Evidence map›Paper›PMID 29179879›Full record

ReviewBiomedical journal2017

P2X4: A fast and sensitive purinergic receptor.

Jaanus Suurväli, Pierre Boudinot, Jean Kanellopoulos, Sirje Rüütel Boudinot

Open access · goldAbstract readReview
In one paragraph

Review in Biomedical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
96citing papers in PubMed, 2 pooled it
10.3field-weighted citation impact, top 1% 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

96 citing papers in PubMed, 2 syntheses or guidelines pooled it, 164 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Medial Olivocochlear Efferent Modulation of Cochlear Micromechanics Requires P2X4 Receptor in Outer Hair Cells.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2025
    Article
  11. Article
  12. Review
  13. Possible Roles for Purinergic Receptor P2RX4 in Breast and Prostate Cancers.International journal of molecular sciences · 2025
    Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Targeting P2X Receptors-Current Progress in Sepsis.International journal of inflammation · 2025
    Review
  19. Article
  20. Article

36 more citing papers are in PubMed but not listed here.

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 2 countries.

Jaanus SuurväliDepartment of Chemistry and Biotechnology, Tallinn University of Technology, Tallinn, Estonia.
Pierre BoudinotVirologie et Immunologie Moléculaires, INRA, Université Paris-Saclay, Jouy-en-Josas, France.
Jean KanellopoulosInstitute for Integrative Biology of the Cell (I2BC) CEA, CNRS, Univ. Paris-Sud, Université Paris-Saclay, Gif-sur-Yvette cedex, France.
Sirje Rüütel BoudinotDepartment of Chemistry and Biotechnology, Tallinn University of Technology, Tallinn, Estonia. Electronic address: sirje.boudinot@gmail.com.
Tallinn University of Technology · EEUniversité Paris-Saclay · FRUniversité Paris-Sud · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Extracellular nucleotides have been recognized as important mediators of activation, triggering multiple responses via plasma membrane receptors known as P2 receptors. P2 receptors comprise P2X ionotropic receptors and G protein-coupled P2Y receptors. P2X receptors are expressed in many tissues, where they are involved in a number of functions including synaptic transmission, muscle contraction, platelet aggregation, inflammation, macrophage activation, differentiation and proliferation, neuropathic and inflammatory pain. P2X4 is one of the most sensitive purinergic receptors (at nanomolar ATP concentrations), about one thousand times more than the archetypal P2X7. P2X4 is widely expressed in central and peripheral neurons, in microglia, and also found in various epithelial tissues and endothelial cells. It localizes on the plasma membrane, but also in intracellular compartments. P2X4 is preferentially localized in lysosomes, where it is protected from proteolysis by its glycosylation. High ATP concentration in the lysosomes does not activate P2X4 at low pH; P2X4 gets activated by intra-lysosomal ATP only in its fully dissociated tetra-anionic form, when the pH increases to 7.4. Thus, P2X4 is functioning as a Ca

Indexed as

Adenosine TriphosphateAnimalsHumansLysosomesMicrogliaReceptors, PurinergicReceptors, Purinergic P2X4Receptors, Purinergic P2X7Adenosine TriphosphateReceptors, PurinergicReceptors, Purinergic P2X4Receptors, Purinergic P2X7ATPNeuropathic painP2X4P2X receptorPurinergic signaling

Identifiers

PMID29179879
PMCPMC6138603
OpenAlexW2767901905

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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 Socratic graph.