Cargando…
Fine-tuning of lysine side chain modulates the activity of histone lysine methyltransferases
Histone lysine methyltransferases (KMTs) play an important role in epigenetic gene regulation and have emerged as promising targets for drug discovery. However, the scope and limitation of KMT catalysis on substrates possessing substituted lysine side chains remain insufficiently explored. Here, we...
Autores principales: | Al Temimi, Abbas H. K., Merx, Jona, van Noortwijk, Christian J., Proietti, Giordano, Buijs, Romano, White, Paul B., Rutjes, Floris P. J. T., Boltje, Thomas J., Mecinović, Jasmin |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7726145/ https://www.ncbi.nlm.nih.gov/pubmed/33299050 http://dx.doi.org/10.1038/s41598-020-78331-0 |
Ejemplares similares
-
Lysine Ethylation by Histone Lysine Methyltransferases
por: Al Temimi, Abbas H. K., et al.
Publicado: (2019) -
Lysine Possesses the Optimal Chain Length for Histone Lysine Methyltransferase Catalysis
por: Temimi, Abbas H. K. Al, et al.
Publicado: (2017) -
Effect of lysine side chain length on histone lysine acetyltransferase catalysis
por: Proietti, Giordano, et al.
Publicado: (2020) -
Examining sterically demanding lysine analogs for histone lysine methyltransferase catalysis
por: Temimi, Abbas H. K. Al, et al.
Publicado: (2020) -
Substrate Scope for Human Histone Lysine Acetyltransferase KAT8
por: Proietti, Giordano, et al.
Publicado: (2021)