Evidence map›Paper›PMID 28389651›Full record

ArticleScientific reports2017

Unique residues in the ATP gated human P2X7 receptor define a novel allosteric binding pocket for the selective antagonist AZ10606120.

Rebecca C Allsopp, Sudad Dayl, Ralf Schmid, Richard J Evans

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed, 1 pooled it
6.5field-weighted citation impact, top 3% 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

47 citing papers in PubMed, 1 synthesis or guideline pooled it, 84 citations in OpenAlex.

  1. Pooled it
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  16. P2XScience advances · 2024
    Article
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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 2 institutions in 2 countries.

Rebecca C AllsoppDepartment of Molecular and Cell Biology, University of Leicester, Leicester, UK.
Sudad DaylDepartment of Molecular and Cell Biology, University of Leicester, Leicester, UK.
Ralf SchmidDepartment of Molecular and Cell Biology, University of Leicester, Leicester, UK.
Richard J EvansDepartment of Molecular and Cell Biology, University of Leicester, Leicester, UK. rje6@le.ac.uk.
University of Leicester · GBUniversity of Baghdad · IQ

Funding

Medical Research Council MR/K027018/1
6 · The paper itself

Abstract

The P2X7 receptor (P2X7R) for ATP is a therapeutic target for pathophysiological states including inflammation, pain management and epilepsy. This is facilitated by the predicted low side effect profile as the high concentrations of ATP required to activate the receptor are usually only found following cell damage/disease and so P2X7Rs respond to a "danger" signal and are not normally active. AZ10606120 is a selective antagonist for P2X7Rs (IC

Indexed as

Allosteric SiteBinding SitesIon Channel GatingAdamantaneAdenosine TriphosphateAllelesAllosteric RegulationAmino Acid SequenceAmino Acid SubstitutionAminoquinolinesHumansLignansModels, MolecularMolecular ConformationMutationProtein BindingAdamantaneAdenosine TriphosphateAminoquinolinesAZ10606120LignansPurinergic P2X Receptor AntagonistsReceptors, Purinergic P2X7

Identifiers

PMID28389651
PMCPMC5429621
OpenAlexW2604255566

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.