Evidence map›Paper›PMID 10639098›Full record

ArticleThe Journal of physiology2000

Inactivation of P2X2 purinoceptors by divalent cations.

S Ding, F Sachs

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of physiology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.8field-weighted citation impact, top 7% 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

23 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Article
  3. Localization of the gate and selectivity filter of the full-length P2X7 receptor.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  4. Role of domain calcium in purinergic P2X2 receptor channel desensitization.American journal of physiology. Cell physiology · 2015
    Article
  5. Review
  6. Heteromeric assembly of P2X subunits.Frontiers in cellular neuroscience · 2013
    Review
  7. Review
  8. Review
  9. Article
  10. Receptor and channel heteromers as pain targets.Pharmaceuticals (Basel, Switzerland) · 2012
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Biophysics of P2X receptors.Pflugers Archiv : European journal of physiology · 2006
    Review
  20. Bimodal action of protons on ATP currents of rat PC12 cells.The Journal of general physiology · 2003
    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

2 authors at 1 institution in 1 country.

S DingDepartments of Chemical Engineering and Physiology and Biophysics, State University of New York at Buffalo, Buffalo, NY 14214, USA.
F Sachs
University at Buffalo, State University of New York · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

1. P2X2 channels are activated by extracellular ATP. Despite being commonly described as non-desensitizing, P2X2 receptors do desensitize or inactivate. In the unspliced, 472 amino acid isoform of the P2X2 receptor, inactivation required membrane disruption and the presence of extracellular Ca2+. 2. The ability to inactivate whole-cell currents developed slowly after breaking in. In contrast, currents from excised patches exhibited rapid (approximately 100 ms) inactivation with a dependence on extracellular Ca2+, ATP and voltage. 3. The inactivation rate increased with the fourth power of [Ca2+] suggesting that the functional channel may be a tetramer. Ca2+ had both a higher affinity and a larger Hill coefficient for inactivation than Mg2+, Ba2+ or Mn2+. Trivalent cations at concentrations up to the solubility product of ATP had no effect. The change in apparent co-operativity with ionic species suggests the presence of experimentally unresolved ligand-insensitive kinetic steps. 4. Based on the weak voltage dependence of inactivation and the lack of effect of intracellular Ca2+ buffers, the Ca2+-binding sites are probably located near the extracellular surface of the membrane. 5. The recovery from inactivation was slow, with a time constant of approximately 7 min. 6. Ca2+-sensitive inactivation only appeared when the membrane was disrupted in some manner. Treatment with actin and microtubule reagents did not induce inactivation, suggesting that an intact cytoskeleton is not necessary. 7. Inactivation rates observed in different patch configurations suggest that the induction of Ca2+-dependent inactivation was due to the loss of a diffusible cofactor located in the membrane or the cytoplasm.

Indexed as

Purinergic P2 Receptor AntagonistsActinsAdenosine TriphosphateAlgorithmsCalciumCations, DivalentCell LineCytoskeletonElectric StimulationElectrophysiologyHumansIon Channel GatingKineticsMembrane PotentialsMicrotubulesPatch-Clamp TechniquesActinsAdenosine TriphosphateCalciumCations, DivalentP2RX2 protein, humanPurinergic P2 Receptor AntagonistsReceptors, Purinergic P2X2

Identifiers

PMID10639098
PMCPMC2269756
OpenAlexW2039721829

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.