William B. Pratt

Steroid Receptor Interactions with Heat Shock Protein and Immunophilin Chaperones*

Regulation of Signaling Protein Function and Trafficking by the hsp90/hsp70-Based Chaperone Machinery

HDAC6 Regulates Hsp90 Acetylation and Chaperone-Dependent Activation of Glucocorticoid Receptor

The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor.

Steroid Receptor Interactions with Heat Shock Protein and Immunophilin Chaperones

Evidence that the 90-kDa phosphoprotein associated with the untransformed L-cell glucocorticoid receptor is a murine heat shock protein.

The hsp90-based Chaperone System: Involvement in Signal Transduction from a Variety of Hormone and Growth Factor Receptors

Evidence That the 90-kDa Heat Shock Protein Is Necessary for the Steroid Binding Conformation of the L Cell Glucocorticoid Receptor

Molybdate inhibition of glucocorticoid receptor inactivation and transformation.

THE ROLE OF THEhsp90-BASED CHAPERONE SYSTEM IN SIGNAL TRANSDUCTION BY NUCLEAR RECEPTORS AND RECEPTORS SIGNALING VIA MAP KINASE

Evidence that the endogenous heat-stable glucocorticoid receptor-activating factor is thioredoxin.

Raf exists in a native heterocomplex with hsp90 and p50 that can be reconstituted in a cell-free system.