D
Dustin J. Maly
Researcher at University of Washington
Publications - 143
Citations - 5205
Dustin J. Maly is an academic researcher from University of Washington. The author has contributed to research in topics: Kinase & Proto-oncogene tyrosine-protein kinase Src. The author has an hindex of 39, co-authored 134 publications receiving 4528 citations. Previous affiliations of Dustin J. Maly include University of California & University of California, Berkeley.
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Journal ArticleDOI
Allosteric Inhibition of the IRE1α RNase Preserves Cell Viability and Function during Endoplasmic Reticulum Stress
Rajarshi Ghosh,Likun Wang,Eric S. Wang,B. Gayani K. Perera,Aeid Igbaria,Shuhei Morita,Kris Prado,Maike Thamsen,Deborah Caswell,Hector Macias,Kurt F. Weiberth,Micah J. Gliedt,Marcel V. Alavi,Sanjay B. Hari,Arinjay K. Mitra,Barun Bhhatarai,Stephan C. Schürer,Erik L. Snapp,Douglas B. Gould,Michael S. German,Bradley J. Backes,Dustin J. Maly,Scott A. Oakes,Feroz R. Papa +23 more
TL;DR: An ATP-competitive IRE1α Kinase-Inhibiting RNase Attenuators-KIRAs-that allosterically inhibit IRE 1α's RNase by breaking oligomers are developed that powerfully controls cell fate but can itself be controlled with small molecules to reduce cell degeneration.
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Peptide Microarrays for the Determination of Protease Substrate Specificity
TL;DR: The utility of these arrays is demonstrated by the selective cleavage of preferred substrates with trypsin, thrombin, and granzyme B, and by assessing the extended substrate specificity ofThrombin using a microarray of 361 different peptidyl coumarin substrates.
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Combinatorial target-guided ligand assembly: Identification of potent subtype-selective c-Src inhibitors
TL;DR: The utility of the combinatorial method was demonstrated by the identification of a potent and subtype-selective small molecule inhibitor of the non-receptor tyrosine kinase c-Src (IC(50) = 64 nM).
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Druggable sensors of the unfolded protein response
Dustin J. Maly,Feroz R. Papa +1 more
TL;DR: The state of the UPR field is summarized with emphasis placed on two of the master UPR regulators, PERK and IRE1, which are both capable of being drugged with small molecules.
Journal ArticleDOI
Divergent allosteric control of the IRE1α endoribonuclease using kinase inhibitors
Likun Wang,B. Gayani K. Perera,Sanjay B. Hari,Barun Bhhatarai,Bradley J. Backes,Markus A. Seeliger,Stephan C. Schürer,Scott A. Oakes,Feroz R. Papa,Dustin J. Maly +9 more
TL;DR: It is shown that IRE1α’s kinase-controlled RNase can be regulated in two distinct modes with kinase inhibitors: one class of ligands occupied by distinct classes of ATP-competitive inhibitors can cause allosteric switching of IRE 1α”s RNase—either on or off.