ArticlePloS one2018
Saccharomyces cerevisiae as a platform for assessing sphingolipid lipid kinase inhibitors.
Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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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.
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Who cites it
6 citing papers in PubMed.
- Discovery of In Vivo Active Sphingosine-1-phosphate Transporter (Spns2) Inhibitors.Journal of medicinal chemistry · 2022Article
- Article
- Probing the substitution pattern of indole-based scaffold reveals potent and selective sphingosine kinase 2 inhibitors.European journal of medicinal chemistry · 2021Article
- Lipophilic tail modifications of 2-(hydroxymethyl)pyrrolidine scaffold reveal dual sphingosine kinase 1 and 2 inhibitors.Bioorganic & medicinal chemistry · 2021Article
- Mechanism of sphingosine 1-phosphate clearance from blood.The Biochemical journal · 2020Article
- Discovery of a Small Side Cavity in Sphingosine Kinase 2 that Enhances Inhibitor Potency and Selectivity.Journal of medicinal chemistry · 2020Article
Corrections and comments
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Authors and funding
10 authors.
Funding
Abstract
Successful medicinal chemistry campaigns to discover and optimize sphingosine kinase inhibitors require a robust assay for screening chemical libraries and for determining rank order potencies. Existing assays for these enzymes are laborious, expensive and/or low throughput. The toxicity of excessive levels of phosphorylated sphingoid bases for the budding yeast, Saccharomyces cerevisiae, affords an assay wherein inhibitors added to the culture media rescue growth in a dose-dependent fashion. Herein, we describe our adaptation of a simple, inexpensive, and high throughput assay for assessing inhibitors of sphingosine kinase types 1 and 2 as well as ceramide kinase and for testing enzymatic activity of sphingosine kinase type 2 mutants. The assay was validated using recombinant enzymes and generally agrees with the rank order of potencies of existing inhibitors.
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Registered trials
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