Interferon action: two distinct pathways for inhibition of protein synthesis by double-stranded RNA.
- 1 December 1978
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 75 (12) , 5893-5897
- https://doi.org/10.1073/pnas.75.12.5893
Abstract
Double-stranded RNA inhibits protein synthesis in at least 2 ways. It activates a protein kinase that blocks peptide chain initiation by phosphorylating the peptide chain initiation factor eIF-2 and also activates an endonuclease that inactivates different mRNA at different rates. The protein kinase and the endonuclease were partially purified from interferon-treated [mouse] Ehrlich ascites tumor cells. The 2'',5''-oligoadenylates [pppA(2''p5''A)n], found earlier to be mediators in the activation of the endonuclease by double-stranded RNA, are not mediators in the activation of the protein kinase by double-stranded RNA. [These findings have relevance to the mechanism of the antiviral effect of interferon.].This publication has 28 references indexed in Scilit:
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