Evidence map›Paper›PMID 20869590›Full record

ReviewNeuron2010

Ion channel voltage sensors: structure, function, and pathophysiology.

William A Catterall

Abstract readReview
In one paragraph

Review in Neuron, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 283 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
283citing papers in PubMed, 1 pooled it
–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

283 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Scalable Crackle-Lithography for Multifunctional Enclosed Plastic Nanofluidic Devices.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Targeting NaInternational journal of molecular sciences · 2026
    Review
  11. Review
  12. Molecular Determinants of Voltage-Dependent Gating in Kv11.1 Channels.Advances in experimental medicine and biology · 2026
    Review
  13. Article
  14. Article
  15. Review
  16. Structure reveals a regulation mechanism of plant outward-rectifying KProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  17. Review
  18. Article
  19. Article
  20. Article

223 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

1 author.

William A CatterallDepartment of Pharmacology, University of Washington, Seattle, WA 98195-7280, USA. wcatt@u.washington.edu

Funding

VOLTAGE-SENSITIVE SODIUM CHANNELS IN BRAINR01NS015751 · NINDS · UNIVERSITY OF WASHINGTON · PI CATTERALL, WILLIAM A · 1985 to 2018
$6.0M
Receptor Sites and Antagonists for Paralytic NeurotoxinsU01NS058039 · NINDS · UNIVERSITY OF WASHINGTON · PI CATTERALL, WILLIAM A · 2006 to 2010
$3.1M
NINDS NIH HHS R01 NS015751NINDS NIH HHS R01 NS15751NINDS NIH HHS U01 NS058039
6 · The paper itself

Abstract

Voltage-gated ion channels generate electrical signals in species from bacteria to man. Their voltage-sensing modules are responsible for initiation of action potentials and graded membrane potential changes in response to synaptic input and other physiological stimuli. Extensive structure-function studies, structure determination, and molecular modeling are now converging on a sliding-helix mechanism for electromechanical coupling in which outward movement of gating charges in the S4 transmembrane segments catalyzed by sequential formation of ion pairs pulls the S4-S5 linker, bends the S6 segment, and opens the pore. Impairment of voltage-sensor function by mutations in Na+ channels contributes to several ion channelopathies, and gating pore current conducted by mutant voltage sensors in Na(V)1.4 channels is the primary pathophysiological mechanism in hypokalemic periodic paralysis. The emerging structural model for voltage sensor function opens the way to development of a new generation of ion-channel drugs that act on voltage sensors rather than blocking the pore.

Indexed as

Amino Acid SequenceAnimalsHumansIon Channel GatingIon ChannelsMembrane PotentialsModels, MolecularNervous System DiseasesProtein Structure, TertiaryStructure-Activity RelationshipIon Channels

Identifiers

PMID20869590
PMCPMC2950829

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.