Evidence map›Paper›PMID 35773594›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2022

Detergent-Free Membrane Protein Purification Using SMA Polymer.

Luke Broadbent, Peer Depping, Alexis Lodé, Afroditi Vaitsopoulou, David Hardy, Hoor Ayub, James Mitchell-White, Ian D Kerr, Alan D Goddard, Roslyn M Bill and 1 more

Abstract read
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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

6 citing papers in PubMed, 7 citations in OpenAlex.

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  5. Review
  6. 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

11 authors at 3 institutions in 1 country.

Luke Broadbent *College of Health & Life Sciences, Aston University, Birmingham, UK.
Peer Depping *College of Health & Life Sciences, Aston University, Birmingham, UK.
Alexis Lodé *College of Health & Life Sciences, Aston University, Birmingham, UK.
Afroditi Vaitsopoulou *College of Health & Life Sciences, Aston University, Birmingham, UK.
David HardyCollege of Health & Life Sciences, Aston University, Birmingham, UK.
Hoor AyubCollege of Health & Life Sciences, Aston University, Birmingham, UK.
James Mitchell-WhiteSchool of Life Sciences, University of Nottingham Medical School, Queen's Medical Centre, Nottingham, UK.
Ian D KerrSchool of Life Sciences, University of Nottingham Medical School, Queen's Medical Centre, Nottingham, UK.
Alan D GoddardCollege of Health & Life Sciences, Aston University, Birmingham, UK.
Roslyn M BillCollege of Health & Life Sciences, Aston University, Birmingham, UK.
Alice J RothnieCollege of Health & Life Sciences, Aston University, Birmingham, UK. a.rothnie@aston.ac.uk.
Aston University · GBUniversity of Nottingham · GBUniversity of Birmingham · GB

Funding

Biotechnology and Biological Sciences Research Council BB/L015846/1Biotechnology and Biological Sciences Research Council BB/R02152X/1Biotechnology and Biological Sciences Research Council BB/S001611/1Biotechnology and Biological Sciences Research Council BB/S008160/1
6 · The paper itself

Abstract

One of the big challenges for the study of structure and function of membrane proteins is the need to extract them from the membrane. Traditionally this was achieved using detergents which disrupt the membrane and form a micelle around the protein, but this can cause issues with protein function and/or stability. In 2009 an alternative approach was reported, using styrene maleic acid (SMA) copolymer to extract small discs of lipid bilayer encapsulated by the polymer and termed SMALPs (SMA lipid particles). Since then this approach has been shown to work for a range of different proteins from many different expression systems. It allows the extraction and purification of a target protein while maintaining a lipid bilayer environment. Recently this has led to several new high-resolution structures and novel insights to function. As with any method there are some limitations and issues to be aware of. Here we describe a standard protocol for preparation of the polymer and its use for membrane protein purification, and also include details of typical challenges that may be encountered and possible ways to address those.

Indexed as

Lipid BilayersMembrane ProteinsChromatography, AffinityMembranesPolymersPolystyrenesLipid BilayersMembrane ProteinsPolymersPolystyrenesDetergentMembrane proteinsNanodiscPolymerPurificationSMALPSolubilization

Identifiers

PMID35773594
OpenAlexW4285126142

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.