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

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          Abstract

          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.

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          Most cited references260

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          The HSP90 chaperone machinery

          The heat shock protein 90 (HSP90) chaperone machinery is a key regulator of proteostasis. Recent progress has shed light on the interactions of HSP90 with its clients and co-chaperones, and on their functional implications. This opens up new avenues for the development of drugs that target HSP90, which could be valuable for the treatment of cancers and protein-misfolding diseases.
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            The heat-shock response.

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              A new puffing pattern induced by temperature shock and DNP in drosophila

              F Ritossa (1962)
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                Author and article information

                Journal
                Int J Mol Sci
                Int J Mol Sci
                ijms
                International Journal of Molecular Sciences
                MDPI
                1422-0067
                29 August 2018
                September 2018
                : 19
                : 9
                : 2560
                Affiliations
                [1 ]Department of Biochemistry and Chemistry of Nutrition, Faculty of Veterinary Medicine, Cairo University, Giza 12211, Egypt; abdullah.hoter@ 123456vet.cu.edu.eg or abdo_hotar@ 123456yahoo.com
                [2 ]Department of Anatomy, Cell Biology and Physiological Sciences, Faculty of Medicine, American University of Beirut, Beirut, Lebanon; me00@ 123456aub.edu.lb
                [3 ]Department of Physiological Chemistry, University of Veterinary Medicine Hannover, Hannover 30559, Germany
                Author notes
                [* ]Correspondence: hassan.naim@ 123456tiho-hannover.de ; Tel.: +49-511-953-8780; Fax: +49-511-953-8585
                Author information
                https://orcid.org/0000-0003-4884-8425
                Article
                ijms-19-02560
                10.3390/ijms19092560
                6164434
                30158430
                e141a5a7-7f0a-4ae2-ace0-fb2c7021a73c
                © 2018 by the authors.

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                : 06 August 2018
                : 27 August 2018
                Categories
                Review

                Molecular biology
                hsp90,grp94,trap1,molecular chaperones,structure and function,pathophysiology
                Molecular biology
                hsp90, grp94, trap1, molecular chaperones, structure and function, pathophysiology

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