Interplay between NS3 protease and human La protein regulates translation-replication switch of Hepatitis C virus
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/srep00001.pdf
Reference22 articles.
1. Barbato, G. et al. The solution structure of the N-terminal proteinase domain of the hepatitis C virus (HCV) NS3 protein provides new insights into its activation and catalytic mechanism. J. Mol. Biol. 289, 371–384 (1999).
2. Beran, R. K. F., Serebrov, V. & Pyle, A. M. The serine protease domain of hepatitis C viral NS3 activates RNA helicase activity by promoting the binding of RNA substrate. J. Biol. Chem. 282, 34913–34920 (2007).
3. Frick, D. N., Rypma, R. S., Lam, A. M. I. & Gu, B. The nonstructural protein 3 protease/helicase requires an intact protease domain to unwind duplex RNA efficiently. J. Biol. Chem. 279, 1269–1280 (2004).
4. Herold, J. & Andino, R. Poliovirus RNA replication requires genome circularization through a protein–protein bridge. Mol. Cell 7, 581–591 (2001).
5. Ali, N., Pruijn, G. J. M., Kenan, D. J., Keene, J. D. & Siddiqqui, A. Human La antigen is required for the Hepatitis C virus internal ribosome entry site mediated translation. J. Biol. Chem. 275, 27531–27540 (2000).
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