Proteome Wide Profiling of N-ε-Lysine Acetylation Reveals a Novel Mechanism of Regulation of the Chitinase Activity in Francisella novicida-Reference-Cited by-同舟云学术

Proteome Wide Profiling of N-ε-Lysine Acetylation Reveals a Novel Mechanism of Regulation of the Chitinase Activity in Francisella novicida

Published:2020-02-14 Issue:4 Volume:19 Page:1409-1422
ISSN:1535-3893
Container-title:Journal of Proteome Research
language:en
Short-container-title:J. Proteome Res.

Author:

Marakasova Ekaterina¹^ORCID,Ii Alexandra¹,Nelson Kristina T.²,van Hoek Monique L.¹^ORCID

Affiliation:

1. School of Systems Biology, George Mason University, 10900 University Blvd, Manassas, Virginia 20110, United States

2. Chemical and Proteomic Mass Spectrometry Core Facility, Virginia Commonwealth University, 1001 W. Main Street, Richmond, Virginia 23284, United States

Funder

George Mason University

Virginia Commonwealth University

Publisher

American Chemical Society (ACS)

Subject

General Chemistry,Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jproteome.9b00512

Reference80 articles.

1. Regulatory potential of post-translational modifications in bacteria

2. Protein acetylation affects acetate metabolism, motility and acid stress response in Escherichia coli

3. The E. coli sirtuin CobB shows no preference for enzymatic and nonenzymatic lysine acetylation substrate sites

4. Bacterial protein acetylation: new discoveries unanswered questions

5. Francisella tularensis: unravelling the secrets of an intracellular pathogen

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