Changes in Metabolic Chemical Reporter Structure Yield a Selective Probe of O-GlcNAc Modification
Author:
Affiliation:
1. Centre de Biophysique Moléculaire, CNRS UPR4301, Université d’Orléans and INSERM, F45071 Orléans Cedex 2, France
Funder
Concern Foundation
Damon Runyon Cancer Research Foundation
Ligue Contre le Cancer
National Cancer Institute
Division of Graduate Education
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja504063c
Reference52 articles.
1. Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc.
2. The subcellular distribution of terminal N-acetylglucosamine moieties. Localization of a novel protein-saccharide linkage, O-linked GlcNAc.
3. The Emerging Significance of O-GlcNAc in Cellular Regulation
4. O-GlcNAc processing enzymes: catalytic mechanisms, substrate specificity, and enzyme regulation
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