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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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Binding of a small molecule at a protein-protein interface regulates the chaperone activity of hsp70-hsp40.

TL;DR: Interestingly, it is found that 115-7c and the Hsp40 do not compete for binding but act in concert, and these chemical probes either promote or inhibit chaperone functions by regulating Hsp70-Hsp40 complex assembly at a native protein-protein interface.
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Insight into Amyloid Structure Using Chemical Probes

TL;DR: How chemical probes, such as Congo red, thioflavin T and their derivatives, have been powerful tools for the better understanding of amyloid structure and function are reviewed and how design and deployment of conformationally selective probes might be used to test emerging models of AD are discussed.
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Conditional protein alleles using knockin mice and a chemical inducer of dimerization

TL;DR: A general method of making conditional alleles that allows the rapid and reversible regulation of specific proteins and may be applied to a wide range of FRB*-tagged mouse genes while retaining their native transcriptional control.
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Hsp70-Bag3 interactions regulate cancer-related signaling networks

TL;DR: It is established that the Hsp70-Bag3 module is a broad-acting regulator of cancer cell signaling by modulating the activity of the transcription factors NF-κB, FoxM1, Hif1α, the translation regulator HuR, and the cell-cycle regulators p21 and survivin.
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High-throughput screen for small molecules that modulate the ATPase activity of the molecular chaperone DnaK.

TL;DR: A robust, colorimetric, high-throughput screening (HTS) method in 96-well plates that reports on the ATPase activity of DnaK and uncovered seven new inhibitors that will likely accelerate discovery of small molecules that modulate DnK/Hsp70 function.