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- W2060792571 abstract "Eukaryotes have evolved complex cellular responses to double-stranded RNA. One response that is highly conserved across many species is the RNA silencing pathway. Tombusviruses have evolved a mechanism to evade the RNA silencing pathway that involves a small protein, p19, that acts as a suppressor of RNA silencing. This protein binds specifically to small-interfering RNAs (siRNAs) with nanomolar affinity in a sequence-independent manner and with size selectivity. Here we demonstrate a new approach for rapidly determining the quantities of siRNA using fluorescence resonance energy transfer (FRET) between the Carnation Italian ringspot virus (CIRV) p19-CFP fusion protein and Cy3-labeled siRNA. The CIRV p19 fusion protein binds double-stranded siRNAs with nanomolar affinity as determined by FRET. [corrected]" @default.
- W2060792571 created "2016-06-24" @default.
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- W2060792571 creator A5042896311 @default.
- W2060792571 creator A5056030836 @default.
- W2060792571 date "2009-08-01" @default.
- W2060792571 modified "2023-10-07" @default.
- W2060792571 title "Studies of a viral suppressor of RNA silencing p19-CFP fusion protein: A FRET-based probe for sensing double-stranded fluorophore tagged small RNAs" @default.
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- W2060792571 doi "https://doi.org/10.1016/j.bpc.2009.05.001" @default.
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