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Issue 42, 2009
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Inhibition of the histone lysine demethylase JMJD2A by ejection of structural Zn(ii)

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Abstract

JMJD2A, a 2-oxoglutarate dependent Nε-methyl lysine histone demethylase, is inhibited by disruption of its Zn-binding site by Zn-ejecting compounds including disulfiram and ebselen; this observation may enable the development of inhibitors selective for this subfamily of 2OG dependent oxygenases that do not rely on binding to the highly-conserved Fe(II)-containing active site.

Graphical abstract: Inhibition of the histone lysine demethylase JMJD2A by ejection of structural Zn(ii)

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Publication details

The article was received on 10 Aug 2009, accepted on 10 Sep 2009 and first published on 28 Sep 2009


Article type: Communication
DOI: 10.1039/B916357C
Chem. Commun., 2009, 6376-6378

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    Inhibition of the histone lysine demethylase JMJD2A by ejection of structural Zn(II)

    R. Sekirnik, N. R. Rose, A. Thalhammer, P. T. Seden, J. Mecinović and C. J. Schofield, Chem. Commun., 2009, 6376
    DOI: 10.1039/B916357C

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