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Issue 6, 2016
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Histone demethylating agents as potential S-adenosyl-l-methionine-competitors

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Histone H3 methylation on K9 and/or K27 depends on histone lysine methyltransferases (KMTs). EZH2, one of the components of the PRC2 complex, catalyzes the trimethylation of histone H3K27, which is associated with transcriptional repression and tumor development. H3K9me3 mediated gene silencing may result from other KDMs such as G9a/GLP, SUV39H1-2, SETDB1, CCLD8 and RIZ1. Their disturbance leads to defective cell mitosis. It is therefore desirable to find small molecules that are able to decrease H3K9 and K27 tagging to reinitiate gene transcription. Most KDM inhibitors are still based on SAM co-factor competition/modulation. Herein, functional screening of a diversity library proved to be a useful tool for finding new specific KDM inhibitors; the use of SAM-based pharmacophoric models facilitated the understanding of their possible mechanism of action.

Graphical abstract: Histone demethylating agents as potential S-adenosyl-l-methionine-competitors

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The article was received on 23 Mar 2016, accepted on 04 May 2016 and first published on 20 May 2016

Article type: Research Article
DOI: 10.1039/C6MD00170J
Med. Chem. Commun., 2016,7, 1245-1255

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    Histone demethylating agents as potential S-adenosyl-L-methionine-competitors

    R. Navakauskienė, M. Mori, M. S. Christodoulou, A. Zentelytė, B. Botta, L. D. Via, F. Ricci, G. Damia, D. Passarella, C. Zilio and N. Martinet, Med. Chem. Commun., 2016, 7, 1245
    DOI: 10.1039/C6MD00170J

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