Evidence map›Paper›PMID 33897694›Full record

ReviewFrontiers in immunology2021

Structural and Functional Features of the P2X4 Receptor: An Immunological Perspective.

Jean M Kanellopoulos, Cássio Luiz Coutinho Almeida-da-Silva, Sirje Rüütel Boudinot, David M Ojcius

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in immunology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
7.2field-weighted citation impact, top 2% 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

33 citing papers in PubMed, 58 citations in OpenAlex.

  1. Review
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  7. Genetic Deletion of the Purinergic ReceptorACS pharmacology & translational science · 2025
    Article
  8. Possible Roles for Purinergic Receptor P2RX4 in Breast and Prostate Cancers.International journal of molecular sciences · 2025
    Review
  9. Article
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  14. Review
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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

4 authors at 3 institutions in 3 countries.

Jean M KanellopoulosInstitute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Saclay, Gif-sur-Yvette, France.
Cássio Luiz Coutinho Almeida-da-SilvaDepartment of Biomedical Sciences, University of the Pacific, Arthur A. Dugoni School of Dentistry, San Francisco, CA, United States.
Sirje Rüütel BoudinotDepartment of Chemistry and Biotechnology, Tallinn University of Technology, Tallinn, Estonia.
David M OjciusDepartment of Biomedical Sciences, University of the Pacific, Arthur A. Dugoni School of Dentistry, San Francisco, CA, United States.
University of the Pacific · USCEA Paris-Saclay · FRTallinn University of Technology · EE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Extracellular nucleotides are important mediators of activation, triggering various responses through plasma membrane P2 and P1 receptors. P2 receptors are further subdivided into ionotropic P2X receptors and G protein-coupled P2Y receptors. P2X4 is an ATP-gated cation channel broadly expressed in most tissues of the body. Within the P2X family, P2X4 has a unique subcellular distribution, being preferentially localized in lysosomes. In these organelles, high ATP concentrations do not trigger P2X4 because of the low pH. However, when the pH increases to 7.4, P2X4 can be stimulated by intra-lysosomal ATP, which is in its active, tetra-anionic form. Elucidation of P2X4, P2X3 and P2X7 structures has shed some light on the functional differences between these purinergic receptors. The potential interaction between P2X4 and P2X7 has been extensively studied. Despite intensive effort, it has not been possible yet to determine whether P2X4 and P2X7 interact as heterotrimers or homotrimers at the plasma membrane. However, several publications have shown that functional interactions between P2X4 and P2X7 do occur. Importantly, these studies indicate that P2X4 potentiates P2X7-dependent activation of inflammasomes, leading to increased release of IL-1β and IL-18. The role of P2X4 in various diseases could be beneficial or deleterious even though the pathophysiological mechanisms involved are still poorly defined. However, in diseases whose physiopathology involves activation of the NLRP3 inflammasome, P2X4 was found to exacerbate severity of disease. The recent production of monoclonal antibodies specific for the human and mouse P2X4, some of which are endowed with agonist or antagonist properties, raises the possibility that they could be used therapeutically. Analysis of single nucleotide polymorphisms of the human

Indexed as

AnimalsAntibodies, MonoclonalCell DegranulationEncephalomyelitis, Autoimmune, ExperimentalEthanolHumansInflammasomesInflammationMast CellsPurinergic P2X Receptor AntagonistsReceptors, Antigen, T-CellReceptors, Purinergic P2X4Receptors, Purinergic P2X7Antibodies, MonoclonalEthanolInflammasomesPurinergic P2X Receptor AntagonistsReceptors, Antigen, T-CellReceptors, Purinergic P2X4Receptors, Purinergic P2X7anti-P2X4 mAbATPinflammasomeinnate immunityNLRP3P2X4 receptorP2X7 receptorpurinergic receptor

Identifiers

PMID33897694
PMCPMC8059410
OpenAlexW3149264931

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.