Evidence map›Paper›PMID 27936329›Full record

ArticleJournal of the American Chemical Society2017

Chemomechanical Coupling in Hexameric Protein-Protein Interfaces Harnesses Energy within V-Type ATPases.

Abhishek Singharoy, Christophe Chipot, Mahmoud Moradi, Klaus Schulten

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

34 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. Review
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  4. The distortion-push mechanism for the γ subunit rotation in FProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  9. Molecular mechanism and energetics of coupling between substrate binding and product release in the FProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  10. Physical pictures of rotation mechanisms of FFrontiers in molecular biosciences · 2023
    Article
  11. Perspective: Path Sampling Methods Applied to Enzymatic Catalysis.Journal of chemical theory and computation · 2022
    Review
  12. Article
  13. Review
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  15. Article
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  18. Poor Person's pH Simulation of Membrane Proteins.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  19. Article
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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

4 authors at 3 institutions in 2 countries.

Abhishek SingharoyTheoretical and Computational Biophysics Group, Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign , 405 North Mathews Avenue, Urbana, Illinois 61801, United States.
Christophe ChipotTheoretical and Computational Biophysics Group, Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign , 405 North Mathews Avenue, Urbana, Illinois 61801, United States.ORCID 0000-0002-9122-1698
Mahmoud MoradiDepartment of Chemistry and Biochemistry, University of Arkansas , Fayetteville, Arkansas 72701, United States.ORCID 0000-0002-0601-402X
Klaus SchultenTheoretical and Computational Biophysics Group, Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign , 405 North Mathews Avenue, Urbana, Illinois 61801, United States.
University of Illinois Urbana-Champaign · USCentre National de la Recherche Scientifique · FRUniversity of Arkansas at Fayetteville · US

Funding

WHOLE CELL SIMULATIONP41GM104601 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI TAJKHORSHID, EMAD · 2012 to 2021
$19.0M
System-Level Simulation of a Bioenergetic MembraneR01GM067887 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI TAJKHORSHID, EMAD · 2003 to 2018
$4.0M
NIGMS NIH HHS P41 GM104601NIGMS NIH HHS R01 GM067887NIGMS NIH HHS R01-GM067887-11
6 · The paper itself

Abstract

ATP synthase is the most prominent bioenergetic macromolecular motor in all life forms, utilizing the proton gradient across the cell membrane to fuel the synthesis of ATP. Notwithstanding the wealth of available biochemical and structural information inferred from years of experiments, the precise molecular mechanism whereby vacuolar (V-type) ATP synthase fulfills its biological function remains largely fragmentary. Recently, crystallographers provided the first high-resolution view of ATP activity in Enterococcus hirae V

Indexed as

Adenosine TriphosphateEnterococcus hiraeHydrolysisModels, MolecularProtein BindingVacuolar Proton-Translocating ATPasesAdenosine TriphosphateVacuolar Proton-Translocating ATPases

Identifiers

PMID27936329
PMCPMC5518570
OpenAlexW2559781202

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.