Evidence map›Paper›PMID 19236918›Full record

ArticleJournal of structural biology2009

The M34A mutant of Connexin26 reveals active conductance states in pore-suspending membranes.

Oliver Gassmann, Mohamed Kreir, Cinzia Ambrosi, Jennifer Pranskevich, Atsunori Oshima, Christian Röling, Gina Sosinsky, Niels Fertig, Claudia Steinem

Abstract read
In one paragraph

Article in Journal of structural biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–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

14 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Cell-free expression of a functional pore-only sodium channel.Protein expression and purification · 2015
    Article
  5. Article
  6. Article
  7. Review
  8. Lipid-bilayer-spanning DNA nanopores with a bifunctional porphyrin anchor.Angewandte Chemie (International ed. in English) · 2013
    Article
  9. Permeation of calcium through purified connexin 26 hemichannels.The Journal of biological chemistry · 2012
    Article
  10. Article
  11. Article
  12. Voltage-gated sodium channel (NaV) protein dissection creates a set of functional pore-only proteins.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  13. Article
  14. Article
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

9 authors.

Oliver GassmannInstitute for Organic and Biomolecular Chemistry, University of Göttingen, Germany.
Mohamed Kreir
Cinzia Ambrosi
Jennifer Pranskevich
Atsunori Oshima
Christian Röling
Gina Sosinsky
Niels Fertig
Claudia Steinem

Funding

VOLUMETRIC CONTOUR-BASED SURFACE RECONSTRUCTIONP41RR004050 · NCRR · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI PASQUALE, ELENA B · 1989 to 2011
$28.0M
STRUCTURE AND DYNAMICS OF CONNEXIN26 GAP JUNCTIONSR01GM065937 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI PERKINS, GUY A · 2003 to 2016
$3.9M
STRUCTURAL ANALYSIS OF GAP JUNCTION TRAFFICKINGR01GM072881 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI PERKINS, GUY A · 2005 to 2015
$2.6M
NCRR NIH HHS P41 RR004050NCRR NIH HHS RR04050NIGMS NIH HHS GM065937NIGMS NIH HHS GM072881NIGMS NIH HHS R01 GM065937NIGMS NIH HHS R01 GM072881
6 · The paper itself

Abstract

Connexin26 (Cx26) is a member of the connexin family, the building blocks for gap junction intercellular channels. These dodecameric assemblies are involved in gap junction-mediated cell-cell communication allowing the passage of ions and small molecules between two neighboring cells. Mutations in Cx26 lead to the disruption of gap junction-mediated intercellular communication with consequences such as hearing loss and skin disorders. We show here that a mutant of Cx26, M34A, forms an active hemichannel in lipid bilayer experiments. A comparison with the Cx26 wild-type is presented. Two different techniques using micro/nano-structured substrates for the formation of pore-suspending lipid membranes are used. We reconstituted the Cx26 wild-type and Cx26M34A into artificial lipid bilayers and observed single channel activity for each technique, with conductance levels of around 35, 70 and 165 pS for the wild-type. The conductance levels of Cx26M34A were found at around 45 and 70 pS.

Indexed as

AnimalsCell LineConnexin 26ConnexinsGap JunctionsHumansLipid BilayersMutationRatsConnexin 26ConnexinsGJB2 protein, humanLipid Bilayers

Identifiers

PMID19236918
PMCPMC2785080

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.