Heat shock protein (Hsp) 90 is an ATP-dependent molecular chaperone that is exploited by
malignant cells to support activated oncoproteins, including many cancer-associated …

Standing watch over the proteome, molecular chaperones are an ancient and evolutionarily
conserved class of proteins that guide the normal folding, intracellular disposition and …

Intratumor heterogeneity is a major clinical problem because tumor cell subtypes display
variable sensitivity to therapeutics and may play different roles in progression. We previously …

Abstract Heat shock protein 90 (Hsp90) is a molecular chaperone that plays a key role in the
conformational maturation of oncogenic signalling proteins, including HER-2/ErbB2, Akt, Raf …

Resveratrol (RES) is the most effective natural products used for the treatment of a variety of
cancers. In this study, we tested the effect of RES in enhancing the efficacy of docetaxel …

The cell cycle represents a series of tightly integrated events that allow the cell to grow and
proliferate. Critical parts of the cell cycle machinery are the cyclin-dependent kinases …

Purpose: HSP90 is a chaperone protein required for the stability of a variety of client
proteins. 17-Demethoxygeldanamycin (17-AAG) is a natural product that binds to HSP90 …

Abstract Heat shock protein 90 (Hsp90) is a molecular chaperone whose association is
required for the stability and function of multiple mutated, chimeric and over-expressed …

We describe the biological properties of NVP-AUY922, a novel resorcinylic isoxazole amide
heat shock protein 90 (HSP90) inhibitor. NVP-AUY922 potently inhibits HSP90 (K d= 1.7 …

Cancer is a disease characterized by genetic instability. Although identification of novel
therapeutic agents via molecular targeting offers the promise of great specificity coupled with …