Product release is rate-limiting for catalytic processing by the Dengue virus protease
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/srep37539.pdf
Reference44 articles.
1. Bhatt, S. et al. The global distribution and burden of dengue. Nature 496, 504–507 (2013).
2. Bazan, J. F. & Fletterick, R. J. Detection of a trypsin-like serine protease domain in flaviviruses and pestiviruses. Virol. 171, 637–639 (1989).
3. Chambers, T. J., Hahn, C. S., Galler, R. & Rice, C. M. Flavivirus genome organisation, expression, and replication. Annu. Rev. Microbiol. 44, 649–688 (1990).
4. Chambers, T. J. et al. Evidence that the N-terminal domain of nonstructural protein NS3 from Yellow-Fever Virus is a serine protease responsible for site-specific cleavages in the viral polyprotein. Proc. Natl. Acad. Sci. USA 87, 8898–8902 (1990).
5. Erbel, P. et al. Structural basis for the activation of flaviviral NS3 proteases from dengue and west nile virus. Nat. Struct. Mol. Biol. 13, 372–373 (2006).
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