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William B. Pratt
Researcher at University of Michigan
Publications - 185
Citations - 21933
William B. Pratt is an academic researcher from University of Michigan. The author has contributed to research in topics: Glucocorticoid receptor & Receptor. The author has an hindex of 82, co-authored 184 publications receiving 21378 citations. Previous affiliations of William B. Pratt include Hong Kong University of Science and Technology & Facultad de Ciencias Exactas y Naturales.
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Journal ArticleDOI
Steroid receptor interactions with heat shock protein and immunophilin chaperones.
William B. Pratt,David O. Toft +1 more
TL;DR: A historical perspective on a body of steroid receptor research dealing with the structure and physiological significance of the untransformed 9S receptor is provided, and it is shown that hsp90 itself exists in a variety of native multiprotein heterocomplexes independent of steroid receptors and other 'substrate' proteins.
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Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery.
William B. Pratt,David O. Toft +1 more
TL;DR: This purified system of five purified proteins should facilitate understanding of how eukaryotlc hsp70 and hsp90 work together as essential components of a process that alters the conformations of substrate proteins to states that respond in signal transduction.
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HDAC6 Regulates Hsp90 Acetylation and Chaperone-Dependent Activation of Glucocorticoid Receptor
Jeffrey J. Kovacs,Patrick J. Murphy,Stephanie Gaillard,Xuan Zhao,June-Tai Wu,Christopher V. Nicchitta,Minoru Yoshida,David O. Toft,William B. Pratt,Tso-Pang Yao +9 more
TL;DR: In this article, the deacetylase HDAC6 was shown to be a target of the molecular chaperone heat shock protein 90 (Hsp90) and its accessory cochaperones.
Journal ArticleDOI
The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor
Journal ArticleDOI
Evidence that the 90-kDa phosphoprotein associated with the untransformed L-cell glucocorticoid receptor is a murine heat shock protein.
TL;DR: It is shown that the 90-kDa receptor-associated phosphoprotein is an abundant cytosolic protein that reacts with a monoclonal antibody that recognizes the 90 -kDa phosphop protein that binds steroid receptors in the chicken oviduct.