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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
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
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
Invasive malignant pleomorphic adenoma (IMPA) results from the malignant transformation of pleomorphic adenoma (PA). The former is a high-grade malignant tumor, whereas the latter is a benign opposite. Study on the molecular mechanism in the progression of PA to IMPA will be of benefit to elucidate ...
ORGANISM(S): Homo sapiens 
2022-01-12 | GSE179895 | GEO
O-glycoproteases are an emerging class of enzymes that selectively digest glycoproteins at positions decorated with specific O-linked glycans. O-glycoprotease substrates range from any O-glycoprotein (albeit with specific O-glycan modifications) to only glycoproteins harboring specific O-glycosylate...
ORGANISM(S): Homo sapiens (Human) 
2023-02-15 | PXD035775 | Pride
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