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

Cells respond to protein-damaging (proteotoxic) stress by activation of the Heat Shock
Response (HSR). The HSR provides cells with an enhanced ability to endure proteotoxic …

Maintaining a healthy proteome is fundamental for the survival of all organisms. Integral to
this are Hsp90 and Hsp70, molecular chaperones that together facilitate the folding …

The aryl hydrocarbon receptor (AHR) is a ligand-dependent transcription factor that
mediates a broad spectrum of (patho) physiological processes in response to numerous …

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 …

The co-chaperone p23 is a central part of the Hsp90 machinery. It stabilizes the closed
conformation of Hsp90, inhibits its ATPase and is important for client maturation. Yet, how …

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 …

Hsp90 (Heat Shock Protein 90) is an ATP (Adenosine triphosphate) molecular chaperone
responsible for the activation and maturation of client proteins. The mechanism by which …