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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
The densely glycosylated spike (S) proteins that are highly exposed on the surface of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) facilitate viral attachment, entry, and membrane fusion. We have previously reported all the 22 N-glycosites and site-specific N-glycans in the S protein...
ORGANISM(S): Homo sapiens (Human) 
2021-11-03 | PXD022896 | Pride
Background: Platelet glycoprotein (GP) Ibα is the major ligand-binding subunit of the GPIb-IX-V complex that binds von Willebrand Factor (VWF). GPIbα is heavily glycosylated, and its glycans have been proposed to play key roles in platelet clearance, VWF binding, and as target antigens in immune thr...
ORGANISM(S): Homo sapiens (Human) 
2023-02-09 | PXD035030 | Pride
Human plasma fibronectin is an adhesive protein that plays a crucial role in wound healing. Many studies had indicated that glycans may mediate the expression and functions of fibronectin, yet a comprehensive understanding of its glycosylation is still missing. Here, we performed a comprehensive N- ...
ORGANISM(S): Homo sapiens (Human) 
2022-02-17 | PXD025886 | 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
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
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