Recent Progress in Histone Demethylase Inhibitors

J Med Chem. 2016 Feb 25;59(4):1308-29. doi: 10.1021/acs.jmedchem.5b01758.

Tom E McAllister ¹ ², Katherine S England ³ ⁴, Richard J Hopkinson ¹, Paul E Brennan ³ ⁴, Akane Kawamura ¹ ², Christopher J Schofield ¹

Affiliations

1 Chemistry Research Laboratory, University of Oxford , 12 Mansfield Road, Oxford, OX1 3TA, U.K.
2 Division of Cardiovascular Medicine, Radcliffe Department of Medicine, University of Oxford , Old Road Campus, Roosevelt Drive, Headington, OX3 7BN, U.K.
3 Structural Genomics Consortium, University of Oxford , Old Road Campus, Roosevelt Drive, Headington, OX3 7DQ, U.K.
4 Target Discovery Institute, University of Oxford , NDM Research Building, Roosevelt Drive, Headington, OX3 7FZ, U.K.

PMID: 26710088 DOI: 10.1021/acs.jmedchem.5b01758

Abstract

There is increasing interest in targeting histone N-methyl-lysine demethylases (KDMs) with small molecules both for the generation of probes for target exploration and for therapeutic purposes. Here we update on previous reviews on the inhibition of the lysine-specific demethylases (LSDs or KDM1s) and JmjC families of N-methyl-lysine demethylases (JmjC KDMs, KDM2-7), focusing on the academic and patent literature from 2014 to date. We also highlight recent biochemical, biological, and structural studies which are relevant to KDM inhibitor development.

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