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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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Derrubone, an inhibitor of the Hsp90 protein folding machinery.

TL;DR: High-throughput screening of a library of diverse molecules has identified derrubone, an isoflavone natural product from Derris robusta, as a potent Hsp90 inhibitor, and subsequently testing in several cellular-based assays established 1 as a low micromolar inhibitor in vitro.
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Visualization of Single Multivalent Receptor–Ligand Complexes by Transmission Electron Microscopy

TL;DR: A method that increased the contrast of receptors would allow visualization of receptors bound to a given ligand and facilitate the characterization of individual small receptor ± ligand complexes is reasoned.
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Genomic Heat Shock Element Sequences Drive Cooperative Human Heat Shock Factor 1 DNA Binding and Selectivity

TL;DR: A role for specific orientations of extended HSE sequences in driving preferential HSF1 DNA binding to target loci in vivo is demonstrated, providing a biochemical basis for understanding differential HSF 1 target gene recognition and transcription in neurodegenerative disease and in cancer.
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Erratum to: Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition) (Autophagy, 12, 1, 1-222, 10.1080/15548627.2015.1100356

Daniel J. Klionsky, +2522 more
- 01 Jan 2016 - 
TL;DR: Author(s): Klionsky, DJ; Abdelmohsen, K; Abe, A; Abedin, MJ; Abeliovich, H; A Frozena, AA; Adachi, H, Adeli, K, Adhihetty, PJ; Adler, SG; Agam, G; Agarwal, R; Aghi, MK; Agnello, M; Agostinis, P; Aguilar, PV; Aguirre-Ghis
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Stabilizing the Hsp70-Tau Complex Promotes Turnover in Models of Tauopathy.

TL;DR: This approach revealed that tight complexes between Hsp70 and tau were associated with enhanced turnover while transient interactions favored tau retention, suggesting that client affinity is one important parameter governing HSp70-mediated quality control.