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Structural Distortion of p53 by the Mutation R249S and its Rescue by a Designed Peptide: Implications for “Mutant Conformation”
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“Further experiments revealed that CDB3 could bind to G245S and R249S structural mutants,508 restore conformational folding,509 improve the affinity of the β-sheet I195T mutant to DNA, and restore the transcriptional activation function of p53 (R175H, R237H).”
From Targeting p53 pathways: mechanisms, structures, and advances in therapy (2023) · cites this paper as [508]
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Cites
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
Hot-spot mutants of p53 core domain evince characteristic local structural changes
Wong, K.-B., DeDecker, B. S., Freund, S. M. V., Proctor, M. R., Bycroft, M., & Fersht, A. R. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.15.8438 · Cited by 221
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Research works printed but not linked: 20
- Vousden, 2002, Live or let die: the cell's response to p53, Nature Rev. Cancer, 2, 594, 10.1038/nrc864 · DOI · Paper page
- Lane, 2003, Drug discovery and p53, Drug Discov. Today, 8, 347, 10.1016/S1359-6446(03)02669-2 · DOI
- 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
- 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
- Bullock, 2001, Rescuing the function of mutant p53, Nature Cancer Rev., 1, 68, 10.1038/35094077 · DOI · Paper page
- 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
- Gannon, 1990, Activating mutations in p53 produce a common conformational effect. A monoclonal antibody specific for the mutant form, EMBO J., 9, 1595, 10.1002/j.1460-2075.1990.tb08279.x · DOI · Paper page
- Legros, 1994, Mutations in p53 produce a common conformational effect that can be detected with a panel of monoclonal antibodies directed toward the central part of the p53 protein, Oncogene, 9, 3689
- Stephen, 1992, Mutant conformation of p53. Precise epitope mapping using a filamentous phage epitope library, J. Mol. Biol., 225, 577, 10.1016/0022-2836(92)90386-X · DOI
- Wang, 2001, The “wildtype” conformation of p53: epitope mapping using hybrid proteins, Oncogene, 20, 2318, 10.1038/sj.onc.1204316 · DOI
- Aguilar, 1993, Aflatoxin B1 induces the transversion of G→T in codon 249 of the p53 tumor suppressor gene in human hepatocytes, Proc. Natl Acad. Sci. USA, 90, 8586, 10.1073/pnas.90.18.8586 · DOI · Paper page
- Ghebranious, 1995, Characterization of a murine p53ser246 mutant equivalent to the human p53ser249 associated with hepatocellular carcinoma and aflatoxin exposure, Mol. Carcinog., 13, 104, 10.1002/mc.2940130207 · doi:10.1002/mc.2940130207
- Lane, 2002, Therapeutic exploitation of the p53 pathway, Trends Mol. Med., 8, S38, 10.1016/S1471-4914(02)02309-2 · DOI
- Friedler, 2002, A peptide that binds and stabilizes p53 core domain: chaperone strategy for rescue of oncogenic mutants, Proc. Natl Acad. Sci. USA, 99, 937, 10.1073/pnas.241629998 · DOI · Paper page
- Issaeva, 2003, Rescue of mutants of the tumour suppressor p53 in cancer cells by a designed peptide, Proc. Natl Acad. Sci. USA, 100, 13303, 10.1073/pnas.1835733100 · DOI · Paper page
- Kay, 1989, Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease, Biochemistry, 28, 8972, 10.1021/bi00449a003 · DOI · Paper page
- 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
- Lee, 1997, Rotational diffusion anisotropy of proteins from simultaneous analysis of 15N and 13C alpha nuclear spin relaxation, J. Biomol. NMR, 9, 287, 10.1023/A:1018631009583 · DOI · Paper page
- Bruschweiler, 1995, Long-range motional restrictions in a multidomain zinc-finger protein from anisotropic tumbling, Science, 268, 886, 10.1126/science.7754375 · DOI · Paper page
- Guex, 1997, SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling, Electrophoresis, 18, 2714, 10.1002/elps.1150181505 · DOI · Paper page
Cited by
Targeting p53 pathways: mechanisms, structures, and advances in therapy
Wang, H., Guo, M., Wei, H., & Chen, Y. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01347-1 · Cited by 1,016
Metadata
- Authors
- Friedler, A., DeDecker, B. S., Freund, S. M. V., Blair, C., Rüdiger, S., & Fersht, A. R.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2004-02
- Volume
- 336
- Issue
- 1
- Pages
- 187-196
- ISSN
- 0022-2836
- Cited by
- 69
- References
- 2
- Language
- en
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
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- Friedler, A., DeDecker, B. S., Freund, S. M. V., Blair, C., Rüdiger, S., & Fersht, A. R. (2004). Structural Distortion of p53 by the Mutation R249S and its Rescue by a Designed Peptide: Implications for “Mutant Conformation”. Journal of Molecular Biology. https://doi.org/10.1016/j.jmb.2003.12.005
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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.