Evidence map›Paper›PMID 18310250›Full record

ArticleBiophysical journal2008

Interaction of anesthetics with open and closed conformations of a potassium channel studied via molecular dynamics and normal mode analysis.

Satyavani Vemparala, Carmen Domene, Michael L Klein

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

11 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Modulation of a voltage-gated Na+ channel by sevoflurane involves multiple sites and distinct mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. KirBac1.1: it's an inward rectifying potassium channel.The Journal of general physiology · 2009
    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

3 authors at 3 institutions in 3 countries.

Satyavani VemparalaThe Institute of Mathematical Sciences, Taramani, Chennai, India. vani@imsc.res.in
Carmen Domene
Michael L Klein
Institute of Mathematical Sciences · INUniversity of Oxford · GBUniversity of Pennsylvania · US

Funding

X-ray and Neutron Interferometry Studies of Anesthetic Interactions with VoltageP01GM055876 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI LOLL, PATRICK J · 1997 to 2017
$22.4M
NIGMS NIH HHS P01 GM055876NIGMS NIH HHS P01-GM055876-09
6 · The paper itself

Abstract

A variety of experiments suggest that membrane proteins are important targets of anesthetic molecules, and that ion channels interact differently with anesthetics in their open and closed conformations. The availability of an open and a closed structural model for the KirBac1.1 potassium channel has made it possible to perform a comparative analysis of the interactions of anesthetics with the same channel in its open and closed states. To this end, all-atom molecular dynamics simulations supplemented by normal mode analysis have been employed to probe the interactions of the inhalational anesthetic halothane with both an open and closed conformer of KirBac1.1 embedded in a lipid bilayer. Normal mode analysis on the closed and open channel, in the presence and absence of halothane, reveals that the anesthetic modulates the global as well as the local dynamics of both conformations differently. In the case of the open channel, the observed reduction of flexibility of residues in the inner helices suggests a functional modification action of anesthetics on ion channels. In this context, preferential quenching of the aromatic residue motion and modulation of global dynamics by halothane may be seen as steps toward potentiating or favoring open state conformations. These molecular dynamics simulations provide the first insights into possible specific interactions between anesthetic molecules and ion channels in different conformations.

Indexed as

Ion Channel GatingModels, ChemicalModels, MolecularAnesthetics, InhalationBinding SitesComputer SimulationHalothanePotassium ChannelsProtein BindingProtein ConformationAnesthetics, InhalationHalothanePotassium Channels

Identifiers

PMID18310250
PMCPMC2480689
OpenAlexW1986488026

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.