Evidence map›Paper›PMID 23033078›Full record

ArticleNature communications2012

Structure of a bacterial voltage-gated sodium channel pore reveals mechanisms of opening and closing.

Emily C McCusker, Claire Bagnéris, Claire E Naylor, Ambrose R Cole, Nazzareno D'Avanzo, Colin G Nichols, B A Wallace

Abstract read
In one paragraph

Article in Nature communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 154 papers.

0numbers the graph read from it
0cells of the map it votes in
154citing 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

154 citing papers in PubMed.

  1. Voltage-Gated Sodium Channel NaBiochemical genetics · 2026
    Article
  2. Article
  3. HInternational journal of molecular sciences · 2025
    Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Microbial membrane transport proteins and their biotechnological applications.World journal of microbiology & biotechnology · 2024
    Review
  9. Review
  10. Article
  11. Ion channel selectivity through ion-modulated changes of selectivity filter pProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Review

94 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

7 authors.

Emily C McCuskerDepartment of Crystallography, Institute of Structural and Molecular Biology, Birkbeck College, University of London, Malet Street, London WC1E 7HX, UK.
Claire Bagnéris
Claire E Naylor
Ambrose R Cole
Nazzareno D'Avanzo
Colin G Nichols
B A Wallace

Funding

Rectification &Block of Ion Channel CurrentsR01HL054171 · NHLBI · WASHINGTON UNIVERSITY · PI NICHOLS, COLIN G · 1995 to 2017
$4.5M
Biotechnology and Biological Sciences Research Council BB/H01070X/1NHLBI NIH HHS HL54171NHLBI NIH HHS R01 HL054171
6 · The paper itself

Abstract

Voltage-gated sodium channels are vital membrane proteins essential for electrical signalling; in humans, they are key targets for the development of pharmaceutical drugs. Here we report the crystal structure of an open-channel conformation of NavMs, the bacterial channel pore from the marine bacterium Magnetococcus sp. (strain MC-1). It differs from the recently published crystal structure of a closed form of a related bacterial sodium channel (NavAb) by having its internal cavity accessible to the cytoplasmic surface as a result of a bend/rotation about a central residue in the carboxy-terminal transmembrane segment. This produces an open activation gate of sufficient diameter to allow hydrated sodium ions to pass through. Comparison of the open and closed structures provides new insight into the features of the functional states present in the activation cycles of sodium channels and the mechanism of channel opening and closing.

Indexed as

Amino Acid SequenceBacterial ProteinsCircular DichroismMolecular Sequence DataProtein Structure, SecondaryProtein Structure, TertiaryStructure-Activity RelationshipVoltage-Gated Sodium ChannelsBacterial ProteinsVoltage-Gated Sodium Channels

Identifiers

PMID23033078
PMCPMC3493636

What OpenQuestion holds

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LicenceCC BY-NC-SA
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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.