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

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 …

Heat shock proteins 90 (Hsp90) and 70 (Hsp70) are two families of highly conserved ATP-
dependent molecular chaperones that fold and remodel proteins. Both are important …

The accumulation of misfolded proteins in the human brain is one of the critical features of
many neurodegenerative diseases, including Alzheimer's disease (AD). Assembles of beta …

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 …

The biological functions of proteins are governed by their three-dimensional fold. Protein
folding, maintenance of proteome integrity, and protein homeostasis (proteostasis) critically …

Chaperones are abundant cellular proteins that promote the folding and function of their
substrate proteins (clients). In vivo, chaperones also associate with a large and diverse set …

The glucocorticoid receptor (GR), like many signaling proteins, depends on the Hsp90
molecular chaperone for in vivo function. Although Hsp90 is required for ligand binding in …

Protein–protein interactions (PPIs) control the assembly of multi-protein complexes and,
thus, these contacts have enormous potential as drug targets. However, the field has …