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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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A Screen for Modulators of Large T Antigen's ATPase Activity Uncovers Novel Inhibitors of Simian Virus 40 and BK Virus Replication

TL;DR: In this paper, small molecule inhibitors of the essential ATPase activity of TAg would inhibit viral replication, and two FDA approved compounds, bithionol and hexachlorophene, were identified as the most potent TAg inhibitors known to date.
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The pleiotropic effects of TNFα in breast cancer subtypes is regulated by TNFAIP3/A20.

TL;DR: It is shown that TNFα contributes to the aggressive properties of triple negative breast cancer (TNBC) cell lines via upregulation of TNFAIP3(A20) and A20 overexpression in luminal breast cancer cells induces aggressive metastatic properties in mouse xenografts via generating a permissive inflammatory microenvironment constituted by granulocytic-MDSCs.
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Heme-dependent activation of neuronal nitric oxide synthase by cytosol is due to an Hsp70-dependent, thioredoxin-mediated thiol-disulfide interchange in the heme/substrate binding cleft.

TL;DR: A model in which Hsp70 binding to apo-nNOS stabilizes an open state of the heme/substrate binding cleft to facilitate thioredoxin access to the active site cysteine that coordinates with heme iron, permitting heme binding and dimerization to theactive enzyme is supported.
Posted ContentDOI

Hsp70 chaperone blocks α-synuclein oligomer formation via a novel engagement mechanism

TL;DR: The findings suggest that new chemical approaches will be required to target Hsp70-ASyn interaction in synucleinopathies, and raise the question of whether other misfolded proteins might also engage via the same non-canonical mechanism.