The DOI matches its Crossref record; 17 of the 17 references it cites were found in a registry or an index.
The Structure‐Based Design of Mdm2/Mdmx–p53 Inhibitors Gets Serious
Open accessAbstract
The p53 protein is the cell’s principal bastion of defense against tumor‐associated DNA damage. Commonly referred as a “guardian of the genome”, p53 is responsible for determining the fate of the cell when the integrity of its genome is damaged. The development of tumors requires breaching this defense line. All known tumor cells either mutate the p53 gene, or in a similar number of cases, use internal cell p53 modulators, Mdm2 and Mdmx proteins, to disable its function. The release of functional p53 from the inhibition by Mdm2 and Mdmx should in principle provide an efficient, nongenotoxic means of cancer therapy. In recent years substantial progress has been made in developing novel p53‐activating molecules thanks to several reported crystal structures of Mdm2/x in complex with p53‐mimicking peptides and nonpeptidic drug candidates. Understanding the structural attributes of ligand binding holds the key to developing novel, highly effective, and selective drug candidates. Two low‐molecular‐weight compounds have just recently progressed into early clinical studies.
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Cites
In Vivo Activation of the p53 Pathway by Small-Molecule Antagonists of MDM2
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Structure of the MDM2 Oncoprotein Bound to the p53 Tumor Suppressor Transactivation Domain
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Restoration of p53 function leads to tumour regression in vivo
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Structure-based design of potent non-peptide MDM2 inhibitors
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Cited by
Discovery of RG7388, a Potent and Selective p53–MDM2 Inhibitor in Clinical Development
Ding, Q., Zhang, Z., Liu, J.-J., Jiang, N., Zhang, J., Ross, T. M., Chu, X.-J., Bartkovitz, D., Podlaski, F., Janson, C., et al. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm400487c · Cited by 595
Zhao, Y., Aguilar, A., Bernard, D., & Wang, S. (2015) · Journal of Medicinal Chemistry · doi:10.1021/jm501092z · Cited by 462
Targeting protein–protein interactions as an anticancer strategy
Ivanov, A. A., Khuri, F. R., & Fu, H. (2013) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2013.04.007 · Cited by 401
Sun, D., Li, Z., Rew, Y., Gribble, M., Bartberger, M. D., Beck, H. P., Canon, J., Chen, A., Chen, X., Chow, D., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm401753e · Cited by 290
Structure of the Stapled p53 Peptide Bound to Mdm2
Baek, S., Kutchukian, P. S., Verdine, G. L., Huber, R., Holak, T. A., Lee, K. W., & Popowicz, G. M. (2012) · Journal of the American Chemical Society · doi:10.1021/ja2090367 · Cited by 259
Self-citation
Metadata
- Authors
- Popowicz, G. M., Dömling, A., & Holak, T. A.
- Venue
- Angewandte Chemie International Edition
- Publisher
- Wiley
- Published
- 2011-02-21
- Volume
- 50
- Issue
- 12
- Pages
- 2680-2688
- ISSN
- 1433-7851 (ISSN-L)
- 1521-3773
- OpenAlex
- W2127506367
- Cited by
- 163
- References
- 17
- FWCI
- 8.69
- Type
- journal article
- Language
- en
- Open access
- green
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