylated) O-glycans, providing orthogonal cleavage rel...
ORGANISM(S): Bos taurus (Bovine) Homo sapiens (Human) 
2020-11-03 | PXD020077 | Pride
We employed the newly available IMPa O-glycoprotease from Pseudomonas aeruginosa for O-glycoproteomics analysis of cultured cells and tissues. The glycopeptides were extracted, purified, and conjugated to a solid support before an enzymatic cleavage by IMPa. O-glycopeptides were analyzed by EThcD, w...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2023-08-28 | PXD037415 | Pride
Analysis of mucin type O-glycans linked to serine/threonine of glycoproteins is technically challenging, in part, due to a lack of effective enzymatic tools that enable their analysis. Recently, several O-glycan-specific endoproteases that can cleave the protein adjacent to the appended glycan have ...
ORGANISM(S): Homo sapiens (Human) 
2022-01-05 | PXD029534 | Pride
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
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
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
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