Linking of 2-Oxoglutarate and Substrate Binding Sites Enables Potent and Highly Selective Inhibition of JmjC Histone Demethylases

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.

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Bibliographic Details
Published in:Angewandte Chemie International Edition 2012-02, Vol.51 (7), p.1631-1634
Main Authors: 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.
Format: Article
Language:English
Subjects:
2-oxoglutarate
Binding sites
Binding Sites - drug effects
Cross-Linking Reagents - chemical synthesis
Cross-Linking Reagents - chemistry
Cross-Linking Reagents - pharmacology
epigenetics
histone lysine demethylases
Histones
Human
Humans
Inhibition
Inhibitors
Isoforms
Joining
Jumonji Domain-Containing Histone Demethylases - antagonists & inhibitors
Jumonji Domain-Containing Histone Demethylases - chemistry
Ketoglutaric Acids - chemistry
Ketoglutaric Acids - pharmacology
Linking
Lysine
Models, Molecular
Molecular Structure
oxygenases
Structure-Activity Relationship
Substrate inhibition
Substrate Specificity
thiol-ene reaction
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Description
Summary: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.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201107833