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 …

The heat shock protein (Hsp) 90 chaperone machinery regulates the activity of hundreds of
client proteins in the eukaryotic cytosol. It undergoes large conformational changes between …

Hsp90 chaperones receive much attention due to their role in cancer and other pathological
conditions, and a tremendous effort of many laboratories has contributed in the past …

The expression of correctly folded and functional heterologous proteins is important in many
biotechnological production processes, whether it is enzymes, biopharmaceuticals or …

Heat shock protein 90 (Hsp90) is a molecular chaperone that folds and remodels proteins,
thereby regulating the activity of numerous substrate proteins. Hsp90 is widely conserved …

To be able to perform their biological function, a protein needs to be correctly folded into its
three dimensional structure. The protein folding process is spontaneous and does not …

Hsp90 is a homodimeric ATP-dependent molecular chaperone that remodels its substrate
'client'proteins, facilitating their folding and activating them for biological function. Despite …

In living organisms, most proteins work in complexes to form multicomponent protein
machines. The function of such multicomponent machines is usually addressed by dividing …

Abstract Heat shock protein 90 (Hsp90) is a molecular chaperone that facilitates the
maturation of its client proteins including protein kinases, transcription factors, and steroid …