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Linking of 2-oxoglutarate and substrate binding sites enables potent and highly selective inhibition of JmjC histone demethylases

DOI: 10.1002/anie.201107833 DOI Help
PMID: 22241642 PMID Help

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)