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• W2365953208 endingPage "757" @default.
• W2365953208 startingPage "744" @default.
• W2365953208 abstract "RNA molecules with high affinity to specific proteins can be isolated from libraries of up to 10 16 different RNA sequences by systematic evolution of ligands by exponential enrichment ( SELEX ). These so‐called protein‐binding RNA aptamers are often interesting, e.g., as modulators of protein function for therapeutic use, for probing the conformations of proteins, for studies of basic aspects of nucleic acid–protein interactions, etc. Studies on the interactions between RNA aptamers and proteins display a number of expected and unexpected features, including the chemical nature of the interacting RNA ‐protein surfaces, the conformation of protein‐bound aptamer versus free aptamer, the conformation of aptamer‐bound protein versus free protein, and the effects of aptamers on protein function. Here, we review current insights into the details of RNA aptamer–protein interactions. WIREs RNA 2016, 7:744–757. doi: 10.1002/wrna.1360 This article is categorized under: RNA Interactions with Proteins and Other Molecules > Protein–RNA Recognition RNA Interactions with Proteins and Other Molecules > RNA–Protein Complexes RNA Interactions with Proteins and Other Molecules > Protein–RNA Interactions: Functional Implications" @default.
• W2365953208 created "2016-06-24" @default.
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• W2365953208 date "2016-05-12" @default.
• W2365953208 modified "2023-10-10" @default.
• W2365953208 title "Expected and unexpected features of protein‐binding <scp>RNA</scp> aptamers" @default.
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• W2365953208 doi "https://doi.org/10.1002/wrna.1360" @default.
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