In vivo determination of substrate specificity of hepatitis C virus NS3 protease: Genetic assay for site-specific proteolysis

Analytical Biochemistry

Volumn 284, Issue 1, 2000, Pages 42-48

  Kim, Sung Yun ^a   Park, Kye Won ^a   Lee, Yong Jae ^a   Back, Sung Hoon ^b   Goo, Jae Hwan ^a   Park, Ohkmae K ^c   Jang, Sung Key ^b   Park, Woo Jin ^a  

^a Gwangju Institute of Science and Technology (GIST)   (South Korea)

^b Pohang University of Science and Technology (POSTECH)   (South Korea)

^c Kumho Life and Environmental Science Laboratory   (South Korea)

Author keywords

HCV; Protease; Randomized sequence; Saccharomyces cerevisae; Substrate specifity

Indexed keywords

CELL MEMBRANES; CELL PROLIFERATION; TRANSCRIPTION; VIRUSES; YEAST;

CYTOPLASMIC MEMBRANE; INTEGRAL MEMBRANE PROTEINS; INTRACELLULAR DOMAIN; PROTEASE; RANDOMIZED SEQUENCE; SACCHAROMYCES CEREVISAE; SPECIFITY; SUBSTRATE SPECIFICITY;

PROTEINS;

PROTEINASE; TRANSCRIPTION FACTOR; VIRUS ENZYME;

ARTICLE; CHEMICAL BOND; CONTROLLED STUDY; ENZYME SPECIFICITY; GENETIC SCREENING; HEPATITIS C VIRUS; IN VIVO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; SACCHAROMYCES CEREVISIAE; SEQUENCE ANALYSIS;

EID: 0034663698     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1006/abio.2000.4662     Document Type: Article

References (30)

1. Detection of antibody to hepatitis C virus in prospectively followed transfusion recipients with acute and chronic non-A, non-B hepatitis
2. Isolation of a cDNA clone derived from a blood-borne non-A, non-B viral hepatitis genome
3. Hepatitis C virus: Historical perspective and current concepts
4. Genetic organization and diversity of the hepatitis C virus
5. Structure and organization of the hepatitis C virus genome isolated from human carriers
6. Characterization of the hepatitis C virus encoded serine proteinase: Determination of proteinase-dependent polyprotein cleavage sites
7. Gene mapping of the putative structural region of the hepatitis C virus genome by in vitro processing analysis
8. A second hepatitis C virus-encoded proteinase
9. Hepatitis C virus-encoded NS2-3 protease: Cleavage-site mutagenesis and requirements for bimolecular cleavage
10. NS3 is a serine protease required for processing of hepatitis C virus polyprotein
11. Both NS3 and NS4A are required for proteolytic processing of hepatitis C virus nonstructural proteins
12. Hepatitis C virus NS3 serine proteinase: Trans-cleavage requirements and processing kinetics
13. An amino-terminal domain of the hepatitis C virus NS3 protease is essential for interaction with NS4A
14. NS3-4A of hepatitis C virus is a chymotrypsin-like protease
15. Identification of the protease domain in NS3 of hepatitis C virus
16. Product inhibition of the hepatitis C virus NS3 protease
17. Potent peptide inhibitors of human hepatitis C virus NS3 protease are obtained by optimizing the cleavage products
18. Specificity of the hepatitis C virus NS3 serine protease: Effects of substitutions at the 3/4A, 4A/4B, 4B/5A, and 5A/5B cleavage sites on polyprotein processing
19. Substrate determinants for cleavage in cis and in trans by the hepatitis C virus NS3 proteinase
20. Substrate specificity of the NS3 serine proteinase of hepatitis C virus as determined by mutagenesis at the NS3/NS4A junction
21. Substrate requirements of hepatitis C virus serine proteinase for intermolecular polypeptide cleavage in Escherichia coli
22. Activity of purified hepatitis C virus protease NS3 on peptide substrates
23. Substrate specificity of the hepatitis C virus serine protease NS3
24. Probing the substrate specificity of hepatitis C virus NS3 serine protease by using synthetic peptides
25. A cloning method to identify caspases and their regulators in yeast: Identification of Drosophila IAP1 as an inhibitor of the Drosophila caspase DCP-1
26. Improved method for high efficiency transformation of intact yeast cells
27. Genamic libraries and a host strain designed for highly efficient two-hybrid selection in yeast
28. Construction and use of gene fusions to lacZ (beta-galactosidase) that are expressed in yeast
29. Substrate phage: Selection of protease substrates by monovalent phage display
30. In vivo selection of protease cleavage sites from retrovirus display libraries