Evidence map›Paper›PMID 23267178›Full record

ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2013

Twisting and subunit rotation in single F(O)(F1)-ATP synthase.

Hendrik Sielaff, Michael Börsch

Abstract readReview
In one paragraph

Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. The regulatory subunit ε in Escherichia coli FBiochimica et biophysica acta. Bioenergetics · 2018
    Review
  7. Visualizing Mitochondrial FFrontiers in physiology · 2018
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Regulatory conformational changes of the ε subunit in single FRET-labeled FProceedings of SPIE--the International Society for Optical Engineering · 2014
    Article
  13. Article
  14. Phosphate release coupled to rotary motion of F1-ATPase.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  15. Review
  16. The physics of life: one molecule at a time.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013
    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

2 authors.

Hendrik SielaffSingle-Molecule Microscopy Group, Jena University Hospital, Nonnenplan 2-4, 07743 Jena, Germany.
Michael Börsch

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

F(O)F(1)-ATP synthases are ubiquitous proton- or ion-powered membrane enzymes providing ATP for all kinds of cellular processes. The mechanochemistry of catalysis is driven by two rotary nanomotors coupled within the enzyme. Their different step sizes have been observed by single-molecule microscopy including videomicroscopy of fluctuating nanobeads attached to single enzymes and single-molecule Förster resonance energy transfer. Here we review recent developments of approaches to monitor the step size of subunit rotation and the transient elastic energy storage mechanism in single F(O)F(1)-ATP synthases.

Indexed as

Adenosine TriphosphateAlgorithmsCatalysisCell MembraneComputational BiologyComputer SimulationEscherichia coliEscherichia coli ProteinsLuminescent ProteinsMembrane ProteinsMembrane Transport ProteinsMicroscopy, FluorescenceMicroscopy, VideoProtein Structure, TertiaryProtein TransportProton-Translocating ATPasesAdenosine TriphosphateEscherichia coli ProteinsLuminescent ProteinsMembrane ProteinsMembrane Transport ProteinsProton-Translocating ATPasesRecombinant Fusion ProteinsTatA protein, E coli

Identifiers

PMID23267178
PMCPMC3538427

What OpenQuestion holds

Textmetadata
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.