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Issue 12, 2014
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Optimisation of a triazolopyridine based histone demethylase inhibitor yields a potent and selective KDM2A (FBXL11) inhibitor

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Abstract

A potent inhibitor of the JmjC histone lysine demethylase KDM2A (compound 35, pIC50 7.2) with excellent selectivity over representatives from other KDM subfamilies has been developed; the discovery that a triazolopyridine compound binds to the active site of JmjC KDMs was followed by optimisation of the triazole substituent for KDM2A inhibition and selectivity.

Graphical abstract: Optimisation of a triazolopyridine based histone demethylase inhibitor yields a potent and selective KDM2A (FBXL11) inhibitor

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Publication details

The article was received on 04 Jul 2014, accepted on 14 Sep 2014 and first published on 15 Sep 2014


Article type: Concise Article
DOI: 10.1039/C4MD00291A
Citation: Med. Chem. Commun., 2014,5, 1879-1886
  • Open access: Creative Commons BY license
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    Optimisation of a triazolopyridine based histone demethylase inhibitor yields a potent and selective KDM2A (FBXL11) inhibitor

    K. S. England, A. Tumber, T. Krojer, G. Scozzafava, S. S. Ng, M. Daniel, A. Szykowska, K. Che, F. von Delft, N. A. Burgess-Brown, A. Kawamura, C. J. Schofield and P. E. Brennan, Med. Chem. Commun., 2014, 5, 1879
    DOI: 10.1039/C4MD00291A

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