Journal
FUTURE MEDICINAL CHEMISTRY
Volume 6, Issue 14, Pages 1587-1605Publisher
FUTURE SCI LTD
DOI: 10.4155/FMC.14.89
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Funding
- NIH/NCI [CA120458, CA109265]
- NATIONAL CANCER INSTITUTE [U01CA120458, U01CA109265] Funding Source: NIH RePORTER
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Hsp90 is responsible for the conformational maturation of newly synthesized polypeptides (client proteins) and the re-maturation of denatured proteins via the Hsp90 chaperone cycle. Inhibition of the Hsp90 N-terminus has emerged as a clinically relevant strategy for anticancer chemotherapeutics due to the involvement of clients in a variety of oncogenic pathways. Several immunophilins, co-chaperones and partner proteins are also necessary for Hsp90 chaperoning activity. Alternative strategies to inhibit Hsp90 function include disruption of the C-terminal dimerization domain and the Hsp90 heteroprotein complex. C-terminal inhibitors and Hsp90 co-chaperone disruptors prevent cancer cell proliferation similar to N-terminal inhibitors and destabilize client proteins without induction of heat shock proteins. Herein, current Hsp90 inhibitors, the chaperone cycle, and regulation of this cycle will be discussed.
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