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

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
Appears in Collections:	Staff Publications

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