Evidence map›Paper›PMID 14769847›Full record

ArticleThe Journal of general physiology2004

Specificity of charge-carrying residues in the voltage sensor of potassium channels.

Christopher A Ahern, Richard Horn

Abstract readComparative Study
In one paragraph

Article in The Journal of general physiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing 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

50 citing papers in PubMed.

  1. Voltage-sensing domains: structural and functional diversity.European biophysics journal : EBJ · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Comparison of KHandbook of experimental pharmacology · 2021
    Article
  8. Gating-induced large aqueous volumetric remodeling and aspartate tolerance in the voltage sensor domain of Shaker KProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  9. Pore size matters for potassium channel conductance.The Journal of general physiology · 2016
    Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Leaky channels make weak muscles.The Journal of clinical investigation · 2012
    Article
  17. Article
  18. Article
  19. Article
  20. Article
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

2 authors.

Christopher A AhernDepartment of Physiology, Jefferson Medical College, 1020 Locust Street, Philadelphia, PA 19107, USA.
Richard Horn

Funding

Molecular Physiology of Voltage gated Ion ChannelsR01AR041691 · NIAMS · THOMAS JEFFERSON UNIVERSITY · PI HORN, RICHARD J · 1992 to 2005
$2.1M
NIAMS NIH HHS AR41691NIAMS NIH HHS R01 AR041691
6 · The paper itself

Abstract

Positively charged voltage sensors of sodium and potassium channels are driven outward through the membrane's electric field upon depolarization. This movement is coupled to channel opening. A recent model based on studies of the KvAP channel proposes that the positively charged voltage sensor, christened the "voltage-sensor paddle", is a peripheral domain that shuttles its charged cargo through membrane lipid like a hydrophobic cation. We tested this idea by attaching charged adducts to cysteines introduced into the putative voltage-sensor paddle of Shaker potassium channels and measuring fractional changes in the total gating charge from gating currents. The only residues capable of translocating attached charges through the membrane-electric field are those that serve this function in the native channel. This remarkable specificity indicates that charge movement involves highly specialized interactions between the voltage sensor and other regions of the protein, a mechanism inconsistent with the paddle model.

Indexed as

Mutagenesis, Site-DirectedAnimalsCysteineFemaleMembrane PotentialsOocytesPotassium ChannelsPotassium Channels, Voltage-GatedShaker Superfamily of Potassium ChannelsCysteinePotassium ChannelsPotassium Channels, Voltage-GatedShaker Superfamily of Potassium Channels

Identifiers

PMID14769847
PMCPMC2217452

What OpenQuestion holds

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LicenceCC BY-NC-SA
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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.