具有碱基修饰腺苷的2-5A的合成及其对人重组核糖核酸酶L的活性
Synthesis of 2-5As possessing base-modified adenosines and their activities to human recombinant RNase L.
作者信息
Kitade Y, Tanida Y, Tuboi T, Yoshimura A, Nakanishi M, Yatome C
机构信息
Laboratory of Molecular Biochemistry, Department of Biomolecular Science, Faculty of Engineering, Gifu University, Yanagido 1-1, Gifu 501-1193, Japan.
出版信息
Nucleic Acids Symp Ser. 2000(44):29-30. doi: 10.1093/nass/44.1.29.
The unique 2',5'-oligoadenylate (2-5A) acts as a potent inhibitor of translation in vertebrate cells through the activation of a constituent latent 2-5A-dependent endoribonuclease (RNase L). This 2-5A system plays a major role in the interferon natural defense mechanism against viral infection. We report the syntheses of base-modified adenosine-substituted 2-5A derivatives, their interaction with recombinant human RNase L and their biological stability.
独特的2',5'-寡腺苷酸（2-5A）通过激活潜在的2-5A依赖性核糖核酸内切酶（RNase L），在脊椎动物细胞中作为一种有效的翻译抑制剂。这个2-5A系统在干扰素抵抗病毒感染的天然防御机制中起主要作用。我们报道了碱基修饰的腺苷取代的2-5A衍生物的合成、它们与重组人RNase L的相互作用以及它们的生物稳定性。
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