Recent studies have shown that the DNA gyrase inhibitor, novobiocin, binds to a previously
unrecognized ATP-binding site located at the C-terminus of Hsp90 and induces degradation …

Purpose: Heat shock protein 90 (HSP90) is required for the proper folding, function, and
stability of various client proteins, two of which (KIT and PDGFRα) are critical in the …

The molecular chaperone heat shock protein 90 (HSP90) has emerged as an exciting
molecular target. Derivatives of the natural product geldanamycin, such as 17-allylamino-17 …

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 …

A ubiquitously expressed chaperone, heat shock protein 90 (HSP 90) is of considerable
interest as an oncology target because tumor cells and oncogenic proteins are acutely …

Abstract β-Elemene is the major constituent of the antitumor drugs elemene extract
approved in China. By incorporating macrocyclization strategy into the β-elemene skeleton …

Supramolecular nanomaterials responsive to specific intracellular proteins should be greatly
promising for protein sensing and imaging, controlled drug release or dynamic regulation of …

Hsp90 is an evolutionarily conserved and ubiquitously expressed molecular chaperone that
mainly modulates, along with a group of co-chaperones, the general platform of protein …

The ansamycin class of natural products is well known for its anti-tumor effects and has been
extensively studied by cancer researchers for nearly four decades. The first description of …

Heat shock protein 90 has emerged as a promising target for the treatment of cancer and
neurodegenerative diseases. This review summarizes recent advancements towards the …