QM/MM MD and Free Energy Simulation Study of Methyl Transfer Processes Catalyzed by PKMTs and PRMTs
Author:
Publisher
Springer Science and Business Media LLC
Subject
Health Informatics,Computer Science Applications,General Biochemistry, Genetics and Molecular Biology
Link
http://link.springer.com/content/pdf/10.1007/s12539-015-0280-y.pdf
Reference50 articles.
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3. Trievel RC (2004) Structure and function of histone methyltransferases. Crit Rev Eukaryot Gene Expr 14(3):147–169
4. Dillon SC, Zhang X, Trievel RC, Cheng X (2005) The SET-domain protein superfamily: protein lysine methyltransferases. Genome Biol 6(8):227. doi: 10.1186/gb-2005-6-8-227
5. Cheng X, Collins RE, Zhang X (2005) Structural and sequence motifs of protein (histone) methylation enzymes. Annu Rev Biophys Biomol Struct 34:267–294. doi: 10.1146/annurev.biophys.34.040204.144452
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1. Mechanistic basis of the increased methylation activity of the SETD2 protein lysine methyltransferase towards a designed super-substrate peptide;Communications Chemistry;2022-10-28
2. QM/MM Investigation of Substrate and Product Specificities of Suv4-20h2: How Does This Enzyme Generate Dimethylated H4K20 from Monomethylated Substrate?;Journal of Chemical Theory and Computation;2017-05-22
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