Evidence map›Paper›PMID 34110372›Full record

ReviewBiochemical Society transactions2021

Biological insights from SMA-extracted proteins.

Lucas Unger, Alejandro Ronco-Campaña, Philip Kitchen, Roslyn M Bill, Alice J Rothnie

Open access · hybridAbstract readReview
In one paragraph

Review in Biochemical Society transactions, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

14 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
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  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Detergent-Free Membrane Protein Purification Using SMA Polymer.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  14. Article
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

5 authors at 1 institution in 1 country.

Lucas Unger *College of Health and Life Sciences, Aston University, Birmingham B4 7ET, U.K.
Alejandro Ronco-Campaña *College of Health and Life Sciences, Aston University, Birmingham B4 7ET, U.K.
Philip Kitchen *College of Health and Life Sciences, Aston University, Birmingham B4 7ET, U.K.
Roslyn M BillCollege of Health and Life Sciences, Aston University, Birmingham B4 7ET, U.K.
Alice J RothnieCollege of Health and Life Sciences, Aston University, Birmingham B4 7ET, U.K.ORCID 0000-0002-4259-7015
Aston University · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In the twelve years since styrene maleic acid (SMA) was first used to extract and purify a membrane protein within a native lipid bilayer, this technological breakthrough has provided insight into the structural and functional details of protein-lipid interactions. Most recently, advances in cryo-EM have demonstrated that SMA-extracted membrane proteins are a rich-source of structural data. For example, it has been possible to resolve the details of annular lipids and protein-protein interactions within complexes, the nature of lipids within central cavities and binding pockets, regions involved in stabilising multimers, details of terminal residues that would otherwise remain unresolved and the identification of physiologically relevant states. Functionally, SMA extraction has allowed the analysis of membrane proteins that are unstable in detergents, the characterization of an ultrafast component in the kinetics of electron transfer that was not possible in detergent-solubilised samples and quantitative, real-time measurement of binding assays with low concentrations of purified protein. While the use of SMA comes with limitations such as its sensitivity to low pH and divalent cations, its major advantage is maintenance of a protein's lipid bilayer. This has enabled researchers to view and assay proteins in an environment close to their native ones, leading to new structural and mechanistic insights.

Indexed as

Cryoelectron MicroscopyLipid BilayersMaleatesMembrane LipidsMembrane ProteinsPolystyrenesProtein BindingProtein ConformationProtein StabilityLipid BilayersMaleatesMembrane LipidsMembrane ProteinsPolystyrenesstyrene-maleic acid polymercryo-electron microscopymembrane proteinsprotein complexesprotein–lipid interactionsSMALP

Identifiers

PMID34110372
PMCPMC8286838
OpenAlexW3170445012

What OpenQuestion holds

Textmetadata
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.