Evidence map›Paper›PMID 23322038›Full record

ArticleNature communications2013

Multiple pore conformations driven by asynchronous movements of voltage sensors in a eukaryotic sodium channel.

Marcel P Goldschen-Ohm, Deborah L Capes, Kevin M Oelstrom, Baron Chanda

Open access · hybridAbstract read
In one paragraph

Article in Nature communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

63 citing papers in PubMed, 102 citations in OpenAlex.

  1. Trial
  2. Electrostatic tuning of NaThe Journal of physiology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Harnessing AlphaFold to reveal hERG channel conformational state secrets.bioRxiv : the preprint server for biology · 2025
    Article
  7. Article
  8. Voltage sensors.Molecular pharmacology · 2025
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Bioelectricity and molecular signaling.Biophysical journal · 2024
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

3 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

4 authors at 2 institutions in 1 country.

Marcel P Goldschen-OhmDepartment of Neuroscience, University of Wisconsin, Madison, Wisconsin 53706, USA.
Deborah L Capes
Kevin M Oelstrom
Baron Chanda
University of Wisconsin–Madison · USHarvard University · US

Funding

Structural basis of modulation of Na+ channels by local anestheticsR01GM084140 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI CHANDA, BARON · 2008 to 2016
$3.3M
Thermodynamics and Energetics of voltage-gated ion channelsR01NS081293 · NINDS · WASHINGTON UNIVERSITY · PI CHANDA, BARON · 2012 to 2019
$2.9M
NIGMS NIH HHS GM084140-01NIGMS NIH HHS R01 GM084140NINDS NIH HHS R01 NS081293
6 · The paper itself

Abstract

Voltage-dependent Na(+) channels are crucial for electrical signalling in excitable cells. Membrane depolarization initiates asynchronous movements in four non-identical voltage-sensing domains of the Na(+) channel. It remains unclear to what extent this structural asymmetry influences pore gating as compared with outwardly rectifying K(+) channels, where channel opening results from a final concerted transition of symmetric pore gates. Here we combine single channel recordings, cysteine accessibility and voltage clamp fluorimetry to probe the relationships between voltage sensors and pore conformations in an inactivation deficient Nav1.4 channel. We observe three distinct conductance levels such that DI-III voltage sensor activation is kinetically correlated with formation of a fully open pore, whereas DIV voltage sensor movement underlies formation of a distinct subconducting pore conformation preceding inactivation in wild-type channels. Our experiments reveal that pore gating in sodium channels involves multiple transitions driven by asynchronous movements of voltage sensors. These findings shed new light on the mechanism of coupling between activation and fast inactivation in voltage-gated sodium channels.

Indexed as

AnimalsEukaryotaHEK293 CellsHumansIon Channel GatingKineticsMesylatesModels, BiologicalMuscle ProteinsMutant ProteinsMutationProtein Structure, TertiaryProtein TransportRatsSodium ChannelsTime Factors(2-(trimethylammonium)ethyl)methanethiosulfonateMesylatesMuscle ProteinsMutant ProteinsScn4a protein, ratSodium Channels

Identifiers

PMID23322038
PMCPMC3562458
OpenAlexW2050472057

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.