A Selective Inhibitor and Probe of the Cellular Functions of Jumonji C Domain-Containing Histone Demethylases
Journal of the American Chemical Society2011Vol. 133(24), pp. 9451–9456
Citations Over TimeTop 10% of 2011 papers
Xuelai Luo, Yongxiang Liu, Stefan Kubicek, Johanna Myllyharju, Anthony Tumber, Stanley S. Ng, Ka Hing, Jessica D. Podoll, Tom D. Heightman, Udo Oppermann, Stuart L. Schreiber, Xiang Wang
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.
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