Publication
Article Metrics
Citations
Online attention
Linking of 2-oxoglutarate and substrate binding sites enables potent and highly selective inhibition of JmjC histone demethylases
DOI:
10.1002/anie.201107833
PMID:
22241642
Authors:
Esther C. Y.
Woon
(University of Oxford)
,
Anthony
Tumber
(University of Oxford)
,
Akane
Kawamura
(University of Oxford)
,
Lars
Hillringhaus
(University of Oxford)
,
Wei
Ge
(University of Oxford)
,
Nathan
Rose
(University of Oxford)
,
Jerome H. Y.
Ma
(University of Oxford)
,
Mun Chiang
Chan
(University of Oxford)
,
Louise J.
Walport
(University of Oxford)
,
Ka Hing
Che
(University of Oxford)
,
Stanley S.
Ng
(University of Oxford)
,
Brian D.
Marsden
(University of Oxford)
,
Udo
Oppermann
(University of Oxford)
,
Michael A.
Mcdonough
(University of Oxford)
,
Christopher J.
Schofield
(University of Oxford)
Co-authored by industrial partner:
No
Type:
Journal Paper
Journal:
Angewandte Chemie International Edition
, VOL 51 (7)
, PAGES 1631 - 1634
State:
Published (Approved)
Published:
February 2012
Abstract: Select an isoform: Linking of cosubstrate and substrate binding sites enables highly selective inhibiton of isoforms of human histone lysine demethylases. The results should provide a basis for the development of potent and selective JmjC inhibitors, possibly suitable for clinical use.
Journal Keywords: 2-oxoglutarate; epigenetics; histone lysine demethylases; oxygenases; thiol–ene reaction
Diamond Keywords: Epigenetics
Subject Areas:
Chemistry,
Biology and Bio-materials,
Medicine
Instruments:
I02-Macromolecular Crystallography
Added On:
24/09/2015 13:47
Discipline Tags:
Health & Wellbeing
Biochemistry
Chemistry
Structural biology
Drug Discovery
Life Sciences & Biotech
Technical Tags:
Diffraction
Macromolecular Crystallography (MX)