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The dynamic regulation of lysine methylation patterns is enabled by two distinct groups of enzymes: histone methyltransferases (KMTs) and demethylases (KDMs). The Jumonji C (JmjC) domain\u2013containing lysine histone demethylases (JmjC\u2010KDMs) alter the methylation levels of histone tails by removing tri\u2010, di\u2010, or mono\u2010methylation marks. Because JmjC\u2010KDMs activities are dysfunctional in cancer and other clinical conditions, they are targets for drug discovery. Efforts are underway to develop high\u2010throughput assays capable of identifying selective, small\u2010molecule inhibitors of KDMs. Detailed in this unit are protocols for mass spectrometry\u2013based and formaldehyde dehydrogenase\u2013coupled enzyme\u2010based assays that can be used to identify inhibitors of JmjC\u2010KDMs. \u00a9 2018 by John Wiley &amp; Sons, Inc.<\/jats:p>","DOI":"10.1002\/cpph.34","type":"journal-article","created":{"date-parts":[[2018,4,6]],"date-time":"2018-04-06T14:50:11Z","timestamp":1523026211000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["In Vitro Enzyme Assays for JmjC\u2010Domain\u2010Containing Lysine Histone Demethylases (JmjC\u2010KDMs)"],"prefix":"10.1002","volume":"80","author":[{"given":"Hanna","family":"Tarhonskaya","sequence":"first","affiliation":[{"name":"Chemistry Research Laboratory, Department of Chemistry, University of Oxford  Oxford United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anthony","family":"Tumber","sequence":"additional","affiliation":[{"name":"Chemistry Research Laboratory, Department of Chemistry, University of Oxford  Oxford United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Akane","family":"Kawamura","sequence":"additional","affiliation":[{"name":"Chemistry Research Laboratory, Department of Chemistry, University of Oxford  Oxford United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christopher J.","family":"Schofield","sequence":"additional","affiliation":[{"name":"Chemistry Research Laboratory, Department of Chemistry, University of Oxford  Oxford United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2018,4,2]]},"reference":[{"key":"e_1_2_8_2_1","volume-title":"Applications of MALDI\u2010TOF spectroscopy","author":"Asakawa D.","year":"2013"},{"key":"e_1_2_8_3_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0704525104"},{"key":"e_1_2_8_4_1","doi-asserted-by":"publisher","DOI":"10.1038\/embor.2011.43"},{"key":"e_1_2_8_5_1","doi-asserted-by":"publisher","DOI":"10.1101\/gad.1652908"},{"key":"e_1_2_8_6_1","first-page":"1","article-title":"Evaluation of enzyme inhibitors in drug discovery. 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