Inhibition of the histone lysine demethylase JMJD2A by ejection of structural Zn(ii). Chemical communications (Cambridge, England) [Chem Commun (Camb)] Journal article | | Title | Inhibition of the histone lysine demethylase JMJD2A by ejection of structural Zn(ii). | | Author(s) | Sekirnik R, Rose NR, Thalhammer A, Seden PT, Mecinović J, Schofield CJ | | Institution | Department of Chemistry and the Oxford Centre for Integrative Systems Biology, Chemistry Research Laboratory, University of Oxford, 12 Mansfield Road, Oxford, UKOX1 3TA. Christopher.schofield@chem.ox.ac.uk. | | Source | Chem Commun (Camb) 2009 Nov 14; (42):6376-8. | | 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. | | Language | eng | | Pub Type(s) | Journal Article
| | PubMed ID | 19841782 |
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