Evidence map›Paper›PMID 32129823›Full record

ReviewBiochemical Society transactions2020

Scratching the surface: native mass spectrometry of peripheral membrane protein complexes.

Cagla Sahin, Deseree J Reid, Michael T Marty, Michael Landreh

Open access · hybridAbstract readReview
In one paragraph

Review in Biochemical Society transactions, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

13 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Understanding a Core Pilin of the Type IVa Pili ofJournal of microbiology and biotechnology · 2024
    Article
  3. Article
  4. Review
  5. Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Nanodiscs: A toolkit for membrane protein science.Protein science : a publication of the Protein Society · 2021
    Review
  12. Review
  13. Native Mass Spectrometry of Iron-Sulfur Proteins.Methods in molecular biology (Clifton, N.J.) · 2021
    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

4 authors at 3 institutions in 3 countries.

Cagla SahinDepartment of Microbiology, Tumor and Cell Biology, Karolinska Institutet - Biomedicum, Solnavägen 9, 17165 Solna, Sweden.
Deseree J ReidDepartment of Chemistry and Biochemistry, University of Arizona, Marvel Hall 542, Tucson, AZ 85721, U.S.A.
Michael T MartyDepartment of Chemistry and Biochemistry, University of Arizona, Marvel Hall 542, Tucson, AZ 85721, U.S.A.
Michael LandrehDepartment of Microbiology, Tumor and Cell Biology, Karolinska Institutet - Biomedicum, Solnavägen 9, 17165 Solna, Sweden.
University of Arizona · USKarolinska Institutet · SEUniversity of Copenhagen · DK

Funding

Unravelling Membrane Protein-Lipid Interactions using Nanodiscs and Mass SpectrometryR35GM128624 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI Michael T Marty · 2018 to 2026
$3.6M
NIGMS NIH HHS R35 GM128624
6 · The paper itself

Abstract

A growing number of integral membrane proteins have been shown to tune their activity by selectively interacting with specific lipids. The ability to regulate biological functions via lipid interactions extends to the diverse group of proteins that associate only peripherally with the lipid bilayer. However, the structural basis of these interactions remains challenging to study due to their transient and promiscuous nature. Recently, native mass spectrometry has come into focus as a new tool to investigate lipid interactions in membrane proteins. Here, we outline how the native MS strategies developed for integral membrane proteins can be applied to generate insights into the structure and function of peripheral membrane proteins. Specifically, native MS studies of proteins in complex with detergent-solubilized lipids, bound to lipid nanodiscs, and released from native-like lipid vesicles all shed new light on the role of lipid interactions. The unique ability of native MS to capture and interrogate protein-protein, protein-ligand, and protein-lipid interactions opens exciting new avenues for the study of peripheral membrane protein biology.

Indexed as

Mass SpectrometryAntigens, CD1Antimicrobial Cationic PeptidesBinding SitesDetergentsGlycosphingolipidsHumansLipid BilayersLipidsMembrane ProteinsPeptidesProtein Interaction MappingSpectrometry, Mass, Electrospray IonizationUbiquinoneAntigens, CD1Antimicrobial Cationic PeptidesCD1b antigenDetergentsGlycosphingolipidsLipid BilayersLipidsMembrane ProteinsPeptidesUbiquinonelipid nanodiscsmembrane protein structureprotein–lipid interactionsstructural proteomics

Identifiers

PMID32129823
PMCPMC7192793
OpenAlexW3010484733

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.