Selective inhibitors of the JMJD2 histone demethylases: combined nondenaturing mass spectrometric screening and crystallographic approaches.

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 combin...

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Бібліографічні деталі
Автори:	Rose, N, Woon, E, Kingham, G, King, O, Mecinović, J, Clifton, I, Ng, S, Talib-Hardy, J, Oppermann, U, McDonough, M, Schofield, C
Формат:	Journal article
Мова:	English
Опубліковано:	2010
Предмети:	Binding, Competitive Spectrometry, Mass, Electrospray Ionization Binding Sites analogs and derivatives chemistry Tyrosine Structure-Activity Relationship Crystallography, X-Ray chemical synthesis Models, Molecular Combinatorial Chemistry Techniques Oxalic Acids antagonists and inhibitors Jumonji Domain-Containing Histone Demethylases Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Selective inhibitors of the JMJD2 histone demethylases: combined nondenaturing mass spectrometric screening and crystallographic approaches.

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