@article{
 title = {Recent Progress in Histone Demethylase Inhibitors},
 type = {article},
 year = {2016},
 keywords = {Amino Acid Sequence,Animals,Drug Discovery,Enzyme Inhibitors,Histone Demethylases,Humans,Models, Molecular,Molecular Sequence Data,Peptides,Small Molecule Libraries},
 pages = {1308-1329},
 volume = {59},
 month = {2},
 id = {187a85c8-5970-363b-beaa-7b269952aca5},
 created = {2016-12-01T10:12:01.000Z},
 file_attached = {false},
 profile_id = {64f7fb50-d000-335d-a02d-06c5f340a97a},
 last_modified = {2018-07-09T12:39:50.287Z},
 read = {false},
 starred = {false},
 authored = {true},
 confirmed = {true},
 hidden = {false},
 citation_key = {McAllister2016},
 source_type = {JOUR},
 private_publication = {false},
 abstract = {There is increasing interest in targeting histone N-methyl-lysine demethylases (KDM) 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.},
 bibtype = {article},
 author = {McAllister, Tom E. and England, Katherine S. and Hopkinson, Richard J. and Brennan, Paul E. and Kawamura, Akane and Schofield, Christopher J.},
 doi = {10.1021/acs.jmedchem.5b01758},
 journal = {Journal of Medicinal Chemistry},
 number = {4}
}

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