Evidence map›Paper›PMID 12438684›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2002

Large-scale molecular dynamics simulations of general anesthetic effects on the ion channel in the fully hydrated membrane: the implication of molecular mechanisms of general anesthesia.

Pei Tang, Yan Xu

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

35 citing papers in PubMed, 110 citations in OpenAlex.

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  8. Fluorine-19 NMR and computational quantification of isoflurane binding to the voltage-gated sodium channel NaChBac.Proceedings of the National Academy of Sciences of the United States of America · 2016
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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 at 2 institutions in 1 country.

Pei TangDepartments of Anesthesiology and Pharmacology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15261, USA. tangp@anes.upmc.edu
Yan Xu
Stanford University · USUniversity of Pittsburgh · US

Funding

YEAST ER MOLECULAR CHAPERONE TRANSLOCATION: GENOME DATABANK HOMOLOGSP41RR006009 · NCRR · MELLON PITTS CORPORATION (MPC CORP) · PI KNOLL, ERIC · 1990 to 2011
$22.0M
ANESTHETIC SITES IN TRANSMEMBRANE PEPTIDES BY NMRR01GM056257 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI TANG, PEI · 1998 to 2017
$4.8M
ANESTHETIC EFFECTS ON ION CHANNEL STRUCTURES & DYNAMICSR01GM066358 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI TANG, PEI · 2002 to 2014
$3.6M
NCRR NIH HHS P41 RR006009NCRR NIH HHS RR06009NIGMS NIH HHS R01 GM056257NIGMS NIH HHS R01 GM066358NIGMS NIH HHS R01GM56267NIGMS NIH HHS R01GM66358
6 · The paper itself

Abstract

Interactions of volatile anesthetics with the central nervous system are characterized by low yet specific binding affinities. Although neurotransmitter-gated ion channels are considered the primary anesthetic targets, the mechanism of action at the molecular level remains elusive. We consider here the theoretical implications of channel dynamics on anesthetic action in a simplified membrane-channel system. Large-scale 2.2-ns all-atom molecular dynamics simulations were performed to study the effects of halothane, a clinical anesthetic, on a gramicidin A (gA) channel in a fully hydrated dimyristoyl phosphatidylcholine membrane. In agreement with experimental results, anesthetics preferentially target the anchoring residues at the channel-lipid-water interface. Although the anesthetic effect on channel structure is minimal, the presence of halothane profoundly affects channel dynamics. For 2.2-ns simulation, the rms fluctuation of gA backbone in the lipid core increases from approximately equal 1 A in the absence of anesthetics to approximately equal 1.5 A in the presence of halothane. Autocorrelation analysis reveals that halothane (i) has no effect on the subpicosecond librational motion, (ii) prolongs the backbone autocorrelation time in the 10- to 100-ps time scale, and (iii) significantly decreases the asymptotic values of generalized order parameter and correlation time of nanosecond motions for the inner but not the outer residues. The simulation results discount the viewpoint of a structure-function paradigm that overrates the importance of structural fitting between general anesthetics and yet-unidentified hydrophobic protein pockets. Instead, the results underscore the global, as opposed to local, effects of anesthetics on protein dynamics as the underlying mechanisms for the action of general anesthetics and possibly of other low-affinity drugs.

Indexed as

Anesthesia, GeneralComputer SimulationModels, NeurologicalAnesthetics, GeneralDimyristoylphosphatidylcholineGramicidinHalothaneIon Channel GatingIon ChannelsMembrane LipidsMembrane ProteinsMembranes, ArtificialModels, MolecularProtein Structure, TertiarySolubilityStructure-Activity RelationshipAnesthetics, GeneralDimyristoylphosphatidylcholineGramicidinHalothaneIon ChannelsMembrane LipidsMembrane ProteinsMembranes, ArtificialTryptophan

Identifiers

PMID12438684
PMCPMC138560
OpenAlexW2108015733

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.