The DOI matches its Crossref record; 38 of the 38 references it cites were found in a registry or an index.
Limiting the power of p53 through the ubiquitin proteasome pathway
Open accessAbstract
The ubiquitin proteasome pathway is critical in restraining the activities of the p53 tumor suppressor. Numerous E3 and E4 ligases regulate p53 levels. Additionally, deubquitinating enzymes that modify p53 directly or indirectly also impact p53 function. When alterations of these proteins result in increased p53 activity, cells arrest in the cell cycle, senesce, or apoptose. On the other hand, alterations that result in decreased p53 levels yield tumor-prone phenotypes. This review focuses on the physiological relevance of these important regulators of p53 and their therapeutic implications.
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Cites
In Vivo Activation of the p53 Pathway by Small-Molecule Antagonists of MDM2
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Mdm2 promotes the rapid degradation of p53
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Regulation of p53 stability by Mdm2
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“Mdm2 is an E3 ubiquitin ligase of the RING finger class that regulates p53 stability and activity (Haupt et al. 1997; Honda et al. 1997; Kubbutat et al. 1997; Marine and Lozano 2009).”
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
RING Domain E3 Ubiquitin Ligases
Deshaies, R. J., & Joazeiro, C. A. P. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.101807.093809 · Cited by 2,679
Senescence and tumour clearance is triggered by p53 restoration in murine liver carcinomas
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Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53
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Transcriptional control of human p53-regulated genes
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p53 mutant mice that display early ageing-associated phenotypes
Tyner, S. D., Venkatachalam, S., Choi, J., Jones, S., Ghebranious, N., Igelmann, H., Lu, X., Soron, G., Cooper, B., Brayton, C., et al. (2002) · Nature · doi:10.1038/415045a · Cited by 1,459 · cited 1×
“Increased p53 activity has been implicated in aging defects (Tyner et al. 2002).”
BackgroundRescue of early embryonic lethality in mdm2-deficient mice by deletion of p53
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Self-citation
Cited by
Clinical Overview of MDM2/X-Targeted Therapies
Burgess, A., Chia, K. M., Haupt, S., Thomas, D., Haupt, Y., & Lim, E. (2016) · Frontiers in Oncology · doi:10.3389/fonc.2016.00007 · Cited by 315
Soussi, T., & Wiman, K. G. (2015) · Cell Death & Differentiation · doi:10.1038/cdd.2015.53 · Cited by 305
Jeay, S., Ferretti, S., Holzer, P., Fuchs, J., Chapeau, E. A., Wartmann, M., Sterker, D., Romanet, V., Murakami, M., Kerr, G., et al. (2018) · Cancer Research · doi:10.1158/0008-5472.can-18-0338 · Cited by 87
Chapeau, E. A., Gembarska, A., Durand, E. Y., Mandon, E., Estadieu, C., Romanet, V., Wiesmann, M., Tiedt, R., Lehar, J., de Weck, A., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1620262114 · Cited by 64
P53: Stability from the Ubiquitin–Proteasome System and Specific 26S Proteasome Inhibitors
do Patrocinio, A. B., Rodrigues, V., & Guidi Magalhães, L. (2022) · ACS Omega · doi:10.1021/acsomega.1c04726 · Cited by 36
Metadata
- Authors
- Pant, V., & Lozano, G.
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2014-08-15
- Volume
- 28
- Issue
- 16
- Pages
- 1739-1751
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- OpenAlex
- W2026140625
- Cited by
- 167
- References
- 38
- Type
- posted content
- Language
- en
- Open access
- diamond
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