Evidence map›Paper›PMID 19297317›Full record

ArticleThe Journal of biological chemistry2009

Modulation of the oligomerization state of p53 by differential binding of proteins of the S100 family to p53 monomers and tetramers.

Jan van Dieck, Maria R Fernandez-Fernandez, Dmitry B Veprintsev, Alan R Fersht

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
6.7field-weighted citation impact, top 2% 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

67 citing papers in PubMed, 119 citations in OpenAlex.

  1. Article
  2. Review
  3. Influence of Calcium Ions on the Membrane Binding of S100B Protein.Langmuir : the ACS journal of surfaces and colloids · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Pathogenic role of S100 proteins in psoriasis.Frontiers in immunology · 2023
    Review
  8. Influence of S100A2 in Human Diseases.Diagnostics (Basel, Switzerland) · 2022
    Review
  9. Article
  10. Anticipating response function in gene regulatory networks.Journal of the Royal Society, Interface · 2021
    Article
  11. Article
  12. Article
  13. Review
  14. Tumor-Suppressor p53TADChembiochem : a European journal of chemical biology · 2020
    Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article

7 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 at 1 institution in 1 country.

Jan van DieckMedical Research Council (MRC) Laboratory of Molecular Biology and MRC Centre for Protein Engineering, Hills Road, Cambridge CB2 0QH, United Kingdom.
Maria R Fernandez-FernandezMedical Research Council (MRC) Laboratory of Molecular Biology and MRC Centre for Protein Engineering, Hills Road, Cambridge CB2 0QH, United Kingdom.
Dmitry B VeprintsevMedical Research Council (MRC) Laboratory of Molecular Biology and MRC Centre for Protein Engineering, Hills Road, Cambridge CB2 0QH, United Kingdom.
Alan R FershtMedical Research Council (MRC) Laboratory of Molecular Biology and MRC Centre for Protein Engineering, Hills Road, Cambridge CB2 0QH, United Kingdom. Electronic address: arf25@cam.ac.uk.
MRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_U105474168
6 · The paper itself

Abstract

We investigated the ways S100B, S100A1, S100A2, S100A4, and S100A6 bind to the different oligomeric forms of the tumor suppressor p53 in vitro, using analytical ultracentrifugation and multiangle light scattering. It is established that members of the S100 protein family bind to the tetramerization domain (residues 325-355) of p53 when it is uncovered in the monomer, and so binding can disrupt the tetramer. We found a stoichiometry of one dimer of S100 bound to a monomer of p53. We discovered that some S100 proteins could also bind to the tetramer. S100B bound the tetramer and also disrupted the dimer by binding monomeric p53. S100A2 bound monomeric p53 as well as tetrameric, whereas S100A1 only bound monomeric p53. S100A6 bound more tightly to tetrameric than to monomeric p53. We also identified an additional binding site for S100 proteins in the transactivation domain (1-57) of p53. Based on our results and published observations in vivo, we propose a model for the binding of S100 proteins to p53 that can explain both activation and inhibition of p53-mediated transcription. Depending on the concentration of p53 and the member of the S100 family, binding can alter the balance between monomer and tetramer in either direction.

Indexed as

HumansMultiprotein ComplexesProtein BindingProtein Structure, QuaternaryProtein Structure, TertiaryS100 ProteinsTumor Suppressor Protein p53Multiprotein ComplexesS100 ProteinsTP53 protein, humanTumor Suppressor Protein p53

Identifiers

PMID19297317
PMCPMC2679481
OpenAlexW2052021051

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.