title: At Long Last Potent and Selective KDM5 Inhibitors.
abstract: Histone lysine demethylase 5 enzymes (KDM5s) have recently been proposed as crucial oncogenic drivers. In this issue of Cell Chemical Biology, Horton et al. (2016) describe results of an extensive structural analysis that reveals how distinct inhibitor chemotypes bind KDM5 and suggest avenues for improving KDM5 inhibitory potency and selectivity.
authors.affiliation: Department of Drug Chemistry and Technologies, Sapienza University of Rome, 00185 Rome, Italy. Electronic address: dante.rotili@uniroma1.it.
authors.forename: Dante
authors.initials: D
authors.lastname: Rotili
authors.affiliation: Department of Biology and Biotechnology, University of Pavia, 27100 Pavia, Italy. Electronic address: andrea.mattevi@unipv.it.
authors.forename: Andrea
authors.initials: A
authors.lastname: Mattevi
mesh_terms: D006657:Histones; D008239:Lysine
chemical_list: D006657:Histones; D008239:Lysine