Evidence map›Paper›PMID 19639312›Full record

ArticleEuropean biophysics journal : EBJ2010

Solution NMR mapping of water-accessible residues in the transmembrane beta-barrel of OmpX.

Laurent J Catoire, Manuela Zoonens, Carine van Heijenoort, Fabrice Giusti, Eric Guittet, Jean-Luc Popot

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Article in European biophysics journal : EBJ, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

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  14. Amphipols for each season.The Journal of membrane biology · 2014
    Review
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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

6 authors.

Laurent J CatoireLaboratoire de Physico-Chimie Moléculaire des Protéines Membranaires, UMR 7099, CNRS/Université Paris-7, Institut de Biologie Physico-Chimique (FRC 550), 75005 Paris, France. laurent.catoire@ibpc.fr
Manuela Zoonens
Carine van Heijenoort
Fabrice Giusti
Eric Guittet
Jean-Luc Popot

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The atomic structure of OmpX, the smallest member of the bacterial outer membrane protein family, has been previously established by X-ray crystallography and NMR spectroscopy. In apparent conflict with electrophysiological studies, the lumen of its transmembrane beta-barrel appears too tightly packed with amino acid side chains to let any solute flow through. In the present study, high-resolution solution NMR spectra were obtained of OmpX kept water-soluble by either amphipol A8-35 or the detergent dihexanoylphosphatidylcholine. Hydrogen/deuterium exchange measurements performed after prolonged equilibration show that, whatever the surfactant used, some of the amide protons of the membrane-spanning region exchange much more readily than others, which likely reflects the dynamics of the barrel.

Indexed as

Cell MembraneNuclear Magnetic Resonance, BiomolecularAmino Acid SequenceBacterial Outer Membrane ProteinsDetergentsDeuterium Exchange MeasurementEscherichia coli ProteinsHydrolasesMolecular Sequence DataPhosphatidylcholinesPolymersPropylaminesProtein Structure, SecondarySolventsWater1,2-hexanoylphosphatidylcholineamphipol A8-35Bacterial Outer Membrane ProteinsDetergentsEscherichia coli ProteinsHydrolasesOmpX protein, E coliPhosphatidylcholinesPolymersPropylaminesSolventsWater

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Registered trials

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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.