Evidence map›Paper›PMID 30297865›Full record

ArticleScientific reports2018

Identification of pharmacological inhibitors of conventional protein secretion.

Liwei Zhao, Peng Liu, Gaelle Boncompain, Friedemann Loos, Sylvie Lachkar, Lucillia Bezu, Guo Chen, Heng Zhou, Franck Perez, Oliver Kepp and 1 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

10 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. ER exit in physiology and disease.Frontiers in molecular biosciences · 2024
    Review
  3. Article
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  5. Article
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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

11 authors at 3 institutions in 2 countries.

Liwei ZhaoFaculty of Medicine, University of Paris Sud, Kremlin-Bicêtre, France.
Peng LiuFaculty of Medicine, University of Paris Sud, Kremlin-Bicêtre, France.ORCID http://orcid.org/0000-0002-1682-9222
Gaelle BoncompainUniversité Pierre et Marie Curie, Paris, France.
Friedemann LoosCell Biology and Metabolomics Platforms, Gustave Roussy Cancer Campus, Villejuif, France.
Sylvie LachkarCell Biology and Metabolomics Platforms, Gustave Roussy Cancer Campus, Villejuif, France.
Lucillia BezuCell Biology and Metabolomics Platforms, Gustave Roussy Cancer Campus, Villejuif, France.
Guo ChenCell Biology and Metabolomics Platforms, Gustave Roussy Cancer Campus, Villejuif, France.
Heng ZhouFaculty of Medicine, University of Paris Sud, Kremlin-Bicêtre, France.
Franck PerezUniversité Pierre et Marie Curie, Paris, France.ORCID http://orcid.org/0000-0002-9129-9401
Oliver KeppFaculty of Medicine, University of Paris Sud, Kremlin-Bicêtre, France. captain.olsen@gmail.com.ORCID http://orcid.org/0000-0002-6081-9558
Guido KroemerCell Biology and Metabolomics Platforms, Gustave Roussy Cancer Campus, Villejuif, France. kroemer@orange.fr.
Délégation Paris 5 · FRUniversité Paris-Sud · FRCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The retention using selective hooks (RUSH) system allows to withhold a fluorescent biosensor such as green fluorescent protein (GFP) fused to a streptavidin-binding peptide (SBP) by an excess of streptavidin molecules that are addressed to different subcellular localizations. Addition of biotin competitively disrupts this interaction, liberating the biosensor from its hook. We constructed a human cell line co-expressing soluble secretory-SBP-GFP (ss-SBP-GFP) and streptavidin within the endoplasmic reticulum (ER) lumen and then used this system to screen a compound library for inhibitors of the biotin-induced release of ss-SBP-GFP via the conventional Golgi-dependent protein secretion pathway into the culture supernatant. We identified and validated a series of molecularly unrelated drugs including antianginal, antidepressant, anthelmintic, antipsychotic, antiprotozoal and immunosuppressive agents that inhibit protein secretion. These compounds vary in their capacity to suppress protein synthesis and to compromise ER morphology and Golgi integrity, as well as in the degree of reversibility of such effects. In sum, we demonstrate the feasibility and utility of a novel RUSH-based phenotypic screening assay.

Indexed as

Cell Line, TumorCluster AnalysisDrug Evaluation, PreclinicalEndoplasmic ReticulumGolgi ApparatusHigh-Throughput Screening AssaysHumansPrincipal Component AnalysisProtein BiosynthesisProteinsProtein Structure, SecondaryReproducibility of ResultsProteins

Identifiers

PMID30297865
PMCPMC6175952
OpenAlexW2895489046

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.