HSP90 inhibitors and cancer: Prospects for use in targeted therapies (Review).

ABSTRACT: Heat shock protein 90 (HSP90) is a vital chaperone protein, regulating signaling pathways and correcting misfolded proteins in cancer cells by interacting with oncogenic client proteins and co‑chaperones. The inhibition of HSP90 chaperone machinery has been demonstrated as a potential approach with which to inhibit tumor survival, proliferation, invasion and migration. Numerous HSP90 inhibitors have been reported and have exhibited value as cancer‑targeted therapies by interrupting the ATPase activity of HSP90, thus suppressing the oncogenic pathways in cancer cells. These inhibitors have been classified into three categories: i) N‑terminal domain (NTD) inhibitors; ii) C‑terminal domain (CTD) inhibitors; and iii) isoform‑selective inhibitors. However, none of these HSP90 inhibitors are use

SUBMITTER: Li ZN 

PROVIDER: S-EPMC9685368 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature