The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Small molecule restoration of wildtype structure and function of mutant p53 using a novel zinc-metallochaperone based mechanism
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“ZMC1 helped coordinate zinc ions at appropriate sites to restore the structure and function of the R175 mutant442 and significantly inhibited tumor growth in mice carrying the R175H mutation.441”
From Targeting p53 pathways: mechanisms, structures, and advances in therapy (2023) · cites this paper as [442]
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“ZMCI treatment increased the folded R175 mutant protein by twofold.442”
From Targeting p53 pathways: mechanisms, structures, and advances in therapy (2023) · cites this paper as [442]
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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
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 · cited 1×
“Structural studies of WT p53 have shown that p53 requires a single zinc ion (coordinated by four amino acids C176, H179 on the L2 loop, and C238, and C242 on the L3 loop) for proper folding [10, 11].”
Senescence and tumour clearance is triggered by p53 restoration in murine liver carcinomas
Xue, W., Zender, L., Miething, C., Dickins, R. A., Hernando, E., Krizhanovsky, V., Cordon-Cardo, C., & Lowe, S. W. (2007) · Nature · doi:10.1038/nature05529 · Cited by 2,473
Restoration of p53 function leads to tumour regression in vivo
Ventura, A., Kirsch, D. G., McLaughlin, M. E., Tuveson, D. A., Grimm, J., Lintault, L., Newman, J., Reczek, E. E., Weissleder, R., & Jacks, T. (2007) · Nature · doi:10.1038/nature05541 · Cited by 1,820 · cited 1×
“Restoration of p53 function in mouse tumor models has been shown to be highly therapeutic, thus reactivating mutant p53 pharmacologically has been a highly sought after goal in anti-cancer drug development [5-7].”
Acetylation of the p53 DNA-binding domain regulates apoptosis induction.
Sykes, S. M., Mellert, H. S., Holbert, M. A., Li, K., Marmorstein, R., Lane, W. S., & McMahon, S. B. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.11.026 · Cited by 752
Modeling the Therapeutic Efficacy of p53 Restoration in Tumors
Martins, C. P., Brown-Swigart, L., & Evan, G. I. (2006) · Cell · doi:10.1016/j.cell.2006.12.007 · Cited by 600 · cited 1×
“Restoration of p53 function in mouse tumor models has been shown to be highly therapeutic, thus reactivating mutant p53 pharmacologically has been a highly sought after goal in anti-cancer drug development [5-7].”
Research works printed but not linked: 21
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- Epstein, 1995, The spectrum of mutations at the p53 locus. Evidence for tissue-specific mutagenesis, selection of mutant alleles, and a “gain of function” phenotype, Ann N Y Acad Sci, 768, 111, 10.1111/j.1749-6632.1995.tb12115.x · DOI
- Moll, 2011, Functional inactivation of endogenous MDM2 and CHIP by HSP90 causes aberrant stabilization of mutant p53 in human cancer cells, Mol Cancer Res, 9, 577, 10.1158/1541-7786.MCR-10-0534 · DOI · Paper page
- Carpizo, 2012, Allele-specific p53 mutant reactivation, Cancer Cell, 21, 614, 10.1016/j.ccr.2012.03.042 · DOI · Paper page
- Richardson, 2009, Thiosemicarbazones from the old to new: iron chelators that are more than just ribonucleotide reductase inhibitors, J Med Chem, 52, 5271, 10.1021/jm900552r · DOI · Paper page
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- D'Orazi, 2011, Restoring p53 active conformation by zinc increases the response of mutant p53 tumor cells to anticancer drugs, Cell Cycle, 10, 1679, 10.4161/cc.10.10.15642 · DOI
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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
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
Soussi, T., & Wiman, K. G. (2015) · Cell Death & Differentiation · doi:10.1038/cdd.2015.53 · Cited by 305
Bykov, V. J. N., Zhang, Q., Zhang, M., Ceder, S., Abrahmsen, L., & Wiman, K. G. (2016) · Frontiers in Oncology · doi:10.3389/fonc.2016.00021 · Cited by 137
Targeting Therapies for the p53 Protein in Cancer Treatments
Levine, A. J. (2019) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-030518-055455 · Cited by 84
Metadata
- Authors
- Yu, X., Blanden, A. R., Narayanan, S., Jayakumar, L., Lubin, D., Augeri, D., David Kimball, S., Loh, S. N., & Carpizo, D. R.
- Affiliations
- Rutgers Cancer Institute of New Jersey, New Jersey
- Department of Biochemistry and Molecular Biology, SUNY Upstate Medical University, Syracuse, New York
- Department of Surgery, Rutgers Robert Wood Johnson Medical School, New Brunswick, New Jersey
- Department of Medicinal Chemistry, Rutgers Ernest Mario School of Pharmacy, Piscataway, New Jersey
- Venue
- Oncotarget
- Publisher
- Impact Journals, LLC
- Published
- 2014-09-03
- Volume
- 5
- Issue
- 19
- Pages
- 8879-8892
- ISSN
- 1949-2553
- Cited by
- 102
- References
- 6
- Language
- en
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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.