Evidence map›Paper›PMID 15565171›Full record

ArticleThe EMBO journal2004

Molecular mechanism of voltage sensor movements in a potassium channel.

David J S Elliott, Edward J Neale, Qadeer Aziz, James P Dunham, Tim S Munsey, Malcolm Hunter, Asipu Sivaprasadarao

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In one paragraph

Article in The EMBO journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

18 citing papers in PubMed, 34 citations in OpenAlex.

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  5. 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
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  16. Voltage sensor conformations in the open and closed states in ROSETTA structural models of K(+) channels.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  17. Structure of the KvAP voltage-dependent K+ channel and its dependence on the lipid membrane.Proceedings of the National Academy of Sciences of the United States of America · 2005
    Article
  18. S3b amino acid residues do not shuttle across the bilayer in voltage-dependent Shaker K+ channels.Proceedings of the National Academy of Sciences of the United States of America · 2005
    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

7 authors at 1 institution in 1 country.

David J S ElliottSchool of Biomedical Sciences, Leeds University, Leeds, UK.
Edward J Neale
Qadeer Aziz
James P Dunham
Tim S Munsey
Malcolm Hunter
Asipu Sivaprasadarao
University of Leeds · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Voltage-gated potassium channels are six-transmembrane (S1-S6) proteins that form a central pore domain (4 x S5-S6) surrounded by four voltage sensor domains (S1-S4), which detect changes in membrane voltage and control pore opening. Upon depolarization, the S4 segments move outward carrying charged residues across the membrane field, thereby leading to the opening of the pore. The mechanism of S4 motion is controversial. We have investigated how S4 moves relative to the pore domain in the prototypical Shaker potassium channel. We introduced pairs of cysteines, one in S4 and the other in S5, and examined proximity changes between each pair of cysteines during activation, using Cd2+ and copper-phenanthroline, which crosslink the cysteines with metal and disulphide bridges, respectively. Modelling of the results suggests a novel mechanism: in the resting state, the top of the S3b-S4 voltage sensor paddle lies close to the top of S5 of the adjacent subunit, but moves towards the top of S5 of its own subunit during depolarization--this motion is accompanied by a reorientation of S4 charges to the extracellular phase.

Indexed as

Protein Structure, SecondaryAnimalsCadmiumCysteineDisulfidesModels, MolecularOocytesPatch-Clamp TechniquesPhenanthrolinesPotassium ChannelsProtein Structure, QuaternaryProtein SubunitsShaker Superfamily of Potassium ChannelsXenopus laevisCadmiumCysteineDisulfidesPhenanthrolinesPotassium ChannelsProtein SubunitsShaker Superfamily of Potassium Channels

Identifiers

PMID15565171
PMCPMC535096
OpenAlexW2044680830

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.