Evidence map›Paper›PMID 27091942›Full record

ReviewCold Spring Harbor perspectives in medicine2017

Structural Evolution and Dynamics of the p53 Proteins.

Giovanni Chillemi, Sebastian Kehrloesser, Francesca Bernassola, Alessandro Desideri, Volker Dötsch, Arnold J Levine, Gerry Melino

Open access · bronzeAbstract readReview
In one paragraph

Review in Cold Spring Harbor perspectives in medicine, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed, 1 pooled it
–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

35 citing papers in PubMed, 1 synthesis or guideline pooled it, 56 citations in OpenAlex.

  1. Targeting p53 pathways: mechanisms, structures, and advances in therapy.Signal transduction and targeted therapy · 2023
    Pooled it
  2. Article
  3. Article
  4. Review
  5. Article
  6. Annals of laboratory medicine · 2025
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Structural Basis of Mutation-Dependent p53 Tetramerization Deficiency.International journal of molecular sciences · 2022
    Article
  13. Article
  14. ΔNp63-Senataxin circuit controls keratinocyte differentiation by promoting the transcriptional termination of epidermal genes.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  15. Review
  16. Review
  17. Review
  18. Article
  19. p73 as a Tissue Architect.Frontiers in cell and developmental biology · 2021
    Review
  20. 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 5 institutions in 4 countries.

Giovanni ChillemiCINECA, SCAI-SuperComputing Applications and Innovation Department, Rome 00185, Italy.
Sebastian KehrloesserInstitute of Biophysical Chemistry, Goethe University, 60438 Frankfurt am Main, Germany.
Francesca BernassolaDepartment of Experimental Medicine and Surgery, University of Rome "Tor Vergata," 00133 Rome, Italy.
Alessandro DesideriBiology Department, University of Rome "Tor Vergata," 00133 Rome, Italy.
Volker DötschInstitute of Biophysical Chemistry, Goethe University, 60438 Frankfurt am Main, Germany.
Arnold J LevineInstitute for Advanced Study, Princeton, New Jersey 08540.
Gerry MelinoMedical Research Council, Toxicology Unit, Leicester University, Leicester LE1 9HN, United Kingdom.
Goethe University Frankfurt · DEUniversity of Rome Tor Vergata · ITCineca · ITLeicester City Council · GBRutgers, The State University of New Jersey · US

Funding

Medical Research Council MC_U132670600
6 · The paper itself

Abstract

The family of the p53 tumor suppressive transcription factors includes p73 and p63 in addition to p53 itself. Given the high degree of amino-acid-sequence homology and structural organization shared by the p53 family members, they display some common features (i.e., induction of cell death, cell-cycle arrest, senescence, and metabolic regulation in response to cellular stress) as well as several distinct properties. Here, we describe the structural evolution of the family members with recent advances on the molecular dynamic studies of p53 itself. A crucial role of the carboxy-terminal domain in regulating the properties of the DNA-binding domain (DBD) supports an induced-fit mechanism, in which the binding of p53 on individual promoters is preferentially regulated by the

Indexed as

Binding SitesHumansMolecular Dynamics SimulationPromoter Regions, GeneticTrans-ActivatorsTranscription FactorsTumor Protein p73Tumor Suppressor Protein p53Tumor Suppressor ProteinsTP53 protein, humanTP63 protein, humanTP73 protein, humanTrans-ActivatorsTranscription FactorsTumor Protein p73Tumor Suppressor Protein p53Tumor Suppressor Proteins

Identifiers

PMID27091942
PMCPMC5378015
OpenAlexW2339239589

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.