Dissecting the roles of VP0 cleavage and RNA packaging in picornavirus capsid stabilization: the structure of empty capsids of foot-and-mouth disease virus.
Empty capsids of foot-and-mouth disease virus (FMDV) type A22 Iraq 24/64, whose structure has been solved by X-ray crystallography, are unusual for picornaviruses since they contain VP2 and VP4, the cleavage products of the protein precursor VP0. Both the N terminus of VP1 and the C terminus of VP4,...
Guardado en:
| Publicado en: | J Virol |
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| Autores principales: | , , , , , , , , |
| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
American Society for Microbiology (ASM)
1997
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| Materias: | |
| Acceso en línea: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC230284/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/9371640/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jvi.71.12.9743-9752.1997 |
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