Objective Geldanamycin, a natural product of Streptomyces geldanus, binds the heat shock
protein 90 (Hsp90), a cell chaperone protein that interacts with Bcl-2. In this study, we …

Background Geldanamycin (GA) can be considered a relatively new component with a
promising mode of action against human malignancies. It specifically targets heat shock …

Geldanamycin is a naturally occurring benzoquinone ansamycin product of Streptomyces
geldanus that binds the protein chaperone heat shock protein 90. As geldanamycin binds to …

Geldanamycin (GA) binds to heat shock protein 90 (Hsp90) and interferes with its function
which is to protect various cellular proteins involved in signaling, growth control, and survival …

Heat shock protein 90 (HSP90) serves as a chaperone protein and plays a critical role in
tumor cell growth and/or survival. Geldanamycin, a specific inhibitor of HSP90, is cytotoxic to …

Background Hsp90 proteins are important therapeutic targets for many anti-cancer drugs in
clinical trials. Geldanamycin (GA) was identified as the first natural inhibitor of Hsp90 …

Abstract Purpose Heat shock protein 90 (Hsp90) is a conserved chaperone involved in
crucial signaling events in normal and malignant cells. Previous research suggests that …

Abstract Heat shock protein 90 (Hsp90) is treated as a molecular therapeutic target for the
prevention and treatment of cancer. Geldanamycin (GA) was the first identified natural …

Geldanamycin, an ansamycin-derivative benzoquinone compound, was originally isolated
as a natural product with anti-fungal activity. Later, geldanamycin was found to have anti …

Objective To investigate the role of HSP90 in proliferation and apoptosis of leukemia cells
K562 through detecting the effect of HSP90 inhibitors 17-[2-(Dimethylamino) ethyl] amino-17 …