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Toward the Rational Design of p53-Stabilizing Drugs: Probing the Surface of the Oncogenic Y220C Mutant
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“The cavity‐creating p53 cancer mutation p.Y220C—a hot spot variant specific for MDS and AML—has been a paradigm for developing small‐molecule drugs based on protein stabilization [118, 119].”
From The TP53 tumor suppressor gene: From molecular biology to clinical investigations (2025) · cites this paper as [118]
In the citing paper
“Y220 is far from the site where p53 binds to DNA, while the tyrosine mutation between S7/S8 becomes cysteine, forming a hydrophobic cavity on the p53 surface.464,465”
From Targeting p53 pathways: mechanisms, structures, and advances in therapy (2023) · cites this paper as [465]
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Scalable molecular dynamics with NAMD
Phillips, J. C., Braun, R., Wang, W., Gumbart, J., Tajkhorshid, E., Villa, E., Chipot, C., Skeel, R. D., Kalé, L., & Schulten, K. (2005) · Journal of Computational Chemistry · doi:10.1002/jcc.20289 · Cited by 16,914
PHENIX : building new software for automated crystallographic structure determination
Adams, P. D., Grosse-Kunstleve, R. W., Hung, L.-W., Ioerger, T. R., McCoy, A. J., Moriarty, N. W., Read, R. J., Sacchettini, J. C., Sauter, N. K., & Terwilliger, T. C. (2002) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444902016657 · Cited by 4,361
Petitjean, A., Mathe, E., Kato, S., Ishioka, C., Tavtigian, S. V., Hainaut, P., & Olivier, M. (2007) · Human Mutation · doi:10.1002/humu.20495 · Cited by 1,598 · cited 1×
“The Y220C mutation, one of the more prevalent oncogenic mutations in p53 (associated with 75,000 new cancer cases per annum; Joerger and Fersht, 2008; Petitjean et al., 2007), presents an almost ideal paradigm for searching for and studying small molecules that stabilize p53 in a mutation-specific way.”
BackgroundRestoration of the tumor suppressor function to mutant p53 by a low-molecular-weight compound
Bykov, V. J. N., Issaeva, N., Shilov, A., Hultcrantz, M., Pugacheva, E., Chumakov, P., Bergman, J., Wiman, K. G., & Selivanova, G. (2002) · Nature Medicine · doi:10.1038/nm0302-282 · Cited by 1,067
Implications of protein flexibility for drug discovery
Teague, S. J. (2003) · Nature Reviews Drug Discovery · doi:10.1038/nrd1129 · Cited by 755
PRIMA-1 reactivates mutant p53 by covalent binding to the core domain
Lambert, J. M. R., Gorzov, P., Veprintsev, D. B., Söderqvist, M., Segerbäck, D., Bergman, J., Fersht, A. R., Hainaut, P., Wiman, K. G., & Bykov, V. J. N. (2009) · Cancer Cell · doi:10.1016/j.ccr.2009.03.003 · Cited by 592
Self-citationLigand efficiency and fragment-based drug discovery
Bembenek, S. D., Tounge, B. A., & Reynolds, C. H. (2009) · Drug Discovery Today · doi:10.1016/j.drudis.2008.11.007 · Cited by 196
Research works printed but not linked: 51
- Bahar, 1997, Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential, Fold. Des., 2, 173, 10.1016/S1359-0278(97)00024-2 · DOI · Paper page
- Bahar, 1998, Correlation between native-state hydrogen exchange and cooperative residue fluctuations from a simple model, Biochemistry, 37, 1067, 10.1021/bi9720641 · DOI
- Bahar, 1999, Collective motions in HIV-1 reverse transcriptase: examination of flexibility and enzyme function, J. Mol. Biol., 285, 1023, 10.1006/jmbi.1998.2371 · DOI · Paper page
- 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
- Bohm, 2004, Fluorine in medicinal chemistry, ChemBioChem, 5, 637, 10.1002/cbic.200301023 · DOI · Paper page
- Brooks, 1983, Charmm—a program for macromolecular energy, minimization, and dynamics calculations, J. Comput. Chem., 4, 187, 10.1002/jcc.540040211 · DOI · Paper page
- Bullock, 2001, Rescuing the function of mutant p53, Nat. Rev. Cancer, 1, 68, 10.1038/35094077 · DOI · Paper page
- 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
- Bykov, 2005, Reactivation of mutant p53 and induction of apoptosis in human tumor cells by maleimide analogs, J. Biol. Chem., 280, 30384, 10.1074/jbc.M501664200 · DOI · Paper page
- Ciulli, 2007, Fragment-based approaches to enzyme inhibition, Curr. Opin. Biotechnol., 18, 489, 10.1016/j.copbio.2007.09.003 · DOI
- Congreve, 2003, A rule of three for fragment-based lead discovery?, Drug Discov. Today, 8, 876, 10.1016/S1359-6446(03)02831-9 · DOI · Paper page
- Das, 2008, High-resolution structures of HIV-1 reverse transcriptase/TMC278 complexes: strategic flexibility explains potency against resistance mutations, Proc. Natl. Acad. Sci. USA, 105, 1466, 10.1073/pnas.0711209105 · DOI · Paper page
- Davis, 2007, MolProbity: all-atom contacts and structure validation for proteins and nucleic acids, Nucleic Acids Res., 35, W375, 10.1093/nar/gkm216 · DOI · Paper page
- Dennis, 2002, Computational mapping identifies the binding sites of organic solvents on proteins, Proc. Natl. Acad. Sci. USA, 99, 4290, 10.1073/pnas.062398499 · DOI
- Di Como, 1998, Human tumor-derived p53 proteins exhibit binding site selectivity and temperature sensitivity for transactivation in a yeast-based assay, Oncogene, 16, 2527, 10.1038/sj.onc.1202041 · DOI · Paper page
- Erlanson, 2006, Fragment-based lead discovery: a chemical update, Curr. Opin. Biotechnol., 17, 643, 10.1016/j.copbio.2006.10.007 · DOI
- Evans, 2006, Scaling and assessment of data quality, Acta Crystallogr. D Biol. Crystallogr., 62, 72, 10.1107/S0907444905036693 · DOI · Paper page
- Foster, 1999, Pharmacological rescue of mutant p53 conformation and function, Science, 286, 2507, 10.1126/science.286.5449.2507 · DOI · Paper page
- 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
- 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
- Guvench, 2009, Computational fragment-based binding site identification by ligand competitive saturation, PLoS Comput. Biol., 5, e1000435, 10.1371/journal.pcbi.1000435 · DOI · Paper page
- Hajduk, 2007, A decade of fragment-based drug design: strategic advances and lessons learned, Nat. Rev. Drug Discov., 6, 211, 10.1038/nrd2220 · DOI · Paper page
- Hajduk, 1997, NMR-based discovery of lead inhibitors that block DNA binding of the human papillomavirus E2 protein, J. Med. Chem., 40, 3144, 10.1021/jm9703404 · DOI · Paper page
- Hajduk, 2005, Druggability indices for protein targets derived from NMR-based screening data, J. Med. Chem., 48, 2518, 10.1021/jm049131r · DOI · Paper page
- Hajduk, 2005, Predicting protein druggability, Drug Discov. Today, 10, 1675, 10.1016/S1359-6446(05)03624-X · DOI · Paper page
- Hann, 1995, The dominating effect of mutant p53, Nat. Genet., 9, 221, 10.1038/ng0395-221 · DOI
- Hess, 2008, GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation, J. Chem. Theory Comput., 4, 435, 10.1021/ct700301q · DOI · Paper page
- Hollstein, 1991, p53 mutations in human cancers, Science, 253, 49, 10.1126/science.1905840 · DOI · Paper page
- Horovitz, 1992, Co-operative interactions during protein folding, J. Mol. Biol., 224, 733, 10.1016/0022-2836(92)90557-Z · DOI
- Humphrey, 1996, VMD: Visual molecular dynamics, J. Mol. Graph., 14, 33, 10.1016/0263-7855(96)00018-5 · DOI · Paper page
- Interlandi, 2008, Characterization and further stabilization of designed ankyrin repeat proteins by combining molecular dynamics simulations and experiments, J. Mol. Biol., 375, 837, 10.1016/j.jmb.2007.09.042 · DOI
- Issaeva, 2003, Rescue of mutants of the tumor suppressor p53 in cancer cells by a designed peptide, Proc. Natl. Acad. Sci. USA, 100, 13303, 10.1073/pnas.1835733100 · DOI · Paper page
- Joerger, 2007, Structure-function-rescue: the diverse nature of common p53 cancer mutants, Oncogene, 26, 2226, 10.1038/sj.onc.1210291 · DOI · Paper page
- Joerger, 2008, Structural biology of the tumor suppressor p53, Annu. Rev. Biochem., 77, 557, 10.1146/annurev.biochem.77.060806.091238 · DOI · Paper page
- 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
- 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
- Kitayner, 2006, Structural basis of DNA recognition by p53 tetramers, Mol. Cell, 22, 741, 10.1016/j.molcel.2006.05.015 · DOI · Paper page
- Leslie, 1999, Integration of macromolecular diffraction data, Acta Crystallogr. D Biol. Crystallogr., 55, 1696, 10.1107/S090744499900846X · DOI · Paper page
- Levine, 1991, The p53 tumour suppressor gene, Nature, 351, 453, 10.1038/351453a0 · DOI · Paper page
- Liepinsh, 1997, Organic solvents identify specific ligand binding sites on protein surfaces, Nat. Biotechnol., 15, 264, 10.1038/nbt0397-264 · DOI
- MacKerell, 1998, All-atom empirical potential for molecular modeling and dynamics studies of proteins, J. Phys. Chem. B, 102, 3586, 10.1021/jp973084f · DOI · Paper page
- Meyer, 2003, NMR spectroscopy techniques for screening and identifying ligand binding to protein receptors, Angew. Chem. Int. Ed. Engl., 42, 864, 10.1002/anie.200390233 · DOI · Paper page
- 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
- North, 2002, Restoration of wild-type conformation and activity of a temperature-sensitive mutant of p53 (p53(V272M)) by the cytoprotective aminothiol WR1065 in the esophageal cancer cell line TE-1, Mol. Carcinog., 33, 181, 10.1002/mc.10038 · DOI
- Seco, 2009, Binding site detection and druggability index from first principles, J. Med. Chem., 52, 2363, 10.1021/jm801385d · DOI · Paper page
- Seeber, 2007, Wordom: a program for efficient analysis of molecular dynamics simulations, Bioinformatics, 23, 2625, 10.1093/bioinformatics/btm378 · DOI · Paper page
- Tobi, 2005, Structural changes involved in protein binding correlate with intrinsic motions of proteins in the unbound state, Proc. Natl. Acad. Sci. USA, 102, 18908, 10.1073/pnas.0507603102 · DOI · Paper page
- Turk, D. (1992). PhD thesis. Technische Universität München, Munich, Germany.
- Vousden, 2007, p53 in health and disease, Nat. Rev. Mol. Cell Biol., 8, 275, 10.1038/nrm2147 · DOI · Paper page
- Yang, 2006, oGNM: online computation of structural dynamics using the Gaussian Network Model, Nucleic Acids Res., 34, W24, 10.1093/nar/gkl084 · DOI
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
Fragment-Based Approaches in Drug Discovery and Chemical Biology
Scott, D. E., Coyne, A. G., Hudson, S. A., & Abell, C. (2012) · Biochemistry · doi:10.1021/bi3005126 · Cited by 460
Pathological Unfoldomics of Uncontrolled Chaos: Intrinsically Disordered Proteins and Human Diseases
Uversky, V. N., Davé, V., Iakoucheva, L. M., Malaney, P., Metallo, S. J., Pathak, R. R., & Joerger, A. C. (2014) · Chemical Reviews · doi:10.1021/cr400713r · Cited by 288
Self-citationThe Free Energy Landscape of Small Molecule Unbinding
Huang, D., & Caflisch, A. (2011) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1002002 · Cited by 116
“Only recently, explicit solvent molecular dynamics (MD) simulations have been used to investigate the binding of small fragments to proteins at atomistic level of detail, which is very helpful for the design of small-molecule inhibitors [5,6,7,8].”
BackgroundAcetylation targeting chimera enables acetylation of the tumor suppressor p53
Kabir, M., Sun, N., Hu, X., Martin, T. C., Yi, J., Zhong, Y., Xiong, Y., Kaniskan, H. Ü., Gu, W., Parsons, R., et al. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.3c04640 · Cited by 65
Metadata
- Authors
- Basse, N., Kaar, J. L., Settanni, G., Joerger, A. C., Rutherford, T. J., & Fersht, A. R.
- Venue
- Chemistry & Biology
- Publisher
- Elsevier BV
- Published
- 2010-01
- Volume
- 17
- Issue
- 1
- Pages
- 46-56
- ISSN
- 1074-5521
- Cited by
- 113
- References
- 7
- Language
- en
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 1293 d)
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- Basse, N., Kaar, J. L., Settanni, G., Joerger, A. C., Rutherford, T. J., & Fersht, A. R. (2010). Toward the Rational Design of p53-Stabilizing Drugs: Probing the Surface of the Oncogenic Y220C Mutant. Chemistry & Biology. https://doi.org/10.1016/j.chembiol.2009.12.011
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