The 90 kDa heat shock proteins (Hsp90) are responsible for the conformational maturation
of nascent polypeptides and the rematuration of denatured proteins. Proteins dependent …

Heat shock protein 90 has emerged as a promising target for the treatment of cancer and
neurodegenerative diseases. This review summarizes recent advancements towards the …

HSP90 is a member of the family of heat shock proteins responsible for folding proteins into
mature conformations and thus maintaining their biological function in cells. Since it is …

The 90 kD heat shock proteins (Hsp90) are molecular chaperones that are responsible for
the folding of select proteins, many of which are directly associated with cancer progression …

Hsp90 has become the target of intensive investigation, as inhibition of its function has the
ability to simultaneously incapacitate proteins that function in pathways that represent the six …

The Hsp90 chaperone is a master regulator of the stability and activity of multiple
oncoproteins such as Her2, Akt, Bcr-Abl, c-Kit, EGFR and mutant BRAF. The promise of …

In the past few decades, the development of heat shock protein 90 (Hsp90) inhibitors for
cancer treatment has not stopped. About twenty compounds have been evaluated in the …

Heat shock protein 90 (Hsp90) is a molecular chaperone whose association is required for
stability and function of multiple mutated, chimeric, and over-expressed signaling proteins …

Heat shock protein (HSP) 90 is the most abundant HSPs, which are chaperone molecules
whose major roles are cell protection and maintenance by means of aiding the folding, the …

Heat shock proteins (HSPs) present as a double edged sword. While they play an important
role in maintaining protein homeostasis in a normal cell, cancer cells have evolved to co-opt …