Evidence map›Paper›PMID 34207150›Full record

ArticleInternational journal of molecular sciences2021

P2X7 Receptors and TMEM16 Channels Are Functionally Coupled with Implications for Macropore Formation and Current Facilitation.

Kate Dunning, Adeline Martz, Francisco Andrés Peralta, Federico Cevoli, Eric Boué-Grabot, Vincent Compan, Fanny Gautherat, Patrick Wolf, Thierry Chataigneau, Thomas Grutter

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2021. 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
2.1field-weighted citation impact, top 15% 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, 22 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. Review
  7. Untangling Macropore Formation and Current Facilitation in P2X7.International journal of molecular sciences · 2023
    Review
  8. Purinergic P2 Receptors: Structure and Function 2.0.International journal of molecular sciences · 2023
    Article
  9. Article
  10. Article
  11. Review
  12. Review
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

10 authors at 1 institution in 1 country.

Kate DunningCNM Team, Centre National de la Recherche Scientifique, CAMB UMR 7199, Faculté de Pharmacie, Université de Strasbourg, 67401 Illkirch, France.ORCID 0000-0001-9811-7087
Adeline MartzCNM Team, Centre National de la Recherche Scientifique, CAMB UMR 7199, Faculté de Pharmacie, Université de Strasbourg, 67401 Illkirch, France.
Francisco Andrés PeraltaCNM Team, Centre National de la Recherche Scientifique, CAMB UMR 7199, Faculté de Pharmacie, Université de Strasbourg, 67401 Illkirch, France.ORCID 0000-0002-0727-1706
Federico CevoliCNM Team, Centre National de la Recherche Scientifique, CAMB UMR 7199, Faculté de Pharmacie, Université de Strasbourg, 67401 Illkirch, France.
Eric Boué-GrabotInstitut des Maladies Neurodégénératives, Université de Bordeaux, UMR 5293, 33000 Bordeaux, France.ORCID 0000-0003-2187-9037
Vincent CompanInstitut de Génomique Fonctionnelle (IGF), Université de Montpellier, CNRS, INSERM, 34094 Montpellier, France.
Fanny GautheratCNM Team, Centre National de la Recherche Scientifique, CAMB UMR 7199, Faculté de Pharmacie, Université de Strasbourg, 67401 Illkirch, France.
Patrick WolfCNM Team, Centre National de la Recherche Scientifique, CAMB UMR 7199, Faculté de Pharmacie, Université de Strasbourg, 67401 Illkirch, France.ORCID 0000-0002-1557-4811
Thierry ChataigneauCNM Team, Centre National de la Recherche Scientifique, CAMB UMR 7199, Faculté de Pharmacie, Université de Strasbourg, 67401 Illkirch, France.
Thomas GrutterCNM Team, Centre National de la Recherche Scientifique, CAMB UMR 7199, Faculté de Pharmacie, Université de Strasbourg, 67401 Illkirch, France.
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

P2X7 receptors (P2X7) are cationic channels involved in many diseases. Following their activation by extracellular ATP, distinct signaling pathways are triggered, which lead to various physiological responses such as the secretion of pro-inflammatory cytokines or the modulation of cell death. P2X7 also exhibit unique behaviors, such as "macropore" formation, which corresponds to enhanced large molecule cell membrane permeability and current facilitation, which is caused by prolonged activation. These two phenomena have often been confounded but, thus far, no clear mechanisms have been resolved. Here, by combining different approaches including whole-cell and single-channel recordings, pharmacological and biochemical assays, CRISPR/Cas9 technology and cell imaging, we provide evidence that current facilitation and macropore formation involve functional complexes comprised of P2X7 and TMEM16, a family of Ca

Indexed as

Adenosine TriphosphateAlgorithmsAnimalsAnoctaminsCell MembraneCell Membrane PermeabilityCholesterolCRISPR-Cas SystemsHEK293 CellsHumansImmunohistochemistryModels, BiologicalOocytesReceptors, Purinergic P2X7Adenosine TriphosphateAnoctaminsCholesterolReceptors, Purinergic P2X7anoctaminATP sensitizationcell permeabilizationion channelP2X7purinergic receptor

Identifiers

PMID34207150
PMCPMC8234106
OpenAlexW3176633792

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.