QM/MM Investigation of Substrate and Product Specificities of Suv4-20h2: How Does This Enzyme Generate Dimethylated H4K20 from Monomethylated Substrate?-Reference-Cited by-同舟云学术

QM/MM Investigation of Substrate and Product Specificities of Suv4-20h2: How Does This Enzyme Generate Dimethylated H4K20 from Monomethylated Substrate?

Published:2017-05-22 Issue:6 Volume:13 Page:2977-2986
ISSN:1549-9618
Container-title:Journal of Chemical Theory and Computation
language:en
Short-container-title:J. Chem. Theory Comput.

Author:

Qian Ping¹,Guo Haobo²,Wang Liang¹,Guo Hong²³^ORCID

Affiliation:

1. Chemistry and Material Science Faculty, Shandong Agricultural University, Tai’an 271018, Shandong, Peoples Republic of China

2. Department of Biochemistry and Cellular and Molecular Biology, University of Tennessee, Knoxville, Tennessee 37996, United States

3. UT/ORNL Center for Molecular Biophysics, Oak Ridge National Laboratory, Oak Ridge, Tennessee 37830, United States

Funder

China Scholarship Council

National Natural Science Foundation of China

National Science Foundation

Postdoctoral Foundation of Shandong Agricultural University

Publisher

American Chemical Society (ACS)

Subject

Physical and Theoretical Chemistry,Computer Science Applications

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jctc.7b00069

Reference62 articles.

1. The language of covalent histone modifications

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4. Molecular basis for substrate recognition by lysine methyltransferases and demethylases

5. Mechanisms of histone lysine-modifying enzymes: A computational perspective on the role of the protein environment

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