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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,...

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書目詳細資料
發表在:	J Virol
Principais autores:	Curry, S, Fry, E, Blakemore, W, Abu-Ghazaleh, R, Jackson, T, King, A, Lea, S, Newman, J, Stuart, D
格式:	Artigo
語言:	Inglês
出版:	American Society for Microbiology (ASM) 1997
主題:	Research Article
在線閱讀:	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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Dissecting the roles of VP0 cleavage and RNA packaging in picornavirus capsid stabilization: the structure of empty capsids of foot-and-mouth disease virus.

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