Evidence map›Paper›PMID 24676477›Full record

ArticleThe Journal of membrane biology2014

The use of amphipols for solution NMR studies of membrane proteins: advantages and constraints as compared to other solubilizing media.

Noelya Planchard, Élodie Point, Tassadite Dahmane, Fabrice Giusti, Marie Renault, Christel Le Bon, Grégory Durand, Alain Milon, Éric Guittet, Manuela Zoonens and 2 more

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Article in The Journal of membrane biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

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

12 authors.

Noelya PlanchardLaboratoire de Biologie Physico-Chimique des Protéines Membranaires, Institut de Biologie Physico-Chimique (FRC 550), UMR 7099, CNRS, Université Paris 7, 13 rue Pierre et Marie Curie, 75005, Paris, France.
Élodie Point
Tassadite Dahmane
Fabrice Giusti
Marie Renault
Christel Le Bon
Grégory Durand
Alain Milon
Éric Guittet
Manuela Zoonens
Jean-Luc Popot
Laurent J Catoire

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Solution-state nuclear magnetic resonance studies of membrane proteins are facilitated by the increased stability that trapping with amphipols confers to most of them as compared to detergent solutions. They have yielded information on the state of folding of the proteins, their areas of contact with the polymer, their dynamics, water accessibility, and the structure of protein-bound ligands. They benefit from the diversification of amphipol chemical structures and the availability of deuterated amphipols. The advantages and constraints of working with amphipols are discussed and compared to those associated with other non-conventional environments, such as bicelles and nanodiscs.

Indexed as

AnimalsArtifactsCell MembraneHumansHydrophobic and Hydrophilic InteractionsLipid BilayersMagnetic Resonance SpectroscopyMembrane ProteinsPolymersSolubilitySolutionsSurface-Active AgentsTechnology Assessment, BiomedicalWaterLipid BilayersMembrane ProteinsPolymersSolutionsSurface-Active AgentsWater

Identifiers

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.