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Linking of 2‐Oxoglutarate and Substrate Binding Sites Enables Potent and Highly Selective Inhibition of JmjC Histone Demethylases
Author(s) -
Woon Esther C. Y.,
Tumber Anthony,
Kawamura Akane,
Hillringhaus Lars,
Ge Wei,
Rose Nathan R.,
Ma Jerome H. Y.,
Chan Mun Chiang,
Walport Louise J.,
Che Ka Hing,
Ng Stanley S.,
Marsden Brian D.,
Oppermann Udo,
McDonough Michael A.,
Schofield Christopher J.
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201107833
Subject(s) - histone , gene isoform , substrate (aquarium) , cofactor , computational biology , binding site , biochemistry , chemistry , biology , gene , enzyme , ecology
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.