Small-molecule drug discovery has traditionally focused on occupancy of a binding site that
directly affects protein function, and this approach typically precludes targeting proteins that …

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 …

Delivery of therapeutic proteins into tissues and across the blood-brain barrier is severely
limited by the size and biochemical properties of the proteins. Here it is shown that …

The Hsp90 chaperone is required for the activation of several families of eukaryotic protein
kinases and nuclear hormone receptors, many of which are proto-oncogenic and play a …

Hsp90 molecular chaperones in eukaryotic cells play essential roles in the folding and
activation of a range of client proteins involved in cell cycle regulation, steroid hormone …

The 90-kDa molecular chaperone family (which comprises, among other proteins, the 90-
kDa heat-shock protein, hsp90 and the 94-kDa glucose-regulated protein, grp94, major …

The molecular chaperone heat shock protein 90 (Hsp90) and its accessory cochaperones
function by facilitating the structural maturation and complex assembly of client proteins …

Hsp90 (heat shock protein of 90 kDa) is a ubiquitous molecular chaperone responsible for
the assembly and regulation of many eukaryotic signalling systems and is an emerging …

▪ Abstract Recent years have witnessed dramatic advances in our understanding of how
newly translated proteins fold in the cell and the contribution of molecular chaperones to this …

Arsenic trioxide has shown substantial efficacy in treating both newly diagnosed and
relapsedpatients with acute promyelocytic leukemia (APL). As a single agent, it induces …