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    A fluopol-ABPP HTS assay to identify PAD inhibitors

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    Authors
    Knuckley, Bryan
    Jones, Justin E.
    Bachovchin, Daniel A.
    Slack, Jessica
    Causey, Corey P.
    Brown, Steven J.
    Rosen, Hugh
    Cravatt, Benjamin F.
    Thompson, Paul R
    UMass Chan Affiliations
    Department of Biochemistry and Molecular Pharmacology
    Document Type
    Journal Article
    Publication Date
    2010-10-14
    Keywords
    Arthritis, Rheumatoid
    Cell Line, Tumor
    Drug Evaluation, Preclinical
    Enzyme Inhibitors
    Fluorescence Polarization
    Fluorescent Dyes
    High-Throughput Screening Assays
    Humans
    Hydrolases
    Inhibitory Concentration 50
    Streptonigrin
    Biochemistry
    Enzymes and Coenzymes
    Medicinal-Pharmaceutical Chemistry
    Therapeutics
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    Link to Full Text
    http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2943038/
    Abstract
    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.
    Source
    Chem Commun (Camb). 2010 Oct 14;46(38):7175-7. doi: 10.1039/c0cc02634d. Link to article on publisher's site. Epub 2010 Aug 25.
    DOI
    10.1039/c0cc02634d
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/50049
    Notes

    At the time of publication, Paul Thompson was not yet affiliated with UMass Medical School.

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    Link to Article in PubMed
    ae974a485f413a2113503eed53cd6c53
    10.1039/c0cc02634d
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