O-GlcNAc: a regulatory post-translational modification
β Scribed by Lance Wells; Stephen A Whelan; Gerald W Hart
- Book ID
- 117053405
- Publisher
- Elsevier Science
- Year
- 2003
- Tongue
- English
- Weight
- 184 KB
- Volume
- 302
- Category
- Article
- ISSN
- 0006-291X
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## Abstract Modification of intracellular proteins by the Ξ²βlinkage of the monosaccharide, Nβacetylglucosamine to serine or threonine hydroxyls (OβGlcNAc) is abundant and reversible. Although many proteins bear this postβtranslational covalent modification, the changes in function of the proteins a
N-Acetylglucosamine O-linked to serines and threonines of cytosolic and nuclear proteins (O-GlcNAc) is an abundant reversible post-translational modification found in all higher eukaryotes. Evidence for functional regulation of proteins by this dynamic saccharide is rapidly accumulating. Deletion of
O-GlcNAc is an ubiquitous post-translational protein modification consisting of a single Nacetlyglucosamine moiety linked to serine or threonine residues on nuclear and cytoplasmic proteins. Recent work has begun to uncover the functional roles of O-GlcNAc in cellular processes. O-GlcNAc modified pr