Substrate selectivity and inhibition of histidine JmjC hydroxylases MINA53 and NO66.
<p>Non-haem Fe(II) and 2-oxoglutarate (2OG) dependent oxygenases catalyse oxidation of multiple proteins in organisms ranging from bacteria to humans. We describe studies on the substrate selectivity and inhibition of the human ribosomal oxygenases (ROX) MINA53 and NO66, members of the JmjC 2O...
المؤلفون الرئيسيون: | Türkmen, VA, Hintzen, JCJ, Tumber, A, Moesgaard, L, Salah, E, Kongsted, J, Schofield, CJ, Mecinović, J |
---|---|
التنسيق: | Journal article |
اللغة: | English |
منشور في: |
Royal Society of Chemistry
2023
|
مواد مشابهة
-
In vitro enzyme assays for JmjC-domain-containing lysine histone demethylases (JmjC-KDMs)
حسب: Tarhonskaya, H, وآخرون
منشور في: (2018) -
Structure–function relationships of human JmjC oxygenases — demethylases versus hydroxylases
حسب: Markolovic, S, وآخرون
منشور في: (2016) -
Kinetic and inhibition studies on human Jumonji-C (JmjC) domain-containing protein 5
حسب: Tumber, A, وآخرون
منشور في: (2023) -
Conservation of the unusual dimeric JmjC fold of JMJD7 from Drosophila melanogaster to humans
حسب: Chowdhury, R, وآخرون
منشور في: (2022) -
Inhibitors of both the N-methyl lysyl- and arginyl- demethylase activities of the JmjC oxygenases
حسب: Bonnici, J, وآخرون
منشور في: (2018)