Evidence map›Paper›PMID 19610671›Full record

ArticleBiochemistry2009

Single molecule measurements of F1-ATPase reveal an interdependence between the power stroke and the dwell duration.

David Spetzler, Robert Ishmukhametov, Tassilo Hornung, Lixia Jin Day, James Martin, Wayne D Frasch

Abstract read
In one paragraph

Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

36 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Catalytic dwell oscillations complete the FCommunications chemistry · 2025
    Article
  3. Eukaryotic yeast VFrontiers in molecular biosciences · 2024
    Article
  4. Review
  5. Article
  6. FFrontiers in microbiology · 2022
    Review
  7. FFrontiers in microbiology · 2022
    Review
  8. pH-dependent 11° FeLife · 2021
    Article
  9. The 3 × 120° rotary mechanism ofProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  10. FliIScientific reports · 2020
    Article
  11. Rotary catalysis of bovine mitochondrial FProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  12. Method to extract multiple states in FProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  13. Article
  14. Elastic coupling power stroke mechanism of the FProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Theory for rates, equilibrium constants, and Brønsted slopes in F1-ATPase single molecule imaging experiments.Proceedings of the National Academy of Sciences of the United States of America · 2015
    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

6 authors at 1 institution in 1 country.

David SpetzlerSchool of Life Sciences, Arizona State University, P.O. Box 874501, Tempe, Arizona 85287-4501, USA.
Robert Ishmukhametov
Tassilo Hornung
Lixia Jin Day
James Martin
Wayne D Frasch
Arizona State University · US

Funding

PARTICIPATION OF METALS IN THE F1-ATPASE MECHANISMR01GM050202 · NIGMS · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI FRASCH, WAYNE D · 1996 to 2010
$2.3M
NIGMS NIH HHS R01 GM050202NIGMS NIH HHS R01GM50202
6 · The paper itself

Abstract

Increases in the power stroke and dwell durations of single molecules of Escherichia coli F(1)-ATPase were measured in response to viscous loads applied to the motor and inhibition of ATP hydrolysis. The load was varied using different sizes of gold nanorods attached to the rotating gamma subunit and/or by increasing the viscosity of the medium using PEG-400, a noncompetitive inhibitor of ATPase activity. Conditions that increase the duration of the power stroke were found to cause 20-fold increases in the length of the dwell. These results suggest that the order of hydrolysis, product release, and substrate binding may change as the result of external load on the motor or inhibition of hydrolysis.

Indexed as

Proton-Motive ForceAdenosine TriphosphateCatalysisCell MembraneEnzyme InhibitorsEscherichia coli ProteinsHydrolysisMolecular Motor ProteinsPolyethylene GlycolsProtein SubunitsProton-Translocating ATPasesTime FactorsViscosityAdenosine TriphosphateEnzyme InhibitorsEscherichia coli Proteinsgamma subunit, F(1) ATPaseMolecular Motor ProteinsPolyethylene GlycolsProtein SubunitsProton-Translocating ATPases

Identifiers

PMID19610671
PMCPMC2737049
OpenAlexW2012712625

What OpenQuestion holds

Textmetadata
LicenceTDM
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.