Evidence map›Paper›PMID 18614032›Full record

ArticleNeuron2008

Extent of voltage sensor movement during gating of shaker K+ channels.

David J Posson, Paul R Selvin

Abstract read
In one paragraph

Article in Neuron, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing 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

43 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Voltage and pH sensing by the voltage-gated proton channel, HJournal of the Royal Society, Interface · 2018
    Review
  7. Mapping of voltage sensor positions in resting and inactivated mammalian sodium channels by LRET.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  8. β1-subunit-induced structural rearrangements of the Ca2+- and voltage-activated K+ (BK) channel.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  9. Article
  10. Article
  11. Article
  12. Structure of potassium channels.Cellular and molecular life sciences : CMLS · 2015
    Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Voltage sensor ring in a native structure of a membrane-embedded potassium channel.Proceedings of the National Academy of Sciences of the United States of America · 2013
    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.

David J PossonDepartment of Physics and Biophysics, University of Illinois Urbana-Champaign, Urbana IL 61801, USA.
Paul R Selvin

Funding

Fluorescence Changes in Shaker Potassium lon ChannelR01GM074770 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI SELVIN, PAUL R · 2005 to 2008
$1.3M
NIGMS NIH HHS GM074770NIGMS NIH HHS R01 GM074770
6 · The paper itself

Abstract

Voltage-driven activation of Kv channels results from conformational changes of four voltage sensor domains (VSDs) that surround the K(+) selective pore domain. How the VSD helices rearrange during gating is an area of active research. Luminescence resonance energy transfer (LRET) is a powerful spectroscopic ruler uniquely suitable for addressing the conformational trajectory of these helices. Using a geometric analysis of numerous LRET measurements, we were able to estimate LRET probe positions relative to existing structural models. The experimental movement of helix S4 does not support a large 15-20 A transmembrane "paddle-type" movement or a near-zero A vertical "transporter-type" model. Rather, our measurements demonstrate a moderate S4 displacement of 10 +/- 5 A, with a vertical component of 5 +/- 2 A. The S3 segment moves 2 +/- 1 A in the opposite direction and is therefore not moving as an S3-S4 rigid body.

Indexed as

Amino Acid SequenceAnimalsDose-Response Relationship, RadiationElectric StimulationIon Channel GatingLipid BilayersMembrane PotentialsModels, BiologicalModels, MolecularOocytesPatch-Clamp TechniquesPotassiumProtein ConformationProtein Structure, TertiaryShaker Superfamily of Potassium ChannelsXenopus laevisLipid BilayersPotassiumShaker Superfamily of Potassium Channels

Identifiers

PMID18614032
PMCPMC2603612

What OpenQuestion holds

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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.