The DOI matches its Crossref record; 56 of the 56 references it cites were found in a registry or an index.
The Roles of MDM2 and MDMX in Cancer
Open accessAbstract
For more than 25 years, MDM2 and its homolog MDMX (also known as MDM4) have been shown to exert oncogenic activity. These two proteins are best understood as negative regulators of the p53 tumor suppressor, although they may have additional p53-independent roles. Understanding the dysregulation of MDM2 and MDMX in human cancers and how they function either together or separately in tumorigenesis may improve methods of diagnosis and for assessing prognosis. Targeting the proteins themselves, or their regulators, may be a promising therapeutic approach to treating some forms of cancer.
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Cites
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In Vivo Activation of the p53 Pathway by Small-Molecule Antagonists of MDM2
Vassilev, L. T., Vu, B. T., Graves, B., Carvajal, D., Podlaski, F., Filipovic, Z., Kong, N., Kammlott, U., Lukacs, C., Klein, C., et al. (2004) · Science · doi:10.1126/science.1092472 · Cited by 4,661
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 1×
“Furthermore, it was demonstrated that MDM2 not only inhibits p53 transactivation of its target genes but also mediates degradation of p53 (14, 15) by serving as an E3 ubiquitin ligase (16).”
BackgroundBlinded by the Light: The Growing Complexity of p53
Vousden, K. H., & Prives, C. (2009) · Cell · doi:10.1016/j.cell.2009.04.037 · Cited by 3,163
Self-citationMomand, J., Zambetti, G. P., Olson, D. C., George, D., & Levine, A. J. (1992) · Cell · doi:10.1016/0092-8674(92)90644-r · Cited by 3,113
Structure of the MDM2 Oncoprotein Bound to the p53 Tumor Suppressor Transactivation Domain
Kussie, P. H., Gorina, S., Marechal, V., Elenbaas, B., Moreau, J., Levine, A. J., & Pavletich, N. P. (1996) · Science · doi:10.1126/science.274.5289.948 · Cited by 2,206
TP53 mutations in human cancers: origins, consequences, and clinical use.
Olivier, M., Hollstein, M., & Hainaut, P. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a001008 · Cited by 2,199 · cited 1×
“The TP53 gene is mutated in approximately one-half of all sporadic human cancers, although mutation frequency varies greatly with tumor type (3).”
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
Self-citationThe first 30 years of p53: growing ever more complex.
Levine, A. J., & Oren, M. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2723 · Cited by 1,967
Cited by
iPLA2β-mediated lipid detoxification controls p53-driven ferroptosis independent of GPX4
Chen, D., Chu, B., Yang, X., Liu, Z., Jin, Y., Kon, N., Rabadan, R., Jiang, X., Stockwell, B. R., & Gu, W. (2021) · Nature Communications · doi:10.1038/s41467-021-23902-6 · Cited by 348
Relevance of the p53–MDM2 axis to aging
Wu, D., & Prives, C. (2018) · Cell Death & Differentiation · doi:10.1038/cdd.2017.187 · Cited by 215
Self-citationTRIM67 Activates p53 to Suppress Colorectal Cancer Initiation and Progression
Wang, S., Zhang, Y., Huang, J., Wong, C. C., Zhai, J., Li, C., Wei, G., Zhao, L., Wang, G., Wei, H., et al. (2019) · Cancer Research · doi:10.1158/0008-5472.can-18-3614 · Cited by 104
Pairawan, S., Zhao, M., Yuca, E., Annis, A., Evans, K., Sutton, D., Carvajal, L., Ren, J.-G., Santiago, S., Guerlavais, V., et al. (2021) · Breast Cancer Research · doi:10.1186/s13058-021-01406-x · Cited by 73
Regulation of the p53 Family Proteins by the Ubiquitin Proteasomal Pathway
Bang, S., Kaur, S., & Kurokawa, M. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms21010261 · Cited by 69
Metadata
- Authors
- Karni-Schmidt, O., Lokshin, M., & Prives, C.
- Venue
- Annual Review of Pathology: Mechanisms of Disease
- Publisher
- Annual Reviews
- Published
- 2016-05-23
- Volume
- 11
- Issue
- 1
- Pages
- 617-644
- ISSN
- 1553-4006 (ISSN-L)
- 1553-4014
- OpenAlex
- W2303171964
- Cited by
- 296
- References
- 56
- FWCI
- 2.75
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Karni-Schmidt, O., Lokshin, M., & Prives, C. (2016). The Roles of MDM2 and MDMX in Cancer. Annual Review of Pathology: Mechanisms of Disease. https://doi.org/10.1146/annurev-pathol-012414-040349
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