Synthesis of 2-5As possessing base-modified adenosines and their activities to human recombinant RNase L.

Nucleic Acids Symp Ser

Laboratory of Molecular Biochemistry, Department of Biomolecular Science, Faculty of Engineering, Gifu University, Yanagido 1-1, Gifu 501-1193, Japan.

Published: October 2003

AI Article Synopsis

  • The 2',5'-oligoadenylate (2-5A) is a key player that inhibits protein translation in vertebrate cells by activating RNase L, an endoribonuclease.
  • This 2-5A mechanism is crucial in the body's defense against viral infections through interferon pathways.
  • The study discusses the creation of modified 2-5A derivatives, their engagement with RNase L, and their stability in biological settings.

Article Abstract

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.

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http://dx.doi.org/10.1093/nass/44.1.29DOI Listing

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