Evidence map›Paper›PMID 22538811›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Tracking a complete voltage-sensor cycle with metal-ion bridges.

Ulrike Henrion, Jakob Renhorn, Sara I Börjesson, Erin M Nelson, Christine S Schwaiger, Pär Bjelkmar, Björn Wallner, Erik Lindahl, Fredrik Elinder

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 100 papers.

0numbers the graph read from it
0cells of the map it votes in
100citing papers in PubMed
7.4field-weighted citation impact, top 2% 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

100 citing papers in PubMed, 143 citations in OpenAlex.

  1. Voltage-sensing domains: structural and functional diversity.European biophysics journal : EBJ · 2026
    Review
  2. Article
  3. Review
  4. Voltage sensors.Molecular pharmacology · 2025
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Fifty years of gating currents and channel gating.The Journal of general physiology · 2023
    Review
  11. Article
  12. Mechanism of voltage gating in the voltage-sensing phosphatase Ci-VSP.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  13. Article
  14. Review
  15. Article
  16. Autism-associated mutations in KProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  17. Review
  18. Article
  19. Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 1 country.

Ulrike HenrionDivision of Cell Biology, Department of Clinical and Experimental Medicine, Linköping University, SE-581 85 Linköping, Sweden.
Jakob Renhorn
Sara I Börjesson
Erin M Nelson
Christine S Schwaiger
Pär Bjelkmar
Björn Wallner
Erik Lindahl
Fredrik Elinder
Linköping University · SEKTH Royal Institute of Technology · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Voltage-gated ion channels open and close in response to changes in membrane potential, thereby enabling electrical signaling in excitable cells. The voltage sensitivity is conferred through four voltage-sensor domains (VSDs) where positively charged residues in the fourth transmembrane segment (S4) sense the potential. While an open state is known from the Kv1.2/2.1 X-ray structure, the conformational changes underlying voltage sensing have not been resolved. We present 20 additional interactions in one open and four different closed conformations based on metal-ion bridges between all four segments of the VSD in the voltage-gated Shaker K channel. A subset of the experimental constraints was used to generate Rosetta models of the conformations that were subjected to molecular simulation and tested against the remaining constraints. This achieves a detailed model of intermediate conformations during VSD gating. The results provide molecular insight into the transition, suggesting that S4 slides at least 12 Å along its axis to open the channel with a 3(10) helix region present that moves in sequence in S4 in order to occupy the same position in space opposite F290 from open through the three first closed states.

Indexed as

AnimalsBinding SitesCadmiumChelating AgentsComputer SimulationDrosophila melanogasterDrosophila ProteinsEgtazic AcidFemaleIon Channel GatingKineticsMembrane PotentialsMetalsModels, MolecularMutationOocytesCadmiumChelating AgentsDrosophila ProteinsEgtazic AcidMetalsShaker Superfamily of Potassium ChannelsSh protein, Drosophila

Identifiers

PMID22538811
PMCPMC3365220
OpenAlexW2000181571

What OpenQuestion holds

Textmetadata
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.