Evidence map›Paper›PMID 29700483›Full record

ArticleNature protocols2018

Identifying key membrane protein lipid interactions using mass spectrometry.

Kallol Gupta, Jingwen Li, Idlir Liko, Joseph Gault, Cherine Bechara, Di Wu, Jonathan T S Hopper, Kevin Giles, Justin L P Benesch, Carol V Robinson

Open access · greenAbstract read
In one paragraph

Article in Nature protocols, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
5.4field-weighted citation impact, top 3% 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

73 citing papers in PubMed, 116 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Endogenous Aquaporin-0 Lipid Binding in Ocular Lens Tissue via Native Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2025
    Article
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  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Phospholipids Differentially Regulate CaACS chemical biology · 2024
    Article
  16. Review
  17. Mechanism of Obesity-Related Lipotoxicity and Clinical Perspective.Advances in experimental medicine and biology · 2024
    Review
  18. Article
  19. Article
  20. Article

13 more citing papers are in PubMed but not listed here.

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

10 authors at 3 institutions in 2 countries.

Kallol GuptaDepartment of Chemistry, University of Oxford, Oxford, UK.
Jingwen LiDepartment of Chemistry, University of Oxford, Oxford, UK.
Idlir LikoDepartment of Chemistry, University of Oxford, Oxford, UK.
Joseph GaultDepartment of Chemistry, University of Oxford, Oxford, UK.ORCID 0000-0001-7686-2983
Cherine BecharaDepartment of Chemistry, University of Oxford, Oxford, UK.
Di WuDepartment of Chemistry, University of Oxford, Oxford, UK.
Jonathan T S HopperDepartment of Chemistry, University of Oxford, Oxford, UK.
Kevin GilesWaters Corporation, Wilmslow, UK.
Justin L P BeneschDepartment of Chemistry, University of Oxford, Oxford, UK.ORCID 0000-0002-1507-3742
Carol V RobinsonDepartment of Chemistry, University of Oxford, Oxford, UK.
University of Oxford · GBCentre National de la Recherche Scientifique · FRWaters (United Kingdom) · GB

Funding

European Research Council 695511Wellcome Trust
6 · The paper itself

Abstract

With the recent success in determining membrane protein structures, further detailed understanding of the identity and function of the bound lipidome is essential. Using an approach that combines high-energy native mass spectrometry (HE-nMS) and solution-phase lipid profiling, this protocol can be used to determine the identity of the endogenous lipids that directly interact with a protein. Furthermore, this method can identify systems in which such lipid binding has a major role in regulating the oligomeric assembly of membrane proteins. The protocol begins with recording of the native mass spectrum of the protein of interest, under successive delipidation conditions, to determine whether delipidation leads to disruption of the oligomeric state. Subsequently, we propose using a bipronged strategy: first, an HE-nMS platform is used that allows dissociation of the detergent micelle at the front end of the instrument. This allows for isolation of the protein-lipid complex at the quadrupole and successive fragmentation at the collision cell, which leads to identification of the bound lipid masses. Next, simultaneous coupling of this with in-solution LC-MS/MS-based identification of extracted lipids reveals the complete identity of the interacting lipidome that copurifies with the proteins. Assimilation of the results of these two sets of experiments divulges the complete identity of the set of lipids that directly interact with the membrane protein of interest, and can further delineate its role in maintaining the oligomeric state of the protein. The entire procedure takes 2 d to complete.

Indexed as

Mass SpectrometryMembrane LipidsMembrane ProteinsProtein BindingProtein MultimerizationMembrane LipidsMembrane Proteins

Identifiers

PMID29700483
PMCPMC6049616
OpenAlexW2802666639

What OpenQuestion holds

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Registered trials

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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.