Evidence map›Paper›PMID 23426683›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2013

P2X7 receptor channels allow direct permeation of nanometer-sized dyes.

Liam E Browne, Vincent Compan, Laricia Bragg, R Alan North

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.

0numbers the graph read from it
0cells of the map it votes in
93citing papers in PubMed
16.1field-weighted citation impact, top 1% 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

93 citing papers in PubMed, 151 citations in OpenAlex.

  1. Molecular mechanisms of NLRP3 inflammasome activation.Experimental & molecular medicine · 2026
    Review
  2. Review
  3. Article
  4. Article
  5. Role of P2X7R in Retinal Diseases: A Review.Immunity, inflammation and disease · 2025
    Review
  6. Article
  7. Role of PScientific reports · 2025
    Article
  8. Article
  9. Dilation of ion selectivity filters in cation channels.Trends in biochemical sciences · 2024
    Review
  10. Review
  11. Article
  12. Review
  13. Untangling Macropore Formation and Current Facilitation in P2X7.International journal of molecular sciences · 2023
    Review
  14. Genetically-encoded BRET probes shed light on ligand bias-induced variable ion selectivity in TRPV1 and P2X5/7.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  15. Review
  16. Reviews in cardiovascular medicine · 2022
    Review
  17. Review
  18. Article
  19. Review
  20. Review

33 more citing papers are in PubMed but not listed here.

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 at 1 institution in 1 country.

Liam E BrowneFaculty of Medical and Human Sciences, and Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, United Kingdom.
Vincent Compan
Laricia Bragg
R Alan North
University of Manchester · GB

Funding

Wellcome TrustWellcome Trust 093Wellcome Trust 140/Z/10/Z
6 · The paper itself

Abstract

P2X receptors are widely distributed in the nervous system, and P2X7 receptors have roles in neuropathic pain and in the release of cytokines from microglia. They are trimeric membrane proteins, which open an integral ion channel when ligated by extracellular ATP. This channel is preferentially permeable to small cations (sodium, potassium, calcium) but also allows permeation of larger cations such as N-methyl-d-glucamine. ATP also leads to entry of fluorescent dyes in many cells expressing P2X7 receptors, but controversy persists as to whether such large molecules pass directly through the open ion channel or enter the cell by a different route. We measured cellular fluorescence and membrane currents in individual human embryonic kidney cells expressing rat P2X7 receptors. Introduction of positive side chains by mutagenesis into the inner half of the pore-forming second transmembrane domain of the receptor (T348K, D352N, D352K) increased relative permeability of chloride ions. It also promoted entry of the large (>1 nm) negative dye fluorescein-5-isothiocyanate while decreasing entry of the structurally similar but positive dye ethidium. Furthermore, larger cysteine-reactive methanethiosulfonates [sulforhodamine-methanethiosulfonate and 2-((biotinoyl)amino)ethyl methanethiosulfonate] reduced both ATP-evoked currents and dye entry when applied to open P2X7[G345C] receptors. The results demonstrate that the open channel of the P2X7 receptor can allow passage of molecules with sizes up to 1.4 nm.

Indexed as

Cell Membrane PermeabilityNanoparticlesParticle SizeAnimalsFluorescent DyesHEK293 CellsHumansRatsReceptors, Purinergic P2X7Fluorescent DyesP2rx7 protein, ratReceptors, Purinergic P2X7

Identifiers

PMID23426683
PMCPMC6619550
OpenAlexW2078156178

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.