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- W2619839156 endingPage "7996" @default.
- W2619839156 startingPage "7984" @default.
- W2619839156 abstract "RGG/RG domains are the second most common RNA binding domain in the human genome, yet their RNA-binding properties remain poorly understood. Here, we report a detailed analysis of the RNA binding characteristics of intrinsically disordered RGG/RG domains from Fused in Sarcoma (FUS), FMRP and hnRNPU. For FUS, previous studies defined RNA binding as mediated by its well-folded domains; however, we show that RGG/RG domains are the primary mediators of binding. RGG/RG domains coupled to adjacent folded domains can achieve affinities approaching that of full-length FUS. Analysis of RGG/RG domains from FUS, FMRP and hnRNPU against a spectrum of contrasting RNAs reveals that each display degenerate binding specificity, while still displaying different degrees of preference for RNA." @default.
- W2619839156 created "2017-06-05" @default.
- W2619839156 creator A5004642468 @default.
- W2619839156 creator A5004741721 @default.
- W2619839156 creator A5008058647 @default.
- W2619839156 creator A5030273216 @default.
- W2619839156 creator A5039405203 @default.
- W2619839156 creator A5081014378 @default.
- W2619839156 date "2017-05-27" @default.
- W2619839156 modified "2023-10-14" @default.
- W2619839156 title "Intrinsically disordered RGG/RG domains mediate degenerate specificity in RNA binding" @default.
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- W2619839156 doi "https://doi.org/10.1093/nar/gkx460" @default.