The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.
Mechanisms of Hsp90 regulation
Open accessAbstract
Heat shock protein 90 (Hsp90) is a molecular chaperone that is involved in the activation of disparate client proteins. This implicates Hsp90 in diverse biological processes that require a variety of co-ordinated regulatory mechanisms to control its activity. Perhaps the most important regulator is heat shock factor 1 (HSF1), which is primarily responsible for upregulating Hsp90 by binding heat shock elements (HSEs) within Hsp90 promoters. HSF1 is itself subject to a variety of regulatory processes and can directly respond to stress. HSF1 also interacts with a variety of transcriptional factors that help integrate biological signals, which in turn regulate Hsp90 appropriately. Because of the diverse clientele of Hsp90 a whole variety of co-chaperones also regulate its activity and some are directly responsible for delivery of client protein. Consequently, co-chaperones themselves, like Hsp90, are also subject to regulatory mechanisms such as post translational modification. This review, looks at the many different levels by which Hsp90 activity is ultimately regulated.
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Cites
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Signaling pathways and targeted therapy for myocardial infarction
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Metadata
- Authors
- Prodromou, C.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2016-08-11
- Volume
- 473
- Issue
- 16
- Pages
- 2439-2452
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- OpenAlex
- W2513455229
- Cited by
- 311
- References
- 20
- FWCI
- 13.84
- Type
- journal article
- Language
- en
- Open access
- hybrid
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