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    Activity-based protein profiling of protein arginine methyltransferase 1

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    Authors
    Obianyo, Obiamaka
    Causey, Corey P.
    Jones, Justin E.
    Thompson, Paul R
    UMass Chan Affiliations
    Department of Biochemistry and Molecular Pharmacology
    Document Type
    Journal Article
    Publication Date
    2011-10-21
    Keywords
    Breast Neoplasms
    Cell Line, Tumor
    *Drug Design
    Enzyme Inhibitors
    Female
    Humans
    Inhibitory Concentration 50
    Protein-Arginine N-Methyltransferases
    Repressor Proteins
    Biochemistry
    Enzymes and Coenzymes
    Medicinal-Pharmaceutical Chemistry
    Therapeutics
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    Link to Full Text
    http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3199286/
    Abstract
    The protein arginine methyltransferases (PRMTs) are SAM-dependent enzymes that catalyze the mono- and dimethylation of peptidyl arginine residues. PRMT1 is the founding member of the PRMT family, and this isozyme is responsible for methylating approximately 85% of the arginine residues in mammalian cells. Additionally, PRMT1 activity is aberrantly upregulated in heart disease and cancer. As a part of a program to develop isozyme-specific PRMT inhibitors, we recently described the design and synthesis of C21, a chloroacetamidine bearing histone H4 tail analogue that acts as an irreversible PRMT1 inhibitor. Given the covalent nature of the interaction, we set out to develop activity-based probes (ABPs) that could be used to characterize the physiological roles of PRMT1. Herein, we report the design, synthesis, and characterization of fluorescein-conjugated C21 (F-C21) and biotin-conjugated C21 (B-C21) as PRMT1-specific ABPs. Additionally, we provide the first evidence that PRMT1 activity is negatively regulated in a spatial and temporal fashion.
    Source
    ACS Chem Biol. 2011 Oct 21;6(10):1127-35. doi: 10.1021/cb2001473. Epub 2011 Aug 23. Link to article on publisher's site
    DOI
    10.1021/cb2001473
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/50034
    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
    10.1021/cb2001473
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