hSIR2SIRT1 Functions as an NAD-Dependent p53 Deacetylase
Top Cited Papers
- 1 October 2001
- Vol. 107 (2), 149-159
- https://doi.org/10.1016/s0092-8674(01)00527-x
Abstract
No abstract availableKeywords
This publication has 31 references indexed in Scilit:
- Negative Control of p53 by Sir2α Promotes Cell Survival under StressCell, 2001
- MDM2 inhibits p300-mediated p53 acetylation and activation by forming a ternary complex with the two proteinsProceedings of the National Academy of Sciences, 2000
- Phylogenetic Classification of Prokaryotic and Eukaryotic Sir2-like ProteinsBiochemical and Biophysical Research Communications, 2000
- The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylasesProceedings of the National Academy of Sciences, 2000
- Post-translational modification of p53 protein in response to ionizing radiation analyzed by mass spectrometryJournal of Molecular Biology, 2000
- Phosphorylation of p53 Serine 15 Increases Interaction with CBPJournal of Biological Chemistry, 1998
- DNA damage activates p53 through a phosphorylation–acetylation cascadeGenes & Development, 1998
- ATM-dependent telomere loss in aging human diploid fibroblasts and DNA damage lead to the post-translational activation of p53 protein involving poly(ADP-ribose) polymeraseThe EMBO Journal, 1997
- WAF1, a potential mediator of p53 tumor suppressionCell, 1993
- Advanced mammalian gene transfer: high titre retroviral vectors with multiple drug selection markers and a complementary helper-free packaging cell lineNucleic Acids Research, 1990