Evidence map›Paper›PMID 31945320›Full record

ArticleBiochimica et biophysica acta. Biomembranes2020

Styrene maleic-acid lipid particles (SMALPs) into detergent or amphipols: An exchange protocol for membrane protein characterisation.

Sophie J Hesketh, David P Klebl, Anna J Higgins, Maren Thomsen, Isabelle B Pickles, Frank Sobott, Asipu Sivaprasadarao, Vincent L G Postis, Stephen P Muench

Open access · hybridAbstract read
In one paragraph

Article in Biochimica et biophysica acta. Biomembranes, 2020. 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
2.3field-weighted citation impact, top 11% 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

23 citing papers in PubMed, 37 citations in OpenAlex.

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  16. Purification of Membrane Proteins Overexpressed in Saccharomyces cerevisiae.Methods in molecular biology (Clifton, N.J.) · 2022
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  19. Structure and function of proteins in membranes and nanodiscs.Biochimica et biophysica acta. Biomembranes · 2021
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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

9 authors at 3 institutions in 2 countries.

Sophie J HeskethSchool of Biomedical Sciences, Faculty of Biological Sciences, University of Leeds, LS2 9JT, UK; Astbury Centre for Structural Molecular Biology, University of Leeds, LS2 9JT, UK.
David P KleblSchool of Biomedical Sciences, Faculty of Biological Sciences, University of Leeds, LS2 9JT, UK; Astbury Centre for Structural Molecular Biology, University of Leeds, LS2 9JT, UK.
Anna J HigginsSchool of Biomedical Sciences, Faculty of Biological Sciences, University of Leeds, LS2 9JT, UK; Astbury Centre for Structural Molecular Biology, University of Leeds, LS2 9JT, UK.
Maren ThomsenSchool of Biomedical Sciences, Faculty of Biological Sciences, University of Leeds, LS2 9JT, UK; Astbury Centre for Structural Molecular Biology, University of Leeds, LS2 9JT, UK.
Isabelle B PicklesAstbury Centre for Structural Molecular Biology, University of Leeds, LS2 9JT, UK; Department of Discovery and Translational Science, Leeds Institute of Cardiovascular and Metabolic Medicine, University of Leeds, Leeds LS2 9JT, UK.
Frank SobottAstbury Centre for Structural Molecular Biology, University of Leeds, LS2 9JT, UK; School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, LS2 9JT, UK; Department of Chemistry, Biomolecular & Analytical Mass Spectrometry group, University of Antwerp, 2020 Antwerpen, Belgium.
Asipu SivaprasadaraoSchool of Biomedical Sciences, Faculty of Biological Sciences, University of Leeds, LS2 9JT, UK.
Vincent L G PostisBiomedicine Research Group, Faculty of Health and Social Sciences, Leeds Beckett University, LS1 3HE, UK.
Stephen P MuenchSchool of Biomedical Sciences, Faculty of Biological Sciences, University of Leeds, LS2 9JT, UK; Astbury Centre for Structural Molecular Biology, University of Leeds, LS2 9JT, UK. Electronic address: s.p.muench@leeds.ac.uk.
University of Leeds · GBInstitute of Structural and Molecular Biology · GBLeeds Beckett University · GB

Funding

Biotechnology and Biological Sciences Research Council BB/M011151/1Biotechnology and Biological Sciences Research Council BB/R018561/1Wellcome Trust 102174/B/13/ZWellcome Trust 108466/Z/15/ZWellcome Trust 208385/Z/17/Z
6 · The paper itself

Abstract

Membrane proteins are traditionally extracted and purified in detergent for biochemical and structural characterisation. This process is often costly and laborious, and the stripping away of potentially stabilising lipids from the membrane protein of interest can have detrimental effects on protein integrity. Recently, styrene-maleic acid (SMA) co-polymers have offered a solution to this problem by extracting membrane proteins directly from their native membrane, while retaining their naturally associated lipids in the form of stable SMA lipid particles (SMALPs). However, the inherent nature and heterogeneity of the polymer renders their use challenging for some downstream applications - particularly mass spectrometry (MS). While advances in cryo-electron microscopy (cryo-EM) have enhanced our understanding of membrane protein:lipid interactions in both SMALPs and detergent, the resolution obtained with this technique is often insufficient to accurately identify closely associated lipids within the transmembrane annulus. Native-MS has the power to fill this knowledge gap, but the SMA polymer itself remains largely incompatible with this technique. To increase sample homogeneity and allow characterisation of membrane protein:lipid complexes by native-MS, we have developed a novel SMA-exchange method; whereby the membrane protein of interest is first solubilised and purified in SMA, then transferred into amphipols or detergents. This allows the membrane protein and endogenously associated lipids extracted by SMA co-polymer to be identified and examined by MS, thereby complementing results obtained by cryo-EM and creating a better understanding of how the lipid bilayer directly affects membrane protein structure and function.

Indexed as

Cryoelectron MicroscopyDetergentsEscherichia coliEscherichia coli ProteinsLipid BilayersLipid DropletsMaleatesMass SpectrometryMembrane LipidsMembrane ProteinsPolymersPolystyrenesDetergentsEscherichia coli ProteinsLipid BilayersMaleatesmaleic acidMembrane LipidsMembrane ProteinsPolymersPolystyrenesstyrene-maleic acid polymerAmphipolsElectron microscopyMass spectrometryMembrane proteinsSMA co-polymerSMALP

Identifiers

PMID31945320
PMCPMC7086155
OpenAlexW2999250470

What OpenQuestion holds

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LicenceCC BY
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.