The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.
Understanding the function–structure and function–mutation relationships of p53 tumor suppressor protein by high-resolution missense mutation analysis
Open accessAbstract
Inactivation of the tumor suppressor p53 by missense mutations is the most frequent genetic alteration in human cancers. The common missense mutations in the TP53 gene disrupt the ability of p53 to bind to DNA and consequently to transactivate downstream genes. However, it is still not fully understood how a large number of the remaining mutations affect p53 structure and function. Here, we used a comprehensive site-directed mutagenesis technique and a yeast-based functional assay to construct, express, and evaluate 2,314 p53 mutants representing all possible amino acid substitutions caused by a point mutation throughout the protein (5.9 substitutions per residue), and correlated p53 function with structure- and tumor-derived mutations. This high-resolution mutation analysis allows evaluation of previous predictions and hypotheses through interrelation of function, structure and mutation.
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“This heterogeneity also extends to the biological activity of the majority of mutant p53 proteins, as demonstrated by the various multiplex assays of variant effect conducted on over 10,000 p53 variants [32, 33, 34, 35].”
From The TP53 tumor suppressor gene: From molecular biology to clinical investigations (2025) · cites this paper as [32]
In the citing paper
“Various saturation mutagenesis studies, with substitutions at every position in this domain, have demonstrated that these changes lead to partial or total loss of DNA binding activity [32, 33, 34, 35].”
From The TP53 tumor suppressor gene: From molecular biology to clinical investigations (2025) · cites this paper as [32]
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Cites
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Cited by
Predicting the Functional Effect of Amino Acid Substitutions and Indels
Choi, Y., Sims, G. E., Murphy, S., Miller, J. R., & Chan, A. P. (2012) · PLoS ONE · doi:10.1371/journal.pone.0046688 · Cited by 2,890
TP53 mutations in human cancers: origins, consequences, and clinical use.
Olivier, M., Hollstein, M., & Hainaut, P. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a001008 · Cited by 2,199
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“…2007 WILEY-LISS, INC. and a single study has performed a systematic analysis of the activity of all possible missense mutations produced by singlenucleotide substitution in the entire sequence of TP53 (2,314 mutations) on eight different p53-RE in yeast cells [Kato et al., 2003].”
BackgroundSelf-citationRegulating the p53 pathway: in vitro hypotheses, in vivo veritas
Toledo, F., & Wahl, G. M. (2006) · Nature reviews. Cancer · doi:10.1038/nrc2012 · Cited by 1,286
When mutants gain new powers: News from the mutant p53 field
Brosh, R., & Rotter, V. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2693 · Cited by 1,132
Metadata
- Authors
- Kato, S., Han, S.-Y., Liu, W., Otsuka, K., Shibata, H., Kanamaru, R., & Ishioka, C.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2003-06-25
- Volume
- 100
- Issue
- 14
- Pages
- 8424-8429
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1990508187
- Cited by
- 874
- References
- 29
- FWCI
- 6.23
- Type
- journal article
- Language
- en
- Open access
- green
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- Kato, S., Han, S.-Y., Liu, W., Otsuka, K., Shibata, H., Kanamaru, R., & Ishioka, C. (2003). Understanding the function–structure and function–mutation relationships of p53 tumor suppressor protein by high-resolution missense mutation analysis. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1431692100
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