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The dense O-glycosylation of mucins plays an important role in the defensive properties of the mucus hydrogel. Aberrant glycosylation is often correlated with inflammation and pathology such as COPD, cancer, and Crohn’s disease. The inherent complexity of glycans and the diversity in the O-core stru...
ORGANISM(S): Homo sapiens (Human) Sus scrofa domesticus (domestic pig) 
2024-03-19 | PXD050530 | Pride
Protein O-glycosylation, the enzymatic attachment of carbohydrates to serine/threonine/tyrosine residues, is a large group of essential post-translational modifications involved in brain development and disease. However, studies of the most abundant O-glycan class in the mammalian brain, termed muci...
ORGANISM(S): Mus musculus (Mouse) 
2025-02-10 | PXD041631 | Pride
Glycosylation, including N-glycosylation and O-glycosylation is generally characterized and controlled as a critical quality attribute for therapeutic glycoproteins because glycans can impact protein-based drug product efficacy, half-life, stability, and safety. Analytical procedures to characterize...
ORGANISM(S): Bos taurus (Bovine) 
2024-08-01 | PXD052172 | Pride
Free glycans derived from O-mannosylated glycoproteins suggest the presence of an O-glycoprotein degradation pathway in yeast
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
Protein O-mannosylation is initiated by the ER-resident enzymes POMT1 and POMT2, both of which carry multiple N-glycans essential for proper folding and activity. Although congenital disorders of glycosylation type I (CDG-I) disrupt the early N-glycosylation process, their impact on POMT biogenesis ...
ORGANISM(S): Homo Sapiens 
In eukaryotic cells, unconjugated oligosaccharides structurally related to N-glycans (FNGs) are generated either from misfolded N-glycoproteins destined for endoplasmic reticulum (ER)-associated degradation (ERAD), or from lipid-linked oligosaccharides, donor substrates for N-glycosylation of protei...
ORGANISM(S): Saccharomyces cerevisiae 
2019-07-24 | GSE130332 | GEO
Host-derived O-glycans inhibit toxigenic conversion by a virulence-encoding phage in Vibrio cholerae
RNA-seq of human gut Bacteroides xylanisolvens and Bacteroides ovatus isolates grown on mucin O-linked glycans compared to glucose
Our studies provide direct evidence that O-glycosylation pathways play a role in the regulation of cell growth through apoptosis and proliferation pathways. Eight small molecular weight analogues of the GalNAc-alpha-1-O-serine/threonine structure based on 1-benzyl-2-acetamido-2- deoxy-alpha-O-D-gala...
ORGANISM(S): Homo sapiens 
2008-08-18 | GSE12422 | GEO
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