Evidence map›Paper›PMID 39699737›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2025

Determining the Relative Affinity of ORPs for Lipid Ligands Using Fluorescence and Thermal Shift Assays.

Vanessa Delfosse, Guillaume Drin

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Article in Methods in molecular biology (Clifton, N.J.), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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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.

Vanessa DelfosseCentre de Biologie Structurale (CBS), Université de Montpellier, INSERM, CNRS, Montpellier, France.
Guillaume DrinUniversité Côte d'Azur, CNRS, INSERM, Institut de Pharmacologie Moléculaire et Cellulaire, Valbonne, France. drin@ipmc.cnrs.fr.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lipid transfer proteins (LTPs) are specialized proteins that convey specific lipids across the cytosol to regulate the lipid composition of organelles and the plasma membrane. Quantifying to which extent these LTPs recognize and transfer various lipid species and subspecies is of prime interest to define their cellular role(s). Here, we describe how to measure in vitro the relative affinity of Osh6p, a yeast phosphatidylserine (PS)/phosphatidylinositol 4-phosphate (PI(4)P) exchanger belonging to the oxysterol-binding protein(OSBP)-related protein (ORP) family, for PS and phosphoinositide subspecies. First, we detail how to produce and purify Osh6p with high purity. Secondly, we describe how to measure its ability to bind PS, PI(4)P, and PI(4,5)P

Indexed as

Carrier ProteinsFluorescence Resonance Energy TransferLigandsLiposomesOxysterol Binding ProteinsPhosphatidylinositol PhosphatesPhosphatidylserinesProtein BindingReceptors, SteroidSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCarrier ProteinsLigandslipid transfer proteinLiposomesOxysterol Binding Proteinsphosphatidylinositol 4-phosphatePhosphatidylinositol PhosphatesPhosphatidylserinesReceptors, SteroidSaccharomyces cerevisiae ProteinsFRETLiposomeORP/Osh proteinsPI(4)PPSRecombinant proteinsThermal shift assay (TSA)

Identifiers

PMID39699737

What Socratic 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 Socratic graph.