Evidence map›Paper›PMID 42156687›Full record

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

Fluorescence Correlation Spectroscopy to Examine Protein-Lipid Interactions in Membranes.

Viktoria Betaneli, Jan-Hagen Krohn, Jonas Mücksch, Petra Schwille

Abstract read
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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. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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.

Viktoria BetaneliInstitute of Physiological Chemistry, Technische Universität Dresden, Dresden, Germany.
Jan-Hagen KrohnMax Planck Institute of Biochemistry, Martinsried, Germany.
Jonas MückschMax Planck Institute of Biochemistry, Martinsried, Germany.
Petra SchwilleMax Planck Institute of Biochemistry, Martinsried, Germany. schwille@biochem.mpg.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fluorescence correlation spectroscopy (FCS) is a versatile technique to study membrane dynamics and protein-lipid interactions. It can provide information about diffusion coefficients, concentrations, and molecular interactions of proteins and lipids in the membrane. These parameters allow the determination of protein partitioning into different lipid environments, the identification of lipid domains, and the detection of lipid-protein complexes on the membrane. During the last decades, FCS studies were successfully performed on model membrane systems as also on living cells, to characterize protein-lipid interactions. Recent developments of the method described here improved quantitative measurements on membranes and decreased the number of potential artifacts. The aim of this chapter is to provide the reader with the necessary information and some practical guidelines to perform FCS studies on artificial and cellular membranes.

Indexed as

Cell MembraneMembrane LipidsMembrane ProteinsDiffusionLipid BilayersMembrane MicrodomainsProtein BindingSpectrometry, FluorescenceUnilamellar LiposomesLipid BilayersMembrane LipidsMembrane ProteinsUnilamellar LiposomesCross-correlationDiffusionFCCSFCSFluorescence correlation spectroscopyGiant unilamellar vesiclesLipid raftsModel membranesProtein–lipid interactions

Identifiers

What OpenQuestion holds

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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.