Abstract Heat shock protein 90 (Hsp90) and cell division cycle 37 (Cdc37) work together as
a molecular chaperone complex to regulate the activity of a multitude of client protein …

Abstract Targeting Hsp90-Cdc37 protein-protein interaction (PPI) is becoming an alternative
approach for future anti-cancer drug development. We previously reported the discovery of …

As an attractive anticancer target, the Hsp90 chaperone machine regulates a wide range of
oncoproteins. Most of the Hsp90 inhibitors in clinical trials employ the same ATP blockage …

Heat shock protein 90 (Hsp90) is a molecular chaperone which regulates maturation and
stabilization of its substrate proteins, known as client proteins. Many client proteins of Hsp90 …

Background: Specifically blocking HSP90–CDC37 interaction is emerging as a prospective
strategy for cancer therapy. Aim: Applying a kinase pseudopeptide rationale to the discovery …

The molecular chaperone Hsp90 is a ubiquitous ATPase-directed protein responsible for the
activation and structural stabilization of a large clientele of proteins. As such, Hsp90 has …

Summary Heat shock protein (Hsp90), a critical molecular chaperone that regulates the
maturation of a large number of oncogenic client proteins, plays an essential role in the …

Abstract Heat shock protein 90 (Hsp90) is one of the most abundant cellular proteins and
plays a substantial role in the folding of client proteins. The inhibition of Hsp90 has been …

Abstract Heat shock protein 90 (HSP90) is a molecular chaperone to fold and maintain the
proper conformation of many signaling proteins, especially some oncogenic proteins and …

Background Breast cancer is a common disease found among women and has been a
serious issue for last two decades. Although various kinds of heat shock proteins (Hsp's) …