ArticleProceedings of the National Academy of Sciences of the United States of America2020
Modulation of the bacterial CobB sirtuin deacylase activity by N-terminal acetylation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
18 citing papers in PubMed, 22 citations in OpenAlex.
- InPathogens (Basel, Switzerland) · 2025Article
- Potential of lactylation as a therapeutic target in cancer treatment (Review).Molecular medicine reports · 2025Review
- Stereospecific lactylation in bacteriology: L/D-lactate partitioning shapes host metabolic-disease axis.Frontiers in microbiology · 2025Review
- Structure-function analysis of carrier protein-dependent 2-sulfamoylacetyl transferase in the biosynthesis of altemicidin.Nature communications · 2024Article
- Synthetic translational coupling element for multiplexed signal processing and cellular control.Nucleic acids research · 2024Article
- YkuR functions as a protein deacetylase inProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Acetyl-CoA synthetase activity is enzymatically regulated by lysine acetylation using acetyl-CoA or acetyl-phosphate as donor molecule.Nature communications · 2024Article
- Spatiotemporal and direct capturing global substrates of lysine-modifying enzymes in living cells.Nature communications · 2024Article
- K235 acetylation couples with PSPC1 to regulate the mNature communications · 2023Article
- YiaC and CobB regulate lysine lactylation in Escherichia coli.Nature communications · 2022Article
- Identification and characterization of a novel GNAT superfamily NMicrobial biotechnology · 2022Article
- Protein N-terminal acylation: An emerging field in bacterial cell physiology.Current trends in microbiology · 2022Article
- Dynamic acylome reveals metabolite driven modifications inFrontiers in microbiology · 2022Article
- Sirtuin-Dependent Reversible Lysine Acetylation Controls the Activity of Acetyl Coenzyme A Synthetase in Campylobacter jejuni.Journal of bacteriology · 2021Article
- Protein Acetyltransferases Mediate Bacterial Adaptation to a Diverse Environment.Journal of bacteriology · 2021Review
- Bacterial Sirtuins Overview: An Open Niche to Explore.Frontiers in microbiology · 2021Review
- Post-translational Lysine Ac(et)ylation in Bacteria: A Biochemical, Structural, and Synthetic Biological Perspective.Frontiers in microbiology · 2021Review
- Investigation of the Importance of Protein 3D Structure for Assessing Conservation of Lysine Acetylation Sites in Protein Homologs.Frontiers in microbiology · 2021Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
In eukaryotic cells, the N-terminal amino moiety of many proteins is modified by N-acetyltransferases (NATs). This protein modification can alter the folding of the target protein; can affect binding interactions of the target protein with substrates, allosteric effectors, or other proteins; or can trigger protein degradation. In prokaryotes, only ribosomal proteins are known to be N-terminally acetylated, and the acetyltransferases responsible for this modification belong to the Rim family of proteins. Here, we report that, in
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Registered trials
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