The Two-component NS2B-NS3 Proteinase Represses DNA Unwinding Activity of the West Nile Virus NS3 Helicase
Open Access
- 1 June 2008
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 283 (25) , 17270-17278
- https://doi.org/10.1074/jbc.m801719200
Abstract
No abstract availableKeywords
This publication has 53 references indexed in Scilit:
- Crystal Structure of the NS3 Protease-Helicase from Dengue VirusJournal of Virology, 2008
- Crystal Structure and Activity of Kunjin Virus NS3 Helicase; Protease and Helicase Domain Assembly in the Full Length NS3 ProteinPublished by Elsevier ,2007
- Switching the Substrate Specificity of the Two-Component NS2B-NS3 Flavivirus Proteinase by Structure-Based MutagenesisJournal of Virology, 2007
- Structural evidence for regulation and specificity of flaviviral proteases and evolution of the Flaviviridae foldProtein Science, 2007
- Expression and purification of a two-component flaviviral proteinase resistant to autocleavage at the NS2B–NS3 junction regionProtein Expression and Purification, 2007
- Cleavage preference distinguishes the two-component NS2B–NS3 serine proteinases of Dengue and West Nile virusesBiochemical Journal, 2007
- Structure-Based Mutational Analysis of the NS3 Helicase from Dengue VirusJournal of Virology, 2006
- Nuclear Localization of Flavivirus RNA Synthesis in Infected CellsJournal of Virology, 2006
- The hepatitis C viral NS3 protein is a processive DNA helicase with cofactor enhanced RNA unwindingThe EMBO Journal, 2002
- RETRACTED: Crystal structure of dengue virus NS3 protease in complex with a bowman-birk inhibitor: implications for flaviviral polyprotein processing and drug designJournal of Molecular Biology, 2000