Cell-free translation of influenza virus messenger RNA

Virology ◽  
1973 ◽  
Vol 56 (2) ◽  
pp. 654-657 ◽  
Author(s):  
D.W. Kingsbury ◽  
R.G. Webster
Keyword(s):  
Influenza Virus ◽  
Messenger Rna ◽  
Free Translation

Glucagon precursors identified by immunoprecipitation of products of cell-free translation of messenger RNA

Diabetes ◽  
1980 ◽  
Vol 29 (7) ◽  
pp. 583-586 ◽  
Author(s):  
P. K. Lund ◽  
R. H. Goodman ◽  
J. W. Jacobs ◽  
J. F. Habener
Keyword(s):  
Messenger Rna ◽  
Free Translation

Evidence for a nuclease in Saccharomycescerevisiae that affects the cell-free translation of natural messenger RNA

1979 ◽  
Vol 88 (4) ◽  
pp. 1263-1270 ◽  
Author(s):  
Flor Herrera ◽  
Eugeniusz Gasior ◽  
Calvin S. McLaughlin ◽  
Kivie Moldave
Keyword(s):  
Messenger Rna ◽  
Free Translation

Mesoionic Heterocyclic Compounds as Candidate Messenger RNA Cap Analogue Inhibitors of the Influenza Virus RNA Polymerase Cap-Binding Activity

2009 ◽  
Vol 19 (5) ◽  
pp. 213-218 ◽  
Author(s):  
Ian Mickleburgh ◽  
Feng Geng ◽  
Laurence Tiley
Keyword(s):  
Influenza Virus ◽  
Rna Polymerase ◽  
Messenger Rna ◽  
Binding Activity ◽  
Endonucleolytic Cleavage ◽  
Virus Rna ◽  
Fused Ring ◽  
Mesoionic Heterocycles ◽  
Potential Inhibitors

Background: An unusual feature of influenza viral messenger RNA (mRNA) synthesis is its dependence upon host cell mRNAs as a source of capped RNA primers. A crucial activity of the influenza polymerase is to steal these primers by binding and cleaving the caps from host mRNAs. The recent structural analysis of the cap-binding fragment of the influenza virus PB2 protein has highlighted the importance of the mesoionic properties of the N7-methylguanine (N7mG) component of the mRNA cap in this interaction. Methods: A series of mesoionic heterocycles with 5,6-fused ring systems analogous to the N7mG component of mRNA cap structures were synthesized and examined for the ability to inhibit the cap-binding activity of the influenza virus RNA polymerase complex using a bead-based in vitro cap-binding assay. Results: None of the compounds tested were able to significantly inhibit binding and subsequent endonucleolytic cleavage of a synthetic radiolabelled capped mRNA substrate by recombinant influenza virus polymerase in vitro. Conclusions: Compounds analogous to the mesoionic N7mG component of mRNA cap structures comprise a large class of potential inhibitors of the influenza virus polymerase. Although this preliminary assessment of a small group of related analogues was unsuccessful, further screening of this class of compounds is warranted.

Cell-free translation of messenger RNA coding for a precursor of human calcitonin

1979 ◽  
Vol 91 (3) ◽  
pp. 932-938 ◽  
Author(s):  
Richard H. Goodman ◽  
John W. Jacobs ◽  
Joel F. Habener
Keyword(s):  
Messenger Rna ◽  
Human Calcitonin ◽  
Free Translation

scholarly journals Cell-Free Translation of Messenger RNA of Simian Virus 40: Synthesis of the Major Capsid Protein

1974 ◽  
Vol 71 (2) ◽  
pp. 302-306 ◽  
Author(s):  
C. L. Prives ◽  
H. Aviv ◽  
B. M. Paterson ◽  
B. E. Roberts ◽  
S. Rozenblatt ◽  
...  
Keyword(s):  
Capsid Protein ◽  
Messenger Rna ◽  
Major Capsid Protein ◽  
Simian Virus 40 ◽  
Simian Virus ◽  
Free Translation
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