Post-translational Protein Acetylation: An Elegant Mechanism for Bacteria to Dynamically Regulate Metabolic Functions-Reference-Cited by-同舟云学术

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Post-translational Protein Acetylation: An Elegant Mechanism for Bacteria to Dynamically Regulate Metabolic Functions

Published:2019-07-12 Issue: Volume:10 Page:
ISSN:1664-302X
Container-title:Frontiers in Microbiology
language:
Short-container-title:Front. Microbiol.

Author:

Christensen David G.,Xie Xueshu,Basisty Nathan,Byrnes James,McSweeney Sean,Schilling Birgit,Wolfe Alan J.

Funder

National Institute of General Medical Sciences

Division of Intramural Research, National Institute of Allergy and Infectious Diseases

National Center for Research Resources

U.S. Department of Energy

Publisher

Frontiers Media SA

Subject

Microbiology (medical),Microbiology

Reference279 articles.

1. The E. coli sirtuin CobB shows no preference for enzymatic and nonenzymatic lysine acetylation substrate sites.;AbouElfetouh;Microbiologyopen,2015

2. Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis.;Allfrey;Proc. Natl. Acad. Sci. U.S.A.,1964

3. Post-translational serine/threonine phosphorylation and lysine acetylation: a novel regulatory aspect of the global nitrogen response regulator GlnR in S. coelicolor M145.;Amin;Front. Mol. Biosci.,2016

4. Are growth rates of Escherichia coli in batch cultures limited by respiration?;Andersen;J. Bacteriol.,1980

5. Mechanism of sirtuin inhibition by nicotinamide: altering the NAD(+) cosubstrate specificity of a Sir2 enzyme.;Avalos;Mol. Cell,2005

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