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

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.
Publication status:
Published

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Publisher copy:
10.1039/b916357c

Authors


Sekirnik, R More by this author
Thalhammer, A More by this author
Mecinović, J More by this author
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Journal:
Chemical communications (Cambridge, England)
Issue:
42
Pages:
6376-6378
Publication date:
2009-11-05
DOI:
EISSN:
1364-548X
ISSN:
1359-7345
URN:
uuid:52cecd68-b065-4b34-a5f7-29e78395044d
Source identifiers:
34940
Local pid:
pubs:34940

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