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Histone methylations are important chromatin marks that regulate gene expression, genomic stability, DNA repair, and genomic imprinting. Histone demethylases are the most recent family of histone-modifying enzymes discovered. Here, we report the characterization of a small-molecule inhibitor of Jumonji C domain-containing histone demethylases. The inhibitor derives from a structure-based design and preferentially inhibits the subfamily of trimethyl lysine demethylases. Its methyl ester prodrug, methylstat, selectively inhibits Jumonji C domain-containing his-tone demethylases in cells and may be a useful small-molecule probe of chromatin and its role in epigenetics.

Original publication

DOI

10.1021/ja201597b

Type

Journal article

Journal

Journal of the American Chemical Society

Publication Date

06/2011

Volume

133

Pages

9451 - 9456

Addresses

Department of Chemistry and Biochemistry, University of Colorado, Boulder, Colorado 80309, USA.

Keywords

Cell Line, Tumor, Humans, Esters, Nuclear Proteins, Prodrugs, Enzyme Inhibitors, Inhibitory Concentration 50, Substrate Specificity, Muscle Development, Drug Design, Histone Demethylases, Jumonji Domain-Containing Histone Demethylases