The DOI matches its Crossref record; 322 of the 322 references it cites were found in a registry or an index.
Structure, Function, and Regulation of the Hsp90 Machinery
Open accessAbstract
Heat shock protein 90 (Hsp90) is a molecular chaperone involved in the maturation of a plethora of substrates ("clients"), including protein kinases, transcription factors, and E3 ubiquitin ligases, positioning Hsp90 as a central regulator of cellular proteostasis. Hsp90 undergoes large conformational changes during its ATPase cycle. The processing of clients by cytosolic Hsp90 is assisted by a cohort of cochaperones that affect client recruitment, Hsp90 ATPase function or conformational rearrangements in Hsp90. Because of the importance of Hsp90 in regulating central cellular pathways, strategies for the pharmacological inhibition of the Hsp90 machinery in diseases such as cancer and neurodegeneration are being developed. In this review, we summarize recent structural and mechanistic progress in defining the function of organelle-specific and cytosolic Hsp90, including the impact of individual cochaperones on the maturation of specific clients and complexes with clients as well as ways of exploiting Hsp90 as a drug target.
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Cited by
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Calcium-calcineurin signaling pathway in Candida albicans: A potential drug target
Li, W., Shrivastava, M., Lu, H., & Jiang, Y. (2021) · Microbiological Research · doi:10.1016/j.micres.2021.126786 · Cited by 47
Cryo-EM structures reveal a multistep mechanism of Hsp90 activation by co-chaperone Aha1
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Metadata
- Authors
- Biebl, M. M., & Buchner, J.
- Venue
- Cold Spring Harbor Perspectives in Biology
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2019-02-11
- Volume
- 11
- Issue
- 9
- Pages
- a034017
- ISSN
- 1943-0264 (ISSN-L)
- OpenAlex
- W2913172834
- Cited by
- 304
- References
- 322
- Type
- posted content
- Language
- en
- Open access
- bronze
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