Evidence map›Paper›PMID 36497084›Full record

ReviewCells2022

Insights into Regulators of p53 Acetylation.

Mai Nagasaka, Chiharu Miyajima, Hiromasa Aoki, Mineyoshi Aoyama, Daisuke Morishita, Yasumichi Inoue, Hidetoshi Hayashi

Open access · goldAbstract readReview
In one paragraph

Review in Cells, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.9field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

33 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
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  7. Article
  8. Article
  9. Review
  10. ACS pharmacology & translational science · 2025
    Article
  11. Article
  12. Ubiquitin E3 Ligases and p53 in Doxorubicin-Induced Cardiotoxicity.International journal of molecular sciences · 2025
    Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Targeting CBP and p300: Emerging Anticancer Agents.Molecules (Basel, Switzerland) · 2024
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Mai NagasakaDepartment of Cell Signaling, Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya 467-8603, Japan.
Chiharu MiyajimaDepartment of Cell Signaling, Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya 467-8603, Japan.
Hiromasa AokiDepartment of Pathobiology, Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya 467-8603, Japan.ORCID 0000-0001-9175-8260
Mineyoshi AoyamaDepartment of Pathobiology, Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya 467-8603, Japan.ORCID 0000-0002-9976-6465
Daisuke MorishitaDepartment of Cell Signaling, Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya 467-8603, Japan.
Yasumichi InoueDepartment of Cell Signaling, Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya 467-8603, Japan.ORCID 0000-0002-1667-1381
Hidetoshi HayashiDepartment of Cell Signaling, Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya 467-8603, Japan.ORCID 0000-0003-3742-5419
Nagoya City University · JP

Funding

Japan Science and Technology Agency JPMJSP2130Japan Society for the Promotion of Science 20K07052, 21H02650, 18K16081Nagoya City University 2021103, 2022005, 2221102
6 · The paper itself

Abstract

The tumor suppressor p53 is a transcription factor that regulates the expression of dozens of target genes and diverse physiological processes. To precisely regulate the p53 network, p53 undergoes various post-translational modifications and alters the selectivity of target genes. Acetylation plays an essential role in cell fate determination through the activation of p53. Although the acetylation of p53 has been examined, the underlying regulatory mechanisms remain unclear and, thus, have attracted the interest of researchers. We herein discuss the role of acetylation in the p53 pathway, with a focus on p53 acetyltransferases and deacetylases. We also review recent findings on the regulators of these enzymes to understand the mode of p53 acetylation from a broader perspective.

Indexed as

Protein Processing, Post-TranslationalTumor Suppressor Protein p53AcetylationAcetyltransferasesTranscription FactorsAcetyltransferasesTranscription FactorsTumor Suppressor Protein p53acetylationdeacetylationp53post-translational modification

Identifiers

PMID36497084
PMCPMC9737083
OpenAlexW4310474581

What Socratic holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.