Evidence map›Paper›PMID 33787280›Full record

ArticleNano letters2021

Detergent-free Lipodisq Nanoparticles Facilitate High-Resolution Mass Spectrometry of Folded Integral Membrane Proteins.

Kin Kuan Hoi, Juan Francisco Bada Juarez, Peter J Judge, Hsin-Yung Yen, Di Wu, Javier Vinals, Garrick F Taylor, Anthony Watts, Carol V Robinson

Open access · hybridAbstract read
In one paragraph

Article in Nano letters, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.7field-weighted citation impact, top 5% 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

22 citing papers in PubMed, 41 citations in OpenAlex.

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  7. Lipid Sorting and Organelle Identity.Cold Spring Harbor perspectives in biology · 2023
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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 1 institution in 1 country.

Kin Kuan HoiDepartment of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QZ, United Kingdom.
Juan Francisco Bada JuarezDepartment of Biochemistry, Biomembrane Structure Unit, University of Oxford, Oxford OX1 3QU, United Kingdom.ORCID 0000-0002-1337-6424
Peter J JudgeDepartment of Biochemistry, Biomembrane Structure Unit, University of Oxford, Oxford OX1 3QU, United Kingdom.ORCID 0000-0003-0609-0900
Hsin-Yung YenDepartment of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QZ, United Kingdom.
Di WuDepartment of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QZ, United Kingdom.
Javier VinalsDepartment of Biochemistry, Biomembrane Structure Unit, University of Oxford, Oxford OX1 3QU, United Kingdom.
Garrick F TaylorDepartment of Biochemistry, Biomembrane Structure Unit, University of Oxford, Oxford OX1 3QU, United Kingdom.
Anthony WattsDepartment of Biochemistry, Biomembrane Structure Unit, University of Oxford, Oxford OX1 3QU, United Kingdom.
Carol V RobinsonDepartment of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QZ, United Kingdom.ORCID 0000-0001-7829-5505
University of Oxford · GB

Funding

Biotechnology and Biological Sciences Research Council BB/N006011/1Cancer Research UK 16896Wellcome TrustWellcome Trust 104633/Z/14/AWellcome Trust 218246/Z/19/Z
6 · The paper itself

Abstract

Integral membrane proteins pose considerable challenges to mass spectrometry (MS) owing to the complexity and diversity of the components in their native environment. Here, we use native MS to study the post-translational maturation of bacteriorhodopsin (bR) and archaerhodopsin-3 (AR3), using both octyl-glucoside detergent micelles and lipid-based nanoparticles. A lower collision energy was required to obtain well-resolved spectra for proteins in styrene-maleic acid copolymer (SMA) Lipodisqs than in membrane scaffold protein (MSP) Nanodiscs. By comparing spectra of membrane proteins prepared using the different membrane mimetics, we found that SMA may favor selective solubilization of correctly folded proteins and better preserve native lipid interactions than other membrane mimetics. Our spectra reveal the correlation between the post-translation modifications (PTMs), lipid-interactions, and protein-folding states of bR, providing insights into the process of maturation of the photoreceptor proteins.

Indexed as

Membrane ProteinsNanoparticlesLipid BilayersLipidsMass SpectrometryMicellesLipid BilayersLipidsMembrane ProteinsMicellesbacteriorhodopsinlipid−protein interactionsLipodisqNative mass spectrometrypost-translational modificationSMALP

Identifiers

PMID33787280
PMCPMC8050825
OpenAlexW3148022885

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.