Article
Client Proteins and Small Molecule Inhibitors Display Distinct Binding Preferences for Constitutive and Stress-Induced HSP90 Isoforms and Their Conformationally Restricted Mutants.
PloS one - 1 Jan 2015
Prince Thomas L, Kijima Toshiki, Tatokoro Manabu, Lee Sunmin, Tsutsumi Shinji, Yim Kendrick, Rivas Candy, Alarcon Sylvia, Schwartz Harvey, Khamit-Kush Kofi, Scroggins Bradley T, Beebe Kristin, Trepel Jane B, Neckers Len
Abstract excerpt
The two cytosolic/nuclear isoforms of the molecular chaperone HSP90, stress-inducible HSP90α and constitutively expressed HSP90β, fold, assemble and maintain the three-dimensional structure of numerous client proteins. Because many HSP90 clients are important in cancer, several HSP90 inhibitors have been evaluated in the clinic. However, little is known concerning possible unique isoform or conformational...
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