Evidence map›Paper›PMID 23112865›Full record

ArticlePloS one2012

Stability of p53 homologs.

Tobias Brandt, Joel L Kaar, Alan R Fersht, Dmitry B Veprintsev

Abstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Article
  2. TP53: the unluckiest of genes?Cell death and differentiation · 2025
    Review
  3. Article
  4. Article
  5. Article
  6. Functional interplay among thiol-based redox signaling, metabolism, and ferroptosis unveiled by a genetic variant ofProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Propagation of aggregated p53: Cross-reaction and coaggregation vs. seeding.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  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

4 authors.

Tobias BrandtMRC Centre for Protein Engineering, Cambridge, United Kingdom.
Joel L Kaar
Alan R Fersht
Dmitry B Veprintsev

Funding

Cancer Research UKMedical Research Council MC_UP_A024_1010
6 · The paper itself

Abstract

Most proteins have not evolved for maximal thermal stability. Some are only marginally stable, as for example, the DNA-binding domains of p53 and its homologs, whose kinetic and thermodynamic stabilities are strongly correlated. Here, we applied high-throughput methods using a real-time PCR thermocycler to study the stability of several full-length orthologs and paralogs of the p53 family of transcription factors, which have diverse functions, ranging from tumour suppression to control of developmental processes. From isothermal denaturation fluorimetry and differential scanning fluorimetry, we found that full-length proteins showed the same correlation between kinetic and thermodynamic stability as their isolated DNA-binding domains. The stabilities of the full-length p53 orthologs were marginal and correlated with the temperature of their organism, paralleling the stability of the isolated DNA-binding domains. Additionally, the paralogs p63 and p73 were significantly more stable and long-lived than p53. The short half-life of p53 orthologs and the greater persistence of the paralogs may be biologically relevant.

Indexed as

Protein StabilityAnimalsBinding SitesDNA-Binding ProteinsDrosophilaHumansKineticsMiceNuclear ProteinsProtein DenaturationProtein Structure, TertiaryThermodynamicsTranscription FactorsTumor Protein p73Tumor Suppressor Protein p53Tumor Suppressor ProteinsDNA-Binding ProteinsNuclear ProteinsTP63 protein, humanTP73 protein, humanTranscription FactorsTrp73 protein, mouseTumor Protein p73Tumor Suppressor Protein p53Tumor Suppressor Proteins

Identifiers

PMID23112865
PMCPMC3480436

What OpenQuestion holds

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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.