Evidence map›Paper›PMID 9625864›Full record

ArticleThe Journal of physiology1998

Calcium permeability and block at homomeric and heteromeric P2X2 and P2X3 receptors, and P2X receptors in rat nodose neurones.

C Virginio, R A North, A Surprenant

Open access · greenAbstract read
In one paragraph

Article in The Journal of physiology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
6.0field-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

45 citing papers in PubMed, 124 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Hearing loss mutations alter the functional properties of human P2X2 receptor channels through distinct mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  5. Article
  6. Article
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  10. Pain-enhancing mechanism through interaction between TRPV1 and anoctamin 1 in sensory neurons.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  11. Review
  12. Structural and molecular modeling features of P2X receptors.International journal of molecular sciences · 2014
    Review
  13. Principles and properties of ion flow in P2X receptors.Frontiers in cellular neuroscience · 2014
    Review
  14. Review
  15. Two open states of P2X receptor channels.Frontiers in cellular neuroscience · 2013
    Review
  16. Subtype-specific control of P2X receptor channel signaling by ATP and Mg2+.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  17. Review
  18. Article
  19. Article
  20. 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

3 authors.

C VirginioGeneva Biomedical Research Institute, Glaxo Wellcome Research and Development, 14 chemin des Aulx, 1228 Plan-les-Ouates, Geneva, Switzerland. cv49987@ggr.co.uk
R A North
A Surprenant

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

1. Whole-cell recordings were made from HEK 293 (human embryonic kidney) cells stably transfected with cDNAs encoding P2X2, P2X3 or both receptors (P2X2/3) and from cultured rat nodose neurones. Nodose neurones all showed immunoreactivity for both P2X2 and P2X3, but not P2X1, receptors. 2. Reversal potentials were measured in extracellular sodium, N-methyl-D-glucamine (NMDG) and NMDG containing 5 mM Ca2+; the values were used to compute relative permeabilities (PNMDG/PNa and PCa/PNa). PNMDG/PNa was not different for P2X2, P2X2/3 and nodose neurones (0.03) but was significantly higher (0.07) for P2X3 receptors. PCa/PNa was not different among P2X3, P2X2/3 and nodose neurones (1.2-1.5) but was significantly higher (2.5) for P2X2 receptors. 3. External Ca2+ inhibited purinoceptor currents with half-maximal concentrations of 5 mM at the P2X2 receptor, 89 mM at the P2X3 receptor and 15 mM at both the P2X2/3 heteromeric receptor and nodose neurones. In each case, the inhibition was voltage independent and was overcome by increasing concentrations of agonist. 4. These results may indicate that Ca2+ permeability of the heteromeric (P2X2/3) channel is dominated by that of the P2X3 subunit, while Ca2+ block of the receptor involves both P2X2 and P2X3 subunits. The correspondence in properties between P2X2/3 receptors and nodose ganglion neurones further supports the conclusion that the native alpha,beta-methylene ATP-sensitive receptor is a P2X2/3 heteromultimer.

Indexed as

AnimalsCalciumCells, CulturedElectric ConductivityHumansNeuronsNodose GanglionPermeabilityPurinergic P2 Receptor AntagonistsRatsReceptors, Purinergic P2CalciumPurinergic P2 Receptor AntagonistsReceptors, Purinergic P2

Identifiers

PMID9625864
PMCPMC2231016
OpenAlexW2035201936

What OpenQuestion holds

Textmetadata
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.