Evidence map›Paper›PMID 31354686›Full record

ReviewFrontiers in microbiology2019

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

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

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in microbiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 110 papers.

0numbers the graph read from it
0cells of the map it votes in
110citing papers in PubMed
8.2field-weighted citation impact, top 2% of its field
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

110 citing papers in PubMed, 172 citations in OpenAlex.

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  17. Structural basis of the catalytic and allosteric mechanism of bacterial acetyltransferase PatZ.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  18. Article
  19. Review
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50 more citing papers are in PubMed but not listed here.

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

7 authors at 3 institutions in 1 country.

David G ChristensenHealth Sciences Division, Department of Microbiology and Immunology, Stritch School of Medicine, Loyola University Chicago, Maywood, IL, United States.
Xueshu XieBuck Institute for Research on Aging, Novato, CA, United States.
Nathan BasistyBuck Institute for Research on Aging, Novato, CA, United States.
James ByrnesEnergy & Photon Sciences Directorate, National Synchrotron Light Source II, Brookhaven National Laboratory, Upton, NY, United States.
Sean McSweeneyEnergy & Photon Sciences Directorate, National Synchrotron Light Source II, Brookhaven National Laboratory, Upton, NY, United States.
Birgit SchillingBuck Institute for Research on Aging, Novato, CA, United States.
Alan J WolfeHealth Sciences Division, Department of Microbiology and Immunology, Stritch School of Medicine, Loyola University Chicago, Maywood, IL, United States.
Buck Institute for Research on Aging · USBrookhaven National Laboratory · USLoyola University Chicago · US

Funding

Life Science and Biomedical technology Research center at NSLS-II LSBRP41GM111244 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI MCSWEENEY, SEAN · 2014 to 2018
$16.4M
Lysine Acetylation in N. gonorrhoeae Quorum Sensing and Biofilm FormationR01AI108255 · NIAID · UNIVERSITY OF IOWA · PI KIRBY, JOHN R, SCHILLING, BIRGIT · 2014 to 2018
$4.1M
Sensing central metabolic stressR01GM066130 · NIGMS · LOYOLA UNIVERSITY CHICAGO · PI WOLFE, ALAN J · 2004 to 2012
$2.7M
TripleTOF 5600 High Resolution Mass SpectrometerS10OD016281 · OD · BUCK INSTITUTE FOR RESEARCH ON AGING · PI GIBSON, BRADFORD WAYNE · 2013 to 2013
$597k
NIAID NIH HHS R01 AI108255NIGMS NIH HHS P41 GM111244NIGMS NIH HHS R01 GM066130NIH HHS S10 OD016281
6 · The paper itself

Abstract

Post-translational modifications (PTM) decorate proteins to provide functional heterogeneity to an existing proteome. The large number of known PTMs highlights the many ways that cells can modify their proteins to respond to diverse stimuli. Recently, PTMs have begun to receive increased interest because new sensitive proteomics workflows and structural methodologies now allow researchers to obtain large-scale, in-depth and unbiased information concerning PTM type and site localization. However, few PTMs have been extensively assessed for functional consequences, leaving a large knowledge gap concerning the inner workings of the cell. Here, we review understanding of

Indexed as

acetylationbacterialysine acetyltransferasemass spectrometryproteomics

Identifiers

PMID31354686
PMCPMC6640162
OpenAlexW2959929739

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.