Lysine benzoylation is a histone mark regulated by SIRT2-Reference-Cited by-同舟云学术

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Lysine benzoylation is a histone mark regulated by SIRT2

Published:2018-08-28 Issue:1 Volume:9 Page:
ISSN:2041-1723
Container-title:Nature Communications
language:en
Short-container-title:Nat Commun

Author:

Huang He,Zhang Di,Wang Yi,Perez-Neut Mathew,Han Zhen,Zheng Y. George,Hao Quan,Zhao Yingming

Funder

U.S. Department of Health & Human Services | National Institutes of Health

U.S. Department of Health & Human Services | NIH | National Center for Advancing Translational Sciences

Publisher

Springer Science and Business Media LLC

Subject

General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry

Link

http://www.nature.com/articles/s41467-018-05567-w.pdf

Reference50 articles.

1. Sabari, B. R., Zhang, D., Allis, C. D. & Zhao, Y. Metabolic regulation of gene expression through histone acylations. Nat. Rev. Mol. Cell Biol. 18, 90–101 (2017).

2. Muller, M. M. & Muir, T. W. Histones: at the crossroads of peptide and protein chemistry. Chem. Rev. 115, 2296–2349 (2015).

3. Xie, Z. Y. et al. Metabolic regulation of gene expression by histone lysine beta-hydroxybutyrylation. Mol. Cell 62, 194–206 (2016).

4. Moellering, R. E. & Cravatt, B. F. Functional lysine modification by an intrinsically reactive primary glycolytic metabolite. Science 341, 549–553 (2013).

5. Simithy, J., Sidoli, S. & Garcia, B. A. Integrating proteomics and targeted metabolomics to understand global changes in histone modifications. Proteomics e1700309 (2018).

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