Evidence map›Paper›PMID 12149275›Full record

ArticleThe Journal of general physiology2002

Control of P2X(2) channel permeability by the cytosolic domain.

Angela N Eickhorst, Amy Berson, Debra Cockayne, Henry A Lester, Baljit S Khakh

Open access · greenAbstract read
In one paragraph

Article in The Journal of general physiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.2field-weighted citation impact, top 15% 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

34 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
  2. Dilation of ion selectivity filters in cation channels.Trends in biochemical sciences · 2024
    Review
  3. Review
  4. Intercellular CaThe Journal of physiology · 2019
    Article
  5. Article
  6. Article
  7. On the permeation of large organic cations through the pore of ATP-gated P2X receptors.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Two open states of P2X receptor channels.Frontiers in cellular neuroscience · 2013
    Review
  13. P2X receptors as drug targets.Molecular pharmacology · 2013
    Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Neuronal P2X2 receptors are mobile ATP sensors that explore the plasma membrane when activated.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011
    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

5 authors at 2 institutions in 2 countries.

Angela N EickhorstMRC Laboratory of Molecular Biology, Cambridge CB2 2QH, United Kingdom.
Amy Berson
Debra Cockayne
Henry A Lester
Baljit S Khakh
California Institute of Technology · USMRC Laboratory of Molecular Biology · GB

Funding

NICOTINIC SYNAPSES, BIOPHYSICAL STUDIESR01NS011756 · NINDS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI LESTER, HENRY A. · 1985 to 2009
$3.4M
NINDS NIH HHS NS-11756NINDS NIH HHS R01 NS011756Wellcome Trust
6 · The paper itself

Abstract

ATP-gated P2X channels are the simplest of the three families of transmitter-gated ion channels. Some P2X channels display a time- and activation-dependent change in permeability as they undergo the transition from the relatively Na(+)-selective I(1) state to the I(2) state, which is also permeable to organic cations. We report that the previously reported permeability change of rat P2X(2) (rP2X(2)) channels does not occur at mouse P2X(2) (mP2X(2)) channels expressed in oocytes. Domain swaps, species chimeras, and point mutations were employed to determine that two specific amino acid residues in the cytosolic tail domain govern this difference in behavior between the two orthologous channels. The change in pore diameter was characterized using reversal potential measurements and excluded field theory for several organic ions; both rP2X(2) and mP2X(2) channels have a pore diameter of approximately 11 A in the I(1) state, but the transition to the I(2) state increases the rP2X(2) diameter by at least 3 A. The I(1) to I(2) transition occurs with a rate constant of approximately 0.5 s(-1). The data focus attention on specific residues of P2X(2) channel cytoplasmic domains as determinants of permeation in a state-specific manner.

Indexed as

AnimalsCytosolIon ChannelsMiceModels, BiologicalOocytesPermeabilityProtein Structure, TertiaryRatsReceptors, Purinergic P2Receptors, Purinergic P2X2Xenopus laevisIon ChannelsP2rx2 protein, mouseP2rx2 protein, ratReceptors, Purinergic P2Receptors, Purinergic P2X2

Identifiers

PMID12149275
PMCPMC2234464
OpenAlexW2159605545

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.