Evidence map›Paper›PMID 25512599›Full record

ReviewThe Journal of general physiology2015

Structural model of the open-closed-inactivated cycle of prokaryotic voltage-gated sodium channels.

Claire Bagnéris, Claire E Naylor, Emily C McCusker, B A Wallace

Open access · bronzeAbstract readReview
In one paragraph

Review in The Journal of general physiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

32 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Proton Quantum Tunneling: Influence and Relevance to Acidosis-Induced Cardiac Arrhythmias/Cardiac Arrest.Pathophysiology : the official journal of the International Society for Pathophysiology · 2021
    Article
  9. Article
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  13. Review
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  19. The discovery of a potent NaMedChemComm · 2017
    Article
  20. Ion channels and ion selectivity.Essays in biochemistry · 2017
    Review
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

4 authors at 2 institutions in 1 country.

Claire BagnérisInstitute of Structural and Molecular Biology, Birkbeck College, University of London, London WC1E 7HX, England, UK.
Claire E NaylorInstitute of Structural and Molecular Biology, Birkbeck College, University of London, London WC1E 7HX, England, UK.
Emily C McCuskerInstitute of Structural and Molecular Biology, Birkbeck College, University of London, London WC1E 7HX, England, UK.
B A WallaceInstitute of Structural and Molecular Biology, Birkbeck College, University of London, London WC1E 7HX, England, UK b.wallace@mail.cryst.bbk.ac.uk.
Birkbeck, University of London · GBInstitute of Structural and Molecular Biology · GB

Funding

Biotechnology and Biological Sciences Research Council
6 · The paper itself

Abstract

In excitable cells, the initiation of the action potential results from the opening of voltage-gated sodium channels. These channels undergo a series of conformational changes between open, closed, and inactivated states. Many models have been proposed for the structural transitions that result in these different functional states. Here, we compare the crystal structures of prokaryotic sodium channels captured in the different conformational forms and use them as the basis for examining molecular models for the activation, slow inactivation, and recovery processes. We compare structural similarities and differences in the pore domains, specifically in the transmembrane helices, the constrictions within the pore cavity, the activation gate at the cytoplasmic end of the last transmembrane helix, the C-terminal domain, and the selectivity filter. We discuss the observed differences in the context of previous models for opening, closing, and inactivation, and present a new structure-based model for the functional transitions. Our proposed prokaryotic channel activation mechanism is then compared with the activation transition in eukaryotic sodium channels.

Indexed as

Ion Channel GatingAmino Acid SequenceBacterial ProteinsMolecular Dynamics SimulationMolecular Sequence DataVoltage-Gated Sodium ChannelsBacterial ProteinsVoltage-Gated Sodium Channels

Identifiers

PMID25512599
PMCPMC4278185
OpenAlexW2108793171

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.