Sulfur–Oxygen Chalcogen Bonding Mediates AdoMet Recognition in the Lysine Methyltransferase SET7/9-Reference-Cited by-同舟云学术

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Sulfur–Oxygen Chalcogen Bonding Mediates AdoMet Recognition in the Lysine Methyltransferase SET7/9

Published:2016-01-12 Issue:3 Volume:11 Page:748-754
ISSN:1554-8929
Container-title:ACS Chemical Biology
language:en
Short-container-title:ACS Chem. Biol.

Author:

Fick Robert J.,Kroner Grace M.,Nepal Binod¹,Magnani Roberta²,Horowitz Scott³,Houtz Robert L.²,Scheiner Steve¹,Trievel Raymond C.

Affiliation:

1. Department of Chemistry and Biochemistry, Utah State University, Logan, Utah 84322, United States

2. Department of Horticulture, University of Kentucky, Lexington, Kentucky 40546, United States

3. Howard Hughes Medical Institute, Ann Arbor, Michigan 48109, United States

Funder

Division of Chemistry

U.S. Department of Energy

Publisher

American Chemical Society (ACS)

Subject

Molecular Medicine,General Medicine,Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acschembio.5b00852

Reference33 articles.

1. Bioinformatic identification of novel methyltransferases

2. Uncovering the Human Methyltransferasome

3. Many paths to methyltransfer: a chronicle of convergence

4. Conservation and Functional Importance of Carbon–Oxygen Hydrogen Bonding in AdoMet-Dependent Methyltransferases

5. Manipulating Unconventional CH-Based Hydrogen Bonding in a Methyltransferase via Noncanonical Amino Acid Mutagenesis

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