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The HSP90 Family: Structure, Regulation, Function, and Implications in Health and Disease

1
Department of Biochemistry and Chemistry of Nutrition, Faculty of Veterinary Medicine, Cairo University, Giza 12211, Egypt
2
Department of Anatomy, Cell Biology and Physiological Sciences, Faculty of Medicine, American University of Beirut, Beirut, Lebanon
3
Department of Physiological Chemistry, University of Veterinary Medicine Hannover, Hannover 30559, Germany
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2018, 19(9), 2560; https://doi.org/10.3390/ijms19092560
Received: 6 August 2018 / Revised: 23 August 2018 / Accepted: 27 August 2018 / Published: 29 August 2018
(This article belongs to the Special Issue Molecular Chaperones)
The mammalian HSP90 family of proteins is a cluster of highly conserved molecules that are involved in myriad cellular processes. Their distribution in various cellular compartments underlines their essential roles in cellular homeostasis. HSP90 and its co-chaperones orchestrate crucial physiological processes such as cell survival, cell cycle control, hormone signaling, and apoptosis. Conversely, HSP90, and its secreted forms, contribute to the development and progress of serious pathologies, including cancer and neurodegenerative diseases. Therefore, targeting HSP90 is an attractive strategy for the treatment of neoplasms and other diseases. This manuscript will review the general structure, regulation and function of HSP90 family and their potential role in pathophysiology. View Full-Text
Keywords: HSP90; GRP94; TRAP1; molecular chaperones; structure and function; pathophysiology HSP90; GRP94; TRAP1; molecular chaperones; structure and function; pathophysiology
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MDPI and ACS Style

Hoter, A.; El-Sabban, M.E.; Naim, H.Y. The HSP90 Family: Structure, Regulation, Function, and Implications in Health and Disease. Int. J. Mol. Sci. 2018, 19, 2560.

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