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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Detalles Bibliográficos
Autores principales: Chen, H. H., Stark, C. J., Atreya, C. D.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer-Verlag 2006
Materias:
Article
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

Internet

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

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