Evidence map›Paper›PMID 36289443›Full record

ArticleCommunications biology2022

Multiple mechanisms contribute to fluorometry signals from the voltage-gated proton channel.

Ferenc Papp, Gilman E S Toombes, Zoltán Pethő, Adrienn Bagosi, Adam Feher, János Almássy, Jesús Borrego, Ákos Kuki, Sándor Kéki, Gyorgy Panyi and 1 more

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.5field-weighted citation impact, top 38% 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

4 citing papers in PubMed, 6 citations in OpenAlex.

  1. Modulators of the Human Voltage-Gated Proton Channel HPharmaceuticals (Basel, Switzerland) · 2025
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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

11 authors at 2 institutions in 2 countries.

Ferenc PappDepartment of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, Egyetem ter 1, Debrecen, H-4032, Hungary. papp.ferenc@med.unideb.hu.
Gilman E S ToombesMolecular Physiology and Biophysics Section, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, National Institutes of Health, 35 Convent Dr., MSC 3701, Bethesda, MD, 20892-3701, USA.ORCID 0000-0001-8346-1790
Zoltán PethőDepartment of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, Egyetem ter 1, Debrecen, H-4032, Hungary.ORCID 0000-0001-7057-4761
Adrienn BagosiDepartment of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, Egyetem ter 1, Debrecen, H-4032, Hungary.
Adam FeherDepartment of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, Egyetem ter 1, Debrecen, H-4032, Hungary.
János AlmássyDepartment of Physiology, Faculty of Medicine, University of Debrecen, Egyetem ter 1, Debrecen, H-4032, Hungary.
Jesús BorregoDepartment of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, Egyetem ter 1, Debrecen, H-4032, Hungary.
Ákos KukiDepartment of Applied Chemistry, University of Debrecen, Egyetem ter 1, Debrecen, H-4032, Hungary.
Sándor KékiDepartment of Applied Chemistry, University of Debrecen, Egyetem ter 1, Debrecen, H-4032, Hungary.
Gyorgy PanyiDepartment of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, Egyetem ter 1, Debrecen, H-4032, Hungary.
Zoltan VargaDepartment of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, Egyetem ter 1, Debrecen, H-4032, Hungary.
University of Debrecen · HUNational Institutes of Health · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Voltage-clamp fluorometry (VCF) supplies information about the conformational changes of voltage-gated proteins. Changes in the fluorescence intensity of the dye attached to a part of the protein that undergoes a conformational rearrangement upon the alteration of the membrane potential by electrodes constitute the signal. The VCF signal is generated by quenching and dequenching of the fluorescence as the dye traverses various local environments. Here we studied the VCF signal generation, using the Hv1 voltage-gated proton channel as a tool, which shares a similar voltage-sensor structure with voltage-gated ion channels but lacks an ion-conducting pore. Using mutagenesis and lipids added to the extracellular solution we found that the signal is generated by the combined effects of lipids during movement of the dye relative to the plane of the membrane and by quenching amino acids. Our 3-state model recapitulates the VCF signals of the various mutants and is compatible with the accepted model of two major voltage-sensor movements.

Indexed as

Ion Channel GatingProtonsAmino AcidsFluorometryIon ChannelsLipidsAmino AcidsIon ChannelsLipidsProtons

Identifiers

PMID36289443
PMCPMC9606259
OpenAlexW4307291528

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.