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O-GlcNAc: a regulatory post-translational modification

✍ 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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Post-translational modification by O-Glc
✍ Jeffrey E. Kudlow πŸ“‚ Article πŸ“… 2006 πŸ› John Wiley and Sons 🌐 English βš– 255 KB

## Abstract Modification of intracellular proteins by the β‐linkage of the monosaccharide, N‐acetylglucosamine to serine or threonine hydroxyls (O‐GlcNAc) is abundant and reversible. Although many proteins bear this post‐translational covalent modification, the changes in function of the proteins a

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✍ Keith Vosseller; Kaoru Sakabe; Lance Wells; Gerald W Hart πŸ“‚ Article πŸ“… 2002 πŸ› Elsevier Science 🌐 English βš– 156 KB

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 cycling: How a single sugar pos
✍ Chad Slawson; Michael P. Housley; Gerald W. Hart πŸ“‚ Article πŸ“… 2005 πŸ› John Wiley and Sons 🌐 English βš– 355 KB

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