A selective inhibitor and probe of the cellular functions of Jumonji C domain-containing histone demethylases.
J Am Chem Soc
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| Abstract | Histone methylations are important chromatin marks that regulate gene expression, genomic stability, DNA repair, and genomic imprinting. Histone demethylases are the most recent family of histone-modifying enzymes discovered. Here, we report the characterization of a small-molecule inhibitor of Jumonji C domain-containing histone demethylases. The inhibitor derives from a structure-based design and preferentially inhibits the subfamily of trimethyl lysine demethylases. Its methyl ester prodrug, methylstat, selectively inhibits Jumonji C domain-containing his-tone demethylases in cells and may be a useful small-molecule probe of chromatin and its role in epigenetics. |
| Year of Publication | 2011
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| Journal | J Am Chem Soc
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| Volume | 133
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| Issue | 24
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| Pages | 9451-6
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| Date Published | 2011 Jun 22
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| ISSN | 1520-5126
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| DOI | 10.1021/ja201597b
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| PubMed ID | 21585201
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| PubMed Central ID | PMC3133600
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| Grant list | R37 GM038627 / GM / NIGMS NIH HHS / United States
R01 GM038627 / GM / NIGMS NIH HHS / United States
Canadian Institutes of Health Research / Canada
Howard Hughes Medical Institute / United States
GM38627 / GM / NIGMS NIH HHS / United States
R01 GM098390 / GM / NIGMS NIH HHS / United States
R01 GM038627-20 / GM / NIGMS NIH HHS / United States
Wellcome Trust / United Kingdom
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