{"title":"利用荧光共振能量转移(FRET)测定2-5A类似物激活RNase L的能力。","authors":"H Cramer, D A Geselowitz, P F Torrence","doi":"10.1080/07328319908044776","DOIUrl":null,"url":null,"abstract":"<p><p>The development of a method for measuring the ability of 2-5A analogues to activate the cleavage of an oligoribonucleotide substrate by RNase L is described. This method is based on fluorescence resonance energy transfer. The method is easily performed with 96-well plates, allowing for quantitative high-throughput analyses of 2-5A analogues under different reaction conditions.</p>","PeriodicalId":19222,"journal":{"name":"Nucleosides & nucleotides","volume":"18 6-7","pages":"1523-5"},"PeriodicalIF":0.0000,"publicationDate":"1999-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/07328319908044776","citationCount":"1","resultStr":"{\"title\":\"Using fluorescence resonance energy transfer (FRET) for measuring 2-5A analogues ability to activate RNase L.\",\"authors\":\"H Cramer, D A Geselowitz, P F Torrence\",\"doi\":\"10.1080/07328319908044776\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The development of a method for measuring the ability of 2-5A analogues to activate the cleavage of an oligoribonucleotide substrate by RNase L is described. This method is based on fluorescence resonance energy transfer. The method is easily performed with 96-well plates, allowing for quantitative high-throughput analyses of 2-5A analogues under different reaction conditions.</p>\",\"PeriodicalId\":19222,\"journal\":{\"name\":\"Nucleosides & nucleotides\",\"volume\":\"18 6-7\",\"pages\":\"1523-5\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1999-06-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1080/07328319908044776\",\"citationCount\":\"1\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Nucleosides & nucleotides\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1080/07328319908044776\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Nucleosides & nucleotides","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1080/07328319908044776","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Using fluorescence resonance energy transfer (FRET) for measuring 2-5A analogues ability to activate RNase L.
The development of a method for measuring the ability of 2-5A analogues to activate the cleavage of an oligoribonucleotide substrate by RNase L is described. This method is based on fluorescence resonance energy transfer. The method is easily performed with 96-well plates, allowing for quantitative high-throughput analyses of 2-5A analogues under different reaction conditions.
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