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 …

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 …

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

Efficient S phase entry is essential for development, tissue repair, and immune defences.
However, hyperactive or expedited S phase entry causes replication stress, DNA damage …

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 …

Abstract Knowledge of the three-dimensional structures of proteins and other biological
macromolecules often aids understanding of how they perform complicated tasks in the cell …

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 …

Conserved families of molecular chaperones assist protein folding in the cell. Here we
review the conceptual advances on three major folding routes:(i) spontaneous, chaperone …