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- W2037802912 abstract "Prion disease is caused by conformational change of normal cellular type of prion protein (PrPc) folding into abnormal type (PrPsc). We succeeded to isolate anti-PrPc aptamers. In the presence of competitor RNA, anti-PrPc aptamers showed high affinity to PrPc (Kd=10 nM). Heparin has prion binding affinity and partially interfered binding of the aptamer to PrPc. 2′-Fluoro pyrimidine nucleotide modification still restored their binding affinity (Kd=20 nM), which was applied for conventional dot- and western-blot assay like as antibody. We also succeeded to isolate anti-PrPsc aptamers appearing higher affinity to PrPsc in a dose-dependent manner. There is no sequence homology between those anti-PrPc and anti-PrPsc aptamers." @default.
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- W2037802912 date "2005-09-01" @default.
- W2037802912 modified "2023-09-25" @default.
- W2037802912 title "In vitro selection of RNA aptamers against cellular and abnormal isoform of mouse prion protein" @default.
- W2037802912 doi "https://doi.org/10.1093/nass/49.1.361" @default.
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