Abstract Heat shock protein 90 (HSP90) is a highly conserved molecular chaperone that
facilitates the maturation of a wide range of proteins (known as clients). Clients are enriched …

The Hsp90 chaperone is a master regulator of the stability and activity of multiple
oncoproteins such as Her2, Akt, Bcr-Abl, c-Kit, EGFR and mutant BRAF. The promise of …

Plants, marine organisms, and microorganisms have evolved complex chemical defense
and signaling systems that are designed to protect them from predators and provide other …

The function of the heat shock proteins (HSPsa) is to fold and maintain the proper
conformation of other proteins, referred to as “clients”. HSPs are therefore molecular …

Novobiocin is a member of the coumermycin family of antibiotics and is a well-established
inhibitor of DNA gyrase. Recent studies have shown that novobiocin binds to a previously …

Inhibition of heat shock protein 90 (Hsp90) results in the degradation of oncoproteins that
drive malignant progression, inducing cell death, making Hsp90 a target of substantial …

Two recent papers attempt to solve both the tumor selectivity and the in vivo tumor
accumulation profiles seen with some Hsp90 inhibitors. They spotlight the higher affinity of …

Heat shock proteins (Hsps) are molecular chaperones that also play important roles in the
activation of the heat shock response (HSR). The HSR is an evolutionary conserved and …

The 90 kDa heat shock proteins (Hsp90) are responsible for the conformational maturation
of nascent polypeptides and the rematuration of denatured proteins. Proteins dependent …

Heat shock protein 90 (Hsp90) plays a central role in signal transduction and has emerged
as a promising target for anti-cancer therapeutics, but its molecular mechanism is poorly …