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• W2025453290 startingPage "4266" @default.
• W2025453290 abstract "FXR (farnesoid X receptor, NRIH4), a nuclear receptor, plays a major role in the control of cholesterol metabolism. FXR ligands have been investigated in preclinical studies for targeted therapy against metabolic diseases, but have shown limitations. Therefore, there is a need for new agonist or antagonist ligands of FXR, both for potential clinical applications, as well as to further elucidate its biological functions. Here we describe the use of the X-ray crystal structure of FXR complexed with the potent small molecule agonist GW4064 to design and synthesize a novel fluorescent, high-affinity probe (DY246) for time resolved fluorescence resonance energy transfer (TR-FRET) assays. We then used the TR-FRET assay for high throughput screening of a library of over 5000 bioactive compounds. From this library, we identified 13 compounds that act as putative FXR transcriptional antagonists." @default.
• W2025453290 created "2016-06-24" @default.
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• W2025453290 creator A5013524274 @default.
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• W2025453290 date "2013-07-01" @default.
• W2025453290 modified "2023-09-27" @default.
• W2025453290 title "Development of time resolved fluorescence resonance energy transfer-based assay for FXR antagonist discovery" @default.
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• W2025453290 doi "https://doi.org/10.1016/j.bmc.2013.04.069" @default.
• W2025453290 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3691817" @default.
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• W2025453290 hasPublicationYear "2013" @default.
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