The heat shock protein 90 (HSP90) chaperone machinery is a key regulator of proteostasis
under both physiological and stress conditions in eukaryotic cells. As HSP90 has several …

Heat shock protein 90 (Hsp90) is a molecular chaperone involved in the maturation of a
plethora of substrates (“clients”), including protein kinases, transcription factors, and E3 …

Abstract Structure-based drug design has often been restricted by the rather static picture of
protein–ligand complexes presented by crystal structures, despite the widely accepted …

Nearly 100 proteins are known to be regulated by hsp90. Most of these substrates or “client
proteins” are involved in signal transduction, and they are brought into complex with hsp90 …

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 …

Hsp90 is an abundant molecular chaperone essential to the establishment of many cellular
regulation and signal transduction systems, but remains one of the least well described …

Molecular chaperones are a functionally defined set of proteins which assist the structure
formation of proteins in vivo. Without certain protective mechanisms, such as binding …

Heat shock protein 90 (Hsp90), an abundant molecular chaperone in the eukaryotic cytosol,
is involved in the folding of a set of cell regulatory proteins and in the re-folding of stress …

Hsp90 is an abundant molecular chaperone that is involved in the folding of a defined set of
signalling molecules including steroid-hormone receptors and kinases. Recent in vitro …

Heat shock protein 90 (Hsp90), one of the most abundant chaperones in eukaryotes,
participates in folding and stabilization of signal-transducing molecules including steroid …