Please use this identifier to cite or link to this item: https://doi.org/10.1002/anie.201107833
Title: Linking of 2-oxoglutarate and substrate binding sites enables potent and highly selective inhibition of JmjC histone demethylases
Authors: Woon, E.C.Y. 
Tumber, A.
Kawamura, A.
Hillringhaus, L.
Ge, W.
Rose, N.R.
Ma, J.H.Y.
Chan, M.C.
Walport, L.J.
Che, K.H.
Ng, S.S.
Marsden, B.D.
Oppermann, U.
McDonough, M.A.
Schofield, C.J.
Keywords: 2-oxoglutarate
epigenetics
histone lysine demethylases
oxygenases
thiol-ene reaction
Issue Date: 13-Feb-2012
Citation: Woon, E.C.Y., Tumber, A., Kawamura, A., Hillringhaus, L., Ge, W., Rose, N.R., Ma, J.H.Y., Chan, M.C., Walport, L.J., Che, K.H., Ng, S.S., Marsden, B.D., Oppermann, U., McDonough, M.A., Schofield, C.J. (2012-02-13). Linking of 2-oxoglutarate and substrate binding sites enables potent and highly selective inhibition of JmjC histone demethylases. Angewandte Chemie - International Edition 51 (7) : 1631-1634. ScholarBank@NUS Repository. https://doi.org/10.1002/anie.201107833
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. Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Source Title: Angewandte Chemie - International Edition
URI: http://scholarbank.nus.edu.sg/handle/10635/125025
ISSN: 14337851
DOI: 10.1002/anie.201107833
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