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- W1751904923 abstract "This chapter focuses on picornains 2A and 3C. They are synthesized in cells following infection by viruses of the family Picornaviridae. The sequences of the picornains are deduced from genomic sequences. Comparison of these sequences with protein data banks revealed similarity to sequences of trypsin and chymotrypsin-like serine proteinases. The active site nucleophile of the picornains is cysteine. The genetic information encoded in picornaviral genomes is expressed as a single polyprotein of about 2200 amino acids, which undergoes proteolytic processing to give the mature viral proteins. Translation of cloned complementary DNA (cDNA) fragments of picornaviral genomes in rabbit reticulocyte lysates (RRLs) allows the production of radiolabeled proteins corresponding to various parts of the polyprotein. To produce substrates for intermolecular cleavage, regions containing the picornain genes are excluded or only partially present. All picornains 2A and 3C are capable of cleaving oligopeptides with sequences derived from viral cleavage sites. Peptides should contain at least 12 amino acids (6 at either side of the cleavage site) for efficient cleavage." @default.
- W1751904923 created "2016-06-24" @default.
- W1751904923 creator A5017348458 @default.
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- W1751904923 date "1994-01-01" @default.
- W1751904923 modified "2023-09-26" @default.
- W1751904923 title "[40] Picornains 2A and 3C" @default.
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- W1751904923 doi "https://doi.org/10.1016/0076-6879(94)44042-5" @default.
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