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...
| المؤلفون الرئيسيون: | , , , , |
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| التنسيق: | Journal article |
| اللغة: | English |
| منشور في: |
Wiley
2015
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