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-Reference-Cited by-同舟云学术

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

Published:1991-10 Issue:2 Volume:184 Page:707-715
ISSN:0042-6822
Container-title:Virology
language:en
Short-container-title:Virology

Author:

Wengler Gerd,Wengler Gisela

Publisher

Elsevier BV

Subject

Virology

Reference19 articles.

1. Detection of a trypsin-like serine protease domain in flaviviruses and pestiviruses;Bazan;Virology,1989

2. Primary structure of the West Nile flavivirus genome regions coding for all nonstructural proteins;Castle;Virology,1986

3. Flavivirus genome organization, expression, and replication;Chambers;Annu. Rev. Microbiol.,1990

4. Evidence that the N-terminal domain of nonstructural protein NS3 from yellow fever virus is a serine protease responsible for sitespecific cleavages in the viral polyprotein;Chambers,1990

5. Replication strategy of Kunjin virus: Evidence for recycling role of replicative form RNA as a template in semiconservative and asymmetric replication;Chu;Virology,1985

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