Dioxygen binding in the active site of histone demethylase JMJD2A and the role of the protein environment
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...
| Váldodahkkit: | , , , , |
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| Materiálatiipa: | Journal article |
| Giella: | English |
| Almmustuhtton: |
Wiley
2015
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Dioxygen binding in the active site of histone demethylase JMJD2A and the role of the protein environment
Almmustuhtton 2015
Journal article