Evidence map›Paper›PMID 30542154›Full record

ArticleNature2018

Structure of native lens connexin 46/50 intercellular channels by cryo-EM.

Janette B Myers, Bassam G Haddad, Susan E O'Neill, Dror S Chorev, Craig C Yoshioka, Carol V Robinson, Daniel M Zuckerman, Steve L Reichow

Open access · greenAbstract read
In one paragraph

Article in Nature, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 102 papers.

0numbers the graph read from it
0cells of the map it votes in
102citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

102 citing papers in PubMed, 166 citations in OpenAlex.

  1. Article
  2. Article
  3. COeLife · 2026
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Connexin50 hemichannels are opened by COFrontiers in physiology · 2026
    Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. A mechanism of CALHM1 ion channel gating.American journal of physiology. Cell physiology · 2025
    Article
  16. Article
  17. Article
  18. Article
  19. Model-based evaluation of connexin hemichannel permeability.Computational and structural biotechnology journal · 2025
    Article
  20. Review

42 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

8 authors at 3 institutions in 2 countries.

Janette B MyersDepartment of Chemistry, Portland State University, Portland, OR, USA.
Bassam G HaddadDepartment of Chemistry, Portland State University, Portland, OR, USA.
Susan E O'NeillDepartment of Chemistry, Portland State University, Portland, OR, USA.
Dror S ChorevPhysical and Theoretical Chemistry Laboratory, University of Oxford, Oxford, UK.
Craig C YoshiokaDepartment of Biomedical Engineering, Oregon Health and Science University, Portland, OR, USA.
Carol V RobinsonPhysical and Theoretical Chemistry Laboratory, University of Oxford, Oxford, UK.
Daniel M ZuckermanDepartment of Biomedical Engineering, Oregon Health and Science University, Portland, OR, USA.
Steve L ReichowDepartment of Chemistry, Portland State University, Portland, OR, USA. reichow@pdx.edu.
Portland State University · USOregon Health & Science University · USUniversity of Oxford · GB

Funding

Dynamic Mechanisms of Membrane Channel Gating by CryoEMR35GM124779 · NIGMS · PORTLAND STATE UNIVERSITY · PI Stephen Loen Reichow · 2017 to 2026
$4.2M
NIGMS NIH HHS R35 GM124779
6 · The paper itself

Abstract

Gap junctions establish direct pathways for cell-to-cell communication through the assembly of twelve connexin subunits that form intercellular channels connecting neighbouring cells. Co-assembly of different connexin isoforms produces channels with unique properties and enables communication across cell types. Here we used single-particle cryo-electron microscopy to investigate the structural basis of connexin co-assembly in native lens gap junction channels composed of connexin 46 and connexin 50 (Cx46/50). We provide the first comparative analysis to connexin 26 (Cx26), which-together with computational studies-elucidates key energetic features governing gap junction permselectivity. Cx46/50 adopts an open-state conformation that is distinct from the Cx26 crystal structure, yet it appears to be stabilized by a conserved set of hydrophobic anchoring residues. 'Hot spots' of genetic mutations linked to hereditary cataract formation map to the core structural-functional elements identified in Cx46/50, suggesting explanations for many of the disease-causing effects.

Indexed as

Cryoelectron MicroscopyAmino Acid SequenceCataractConnexin 26Connexin 50ConnexinsGap JunctionsHumansLens, CrystallineModels, MolecularMutationConnexin 26Connexin 50ConnexinsGJA3 protein, human

Identifiers

PMID30542154
PMCPMC6309215
OpenAlexW2904888175

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.