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Review

The O-GlcNAc Modification

In: Essentials of Glycobiology. 2nd edition. Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 2009. Chapter 18.
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Review

The O-GlcNAc Modification

Gerald W Hart et al.
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Excerpt

This chapter presents an overview of the dynamic modification of serine or threonine hydroxyl moieties on nuclear and cytoplasmic proteins by β-linked N-acetylglucosamine, termed O-β-GlcNAc or simply O-GlcNAc.

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References

    1. Torres C.-R, Hart GW. Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc. J Biol Chem. 1984;259:3308–3317. - PubMed
    1. Hart GW. Dynamic O-linked glycosylation of nuclear and cytoskeletal proteins. Annu Rev Biochem. 1997;66:315–335. - PubMed
    1. Comer FI, Hart GW. O-Glycosylation of nuclear and cytosolic proteins. Dynamic interplay between O-GlcNAc and O-phosphate. J Biol Chem. 2000;275:29179–29182. - PubMed
    1. Wells L, Vosseller K, Hart GW. Glycosylation of nucleocytoplasmic proteins: Signal transduction and O-GlcNAc. Science. 2001;291:2376–2378. - PubMed
    1. Vocadlo DJ, Hang HC, Kim E.-J, Hanover JA, Bertozzi CR. A chemical approach for identifying O-GlcNAc-modified proteins in cells. Proc Natl Acad Sci. 2003;100:9116–9121. - PMC - PubMed

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