Evidence map›Paper›PMID 18247022›Full record

ReviewEuropean biophysics journal : EBJ2009

Orthosteric and allosteric binding sites of P2X receptors.

R J Evans

Open access · hybridAbstract readReview
PubMed Publisher
In one paragraph

Review in European biophysics journal : EBJ, 2009. 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
5.4field-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

32 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Exploring the ATP-binding site of P2X receptors.Frontiers in cellular neuroscience · 2013
    Review
  10. Heteromeric assembly of P2X subunits.Frontiers in cellular neuroscience · 2013
    Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Allosteric modulation of purine and pyrimidine receptors.Advances in pharmacology (San Diego, Calif.) · 2011
    Review
  18. Review
  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

1 author at 1 institution in 1 country.

R J EvansDepartment of Cell Physiology and Pharmacology, University of Leicester, Leicester LE19HN, UK. rje6@le.ac.uk
University of Leicester · GB

Funding

British Heart FoundationWellcome Trust
6 · The paper itself

Abstract

P2X receptors for ATP comprise a distinct family of ligand gated ion channels with a range of properties. They have been shown to be involved in a variety of physiological processes including blood clotting, sensory perception, pain sensation, bone formation as well as inflammation and may provide a number of novel drug targets. In addition to the orthosteric site for ATP binding it has been suggested that there may be additional allosteric sites that regulate agonist action at the receptor. There is currently no crystal structure available for P2X receptors and the lack of sequence similarity to other ATP binding proteins has meant that a mutagenesis-based approach has been used primarily to investigate receptor structure-function. This review aims to provide an overview of recent work that gives an insight into residues involved in ATP action and allosteric regulation.

Indexed as

Models, MolecularAdenosine TriphosphateAllosteric SiteAmino Acid SequenceAnimalsBinding SitesHumansIon Channel GatingMolecular Sequence DataProtein ConformationReceptors, Purinergic P2Receptors, Purinergic P2XAdenosine TriphosphateReceptors, Purinergic P2Receptors, Purinergic P2X

Identifiers

PMID18247022
OpenAlexW1980224706

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.