Evidence map›Paper›PMID 35897750›Full record

ReviewInternational journal of molecular sciences2022

Alternatively Spliced Isoforms of the P2X7 Receptor: Structure, Function and Disease Associations.

Sophie K F De Salis, Lanxin Li, Zheng Chen, Kam Wa Lam, Kristen K Skarratt, Thomas Balle, Stephen J Fuller

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

22 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
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  11. Role of P2X7R in Retinal Diseases: A Review.Immunity, inflammation and disease · 2025
    Review
  12. Article
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  15. 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

7 authors at 1 institution in 1 country.

Sophie K F De SalisSydney Pharmacy School, Faculty of Medicine and Health, The University of Sydney, Sydney, NSW 2006, Australia.
Lanxin LiSydney Medical School Nepean, Faculty of Medicine and Health, The University of Sydney, Nepean Hospital, Penrith, NSW 2750, Australia.
Zheng ChenSydney Pharmacy School, Faculty of Medicine and Health, The University of Sydney, Sydney, NSW 2006, Australia.ORCID 0000-0003-0607-0483
Kam Wa LamSydney Medical School Nepean, Faculty of Medicine and Health, The University of Sydney, Nepean Hospital, Penrith, NSW 2750, Australia.
Kristen K SkarrattSydney Medical School Nepean, Faculty of Medicine and Health, The University of Sydney, Nepean Hospital, Penrith, NSW 2750, Australia.ORCID 0000-0003-4971-2773
Thomas BalleSydney Pharmacy School, Faculty of Medicine and Health, The University of Sydney, Sydney, NSW 2006, Australia.
Stephen J FullerSydney Medical School Nepean, Faculty of Medicine and Health, The University of Sydney, Nepean Hospital, Penrith, NSW 2750, Australia.ORCID 0000-0003-4637-7391
The University of Sydney · AU

Funding

Nepean Medical Research Foundation 2018
6 · The paper itself

Abstract

The P2X7 receptor (P2X7R) is an ATP-gated membrane ion channel that is expressed by multiple cell types. Following activation by extracellular ATP, the P2X7R mediates a broad range of cellular responses including cytokine and chemokine release, cell survival and differentiation, the activation of transcription factors, and apoptosis. The P2X7R is made up of three P2X7 subunits that contain specific domains essential for the receptor's varied functions. Alternative splicing produces P2X7 isoforms that exclude one or more of these domains and assemble in combinations that alter P2X7R function. The modification of the structure and function of the P2X7R may adversely affect cellular responses to carcinogens and pathogens, and alternatively spliced (AS) P2X7 isoforms have been associated with several cancers. This review summarizes recent advances in understanding the structure and function of AS P2X7 isoforms and their associations with cancer and potential role in modulating the inflammatory response.

Indexed as

NeoplasmsReceptors, Purinergic P2X7Adenosine TriphosphateCytokinesHumansProtein IsoformsAdenosine TriphosphateCytokinesProtein IsoformsReceptors, Purinergic P2X7alternative splicingATPcancerinflammationP2X7R

Identifiers

PMID35897750
PMCPMC9329894
OpenAlexW4287838975

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.