Evidence map›Paper›PMID 19558684›Full record

ArticlePMC biophysics2009

Structural and functional implications of p53 missense cancer mutations.

Yuhong Tan, Ray Luo

Open access · hybridAbstract read
In one paragraph

Article in PMC biophysics, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.7field-weighted citation impact, top 27% 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

14 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Article
  3. A Continuum Poisson-Boltzmann Model for Membrane Channel Proteins.Journal of chemical theory and computation · 2017
    Article
  4. Article
  5. Article
  6. Recent Developments and Applications of the MMPBSA Method.Frontiers in molecular biosciences · 2017
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Analyzing effects of naturally occurring missense mutations.Computational and mathematical methods in medicine · 2012
    Article
  12. Article
  13. Impact of the 237th residue on the folding of human carbonic anhydrase II.International journal of molecular sciences · 2011
    Article
  14. Article
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

2 authors at 1 institution in 1 country.

Yuhong TanDepartment of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900, USA. rluo@uci.edu.
Ray Luo
University of California, Irvine · US

Funding

Determinants of Folding Mechanism in Small ProteinsR01GM069620 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI LUO, RAY · 2004 to 2008
$1.1M
NIGMS NIH HHS R01 GM069620
6 · The paper itself

Abstract

Most human cancers contain mutations in the transcription factor p53 and majority of these are missense and located in the DNA binding core domain. In this study, the stabilities of all core domain missense mutations are predicted and are used to infer their likely inactivation mechanisms. Overall, 47.0% non-PRO/GLY mutants are stable (DeltaDeltaG < 1.0 kT) and 36.3% mutants are unstable (DeltaDeltaG > 3.0 kT), 12.2% mutants are with 1.0 kT < DeltaDeltaG < 3.0 kT. Only 4.5% mutants are with no conclusive predictions. Certain types of either stable or unstable mutations are found not to depend on their local structures. Y, I, C, V, F and W (W, R and F) are the most common residues before (after) mutation in unstable mutants. Q, N, K, D, A, S and T (I, T, L and V) are the most common residues before (after) mutation in stable mutants. The stability correlations with sequence, structure, and molecular contacts are also analyzed. No direct correlation between secondary structure and stability is apparent, but a strong correlation between solvent exposure and stability is noticeable. Our correlation analysis shows that loss of protein-protein contacts may be an alternative cause for p53 inactivation. Correlation with clinical data shows that loss of stability and loss of DNA contacts are the two main inactivation mechanisms. Finally, correlation with functional data shows that most mutations which retain functions are stable, and most mutations that gain functions are unstable, indicating destabilized and deformed p53 proteins are more likely to find new binding partners.PACS codes: 87.14.E-

Identifiers

PMID19558684
PMCPMC2709103
OpenAlexW2152160921

What OpenQuestion holds

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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 OpenQuestion graph.