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ProteomicsMass spectrometric analysis of proteolytic cleavage related to ArtA and PssA from Haloferax volcanii
The S-layer glycoprotein (SLG) of Haloferax volcanii has been shown to be processed and C-terminally linked to a lipid in an archaeosortase A (ArtA)-dependent manner. A C-terminal tripartite structure including a PGF motif is required for the processing of SLG as well as other substrates (Abdul Hali...
ORGANISM(S): Haloferax volcanii (Halobacterium volcanii) 
2020-05-11 | PXD011050 | Pride
Haloferax volcanii Lipid anchoring Archaeosortase S-layer glycoprotein 
ProteomicsTMEM260 is a protein-specific O-mannosyltransferase
Mutations in the TMEM260 gene cause structural heart defects and renal anomalies syndrome (SHDRA), but the function of the encoded protein remains unknown. We report that TMEM260 is an ER-located protein O-mannosyltransferase that selectively glycosylates defined extracellular immunoglobulin, plexin...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2023-05-05 | PXD032328 | Pride
O-mannosylation Glycoproteomics Glycopeptide Tmem260 
UnknownIntegrative analysis of H&E and IHC identifies prognostic immune subtypes in HPV related oropharyngeal cancer.
Not available
S-EPMC11450009 | biostudies-literature
ProteomicsNucleocytoplasmic O-Man glycoproteome
Dynamic cycling of N-Acetylglucosamine (GlcNAc) on serine (Ser) and threonine (Thr) residues (O-GlcNAcylation) is an essential process in all eukaryotic cells except yeast, e.g Saccharomyces cerevisiae. O-GlcNAcylation modulates signaling and cellular processes in an intricate interplay with protein...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) Schizosaccharomyces pombe 
2015-12-08 | PXD002924 | Pride
O-glycoproteomics Saccharomyces cerevisiae 
ProteomicsFruit fly O-GlcNAc glycoproteomics
The reversible posttranslational O-GlcNAc modification of serine or threonine residues of intracellular proteins is involved in many cellular events from signaling cascades to epigenetic and transcriptional regulation. O-GlcNAcylation is a conserved nutrient-dependent process involving two enzymes,...
ORGANISM(S): Drosophila melanogaster (Fruit fly) 
2021-04-26 | PXD025344 | Pride
Fusion O-glcnac Drosophila melanogaster 
UnknownEriodictyol Attenuates H2O2-Induced Oxidative Damage in Human Dermal Fibroblasts through Enhanced Capacity of Antioxidant Machinery.
Not available
S-EPMC9228723 | biostudies-literature
ProteomicsMapping the O-mannose glycoproteome in Saccharomyces cerevisiae
O-Mannosylation is a vital protein modification conserved from fungi to humans. In an essential step towards the full understanding of O-mannosylation we mapped the O mannose glycoproteome in baker´s yeast.
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2016-01-18 | PXD003238 | Pride
Saccharomyces cerevisiae Glycoproteome O-mannose 
UnknownDesign and synthesis of conformationally constraint Dyrk1A inhibitors by creating an intramolecular H-bond involving a benzothiazole core.
Not available
S-EPMC6071757 | biostudies-literature
ProteomicsCHO O-Mannosylation independent of POMT1/2
Protein O-mannosylation is found in yeast and metazoans and a family of conserved orthologous polypeptide O-mannosyltransferases is believed to initiate this important posttranslational modification. We recently discovered that the large families of cadherins and protocadherins carry highly conserve...
ORGANISM(S): Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) 
2017-05-18 | PXD004341 | Pride
Mannose Glycoproteomics O-mannosyltransferase O-glycosylation 
ProteomicsHuman O-Mannosylation independent of POMT1/2
Protein O-mannosylation is found in yeast and metazoans and a family of conserved orthologous polypeptide O-mannosyltransferases is believed to initiate this important posttranslational modification. We recently discovered that the large families of cadherins and protocadherins carry highly conserve...
ORGANISM(S): Homo sapiens (Human) 
2017-05-18 | PXD004358 | Pride
O-glycosylation Glycoproteomics O-mannose Mannosyltransferase 
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