Evidence map›Paper›PMID 17993502›Full record

ArticleBiophysical journal2008

NMR study of general anesthetic interaction with nAChR beta2 subunit.

Vasyl Bondarenko, Victor E Yushmanov, Yan Xu, Pei Tang

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 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

16 citing papers in PubMed, 24 citations in OpenAlex.

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  5. 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

4 authors at 1 institution in 1 country.

Vasyl BondarenkoDepartments of Anesthesiology, Pharmacology, and Computational Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania.
Victor E Yushmanov
Yan Xu
Pei Tang
University of Pittsburgh · US

Funding

NMR STUDIES OF MECHANISMS OF GENERAL ANESTHESIAR37GM049202 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI XU, YAN · 2004 to 2013
$4.9M
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
TM Domain Structures of Ligand-Gated Ion Channels by NMRR01GM069766 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI XU, YAN · 2004 to 2007
$1.0M
NIGMS NIH HHS R01 GM056257NIGMS NIH HHS R01 GM066358NIGMS NIH HHS R01 GM069766NIGMS NIH HHS R01GM56257NIGMS NIH HHS R01GM66358NIGMS NIH HHS R37 GM049202NIGMS NIH HHS R37GM049202
6 · The paper itself

Abstract

The molecular basis of anesthetic interaction with membrane proteins has been explored via determination of anesthetic effects on the structure and dynamics of the extended second transmembrane domain (TM2e) of the human neuronal nicotinic acetylcholine receptor (nAChR) beta(2) subunit in dodecylphosphocholine (DPC) micelles by (1)H and (15)N solution-state NMR. Both 1-chloro-1,2,2-trifluorocyclobutane (F3) and isoflurane, two volatile general anesthetics, induced nonuniform changes in chemical shifts among residues in TM2e. Saturation transfer difference NMR experiments further confirmed the direct anesthetic interaction with TM2e. A significant and more specific anesthetic interaction was observed on three leucine residues at the helix C-terminus. Although the TM2e helical structure remained after addition of anesthetics, plausible shortening and lengthening of helix hydrogen bonds were evidenced by periodic changes in backbone amide chemical shifts. The TM2e backbone dynamics were determined on the basis of the (15)N relaxation rate constants, R(1) and R(2), and the (15)N-[(1)H] NOE using the model-free approach. The global tumbling time (11.7 ns) of TM2e in micelles slightly increased ( approximately 12.3-12.5 ns) in the presence of anesthetics. The order parameter, S(2), exceeded 0.9 for all (15)N-labeled residues, showing a restricted internal motion. Anesthetics appear to have minor effect on the TM2e's internal motion. This study provided the basis for subsequent more comprehensive studies of anesthetic effects on the transmembrane domain complex of neuronal nAChR.

Indexed as

Anesthetics, GeneralBinding SitesCell MembraneHumansKineticsMagnetic Resonance SpectroscopyProtein Structure, SecondaryProtein SubunitsReceptors, NicotinicAnesthetics, GeneralProtein SubunitsReceptors, Nicotinic

Identifiers

PMID17993502
PMCPMC2242774
OpenAlexW2083991928

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.