Evidence map›Paper›PMID 9575290›Full record

ArticleThe Journal of physiology1998

The antagonist trinitrophenyl-ATP reveals co-existence of distinct P2X receptor channels in rat nodose neurones.

S Thomas, C Virginio, R A North, A Surprenant

Open access · bronzeAbstract 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 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
6.7field-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

33 citing papers in PubMed, 103 citations in OpenAlex.

  1. Endogenous forms of ATP-ATPProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Heteromeric assembly of P2X subunits.Frontiers in cellular neuroscience · 2013
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. P2X3 receptor involvement in pain states.Molecular neurobiology · 2007
    Review
  13. Pharmacology of P2X channels.Pflugers Archiv : European journal of physiology · 2006
    Review
  14. Molecular properties of P2X receptors.Pflugers Archiv : European journal of physiology · 2006
    Review
  15. Article
  16. Purinergic and vanilloid receptor activation releases glutamate from separate cranial afferent terminals in nucleus tractus solitarius.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2004
    Article
  17. Article
  18. P2X3 receptors and peripheral pain mechanisms.The Journal of physiology · 2004
    Review
  19. Pivotal role of nucleotide P2X2 receptor subunit of the ATP-gated ion channel mediating ventilatory responses to hypoxia.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2003
    Article
  20. Article
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.

S ThomasGeneva Biomedical Research Institute, GlaxoWellcome Research and Development, 14 chemin des Aulx, Plan-les-0uates, Geneva 1228, Switzerland.
C Virginio
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 rat nodose ganglion neurones in culture and from human embryonic kidney (HEK293) cells stably transfected to express P2X2, P2X3 or both receptor subunits. We examined the blocking actions of 2',3'-O-trinitrophenyl-ATP (TNP-ATP) on currents evoked by the agonists ATP and alpha, beta-methylene ATP. 2. In cells expressing only P2X2 or P2X3 receptor subunits, the inhibition by TNP-ATP was fitted by a single binding site model with half-maximal concentrations of about 3 microM and 3 nM, respectively. In cells expressing both P2X2 and P2X3 receptor subunits, currents showed little or no desensitization, thus excluding contributions from homomeric P2X3 receptors. When alpha,beta-methylene ATP was the agonist (activating heteromeric P2X2/3 receptors), the inhibition by TNP-ATP conformed to a single binding site (half-maximal concentration about 3 nM). When ATP (30 microM) was the agonist, activating both heteromeric P2X2/3 as well as homomeric P2X2 receptors, the inhibition curve was biphasic (half-maximal concentrations about 3 nM and 3 microM); the proportion of high affinity sites in all six cells tested was about 40 %. 3. In nodose ganglion neurones, the inhibition by TNP-ATP of currents evoked by ATP (30 microM) was also clearly biphasic. In this case, individual neurones showed more variability in the proportion of high and low affinity sites for TNP-ATP. 4. We conclude that more than one form of multimeric P2X receptor channels are functionally expressed on the cell bodies of individual nodose ganglion neurones. On the basis of sensitivity to TNP-ATP, and other properties, one of these may correspond to the homomeric P2X2 receptor and the other(s) to heteromeric P2X2/3 receptors.

Indexed as

Adenosine TriphosphateAnimalsCell LineEvoked PotentialsHumansKidneyMembrane PotentialsNeuronsNodose GanglionRatsReceptors, Purinergic P2Recombinant ProteinsTransfection2',3'-O-(2,4,6-trinitrophenyl)adenosine 5'-triphosphateAdenosine Triphosphatealpha,beta-methyleneadenosine 5'-triphosphateReceptors, Purinergic P2Recombinant Proteins

Identifiers

PMID9575290
PMCPMC2230974
OpenAlexW2139506271

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.