Student or educator? Sign up with your school email and get 6 months of Pro free.
CoChat
Sign Up
Cited by 32

The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

Adaptive Evolution of p53 Thermodynamic Stability

Khoo, Kian Hoe, Andreeva, Antonina, Fersht, Alan R.·2009·Journal of Molecular Biology
DOI 10.1016/j.jmb.2009.08.013
Open this paper in CoChat — free account

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1016/j.jmb.2009.08.013

Cites

3 of 3 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Show all 3 references

Research works printed but not linked: 49

  1. Vogelstein, 2000, Surfing the p53 network, Nature, 408, 307, 10.1038/35042675 · DOI · Paper page
  2. Joerger, 2008, Structural biology of the tumor suppressor p53, Annu. Rev. Biochem., 77, 557, 10.1146/annurev.biochem.77.060806.091238 · DOI · Paper page
  3. Bullock, 2000, Quantitative analysis of residual folding and DNA binding in mutant p53 core domain: definition of mutant states for rescue in cancer therapy, Oncogene, 19, 1245, 10.1038/sj.onc.1203434 · DOI · Paper page
  4. Friedler, 2003, Kinetic instability of p53 core domain mutants: implications for rescue by small molecules, J. Biol. Chem., 278, 24108, 10.1074/jbc.M302458200 · DOI · Paper page
  5. Joerger, 2007, Structure-function-rescue: the diverse nature of common p53 cancer mutants, Oncogene, 26, 2226, 10.1038/sj.onc.1210291 · DOI · Paper page
  6. Kubbutat, 1997, Regulation of p53 stability by Mdm2, Nature, 387, 299, 10.1038/387299a0 · DOI · Paper page
  7. Mayer, 2007, Correlation of levels of folded recombinant p53 in Escherichia coli with thermodynamic stability in vitro, J. Mol. Biol., 372, 268, 10.1016/j.jmb.2007.06.044 · DOI
  8. Patel, 2008, The p73 DNA binding domain displays enhanced stability relative to its homologue, the tumor suppressor p53 and exhibits cooperative DNA binding, Biochemistry, 47, 3235, 10.1021/bi7023207 · DOI
  9. Klein, 2001, High thermostability and lack of cooperative DNA binding distinguish the p63 core domain from the homologous tumor suppressor p53, J. Biol. Chem., 276, 37390, 10.1074/jbc.M103801200 · DOI
  10. Nikolova, 1998, Semirational design of active tumor suppressor p53 DNA binding domain with enhanced stability, Proc. Natl Acad. Sci. USA, 95, 14675, 10.1073/pnas.95.25.14675 · DOI · Paper page
  11. Matsumura, 1999, In vitro evolution of thermostable p53 variants, Protein Sci., 8, 731, 10.1110/ps.8.4.731 · DOI
  12. Joerger, 2004, Crystal structure of a superstable mutant of human p53 core domain. Insights into the mechanism of rescuing oncogenic mutations, J. Biol. Chem., 279, 1291, 10.1074/jbc.M309732200 · DOI · Paper page
  13. Joerger, 2005, Structures of p53 cancer mutants and mechanism of rescue by second-site suppressor mutations, J. Biol. Chem., 280, 16030, 10.1074/jbc.M500179200 · DOI · Paper page
  14. Ang, 2006, Effects of common cancer mutations on stability and DNA binding of full-length p53 compared with isolated core domains, J. Biol. Chem., 281, 21934, 10.1074/jbc.M604209200 · DOI · Paper page
  15. Boeckler, 2008, Targeted rescue of a destabilized mutant of p53 by an in silico screened drug, Proc. Natl Acad. Sci. USA, 105, 10360, 10.1073/pnas.0805326105 · DOI · Paper page
  16. Bullock, 1997, Thermodynamic stability of wild-type and mutant p53 core domain, Proc. Natl Acad. Sci. USA, 94, 14338, 10.1073/pnas.94.26.14338 · DOI · Paper page
  17. Ho, 2006, Structure of the p53 core domain dimer bound to DNA, J. Biol. Chem., 281, 20494, 10.1074/jbc.M603634200 · DOI · Paper page
  18. Huyen, 2004, Structural differences in the DNA binding domains of human p53 and its C. elegans ortholog Cep-1, Structure, 12, 1237, 10.1016/j.str.2004.05.007 · DOI
  19. Fersht, 1985, Hydrogen bonding and biological specificity analysed by protein engineering, Nature, 314, 235, 10.1038/314235a0 · DOI · Paper page
  20. Serrano, 1992, The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability, J. Mol. Biol., 224, 783, 10.1016/0022-2836(92)90562-X · DOI · Paper page
  21. Joerger, 2006, Structural basis for understanding oncogenic p53 mutations and designing rescue drugs, Proc. Natl Acad. Sci. USA, 103, 15056, 10.1073/pnas.0607286103 · DOI · Paper page
  22. Xu, 1998, The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect, Protein Sci., 7, 158, 10.1002/pro.5560070117 · DOI
  23. Buckle, 1996, Structural and energetic responses to cavity-creating mutations in hydrophobic cores: observation of a buried water molecule and the hydrophilic nature of such hydrophobic cavities, Biochemistry, 35, 4298, 10.1021/bi9524676 · DOI
  24. Buckle, 1993, Crystal structural analysis of mutations in the hydrophobic cores of barnase, J. Mol. Biol., 234, 847, 10.1006/jmbi.1993.1630 · doi:10.1006/jmbi.1993.1630
  25. Nikolova, 2000, Mechanism of rescue of common p53 cancer mutations by second-site suppressor mutations, EMBO J., 19, 370, 10.1093/emboj/19.3.370 · DOI · Paper page
  26. Khoo, 2009, Stabilising the DNA-binding domain of p53 by rational design of its hydrophobic core, Protein Eng. Des. Sel., 22, 421, 10.1093/protein/gzp018 · DOI
  27. Ridgway, 1994, Functional characterization of Xenopus laevis p53: evidence of temperature-sensitive transactivation but not of repression, J. Virol., 68, 7178, 10.1128/JVI.68.11.7178-7187.1994 · DOI
  28. Villiard, 2007, Urodele p53 tolerates amino acid changes found in p53 variants linked to human cancer, BMC Evol. Biol., 7, 180, 10.1186/1471-2148-7-180 · DOI
  29. Levine, 1990, Tumor suppressor genes: the p53 and retinoblastoma sensitivity genes and gene products, Biochim. Biophys. Acta, 1032, 119
  30. Delmolino, 1993, Expression and stability of p53 protein in normal human mammary epithelial cells, Carcinogenesis, 14, 827, 10.1093/carcin/14.5.827 · DOI
  31. Reihsaus, 1990, Regulation of the level of the oncoprotein p53 in non-transformed and transformed cells, Oncogene, 5, 137
  32. Adelman, 1988, Oxidative damage to DNA: relation to species metabolic rate and life span, Proc. Natl Acad. Sci. USA, 85, 2706, 10.1073/pnas.85.8.2706 · DOI · Paper page
  33. Miquel, 1976, Effects of temperature on the life span, vitality and fine structure of Drosophila melanogaster, Mech. Ageing Dev., 5, 347, 10.1016/0047-6374(76)90034-8 · DOI · Paper page
  34. Schmidt-Nielsen, 1984, August and Marie Krogh and respiratory physiology, J. Appl. Physiol., 57, 293, 10.1152/jappl.1984.57.2.293 · doi:10.1152/jappl.1984.57.2.293
  35. Shigenaga, 1989, Urinary 8-hydroxy-2′-deoxyguanosine as a biological marker of in vivo oxidative DNA damage, Proc. Natl Acad. Sci. USA, 86, 9697, 10.1073/pnas.86.24.9697 · DOI · Paper page
  36. Greiss, 2008, Transcriptional profiling in C. elegans suggests DNA damage dependent apoptosis as an ancient function of the p53 family, BMC Genomics, 9, 334, 10.1186/1471-2164-9-334 · DOI
  37. Serrano, 1993, Step-wise mutation of barnase to binase. A procedure for engineering increased stability of proteins and an experimental analysis of the evolution of protein stability, J. Mol. Biol., 233, 305, 10.1006/jmbi.1993.1508 · DOI · Paper page
  38. Spector, 2000, Rational modification of protein stability by the mutation of charged surface residues, Biochemistry, 39, 872, 10.1021/bi992091m · DOI · Paper page
  39. Ventura, 2004, Designing proteins from the inside out, Proteins, 56, 1, 10.1002/prot.20142 · DOI
  40. Munson, 1996, What makes a protein a protein? Hydrophobic core designs that specify stability and structural properties, Protein Sci., 5, 1584, 10.1002/pro.5560050813 · DOI · Paper page
  41. Vogt, 1997, Protein thermal stability: hydrogen bonds or internal packing?, Fold. Des., 2, S40, 10.1016/S1359-0278(97)00062-X · DOI
  42. Dieter Perl, 2002, Some like it hot: the molecular determinants of protein thermostability, ChemBioChem, 39, 10.1002/1439-7633(20020104)3:1<39::AID-CBIC39>3.0.CO;2-D · DOI
  43. Razvi, 2006, Lessons in stability from thermophilic proteins, Protein Sci., 15, 1569, 10.1110/ps.062130306 · DOI · Paper page
  44. LeMaster, 2007, Residue cluster additivity of thermodynamic stability in the hydrophobic core of mesophile vs. hyperthermophile rubredoxins, Biophys. Chem., 125, 483, 10.1016/j.bpc.2006.10.013 · doi:10.1016/j.bpc.2006.10.013
  45. Altschul, 1997, Gapped BLAST and PSI-BLAST: a new generation of protein database search programs, Nucleic Acids Res., 25, 3389, 10.1093/nar/25.17.3389 · DOI · Paper page
  46. Clamp, 2004, The Jalview Java alignment editor, Bioinformatics, 20, 426, 10.1093/bioinformatics/btg430 · DOI · Paper page
  47. Sali, 1993, Comparative protein modelling by satisfaction of spatial restraints, J. Mol. Biol., 234, 779, 10.1006/jmbi.1993.1626 · DOI · Paper page
  48. Ikai, 1980, Thermostability and aliphatic index of globular proteins, J. Biochem., 88, 1895
  49. Kyte, 1982, A simple method for displaying the hydropathic character of a protein, J. Mol. Biol., 157, 105, 10.1016/0022-2836(82)90515-0 · DOI · Paper page

Cited by

See all 32

Metadata

Authors
Khoo, K. H., Andreeva, A., & Fersht, A. R.
Venue
Journal of Molecular Biology
Publisher
Elsevier BV
Published
2009-10
Volume
393
Issue
1
Pages
161-175
ISSN
0022-2836
DOI
10.1016/j.jmb.2009.08.013
Cited by
32
References
3
Language
en
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: Adaptive Evolution of p53 Thermodynamic Stability. https://app.cochat.ai/papers/10.1016/j.jmb.2009.08.013
The paper
Khoo, K. H., Andreeva, A., & Fersht, A. R. (2009). Adaptive Evolution of p53 Thermodynamic Stability. Journal of Molecular Biology. https://doi.org/10.1016/j.jmb.2009.08.013

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.