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• W2951781521 abstract "Abstract Small molecule probes are indispensable tools to explore diverse cellular events. However, finding a specific probe of a target remains a high challenge. Here we report the discovery of Fast-TRFS, a specific and superfast fluorogenic probe of mammalian thioredoxin reductase, a ubiquitous enzyme involved in regulation of diverse cellular redox signaling pathways. By systematically examining the processes of fluorophore release and reduction of cyclic disulfides/diselenides by the enzyme, structural factors that determine the response rate and specificity of the probe are disclosed. Mechanistic studies reveal that the fluorescence signal is switched on by a simple reduction of the disulfide bond within the probe, which is in stark contrast to the sensing mechanism of published probes. The favorable properties of Fast-TRFS enable development of a high-throughput screening assay to discover inhibitors of thioredoxin reductase by using crude tissue extracts as a source of the enzyme." @default.
• W2951781521 created "2019-06-27" @default.
• W2951781521 creator A5005426960 @default.
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• W2951781521 date "2019-06-21" @default.
• W2951781521 modified "2023-10-14" @default.
• W2951781521 title "A fast and specific fluorescent probe for thioredoxin reductase that works via disulphide bond cleavage" @default.
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• W2951781521 doi "https://doi.org/10.1038/s41467-019-10807-8" @default.
• W2951781521 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6588570" @default.
• W2951781521 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31227705" @default.
• W2951781521 hasPublicationYear "2019" @default.
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