Evidence map›Paper›PMID 20977449›Full record

ReviewBritish journal of pharmacology2010

Structural interpretation of P2X receptor mutagenesis studies on drug action.

Richard J Evans

Open access · bronzeAbstract readReview
In one paragraph

Review in British journal of pharmacology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
8.7field-weighted citation impact, top 2% 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

32 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. P2YPurinergic signalling · 2018
    Article
  3. Article
  4. P2X receptors.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2016
    Review
  5. Review
  6. Review
  7. Article
  8. Review
  9. Review
  10. Exploring the ATP-binding site of P2X receptors.Frontiers in cellular neuroscience · 2013
    Review
  11. Heteromeric assembly of P2X subunits.Frontiers in cellular neuroscience · 2013
    Review
  12. P2X receptor intermediate activation states have altered nucleotide selectivity.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  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

1 author at 1 institution in 1 country.

Richard J EvansCell Physiology & Pharmacology, University of Leicester, Leicester, UK. rje6@le.ac.uk
University of Leicester · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

P2X receptors for ATP are ligand gated cation channels that form from the trimeric assembly of subunits with two transmembrane segments, a large extracellular ligand binding loop, and intracellular amino and carboxy termini. The receptors are expressed throughout the body, involved in functions ranging from blood clotting to inflammation, and may provide important targets for novel therapeutics. Mutagenesis based studies have been used to develop an understanding of the molecular basis of their pharmacology with the aim of developing models of the ligand binding site. A crystal structure for the zebra fish P2X4 receptor in the closed agonist unbound state has been published recently, which provides a major advance in our understanding of the receptors. This review gives an overview of mutagenesis studies that have led to the development of a model of the ATP binding site, as well as identifying residues contributing to allosteric regulation and antagonism. These studies are discussed with reference to the crystal to provide a structural interpretation of the molecular basis of drug action.

Indexed as

Models, MolecularMutagenesisAdenosine TriphosphateAllosteric RegulationAnimalsBinding SitesHumansLigandsProtein BindingProtein ConformationReceptors, Purinergic P2XReceptors, Purinergic P2X4Adenosine TriphosphateLigandsReceptors, Purinergic P2XReceptors, Purinergic P2X4

Identifiers

PMID20977449
PMCPMC2972645
OpenAlexW2149322003

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.