Evidence map›Paper›PMID 34129834›Full record

ArticleStructure (London, England : 1993)2021

Cryo-EM structure of an open conformation of a gap junction hemichannel in lipid bilayer nanodiscs.

Ali K Khan, Maciej Jagielnicki, Brad C Bennett, Michael D Purdy, Mark Yeager

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. A mechanism of CALHM1 ion channel gating.American journal of physiology. Cell physiology · 2025
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. A Quantitative Assay for CaInternational journal of molecular sciences · 2022
    Article
  15. Connexin Mutations and Hereditary Diseases.International journal of molecular sciences · 2022
    Review
  16. Review
  17. Review
  18. Article
  19. 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

5 authors.

Ali K KhanDepartment of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Sheridan G. Snyder Translational Research Building, Rm 320, 480 Ray C. Hunt Drive, Charlottesville, VA 22908, USA.
Maciej JagielnickiDepartment of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Sheridan G. Snyder Translational Research Building, Rm 320, 480 Ray C. Hunt Drive, Charlottesville, VA 22908, USA.
Brad C BennettDepartment of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Sheridan G. Snyder Translational Research Building, Rm 320, 480 Ray C. Hunt Drive, Charlottesville, VA 22908, USA.
Michael D PurdyDepartment of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Sheridan G. Snyder Translational Research Building, Rm 320, 480 Ray C. Hunt Drive, Charlottesville, VA 22908, USA.
Mark YeagerDepartment of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Sheridan G. Snyder Translational Research Building, Rm 320, 480 Ray C. Hunt Drive, Charlottesville, VA 22908, USA; Center for Membrane Biology, University of Virginia School of Medicine, Charlottesville, VA 22908, USA; Cardiovascular Research Center, University of Virginia School of Medicine, Charlottesville, VA 22908, USA; Department of Medicine, Division of Cardiovascular Medicine, University of Virginia School of Medicine, Charlottesville, VA 22908, USA. Electronic address: yeager@virginia.edu.

Funding

Resource for Biocomputing Visualization and InformaticsP41GM103311 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2012 to 2017
$8.2M
Structure and Dynamics of Gap Junction ChannelsR01HL048908 · NHLBI · UNIVERSITY OF VIRGINIA · PI YEAGER, MARK JAY · 1994 to 2013
$5.1M
Molecular Electron Microscopy Core Facility ImprovementsG20RR031199 · NCRR · UNIVERSITY OF VIRGINIA · PI SHUPNIK, MARGARET A · 2010 to 2010
$2.0M
300 keV Liquid Helium Robotic MicroscopeS10RR025067 · NCRR · UNIVERSITY OF VIRGINIA · PI EGELMAN, EDWARD H. · 2009 to 2009
$2.0M
Structural Biology of Connexin Membrane ChannelsR01GM138532 · NIGMS · UNIVERSITY OF VIRGINIA · PI YEAGER, MARK JAY · 2020 to 2023
$1.9M
Direct Electron Detector for a Titan Krios Robotic Electron Cryo-MicroscopeS10OD018149 · OD · UNIVERSITY OF VIRGINIA · PI EGELMAN, EDWARD H., YEAGER, MARK JAY · 2014 to 2014
$500k
NCRR NIH HHS G20 RR031199NCRR NIH HHS S10 RR025067NHLBI NIH HHS R01 HL048908NIGMS NIH HHS P41 GM103311NIGMS NIH HHS R01 GM138532NIH HHS S10 OD018149
6 · The paper itself

Abstract

To mediate cell-to-cell communication via gap junction channels (GJCs), connexins (Cx) traffic as hexameric hemichannels to the plasma membrane, which dock end-to-end between adjacent cell membranes, thereby forming a dodecameric intercellular conduit. Hemichannels also function independently to mediate the passage of contents between the cytoplasm and extracellular space. To generate hemichannels, the mutation N176Y was introduced into the second extracellular loop of Cx26. The electron cryomicroscopy structure of the hexameric hemichannel in lipid bilayer nanodiscs displays an open pore and a 4-helix bundle transmembrane design that is nearly identical to dodecameric GJCs. In contrast to the high resolution of the transmembrane α-helices, the extracellular loops are less well resolved. The conformational flexibility of the extracellular loops may be essential to facilitate surveillance of hemichannels in apposed cells to identify compatible Cx isoforms that enable intercellular docking. Our results also provide a structural foundation for previous electrophysiologic and permeation studies of Cx hemichannels.

Indexed as

Connexin 26HumansLipid BilayersMolecular Dynamics SimulationProtein Conformation, alpha-HelicalConnexin 26GJB2 protein, humanLipid Bilayersconnexinscryo-EMgap junction hemichannelsmembrane proteinsprotein structure

Identifiers

PMID34129834
PMCPMC9616683

What OpenQuestion holds

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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.