The DOI matches its Crossref record; 25 of the 25 references it cites were found in a registry or an index.
Terphenyl‐Based Helical Mimetics That Disrupt the p53/HDM2 Interaction
Abstract
HDM2 regulates p53 by binding to its transactivation domain and promoting its ubiquitin-dependent degradation. Crystallographic analysis of the HDM2/p53 complex revealed that three hydrophobic residues (F19, W23, L26) along one face of the p53 helical peptide are essential for binding (see picture). Terphenyl-based antagonists mimic the α-helical region of p53 and disrupt HDM2/p53 complexation.
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Citations
Cites
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Mdm2 promotes the rapid degradation of p53
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Cited by
Metal-Free, Visible-Light-Mediated Direct C–H Arylation of Heteroarenes with Aryl Diazonium Salts
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Drugging the p53 pathway: understanding the route to clinical efficacy
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Metadata
- Authors
- Yin, H., Lee, G., Park, H. S., Payne, G. A., Rodriguez, J. M., Sebti, S. M., & Hamilton, A. D.
- Venue
- Angewandte Chemie International Edition
- Publisher
- Wiley
- Published
- 2005-04-25
- Volume
- 44
- Issue
- 18
- Pages
- 2704-2707
- ISSN
- 1433-7851 (ISSN-L)
- 1521-3773
- OpenAlex
- W2164316626
- Cited by
- 255
- References
- 25
- FWCI
- 8.48
- Type
- journal article
- Language
- en
- Open access
- closed
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- Yin, H., Lee, G., Park, H. S., Payne, G. A., Rodriguez, J. M., Sebti, S. M., & Hamilton, A. D. (2005). Terphenyl‐Based Helical Mimetics That Disrupt the p53/HDM2 Interaction. Angewandte Chemie International Edition. https://doi.org/10.1002/anie.200462316
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