The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Effects of Common Cancer Mutations on Stability and DNA Binding of Full-length p53 Compared with Isolated Core Domains
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“Both Taz2 and a 24-residue gadd45 response element DNA bind p53 with Kd in the low nanomolar range (11, 30, 31)”
From Structure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain (2008) · cites this paper as [30]
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Crystal Structure of a p53 Tumor Suppressor-DNA Complex: Understanding Tumorigenic Mutations
Cho, Y., Gorina, S., Jeffrey, P. D., & Pavletich, N. P. (1994) · Science · doi:10.1126/science.8023157 · Cited by 2,551
Definition of a consensus binding site for p53
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The p53 pathway: positive and negative feedback loops
Harris, S. L., & Levine, A. J. (2005) · Oncogene · doi:10.1038/sj.onc.1208615 · Cited by 1,967
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Core domain interactions in full-length p53 in solution
Veprintsev, D. B., Freund, S. M. V., Andreeva, A., Rutledge, S. E., Tidow, H., Cañadillas, J. M. P., Blair, C. M., & Fersht, A. R. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0511130103 · Cited by 95
Self-citationMenendez, D., Inga, A., & Resnick, M. A. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.6.2297-2308.2006 · Cited by 81
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Cited by
mCSM: Predicting the effects of mutations in proteins using graph-based signatures
Pires, D. E. V., Ascher, D. B., & Blundell, T. L. (2014) · Bioinformatics · doi:10.1093/bioinformatics/btt691 · Cited by 1,066
Targeting mutant p53 for efficient cancer therapy
Bykov, V. J. N., Eriksson, S. E., Bianchi, J., & Wiman, K. G. (2018) · Nature Reviews Cancer · doi:10.1038/nrc.2017.109 · Cited by 889
Gain of function of mutant p53 by coaggregation with multiple tumor suppressors
Xu, J., Reumers, J., Couceiro, J. R., De Smet, F., Gallardo, R., Rudyak, S., Cornelis, A., Rozenski, J., Zwolinska, A., Marine, J.-C., et al. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.546 · Cited by 543
Structure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain
Wells, M., Tidow, H., Rutherford, T. J., Markwick, P., Jensen, M. R., Mylonas, E., Svergun, D. I., Blackledge, M., & Fersht, A. R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0801353105 · Cited by 434
Self-citationStructural basis for understanding oncogenic p53 mutations and designing rescue drugs
Joerger, A. C., Ang, H. C., & Fersht, A. R. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607286103 · Cited by 353
Self-citation
Metadata
- Authors
- Ang, H. C., Joerger, A. C., Mayer, S., & Fersht, A. R.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2006-08
- Volume
- 281
- Issue
- 31
- Pages
- 21934-21941
- ISSN
- 0021-9258
- Cited by
- 134
- References
- 8
- Language
- en
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- creativecommons.org/licenses/by/4.0/ (vor, 5186 d)
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- CoChat. (2026). Citation check: Effects of Common Cancer Mutations on Stability and DNA Binding of Full-length p53 Compared with Isolated Core Domains. https://app.cochat.ai/papers/10.1074/jbc.m604209200
- The paper
- Ang, H. C., Joerger, A. C., Mayer, S., & Fersht, A. R. (2006). Effects of Common Cancer Mutations on Stability and DNA Binding of Full-length p53 Compared with Isolated Core Domains. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m604209200
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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.
