Evidence map›Paper›PMID 28611396›Full record

ArticleScientific reports2017

Coupling neutron reflectivity with cell-free protein synthesis to probe membrane protein structure in supported bilayers.

Thomas Soranzo, Donald K Martin, Jean-Luc Lenormand, Erik B Watkins

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

9 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
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  3. Increasing cellular NADAmerican journal of physiology. Cell physiology · 2025
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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 2 institutions in 1 country.

Thomas SoranzoSynthelis SAS, 5 avenue du Grand Sablon, 38700, La Tronche, France.
Donald K MartinUniversity Grenoble Alpes, SyNaBi, TIMC IMAG/CNRS, UMR 5525, F-38000, Grenoble, France.
Jean-Luc LenormandUniversity Grenoble Alpes, TheREx, TIMC IMAG/CNRS, UMR 5525, F-38000, Grenoble, France.
Erik B WatkinsInstitut Laue-Langevin, 6 rue Jules Horowitz, BP 156, 38042, Grenoble, Cedex 9, France. ebw@lanl.gov.
Université Grenoble Alpes · FRInstitut Laue-Langevin · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The structure of the p7 viroporin, an oligomeric membrane protein ion channel involved in the assembly and release of the hepatitis C virus, was determined from proteins expressed and inserted directly into supported model lipid membranes using cell-free protein expression. Cell-free protein expression allowed (i ) high protein concentration in the membrane, (ii ) control of the protein's isotopic constitution, and (iii ) control over the lipid environment available to the protein. Here, we used cell-free protein synthesis to directly incorporate the hepatitis C virus (HCV) p7 protein into supported lipid bilayers formed from physiologically relevant lipids (POPC or asolectin) for both direct structural measurements using neutron reflectivity (NR) and conductance measurements using electrical impedance spectroscopy (EIS). We report that HCV p7 from genotype 1a strain H77 adopts a conical shape within lipid bilayers and forms a viroporin upon oligomerization, confirmed by EIS conductance measurements. This combination of techniques represents a novel approach to the study of membrane proteins and, through the use of selective deuteration of particular amino acids to enhance neutron scattering contrast, has the promise to become a powerful tool for characterizing the protein conformation in physiologically relevant environments and for the development of biosensor applications.

Indexed as

NeutronsProtein BiosynthesisCell MembraneLipid BilayersMembrane LipidsModels, MolecularProtein ConformationViral ProteinsViroporin ProteinsLipid BilayersMembrane Lipidsp7 protein, Hepatitis C virusViral ProteinsViroporin Proteins

Identifiers

PMID28611396
PMCPMC5469739
OpenAlexW2623154989

What OpenQuestion holds

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LicenceCC BY
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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.