Crystal Structure of the Hepatitis C Virus NS3 Protease Domain Complexed with a Synthetic NS4A Cofactor Peptide
- 1 October 1996
- Vol. 87 (2) , 343-355
- https://doi.org/10.1016/s0092-8674(00)81351-3
Abstract
No abstract availableKeywords
This publication has 73 references indexed in Scilit:
- At least 12 genotypes of hepatitis C virus predicted by sequence analysis of the putative E1 gene of isolates collected worldwide.Proceedings of the National Academy of Sciences, 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
- Free R value: a novel statistical quantity for assessing the accuracy of crystal structuresNature, 1992
- RIBBONS 2.0Journal of Applied Crystallography, 1991
- 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.Proceedings of the National Academy of Sciences, 1990
- Detection of Antibody to Hepatitis C Virus in Prospectively Followed Transfusion Recipients with Acute and Chronic Non-A, Non-B HepatitisNew England Journal of Medicine, 1989
- Detection of a trypsin-like serine protease domain in flaviviruses and pestvirusesVirology, 1989
- Yellow fever virus proteins NS2A, NS213, and NS4B: Identification and partial N-terminal amino acid sequence analysisVirology, 1989
- Weakly Polar Interactions In ProteinsAdvances in Protein Chemistry, 1988
- Chymotrypsin: Molecular and catalytic propertiesClinical Biochemistry, 1986