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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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Steroid receptor interactions with heat shock protein and immunophilin chaperones.

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.

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

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

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.
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The hsp90-related protein TRAP1 is a mitochondrial protein with distinct functional properties.

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.