Evidence map›Paper›PMID 19175309›Full record

ArticleJournal of the American Chemical Society2009

Initial response of the potassium channel voltage sensor to a transmembrane potential.

Werner Treptow, Mounir Tarek, Michael L Klein

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

31 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Does Proton Conduction in the Voltage-Gated HThe journal of physical chemistry. B · 2017
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Free-energy landscape of ion-channel voltage-sensor-domain activation.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  17. Electric fingerprint of voltage sensor domains.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  18. Article
  19. Exploring conformational states of the bacterial voltage-gated sodium channel NavAb via molecular dynamics simulations.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  20. Review
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

3 authors at 3 institutions in 2 countries.

Werner TreptowCenter for Molecular Modeling and Department of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania, USA.
Mounir Tarek
Michael L Klein
Centre National de la Recherche Scientifique · FRInstitut de Recherche sur les Systèmes Atomiques et Moléculaires Complexes · FRUniversity of Pennsylvania · US

Funding

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

Abstract

Early transition events of the voltage sensor (VS) of Kv1.2 potassium channel embedded in a lipid membrane are triggered using full atomistic molecular dynamics (MD) simulations. When subject to an applied hyperpolarized transmembrane (TM) voltage, the VS undergoes conformational changes and reaches a stable kinetic intermediate state, beta', within 20 ns. The gating charge ( approximately 2e) associated with this fast transition results mainly from salt-bridge rearrangements involving negative charges in S2 and S3 and all but the two top residues R(294) and R(297) of S4. Interactions of the latter with phosphomoieties of the lipid head groups appear to stabilize the kinetic state beta'.

Indexed as

Ion Channel GatingKineticsKv1.2 Potassium ChannelLipid BilayersMembrane PotentialsModels, MolecularPhosphatidylcholinesProtein ConformationProtein Structure, TertiaryStatic ElectricityThermodynamics1-palmitoyl-2-oleoylphosphatidylcholineKv1.2 Potassium ChannelLipid BilayersPhosphatidylcholines

Identifiers

PMID19175309
PMCPMC2668160
OpenAlexW1979023551

What OpenQuestion holds

Textmetadata
LicenceTDM
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.