D
David O. Toft
Researcher at University of Rochester
Publications - 23
Citations - 7765
David O. Toft is an academic researcher from University of Rochester. The author has contributed to research in topics: Hsp90 & Chaperone (protein). The author has an hindex of 19, co-authored 23 publications receiving 7493 citations.
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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.
Journal ArticleDOI
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.
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The Amino-terminal Domain of Heat Shock Protein 90 (hsp90) That Binds Geldanamycin Is an ATP/ADP Switch Domain That Regulates hsp90 Conformation
James P. Grenert,William P. Sullivan,Patrick Fadden,Timothy A.J. Haystead,Jenny Clark,Edward G. Mimnaugh,Henry C. Krutzsch,Hans Joachim Ochel,Theodor W. Schulte,Edward A. Sausville,Leonard M. Neckers,David O. Toft +11 more
TL;DR: An amino-terminal domain of hsp90 whose crystal structure has recently been solved and determined to contain a geldanamycin-binding site is studied and it is demonstrated that, in solution, drug binding is exclusive to this domain.
Journal ArticleDOI
The hsp90-related protein TRAP1 is a mitochondrial protein with distinct functional properties.
Sara J. Felts,Barbara A.L. Owen,Phuongmai Nguyen,Jane B. Trepel,David B. Donner,David O. Toft +5 more
TL;DR: TRAP1 has functions that are distinct from those of hsp90, and immunofluorescence data show that human TRAP1 is localized to mitochondria, supported by the existence of mitochondrial localization sequences in the amino termini of both the human and Drosophila proteins.