The carboxy-terminal part of the NS 3 protein of the West Nile Flavivirus can be isolated as a soluble protein after proteolytic cleavage and represents an RNA-stimulated NTPase
- 17 June 2004
- journal article
- Published by Elsevier
- Vol. 184 (2) , 707-715
- https://doi.org/10.1016/0042-6822(91)90440-m
Abstract
No abstract availableKeywords
This publication has 18 references indexed in Scilit:
- In vitro synthesis of West Nile virus proteins indicates that the amino-terminal segment of the NS3 protein contains the active centre of the protease which cleaves the viral polyprotein after multiple basic amino acidsJournal of General Virology, 1991
- FLAVIVIRUS GENOME ORGANIZATION, EXPRESSION, AND REPLICATIONAnnual Review of Microbiology, 1990
- Homologous potyvirus and flavivirus proteins belonging to a superfamily of helicase-like proteinsGene, 1989
- Detection of a trypsin-like serine protease domain in flaviviruses and pestvirusesVirology, 1989
- A new superfamily of replicative proteinsNature, 1988
- Characterization of Kunjin virus RNA-dependent RNA polymerase: Reinitiation of synthesis in VitroVirology, 1987
- Primary structure of the West Nile flavivirus genome region coding for all nonstructural proteinsVirology, 1986
- Replication strategy of Kunjin Virus: Evidence for recycling role of replicative form RNA as template in semiconservative and asymmetric replicationVirology, 1985
- FlaviviridaeIntervirology, 1985
- A two-dimensional fractionation procedure for radioactive nucleotidesJournal of Molecular Biology, 1965