Inhibition of the histone lysine demethylase JMJD2A by ejection of structural Zn(ii)
Chemical Communications2009Iss. 42, pp. 6376–6376
Citations Over TimeTop 10% of 2009 papers
Rok Sekirnik, Nathan R. Rose, Armin Thalhammer, Peter Seden, Jasmin Mecinović, Christopher J. Schofield
Abstract
JMJD2A, a 2-oxoglutarate dependent N(epsilon)-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.
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