The DOI matches its Crossref record; 16 of the 16 references it cites were found in a registry or an index.
The impact of acetylation and deacetylation on the p53 pathway
Open accessAbstract
The p53 tumor suppressor is a sequence-specific transcription factor that undergoes an abundance of post-translational modifications for its regulation and activation. Acetylation of p53 is an important reversible enzymatic process that occurs in response to DNA damage and genotoxic stress and is indispensible for p53 transcriptional activity. p53 was the first non-histone protein shown to be acetylated by histone acetyl transferases, and a number of more recent in vivo models have underscored the importance of this type of modification for p53 activity. Here, we review the current knowledge and recent findings of p53 acetylation and deacetylation and discuss the implications of these processes for the p53 pathway.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Histone deacetylases (HDACs): characterization of the classical HDAC family
RUIJTER, A. J. M. D., GENNIP, A. H. V., CARON, H. N., KEMP, S., & KUILENBURG, A. B. P. V. (2003) · Biochemical Journal · doi:10.1042/bj20021321 · Cited by 3,114
Combinatorial patterns of histone acetylations and methylations in the human genome
Wang, Z., Zang, C., Rosenfeld, J. A., Schones, D. E., Barski, A., Cuddapah, S., Cui, K., Roh, T.-Y., Peng, W., Zhang, M. Q., et al. (2008) · Nature Genetics · doi:10.1038/ng.154 · Cited by 2,331
DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2
Shieh, S.-Y., Ikeda, M., Taya, Y., & Prives, C. (1997) · Cell · doi:10.1016/s0092-8674(00)80416-x · Cited by 2,100
The first 30 years of p53: growing ever more complex.
Levine, A. J., & Oren, M. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2723 · Cited by 1,967
CBP/p300 in cell growth, transformation, and development
Goodman, R. H., & Smolik, S. (2000) · Genes & Development · doi:10.1101/gad.14.13.1553 · Cited by 1,778
Kruse, J.-P., & Gu, W. (2009) · Cell · doi:10.1016/j.cell.2009.04.050 · Cited by 1,610 · cited 5×
“A number of post-translational modifications can occur in p53 that have critical effects on its stability and function, including phosphorylation, acetylation, sumoylation, neddylation, and methylation (Kruse and Gu, 2009a).”
BackgroundInfluentialSelf-citationp53 mutant mice that display early ageing-associated phenotypes
Tyner, S. D., Venkatachalam, S., Choi, J., Jones, S., Ghebranious, N., Igelmann, H., Lu, X., Soron, G., Cooper, B., Brayton, C., et al. (2002) · Nature · doi:10.1038/415045a · Cited by 1,459 · cited 1×
“Nevertheless, p53 has a clear functional role in cellular senescence and premature aging (Tyner et al., 2002), and SIRT1-mediated deacetylation may promote this phenotype and provide a regulatory link to cellular longevity.”
BackgroundRescue of early embryonic lethality in mdm2-deficient mice by deletion of p53
de Oca Luna, R. M., Wagner, D. S., & Lozano, G. (1995) · Nature · doi:10.1038/378203a0 · Cited by 1,420 · cited 1×
“5 (Jones et al., 1995; Montes de Oca Luna et al., 1995).”
Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53
Jones, S. N., Roe, A. E., Donehower, L. A., & Bradley, A. (1995) · Nature · doi:10.1038/378206a0 · Cited by 1,280
DNA damage activates p53 through a phosphorylation–acetylation cascade
Sakaguchi, K., Herrera, J. E., Saito, S., Miki, T., Bustin, M., Vassilev, A., Anderson, C. W., & Appella, E. (1998) · Genes & Development · doi:10.1101/gad.12.18.2831 · Cited by 1,204
Cited by
Genetics of diffuse large B-cell lymphoma
Pasqualucci, L., & Dalla-Favera, R. (2018) · Blood · doi:10.1182/blood-2017-11-764332 · Cited by 282
Aberrant protein S-nitrosylation contributes to the pathophysiology of neurodegenerative diseases
Nakamura, T., Prikhodko, O. A., Pirie, E., Nagar, S., Akhtar, M. W., Oh, C.-K., McKercher, S. R., Ambasudhan, R., Okamoto, S.-I., & Lipton, S. A. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.03.017 · Cited by 165
Aubry, S., Shin, W., Crary, J. F., Lefort, R., Qureshi, Y. H., Lefebvre, C., Califano, A., & Shelanski, M. L. (2015) · PLOS ONE · doi:10.1371/journal.pone.0120352 · Cited by 106
Takayama, K.-I., Suzuki, T., Fujimura, T., Takahashi, S., & Inoue, S. (2018) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-17-0471 · Cited by 104
Extensive Post-translational Modification of Active and Inactivated Forms of Endogenous p53
DeHart, C. J., Chahal, J. S., Flint, S. J., & Perlman, D. H. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.030254 · Cited by 70
Metadata
- Authors
- Brooks, C. L., & Gu, W.
- Venue
- Protein & Cell
- Publisher
- Oxford University Press (OUP)
- Published
- 2011-06
- Volume
- 2
- Issue
- 6
- Pages
- 456-462
- ISSN
- 1674-800X (ISSN-L)
- 1674-8018
- OpenAlex
- W2134354168
- Cited by
- 280
- References
- 16
- FWCI
- 8.55
- Type
- journal article
- Language
- en
- Open access
- bronze
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: The impact of acetylation and deacetylation on the p53 pathway. https://app.cochat.ai/papers/10.1007/s13238-011-1063-9
- The paper
- Brooks, C. L., & Gu, W. (2011). The impact of acetylation and deacetylation on the p53 pathway. Protein & Cell. https://doi.org/10.1007/s13238-011-1063-9
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
