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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...
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| Опубликовано в: : | Arch Virol |
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| Главные авторы: | , , |
| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
Springer-Verlag
2006
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| Предметы: | |
| Online-ссылка: | https://ncbi.nlm.nih.gov/pmc/articles/PMC7086818/ https://ncbi.nlm.nih.gov/pubmed/16570206 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1007/s00705-006-0744-9 |
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