Evidence map›Paper›PMID 15548662›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2004

Time-resolved measurement of state-specific P2X2 ion channel cytosolic gating motions.

James A Fisher, Gemma Girdler, Baljit S Khakh

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

30 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Dilation of ion selectivity filters in cation channels.Trends in biochemical sciences · 2024
    Review
  3. Review
  4. 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
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Review
  13. Review
  14. Article
  15. P2X2 and P2X5 subunits define a new heteromeric receptor with P2X7-like properties.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012
    Article
  16. 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
  17. Article
  18. Review
  19. 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

3 authors at 2 institutions in 1 country.

James A FisherMedical Research Council Laboratory of Molecular Biology, Cambridge CB2 2QH, United Kingdom.
Gemma Girdler
Baljit S Khakh
MRC Laboratory of Molecular Biology · GBMedical Research Council · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ATP-gated P2X2 channels undergo permeability changes through a process that is incompletely understood. In the present study, we used fluorescence resonance energy transfer (FRET) and electrophysiology to measure cytosolic gating motions in P2X2 channels as they enter a state with increased permeability. P2X2 channels underwent permeability changes with a time course that was similar to decreases in FRET between cyan fluorescent protein and yellow fluorescent protein attached to the cytosolic domain of P2X2 channels. Wild-type and mutant channels that did not undergo permeability changes also did not show evidence of cytosolic gating motions. Moreover, immobilizing the cytosolic domain by tethering it to the plasma membrane prevented the switch in permeability and impaired the cytosolic gating motions. Both of these phenotypes were restored when the immobilizing tether was cleaved. The data provide a time-resolved measure of state-specific gating motions and suggest how a cytosolic domain may control ion channel permeability.

Indexed as

Bacterial ProteinsCell LineCytosolFluorescence Resonance Energy TransferFluorescent DyesGreen Fluorescent ProteinsHumansIon Channel GatingIon ChannelsLuminescent ProteinsMutationPatch-Clamp TechniquesProtein ConformationProtein SubunitsReceptors, Purinergic P2Receptors, Purinergic P2X2Bacterial ProteinsCyan Fluorescent ProteinFluorescent DyesGreen Fluorescent ProteinsIon ChannelsLuminescent ProteinsP2RX2 protein, humanProtein SubunitsReceptors, Purinergic P2Receptors, Purinergic P2X2yellow fluorescent protein, Bacteria

Identifiers

PMID15548662
PMCPMC6730295
OpenAlexW2166577131

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.