Evidence map›Paper›PMID 33582991›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2020

Examining Membrane Proteins by Neutron Scattering.

Christine Ebel, Cécile Breyton, Anne Martel

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact, top 73% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. Review
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

3 authors at 3 institutions in 1 country.

Christine EbelUniversité Grenoble Alpes, CNRS, CEA, IBS, Grenoble, France. christine.ebel@ibs.fr.
Cécile BreytonUniversité Grenoble Alpes, CNRS, CEA, IBS, Grenoble, France.
Anne MartelInstitut Laue Langevin, Grenoble, France.
CEA Grenoble · FRInstitut Laue-Langevin · FRUniversité Grenoble Alpes · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Small angle neutron scattering (SANS) is a powerful tool for studying the structure of solubilized membrane proteins. It allows describing the general dimension of the membrane protein , evidence conformational changes, and may provide a low-resolution structure at the nm resolution range. This is because SANS can discriminate between the membrane protein and its amphiphilic partner by specific deuteration of the partners and of the buffer. This chapter was written to offer to a scientist aiming to describe a membrane protein structure the basic tools to consider a SANS experiment. It presents the general principle of contrast variation and a bibliographic survey of experimental strategies used for membrane proteins, some basic theoretical background, and a succinct description of the principles of analysis, of the instrumental and sample requirement, and of the practical steps, prior to the experiments, during the experiments and for data analysis.

Indexed as

Scattering, Small AngleDetergentsDeuterium Exchange MeasurementHumansMembrane ProteinsNeutron DiffractionDetergentsMembrane ProteinsContrast variationDetergentMembrane proteinsModellingSmall angle neutron scattering

Identifiers

PMID33582991
OpenAlexW3130360815

What Socratic 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 Socratic graph.