Substrate Specificity of the Hepatitis C Virus Serine Protease NS3

This publication has 50 references indexed in Scilit:

• A central hydrophobic domain of the hepatitis C virus NS4A protein is necessary and sufficient for the activation of the NS3 protease
  Journal of General Virology, 1996
• In Vitro Activity of Hepatitis C Virus Protease NS3 Purified from Recombinant Baculovirus-infected Sf9 Cells
  Journal of Biological Chemistry, 1996
• Distinct Mechanisms Contribute to Stringent Substrate Specificity of Tissue-type Plasminogen Activator
  Published by Elsevier ,1996
• Enzymatic characterization of purified NS3 serine proteinase of hepatitis C virus expressed in Escherichia coli
  FEBS Letters, 1996
• Stimulation of the Herpes Simplex Virus Type I Protease by Antichaeotrophic Salts
  Published by Elsevier ,1995
• In vivo and in vitro trans-cleavage activity of hepatitis C virus serine proteinase expressed by recombinant baculoviruses
  Journal of General Virology, 1995
• Recombinant baculovirus-expressed NS3 proteinase of hepatitis C virus shows activity in cell-based and in vitro assays
  Journal of General Virology, 1995
• In vitro cleavage of hepatitis C virus polyprotein substrates by purified recombinant NS3 protease
  Journal of General Virology, 1995
• Substrate specificity of porcine renin: P1', P1, and P3 residues of renin substrates are crucial for activity
  Biochemistry, 1994
• The Hepatitis C Virus Encodes a Serine Protease Involved in Processing of the Putative Nonstructural Proteins from the Viral Polyprotein Precursor
  Biochemical and Biophysical Research Communications, 1993