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The dynamic methylation of histone lysyl residues plays an important role in biology by regulating transcription, maintaining genomic integrity, and by contributing to epigenetic effects. Here we describe a variety of inhibitor scaffolds that inhibit the human 2-oxoglutarate-dependent JMJD2 subfamily of histone demethylases. Combined with structural data, these chemical starting points will be useful to generate small-molecule probes to analyze the physiological roles of these enzymes in epigenetic signaling.

Original publication

DOI

10.1021/jm800936s

Type

Journal article

Journal

J Med Chem

Publication Date

27/11/2008

Volume

51

Pages

7053 - 7056

Keywords

Crystallography, X-Ray, Dose-Response Relationship, Drug, Enzyme Inhibitors, Humans, Ketoglutaric Acids, Models, Molecular, Molecular Structure, Oxidoreductases, N-Demethylating, Protein Structure, Tertiary, Stereoisomerism, Structure-Activity Relationship