Evidence map›Paper›PMID 22505655›Full record

ReviewCarcinogenesis2012

p53 N-terminal phosphorylation: a defining layer of complex regulation.

Lisa M Miller Jenkins, Stewart R Durell, Sharlyn J Mazur, Ettore Appella

Abstract readReview
In one paragraph

Review in Carcinogenesis, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
–field-weighted citation impact
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

62 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Review
  7. PBLD enhances antiviral innate immunity by promoting the p53-USP4-MAVS signaling axis.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Accelerated Multiphosphorylated Peptide Synthesis.Organic process research & development · 2022
    Review
  19. Review
  20. SelectiveAngewandte Chemie (International ed. in English) · 2022
    Article

2 more citing papers are in PubMed but not listed here.

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

4 authors.

Lisa M Miller JenkinsLaboratory of Cell Biology, National Cancer Institute, NIH, 37 Convent Drive, Room 2140, Bethesda, MD 20892, USA.
Stewart R Durell
Sharlyn J Mazur
Ettore Appella

Funding

Tumor Suppressor Protein, p53ZIABC005599 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI APPELLA, ETTORE · 2009 to 2025
$8.1M
Intramural NIH HHS
6 · The paper itself

Abstract

The p53 tumor suppressor is a critical component of the cellular response to stress. As it can inhibit cell growth, p53 is mutated or functionally inactivated in most tumors. A multitude of protein-protein interactions with transcriptional cofactors are central to p53-dependent responses. In its activated state, p53 is extensively modified in both the N- and C-terminal regions of the protein. These modifications, especially phosphorylation of serine and threonine residues in the N-terminal transactivation domain, affect p53 stability and activity by modulating the affinity of protein-protein interactions. Here, we review recent findings from in vitro and in vivo studies on the role of p53 N-terminal phosphorylation. These modifications can either positively or negatively affect p53 and add a second layer of complex regulation to the divergent interactions of the p53 transactivation domain.

Indexed as

AnimalsHumansMiceModels, MolecularPhosphorylationTumor Suppressor Protein p53Tumor Suppressor Protein p53

Identifiers

PMID22505655
PMCPMC3499055

What OpenQuestion holds

Textmetadata
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 OpenQuestion graph.