Evidence map›Paper›PMID 33135152›Full record

ReviewFEBS letters2021

ABC-F translation factors: from antibiotic resistance to immune response.

Corentin R Fostier, Laura Monlezun, Farès Ousalem, Shikha Singh, John F Hunt, Grégory Boël

Open access · greenAbstract readReview
In one paragraph

Review in FEBS letters, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

27 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
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  6. Review
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  10. Review
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  12. HflX-mediated drug resistance through ribosome splitting and rRNA disordering in mycobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  13. Article
  14. Article
  15. Article
  16. Ribosome-targeting antibiotics and resistanceRSC medicinal chemistry · 2023
    Review
  17. Article
  18. Review
  19. Article
  20. Review
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

6 authors at 2 institutions in 2 countries.

Corentin R FostierUMR 8261, CNRS, Université de Paris, Institut de Biologie Physico-Chimique, Paris, France.ORCID 0000-0002-8913-0252
Laura MonlezunUMR 8261, CNRS, Université de Paris, Institut de Biologie Physico-Chimique, Paris, France.ORCID 0000-0003-4661-3366
Farès OusalemUMR 8261, CNRS, Université de Paris, Institut de Biologie Physico-Chimique, Paris, France.ORCID 0000-0002-0634-6753
Shikha SinghDepartment of Biological Sciences, 702A Sherman Fairchild Center, Columbia University, New York, NY, USA.
John F HuntDepartment of Biological Sciences, 702A Sherman Fairchild Center, Columbia University, New York, NY, USA.
Grégory BoëlUMR 8261, CNRS, Université de Paris, Institut de Biologie Physico-Chimique, Paris, France.ORCID 0000-0001-9900-6493
Centre National de la Recherche Scientifique · FRColumbia University · US

Funding

University of Georgia ProjectU54GM094597 · NIGMS · RUTGERS, THE STATE UNIV OF N.J. · PI MONTELIONE, GAETANO T · 2010 to 2014
$36.9M
Sub 9 at AECMU54GM075026 · NIGMS · NEW YORK STRUCTURAL BIOLOGY CENTER · PI SZYPERSKI, THOMAS A. · 2005 to 2009
$16.8M
Biophysical mechanisms of ABC-F proteinsR01GM120579 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI HUNT, JOHN FRANCIS · 2016 to 2019
$1.3M
NIGMS NIH HHS R01 GM120579NIGMS NIH HHS U54 GM075026NIGMS NIH HHS U54 GM094597
6 · The paper itself

Abstract

Energy-dependent translational throttle A (EttA) from Escherichia coli is a paradigmatic ABC-F protein that controls the first step in polypeptide elongation on the ribosome according to the cellular energy status. Biochemical and structural studies have established that ABC-F proteins generally function as translation factors that modulate the conformation of the peptidyl transferase center upon binding to the ribosomal tRNA exit site. These factors, present in both prokaryotes and eukaryotes but not in archaea, use related molecular mechanisms to modulate protein synthesis for heterogenous purposes, ranging from antibiotic resistance and rescue of stalled ribosomes to modulation of the mammalian immune response. Here, we review the canonical studies characterizing the phylogeny, regulation, ribosome interactions, and mechanisms of action of the bacterial ABC-F proteins, and discuss the implications of these studies for the molecular function of eukaryotic ABC-F proteins, including the three human family members.

Indexed as

AnimalsATP-Binding Cassette TransportersDrug Resistance, BacterialEscherichia coliEscherichia coli ProteinsHumansProtein BiosynthesisRibosomesATP-Binding Cassette TransportersEscherichia coli ProteinsEttA protein, E coliABC ATPaseABC-F protein familyantibiotic resistanceimmune responseinfectionmRNA translationprotein synthesis

Identifiers

PMID33135152
PMCPMC8609467
OpenAlexW3097745403

What OpenQuestion holds

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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.