Identification of the domain required for trans-cleavage activity of hepatitis C viral serine proteinase
- 5 August 1994
- Vol. 145 (2) , 215-219
- https://doi.org/10.1016/0378-1119(94)90008-6
Abstract
No abstract availableKeywords
Funding Information
- Ministry of Education, Culture, Sports, Science and Technology
- Ministry of Health and Welfare
This publication has 9 references indexed in Scilit:
- Two distinct proteinase activities required for the processing of a putative nonstructural precursor protein of hepatitis C virusJournal of Virology, 1993
- NS3 is a serine protease required for processing of hepatitis C virus polyproteinJournal of Virology, 1993
- Nonstructural protein 3 of the hepatitis C virus encodes a serine-type proteinase required for cleavage at the NS3/4 and NS4/5 junctionsJournal of Virology, 1993
- The Hepatitis C Virus Encodes a Serine Protease Involved in Processing of the Putative Nonstructural Proteins from the Viral Polyprotein PrecursorBiochemical and Biophysical Research Communications, 1993
- Expression and identification of hepatitis C virus polyprotein cleavage productsJournal of Virology, 1993
- Amino-terminal presequence of the precursor of peroxisomal 3-ketoacyl-CoA thiolase is a cleavable signal peptide for peroxisomal targetingBiochemical and Biophysical Research Communications, 1991
- Processing of the yellow fever virus nonstructural polyprotein: a catalytically active NS3 proteinase domain and NS2B are required for cleavages at dibasic sitesJournal of Virology, 1991
- Both nonstructural proteins NS2B and NS3 are required for the proteolytic processing of dengue virus nonstructural proteinsJournal of Virology, 1991
- Molecular structure of the Japanese hepatitis C viral genomeFEBS Letters, 1991