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. Copyright © 2...
Váldodahkkit: | Woon, E, Tumber, A, Kawamura, A, Hillringhaus, L, Ge, W, Rose, N, Ma, J, Chan, M, Walport, L, Che, K, Ng, S, Marsden, B, Oppermann, U, McDonough, M, Schofield, C |
---|---|
Materiálatiipa: | Journal article |
Giella: | English |
Almmustuhtton: |
2012
|
Geahča maid
-
In vitro enzyme assays for JmjC-domain-containing lysine histone demethylases (JmjC-KDMs)
Dahkki: Tarhonskaya, H, et al.
Almmustuhtton: (2018) -
Arginine demethylation is catalysed by a subset of JmjC histone lysine demethylases.
Dahkki: Walport, L, et al.
Almmustuhtton: (2016) -
Inhibitors of JmjC-containing histone demethylases
Dahkki: Wright, M, et al.
Almmustuhtton: (2020) -
JmjC ‐domain‐containing histone demethylases
Dahkki: Højrup, C, et al.
Almmustuhtton: (2019) -
Arginine demethylation is catalysed by a subset of JmjC histone lysine demethylases
Dahkki: Louise J. Walport, et al.
Almmustuhtton: (2016-06-01)