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Inhibition of Histone Demethylases by 4-Carboxy-2,2-Bipyridyl Compounds
DOI:
10.1002/cmdc.201100026
PMID:
21412984
Authors:
Kai-hsuan
Chang
(University of Oxford)
,
Oliver
King
(University of Oxford)
,
Antony
Tumber
(University of Oxford)
,
Esther
Woon
(University of Oxford)
,
Tom
Heightman
(University of Oxford)
,
Michael
Mcdonough
(University of Oxford)
,
Christopher
Schofield
(University of Oxford)
,
Nathan
Rose
(University of Oxford)
Co-authored by industrial partner:
No
Type:
Journal Paper
Journal:
Chemmedchem
, VOL 6 (5)
, PAGES 759 - 764
State:
Published (Approved)
Published:
March 2011
Abstract: Exploiting epigenetics: 2-Oxoglutarate (2OG)-dependent histone lysine demethylases, such as JMJD2E, are potential therapeutic targets in a range of diseases. Through structure–activity relationship studies and analyses, we identified a potent 4-carboxy-2,2′-bipyridyl compound, which inhibits JMJD2E with an IC50 value of 110 nM, representing a 66-fold improvement over the lead compound. These bipyridyl derivatives bind in the 2-oxoglutarate binding site.
Journal Keywords: Binding; Computer; Crystallography; X-Ray; Enzyme; Humans; Jumonji; Ketoglutaric; Protein; Tertiary; Structure-Activity Relationship
Subject Areas:
Chemistry
Instruments:
I02-Macromolecular Crystallography
Added On:
06/04/2011 10:38
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