Evidence map›Paper›PMID 31053046›Full record

ArticleExperimental biology and medicine (Maywood, N.J.)2019

Probing membrane protein properties using droplet interface bilayers.

Maxwell Allen-Benton, Heather E Findlay, Paula J Booth

Abstract read
In one paragraph

Article in Experimental biology and medicine (Maywood, N.J.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Article
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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

3 authors.

Maxwell Allen-BentonDepartment of Chemistry, King's College London, London SE1 1DB, UK.
Heather E FindlayDepartment of Chemistry, King's College London, London SE1 1DB, UK.
Paula J BoothDepartment of Chemistry, King's College London, London SE1 1DB, UK.ORCID 0000-0003-3893-360X

Funding

Wellcome Trust 214259
6 · The paper itself

Abstract

impact statementThe paper presents a comprehensive review of integral membrane protein studies utilizing droplet interface bilayers. Droplet interface bilayers are a novel method of constructing artificial lipid bilayers with enhanced stability and physicochemical complexity compared to existing methods. Their unique morphology also suggests applications in the construction of synthetic biological systems and protocells. As well as serving as a guide to in vitro membrane protein functional studies using droplet interface bilayers in the literature to date, a novel in vitro study of a flippase protein in a droplet interface bilayer is presented.

Indexed as

ATP-Binding Cassette TransportersBacterial ProteinsBacterial ToxinsCell-Free SystemDetergentsHemolysin ProteinsIn Vitro TechniquesLipid BilayersLiposomesMembrane LipidsMembrane ProteinsMicellesMicromanipulationPotassium ChannelsProtein BiosynthesisTranscription, GeneticATP-Binding Cassette TransportersBacterial ProteinsBacterial ToxinsDetergentsHemolysin ProteinsLipid BilayersLiposomesMembrane LipidsMembrane ProteinsMicellesMsbA protein, BacteriaPotassium Channelsstaphylococcal alpha-toxinartificial bilayerdroplet interface bilayerflippaseMembrane proteinssynthetic biology

Identifiers

PMID31053046
PMCPMC6552395

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.