Modulation of protein fate decision and protein homeostasis plays a significant role in
altering the protein level, which acts as an orientation to develop drugs with new …

Hsp90 is a conserved molecular chaperone and is responsible for the folding and activation
of several hundred client proteins, involved in various cellular processes. The large number …

Hsp90 is a dimeric molecular chaperone responsible for the folding, maturation, and
activation of hundreds of substrate proteins called 'clients'. Numerous co-chaperone proteins …

Molecular chaperones play a key role in maintaining proteostasis and cellular health. The
abundant, essential, cytosolic Hsp90 (Heat shock protein, 90 kDa) facilitates the folding and …

Hsp90 is a molecular chaperone that acts on its clients through an ATP-dependent and
conformationally dynamic functional cycle. The cochaperone Accelerator of Hsp90 ATPase …

Hsp90 plays an important role in health and is a therapeutic target for managing misfolding
disease. Compounds that disrupt co-chaperone delivery of clients to Hsp90 target a subset …

Hsp90 is a dimeric molecular chaperone that is essential for the folding and activation of
hundreds of client proteins. Co-chaperone proteins regulate the ATP-driven Hsp90 client …

Molecular chaperones are a diverse group of highly conserved proteins that transiently
interact with partially folded polypeptide chains during normal cellular processes such as …

Hsp90 is a conserved molecular chaperone regulating the folding and activation of a diverse
array of several hundreds of client proteins. The function of Hsp90 in client processing is fine …

Most of the fundamental processes of cells are mediated by proteins. However, the
biologically-relevant mechanism of most proteins are poorly understood. Dominant negative …