Site-specific mutations at a picornavirus VP3/VP1 cleavage site disrupt in vitro processing and assembly of capsid precursors.
Most proteolytic cleavages within the picornavirus polyproteins are carried out by viral protease 3C. For encephalomyocarditis virus, the protease 3C-catalyzed processing occurs between Gln-Gly or Gln-Ser amino acid pairs which are flanked by proline residues, but the sequence-specific constraints o...
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| Gepubliceerd in: | J Virol |
|---|---|
| Hoofdauteurs: | , |
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
American Society for Microbiology (ASM)
1987
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC255979/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/2824807/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jvi.61.12.3680-3687.1987 |
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