Abstract
Background & Objective: The Hsp90 chaperone protein regulates the folding, maturation and stability of a wide variety of oncoproteins. In recent years, many Hsp90 inhibitors have entered into the clinical trials while all of them target ATPase showing similar binding capacity and kinds of side-effects so that none have reached to the market. During the regulation progress, numerous protein- protein interactions (PPI) such as Hsp90 and client proteins or cochaperones are involved. With the Hsp90-cochaperones PPI networks being more and more clear, many cancerous proteins have been reported to be tightly correlated to Hsp90-cochaperones PPI. Among them, Hsp90-Cdc37 PPI has been widely reported to associate with numerous protein kinases, making it a novel target for the treatment of cancers.
Results and Conclusion: In this paper, we briefly review the strategies and modulators targeting Hsp90-Cdc37 complex including direct and indirect regulation mechanism. Through these discussions we expect to present inspirations for new insights into an alternative way to inhibit Hsp90 chaperone function.Keywords: Hsp90/Cdc37, protein-protein interaction, PPI inhibitors, targeting strategies, protein kinases.
Current Drug Targets
Title:Targeting Hsp90-Cdc37: A Promising Therapeutic Strategy by Inhibiting Hsp90 Chaperone Function
Volume: 18 Issue: 13
Author(s): Lei Wang, Li Li, Kai Gu, Xiao-Li Xu, Yuan Sun and Qi-Dong You*
Affiliation:
- China Pharmaceutical University, Nanjing 210009,China
Keywords: Hsp90/Cdc37, protein-protein interaction, PPI inhibitors, targeting strategies, protein kinases.
Abstract: Background & Objective: The Hsp90 chaperone protein regulates the folding, maturation and stability of a wide variety of oncoproteins. In recent years, many Hsp90 inhibitors have entered into the clinical trials while all of them target ATPase showing similar binding capacity and kinds of side-effects so that none have reached to the market. During the regulation progress, numerous protein- protein interactions (PPI) such as Hsp90 and client proteins or cochaperones are involved. With the Hsp90-cochaperones PPI networks being more and more clear, many cancerous proteins have been reported to be tightly correlated to Hsp90-cochaperones PPI. Among them, Hsp90-Cdc37 PPI has been widely reported to associate with numerous protein kinases, making it a novel target for the treatment of cancers.
Results and Conclusion: In this paper, we briefly review the strategies and modulators targeting Hsp90-Cdc37 complex including direct and indirect regulation mechanism. Through these discussions we expect to present inspirations for new insights into an alternative way to inhibit Hsp90 chaperone function.Export Options
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Cite this article as:
Wang Lei, Li Li, Gu Kai, Xu Xiao-Li, Sun Yuan and You Qi-Dong*, Targeting Hsp90-Cdc37: A Promising Therapeutic Strategy by Inhibiting Hsp90 Chaperone Function, Current Drug Targets 2017; 18 (13) . https://dx.doi.org/10.2174/1389450117666160527125522
DOI https://dx.doi.org/10.2174/1389450117666160527125522 |
Print ISSN 1389-4501 |
Publisher Name Bentham Science Publisher |
Online ISSN 1873-5592 |
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