- A selective inhibitor and probe of the cellular functions of Jumonji C domain-containing histone demethylases.
A selective inhibitor and probe of the cellular functions of Jumonji C domain-containing histone demethylases.
Journal of the American Chemical Society (2011-05-19)
Xuelai Luo, Yongxiang Liu, Stefan Kubicek, Johanna Myllyharju, Anthony Tumber, Stanley Ng, Ka Hing Che, Jessica Podoll, Tom D Heightman, Udo Oppermann, Stuart L Schreiber, Xiang Wang
PMID21585201
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.
MATERIALS
Product Number
Brand
Product Description
Sigma-Aldrich
JMJD Histone Demethylase Inhibitor III, The JMJD Histone Demethylase Inhibitor III controls the biological activity of JMJD Histone Demethylase. This small molecule/inhibitor is primarily used for Cell Structure applications.