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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

Journal of medicinal chemistry

Publication Date

11/2008

Volume

51

Pages

7053 - 7056

Addresses

The Department of Chemistry and the Oxford Centre for Integrative Systems Biology, Chemistry Research Laboratory, University of Oxford, 12 Mansfield Road, Oxford, OX1 3TA, United Kingdom.

Keywords

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