Evidence map›Paper›PMID 16423852›Full record

ArticleThe Journal of physiology2006

Pore properties and pharmacological features of the P2X receptor channel in airway ciliated cells.

Weiyuan Ma, Alon Korngreen, Simy Weil, Enbal Ben-Tal Cohen, Avi Priel, Liubov Kuzin, Shai D Silberberg

Open access · greenAbstract readComparative Study
In one paragraph

Article in The Journal of physiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
5.9field-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

37 citing papers in PubMed, 87 citations in OpenAlex.

  1. Article
  2. Animal Models for the Investigation of P2X7 Receptors.International journal of molecular sciences · 2023
    Review
  3. Article
  4. Article
  5. Differential Regulation of ATP- and UTP-Evoked Prostaglandin EJournal of immunology (Baltimore, Md. : 1950) · 2021
    Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. P2X7 Interactions and Signaling - Making Head or Tail of It.Frontiers in molecular neuroscience · 2019
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Heteromeric assembly of P2X subunits.Frontiers in cellular neuroscience · 2013
    Review
  16. Article
  17. Article
  18. Article
  19. Review
  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

7 authors at 3 institutions in 2 countries.

Weiyuan MaDepartment of Chemistry, Ben-Gurion University of the Negev, Beer-Sheva.
Alon Korngreen
Simy Weil
Enbal Ben-Tal Cohen
Avi Priel
Liubov Kuzin
Shai D Silberberg
Ben-Gurion University of the Negev · ILBar-Ilan University · ILCenter for Neurosciences · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Airway ciliated cells express an ATP-gated P2X receptor channel of unknown subunit composition (P2X(cilia)) which is modulated by Na+ and by long exposures to ATP. P2X(cilia) was investigated by recording currents from freshly dissociated rabbit airway ciliated cells with the patch-clamp technique in the whole-cell configuration. During the initial continuous exposure to extracellular ATP, P2X(cilia) currents gradually increase in magnitude (priming), yet the permeability to N-methyl-D-glucamine (NMDG) does not change, indicating that priming does not arise from a progressive change in pore diameter. Na+, which readily permeates P2X(cilia) receptor channels, was found to inhibit the channel extracellular to the electric field. The rank order of permeability to various monovalent cations is: Li+, Na+, K+, Rb+, Cs+, NMDG+ and TEA+, with a relative permeability of 1.35, 1.0, 0.99, 0.91, 0.79, 0.19 and 0.10, respectively. The rank order for the alkali cations follows an Eisenman series XI for a high-strength field site. Ca2+ has been estimated to be 7-fold more permeant than Na+. The rise in [Ca2+]i in ciliated cells, induced by the activation of P2X(cilia), is largely inhibited by either Brilliant Blue G or KN-62, indicating that P2X7 may be a part of P2X(cilia). P2X(cilia) is augmented by Zn2+ and by ivermectin, and P2X4 receptor protein is detected by immunolabelling at the basal half of the cilia, strongly suggesting that P2X4 is a component of P2X(cilia) receptor channels. Taken together, these results suggest that P2X(cilia) is either assembled from P2X4 and P2X7 subunits, or formed from modified P2X4 subunits.

Indexed as

1-(5-Isoquinolinesulfonyl)-2-MethylpiperazineAdenosine TriphosphateAnimalsCalciumCesiumCiliaEpithelial CellsIn Vitro TechniquesIon ChannelsIvermectinMaleMembrane PotentialsRabbitsReceptors, Purinergic P2Receptors, Purinergic P2XReceptors, Purinergic P2X41-(5-Isoquinolinesulfonyl)-2-MethylpiperazineAdenosine TriphosphateCalciumCesiumIon ChannelsIvermectinKN 62Receptors, Purinergic P2Receptors, Purinergic P2XReceptors, Purinergic P2X4Receptors, Purinergic P2X7Sodium

Identifiers

PMID16423852
PMCPMC1805806
OpenAlexW2172276513

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.