Heat shock protein 90, also known as Hsp90, is an extensively preserved molecular
chaperone that performs a critical function in organizing various biological pathways and …

Heat shock protein (HSP) 90 is the most abundant HSPs, which are chaperone molecules
whose major roles are cell protection and maintenance by means of aiding the folding, the …

In patients with peritoneal carcinomatosis cytoreductive surgery combined with hyperthermic
intraperitoneal chemotherapy (HIPEC) represents a promising treatment strategy. Here, we …

Despite Hsp90's well documented promise as a target for developing cancer
chemotherapeutics, its inhibitors have struggled to progress through clinical trials. This is, in …

The inhibition of heat shock protein 90 (Hsp90) is a promising strategy to increase the
radiosensitivity of tumor cells. However, Hsp90 inhibition induces the expression of Hsp70 …

Sixteen linear and cyclic peptides were designed de novo to target the C-terminus of heat
shock protein 90 (Hsp90). Protein binding data indicates that three compounds directly block …

Described is the role that heat shock factor 1 (HSF1) plays in regulating cellular stress.
Focusing on the current state of the HSF1 field in chemotherapeutics we outline the …

Proteostasis in the cytosol is governed by the heat shock response. The master regulator of
the heat shock response, heat shock factor 1 (HSF1), and key chaperones whose levels are …

BACKGROUND While there is compelling rationale to use heat shock protein 90 (Hsp90)
inhibitors for treatment of advanced prostate cancer, agents that target the N‐terminal ATP …

Selectively inhibiting target proteins in cancer cells over normal cells is one of the most
critical features of a successful protein inhibitor for clinical applications. By evaluating and …