| Literature DB >> 25336646 |
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.Entities:
Keywords: Alzheimer Disease; Cancer; Diabetes; Gene Transcription; O-GlcNAcylation; O-Linked N-Acetylglucosamine (O-GlcNAc)
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Year: 2014 PMID: 25336646 PMCID: PMC4263848 DOI: 10.1074/jbc.R114.609776
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157