Evidence map›Paper›PMID 32075908›Full record

ArticleThe Journal of biological chemistry2020

Molecular and cellular dissection of the oxysterol-binding protein cycle through a fluorescent inhibitor.

Tiphaine Péresse, David Kovacs, Mélody Subra, Joëlle Bigay, Meng-Chen Tsai, Joël Polidori, Romain Gautier, Sandy Desrat, Lucile Fleuriot, Delphine Debayle and 6 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

18 citing papers in PubMed, 42 citations in OpenAlex.

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  16. Synthesis of a Coumarin-Based Analogue of Schweinfurthin F.The Journal of organic chemistry · 2021
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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

16 authors at 2 institutions in 2 countries.

Tiphaine PéresseInstitut de Chimie des Substances Naturelles, CNRS, Université Paris-Saclay, Gif-sur-Yvette, France.
David KovacsUniversité Côte d'Azur, Inserm, CNRS, Institut de Pharmacologie Moléculaire et Cellulaire, Valbonne, France.
Mélody SubraUniversité Côte d'Azur, Inserm, CNRS, Institut de Pharmacologie Moléculaire et Cellulaire, Valbonne, France.
Joëlle BigayUniversité Côte d'Azur, Inserm, CNRS, Institut de Pharmacologie Moléculaire et Cellulaire, Valbonne, France.
Meng-Chen TsaiUniversité Côte d'Azur, Inserm, CNRS, Institut de Pharmacologie Moléculaire et Cellulaire, Valbonne, France.
Joël PolidoriUniversité Côte d'Azur, Inserm, CNRS, Institut de Pharmacologie Moléculaire et Cellulaire, Valbonne, France.
Romain GautierUniversité Côte d'Azur, Inserm, CNRS, Institut de Pharmacologie Moléculaire et Cellulaire, Valbonne, France.
Sandy DesratInstitut de Chimie des Substances Naturelles, CNRS, Université Paris-Saclay, Gif-sur-Yvette, France.
Lucile FleuriotUniversité Côte d'Azur, Inserm, CNRS, Institut de Pharmacologie Moléculaire et Cellulaire, Valbonne, France.
Delphine DebayleUniversité Côte d'Azur, Inserm, CNRS, Institut de Pharmacologie Moléculaire et Cellulaire, Valbonne, France.
Marc LitaudonInstitut de Chimie des Substances Naturelles, CNRS, Université Paris-Saclay, Gif-sur-Yvette, France.
Van-Cuong PhamAdvanced Center for Bioorganic Chemistry of the Institute of Marine Biochemistry, Vietnam Academy of Science and Technology, 18 Hoang Quoc Viet, 8404, Caugiay, Hanoi, Vietnam.
Jérôme BignonInstitut de Chimie des Substances Naturelles, CNRS, Université Paris-Saclay, Gif-sur-Yvette, France.
Bruno AntonnyUniversité Côte d'Azur, Inserm, CNRS, Institut de Pharmacologie Moléculaire et Cellulaire, Valbonne, France.
Fanny RoussiInstitut de Chimie des Substances Naturelles, CNRS, Université Paris-Saclay, Gif-sur-Yvette, France. Electronic address: fanny.roussi@cnrs.fr.
Bruno MesminUniversité Côte d'Azur, Inserm, CNRS, Institut de Pharmacologie Moléculaire et Cellulaire, Valbonne, France. Electronic address: mesmin@ipmc.cnrs.fr.
Centre National de la Recherche Scientifique · FRVietnam Academy of Science and Technology · VN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ORPphilins are bioactive natural products that strongly and selectively inhibit the growth of some cancer cell lines and are proposed to target intracellular lipid-transfer proteins of the oxysterol-binding protein (OSBP) family. These conserved proteins exchange key lipids, such as cholesterol and phosphatidylinositol 4-phosphate (PI(4)P), between organelle membranes. Among ORPphilins, molecules of the schweinfurthin family interfere with intracellular lipid distribution and metabolism, but their functioning at the molecular level is poorly understood. We report here that cell line sensitivity to schweinfurthin G (SWG) is inversely proportional to cellular OSBP levels. By taking advantage of the intrinsic fluorescence of SWG, we followed its fate in cell cultures and show that its incorporation at the

Indexed as

Biological TransportCarrier ProteinsEndoplasmic ReticulumFluorescenceHumansLipidsOxysterol Binding ProteinsProtein BindingProtein TransportReceptors, SteroidStilbenestrans-Golgi NetworkCarrier ProteinsLipidslipid transfer proteinOxysterol Binding ProteinsReceptors, Steroidschweinfurthin GStilbenescholesterolGolgilipid-transfer proteinlipid transportORPphilinOSBPphosphoinositideprotein drug interactionschweinfurthin

Identifiers

PMID32075908
PMCPMC7105299
OpenAlexW3008766857

What OpenQuestion holds

Textmetadata
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.