Evidence map›Paper›PMID 21044565›Full record

ArticleBiophysical journal2010

Effect of sensor domain mutations on the properties of voltage-gated ion channels: molecular dynamics studies of the potassium channel Kv1.2.

Lucie Delemotte, Werner Treptow, Michael L Klein, Mounir Tarek

Erratum issuedAbstract readLetter
In one paragraph

Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing 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

30 citing papers in PubMed.

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4 · The record

Corrections and comments

  • Erratum issued
  • Erratum issued
5 · Who and what money

Authors and funding

4 authors.

Lucie DelemotteUMR 7565, Structure et Réactivité des Systèmes Moléculaires Complexes, Centre National de Recherche Scientifique-Nancy University, Nancy cedex, France.
Werner Treptow
Michael L Klein
Mounir Tarek

Funding

COMPUTER SIMULATION OF AMPHIPHILIC AGGREGATESR01GM040712 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI KLEIN, MICHAEL L. · 1988 to 2009
$2.2M
NIGMS NIH HHS GM 40712NIGMS NIH HHS R01 GM040712
6 · The paper itself

Abstract

The effects on the structural and functional properties of the Kv1.2 voltage-gated ion channel, caused by selective mutation of voltage sensor domain residues, have been investigated using classical molecular dynamics simulations. Following experiments that have identified mutations of voltage-gated ion channels involved in state-dependent omega currents, we observe for both the open and closed conformations of the Kv1.2 that specific mutations of S4 gating-charge residues destabilize the electrostatic network between helices of the voltage sensor domain, resulting in the formation of hydrophilic pathways linking the intra- and extracellular media. When such mutant channels are subject to transmembrane potentials, they conduct cations via these so-called "omega pores." This study provides therefore further insight into the molecular mechanisms that lead to omega currents, which have been linked to certain channelopathies.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionBiophysical PhenomenaHumansHydrophobic and Hydrophilic InteractionsIn Vitro TechniquesIon Channel GatingKv1.2 Potassium ChannelMembrane PotentialsModels, MolecularMolecular Dynamics SimulationMolecular Sequence DataMutagenesis, Site-DirectedMutant ProteinsProtein ConformationProtein Structure, TertiaryKv1.2 Potassium ChannelMutant Proteins

Identifiers

PMID21044565
PMCPMC2966007

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.