Evidence map›Paper›PMID 41774794›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2026

ATP synthase activity boosts membrane proton acceptance and lateral diffusion.

Hendrik Flegel, Ambili Ramanthrikkovil Variyam, Nadav Amdursky, Claudia Steinem

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Hendrik FlegelFaculty of Chemistry, Institute of Organic and Biomolecular Chemistry, University of Göttingen, Göttingen 37077, Germany.
Ambili Ramanthrikkovil VariyamSchulich Faculty of Chemistry, Technion-Israel Institute of Technology, Haifa 3200003, Israel.
Nadav AmdurskySchulich Faculty of Chemistry, Technion-Israel Institute of Technology, Haifa 3200003, Israel.ORCID 0000-0003-1543-5333
Claudia SteinemFaculty of Chemistry, Institute of Organic and Biomolecular Chemistry, University of Göttingen, Göttingen 37077, Germany.ORCID 0000-0001-8778-9283

Funding

Volkswagen Foundation (VolkswagenStiftung) grant no. 76251-10-4/20 (ZN 3625)
6 · The paper itself

Abstract

In most organisms, ATP synthesis is powered by the proton motive force (pmf) and catalyzed by ATP synthase. While the chemiosmotic theory originally proposed a "delocalized coupling" between proton pumps and consumers, growing evidence implicates the membrane in mediating localized proton transfer (PT). To directly track ultrafast PT at the membrane surface as a function of ATP synthase activity, we developed an in vitro system. We tethered a light-activated excited-state photoacid to the bilayer of unilamellar vesicles to confine PT to the membrane interface and co-reconstituted a thermophilic

Indexed as

Cell MembraneProtonsProton-Translocating ATPasesAdenosine TriphosphateBacillusDiffusionLipid BilayersProton-Motive ForceSpectrometry, FluorescenceUnilamellar LiposomesAdenosine TriphosphateLipid BilayersProtonsProton-Translocating ATPasesUnilamellar Liposomesenergy conversionHPTSproton transfertime-correlated single photon countingunilamellar vesicles

Identifiers

PMID41774794
PMCPMC12974407

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.