The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
Hsp90 and co‐chaperones twist the functions of diverse client proteins
Open accessAbstract
Hsp90 molecular chaperones are required for the stability and activity of a diverse range of client proteins that have critical roles in signal transduction, cellular trafficking, chromatin remodeling, cell growth, differentiation, and reproduction. Mammalian cells contain three types of Hsp90s: cytosolic Hsp90, mitochondrial Trap‐1, and Grp94 of the endoplasmic reticulum. Each of the Hsp90s, as well as the bacterial homolog, HtpG, hydrolyze ATP and undergo similar conformational changes. Unlike the other forms of Hsp90, cytosolic Hsp90 function is dependent on a battery of co‐chaperone proteins that regulate the ATPase activity of Hsp90 or direct Hsp90 to interact with specific client proteins. This review will summarize what is known about Hsp90's ability to mediate the folding and activation of diverse client proteins that contribute to human diseases, such as cancer and fungal and viral infections. © 2009 Wiley Periodicals, Inc. Biopolymers 93: 211–217, 2010. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com
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Cites
HSP90 and the chaperoning of cancer
Whitesell, L., & Lindquist, S. L. (2005) · Nature Reviews Cancer · doi:10.1038/nrc1716 · Cited by 2,502
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Crystal structure of an Hsp90–nucleotide–p23/Sba1 closed chaperone complex
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Diverse Cellular Functions of the Hsp90 Molecular Chaperone Uncovered Using Systems Approaches
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An Acetylation Site in the Middle Domain of Hsp90 Regulates Chaperone Function
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Cited by
The HSP90 Family: Structure, Regulation, Function, and Implications in Health and Disease
Hoter, A., El-Sabban, M. E., & Naim, H. Y. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19092560 · Cited by 693
Jackson, S. E. (2012) · Topics in Current Chemistry · doi:10.1007/128_2012_356 · Cited by 338
Affinity-based proteomics reveal cancer-specific networks coordinated by Hsp90
Moulick, K., Ahn, J. H., Zong, H., Rodina, A., Cerchietti, L., Gomes DaGama, E. M., Caldas-Lopes, E., Beebe, K., Perna, F., Hatzi, K., et al. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.670 · Cited by 261
Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis
Finka, A., & Goloubinoff, P. (2013) · Cell Stress and Chaperones · doi:10.1007/s12192-013-0413-3 · Cited by 218
Hsp90 inhibitors as senolytic drugs to extend healthy aging
Fuhrmann-Stroissnigg, H., Niedernhofer, L. J., & Robbins, P. D. (2018) · Cell Cycle · doi:10.1080/15384101.2018.1475828 · Cited by 92
Metadata
- Authors
- Zuehlke, A., & Johnson, J. L.
- Venue
- Biopolymers
- Publisher
- Wiley
- Published
- 2009-08-20
- Volume
- 93
- Issue
- 3
- Pages
- 211-217
- ISSN
- 0006-3525 (ISSN-L)
- 1097-0282
- OpenAlex
- W1982826698
- Cited by
- 251
- References
- 13
- FWCI
- 4.80
- Type
- journal article
- Language
- en
- Open access
- bronze
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