Abstract Heat shock protein 90 (HSP90) is a chaperone with vital roles in regulating
proteostasis, long recognized for its function in protein folding and maturation. A view is …

The heat shock proteins (HSPs) are ubiquitous and conserved protein families in both
prokaryotic and eukaryotic organisms, and they maintain cellular proteostasis and protect …

Hsp90 is a conserved and essential molecular chaperone responsible for the folding and
activation of hundreds of 'client'proteins,–. The glucocorticoid receptor (GR) is a model client …

Molecular chaperones govern proteome health to support cell homeostasis. An essential
eukaryotic component of the chaperone system is Hsp90. Using a chemical-biology …

HSP70 and HSP90 are two powerful chaperone machineries involved in survival and
proliferation of tumor cells. Residing in various cellular compartments, HSP70 and HSP90 …

Hsp90 is an essential molecular chaperone responsible for the folding and activation of
hundreds of 'client'proteins, including the glucocorticoid receptor (GR). Previously, we …

The Hsp90 chaperone promotes folding and activation of hundreds of client proteins in the
cell through an ATP-dependent conformational cycle guided by distinct cochaperone …

Aryl hydrocarbon receptor (AhR) is an important ligand-activated transcription factor
involved in the regulation of various important physiological functions. Here, we report the …

In the eukaryotic cytosol, the Hsp70 and the Hsp90 chaperone machines work in tandem
with the maturation of a diverse array of client proteins. The transfer of nonnative clients …

Hsp90s are ATP-dependent chaperones that collaborate with co-chaperones and Hsp70s to
remodel client proteins. Grp94 is the ER Hsp90 homolog essential for folding multiple …