Dioxygen binding in the active site of histone demethylase JMJD2A and the role of the protein environment

Dioxygen binding in the active site of histone demethylase JMJD2A and the role of the protein environment

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JMJD2A catalyses the demethylation of di- and trimethylated lysine residues in histone tails and is a target for the development of new anticancer medicines. Mechanistic details of demethylation are yet to be elucidated and are important for the understanding of epigenetic processes. We have evaluat...

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Bibliographic Details
Main Authors:	Cortopassi, W, Simion, R, Honsby, C, França, T, Paton, R
Format:	Journal article
Language:	English
Published:	Wiley 2015

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