Discovery of new molecular entities able to strongly interfere with Hsp90 C-terminal domain.

ABSTRACT: Heat shock protein 90 (Hsp90) is an ATP dependent molecular chaperone deeply involved in the complex network of cellular signaling governing some key functions, such as cell proliferation and survival, invasion and angiogenesis. Over the past years the N-terminal protein domain has been fully investigated as attractive strategy against cancer, but despite the many efforts lavished in the field, none of the N-terminal binders (termed "classical inhibitors"), currently in clinical trials, have yet successfully reached the market, because of the detrimental heat shock response (HSR) that showed to induce; thus, recently, the selective inhibition of Hsp90 C-terminal domain has powerfully emerged as a more promising alternative strategy for anti-cancer therapy, not eliciting this cell rescue ca

SUBMITTER: Terracciano S 

PROVIDER: S-EPMC5786060 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature