Deacetylation of p53 modulates its effect on cell growth and apoptosis
By Jianyuan Luo, F. Su, Delin Chen, A. Shiloh, W. Gu. Nature, 2000
855 citations recorded by the source corpus.
Subfields: Molecular Biology, Oncology
View Paper: https://www.semanticscholar.org/paper/2897b68ced3df7452156d105f6348252e924bba9
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Citations in the corpus
- miR-34a repression of SIRT1 regulates apoptosis (2008, result): “Our study extends the results of others showing that SIRT1 deacetylates p53, limiting the ability of p53 to transactivate its target genes (51, 52, 57).”
- Acetylation is indispensable for p53 activation. (2008, background): “The acetylation levels of p53 are significantly enhanced in response to stress and correlate well with p53 activation and stabilization (Luo et al., 2000, 2001; Vaziri et al., 2001; Ito et al., 2001; Barlev et al., 2001; Knights et al., 2006; Li et al., 2007; Zhao et al., 2008; Kim et al., 2008).”
- Ubiquitination, phosphorylation and acetylation: the molecular basis for p53 regulation. (2003, background): “metastasis-associated protein 2), a component of the HDAC1 complex that can enhance HDAC1-mediated deacetylation of p53 [73 ,74].”
- Pirh2, a p53-induced ubiquitin-protein ligase, promotes p53 degradation. (2003, neutral): “, 2001) and the HDAC1 complex (Luo et al., 2000).”
- Erasers of histone acetylation: the histone deacetylase enzymes. (2014, background): “HDAC1 interacts with and deacetylates p53, promoting p53 ubiquitination and degradation (Luo et al. 2000).”
- Post-translational modification of p53 in tumorigenesis (2004, background): “Luo et al.15 also showed that Sir2α expression suppressed p53 transcriptional activation and p53-mediated apoptosis.”
- Regulation of p53 activity by its interaction with homeodomain-interacting protein kinase-2 (2002, methodology): “c, GST–p53(1-80) or a point mutant of this fusion protein containing a Ser 46 to alanine exchange were employed as substrate proteins, typical autoradiograms are displayed.”