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Stabilization of p53 by CP-31398 Inhibits Ubiquitination without Altering Phosphorylation at Serine 15 or 20 or MDM2 Binding
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“CP-31398 inhibited ubiquitination and degradation of p53457 and activated BAX independently of p53 to promote apoptosis of tumor cells.455”
From Targeting p53 pathways: mechanisms, structures, and advances in therapy (2023) · cites this paper as [457]
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Citations
Cites
Mdm2 promotes the rapid degradation of p53
Haupt, Y., Maya, R., Kazaz, A., & Oren, M. (1997) · Nature · doi:10.1038/387296a0 · Cited by 4,506
Regulation of p53 stability by Mdm2
Kubbutat, M. H. G., Jones, S. N., & Vousden, K. H. (1997) · Nature · doi:10.1038/387299a0 · Cited by 3,312 · cited 3×
“Under physiological conditions, p53 is under strict control with a very short half-life, in part due to the MDM2p53 autoregulatory feedback loop (19, 25, 49).”
BackgroundDNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2
Shieh, S.-Y., Ikeda, M., Taya, Y., & Prives, C. (1997) · Cell · doi:10.1016/s0092-8674(00)80416-x · Cited by 2,100
Restoration 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
Functional and physical interactions of the ARF tumor suppressor with p53 and Mdm2
Kamijo, T., Weber, J. D., Zambetti, G., Zindy, F., Roussel, M. F., & Sherr, C. J. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.14.8292 · Cited by 899
Association of p19ARF with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53
Honda, R., & Yasuda, H. (1999) · The EMBO Journal · doi:10.1093/emboj/18.1.22 · Cited by 724
MDM2 suppresses p73 function without promoting p73 degradation
Zeng, X., Chen, L., Jost, C. A., Maya, R., Keller, D., Wang, X., Kaelin, W. G., Oren, M., Chen, J., & Lu, H. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.5.3257 · Cited by 334
Research works printed but not linked: 43
- 10.1006/excr.1998.4193 · DOI
- 10.1128/MCB.20.9.3224-3233.2000 · DOI · Paper page
- Banerjee D., 2001, Anticancer Res., 21, 3941
- 10.1002/j.1460-2075.1993.tb05678.x · DOI · Paper page
- 10.1038/sj.onc.1204204 · DOI
- 10.1038/sj.onc.1201374 · doi:10.1038/sj.onc.1201374
- 10.1038/sj.onc.1202480 · DOI · Paper page
- 10.1073/pnas.96.24.13777 · DOI · Paper page
- 10.1042/bj3590459 · doi:10.1042/bj3590459
- 10.1016/S0955-0674(00)00201-5 · DOI · Paper page
- 10.1006/scbi.1998.0097 · DOI · Paper page
- 10.1074/jbc.275.12.8945 · DOI · Paper page
- 10.1126/science.286.5449.2507 · DOI · Paper page
- 10.1073/pnas.241629998 · DOI · Paper page
- 10.1038/35023507 · DOI · Paper page
- 10.1128/MCB.20.4.1243-1253.2000 · DOI
- 10.1128/MCB.21.24.8533-8546.2001 · DOI
- 10.1073/pnas.95.5.2509 · DOI · Paper page
- 10.1073/pnas.97.15.8501 · DOI · Paper page
- Hollstein M., 1994, Nucleic Acids Res., 22, 3551
- 10.1128/MCB.17.1.460 · DOI · Paper page
- 10.1038/sj.onc.1204883 · DOI
- 10.1038/nature737 · DOI · Paper page
- 10.1038/sj.onc.1204615 · DOI
- 10.1128/MCB.21.24.8521-8532.2001 · DOI · Paper page
- 10.1006/excr.2002.5526 · DOI
- Maki C. G., 1996, Cancer Res., 56, 2649
- 10.1016/S1097-2765(01)00284-2 · DOI · Paper page
- Prabhu N. S., 1998, Int. J. Oncol., 13, 5
- 10.1038/sj.onc.1205362 · DOI · Paper page
- 10.1016/S0027-5107(00)00089-0 · DOI
- 10.1128/MCB.19.5.3395 · DOI · Paper page
- 10.1074/jbc.M202296200 · DOI
- 10.4161/cbt.1.1.42 · DOI
- 10.1111/j.1749-6632.2000.tb06705.x · DOI · Paper page
- 10.4161/cbt.1.1.41 · DOI
- 10.1093/emboj/18.7.1805 · DOI · Paper page
- 10.1038/35091170 · DOI
- 10.1016/S0092-8674(00)00171-9 · DOI · Paper page
- 10.1038/ng1097-141 · DOI · Paper page
- 10.1006/excr.2001.5314 · DOI
- 10.1074/jbc.M004894200 · DOI
- 10.1038/sj.onc.1203980 · DOI
Cited by
Haupt, S., Berger, M., Goldberg, Z., & Haupt, Y. (2003) · Journal of Cell Science · doi:10.1242/jcs.00739 · Cited by 1,136
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
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
The Ubiquitin-Proteasome Pathway and Its Role in Cancer
Mani, A., & Gelmann, E. P. (2005) · Journal of Clinical Oncology · doi:10.1200/jco.2005.05.081 · Cited by 549
Therapeutic targeting of p53: all mutants are equal, but some mutants are more equal than others
Sabapathy, K., & Lane, D. P. (2018) · Nature Reviews Clinical Oncology · doi:10.1038/nrclinonc.2017.151 · Cited by 517
Metadata
- Authors
- Wang, W., Takimoto, R., Rastinejad, F., & El-Deiry, W. S.
- Affiliations
- Laboratory of Molecular Oncology and Cell Cycle Regulation, Howard Hughes Medical Institute, Departments of Medicine, Genetics, Pharmacology, and Cancer Center, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104
- Cancer Drug Discovery, Pfizer Global Research and Development, Groton, Connecticut 06340
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2003-03-01
- Volume
- 23
- Issue
- 6
- Pages
- 2171-2181
- ISSN
- 1098-5549
- Cited by
- 126
- References
- 7
- Language
- en
- Licence
- journals.asm.org/non-commercial-tdm-license (tdm)
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- CoChat. (2026). Citation check: Stabilization of p53 by CP-31398 Inhibits Ubiquitination without Altering Phosphorylation at Serine 15 or 20 or MDM2 Binding. https://app.cochat.ai/papers/10.1128/mcb.23.6.2171-2181.2003
- The paper
- Wang, W., Takimoto, R., Rastinejad, F., & El-Deiry, W. S. (2003). Stabilization of p53 by CP-31398 Inhibits Ubiquitination without Altering Phosphorylation at Serine 15 or 20 or MDM2 Binding. Molecular and Cellular Biology. https://doi.org/10.1128/mcb.23.6.2171-2181.2003
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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.
