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NS3 is a serine protease required for processing of hepatitis C virus polyprotein.
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Crystal structure of the RNA-dependent RNA polymerase of hepatitis C virus.
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Both NS3 and NS4A are required for proteolytic processing of hepatitis C virus nonstructural proteins.
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1990
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1998
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1.90
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9
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An amino-terminal domain of the hepatitis C virus NS3 protease is essential for interaction with NS4A.
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J Virol
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1995
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1.78
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10
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Hyperphosphorylation of the hepatitis C virus NS5A protein requires an active NS3 protease, NS4A, NS4B, and NS5A encoded on the same polyprotein.
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J Virol
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1999
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1.75
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Molecular model of the specificity pocket of the hepatitis C virus protease: implications for substrate recognition.
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The solution structure of the N-terminal proteinase domain of the hepatitis C virus (HCV) NS3 protein provides new insights into its activation and catalytic mechanism.
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J Mol Biol
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1999
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1.44
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14
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A continuous assay of hepatitis C virus protease based on resonance energy transfer depsipeptide substrates.
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Anal Biochem
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1.40
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Activity of purified hepatitis C virus protease NS3 on peptide substrates.
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J Virol
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1.32
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16
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Product inhibition of the hepatitis C virus NS3 protease.
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Biochemistry
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1.32
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17
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A central hydrophobic domain of the hepatitis C virus NS4A protein is necessary and sufficient for the activation of the NS3 protease.
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J Gen Virol
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1996
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1.29
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18
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GB virus B and hepatitis C virus NS3 serine proteases share substrate specificity.
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J Virol
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Biochemical characterization of a hepatitis C virus RNA-dependent RNA polymerase mutant lacking the C-terminal hydrophobic sequence.
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J Gen Virol
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Enzymatic properties of hepatitis C virus NS3-associated helicase.
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J Gen Virol
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In vitro activity of hepatitis C virus protease NS3 purified from recombinant Baculovirus-infected Sf9 cells.
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J Biol Chem
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1996
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1.09
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24
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Potent peptide inhibitors of human hepatitis C virus NS3 protease are obtained by optimizing the cleavage products.
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Biochemistry
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1998
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1.07
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25
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Modulation of hepatitis C virus NS3 protease and helicase activities through the interaction with NS4A.
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Biochemistry
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1999
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1.06
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26
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Affinity selection of a camelized V(H) domain antibody inhibitor of hepatitis C virus NS3 protease.
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Protein Eng
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1997
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1.06
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27
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Inhibition of the hepatitis C virus NS3/4A protease. The crystal structures of two protease-inhibitor complexes.
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J Biol Chem
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2000
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1.04
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28
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Substrate specificity of the hepatitis C virus serine protease NS3.
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J Biol Chem
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1997
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1.01
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29
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The metal binding site of the hepatitis C virus NS3 protease. A spectroscopic investigation.
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J Biol Chem
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1998
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1.01
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30
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Structural characterization of the interactions of optimized product inhibitors with the N-terminal proteinase domain of the hepatitis C virus (HCV) NS3 protein by NMR and modelling studies.
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J Mol Biol
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1999
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0.99
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31
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Mutational analysis of hepatitis C virus NS3-associated helicase.
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2000
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Conformational changes in the NS3 protease from hepatitis C virus strain Bk monitored by limited proteolysis and mass spectrometry.
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Protein Sci
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1999
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0.97
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33
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The three-dimensional NMR-solution structure of the polypeptide fragment 195-286 of the LFB1/HNF1 transcription factor from rat liver comprises a nonclassical homeodomain.
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EMBO J
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1993
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0.96
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34
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Alpha-ketoacids are potent slow binding inhibitors of the hepatitis C virus NS3 protease.
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Biochemistry
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35
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The dimerization domain of LFB1/HNF1 related transcription factors: a hidden four helix bundle?
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Protein Eng
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1992
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36
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Multiple determinants influence complex formation of the hepatitis C virus NS3 protease domain with its NS4A cofactor peptide.
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Biochemistry
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Inhibitor binding induces active site stabilization of the HCV NS3 protein serine protease domain.
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2000
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0.90
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Synthetic depsipeptide substrates for the assay of human hepatitis C virus protease.
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39
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1H resonance assignment and secondary structure determination of the dimerization domain of transcription factor LFB1.
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Biochemistry
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1991
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Rational design and functional expression of a constitutively active single-chain NS4A-NS3 proteinase.
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1998
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41
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Redesigning the substrate specificity of the hepatitis C virus NS3 protease.
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42
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Complex formation between the hepatitis C virus serine protease and a synthetic NS4A cofactor peptide.
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Biochemistry
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1997
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43
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Probing the active site of the hepatitis C virus serine protease by fluorescence resonance energy transfer.
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J Biol Chem
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2000
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Characterization of engineered hepatitis C virus NS3 protease inhibitors affinity selected from human pancreatic secretory trypsin inhibitor and minibody repertoires.
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J Virol
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1997
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45
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Flavodoxin-cytochrome c interactions: circular dichroism and nuclear magnetic resonance studies.
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Biochemistry
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1987
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46
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Selection of functional variants of the NS3-NS4A protease of hepatitis C virus by using chimeric sindbis viruses.
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47
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A loop-mimetic inhibitor of the HCV-NS3 protease derived from a minibody.
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48
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LFB1/HNF1 acts as a repressor of its own transcription.
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Nucleic Acids Res
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49
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Why is it so difficult to develop a hepatitis C virus preventive vaccine?
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Time dependent density functional theory of X-ray absorption spectroscopy of alkaline-earth oxides.
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X-ray absorption spectroscopy of titanium oxide by time dependent density functional calculations.
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A high-throughput radiometric assay for hepatitis C virus NS3 protease.
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Anal Biochem
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Design of selective eglin inhibitors of HCV NS3 proteinase.
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Biochemistry
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Measurement of homonuclear three-bond J(H(N)Halpha) coupling constants in unlabeled peptides complexed with labeled proteins: application to a decapeptide inhibitor bound to the proteinase domain of the NS3 protein of hepatitis C virus (HCV).
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J Biomol NMR
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Spin-orbit relativistic calculations of the core excitation spectra of SO2.
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