Evidence map›Paper›PMID 20227116›Full record

ReviewTrends in pharmacological sciences2010

New structure enlivens interest in P2X receptors.

Liam E Browne, Lin-Hua Jiang, R Alan North

Open access · hybridAbstract readReview
In one paragraph

Review in Trends in pharmacological sciences, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed
17.1field-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

80 citing papers in PubMed, 149 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Identification of a distinct desensitisation gate in the ATP-gated P2X2 receptor.Biochemical and biophysical research communications · 2020
    Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Review
  14. ATP-induced CaCellular and molecular life sciences : CMLS · 2017
    Review
  15. Article
  16. 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
  17. Localization of the gate and selectivity filter of the full-length P2X7 receptor.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  18. Article
  19. Article
  20. Article

20 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

3 authors at 2 institutions in 1 country.

Liam E BrowneFaculty of Medical and Human Sciences, University of Manchester, UK.
Lin-Hua Jiang
R Alan North
University of Manchester · GBUniversity of Leeds · GB

Funding

Biotechnology and Biological Sciences Research Council BB/C517317/1
6 · The paper itself

Abstract

P2X receptors are ATP-gated membrane ion channels with multifarious roles, including afferent sensation, autocrine feedback loops, and inflammation. Their molecular operation has been less well elucidated compared with other ligand-gated channels (nicotinic acetylcholine receptors, ionotropic glutamate receptors). This will change with the recent publication of the crystal structure of a closed P2X receptor. Here we re-interpret results from 15 years of experiments using site-directed mutagenesis with a model based on the new structure. Previous predictions of receptor stoichiometry, the extracellular ATP binding site, inter-subunit contacts, and many details of the permeation pathway fall into place in three dimensions. We can therefore quickly understand how the channel operates at the molecular level. This is important not only for ion- channel aficionados, but also those engaged in developing effective antagonists at P2X receptors for potential therapeutic use.

Indexed as

Models, MolecularAdenosine TriphosphateAnimalsBinding SitesHumansMutagenesis, Site-DirectedPermeabilityProtein BindingProtein ConformationReceptors, Purinergic P2Receptors, Purinergic P2XAdenosine TriphosphateReceptors, Purinergic P2Receptors, Purinergic P2X

Identifiers

PMID20227116
PMCPMC2954318
OpenAlexW2128354701

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.