Evidence map›Paper›PMID 33029714›Full record

ArticlePurinergic signalling2020

Contribution of Val/Ile87 residue in the extracellular domain in agonist-induced current responses of the human and rat P2X7 receptors.

Emily A Caseley, Stephen P Muench, Lin-Hua Jiang

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Purinergic signalling, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.5field-weighted citation impact, top 34% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. 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

3 authors at 1 institution in 1 country.

Emily A CaseleyLeeds Institute of Rheumatic and Musculoskeletal Medicine, St James's University Hospital, Faculty of Medicine and Health, Leeds, UK.
Stephen P MuenchSchool of Biomedical Sciences, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 JT, UK.
Lin-Hua JiangSchool of Biomedical Sciences, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 JT, UK. l.h.jiang@leeds.ac.uk.ORCID 0000-0001-6398-0411
University of Leeds · GB

Funding

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

Abstract

The P2X7 receptor (P2X7R) is an ATP-gated cation channel with a critical role in many physiological and pathological processes, and shows prominent functional differences across mammalian species, exemplified by larger current responses of the rat (r) P2X7R to ATP and its analogue BzATP and a greater sensitivity to agonists compared with the human (h) P2X7R. Here, we showed that substitution of Val87 residue in the extracellular domain of the hP2X7R with isoleucine in the rP2X7R increased the current responses of the hP2X7R to both ATP and BzATP. Conversely, introduction of reciprocal I87V mutation in the rP2X7R led to a noticeable but statistically insignificant reduction in the current responses of the rP2X7R to ATP and BzATP. The mutations did not affect the sensitivity of the human and rat P2X7Rs to ATP and BzATP. These results suggest a contribution of Val/Ile87 in agonist-induced current responses of human and rat P2X7Rs, which helps to better understand the molecular determinants for species-dependent function of the mammalian P2X7Rs.

Indexed as

AnimalsHEK293 CellsHumansMutationRatsReceptors, Purinergic P2X7Receptors, Purinergic P2X7Agonist-induced currentsP2X7 receptorSpecies differenceWhole-cell recording

Identifiers

PMID33029714
PMCPMC7855165
OpenAlexW3091786251

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.