Evidence map›Paper›PMID 28559187›Full record

ReviewBiochimica et biophysica acta. Biomembranes2018

Gap junction gene and protein families: Connexins, innexins, and pannexins.

Eric C Beyer, Viviana M Berthoud

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta. Biomembranes, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 120 papers.

0numbers the graph read from it
0cells of the map it votes in
120citing papers in PubMed
5.7field-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

120 citing papers in PubMed, 224 citations in OpenAlex.

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60 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

Eric C BeyerDepartment of Pediatrics, University of Chicago, Chicago, IL 60637, United States. Electronic address: ecbeyer@uchicago.edu.
Viviana M BerthoudDepartment of Pediatrics, University of Chicago, Chicago, IL 60637, United States.
University of Chicago · US

Funding

BIOLOGY OF LENS INTERCELLULAR COMMUNICATIONR01EY008368 · NEI · WASHINGTON UNIVERSITY · PI BEYER, ERIC C · 1995 to 2018
$7.1M
NEI NIH HHS R01 EY008368
6 · The paper itself

Abstract

Gap junction channels facilitate the intercellular exchange of ions and small molecules. While this process is critical to all multicellular organisms, the proteins that form gap junction channels are not conserved. Vertebrate gap junctions are formed by connexins, while invertebrate gap junctions are formed by innexins. Interestingly, vertebrates and lower chordates contain innexin homologs, the pannexins, which also form channels, but rarely (if ever) make intercellular channels. While the connexin and the innexin/pannexin polypeptides do not share significant sequence similarity, all three of these protein families share a similar membrane topology and some similarities in quaternary structure. This article is part of a Special Issue entitled: Gap Junction Proteins edited by Jean Claude Herve.

Indexed as

AnimalsConnexinsGap JunctionsHumansIon TransportConnexinsConnexinInnexinPannexin

Identifiers

PMID28559187
PMCPMC5704981
OpenAlexW2620198502

What OpenQuestion holds

Textmetadata
LicenceTDM
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.