Evidence map›Paper›PMID 42156678›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2026

Probing the Annular Lipid Belt of Membrane Proteins Using Native Mass Spectrometry.

Smriti Kumar, Arthur Laganowsky

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

2 authors.

Smriti KumarDepartment of Chemistry, Texas A&M University, College Station, TX, USA.
Arthur LaganowskyDepartment of Chemistry, Texas A&M University, College Station, TX, USA. alaganowsky@chem.tamu.edu.

Funding

Understanding the role of lipids in structure and function of membrane proteinsRM1GM145416 · NIGMS · TEXAS A&M UNIVERSITY · PI Erin S Baker, Arthur D Laganowsky · 2022 to 2026
$7.4M
Developing new tools to probe membrane protein-lipid interactions for biomedical applicationsR01GM139876 · NIGMS · TEXAS A&M UNIVERSITY · PI LAGANOWSKY, ARTHUR D · 2021 to 2024
$1.2M
NIGMS NIH HHS R01 GM139876NIGMS NIH HHS RM1 GM145416
6 · The paper itself

Abstract

Membrane proteins are embedded within the biological membrane and encircled by an annular belt of lipids. Understanding the composition and dynamics of this annular belt is essential for advancing our knowledge of membrane proteins, which play critical roles in various physiological functions of living cells. Native mass spectrometry (MS) allows for the detection of intact membrane protein-lipid complexes in the gas phase. However, the conventional approach of solubilizing membrane proteins in detergents often interferes with the analysis of protein-lipid interactions due to the properties of the chosen detergent. In this study, we demonstrate how charge-reducing detergents and molecules, such as spermine, reduce the overall charge of membrane protein-lipid complexes, enabling the investigation of the annular lipid belt surrounding membrane proteins.

Indexed as

Mass SpectrometryMembrane LipidsMembrane ProteinsDetergentsDetergentsMembrane LipidsMembrane ProteinsCharge-reducing moleculesEquilibrium dissociation constantsMembrane protein–lipid bindingNative mass spectrometry

Identifiers

PMID42156678
PMCPMC13411006

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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.