Evidence map›Paper›PMID 19005548›Full record

ArticleNature2008

Deconstructing voltage sensor function and pharmacology in sodium channels.

Frank Bosmans, Marie-France Martin-Eauclaire, Kenton J Swartz

Abstract read
In one paragraph

Article in Nature, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 159 papers.

0numbers the graph read from it
0cells of the map it votes in
159citing 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

159 citing papers in PubMed.

  1. Electrostatic tuning of NaThe Journal of physiology · 2026
    Article
  2. Article
  3. Modular architecture of KEMBO reports · 2025
    Review
  4. Structural basis of inhibition of human NaNature communications · 2025
    Article
  5. Review
  6. A structural atlas of druggable sites on NaChannels (Austin, Tex.) · 2024
    Review
  7. Article
  8. Structural basis of inhibition of human NabioRxiv : the preprint server for biology · 2024
    Article
  9. Review
  10. Article
  11. Frontiers in molecular neuroscience · 2023
    Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Pharmacological Inhibition of the Voltage-Gated Sodium Channel NaACS pharmacology & translational science · 2021
    Article

99 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors.

Frank BosmansMolecular Physiology and Biophysics Section, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, Maryland 20892, USA.
Marie-France Martin-Eauclaire
Kenton J Swartz

Funding

Gating mechanisms and pharmacology of sodium and calcium channelsZIANS003017 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI SWARTZ, KENTON · 2009 to 2014
$3.3M
Intramural NIH HHS ZIA NS003017
6 · The paper itself

Abstract

Voltage-activated sodium (Na(v)) channels are crucial for the generation and propagation of nerve impulses, and as such are widely targeted by toxins and drugs. The four voltage sensors in Na(v) channels have distinct amino acid sequences, raising fundamental questions about their relative contributions to the function and pharmacology of the channel. Here we use four-fold symmetric voltage-activated potassium (K(v)) channels as reporters to examine the contributions of individual S3b-S4 paddle motifs within Na(v) channel voltage sensors to the kinetics of voltage sensor activation and to forming toxin receptors. Our results uncover binding sites for toxins from tarantula and scorpion venom on each of the four paddle motifs in Na(v) channels, and reveal how paddle-specific interactions can be used to reshape Na(v) channel activity. One paddle motif is unique in that it slows voltage sensor activation, and toxins selectively targeting this motif impede Na(v) channel inactivation. This reporter approach and the principles that emerge will be useful in developing new drugs for treating pain and Na(v) channelopathies.

Indexed as

Amino Acid MotifsAnimalsIon Channel GatingModels, MolecularMutagenesisPotassium Channels, Voltage-GatedProtein Interaction Domains and MotifsRatsRecombinant Fusion ProteinsScorpion VenomsSodium ChannelsSpider VenomsXenopusPotassium Channels, Voltage-GatedRecombinant Fusion ProteinsScorpion VenomsSodium ChannelsSpider Venoms

Identifiers

PMID19005548
PMCPMC2587061

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.