Evidence map›Paper›PMID 29932911›Full record

ReviewBiochimica et biophysica acta. Bioenergetics2018

The regulatory subunit ε in Escherichia coli F

Hendrik Sielaff, Thomas M Duncan, Michael Börsch

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta. Bioenergetics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Detection of Antibiotic Resistance in Feline-Origin ESBLInternational journal of molecular sciences · 2023
    Article
  8. FInternational journal of molecular sciences · 2023
    Review
  9. Changes within the central stalk of E. coli FCommunications biology · 2023
    Article
  10. Article
  11. How Does FFrontiers in microbiology · 2022
    Review
  12. Modulation of the HFrontiers in molecular biosciences · 2022
    Review
  13. Structure of the ATP synthase fromProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  14. Article
  15. Article
  16. Gain of SpontaneousFrontiers in bioengineering and biotechnology · 2021
    Article
  17. Article
  18. Article
  19. Article
  20. Article
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

3 authors.

Hendrik SielaffSingle-Molecule Microscopy Group, Jena University Hospital, Friedrich Schiller University, Jena, Germany.
Thomas M DuncanDepartment of Biochemistry & Molecular Biology, SUNY Upstate Medical University, Syracuse, NY, USA.
Michael BörschSingle-Molecule Microscopy Group, Jena University Hospital, Friedrich Schiller University, Jena, Germany. Electronic address: michael.boersch@uni-jena.de.

Funding

Energy Coupling and Regulation in the ATP Synthase of E. coliR01GM083088 · NIGMS · UPSTATE MEDICAL UNIVERSITY · PI DUNCAN, THOMAS M · 2009 to 2012
$1.6M
NIGMS NIH HHS R01 GM083088
6 · The paper itself

Abstract

F-type ATP synthases are extraordinary multisubunit proteins that operate as nanomotors. The Escherichia coli (E. coli) enzyme uses the proton motive force (pmf) across the bacterial plasma membrane to drive rotation of the central rotor subunits within a stator subunit complex. Through this mechanical rotation, the rotor coordinates three nucleotide binding sites that sequentially catalyze the synthesis of ATP. Moreover, the enzyme can hydrolyze ATP to turn the rotor in the opposite direction and generate pmf. The direction of net catalysis, i.e. synthesis or hydrolysis of ATP, depends on the cell's bioenergetic conditions. Different control mechanisms have been found for ATP synthases in mitochondria, chloroplasts and bacteria. This review discusses the auto-inhibitory behavior of subunit ε found in F

Indexed as

Adenosine TriphosphateEnergy MetabolismEscherichia coliEscherichia coli ProteinsProtein SubunitsProton-Translocating ATPasesAdenosine TriphosphateEscherichia coli ProteinsProtein SubunitsProton-Translocating ATPasesEpsilon subunitEscherichia coliF(O)F(1)-ATP synthaseFörster resonance energy transfer (FRET)RegulationSingle molecule

Identifiers

PMID29932911
PMCPMC6114093

What OpenQuestion holds

Textmetadata
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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.