Evidence map›Paper›PMID 33303878›Full record

ArticleScientific reports2020

Unravelling the intricate cooperativity of subunit gating in P2X2 ion channels.

Christian Sattler, Thomas Eick, Sabine Hummert, Eckhard Schulz, Ralf Schmauder, Andrea Schweinitz, Christopher Unzeitig, Frank Schwede, Klaus Benndorf

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
5.5field-weighted citation impact, top 3% 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

12 citing papers in PubMed, 48 citations in OpenAlex.

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  9. Optical control of PIEZO1 channels.Nature communications · 2023
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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

9 authors at 4 institutions in 1 country.

Christian SattlerInstitut für Physiologie II, Universitätsklinikum Jena, Friedrich-Schiller-Universität Jena, Kollegiengasse 9, 07743, Jena, Germany.
Thomas EickInstitut für Physiologie II, Universitätsklinikum Jena, Friedrich-Schiller-Universität Jena, Kollegiengasse 9, 07743, Jena, Germany.
Sabine HummertInstitut für Physiologie II, Universitätsklinikum Jena, Friedrich-Schiller-Universität Jena, Kollegiengasse 9, 07743, Jena, Germany.
Eckhard SchulzFakultät Elektrotechnik, Fachhochschule Schmalkalden, Blechhammer, 98574, Schmalkalden, Germany.
Ralf SchmauderInstitut für Physiologie II, Universitätsklinikum Jena, Friedrich-Schiller-Universität Jena, Kollegiengasse 9, 07743, Jena, Germany.
Andrea SchweinitzInstitut für Physiologie II, Universitätsklinikum Jena, Friedrich-Schiller-Universität Jena, Kollegiengasse 9, 07743, Jena, Germany.
Christopher UnzeitigInstitut für Physiologie II, Universitätsklinikum Jena, Friedrich-Schiller-Universität Jena, Kollegiengasse 9, 07743, Jena, Germany.
Frank SchwedeBIOLOG Life Science Institute GmbH & Co. KG, Flughafendamm 9A, 28199, Bremen, Germany.
Klaus BenndorfInstitut für Physiologie II, Universitätsklinikum Jena, Friedrich-Schiller-Universität Jena, Kollegiengasse 9, 07743, Jena, Germany. Klaus.Benndorf@med.uni-jena.de.
Jena University Hospital · DEFriedrich Schiller University Jena · DEBiolog Life Science Institute · DESchmalkalden University of Applied Sciences · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ionotropic purinergic (P2X) receptors are trimeric channels that are activated by the binding of ATP. They are involved in multiple physiological functions, including synaptic transmission, pain and inflammation. The mechanism of activation is still elusive. Here we kinetically unraveled and quantified subunit activation in P2X2 receptors by an extensive global fit approach with four complex and intimately coupled kinetic schemes to currents obtained from wild type and mutated receptors using ATP and its fluorescent derivative 2-[DY-547P1]-AET-ATP (fATP). We show that the steep concentration-activation relationship in wild type channels is caused by a subunit flip reaction with strong positive cooperativity, overbalancing a pronounced negative cooperativity for the three ATP binding steps, that the net probability fluxes in the model generate a marked hysteresis in the activation-deactivation cycle, and that the predicted fATP binding matches the binding measured by fluorescence. Our results shed light into the intricate activation process of P2X channels.

Indexed as

Adenosine TriphosphateHEK293 CellsHumansInflammationPainProtein BindingReceptors, Purinergic P2X2Synaptic TransmissionAdenosine TriphosphateReceptors, Purinergic P2X2

Identifiers

PMID33303878
PMCPMC7729398
OpenAlexW3111039151

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.