| Literature DB >> 21465572 |
Do-Hee Kim1, Joydeb Kumar Kundu, Young-Joon Surh.
Abstract
The tumor suppressor protein p53 functions as a stress-responsive transcription factor. In response to oxidative, nitrosative, and electrophilic insults, p53 undergoes post-translational modifications, such as oxidation and covalent modification of cysteines, nitration of tyrosines, acetylation of lysines, phosphorylation of serine/threonine residues, etc. Because p53 plays a vital role in the transcriptional regulation of genes encoding proteins involved in a wide spectrum of biochemical processes including DNA repair, cell-cycle regulation, and programmed cell death, the redox-modification of p53 appears to be an important determinant of cell fate. This review highlights the redox regulation of p53 and its consequences on cellular function.Entities:
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Year: 2011 PMID: 21465572 DOI: 10.1002/mc.20709
Source DB: PubMed Journal: Mol Carcinog ISSN: 0899-1987 Impact factor: 4.784