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Updated: Jun 19, 2026

Assays for Validating Histone Acetyltransferase Inhibitors
Published on: August 6, 2020
Inhibition of the histone lysine demethylase JMJD2A by ejection of structural Zn(II)
Rok Sekirnik1, Nathan R Rose, Armin Thalhammer
1Department of Chemistry and the Oxford Centre for Integrative Systems Biology, Chemistry Research Laboratory, University of Oxford, 12 Mansfield Road, Oxford, UK OX1 3TA.
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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