Evidence map›Paper›PMID 24367083›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Optical control of trimeric P2X receptors and acid-sensing ion channels.

Liam E Browne, João P M Nunes, Joan A Sim, Vijay Chudasama, Laricia Bragg, Stephen Caddick, R Alan North

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
5.6field-weighted citation impact, top 4% 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

26 citing papers in PubMed, 58 citations in OpenAlex.

  1. Review
  2. Article
  3. Optical control of PIEZO1 channels.Nature communications · 2023
    Article
  4. Article
  5. Optical control of purinergic signaling.Purinergic signalling · 2021
    Review
  6. Article
  7. Review
  8. Review
  9. Review
  10. Article
  11. Review
  12. Review
  13. Article
  14. 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
  15. Article
  16. Article
  17. P2X receptors.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2016
    Review
  18. Article
  19. Review
  20. Review
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 2 institutions in 1 country.

Liam E BrowneFaculty of Life Sciences and Faculty of Medical and Human Sciences, University of Manchester, Manchester M13 9PL, United Kingdom.
João P M Nunes
Joan A Sim
Vijay Chudasama
Laricia Bragg
Stephen Caddick
R Alan North
University College London · GBUniversity of Manchester · GB

Funding

Biotechnology and Biological Sciences Research Council BB/J010448Wellcome TrustWellcome Trust 093140/Z/10/Z
6 · The paper itself

Abstract

P2X receptors are trimeric membrane proteins that function as ion channels gated by extracellular ATP. We have engineered a P2X2 receptor that opens within milliseconds by irradiation at 440 nm, and rapidly closes at 360 nm. This requires bridging receptor subunits via covalent attachment of 4,4'-bis(maleimido)azobenzene to a cysteine residue (P329C) introduced into each second transmembrane domain. The cis-trans isomerization of the azobenzene pushes apart the outer ends of the transmembrane helices and opens the channel in a light-dependent manner. Light-activated channels exhibited similar unitary currents, rectification, calcium permeability, and dye uptake as P2X2 receptors activated by ATP. P2X3 receptors with an equivalent mutation (P320C) were also light sensitive after chemical modification. They showed typical rapid desensitization, and they could coassemble with native P2X2 subunits in pheochromocytoma cells to form light-activated heteromeric P2X2/3 receptors. A similar approach was used to open and close human acid-sensing ion channels (ASICs), which are also trimers but are unrelated in sequence to P2X receptors. The experiments indicate that the opening of the permeation pathway requires similar and substantial movements of the transmembrane helices in both P2X receptors and ASICs, and the method will allow precise optical control of P2X receptors or ASICs in intact tissues.

Indexed as

LightAdenosine TriphosphateAmino Acid SequenceAnimalsAzo CompoundsElectrophysiologyGene Expression Regulation, NeoplasticIon Channel GatingIon ChannelsIonsLigandsMicroscopy, ConfocalModels, MolecularMolecular ConformationMolecular Sequence DataMutagenesis, Site-DirectedAdenosine TriphosphateazobenzeneAzo CompoundsIon ChannelsIonsLigandsReceptors, Purinergic P2X2Receptors, Purinergic P2X3

Identifiers

PMID24367083
PMCPMC3890850
OpenAlexW2085824541

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.