ArticleMolecular & cellular proteomics : MCP2009
Identification of new p53 acetylation sites in COS-1 cells.
Article in Molecular & cellular proteomics : MCP, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- Functional Investigations of p53 Acetylation Enabled by Heterobifunctional Molecules.ACS chemical biology · 2024Article
- Insights into Regulators of p53 Acetylation.Cells · 2022Review
- Lysines in the tetramerization domain of p53 selectively modulate G1 arrest.Cell cycle (Georgetown, Tex.) · 2016Article
- Extensive post-translational modification of active and inactivated forms of endogenous p53.Molecular & cellular proteomics : MCP · 2014Article
- Discovery and mechanism of natural products as modulators of histone acetylation.Current drug targets · 2012Review
- Aurora A mediates cross-talk between N- and C-terminal post-translational modifications of p53.Cancer biology & therapy · 2011Article
- Understanding wild-type and mutant p53 activities in human cancer: new landmarks on the way to targeted therapies.Cancer gene therapy · 2011Review
- Posttranslational modification of p53: cooperative integrators of function.Cold Spring Harbor perspectives in biology · 2009Review
- Mechanism of diepoxybutane-induced p53 regulation in human cells.Journal of biochemical and molecular toxicologyArticle
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The p53 tumor suppressor protein is a key regulator of cell cycle and death that is involved in many cell signaling pathways and is tightly regulated in mammalian cells. Post-translational modifications of p53 have been investigated previously mainly using antibodies. In this study, utilizing LC-MS/MS analysis, we have characterized p53 protein from COS-1 cells. Several already known post-translational modifications were observed, such as phosphorylation on serines 15, 33, 315, and 392 as well as acetylation on lysines 305, 370, 372, 373, 381, 382, and 386. Interestingly novel acetylation sites were identified at lysines 319 and 357. This study confirmed that p53 is a highly acetylated protein and revealed new acetylation sites that might aid the further understanding of p53 regulation.
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Registered trials
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