Evidence map›Paper›PMID 29073046›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Nonequilibrium fluctuations of lipid membranes by the rotating motor protein F

Víctor G Almendro-Vedia, Paolo Natale, Michael Mell, Stephanie Bonneau, Francisco Monroy, Frederic Joubert, Iván López-Montero

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. 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
1.9field-weighted citation impact, top 14% 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, 55 citations in OpenAlex.

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  10. Synthetic Cells Revisited: Artificial Cells Construction Using Polymeric Building Blocks.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Review
  11. Article
  12. Rotation of the c-Ring Promotes the Curvature Sorting of Monomeric ATP Synthases.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    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

7 authors at 2 institutions in 2 countries.

Víctor G Almendro-VediaDepartamento Química Física I, Universidad Complutense de Madrid, 28040 Madrid, Spain.
Paolo NataleDepartamento Química Física I, Universidad Complutense de Madrid, 28040 Madrid, Spain.
Michael MellDepartamento Química Física I, Universidad Complutense de Madrid, 28040 Madrid, Spain.
Stephanie BonneauLaboratoire Jean Perrin, CNRS, Université Pierre et Marie Curie, 75005 Paris, France.ORCID 0000-0003-2039-0037
Francisco MonroyDepartamento Química Física I, Universidad Complutense de Madrid, 28040 Madrid, Spain.ORCID 0000-0001-6455-3083
Frederic JoubertLaboratoire Jean Perrin, CNRS, Université Pierre et Marie Curie, 75005 Paris, France.
Iván López-MonteroDepartamento Química Física I, Universidad Complutense de Madrid, 28040 Madrid, Spain; ivanlopez@quim.ucm.es.ORCID 0000-0001-8131-6063
Universidad Complutense de Madrid · ESCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ATP synthase is a rotating membrane protein that synthesizes ATP through proton-pumping activity across the membrane. To unveil the mechanical impact of this molecular active pump on the bending properties of its lipid environment, we have functionally reconstituted the ATP synthase in giant unilamellar vesicles and tracked the membrane fluctuations by means of flickering spectroscopy. We find that ATP synthase rotates at a frequency of about 20 Hz, promoting large nonequilibrium deformations at discrete hot spots in lipid vesicles and thus inducing an overall membrane softening. The enhanced nonequilibrium fluctuations are compatible with an accumulation of active proteins at highly curved membrane sites through a curvature-protein coupling mechanism that supports the emergence of collective effects of rotating ATP synthases in lipid membranes.

Indexed as

Adenosine TriphosphateBacterial Proton-Translocating ATPasesCell MembraneEscherichia coli ProteinsFluorescent DyesHydrogen-Ion ConcentrationLipid BilayersMicroscopy, VideoRecombinant ProteinsRhodamine 123Unilamellar LiposomesValinomycinAdenosine TriphosphateBacterial Proton-Translocating ATPasesEscherichia coli ProteinsEscherichia coli Proton-Translocating ATPaseFluorescent DyesLipid BilayersRecombinant ProteinsRhodamine 123Unilamellar LiposomesValinomycinactive membranesbiological nanorotorsflickering spectroscopygiant vesiclesmechanical properties

Identifiers

PMID29073046
PMCPMC5664490
OpenAlexW2762941337

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.