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A selective inhibitor and probe of the cellular functions of Jumonji C domain-containing histone demethylases.
|Publication Type||Journal Article|
|Authors||Luo, X., Liu Y., Kubicek S., Myllyharju J., Tumber A., Ng S., Che KH, Podoll J., Heightman TD, Oppermann U., Schreiber SL, and Wang X.|
|Abstract||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.|
|Year of Publication||2011|
|Journal||Journal of the American Chemical Society|
|Date Published (YYYY/MM/DD)||2011/06/22|