Evidence map›Paper›PMID 8961184›Full record

ArticleThe Journal of physiology1996

Ionic permeability of, and divalent cation effects on, two ATP-gated cation channels (P2X receptors) expressed in mammalian cells.

R J Evans, C Lewis, C Virginio, K Lundstrom, G Buell, A Surprenant, R A North

Open access · greenAbstract read
In one paragraph

Article in The Journal of physiology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers.

0numbers the graph read from it
0cells of the map it votes in
99citing papers in PubMed
7.9field-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

99 citing papers in PubMed, 255 citations in OpenAlex.

  1. Subtype-specific structural features of the hearing loss-associated human P2X2 receptor.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. The P2X1 receptor as a therapeutic target.Purinergic signalling · 2022
    Review
  7. Review
  8. Article
  9. Review
  10. 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
  11. CaThe Journal of biological chemistry · 2019
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Conductance of P2X4 purinergic receptor is determined by conformational equilibrium in the transmembrane region.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  17. Review
  18. Role of domain calcium in purinergic P2X2 receptor channel desensitization.American journal of physiology. Cell physiology · 2015
    Article
  19. Review
  20. Article

39 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

7 authors.

R J EvansGlaxo Institute for Molecular Biology, Plan-les-Ouates, Geneva, Switzerland.
C Lewis
C Virginio
K Lundstrom
G Buell
A Surprenant
R A North

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

1. Complementary DNAs for the ATP-gated ion channel subunits P2X1 (from human bladder) and P2X2 (from rat phaeochromocytoma (PC12) cells) were used to express the receptors in human embryonic kidney cells by stable transfection, and in Chinese hamster ovary cells by viral infection. 2. Membrane currents evoked by ATP were recorded by the whole-cell patch clamp method. The reversal potential of the current was measured with various intracellular and extracellular solutions and used to compute the relative permeability of the P2X receptor channels. 3. There was no difference between the two receptors with respect to their permeability to monovalent organic cations. The relative permeabilities (PX/PNa) were 2.3, 1.0, 1.0, 0.95, 0.72, 0.5, 0.29, 0.16, 0.04 and 0.03 for guanidinium, potassium, sodium, methylamine, caesium, dimethylamine, 2-methylethanolamine, tris(hydroxymethyl)-aminomethane, tetraethylammonium and N-methyl-D-glucamine, respectively (values for P2X2 receptor). 4. The calcium permeability of P2X1 receptors was greater than that of P2X2 receptors. Under biionic conditions (112 mM calcium outside, 154 mM sodium inside), PCa/PNa values were 3.9 and 2.2, respectively (corrected for ionic activities). 5. ATP-evoked currents in cells expressing the P2X2 receptor were strongly inhibited when the extracellular calcium concentration was increased (0.3-30 mM); the action of ATP could be restored by increasing the ATP concentration. ATP-evoked currents in cells expressing the P2X1 receptor were not inhibited by such increases in the extracellular calcium concentration.

Indexed as

Adenosine TriphosphateAnimalsBiological TransportCalciumCations, DivalentCations, MonovalentDNA, ComplementaryElectrophysiologyHumansIon Channel GatingMuscle, SmoothPC12 CellsRatsReceptors, Purinergic P2TransfectionUrinary BladderAdenosine TriphosphateCalciumCations, DivalentCations, MonovalentDNA, ComplementaryReceptors, Purinergic P2

Identifiers

PMID8961184
PMCPMC1160993
OpenAlexW1969906502

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.