The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
A peptide that binds and stabilizes p53 core domain: Chaperone strategy for rescue of oncogenic mutants
Open accessAbstract
Conformationally compromised oncogenic mutants of the tumor suppressor protein p53 can, in principle, be rescued by small molecules that bind the native, but not the denatured state. We describe a strategy for the rational search for such molecules. A nine-residue peptide, CDB3, which was derived from a p53 binding protein, binds to p53 core domain and stabilizes it in vitro . NMR studies showed that CDB3 bound to p53 at the edge of the DNA binding site, partly overlapping it. The fluorescein-labeled peptide, FL-CDB3, binds wild-type p53 core domain with a dissociation constant of 0.5 μM, and raises the apparent melting temperatures of wild-type and a representative oncogenic mutant, R249S core domain. gadd45 DNA competes with CDB3 and displaces it from its binding site. But this competition does not preclude CDB3 from being a lead compound. CDB3 may act as a “chaperone” that maintains existing or newly synthesized destabilized p53 mutants in a native conformation and then allows transfer to specific DNA, which binds more tightly. Indeed, CDB3 restored specific DNA binding activity to a highly destabilized mutant I195T to close to that of wild-type level.
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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
ASPP Proteins Specifically Stimulate the Apoptotic Function of p53
Samuels-Lev, Y., O'Connor, D. J., Bergamaschi, D., Trigiante, G., Hsieh, J.-K., Zhong, S., Campargue, I., Naumovski, L., Crook, T., & Lu, X. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00367-7 · Cited by 664
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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Kastenhuber, E. R., & Lowe, S. W. (2017) · Cell · doi:10.1016/j.cell.2017.08.028 · Cited by 1,906
Muller, P. A. J., & Vousden, K. H. (2013) · Nature Cell Biology · doi:10.1038/ncb2641 · Cited by 1,647
Haupt, S., Berger, M., Goldberg, Z., & Haupt, Y. (2003) · Journal of Cell Science · doi:10.1242/jcs.00739 · Cited by 1,136
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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
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
APR-246 reactivates mutant p53 by targeting cysteines 124 and 277
Zhang, Q., Bykov, V. J. N., Wiman, K. G., & Zawacka-Pankau, J. (2018) · Cell Death & Disease · doi:10.1038/s41419-018-0463-7 · Cited by 261
Reactivation of mutant p53: molecular mechanisms and therapeutic potential
Selivanova, G., & Wiman, K. G. (2007) · Oncogene · doi:10.1038/sj.onc.1210295 · Cited by 186
Structural analysis of the interaction between Hsp90 and the tumor suppressor protein p53
Hagn, F., Lagleder, S., Retzlaff, M., Rohrberg, J., Demmer, O., Richter, K., Buchner, J., & Kessler, H. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2114 · Cited by 127
Tropak, M. B., Blanchard, J. E., Withers, S. G., Brown, E. D., & Mahuran, D. (2007) · Chemistry & Biology · doi:10.1016/j.chembiol.2006.12.006 · Cited by 105
Pharmacological reactivation of p53 as a strategy to treat cancer
Zawacka‐Pankau, J., & Selivanova, G. (2015) · Journal of Internal Medicine · doi:10.1111/joim.12336 · Cited by 82
Restoring the p53 ‘Guardian’ Phenotype in p53-Deficient Tumor Cells with CRISPR/Cas9
Chira, S., Gulei, D., Hajitou, A., & Berindan-Neagoe, I. (2018) · Trends in Biotechnology · doi:10.1016/j.tibtech.2018.01.014 · Cited by 56
Determining Biophysical Protein Stability in Lysates by a Fast Proteolysis Assay, FASTpp
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Metadata
- Authors
- Friedler, A., Hansson, L. O., Veprintsev, D. B., Freund, S. M. V., Rippin, T. M., Nikolova, P. V., Proctor, M. R., Rüdiger, S., & Fersht, A. R.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2002-01-08
- Volume
- 99
- Issue
- 2
- Pages
- 937-942
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2010370535
- Cited by
- 268
- References
- 3
- FWCI
- 7.13
- Type
- journal article
- Language
- en
- Open access
- green
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