Knuckley, BryanJones, Justin E.Bachovchin, Daniel A.Slack, JessicaCausey, Corey P.Brown, Steven J.Rosen, HughCravatt, Benjamin F.Thompson, Paul R2022-08-232022-08-232010-10-142015-05-27Chem Commun (Camb). 2010 Oct 14;46(38):7175-7. doi: 10.1039/c0cc02634d. <a href="http://dx.doi.org/10.1039/c0cc02634d">Link to article on publisher's site</a>. Epub 2010 Aug 25.1359-7345 (Linking)10.1039/c0cc02634dhttps://hdl.handle.net/20.500.14038/50049<p>At the time of publication, Paul Thompson was not yet affiliated with UMass Medical School.</p>Protein Arginine Deiminase (PAD) activity is dysregulated in numerous diseases, e.g., Rheumatoid Arthritis. Herein we describe the development of a fluorescence polarization-Activity Based Protein Profiling (fluopol-ABPP) based high throughput screening assay that can be used to identify PAD-selective inhibitors. Using this assay, streptonigrin was identified as a potent, selective, and irreversible PAD4 inactivator.en-USArthritis, RheumatoidCell Line, TumorDrug Evaluation, PreclinicalEnzyme InhibitorsFluorescence PolarizationFluorescent DyesHigh-Throughput Screening AssaysHumansHydrolasesInhibitory Concentration 50StreptonigrinBiochemistryEnzymes and CoenzymesMedicinal-Pharmaceutical ChemistryTherapeuticsJournal Articlehttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1056&amp;context=thompson&amp;unstamped=1https://escholarship.umassmed.edu/thompson/577144791thompson/57