Evidence map›Paper›PMID 42506740›Full record

ArticleJournal of bacteriology2026

Identification of a conserved GNAT-family lysine acetyltransferase in

Joseph O'Brien, Flavia M Saavedra, Irene Choi, Kyle J McCulloch, Maria Martell, Alexandra M Peterson, Christopher Staley, Mark C Herzberg, Bruno P Lima

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of bacteriology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Joseph O'BrienDepartment of Emergency Medicine, Denver Health, Denver, Colorado, USA.
Flavia M SaavedraDepartment of Inflammation and Immunity, Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, Ohio, USA.
Irene ChoiDepartment of Diagnostic and Biological Sciences, University of Minnesota School of Dentistry, Minneapolis, Minnesota, USA.
Kyle J McCullochDepartment of Biology, University of Florida, Gainesville, Florida, USA.
Maria MartellDivision of Basic & Translational Research, Department of Surgery, University of Minnesota, Minneapolis, Minnesota, USA.
Alexandra M PetersonDepartment of Endodontics, University of Florida College of Dentistry, Gainesville, Florida, USA.ORCID 0000-0003-1124-3385
Christopher StaleyDivision of Basic & Translational Research, Department of Surgery, University of Minnesota, Minneapolis, Minnesota, USA.ORCID 0000-0002-2309-0083
Mark C HerzbergDepartment of Diagnostic and Biological Sciences, University of Minnesota School of Dentistry, Minneapolis, Minnesota, USA.ORCID 0000-0002-1195-1704
Bruno P LimaDepartment of Diagnostic and Biological Sciences, University of Minnesota School of Dentistry, Minneapolis, Minnesota, USA.ORCID 0000-0003-4619-4712

Funding

Regulation of Surface Protein Presentation on Streptococcus gordoniiR01DE025618 · NIDCR · UNIVERSITY OF MINNESOTA · PI HERZBERG, MARK C · 2016 to 2020
$2.2M
Investigating the role of lipoteichoic acid in surface protein presentationK08DE027705 · NIDCR · UNIVERSITY OF MINNESOTA · PI LIMA, BRUNO P · 2018 to 2022
$620k
The role of protein acetylation in Streptococcus gordonii biofilmsR03DE031337 · NIDCR · UNIVERSITY OF MINNESOTA · PI LIMA, BRUNO P · 2022 to 2023
$310k
American Association for Dental, Oral, and Craniofacial ResearchNIDCR NIH HHS K08 DE027705NIDCR NIH HHS R01 DE025618NIDCR NIH HHS R03 DE031337NIH HHS DE025618NIH HHS DE027705NIH HHS DE031337
6 · The paper itself

Abstract

IMPORTANCE: Protein acetylation is a common posttranslational modification conserved across all domains of life. In bacteria, protein acetylation is carried out by homologs of the GCN5-related N-acetyltransferase (GNAT) family. GNATs catalyze the transfer of an acetyl group from acetyl-CoA to the ε-amino group of lysine residues on proteins. This process changes the charge and length of lysine residues, resulting in changes to protein function.

Indexed as

BiofilmsLysine AcetyltransferasesMouthStreptococcus gordoniiAnimalsBacterial ProteinsGene DeletionMiceBacterial ProteinsLysine Acetyltransferasesacetylationbiofilmsoral streptococci

Identifiers

PMID42506740
PMCPMC13492136

What OpenQuestion holds

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LicenceCC BY
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.