Related Experiment Video
Updated: Jun 15, 2026

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors
Published on: January 20, 2023
ATPase inhibitors of heat-shock protein 90, second season
1Institut Pasteur, 28 rue du Dr. Roux, 75724 Paris Cedex 15, France. yves.janin@pasteur.fr
Abstract:
In the past four years, the ATP-dependent heat-shock protein 90 has remained the focus of much interest. Phase I and phase II anticancer clinical trials with first-generation inhibitors, although sometimes disappointing, have yet to report a forbidding side-effect inherent to the inhibition of this chaperone, which has a very complex and widespread role in cell biochemistry. Research in the field has started to unravel an elaborate regulation picture leading to the proper folding of many proteins. On the medicinal chemistry side, a second wave of inhibitors has been reported. This review attempts to describe all the ATPase inhibitors of HSP90 reported since our last survey.
Related Concept Videos
Molecular Chaperones and Protein Folding
The...
Molecular Chaperones and Protein Folding
The...
Bacterial Protein Maturation
ATP Synthase: Mechanism
Diversity of Archaea IV
ATP Driven Pumps III: V-type Pumps
The peripheral or cytosolic V1 domain with eight subunits is involved in ATP hydrolysis. The integral or transmembrane V0 domain containing at least five subunits...

