The 90-kDa heat-shock protein (Hsp90) is a molecular chaperone responsible for the
stability and function of a wide variety of client proteins that are critical for cell growth and …

Molecular chaperones HSP90 and HSP70 are essential regulators of the folding and
activation of a disparate ensemble of client proteins. They function through ATP hydrolysis …

Hsp90 is an essential chaperone that guards proteome integrity and amounts to 2% of
cellular protein. We now find that Hsp90 also has the ability to directly interact with and …

The discovery and clinical development of heat shock protein 90 (Hsp90) inhibitors continue
to progress. A number of Hsp90 inhibitors are in clinical trials, and preclinical discoveries of …

Heat shock proteins 90 (Hsp90) are promising therapeutic targets due to their involvement in
stabilizing several aberrantly expressed oncoproteins. In cancerous cells, Hsp90 expression …

Cells constantly need to adopt to changing environmental conditions, maintaining
homeostasis and proteostasis. Heat shock proteins are a diverse class of molecular …

Mechanical ventilation is a life-saving intervention in critically ill patients with respiratory
failure due to acute respiratory distress syndrome (ARDS). Paradoxically, mechanical …

Abstract Heat shock protein 90 (HSP90) stabilizes many client proteins, including the BCR-
ABL1 oncoprotein. BCR-ABL1 is the hallmark of chronic myeloid leukemia (CML) in which …

The molecular chaperone heat shock protein 90 (HSP90) is a promising target for cancer
therapy, as it assists in the stabilization of cancer-related proteins, promoting cancer cell …

Classic oncogenic heat shock protein 90 (Hsp90) inhibitors target the N-terminus of the
protein, triggering a survival mechanism in cancer cells referred to as the heat shock …