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ProteomicsDeciphering O-glycoprotease substrate preferences with O-Pair Search
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
O-glycoproteomics Glycoproteins Cleavage Glycoproteomics Informatics O-pair search O-glycoprotease 
UnknownDeciphering <i>O</i>-glycoprotease substrate preferences with O-Pair Search.
Not available
S-EPMC10010678 | biostudies-literature
UnknownThe Glycoprotease CpaA Secreted by Medically Relevant Acinetobacter Species Targets Multiple O-Linked Host Glycoproteins.
Not available
S-EPMC7542363 | biostudies-literature
ProteomicsA broad-specificity O-glycoprotease that enables improved analysis of glycoproteins and glycopeptides containing intact complex O-glycans
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
G-csf Cd45 
UnknownL-Selectin ligands that are O-glycoprotease resistant and distinct from MECA-79 antigen are sufficient for tethering and rolling of lymphocytes on human high endothelial venules.
Not available
S-EPMC2140156 | biostudies-literature
ProteomicsLarge-scale and Site-specific Mapping of Intact O-glycans on Glycopeptides with IMPa
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
O-glycoproteomics  impa  vva  rax  tn antigen 
ProteomicsReceptor Binding, Immune Escape, and Cross-Species Transmission of the Recently Surging SARS-CoV-2 variant BA.3.2.2 (RE.2.2)
Glycoproteomics data of RE.2.2 Spike Protein by nano-LC-MSMS using five protease treatment with PNGaseF in 18O-water and O-glycoprotease
ORGANISM(S): Homo Sapiens Severe Acute Respiratory Syndrome Coronavirus 2 
PXD078197 |
ProteomicsGlycoFASP: A Universal Method to Prepare Complex Mixtures for O-Glycoproteomic Analysis
Here we describe a method titled filter-aided preparation of O-glycoproteomic samples (GlycoFASP) which takes advantage of molecular-weight cut-off filters and O-glycoprotease digestion specificity. Using GlycoFASP, preparation for MS analysis of biological samples is completed within one day and on...
ORGANISM(S): Homo sapiens (Human) 
2026-07-08 | PXD061804 | Pride
Human Method Serum Lc-ms Glycoproteomics O-glycoproteomics Seminal fluid 
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 
ProteomicsElectron-based dissociation is needed for O-glycopeptides derived from OpeRATOR proteolysis
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
Glycoproteomics O-glycosites Operator Protease Electron transfer dissociation 
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