Journal
MOLECULAR CARCINOGENESIS
Volume 50, Issue 4, Pages 222-234Publisher
WILEY
DOI: 10.1002/mc.20709
Keywords
p53; redox modulation; thiol modification; redox status
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Funding
- MEST (Ministry of Education, Science and Technology) [C00025, R31-2008-000-10103-0]
- NRF (National Research Foundation), Republic of Korea
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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. (C) 2011 Wiley-Liss, Inc.
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