Negative control of p53 by Sir2alpha promotes cell survival under stress.

By J. Luo, A. Nikolaev, S. Imai, D. Chen, F. Su, A. Shiloh, L. Guarente, W. Gu. Cell, 2001

1,098 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/ecfffa62b879285fc6bf2bd4c63a30e2a6361aae

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Citations in the corpus

• Hepatocyte-specific Deletion of SIRT1 Alters Fatty Acid Metabolism and Results in Hepatic Steatosis and Inflammation (2009, unknown): “SIRT1 has been shown to deacetylate many nonhistone proteins, including p53 (Luo et al., 2001; Vaziri et al., 2001), NFkB (Yeung et al.”
• Cellular Senescence: Aging, Cancer, and Injury. (2019, background): “Indeed, SIRT1, by deacetylating p53, leads to its ubiquitination and degradation, thus suppressing its function (216, 326).”
• REACTIVE OXYGEN SPECIES, CELLULAR REDOX SYSTEMS AND APOPTOSIS (2010, unknown): “At low H2O2, Sirt1-mediated p53 deacetylation promoted p53 destruction via MDM2-dependent ubiquitination [76,77], and Sirt1 overexpression inhibited p53-mediated nuclear transactivation and blocked oxidantinduced apoptosis [78].”
• Sirtuins in aging and age-related disease. (2006, background): “Whereas Sirt1 activity was originally reported to inhibit apoptosis through deacetylation of p53 (Langley et al., 2002; Luo et al., 2001), more recent reports suggest that although Sirt1 can deacetylate p53 there is little effect on p53-mediated biological outcomes (Kamel et al.”
• SIRTUIN 1 AND SIRTUIN 3: PHYSIOLOGICAL MODULATORS OF METABOLISM (2012, background): “As SIRT1 binds and deacetylates p53 to decrease its transcriptional activity, p53 is suggested to play a central role in SIRT1-mediated functions in tumorigenesis and senescence (78, 189, 208, 339).”
• NAD+/NADH and NADP+/NADPH in Cellular Functions and Cell Death: Regulation and Biological Consequences (2008, unknown): “A number of studies have suggested that sirtuins can also mediate gene expression through multiple pathways: First, both yeast Sir2 and mammalian SIRT1 can produce histone hypoacetylation and gene repression by promoting the formation of heterochromatin—-a tightly packed form of chromatin (200); sec”
• SIRT1 deacetylase protects against neurodegeneration in models for Alzheimer's disease and amyotrophic lateral sclerosis (2007, methodology): “Membranes were incubated with Abs against SIRT1 (07–131, Upstate), a-tubulin (B512, Sigma), actin (MAB 1501, Chemicon), FAK (C-20, Santa Cruz Biotechnology), Bax (N-20, Santa Cruz) and GFP (B-2, Santa Cruz).”
• The NAD+-Dependent Deacetylase SIRT1 Modulates CLOCK-Mediated Chromatin Remodeling and Circadian Control (2008, unknown): “To confirm that equal levels of SIRT1 could still generate circadian HDAC function, we complemented cellular extracts with equal amounts of recombinant SIRT1 protein and acetylated p53 peptide as SIRT1 substrate (Luo et al., 2001; Vaziri et al., 2001).”
• SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic beta cells. (2006, background): “SIRT4 Is a Mitochondrial ADP-Ribosyltransferase Mammalian homologs of SIR2 are localized to the nucleus (Liszt et al., 2005; Luo et al., 2001; Vaziri et al., 2001), cytosol (North et al.”
• SIRT5 Deacetylates Carbamoyl Phosphate Synthetase 1 and Regulates the Urea Cycle (2009, unknown): “SIRT1 has numerous nuclear substrates that are important metabolic regulators, including PGC-1a, LXR, NF-kB, p53, and forkhead proteins (Brunet et al., 2004; Li et al., 2007; Luo et al., 2001; Motta et al., 2004; Rodgers et al., 2005; Vaziri et al., 2001; Yeung et al., 2004).”
• Sirt1 and the Mitochondria (2016, background): “One prominent transcription factor substrate of Sirt1 is the tumor suppressor TP53 (Vaziri et al., 2001), and Sirt1 deacetylation of p53 suppresses its transactivation capacity and promotes cell survival (Luo et al., 2001).”
• A Mitochondrial Paradigm of Metabolic and Degenerative Diseases, Aging, and Cancer: A Dawn for Evolutionary Medicine (2005, background): “Hence, caloric restriction also protects the mtPTP from p53-mediated activation and apoptosis (82,104,123,229).”