Evidence map›Paper›PMID 38570597›Full record

ArticleScientific reports2024

Cloning, functional expression, and pharmacological characterization of inwardly rectifying potassium channels (Kir) from Apis mellifera.

Fabien Sourisseau, Chaimaa Chahine, Valérie Pouliot, Thierry Cens, Pierre Charnet, Mohamed Chahine

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Review
  2. Article
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

6 authors at 3 institutions in 2 countries.

Fabien SourisseauCERVO Brain Research Centre, 2601, chemin de la Canardière, Quebec City, QC, G1J 2G3, Canada.
Chaimaa ChahineCERVO Brain Research Centre, 2601, chemin de la Canardière, Quebec City, QC, G1J 2G3, Canada.
Valérie PouliotCERVO Brain Research Centre, 2601, chemin de la Canardière, Quebec City, QC, G1J 2G3, Canada.
Thierry CensInstitut des Biomolécules Max Mousseron (IBMM), CNRS UMR 5247, 1919 Route de Mende, Montpellier, France.
Pierre CharnetInstitut des Biomolécules Max Mousseron (IBMM), CNRS UMR 5247, 1919 Route de Mende, Montpellier, France.
Mohamed ChahineCERVO Brain Research Centre, 2601, chemin de la Canardière, Quebec City, QC, G1J 2G3, Canada. Mohamed.Chahine@phc.ulaval.ca.
Institut Universitaire en Santé Mentale de Québec · CACentre National de la Recherche Scientifique · FRUniversité Laval · CA

Funding

Agence Nationale de la Recherche ANR-20-CE34-0017-01Natural Sciences and Engineering Research Council of Canada RGPIN-2020-06359NSERC Alliance International Catalyst grant 572132-2022
6 · The paper itself

Abstract

Potassium channels belong to the super family of ion channels and play a fundamental role in cell excitability. Kir channels are potassium channels with an inwardly rectifying property. They play a role in setting the resting membrane potential of many excitable cells including neurons. Although putative Kir channel family genes can be found in the Apis mellifera genome, their functional expression, biophysical properties, and sensitivity to small molecules with insecticidal activity remain to be investigated. We cloned six Kir channel isoforms from Apis mellifera that derive from two Kir genes, AmKir1 and AmKir2, which are present in the Apis mellifera genome. We studied the tissue distribution, the electrophysiological and pharmacological characteristics of three isoforms that expressed functional currents (AmKir1.1, AmKir2.2, and AmKir2.3). AmKir1.1, AmKir2.2, and AmKir2.3 isoforms exhibited distinct characteristics when expressed in Xenopus oocytes. AmKir1.1 exhibited the largest potassium currents and was impermeable to cesium whereas AmKir2.2 and AmKir2.3 exhibited smaller currents but allowed cesium to permeate. AmKir1 exhibited faster opening kinetics than AmKir2. Pharmacological experiments revealed that both AmKir1.1 and AmKir2.2 are blocked by the divalent ion barium, with IC

Indexed as

Potassium Channels, Inwardly RectifyingAnimalsBeesCesiumCloning, MolecularMembrane PotentialsPotassiumProtein IsoformsCesiumPotassiumPotassium Channels, Inwardly RectifyingProtein IsoformsApis melliferaCloningExpressionInsecticidesInsectsKir channelsPotassium channelsVU041

Identifiers

PMID38570597
PMCPMC10991380
OpenAlexW4393858335

What OpenQuestion holds

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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.