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 HSP90 paralog TRAP1 was discovered more than 20 years ago; yet, a detailed
understanding of the function of this mitochondrial molecular chaperone remains elusive …

Background The molecular chaperone TRAP1, the mitochondrial isoform of cytosolic
HSP90, remains poorly understood with respect to its pivotal role in the regulation of …

Background The human 90-kDa heat shock protein (HSP90) functions as a dimeric
molecular chaperone. HSP90 identified on the cell surface has been found to play a crucial …

Abstract Background Inhibition of Hsp90 is desirable due to potential downregulation of
oncogenic clients. Early generation inhibitors bind to the N-terminal domain (NTD) but C …

Human heat shock protein of 90 kDa (hHsp90) is a homodimer that has an essential role in
facilitating malignant transformation at the molecular level. Inhibiting hHsp90 function is a …

Hsp90 is an essential chaperone for more than 200 client proteins in eukaryotic cells. The
human genome encodes two highly similar cytosolic Hsp90 proteins called Hsp90α and …

Background The 90 kDa heat shock protein (Hsp90) participates in regulating the
homeostasis of cellular proteins and was considered one of the key chaperones involved in …

Myelin protein zero (MPZ or P0) is a transmembrane protein which functions to glue
membranes in peripheral myelin. Inter-membrane adhesion is mediated by homophilic …

The 90-kDa heat shock protein (Hsp90) is a highly flexible dimer able to self-associate in the
presence of divalent cations or under heat shock. This study investigated the relationship …