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Volumn 6, Issue 3, 1999, Pages 165-181

The NS3/4A proteinase of the hepatitis C virus: Unravelling structure and function of an unusual enzyme and a prime target for antiviral therapy

Author keywords

HCV replication; HCV specific antiviral therapy; HCV specific drug targets; Hepatitis C virus; NS3 4A proteinase; Three dimensional structure of NS3 4A HCV proteinase

Indexed keywords

PHENANTHRENE DERIVATIVE; PROTEINASE; SERINE PROTEINASE INHIBITOR; THIAZOLIDINE DERIVATIVE;

EID: 0032974384     PISSN: 13520504     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2893.1999.00152.x     Document Type: Review
Times cited : (129)

References (150)
  • 1
    • 0031851113 scopus 로고    scopus 로고
    • Chronic hepatitis C: The virus, its discovery and the natural history of the disease
    • Booth JL. Chronic hepatitis C: the virus, its discovery and the natural history of the disease. J Viral Hep 1998; 5: 213-222.
    • (1998) J Viral Hep , vol.5 , pp. 213-222
    • Booth, J.L.1
  • 2
    • 0000361013 scopus 로고    scopus 로고
    • Hepatitis C viruses
    • Fields BN, Knipe PM, Howley PM, eds. Philadelphia: Lippincott-Raven
    • Houghton M. Hepatitis C viruses. In: Fields BN, Knipe PM, Howley PM, eds. Virology. 4th edn. Philadelphia: Lippincott-Raven, 1998: 1035-1058.
    • (1998) Virology. 4th Edn. , pp. 1035-1058
    • Houghton, M.1
  • 4
    • 0030955346 scopus 로고    scopus 로고
    • Epidemiology of hepatitis C
    • Alter MJ. Epidemiology of hepatitis C. Hepatology 1997; 26: 62S-65S.
    • (1997) Hepatology , vol.26
    • Alter, M.J.1
  • 5
    • 0031884766 scopus 로고    scopus 로고
    • Hepatitis C virus: Epidemiology, transmission and prevention
    • van-der Poel, Ebeling F. Hepatitis C virus: epidemiology, transmission and prevention. Curr Stud Hematol Blood Transfus 1998; 62: 208-236.
    • (1998) Curr Stud Hematol Blood Transfus , vol.62 , pp. 208-236
    • Poel, V.-D.1    Ebeling, F.2
  • 6
    • 0030928696 scopus 로고    scopus 로고
    • Therapy of hepatitis C
    • Lindsay KL. Therapy of hepatitis C. Overview Hepatol 1997; 26: 71S-77S.
    • (1997) Overview Hepatol , vol.26
    • Lindsay, K.L.1
  • 8
    • 0031898959 scopus 로고    scopus 로고
    • Virus-encoded proteinases of the Flaviviridae
    • Ryan MD, Monaghan S, Flint M. Virus-encoded proteinases of the Flaviviridae. J Gen Virol 1998; 79: 947-959.
    • (1998) J Gen Virol , vol.79 , pp. 947-959
    • Ryan, M.D.1    Monaghan, S.2    Flint, M.3
  • 9
    • 0029166009 scopus 로고
    • Genomic organization of GB viruses A and B: Two new members of the Flaviviridae associated with GB agent hepatitis
    • Muerhoff AS, Leary TP, Simons JN et al. Genomic organization of GB viruses A and B: two new members of the Flaviviridae associated with GB agent hepatitis. J Virol 1995; 69: 5621-5630.
    • (1995) J Virol , vol.69 , pp. 5621-5630
    • Muerhoff, A.S.1    Leary, T.P.2    Simons, J.N.3
  • 11
    • 0030823630 scopus 로고    scopus 로고
    • Secondary structure determination of the conserved 98-base sequence at the 3′ terminus of hepatitis C virus genome RNA
    • Blight KJ, Rice CM. Secondary structure determination of the conserved 98-base sequence at the 3′ terminus of hepatitis C virus genome RNA. J Virol 1997; 71: 7345-7352.
    • (1997) J Virol , vol.71 , pp. 7345-7352
    • Blight, K.J.1    Rice, C.M.2
  • 12
    • 0026674719 scopus 로고
    • Secondary structure of the 5′ nontranslated regions of hepatitis C virus and pestivirus genomic RNAs
    • Brown EA, Zhang H, Ping LH, Lemon SM. Secondary structure of the 5′ nontranslated regions of hepatitis C virus and pestivirus genomic RNAs. Nucl Acids Res 1992; 20: 5041-5045.
    • (1992) Nucl Acids Res , vol.20 , pp. 5041-5045
    • Brown, E.A.1    Zhang, H.2    Ping, L.H.3    Lemon, S.M.4
  • 13
    • 0029938477 scopus 로고    scopus 로고
    • Identification of a highly conserved sequence element at the 3′ terminus of hepatitis C virus genome RNA
    • Kolykhalov AA, Feinstone SM, Rice CM. Identification of a highly conserved sequence element at the 3′ terminus of hepatitis C virus genome RNA. J Virol 1996; 70: 3363-3371.
    • (1996) J Virol , vol.70 , pp. 3363-3371
    • Kolykhalov, A.A.1    Feinstone, S.M.2    Rice, C.M.3
  • 14
    • 0028785460 scopus 로고
    • A novel sequence found at the 3′ terminus of hepatitis C virus genome
    • Tanaka T, Kato N, Cho MJ, Shimotohno K. A novel sequence found at the 3′ terminus of hepatitis C virus genome. Biochem Biophys Res Commun 1995; 215: 744-749.
    • (1995) Biochem Biophys Res Commun , vol.215 , pp. 744-749
    • Tanaka, T.1    Kato, N.2    Cho, M.J.3    Shimotohno, K.4
  • 15
    • 0029927642 scopus 로고    scopus 로고
    • Structure of the 3′ terminus of the hepatitis C virus genome
    • Tanaka T, Kato N, Cho MJ, Sugiyama K, Shimotohno K. Structure of the 3′ terminus of the hepatitis C virus genome. J Virol 1996; 70: 3307-3312.
    • (1996) J Virol , vol.70 , pp. 3307-3312
    • Tanaka, T.1    Kato, N.2    Cho, M.J.3    Sugiyama, K.4    Shimotohno, K.5
  • 16
    • 0029331431 scopus 로고
    • An RNA pseudoknot is an essential structural element of the internal ribosome entry site located within the hepatitis C virus 5′ noncoding region
    • Wang CY, Le SY, Ali N, Siddiqui A. An RNA pseudoknot is an essential structural element of the internal ribosome entry site located within the hepatitis C virus 5′ noncoding region. RNA 1995; 1: 526-537.
    • (1995) RNA , vol.1 , pp. 526-537
    • Wang, C.Y.1    Le, S.Y.2    Ali, N.3    Siddiqui, A.4
  • 17
    • 0026513651 scopus 로고
    • Internal ribosome entry site within hepatitis C virus RNA
    • Tsukiyama-Kohara K, Iizuka N, Kohara M, Nomoto A. Internal ribosome entry site within hepatitis C virus RNA. J Virol 1992; 66: 1476-1783.
    • (1992) J Virol , vol.66 , pp. 1476-1783
    • Tsukiyama-Kohara, K.1    Iizuka, N.2    Kohara, M.3    Nomoto, A.4
  • 18
    • 0027153210 scopus 로고
    • Translation of human hepatitis C virus RNA in cultured cells is mediated by an internal ribosome-binding mechanism
    • Wang C, Sarnow P, Siddiqui A. Translation of human hepatitis C virus RNA in cultured cells is mediated by an internal ribosome-binding mechanism. J Virol 1993; 67: 3338-3344.
    • (1993) J Virol , vol.67 , pp. 3338-3344
    • Wang, C.1    Sarnow, P.2    Siddiqui, A.3
  • 19
    • 0027176287 scopus 로고
    • NS3 is a serine protease required for processing of hepatitis C virus polyprotein
    • Tomei L, Failla C, De Francesco R, La Monica N, Santolini E. NS3 is a serine protease required for processing of hepatitis C virus polyprotein. J Virol 1993; 67: 4017-4026.
    • (1993) J Virol , vol.67 , pp. 4017-4026
    • Tomei, L.1    Failla, C.2    De Francesco, R.3    La Monica, N.4    Santolini, E.5
  • 20
    • 0027225699 scopus 로고
    • Expression, identification and subcellular localization of the proteins encoded by the hepatitis C viral genome
    • Selby MJ, Choo QL, Berger K et al. Expression, identification and subcellular localization of the proteins encoded by the hepatitis C viral genome. J Gen Virol 1993; 74: 1103-1113.
    • (1993) J Gen Virol , vol.74 , pp. 1103-1113
    • Selby, M.J.1    Choo, Q.L.2    Berger, K.3
  • 21
    • 0028265186 scopus 로고
    • Analysis of N-terminal processing of hepatitis C virus nonstructural protein 2
    • Mizushima H, Hijikata M, Tanji Y, Kimura K, Shimotohno K. Analysis of N-terminal processing of hepatitis C virus nonstructural protein 2. J Virol 1994; 68: 2731-2734.
    • (1994) J Virol , vol.68 , pp. 2731-2734
    • Mizushima, H.1    Hijikata, M.2    Tanji, Y.3    Kimura, K.4    Shimotohno, K.5
  • 23
    • 0028332810 scopus 로고
    • Production of non-structural proteins of hepatitis C virus requires a putative viral protease encoded by NS3
    • Manabe S, Fuke I, Tanishita O et al. Production of non-structural proteins of hepatitis C virus requires a putative viral protease encoded by NS3. Virology 1994; 198: 636-644.
    • (1994) Virology , vol.198 , pp. 636-644
    • Manabe, S.1    Fuke, I.2    Tanishita, O.3
  • 24
    • 0028290389 scopus 로고
    • Processing in the hepatitis C virus E2-NS2 region: Identification of p7 and two distinct E2-specific products with different C termini
    • Lin C, Lindenbach BD, Pragai BM, McCourt DW, Rice CM. Processing in the hepatitis C virus E2-NS2 region: identification of p7 and two distinct E2-specific products with different C termini. J Virol 1994; 68: 5063-5073.
    • (1994) J Virol , vol.68 , pp. 5063-5073
    • Lin, C.1    Lindenbach, B.D.2    Pragai, B.M.3    McCourt, D.W.4    Rice, C.M.5
  • 25
    • 0025991559 scopus 로고
    • Gene mapping of the putative structural region of the hepatitis C virus genome by in vitro processing analysis
    • Hijikata M, Kato N, Ootsuyama Y, Nakagawa M, Shimotohno K. Gene mapping of the putative structural region of the hepatitis C virus genome by in vitro processing analysis. Proc Natl Acad Sci USA 1991; 88: 5547-5551.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 5547-5551
    • Hijikata, M.1    Kato, N.2    Ootsuyama, Y.3    Nakagawa, M.4    Shimotohno, K.5
  • 26
    • 0027515735 scopus 로고
    • Proteolytic processing and membrane association of putative nonstructural proteins of hepatitis C virus
    • Hijikata M, Mizushima H, Tanji Y et al. Proteolytic processing and membrane association of putative nonstructural proteins of hepatitis C virus. Proc Natl Acad Sci USA 1993; 90: 10773-10777.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10773-10777
    • Hijikata, M.1    Mizushima, H.2    Tanji, Y.3
  • 27
    • 0027414062 scopus 로고
    • Characterization of the hepatitis C virus-encoded serine proteinase: Determination of proteinase-dependent polyprotein cleavage sites
    • Grakoui A, McCourt DW, Wychowski C, Feinstone SM, Rice CM. Characterization of the hepatitis C virus-encoded serine proteinase: determination of proteinase-dependent polyprotein cleavage sites. J Virol 1993; 67: 2832-2843.
    • (1993) J Virol , vol.67 , pp. 2832-2843
    • Grakoui, A.1    McCourt, D.W.2    Wychowski, C.3    Feinstone, S.M.4    Rice, C.M.5
  • 28
    • 0027476809 scopus 로고
    • Expression and identification of hepatitis C virus polyprotein cleavage products
    • Grakoui A, Wychowski C, Lin C, Feinstone SM, Rice CM. Expression and identification of hepatitis C virus polyprotein cleavage products. J Virol 1993; 67: 1385-1395.
    • (1993) J Virol , vol.67 , pp. 1385-1395
    • Grakoui, A.1    Wychowski, C.2    Lin, C.3    Feinstone, S.M.4    Rice, C.M.5
  • 29
    • 0027170423 scopus 로고
    • The hepatitis C virus encodes a serine protease involved in processing of the putative nonstructural proteins from the viral polyprotein precursor
    • Eckart MR, Selby M, Masiarz F et al. The hepatitis C virus encodes a serine protease involved in processing of the putative nonstructural proteins from the viral polyprotein precursor. Biochem Biophys Res Commun 1993; 192: 399-406.
    • (1993) Biochem Biophys Res Commun , vol.192 , pp. 399-406
    • Eckart, M.R.1    Selby, M.2    Masiarz, F.3
  • 30
    • 0027287798 scopus 로고
    • Nonstructural protein 3 of the hepatitis C virus encodes a serine-type proteinase required for cleavage at the NS3/4 and NS4/5 junctions
    • Bartenschlager R, Ahlborn LL, Mous J, Jacobsen H. Nonstructural protein 3 of the hepatitis C virus encodes a serine-type proteinase required for cleavage at the NS3/4 and NS4/5 junctions. J Virol 1993; 67: 3835-3844.
    • (1993) J Virol , vol.67 , pp. 3835-3844
    • Bartenschlager, R.1    Ahlborn, L.L.2    Mous, J.3    Jacobsen, H.4
  • 31
    • 0026014610 scopus 로고
    • Expression of processed core protein of hepatitis C virus in mammalian cells
    • Harada S, Watanabe Y, Takeuchi K et al. Expression of processed core protein of hepatitis C virus in mammalian cells. J Virol 1991; 65: 3015-3021.
    • (1991) J Virol , vol.65 , pp. 3015-3021
    • Harada, S.1    Watanabe, Y.2    Takeuchi, K.3
  • 32
    • 0027420380 scopus 로고
    • Analysis of hepatitis C virus capsid, E1, and E2/NS1 proteins expressed in insect cells
    • Lanford RE, Notvall L, Chavez D et al. Analysis of hepatitis C virus capsid, E1, and E2/NS1 proteins expressed in insect cells. Virology 1993; 197: 225-235.
    • (1993) Virology , vol.197 , pp. 225-235
    • Lanford, R.E.1    Notvall, L.2    Chavez, D.3
  • 33
    • 0029930196 scopus 로고    scopus 로고
    • Homotypic interaction and multimerization of hepatitis C virus core protein
    • Matsumoto M, Hwang SB, Jeng KS, Zhu N, Lai MM. Homotypic interaction and multimerization of hepatitis C virus core protein. Virology 1996; 218: 43-51.
    • (1996) Virology , vol.218 , pp. 43-51
    • Matsumoto, M.1    Hwang, S.B.2    Jeng, K.S.3    Zhu, N.4    Lai, M.M.5
  • 34
    • 0030950331 scopus 로고    scopus 로고
    • Analysis of hepatitis C virus core protein interaction domains
    • Nolandt O, Kern V, Müller H et al. Analysis of hepatitis C virus core protein interaction domains. J Gen Virol 1997; 78: 1331-1340.
    • (1997) J Gen Virol , vol.78 , pp. 1331-1340
    • Nolandt, O.1    Kern, V.2    Müller, H.3
  • 35
    • 0028233530 scopus 로고
    • Biosynthesis and biochemical properties of the hepatitis C virus core protein
    • Santolini E, Migliaccio G, La Monica N. Biosynthesis and biochemical properties of the hepatitis C virus core protein. J Virol 1994; 68: 3631-3641.
    • (1994) J Virol , vol.68 , pp. 3631-3641
    • Santolini, E.1    Migliaccio, G.2    La Monica, N.3
  • 36
    • 0031901556 scopus 로고    scopus 로고
    • Hepatitis C virus core from two different genotypes has an oncogenic potential but is not sufficient for transforming primary rat embryo fibroblasts in cooperation with the H-ras oncogene
    • Chang J, Yang SH, Cho YG, Hwang SB, Hahn YS, Sung YC. Hepatitis C virus core from two different genotypes has an oncogenic potential but is not sufficient for transforming primary rat embryo fibroblasts in cooperation with the H-ras oncogene. J Virol 1998; 72: 3060-3065.
    • (1998) J Virol , vol.72 , pp. 3060-3065
    • Chang, J.1    Yang, S.H.2    Cho, Y.G.3    Hwang, S.B.4    Hahn, Y.S.5    Sung, Y.C.6
  • 37
    • 0030729202 scopus 로고    scopus 로고
    • Direct interaction of hepatitis C virus core protein with the cellular lymphotoxin-beta receptor modulates the signal pathway of the lymphotoxin-beta receptor
    • Chen CM, You LR, Hwang LH, Lee YW. Direct interaction of hepatitis C virus core protein with the cellular lymphotoxin-beta receptor modulates the signal pathway of the lymphotoxin-beta receptor. J Virol 1997; 71: 9417-9426.
    • (1997) J Virol , vol.71 , pp. 9417-9426
    • Chen, C.M.1    You, L.R.2    Hwang, L.H.3    Lee, Y.W.4
  • 38
    • 18844480671 scopus 로고    scopus 로고
    • Hepatitis C virus core protein interacts with the cytoplasmic tail of lymphotoxin-beta receptor
    • Matsumoto M, Hsieh TY, Zhu NL et al. Hepatitis C virus core protein interacts with the cytoplasmic tail of lymphotoxin-beta receptor. J Virol 1997; 71: 1301-1309.
    • (1997) J Virol , vol.71 , pp. 1301-1309
    • Matsumoto, M.1    Hsieh, T.Y.2    Zhu, N.L.3
  • 39
    • 0029114785 scopus 로고
    • Transcriptional regulation of cellular and viral promoters by the hepatitis C virus core protein
    • Ray RB, Lagging LM, Meyer K, Steele R, Ray R. Transcriptional regulation of cellular and viral promoters by the hepatitis C virus core protein. Virus Res 1995; 37: 209-220.
    • (1995) Virus Res , vol.37 , pp. 209-220
    • Ray, R.B.1    Lagging, L.M.2    Meyer, K.3    Steele, R.4    Ray, R.5
  • 40
    • 0030589563 scopus 로고    scopus 로고
    • Suppression of apoptotic cell death by hepatitis C virus core protein
    • Ray RB, Meyer K, Ray R. Suppression of apoptotic cell death by hepatitis C virus core protein. Virology 1996; 226: 176-182.
    • (1996) Virology , vol.226 , pp. 176-182
    • Ray, R.B.1    Meyer, K.2    Ray, R.3
  • 41
    • 8944262349 scopus 로고    scopus 로고
    • Hepatitis C virus core protein cooperates with ras and transforms primary rat embryo fibroblasts to tumorigenic phenotype
    • Ray RB, Lagging LM, Meyer K, Ray R. Hepatitis C virus core protein cooperates with ras and transforms primary rat embryo fibroblasts to tumorigenic phenotype. J Virol 1996; 70: 4438-4443.
    • (1996) J Virol , vol.70 , pp. 4438-4443
    • Ray, R.B.1    Lagging, L.M.2    Meyer, K.3    Ray, R.4
  • 42
    • 0030891710 scopus 로고    scopus 로고
    • Transcriptional repression of p53 promoter by hepatitis C virus core protein
    • Ray RB, Steele R, Meyer K, Ray R. Transcriptional repression of p53 promoter by hepatitis C virus core protein. J Biol Chem 1997; 272: 10983-10986.
    • (1997) J Biol Chem , vol.272 , pp. 10983-10986
    • Ray, R.B.1    Steele, R.2    Meyer, K.3    Ray, R.4
  • 43
    • 0031892177 scopus 로고    scopus 로고
    • Inhibition of tumor necrosis factor (TNF-alpha)-mediated apoptosis by hepatitis C virus core protein
    • Ray RB, Meyer K, Steele R, Shrivastava A, Aggarwal BB, Ray R. Inhibition of tumor necrosis factor (TNF-alpha)-mediated apoptosis by hepatitis C virus core protein. J Biol Chem 1998; 273: 2256-2259.
    • (1998) J Biol Chem , vol.273 , pp. 2256-2259
    • Ray, R.B.1    Meyer, K.2    Steele, R.3    Shrivastava, A.4    Aggarwal, B.B.5    Ray, R.6
  • 44
    • 0032570876 scopus 로고    scopus 로고
    • Hepatitis C virus core protein represses p21WAF1/Cip1/Sid1 promoter activity
    • Ray RB, Steele R, Meyer K, Ray R. Hepatitis C virus core protein represses p21WAF1/Cip1/Sid1 promoter activity. Gene 1998; 208: 331-336.
    • (1998) Gene , vol.208 , pp. 331-336
    • Ray, R.B.1    Steele, R.2    Meyer, K.3    Ray, R.4
  • 45
    • 0028021952 scopus 로고
    • Formation and intracellular localization of hepatitis C virus envelope glycoprotein complexes expressed by recombinant vaccinia and Sindbis viruses
    • Dubuisson J, Hsu HH, Cheung RC, Greenberg HB, Russell DG, Rice CM. Formation and intracellular localization of hepatitis C virus envelope glycoprotein complexes expressed by recombinant vaccinia and Sindbis viruses. J Virol 1994; 68: 6147-6160.
    • (1994) J Virol , vol.68 , pp. 6147-6160
    • Dubuisson, J.1    Hsu, H.H.2    Cheung, R.C.3    Greenberg, H.B.4    Russell, D.G.5    Rice, C.M.6
  • 46
    • 0027215726 scopus 로고
    • Characterization of hepatitis C virus structural proteins with a recombinant baculovirus expression system
    • Hsu HH, Donets M, Greenberg HB, Feinstone SM. Characterization of hepatitis C virus structural proteins with a recombinant baculovirus expression system. Hepatology 1993; 17: 763-771.
    • (1993) Hepatology , vol.17 , pp. 763-771
    • Hsu, H.H.1    Donets, M.2    Greenberg, H.B.3    Feinstone, S.M.4
  • 47
    • 0026722262 scopus 로고
    • Expression and characterization of glycoprotein gp35 of hepatitis C virus using recombinant vaccinia virus
    • Kohara M, Tsukiyama KK, Maki N et al. Expression and characterization of glycoprotein gp35 of hepatitis C virus using recombinant vaccinia virus. J Gen Virol 1992; 73: 2313-2318.
    • (1992) J Gen Virol , vol.73 , pp. 2313-2318
    • Kohara, M.1    Tsukiyama, K.K.2    Maki, N.3
  • 48
    • 0026590695 scopus 로고
    • Expression of processed envelope protein of hepatitis C virus in mammalian and insect cells
    • Matsuura Y, Harada S, Suzuki R et al. Expression of processed envelope protein of hepatitis C virus in mammalian and insect cells. J Virol 1992; 66: 1425-1431.
    • (1992) J Virol , vol.66 , pp. 1425-1431
    • Matsuura, Y.1    Harada, S.2    Suzuki, R.3
  • 49
    • 0027442136 scopus 로고
    • Characterization of hepatitis C virus envelope glycoprotein complexes expressed by recombinant vaccinia viruses
    • Ralston R, Thudium K, Berger K et al. Characterization of hepatitis C virus envelope glycoprotein complexes expressed by recombinant vaccinia viruses. J Virol 1993; 67: 6753-6761.
    • (1993) J Virol , vol.67 , pp. 6753-6761
    • Ralston, R.1    Thudium, K.2    Berger, K.3
  • 50
    • 0028040540 scopus 로고
    • Complex processing and protein:protein interactions in the E2:NS2 region of HCV
    • Selby MJ, Glazer E, Masiarz F, Houghton M. Complex processing and protein:protein interactions in the E2:NS2 region of HCV. Virology 1994; 204: 114-122.
    • (1994) Virology , vol.204 , pp. 114-122
    • Selby, M.J.1    Glazer, E.2    Masiarz, F.3    Houghton, M.4
  • 51
    • 0026724046 scopus 로고
    • Characterization of the hepatitis C virus E2/NS1 gene product expressed in mammalian cells
    • Spaete RR, Alexander D, Rugroden ME et al. Characterization of the hepatitis C virus E2/NS1 gene product expressed in mammalian cells. Virology 1992; 188: 819-830.
    • (1992) Virology , vol.188 , pp. 819-830
    • Spaete, R.R.1    Alexander, D.2    Rugroden, M.E.3
  • 53
    • 0027163740 scopus 로고
    • Two distinct proteinase activities required for the processing of a putative nonstructural precursor protein of hepatitis C virus
    • Hijikata M, Mizushima H, Akagi T et al. Two distinct proteinase activities required for the processing of a putative nonstructural precursor protein of hepatitis C virus. J Virol 1993; 67: 4665-4675.
    • (1993) J Virol , vol.67 , pp. 4665-4675
    • Hijikata, M.1    Mizushima, H.2    Akagi, T.3
  • 54
    • 0027139660 scopus 로고
    • Two proteinase activities in HCV polypeptide expressed in insect cells using baculovirus vector
    • Hirowatari Y, Hijikata M, Tanji Y et al. Two proteinase activities in HCV polypeptide expressed in insect cells using baculovirus vector. Arch Virol 1993; 133: 349-356.
    • (1993) Arch Virol , vol.133 , pp. 349-356
    • Hirowatari, Y.1    Hijikata, M.2    Tanji, Y.3
  • 55
    • 0029042438 scopus 로고
    • In vitro cleavage of hepatitis C virus polyprotein substrates by purified recombinant NS3 protease
    • D'Souza ED, Grace K, Sangar DV, Rowlands DJ, Clarke BE. In vitro cleavage of hepatitis C virus polyprotein substrates by purified recombinant NS3 protease. J Gen Virol 1995; 76: 1729-1736.
    • (1995) J Gen Virol , vol.76 , pp. 1729-1736
    • D'Souza, E.D.1    Grace, K.2    Sangar, D.V.3    Rowlands, D.J.4    Clarke, B.E.5
  • 56
    • 0028817781 scopus 로고
    • C-terminal domain of the hepatitis C virus NS3 protein contains an RNA helicase activity
    • Kim DW, Gwack Y, Han JH, Choe J. C-terminal domain of the hepatitis C virus NS3 protein contains an RNA helicase activity. Biochem Biophys Res Commun 1995; 215: 160-166.
    • (1995) Biochem Biophys Res Commun , vol.215 , pp. 160-166
    • Kim, D.W.1    Gwack, Y.2    Han, J.H.3    Choe, J.4
  • 57
    • 0029950090 scopus 로고    scopus 로고
    • Enzymatic characterization of hepatitis C virus NS3/4A complexes expressed in mammalian cells by using the herpes simplex virus amplicon system
    • Hong Z, Ferrari E, Wright MJ et al. Enzymatic characterization of hepatitis C virus NS3/4A complexes expressed in mammalian cells by using the herpes simplex virus amplicon system. J Virol 1996; 70: 4261-4268.
    • (1996) J Virol , vol.70 , pp. 4261-4268
    • Hong, Z.1    Ferrari, E.2    Wright, M.J.3
  • 58
    • 0029784485 scopus 로고    scopus 로고
    • A steady-state and pre-steady-state kinetic analysis of the NTPase activity associated with the hepatitis C virus NS3 helicase domain
    • Preugschat F, Averett DR, Clarke BE, Porter DT. A steady-state and pre-steady-state kinetic analysis of the NTPase activity associated with the hepatitis C virus NS3 helicase domain. J Biol Chem 1996; 271: 24449-24457.
    • (1996) J Biol Chem , vol.271 , pp. 24449-24457
    • Preugschat, F.1    Averett, D.R.2    Clarke, B.E.3    Porter, D.T.4
  • 59
    • 0027199917 scopus 로고
    • Hepatitis C virus NS3 protein polynucleotide-stimulated nucleoside triphosphatase and comparison with the related pestivirus and flavivirus enzymes
    • Suzich JA, Tamura JK, Palmer HF et al. Hepatitis C virus NS3 protein polynucleotide-stimulated nucleoside triphosphatase and comparison with the related pestivirus and flavivirus enzymes. J Virol 1993; 67: 6152-6158.
    • (1993) J Virol , vol.67 , pp. 6152-6158
    • Suzich, J.A.1    Tamura, J.K.2    Palmer, H.F.3
  • 60
    • 0029970903 scopus 로고    scopus 로고
    • The helicase activity associated with hepatitis C virus nonstructural protein 3 (Ns3)
    • Tai CL, Chi WK, Chen DS, Hwang LH. The helicase activity associated with hepatitis C virus nonstructural protein 3 (Ns3). J Virol 1996; 70: 8477-8484.
    • (1996) J Virol , vol.70 , pp. 8477-8484
    • Tai, C.L.1    Chi, W.K.2    Chen, D.S.3    Hwang, L.H.4
  • 61
    • 0029992405 scopus 로고    scopus 로고
    • Non-structural protein 3 of hepatitis C virus inhibits phosphorylation mediated by cAMP-dependent protein kinase
    • Borowski P, Heiland M, Oehlmann K et al. Non-structural protein 3 of hepatitis C virus inhibits phosphorylation mediated by cAMP-dependent protein kinase. Eur J Biochem 1996; 237: 611-618.
    • (1996) Eur J Biochem , vol.237 , pp. 611-618
    • Borowski, P.1    Heiland, M.2    Oehlmann, K.3
  • 62
    • 0029063640 scopus 로고
    • Hepatitis C virus nonstructural protein NS3 transforms NIH 3T3 cells
    • Sakamuro D, Furukawa T, Takegami T. Hepatitis C virus nonstructural protein NS3 transforms NIH 3T3 cells. J Virol 1995; 69: 3893-3896.
    • (1995) J Virol , vol.69 , pp. 3893-3896
    • Sakamuro, D.1    Furukawa, T.2    Takegami, T.3
  • 63
    • 0028241489 scopus 로고
    • Kinetic and structural analyses of hepatitis C virus polyprotein processing
    • Bartenschlager R, Ahlborn LL, Mous J, Jacobsen H. Kinetic and structural analyses of hepatitis C virus polyprotein processing. J Virol 1994; 68: 5045-5055.
    • (1994) J Virol , vol.68 , pp. 5045-5055
    • Bartenschlager, R.1    Ahlborn, L.L.2    Mous, J.3    Jacobsen, H.4
  • 64
    • 0028290579 scopus 로고
    • Both NS3 and NS4A are required for proteolytic processing of hepatitis c virus nonstructural proteins
    • Failla C, Tomei L, De Francesco R. Both NS3 and NS4A are required for proteolytic processing of hepatitis c virus nonstructural proteins. J Virol 1994; 68: 3753-3760.
    • (1994) J Virol , vol.68 , pp. 3753-3760
    • Failla, C.1    Tomei, L.2    De Francesco, R.3
  • 65
    • 0028089739 scopus 로고
    • Hepatitis C virus NS3 serine proteinase: Trans-cleavage requirements and processing kinetics
    • Lin C, Pragai BM, Grakoui A, Xu J, Rice CM. Hepatitis C virus NS3 serine proteinase: trans-cleavage requirements and processing kinetics. J Virol 1994; 68: 8147-8157.
    • (1994) J Virol , vol.68 , pp. 8147-8157
    • Lin, C.1    Pragai, B.M.2    Grakoui, A.3    Xu, J.4    Rice, C.M.5
  • 66
    • 0028831056 scopus 로고
    • Hepatitis C virus-encoded nonstructural protein NS4A has versatile functions in viral protein processing
    • Tanji Y, Hijikata M, Satoh S, Kaneko T, Shimotohno K. Hepatitis C virus-encoded nonstructural protein NS4A has versatile functions in viral protein processing. J Virol 1995; 69: 1575-1581.
    • (1995) J Virol , vol.69 , pp. 1575-1581
    • Tanji, Y.1    Hijikata, M.2    Satoh, S.3    Kaneko, T.4    Shimotohno, K.5
  • 67
    • 0031060172 scopus 로고    scopus 로고
    • The N-terminal region of hepatitis C virus-encoded NS5A is important for NS4A-dependent phosphorylation
    • Asabe SI, Tanji Y, Satoh S, Kaneko T, Kimura K, Shimotohno K. The N-terminal region of hepatitis C virus-encoded NS5A is important for NS4A-dependent phosphorylation. J Virol 1997; 71: 790-796.
    • (1997) J Virol , vol.71 , pp. 790-796
    • Asabe, S.I.1    Tanji, Y.2    Satoh, S.3    Kaneko, T.4    Kimura, K.5    Shimotohno, K.6
  • 68
    • 0028096675 scopus 로고
    • Production of two phosphoproteins from the NS5A region of the hepatitis C viral genome
    • Kaneko T, Tanji Y, Satoh S et al. Production of two phosphoproteins from the NS5A region of the hepatitis C viral genome. Biochem Biophys Res Commun 1994; 205: 320-326.
    • (1994) Biochem Biophys Res Commun , vol.205 , pp. 320-326
    • Kaneko, T.1    Tanji, Y.2    Satoh, S.3
  • 69
    • 0028978937 scopus 로고
    • Phosphorylation of hepatitis C virus-encoded nonstructural protein NS5A
    • Tanji Y, Kaneko T, Satoh S, Shimotohno K. Phosphorylation of hepatitis C virus-encoded nonstructural protein NS5A. J Virol 1995; 69: 3980-3986.
    • (1995) J Virol , vol.69 , pp. 3980-3986
    • Tanji, Y.1    Kaneko, T.2    Satoh, S.3    Shimotohno, K.4
  • 70
    • 0343924357 scopus 로고    scopus 로고
    • Evidence that hepatitis C virus resistance to interferon is mediated through repression of the PKR protein kinase by the nonstructural 5A protein
    • Gale MJ, Korth MJ, Tang NM et al. Evidence that hepatitis C virus resistance to interferon is mediated through repression of the PKR protein kinase by the nonstructural 5A protein. Virology 1997; 230: 217-227.
    • (1997) Virology , vol.230 , pp. 217-227
    • Gale, M.J.1    Korth, M.J.2    Tang, N.M.3
  • 71
    • 17144463221 scopus 로고    scopus 로고
    • Control of PKR protein kinase by hepatitis C virus nonstructural 5A protein: Molecular mechanism of kinase regulation
    • Gale MJ Jr, Blakely SM, Kwieciszewski B et al. Control of PKR protein kinase by hepatitis C virus nonstructural 5A protein: molecular mechanism of kinase regulation. Mol Cell Biol 1998; 18: 5208-5218.
    • (1998) Mol Cell Biol , vol.18 , pp. 5208-5218
    • Gale Jr., M.J.1    Blakely, S.M.2    Kwieciszewski, B.3
  • 72
    • 0029161576 scopus 로고
    • Comparison of full-length sequences of interferon-sensitive and resistant hepatitis C virus 1b sensitivity to interferon is conferred by amino acid substitutions in the NS5A region
    • Enomoto N, Sakuma I, Asahina Y et al. Comparison of full-length sequences of interferon-sensitive and resistant hepatitis C virus 1b sensitivity to interferon is conferred by amino acid substitutions in the NS5A region. J Clin Invest 1995; 96: 224-230.
    • (1995) J Clin Invest , vol.96 , pp. 224-230
    • Enomoto, N.1    Sakuma, I.2    Asahina, Y.3
  • 73
    • 9144257569 scopus 로고    scopus 로고
    • Mutations in the nonstructural protein 5A gene and response to interferon in patients with chronic hepatitis C virus 1b infection
    • Enomoto N, Sakuma I, Asahina Y et al. Mutations in the nonstructural protein 5A gene and response to interferon in patients with chronic hepatitis C virus 1b infection. N Engl J Med 1996; 334: 77-81.
    • (1996) N Engl J Med , vol.334 , pp. 77-81
    • Enomoto, N.1    Sakuma, I.2    Asahina, Y.3
  • 74
    • 0031836249 scopus 로고    scopus 로고
    • Sequence analysis of the NS5A protein of European hepatitis C virus 1b isolates and relation to interferon sensitivity
    • Duverlie G, Khorsi H, Castelain S et al. Sequence analysis of the NS5A protein of European hepatitis C virus 1b isolates and relation to interferon sensitivity. J Gen Virol 1998; 79: 1373-1381.
    • (1998) J Gen Virol , vol.79 , pp. 1373-1381
    • Duverlie, G.1    Khorsi, H.2    Castelain, S.3
  • 75
    • 0030051777 scopus 로고    scopus 로고
    • Identification and properties of the RNA-dependent RNA polymerase of hepatitis C virus
    • Behrens SE, Tomei L, De Francesco R. Identification and properties of the RNA-dependent RNA polymerase of hepatitis C virus. EMBO J 1996; 15: 12-22.
    • (1996) EMBO J , vol.15 , pp. 12-22
    • Behrens, S.E.1    Tomei, L.2    De Francesco, R.3
  • 76
    • 1842289764 scopus 로고    scopus 로고
    • Biochemical properties of hepatitis C virus NS5B RNA-dependent RNA polymerase and identification of amino acid sequence motifs essential for enzymatic activity
    • Lohmann V, Körner F, Herian U, Bartenschlager R. Biochemical properties of hepatitis C virus NS5B RNA-dependent RNA polymerase and identification of amino acid sequence motifs essential for enzymatic activity. J Virol 1997; 71: 8416-8428.
    • (1997) J Virol , vol.71 , pp. 8416-8428
    • Lohmann, V.1    Körner, F.2    Herian, U.3    Bartenschlager, R.4
  • 77
    • 0032546963 scopus 로고    scopus 로고
    • RNA-dependent RNA polymerase activity of the soluble recombinant hepatitis C virus NS5B protein truncated at the C-terminal region
    • Yamashita T, Kaneko S, Shirota Y et al. RNA-dependent RNA polymerase activity of the soluble recombinant hepatitis C virus NS5B protein truncated at the C-terminal region. J Biol Chem 1998; 273: 15479-15486.
    • (1998) J Biol Chem , vol.273 , pp. 15479-15486
    • Yamashita, T.1    Kaneko, S.2    Shirota, Y.3
  • 79
    • 0031951177 scopus 로고    scopus 로고
    • Expression of recombinant hepatitis C virus non-structural protein 5B in Escherichia coli
    • Al RH, Xie YP, Wang YH, Hagedorn CH. Expression of recombinant hepatitis C virus non-structural protein 5B in Escherichia coli. Virus Res 1998; 53: 141-149.
    • (1998) Virus Res , vol.53 , pp. 141-149
    • Al, R.H.1    Xie, Y.P.2    Wang, Y.H.3    Hagedorn, C.H.4
  • 80
    • 0030273064 scopus 로고    scopus 로고
    • Hepatitis C virus core protein: Carboxy-terminal boundaries of two processed species suggest cleavage by a signal peptide peptidase
    • Hüssy P, Langen H, Mous J, Jacobsen H. Hepatitis C virus core protein: carboxy-terminal boundaries of two processed species suggest cleavage by a signal peptide peptidase. Virology 1996; 224: 93-104.
    • (1996) Virology , vol.224 , pp. 93-104
    • Hüssy, P.1    Langen, H.2    Mous, J.3    Jacobsen, H.4
  • 82
    • 0030700403 scopus 로고    scopus 로고
    • Hepatitis C virus NS2-3 proteinase
    • Wilkinson CS. Hepatitis C virus NS2-3 proteinase. Biochem Soc Trans 1997; 25: S611-S611.
    • (1997) Biochem Soc Trans , vol.25
    • Wilkinson, C.S.1
  • 83
    • 0029059334 scopus 로고
    • Hepatitis C virus-encoded NS2-3 protease: Cleavage-site mutagenesis and requirements for bimolecular cleavage
    • Reed KE, Grakoui A, Rice CM. Hepatitis C virus-encoded NS2-3 protease: cleavage-site mutagenesis and requirements for bimolecular cleavage. J Virol 1995; 69: 4127-4136.
    • (1995) J Virol , vol.69 , pp. 4127-4136
    • Reed, K.E.1    Grakoui, A.2    Rice, C.M.3
  • 84
    • 0028089750 scopus 로고
    • Hepatitis C virus polyprotein processing: Kinetics and mutagenic analysis of serine proteinase-dependent cleavage
    • Tanji Y, Hijikata M, Hirowatari Y, Shimotohno K. Hepatitis C virus polyprotein processing: kinetics and mutagenic analysis of serine proteinase-dependent cleavage. J Virol 1994; 68: 8418-8422.
    • (1994) J Virol , vol.68 , pp. 8418-8422
    • Tanji, Y.1    Hijikata, M.2    Hirowatari, Y.3    Shimotohno, K.4
  • 85
    • 0026451216 scopus 로고
    • Families of metalloendopeptidases and their relationships
    • Jiang W, Bond JS. Families of metalloendopeptidases and their relationships. FEBS Lett 1992; 312: 110-114.
    • (1992) FEBS Lett , vol.312 , pp. 110-114
    • Jiang, W.1    Bond, J.S.2
  • 87
    • 0032031975 scopus 로고    scopus 로고
    • Mechanism of autoproteolysis at the NS2-NS3 junction of the hepatitis C virus polyprotein
    • Wu Z, Yao NH, Le HV, Weber PC. Mechanism of autoproteolysis at the NS2-NS3 junction of the hepatitis C virus polyprotein. Trends Biochem Sci 1998; 23: 92-94.
    • (1998) Trends Biochem Sci , vol.23 , pp. 92-94
    • Wu, Z.1    Yao, N.H.2    Le, H.V.3    Weber, P.C.4
  • 88
    • 0025249362 scopus 로고
    • Hepatitis C virus shares amino acid sequence similarity with pestiviruses and flaviviruses as well as members of two plant virus super-groups
    • Miller RH, Purcell RH. Hepatitis C virus shares amino acid sequence similarity with pestiviruses and flaviviruses as well as members of two plant virus super-groups. Proc Natl Acad Sci USA 1990; 87: 2057-2061.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 2057-2061
    • Miller, R.H.1    Purcell, R.H.2
  • 89
    • 0024372153 scopus 로고
    • Detection of a trypsin-like serine protease domain in flaviviruses and pestiviruses
    • Bazan JF, Fletterick RJ. Detection of a trypsin-like serine protease domain in flaviviruses and pestiviruses. Virology 1989; 171: 637-639.
    • (1989) Virology , vol.171 , pp. 637-639
    • Bazan, J.F.1    Fletterick, R.J.2
  • 90
    • 0000651334 scopus 로고
    • Structural and catalytic models of trypsin-like viral proteases
    • Bazan JF, Fletterick RJ. Structural and catalytic models of trypsin-like viral proteases. Semin Virol 1990; 1: 311-322.
    • (1990) Semin Virol , vol.1 , pp. 311-322
    • Bazan, J.F.1    Fletterick, R.J.2
  • 91
    • 0024341494 scopus 로고
    • N-terminal domains of putative helicases of flavi- and pestiviruses may be serine proteases
    • Gorbalenya AE, Donchenko AP, Koonin EV, Blinov VM. N-terminal domains of putative helicases of flavi- and pestiviruses may be serine proteases. Nucl Acids Res 1989; 17: 3889-3897.
    • (1989) Nucl Acids Res , vol.17 , pp. 3889-3897
    • Gorbalenya, A.E.1    Donchenko, A.P.2    Koonin, E.V.3    Blinov, V.M.4
  • 92
    • 0027999994 scopus 로고
    • 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
    • Kolykhalov AA, Agapov EV, Rice CM. 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. J Virol 1994; 68: 7525-7533.
    • (1994) J Virol , vol.68 , pp. 7525-7533
    • Kolykhalov, A.A.1    Agapov, E.V.2    Rice, C.M.3
  • 93
    • 14444272750 scopus 로고    scopus 로고
    • Purification and characterization of the NS3 serine protease domain of hepatitis C virus expressed in Saccharomyces cerevisiae
    • Markland W, Petrillo RA, Fitzgibbon M et al. Purification and characterization of the NS3 serine protease domain of hepatitis C virus expressed in Saccharomyces cerevisiae. J Gen Virol 1997; 78: 39-43.
    • (1997) J Gen Virol , vol.78 , pp. 39-43
    • Markland, W.1    Petrillo, R.A.2    Fitzgibbon, M.3
  • 94
    • 0027991586 scopus 로고
    • Identification of the domain required for trans-cleavage activity of hepatitis C viral serine proteinase
    • Tanji Y, Hijikata M, Hirowatari Y, Shimotohno K. Identification of the domain required for trans-cleavage activity of hepatitis C viral serine proteinase. Gene 1994; 145: 215-219.
    • (1994) Gene , vol.145 , pp. 215-219
    • Tanji, Y.1    Hijikata, M.2    Hirowatari, Y.3    Shimotohno, K.4
  • 95
    • 0028851296 scopus 로고
    • An amino-terminal domain of the hepatitis C virus NS3 protease is essential for interaction with NS4A
    • Failla C, Tomei L, De Francesco R. An amino-terminal domain of the hepatitis C virus NS3 protease is essential for interaction with NS4A. J Virol 1995; 69: 1769-1777.
    • (1995) J Virol , vol.69 , pp. 1769-1777
    • Failla, C.1    Tomei, L.2    De Francesco, R.3
  • 96
    • 0028820118 scopus 로고
    • Complex formation between the NS3 serine-type proteinase of the hepatitis C virus and NS4A and its importance for polyprotein maturation
    • Bartenschlager R, Lohmann V, Wilkinson T, Koch JO. Complex formation between the NS3 serine-type proteinase of the hepatitis C virus and NS4A and its importance for polyprotein maturation. J Virol 1995; 69: 7519-7528.
    • (1995) J Virol , vol.69 , pp. 7519-7528
    • Bartenschlager, R.1    Lohmann, V.2    Wilkinson, T.3    Koch, J.O.4
  • 97
    • 0029814495 scopus 로고    scopus 로고
    • Activity of purified hepatitis C virus protease NS3 on peptide substrates
    • Steinkühler C, Urbani A, Tomei L et al. Activity of purified hepatitis C virus protease NS3 on peptide substrates. J Virol 1996; 70: 6694-6700.
    • (1996) J Virol , vol.70 , pp. 6694-6700
    • Steinkühler, C.1    Urbani, A.2    Tomei, L.3
  • 98
    • 0029981534 scopus 로고    scopus 로고
    • In vitro activity of hepatitis C virus protease NS3 purified from recombinant Baculovirus-infected Sf9 cells
    • Steinkühlcr C, Tomei L, DeFrancesco R. In vitro activity of hepatitis C virus protease NS3 purified from recombinant Baculovirus-infected Sf9 cells. J Biol Chem 1996; 271: 6367-6373.
    • (1996) J Biol Chem , vol.271 , pp. 6367-6373
    • Steinkühlcr, C.1    Tomei, L.2    DeFrancesco, R.3
  • 99
    • 0029074519 scopus 로고
    • A central region in the hepatitis C virus NS4A protein allows formation of an active NS3-NS4A serine proteinase complex in vivo and in vitro
    • Lin C, Thomson JA, Rice CM. A central region in the hepatitis C virus NS4A protein allows formation of an active NS3-NS4A serine proteinase complex in vivo and in vitro. J Virol 1995; 69: 4373-4780.
    • (1995) J Virol , vol.69 , pp. 4373-4780
    • Lin, C.1    Thomson, J.A.2    Rice, C.M.3
  • 100
    • 0029076837 scopus 로고
    • The N-terminal region of hepatitis C virus nonstructural protein 3 (NS3) is essential for stable complex formation with NS4A
    • Satoh S, Tanji Y, Hijikata M, Kimura K, Shimotohno K. The N-terminal region of hepatitis C virus nonstructural protein 3 (NS3) is essential for stable complex formation with NS4A. J Virol 1995; 69: 4255-4260.
    • (1995) J Virol , vol.69 , pp. 4255-4260
    • Satoh, S.1    Tanji, Y.2    Hijikata, M.3    Kimura, K.4    Shimotohno, K.5
  • 101
    • 0030589011 scopus 로고    scopus 로고
    • Enhancement of hepatitis C virus NS3 proteinase activity by association with NS4A-specific synthetic peptides: Identification of sequence and critical residues of NS4A for the cofactor activity
    • Butkiewicz NJ, Wendel M, Zhang R et al. Enhancement of hepatitis C virus NS3 proteinase activity by association with NS4A-specific synthetic peptides: identification of sequence and critical residues of NS4A for the cofactor activity. Virology 1996; 225: 328-338.
    • (1996) Virology , vol.225 , pp. 328-338
    • Butkiewicz, N.J.1    Wendel, M.2    Zhang, R.3
  • 102
    • 0029655995 scopus 로고    scopus 로고
    • Identification of the sequence on NS4A required for enhanced cleavage of the NS5A/5B site by hepatitis C virus NS3 protease
    • Shimizu Y, Yamaji K, Masuho Y et al. Identification of the sequence on NS4A required for enhanced cleavage of the NS5A/5B site by hepatitis C virus NS3 protease. J Virol 1996; 70: 127-132.
    • (1996) J Virol , vol.70 , pp. 127-132
    • Shimizu, Y.1    Yamaji, K.2    Masuho, Y.3
  • 103
    • 0029940111 scopus 로고    scopus 로고
    • A central hydrophobic domain of the hepatitis C virus NS4A protein is necessary and sufficient for the activation of the NS3 protease
    • Tomei L, Failla C, Vitale RL, Bianchi E, DeFrancesco R. A central hydrophobic domain of the hepatitis C virus NS4A protein is necessary and sufficient for the activation of the NS3 protease. J Gen Virol 1996; 77: 1065-1070.
    • (1996) J Gen Virol , vol.77 , pp. 1065-1070
    • Tomei, L.1    Failla, C.2    Vitale, R.L.3    Bianchi, E.4    DeFrancesco, R.5
  • 104
    • 0030198933 scopus 로고    scopus 로고
    • In vitro studies on the activation of the hepatitis C virus NS3 proteinase by the NS4A cofactor
    • Koch JO, Lohmann V, Herian U, Bartenschlager R. In vitro studies on the activation of the hepatitis C virus NS3 proteinase by the NS4A cofactor. Virology 1996; 221: 54-66.
    • (1996) Virology , vol.221 , pp. 54-66
    • Koch, J.O.1    Lohmann, V.2    Herian, U.3    Bartenschlager, R.4
  • 105
    • 0030871616 scopus 로고    scopus 로고
    • Mechanistic role of an NS4A peptide cofactor with the truncated NS3 protease of hepatitis C virus: Elucidation of the NS4A stimulatory effect via kinetic analysis and inhibitor mapping
    • Landro JA, Raybuck SA, Luong YC et al. Mechanistic role of an NS4A peptide cofactor with the truncated NS3 protease of hepatitis C virus: elucidation of the NS4A stimulatory effect via kinetic analysis and inhibitor mapping. Biochemistry 1997; 36: 9340-9348.
    • (1997) Biochemistry , vol.36 , pp. 9340-9348
    • Landro, J.A.1    Raybuck, S.A.2    Luong, Y.C.3
  • 106
    • 0030592514 scopus 로고    scopus 로고
    • The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site
    • Love RA, Parge HE, Wickersham JA et al. The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site. Cell 1996; 87: 331-342.
    • (1996) Cell , vol.87 , pp. 331-342
    • Love, R.A.1    Parge, H.E.2    Wickersham, J.A.3
  • 107
    • 16044364658 scopus 로고    scopus 로고
    • Crystal structure of the hepatitis C virus NS3 protease domain complexed with a synthetic NS4A cofactor peptide
    • Kim JL, Morgenstern KA, Lin C et al. Crystal structure of the hepatitis C virus NS3 protease domain complexed with a synthetic NS4A cofactor peptide. Cell 1996; 87: 343-355.
    • (1996) Cell , vol.87 , pp. 343-355
    • Kim, J.L.1    Morgenstern, K.A.2    Lin, C.3
  • 108
    • 2642590958 scopus 로고    scopus 로고
    • Complex of NS3 protease and NS4A peptide of BK strain hepatitis C virus: A 2.2 angstrom resolution structure in a hexagonal crystal form
    • Yan YW, Li Y, Munshi S, Sardana V et al. Complex of NS3 protease and NS4A peptide of BK strain hepatitis C virus: a 2.2 angstrom resolution structure in a hexagonal crystal form. Protein Sci 1998; 7: 837-847.
    • (1998) Protein Sci , vol.7 , pp. 837-847
    • Yan, Y.W.1    Li, Y.2    Munshi, S.3    Sardana, V.4
  • 110
    • 0029866646 scopus 로고    scopus 로고
    • The galvanization of biology: A growing appreciation for the roles of zinc
    • Berg JM, Shi Y. The galvanization of biology: a growing appreciation for the roles of zinc. Science 1996; 271: 1081-1085.
    • (1996) Science , vol.271 , pp. 1081-1085
    • Berg, J.M.1    Shi, Y.2
  • 111
    • 0030933215 scopus 로고    scopus 로고
    • The NS3 proteinase domain of hepatitis C virus is a zinc-containing enzyme
    • Stempniak M, Hostomska Z, Nodes BR, Hostomsky Z. The NS3 proteinase domain of hepatitis C virus is a zinc-containing enzyme. J Virol 1997; 71: 2881-2886.
    • (1997) J Virol , vol.71 , pp. 2881-2886
    • Stempniak, M.1    Hostomska, Z.2    Nodes, B.R.3    Hostomsky, Z.4
  • 112
    • 0026084948 scopus 로고
    • Structure and organization of the hepatitis C virus genome isolated from human carriers
    • Takamizawa A, Mori C, Fuke I et al. Structure and organization of the hepatitis C virus genome isolated from human carriers. J Virol 1991; 65: 1105-1113.
    • (1991) J Virol , vol.65 , pp. 1105-1113
    • Takamizawa, A.1    Mori, C.2    Fuke, I.3
  • 113
    • 0027936508 scopus 로고
    • Substrate specificity of the NS3 serine proteinase of hepatitis C virus as determined by mutagenesis at the NS3/NS4A junction
    • Leinbach SS, Bhat RA, Xia SM et al. Substrate specificity of the NS3 serine proteinase of hepatitis C virus as determined by mutagenesis at the NS3/NS4A junction. Virology 1994; 204: 163-169.
    • (1994) Virology , vol.204 , pp. 163-169
    • Leinbach, S.S.1    Bhat, R.A.2    Xia, S.M.3
  • 114
    • 0028156982 scopus 로고
    • Molecular model of the specificity pocket of the hepatitis C virus protease: Implications for substrate recognition
    • Pizzi E, Tramontano A, Tomei L et al. Molecular model of the specificity pocket of the hepatitis C virus protease: implications for substrate recognition. Proc Natl Acad Sci USA 1994; 91: 888-892.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 888-892
    • Pizzi, E.1    Tramontano, A.2    Tomei, L.3
  • 115
    • 0030844455 scopus 로고    scopus 로고
    • Probing the substrate specificity of hepatitis C virus NS3 serine protease by using synthetic peptides
    • Zhang RM, Durkin J, Windsor WT, McNemar C, Ramanathan L, Le HV. Probing the substrate specificity of hepatitis C virus NS3 serine protease by using synthetic peptides. J Virol 1997; 71: 6208-6213.
    • (1997) J Virol , vol.71 , pp. 6208-6213
    • Zhang, R.M.1    Durkin, J.2    Windsor, W.T.3    McNemar, C.4    Ramanathan, L.5    Le, H.V.6
  • 116
    • 0030944102 scopus 로고    scopus 로고
    • Substrate specificity of the hepatitis C virus serine protease NS3
    • Urbani A, Bianchi E, Narjes F et al. Substrate specificity of the hepatitis C virus serine protease NS3. J Biol Chem 1997; 272: 9204-9209.
    • (1997) J Biol Chem , vol.272 , pp. 9204-9209
    • Urbani, A.1    Bianchi, E.2    Narjes, F.3
  • 117
    • 0028908783 scopus 로고
    • Substrate determinants for cleavage in cis and in trans by the hepatitis C virus NS3 proteinase
    • Bartenschlager R, Ahlborn-Laake L, Yasargil K, Mous J, Jacobsen H. Substrate determinants for cleavage in cis and in trans by the hepatitis C virus NS3 proteinase. J Virol 1995; 69: 198-205.
    • (1995) J Virol , vol.69 , pp. 198-205
    • Bartenschlager, R.1    Ahlborn-Laake, L.2    Yasargil, K.3    Mous, J.4    Jacobsen, H.5
  • 118
    • 0028075902 scopus 로고
    • Substrate requirements of hepatitis C virus serine proteinase for intermolecular polypeptide cleavage in Escherichia coli
    • Komoda Y, Hijikata M, Sato S, Asabe S, Kimura K, Shimotohno K. Substrate requirements of hepatitis C virus serine proteinase for intermolecular polypeptide cleavage in Escherichia coli. J Virol 1994; 68: 7351-7357.
    • (1994) J Virol , vol.68 , pp. 7351-7357
    • Komoda, Y.1    Hijikata, M.2    Sato, S.3    Asabe, S.4    Kimura, K.5    Shimotohno, K.6
  • 119
    • 0030334850 scopus 로고    scopus 로고
    • Redesigning the substrate specificity of the hepatitis C virus NS3 protease
    • Failla CM, Pizzi E, DeFrancesco R, Tramontano A. Redesigning the substrate specificity of the hepatitis C virus NS3 protease. Folding Design 1996; 1: 35-42.
    • (1996) Folding Design , vol.1 , pp. 35-42
    • Failla, C.M.1    Pizzi, E.2    DeFrancesco, R.3    Tramontano, A.4
  • 120
    • 0030699529 scopus 로고    scopus 로고
    • Determinants of substrate specificity in the NS3 serine proteinase of the hepatitis C virus
    • Koch JO, Bartenschlager R. Determinants of substrate specificity in the NS3 serine proteinase of the hepatitis C virus. Virology 1997; 237: 78-88.
    • (1997) Virology , vol.237 , pp. 78-88
    • Koch, J.O.1    Bartenschlager, R.2
  • 121
    • 0342872087 scopus 로고    scopus 로고
    • Towards defining a minimal functional domain for NTPase and RNA helicase activities of the hepatitis C virus NS3 protein
    • Kim DW, Gwack Y, Han JH, Choe J. Towards defining a minimal functional domain for NTPase and RNA helicase activities of the hepatitis C virus NS3 protein. Virus Res 1997; 49: 17-25.
    • (1997) Virus Res , vol.49 , pp. 17-25
    • Kim, D.W.1    Gwack, Y.2    Han, J.H.3    Choe, J.4
  • 122
    • 0031000887 scopus 로고    scopus 로고
    • Polynucleotide modulation of the protease, nucleoside triphosphatase, and helicase activities of a hepatitis C virus NS3-NS4A complex isolated from transfected COS cells
    • Morgenstern KA, Landro JA, Hsaio K et al. Polynucleotide modulation of the protease, nucleoside triphosphatase, and helicase activities of a hepatitis C virus NS3-NS4A complex isolated from transfected COS cells. J Virol 1997; 71: 3767-3775.
    • (1997) J Virol , vol.71 , pp. 3767-3775
    • Morgenstern, K.A.1    Landro, J.A.2    Hsaio, K.3
  • 123
    • 0028800155 scopus 로고
    • Poly (U) binding activity of hepatitis C virus NS3 protein, a putative RNA helicase
    • Kanai A, Tanabe K, Kohara M. Poly (U) binding activity of hepatitis C virus NS3 protein, a putative RNA helicase. FEBS Lett 1995; 376: 221-224.
    • (1995) FEBS Lett , vol.376 , pp. 221-224
    • Kanai, A.1    Tanabe, K.2    Kohara, M.3
  • 124
    • 0031902992 scopus 로고    scopus 로고
    • Multiple enzymatic activities associated with recombinant NS3 protein of hepatitis C virus
    • Gallinari P, Brennan D, Nardi C et al. Multiple enzymatic activities associated with recombinant NS3 protein of hepatitis C virus. J Virol 1998; 72: 6758-6769.
    • (1998) J Virol , vol.72 , pp. 6758-6769
    • Gallinari, P.1    Brennan, D.2    Nardi, C.3
  • 125
    • 0025201350 scopus 로고
    • 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
    • Chambers TJ, Weir RC, Grakoui A et al. 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. Proc Natl Acad Sci USA 1990; 87: 8898-8902.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 8898-8902
    • Chambers, T.J.1    Weir, R.C.2    Grakoui, A.3
  • 127
    • 0028942494 scopus 로고
    • NS3-4A of hepatitis C virus is a chymotrypsin-like protease
    • Hahm B, Han DS, Back SH et al. NS3-4A of hepatitis C virus is a chymotrypsin-like protease. J Virol 1995; 69: 2534-2539.
    • (1995) J Virol , vol.69 , pp. 2534-2539
    • Hahm, B.1    Han, D.S.2    Back, S.H.3
  • 128
    • 0029094449 scopus 로고
    • The hepatitis C virus NS3 serine proteinase and NS4A cofactor: Establishment of a cell-free trans-processing assay
    • Lin C, Rice CM. The hepatitis C virus NS3 serine proteinase and NS4A cofactor: establishment of a cell-free trans-processing assay. Proc Natl Acad Sci USA 1995; 92: 7622-7626.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7622-7626
    • Lin, C.1    Rice, C.M.2
  • 129
    • 0029585447 scopus 로고
    • In vivo and in vitro transcleavage activity of hepatitis C virus serine proteinase expressed by recombinant baculoviruses
    • Suzuki T, Sato M, Chieda S et al. In vivo and in vitro transcleavage activity of hepatitis C virus serine proteinase expressed by recombinant baculoviruses. J Gen Virol 1995; 76: 3021-3029.
    • (1995) J Gen Virol , vol.76 , pp. 3021-3029
    • Suzuki, T.1    Sato, M.2    Chieda, S.3
  • 130
    • 0029609892 scopus 로고
    • Recombinant baculovirus-expressed NS3 proteinase of hepatitis C virus shows activity in cell-based and in vitro assays
    • Overton H, McMillan D, Gillespie F, Mills J. Recombinant baculovirus-expressed NS3 proteinase of hepatitis C virus shows activity in cell-based and in vitro assays. J Gen Virol 1995; 76: 3009-3019.
    • (1995) J Gen Virol , vol.76 , pp. 3009-3019
    • Overton, H.1    McMillan, D.2    Gillespie, F.3    Mills, J.4
  • 132
    • 0032540120 scopus 로고    scopus 로고
    • Expression of a hepatitis C virus NS3 protease-NS4A fusion protein in Escherichia coli
    • Inoue H, Sakashita H, Shimizu Y et al. Expression of a hepatitis C virus NS3 protease-NS4A fusion protein in Escherichia coli. Biochem Biophys Res Commun 1998; 245: 478-182.
    • (1998) Biochem Biophys Res Commun , vol.245 , pp. 478-1182
    • Inoue, H.1    Sakashita, H.2    Shimizu, Y.3
  • 133
    • 0029122587 scopus 로고
    • Bacterial expression and analysis of cleavage activity of HCV serine proteinase using recombinant and synthetic substrate
    • Kakiuchi N, Hijikata M, Komoda Y, Tanji Y, Hirowatari Y, Shimotohno K. Bacterial expression and analysis of cleavage activity of HCV serine proteinase using recombinant and synthetic substrate. Biochem Biophys Res Commun 1995; 210: 1059-1065.
    • (1995) Biochem Biophys Res Commun , vol.210 , pp. 1059-1065
    • Kakiuchi, N.1    Hijikata, M.2    Komoda, Y.3    Tanji, Y.4    Hirowatari, Y.5    Shimotohno, K.6
  • 134
    • 0030222125 scopus 로고    scopus 로고
    • Establishment of an in vitro assay system for screening hepatitis C virus protease inhibitors using high performance liquid chromatography
    • Sudo K, Inoue H, Shimizu Y et al. Establishment of an in vitro assay system for screening hepatitis C virus protease inhibitors using high performance liquid chromatography. Antiviral Res 1996; 32: 9-18.
    • (1996) Antiviral Res , vol.32 , pp. 9-18
    • Sudo, K.1    Inoue, H.2    Shimizu, Y.3
  • 135
    • 0030586870 scopus 로고    scopus 로고
    • A continuous assay of hepatitis C virus protease based on resonance energy transfer depsipeptide substrates
    • Taliani M, Bianchi E, Narjes F et al. A continuous assay of hepatitis C virus protease based on resonance energy transfer depsipeptide substrates. Anal Biochem 1996; 240: 60-67.
    • (1996) Anal Biochem , vol.240 , pp. 60-67
    • Taliani, M.1    Bianchi, E.2    Narjes, F.3
  • 136
    • 0030047195 scopus 로고    scopus 로고
    • Enzymatic characterization of purified NS3 serine proteinase of hepatitis C virus expressed in Escherichia coli
    • Mori A, Yamada K, Kimura J et al. Enzymatic characterization of purified NS3 serine proteinase of hepatitis C virus expressed in Escherichia coli. FEBS Lett 1996; 378: 37-42.
    • (1996) FEBS Lett , vol.378 , pp. 37-42
    • Mori, A.1    Yamada, K.2    Kimura, J.3
  • 137
    • 0028860369 scopus 로고
    • Proteolytic activity of NS3 serine proteinase of hepatitis C virus efficiently expressed in Escherichia coli
    • Shoji I, Suzuki T, Chieda S et al. Proteolytic activity of NS3 serine proteinase of hepatitis C virus efficiently expressed in Escherichia coli. Hepatology 1995; 22: 1648-1655.
    • (1995) Hepatology , vol.22 , pp. 1648-1655
    • Shoji, I.1    Suzuki, T.2    Chieda, S.3
  • 138
    • 0038343796 scopus 로고    scopus 로고
    • Product inhibition of the hepatitis C virus NS3 protease
    • Steinkühler C, Biasiol G, Brunetti M et al. Product inhibition of the hepatitis C virus NS3 protease. Biochemistry 1998; 37: 8899-8905.
    • (1998) Biochemistry , vol.37 , pp. 8899-8905
    • Steinkühler, C.1    Biasiol, G.2    Brunetti, M.3
  • 139
    • 0032560602 scopus 로고    scopus 로고
    • Potent peptide inhibitors of human hepatitis C virus NS3 protease are obtained by optimizing the cleavage products
    • Ingallinella P, Altamura S, Bianchi E et al. Potent peptide inhibitors of human hepatitis C virus NS3 protease are obtained by optimizing the cleavage products. Biochemistry 1998; 37: 8906-8914.
    • (1998) Biochemistry , vol.37 , pp. 8906-8914
    • Ingallinella, P.1    Altamura, S.2    Bianchi, E.3
  • 140
    • 0030796292 scopus 로고    scopus 로고
    • Characterization of engineered hepatitis C virus NS3 protease inhibitors affinity selected from human pancreatic secretory trypsin inhibitor and minibody repertoires
    • Dimasi N, Martin F, Volpari C et al. Characterization of engineered hepatitis C virus NS3 protease inhibitors affinity selected from human pancreatic secretory trypsin inhibitor and minibody repertoires. J Virol 1997; 71: 7461-7469.
    • (1997) J Virol , vol.71 , pp. 7461-7469
    • Dimasi, N.1    Martin, F.2    Volpari, C.3
  • 141
    • 0030719462 scopus 로고    scopus 로고
    • Isolation of RNA aptamers specific to the NS3 protein of hepatitis C virus from a pool of completely random RNA
    • Kumar PR, Machida K, Urvil PT et al. Isolation of RNA aptamers specific to the NS3 protein of hepatitis C virus from a pool of completely random RNA. Virology 1997; 237: 270-282.
    • (1997) Virology , vol.237 , pp. 270-282
    • Kumar, P.R.1    Machida, K.2    Urvil, P.T.3
  • 142
    • 0031577565 scopus 로고    scopus 로고
    • Novel hepatitis C virus protease inhibitors: Thiazolidine derivatives
    • Sudo K, Matsumoto Y, Matsushima M et al. Novel hepatitis C virus protease inhibitors: thiazolidine derivatives. Biochem Biophys Res Commun 1997; 238: 643-647.
    • (1997) Biochem Biophys Res Commun , vol.238 , pp. 643-647
    • Sudo, K.1    Matsumoto, Y.2    Matsushima, M.3
  • 143
    • 16044365570 scopus 로고    scopus 로고
    • Structure of sch 68631: A new hepatitis C virus proteinase inhibitor from Streptomyces sp
    • Chu M, Mierzwa R, Truumees I et al. Structure of sch 68631: a new hepatitis C virus proteinase inhibitor from Streptomyces sp. Tetrahedron Lett 1996; 37: 7229-7232.
    • (1996) Tetrahedron Lett , vol.37 , pp. 7229-7232
    • Chu, M.1    Mierzwa, R.2    Truumees, I.3
  • 144
    • 0028838013 scopus 로고
    • A novel method for analysis of viral proteinase activity encoded by hepatitis C virus in cultured cells
    • Hirowatari Y, Hijikata M, Shimotohno K. A novel method for analysis of viral proteinase activity encoded by hepatitis C virus in cultured cells. Anal Biochem 1995; 225: 113-120.
    • (1995) Anal Biochem , vol.225 , pp. 113-120
    • Hirowatari, Y.1    Hijikata, M.2    Shimotohno, K.3
  • 145
    • 0010353691 scopus 로고    scopus 로고
    • Development of an in vivo assay system suitable for screening inhibitors of hepatitis C viral protease
    • Song OK, Cho OH, Hahm B, Jang SK. Development of an in vivo assay system suitable for screening inhibitors of hepatitis C viral protease. Mol Cell 1996; 6: 183-189.
    • (1996) Mol Cell , vol.6 , pp. 183-189
    • Song, O.K.1    Cho, O.H.2    Hahm, B.3    Jang, S.K.4
  • 146
    • 0031036325 scopus 로고    scopus 로고
    • Chimeric Sindbis viruses dependent on the NS3 protease of hepatitis C virus
    • Filocamo G, Pacini L, Migliaccio G. Chimeric Sindbis viruses dependent on the NS3 protease of hepatitis C virus. J Virol 1997; 71: 1417-1427.
    • (1997) J Virol , vol.71 , pp. 1417-1427
    • Filocamo, G.1    Pacini, L.2    Migliaccio, G.3
  • 147
    • 0030589469 scopus 로고    scopus 로고
    • Generation of a novel poliovirus with a requirement of hepatitis C virus protease NS3 activity
    • Hahm B, Back SH, Lee TG, Wimmer E, Jang SK. Generation of a novel poliovirus with a requirement of hepatitis C virus protease NS3 activity. Virology 1996; 226: 318-326.
    • (1996) Virology , vol.226 , pp. 318-326
    • Hahm, B.1    Back, S.H.2    Lee, T.G.3    Wimmer, E.4    Jang, S.K.5
  • 149
    • 0028900785 scopus 로고
    • Identification of two flavivirus-like genomes in the GB hepatitis agent
    • Simons JN, Pilot-Matias TJ, Leary TP et al. Identification of two flavivirus-like genomes in the GB hepatitis agent. Proc Natl Acad Sci USA 1995; 92: 3401-3405.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 3401-3405
    • Simons, J.N.1    Pilot-Matias, T.J.2    Leary, T.P.3
  • 150
    • 0014405092 scopus 로고
    • On the active site of proteases. 3. Mapping the active site of papain; specific peptide inhibitors of papain
    • Schechter I, Berger A. On the active site of proteases. 3. Mapping the active site of papain; specific peptide inhibitors of papain. Biochem Biophys Res Commun 1968; 32: 898-902.
    • (1968) Biochem Biophys Res Commun , vol.32 , pp. 898-902
    • Schechter, I.1    Berger, A.2


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