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...

Täydet tiedot

Bibliografiset tiedot
Päätekijät:	Rose, N, Woon, E, Kingham, G, King, O, Mecinović, J, Clifton, I, Ng, S, Talib-Hardy, J, Oppermann, U, McDonough, M, Schofield, C
Aineistotyyppi:	Journal article
Kieli:	English
Julkaistu:	2010
Aiheet:	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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