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- W2069185856 endingPage "1605" @default.
- W2069185856 startingPage "1587" @default.
- W2069185856 abstract "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." @default.
- W2069185856 created "2016-06-24" @default.
- W2069185856 creator A5043830739 @default.
- W2069185856 creator A5062921807 @default.
- W2069185856 creator A5075932767 @default.
- W2069185856 date "2014-09-01" @default.
- W2069185856 modified "2023-09-27" @default.
- W2069185856 title "Alternative approaches to Hsp90 modulation for the treatment of cancer" @default.
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