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The rubella virus nonstructural protease recognizes itself via an internal sequence present upstream of the cleavage site for trans-activity
The substrate requirement for rubella virus protease trans-activity is unknown. Here, we analyzed the cleavability of RV P200-derived substrates varying in their N-terminal lengths (72–475 amino acids) from the cleavage site by the RV protease trans-activity. Only substrates with at least 309 amino...
| Autores principales: | , , |
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| Formato: | Online Artículo Texto |
| Lenguaje: | English |
| Publicado: |
Springer-Verlag
2006
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| Materias: | |
| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7086818/ https://www.ncbi.nlm.nih.gov/pubmed/16570206 http://dx.doi.org/10.1007/s00705-006-0744-9 |