Evidence map›Paper›PMID 16187128›Full record

ArticleEuropean biophysics journal : EBJ2006

Reconstitution and alignment by a magnetic field of a beta-barrel membrane protein in bicelles.

Mohamed N Triba, Manuela Zoonens, Jean-Luc Popot, Philippe F Devaux, Dror E Warschawski

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Article in European biophysics journal : EBJ, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. ChronicJournal of clinical medicine · 2024
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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

5 authors.

Mohamed N TribaUnité Mixte de Recherche No 7099, Institut de Biologie Physico-Chimique, CNRS - Université Paris 7-Denis Diderot, 13 rue Pierre et Marie Curie, 75005 Paris, France.
Manuela Zoonens
Jean-Luc Popot
Philippe F Devaux
Dror E Warschawski

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A protocol is described for the reconstitution of a transmembrane beta-barrel protein domain, tOmpA, into lipid bicelles. tOmpA is the largest protein to be reconstituted in bicelles to date. Its insertion does not prevent bicelles from orienting with their plane either parallel or perpendicular to the magnetic field, depending on the absence or presence of paramagnetic ions. In the latter case, tOmpA is shown to align with the axis of the beta-barrel parallel to the magnetic field, i.e. perpendicular to the plane of the bilayer, an orientation conforming to that in natural membranes and favourable to structural studies by solid-state NMR. Reconstitution into bicelles may offer an interesting approach for structural studies of membrane proteins in a medium resembling a biological membrane, using either NMR or other biophysical techniques. Our data suggest that alignment in the magnetic field of membrane proteins included into bicelles may be facilitated if the protein is folded as a beta-barrel structure.

Indexed as

MicellesProtein ConformationAnalytic Sample Preparation MethodsAnisotropyBacterial Outer Membrane ProteinsCircular DichroismElectromagnetic FieldsGlycerophosphatesLipid BilayersNuclear Magnetic Resonance, BiomolecularPhosphorus IsotopesProtein RenaturationProtein Structure, TertiarySodium IsotopesBacterial Outer Membrane ProteinsGlycerophosphatesLipid BilayersMicellesOMPA outer membrane proteinsPhosphorus IsotopesSodium Isotopes

Identifiers

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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.