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Jason E. Gestwicki

Researcher at University of California, San Francisco

Publications -  280
Citations -  27231

Jason E. Gestwicki is an academic researcher from University of California, San Francisco. The author has contributed to research in topics: Chaperone (protein) & Heat shock protein. The author has an hindex of 69, co-authored 250 publications receiving 23446 citations. Previous affiliations of Jason E. Gestwicki include Research Triangle Park & Stanford University.

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The structure of an Hsp90-immunophilin complex reveals cochaperone recognition of the client maturation state

TL;DR: In this article, the authors determined the structure of the human Hsp90:FKBP51:p23 complex to 3.3 A using a cryoelectron microscopy (cryo-EM) method.
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Anticancer Effects of Targeting Hsp70 in Tumor Stromal Cells.

TL;DR: The results illustrate how Hsp70 inhibitors mediate the anticancer effects by targeting both tumor cells and tumor stromal cells, with implications for the broad use of these inhibitors as tools to ablate tumor-associated macrophages that enable malignant progression.
Posted ContentDOI

Three Essential Resources to Improve Differential Scanning Fluorimetry (DSF) Experiments

TL;DR: This work aims to reconcile these disparate reputations of DSF and help users perform more successful DSF experiments with three resources: an updated, interactive theoretical framework, practical tips, and online data analysis.
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Development of a capillary electrophoresis platform for identifying inhibitors of protein-protein interactions.

TL;DR: Capillary electrophoresis has been evaluated as a method to screen for PPI inhibitors using the challenging system of Hsp70 interacting with its co-chaperone Bag3, and it is attractive as a secondary screen to test hits found by higher-throughput methods.
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The active Hsc70/tau complex can be exploited to enhance tau turnover without damaging microtubule dynamics

TL;DR: It is found for the first time that Hsc70 activity is required to stimulate MT assembly in cells and brain, and it is shown that in tauopathies, where MT injury would be detrimental to neurons, the unique relationship of tau with the Hsp70 machinery can be exploited to deplete tau levels without damaging MT networks.