Review paper
Hsp90: Friends, clients and natural foes
Abstract
Hsp90, a homodimeric ATPase, is responsible for the correct folding of a number of newly synthesized polypeptides in addition to the correct folding of denatured/misfolded client proteins. It requires several co-chaperones and other partner proteins for chaperone activity. Due to the involvement of Hsp90-dependent client proteins in a variety of oncogenic signaling pathways, Hsp90 inhibition has emerged as one of the leading strategies for...
Paper Details
Title
Hsp90: Friends, clients and natural foes
Published Date
Aug 1, 2016
Journal
Volume
127
Pages
227 - 240
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