Selective inhibitors of the JMJD2 histone demethylases: combined nondenaturing mass spectrometric screening and crystallographic approaches.
|Abstract||Ferrous ion and 2-oxoglutarate (2OG) oxygenases catalyze the demethylation of N(epsilon)-methylated lysine residues in histones. Here we report studies on the inhibition of the JMJD2 subfamily of histone demethylases, employing binding analyses by nondenaturing mass spectrometry (MS), dynamic combinatorial chemistry coupled to MS, turnover assays, and crystallography. The results of initial binding and inhibition assays directed the production an ... [truncated at 450 characters in length]|
|Author||Rose, Nathan R; Woon, Esther C Y; Kingham, Guy L; et al|
|Subject||Binding Sites Binding, Competitive Combinatorial Chemistry Techniques Crystallography, X-Ray Humans Jumonji Domain-Containing Histone Demethylases Models, Molecular Oxalic Acids Spectrometry, Mass, Electrospray Ionization Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Structure-Activity Relationship Tyrosine antagonists and inhibitors chemistry chemical synthesis chemistry analogs and derivatives chemical synthesis chemistry|