Evidence map›Paper›PMID 33987781›Full record

ReviewPurinergic signalling2021

Structural basis for the functional properties of the P2X7 receptor for extracellular ATP.

Lin-Hua Jiang, Emily A Caseley, Steve P Muench, Sébastien Roger

Abstract readReview
In one paragraph

Review in Purinergic signalling, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

38 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
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  18. Journal of Parkinson's disease · 2024
    Article
  19. Review
  20. P2X7 Variants in Pathophysiology.International journal of molecular sciences · 2024
    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

4 authors.

Lin-Hua JiangSchool of Biomedical Sciences, Faculty of Biological Sciences, University of Leeds, Leeds, UK. l.h.jiang@leeds.ac.uk.ORCID 0000-0001-6398-0411
Emily A CaseleySchool of Biomedical Sciences, Faculty of Biological Sciences, University of Leeds, Leeds, UK.
Steve P MuenchSchool of Biomedical Sciences, Faculty of Biological Sciences, University of Leeds, Leeds, UK.
Sébastien RogerEA4245, Transplantation, Immunology and Inflammation, Faculty of Medicine, University of Tours, Tours, France.

Funding

Biotechnology and Biological Sciences Research Council BB/C517317/1Wellcome Trust 099758/Z/12/Z
6 · The paper itself

Abstract

The P2X7 receptor, originally known as the P2Z receptor due to its distinctive functional properties, has a structure characteristic of the ATP-gated ion channel P2X receptor family. The P2X7 receptor is an important mediator of ATP-induced purinergic signalling and is involved the pathogenesis of numerous conditions as well as in the regulation of diverse physiological functions. Functional characterisations, in conjunction with site-directed mutagenesis, molecular modelling, and, recently, structural determination, have provided significant insights into the structure-function relationships of the P2X7 receptor. This review discusses the current understanding of the structural basis for the functional properties of the P2X7 receptor.

Indexed as

Adenosine TriphosphateAmino Acid SequenceAnimalsBinding SitesExtracellular FluidHumansProtein Structure, SecondaryReceptors, Purinergic P2X7Adenosine TriphosphateReceptors, Purinergic P2X7Agonist bindingAntagonismIon permeationLarge pore formationReceptor activation

Identifiers

PMID33987781
PMCPMC8410900

What OpenQuestion holds

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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.