title: Minireview series on the thirtieth anniversary of research on O-GlcNAcylation of nuclear and cytoplasmic proteins: Nutrient regulation of cellular metabolism and physiology by O-GlcNAcylation.
abstract: The dynamic cycling of N-acetylglucosamine (termed O-GlcNAcylation) on serine or threonine residues of nuclear or cytoplasmic proteins serves as a nutrient sensor, both independently and also via its interplay with other post-translational modifications, to regulate signaling, transcription, and cellular physiology. Emerging evidence suggests that dysregulation of this ubiquitous post-translational modification contributes to the etiology of some the most important human chronic diseases.
authors.affiliation: From the Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205-2185 ghart@asbmb.org.
authors.forename: Gerald W
authors.initials: GW
authors.lastname: Hart
mesh_terms: D000117:Acetylglucosamine / Q000378:metabolism*; D000846:Anniversaries and Special Events; D002477:Cells / Q000378:metabolism*; D003593:Cytoplasm / Q000378:metabolism*; D006031:Glycosylation; D009687:Nuclear Proteins / Q000378:metabolism*; D012196:Review Literature as Topic
chemical_list: D009687:Nuclear Proteins; D000117:Acetylglucosamine
keywords: Alzheimer Disease; Cancer; Diabetes; Gene Transcription; O-GlcNAcylation; O-Linked N-Acetylglucosamine (O-GlcNAc)