Recent developments in hepatitis C antiviral research 1999 - 2000

Bibliography

• POORDAD FF, GISH RG: Developments in hepatitis Cduring 1997-1999. Exp. Opin. Ther. Patents (1999) 9:1249–1262.
   Web of Science ®Google Scholar
• KOFF RS: Hepatitis C. ScL Med. (1999) 5:16–25.
   Google Scholar
• WALKER MA: Hepatitis C virus: an overview of currentapproaches and progress. Drug Disc. Today (1999) 4:518–529.
   PubMedGoogle Scholar
• FARCI P, SHIMODA A, COIANA A et al.: The outcome ofacute hepatitis C predicted by the evolution of the viral quasispecies. Science (2000) 288:339–344.
   PubMed Web of Science ®Google Scholar
• REED KE, RICE CE: Overview of hepatitis C virus structure. polyprotein processing and protein properties. Curr. Top. Microbiol. Immunol. (2000) 242:55–84.
   Google Scholar
• ••This entire volume (242) is devoted to the HCV.
   Google Scholar
• RIJNBRAND RCA, LEMON SM: Internal ribosome entry site-mediated translation in hepatitis C virus replica-tion. Curr. Top. Microbiol. Immunol. (2000) 242:85–116.
   PubMedGoogle Scholar
• SUZUKI R, T SUZUKI, ISHII K et al: Processing and functions of hepatitis C virus proteins. Intel-virology (1999) 42:145–152.
   Google Scholar
• BARTENSCHLAGER R: Candidate Targets for hepatitis C virus-specific antiviral therapy. interviroiogy (1997) 40:378–393.
   PubMed Web of Science ®Google Scholar
• DAVIS GL, NELSON DR, REYES GR: Future options for the management of hepatitis C. Sem. Liver Dis. (1999) 19:103–112.
   PubMedGoogle Scholar
• ••This entire issue (19 (Suppl. 1)) is devoted to hepatitis C.
   Google Scholar
• DI BISCEGLIE AM: Hepatitis C - virology and future targets. Am. J. Med. (1999) 107:45S–48S.
   Google Scholar
• ••This entire issue (107 :6B) is devoted to hepatitis C.
   Google Scholar
• ROSEN HR, GRETCH DR: Hepatitis C virus: current understanding and prospects for future therapies. Mol. Med. Today (1999) 5:393–399.
   PubMedGoogle Scholar
• RICE CM, KOLYKHALOV AA, LIN C et al.: Hepatitis C virus genome organization and expression: potential antiviral targets. Antiviral Ther. (1996) 1:11–17.
   Google Scholar
• BARTENSCHLAGER R: Molecular targets in inhibition of hepatitis C virus replication. Antiviral Chem. Chemother. (1997) 8:281–301.
   Web of Science ®Google Scholar
• BLIGHT KJ, KOLYKHALOV AA, REED KE et al: Molecular virology of hepatitis C virus: an update with respect to potential antiviral targets. Antiviral Ther. (1998) 3:71–81.
   PubMedGoogle Scholar
• LITTLEJOHN M, LOCARINI SA, BARTHOLOMEUS Z: Targets for inhibition of hepatitis C virus replication. Ther. (1998) 3:83–91.
   Google Scholar
• FLAJOLET M, ROTONDO G, DAVIET L et al.: A genomic approach of the hepatitis C virus generates a protein interaction map. Gene (2000) 242:369–379.
   PubMed Web of Science ®Google Scholar
• KOLYKHALOV AA, MIHALIK K, FEINSTONE SM et al.: Hepatitis C virus-encoded enzymatic activities and conserved RNA elements in the 3' nontranslated region are essential for virus replication in vivo. J. Virology (2000) 74:2046–2051.
   PubMed Web of Science ®Google Scholar
• GISH RG: Standards of treatment in chronic hepatitis. Sem. Liver Dis. (1999) 19:35–47.
   PubMedGoogle Scholar
• PERRY CM, WILDE MI: Interferon-a-2a. BioDrugs (1998) 10:65–89.
   PubMedGoogle Scholar
• IINO S: Problems in the treatment of hepatitis C with interferon. Intervirology (1999) 42:166–172.
   PubMedGoogle Scholar
• HOUGHTON M: Strategies and prospects for vaccina-tion against the hepatitis C viruses. Curr. Top. Microbiol Immunol. (2000) 2 42:327–339.
   Google Scholar
• BERZOFSKY JA, AHLERS JD, DERBY MA et al.:Approaches to improve engineered vaccines for immunodeficiency virus and other viruses that cause chronic infections. Immunol Rev. (1999) 170:151–172.
   PubMed Web of Science ®Google Scholar
• LAMONACA V, MISSALE G, URBANI S et al: Conserved hepatitis C virus sequences are highly immunogenic for CD4+ T cells: implications for vaccine develop-ment. Hepatology (1999) 30:1088–1098.
   PubMedGoogle Scholar
• SHANG D, ZHAI W, ALLAIN JP: Broadly cross-reactive, high-affinity antibody to the hypervariable region of the hepatitis C virus in rabbits. Virology (1999) 258:396–405.
   PubMedGoogle Scholar
• CHANG JC, RUDINGER B, CONG M et al.: Artificial NS4mosaic antigen of hepatitis C virus. J Med. Vim]. (1999) 59:437–450.
   PubMedGoogle Scholar
• ESUMI M, RIKIHISA T, NISHIMURA S et al.: Experimental vaccine activities of recombinant El and E2 glycopro-teins and hypervariable region 1 peptides of hepatitis virus in chimpanzees. Arch. Virol. (1999) 144:973–980.
   PubMedGoogle Scholar
• OYASKI ML, ERTL HCJ: DNA vaccines. Sci. Med. (2000) 7:30–39.
   Google Scholar
• ENCKE J, ZU PUTLITZ J, WANDS JR: DNA vaccines. Intervirology (1999) 42:117–124.
   PubMedGoogle Scholar
• INCHAUSK G: DNA vaccine strategies for hepatitis C. j Hepatol. (1999) 30:339–346.
   PubMedGoogle Scholar
• •An excellent discussion of DNA vaccines in the context of hepatitis C.
   Google Scholar
• FOURNILLIER A, DEPLA E, KARAYIANNIS P et al.: Expres-sion of noncovalent hepatitis C virus envelope El-F2 complexes is not required for the induction of antibodies with neutralizing properties following DNA immunization. J Virol. (1999) 73:7497–7504.
   PubMedGoogle Scholar
• NISHIMURA Y, KAMEI A, UNO-FURUTA S et al.: A single immunization with a plasmid encoding hepatitis C virus (HCV) structural proteins under the elongation factor 1-alpha promoter elicits HCV-specific cytotoxic T-lymphocytes (CTL). Vaccine (1999) 18:675–680.
   PubMed Web of Science ®Google Scholar
• KIM N, SOHN H, CHOE J et al: Induction of cytotoxic T lymphocyte response against the core and NS3 genes of the hepatitis C virus in Balb/c mice. Korean J. Biol. Sci. (1999) 3:337–341.
   Google Scholar
• HU GJ, WANG RYH, HAN DS et al: Characterization of the humoral and cellular immune responses against hepatitis C virus core induced by DNA-based immuni-zation. Vaccine (1999) 17:3160–3170.
   PubMedGoogle Scholar
• GORDON EJ, BHAT R, LIU Q et al.: Immune responses to hepatitis C virus structural and nonstructural proteins induced by plasmid DNA immunizations. J. Infect. Dis. (2000) 181:42–50.
   PubMed Web of Science ®Google Scholar
• VIDALIN O, SPENGLER U, TREPO C et al: Targeting of hepatitis C virus core protein for MHC I or MHC II presentation does not enhance induction of immune responses to DNA vaccination. DNA Cell Biol. (1999) 18:611–621.
   PubMed Web of Science ®Google Scholar
• CHO JH, LEE SW, SUNG YC: Enhanced cellularimmunity to hepatitis C virus nonstructural proteins by codelivery of granulocyte macrophage-colony factor gene in intramuscular DNA immunization. Vaccine (1999) 17:1136–1144.
   PubMed Web of Science ®Google Scholar
• ARICHI T, SAITO T, MAJOR ME et al.: Prophylactic DNA vaccine for hepatitis C virus (HCV) infection: HCV-specific cytotoxic T lymphocyte induction and protection from HCV-recombinant vaccinia infection in an HLA-A2.1 transgenic mouse model. Proc. Nail Acad. Sci. USA (2000) 97:297–302.
   Google Scholar
• PILERI P, UEMATSU Y, CAMPAGNOLI S et al.: Binding of Hepatitis C virus to CD81. Science (1998) 282:938–941.
   PubMed Web of Science ®Google Scholar
• ••The definitive study describing the role of CD81 in thebinding of HCV to host cells.
   Google Scholar
• ODREMAN-MACCHIOLI FE, TISMENETZKY SG, ZOTTI Met al.: Influence of correct secondary and tertiary RNA folding on the binding of cellular factors to the HCV 'RFS. Nucleic Acids Res. (2000) 28:875–885.
   Google Scholar
• ZHANG H, HANECAK R, BROWN-DRIVER V et al.: Antisense oligonucleotide inhibition of hepatitis C virus (HCV) gene expression in livers of mice infected with an HCV-vaccinia virus recombinant. Antimirob. Agents Chemother. (1999) 43:347–353.
   PubMed Web of Science ®Google Scholar
• ••Work describing the antisense compounds now in clinicaltrials.
   Google Scholar
• ALT M, EISENHARDT S, SERWE M et al.: Comparativeinhibitory potential of differently modified antisense oligodeoxynucleotides on hepatitis C virus transla-tion. Eur. j Clin. Invest. (1999) 29:868–876.
   PubMed Web of Science ®Google Scholar
• WAKITA T, MORADPOUR D, TOKUSHIHGE K et al.: Antiviral effects of antisense RNA on hepatitis C virus RNA translation and expression. J Med. Virol. (1999) 57:217–222.
   PubMed Web of Science ®Google Scholar
• BROWN-DRIVER V, ETO T, LESNIK E et al: Inhibition oftranslation of hepatitis C virus RNA by 2t-modified antisense nucleotides. Antisense Nucl. Acid Drug Dev. (1999) 9:145–154.
   PubMedGoogle Scholar
• OKETANI M, ASAHINA Y, WU C et al.: Inhibition of hepatitis C virus-directed gene expression by a DNA ribonuclease. j Hepatol. (1999) 31:628–634.
   PubMed Web of Science ®Google Scholar
• MACEJAK DG, JENSEN KL, JAMISON SF et al.: Inhibition of hepatitis C virus (HCV)-RNA-dependent translation and replication of a chimeric HCV poliovirus using synthetic stabilized ribozymes. Hepatology (2000) 31:768–776.
   Google Scholar
• VOS S, NUNNS CL, SPENCE LA et al.: Structural analysis ofviral RNA fragments and their recognition by small molecule ligands. Nucleic Acids Symp. Ser. (1999) 41:176–178.
   Google Scholar
• KIEFT JS, ZHOU K, JUBIN R et al.: The hepatitis C virus internal ribosome entry site adopts an ion-dependent tertiary fold. j Mol. Biol. (1999) 292:513–529.
   Google Scholar
• KATZ BA, LUONG C: Recruiting Zn 2+ to mediate potent, specific inhibition of serine proteases. j Moi Biol. (1999) 292:669–684.
   PubMedGoogle Scholar
• DE FRANCESCO R, STEINKCJHLER C: Structure and function of the hepatitis C virus N53-NS4A serine proteinase. Curr. Top. Microbiol. Immunol. (2000) 242:149–169.
   PubMedGoogle Scholar
• SHOEMAKER KR: Recent progress on N53 protease as HCV drug target. Curr. Opin. AntiInfect. Invest. Drugs (2000) 1 :559–564.
   Google Scholar
• •An excellent overview of the latest N53 protease research.
   Google Scholar
• KWONG AD, KIM JL, RAO GL et al: Hepatitis C virus NS3/4A protease. Antiviral Res. (1998) 40:1–18.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• KIM JL, MORGENSTERN KA, LIN C et al: Crystal structure of the hepatitis C virus NS3 protease domain complex ed with a synthetic NS4A copep tide. Cell (1996) 87:343–355.
   PubMed Web of Science ®Google Scholar
• YAO N, REICHERT P, TAREMI SS et al: Molecular views ofviral polyprotein processing revealed by the crystal structure of the hepatitis C virus bifunctional protease-helicase. Structure (1999) 7:1353–1363.
   PubMed Web of Science ®Google Scholar
• •The first crystal structure of the entire N53 helicase/protease.
   Google Scholar
• BARBATO G, CICERO DO, NARDI MC et al.: 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. j Mol. Biol. (1999) 289:371–384.
   PubMed Web of Science ®Google Scholar
• BIANCHI E, INGENITO R, SIMON RJ et al.: Engineering and chemical synthesis of a transmembrane protein: the HCV protease cofactor protein N24A. j Am. Chem. Soc. (1999) 121:7689–7699.
   Google Scholar
• URBANI AB, BIASOL G, BRUNETTI M et al.: Multiple determinants influence complex formation of the hepatitis C virus N53 protease domain with its NS4A cofactor peptide. Biochemistry (1999) 38:5206–5215.
   PubMed Web of Science ®Google Scholar
• CICERO DO, BARBATO G, KOCH U et al.: Structural characterization of the interactions of optimized product inhibitors with the N-terminal proteinase domain of the hepatitis C virus (HCV) N53 protein by NMR and modeling studies. J. Mof Biol. (1999) 289:385–396.
   PubMed Web of Science ®Google Scholar
• BARBATO G, CICERO DO, CORDIER F et al.: Inhibitorbinding induces active site stabilization of the HCVNS3 protein serine protease domain. EMBO J. (2000) 289:385–396.
   Google Scholar
• LEUNG D, ABBENANTE G, FAIRLIE DP: Protease inhibi-: current status and future prospects. J Med. Chem. (2000) 43:305–341.
   PubMed Web of Science ®Google Scholar
• •An excellent overview of the medicinal chemistry of protease inhibitors, with a section devoted to HCV protease.
   Google Scholar
• SARDANA W, BLUE JT, ZUGAY-MURPHY J et al.: An uniquely purified HCV N53 protease and N54A21-34 peptide form a highly active serine protease complex in peptide hydrolysis. Protein Expr. Puri (1999) 16:440–447.
   PubMed Web of Science ®Google Scholar
• ZHANG R, BEYER BM, DURKIN J et al.: A continuousspectrophotometric assay for the hepatitis C virus serine protease. Anal. Biochem. (1999) 270:268–275.
   PubMed Web of Science ®Google Scholar
• KAKIUCHI N, NISHIKAWA S, HATTORI M et al.: A highthroughput assay of the hepatitis C virus protein 3 serine proteinase. Virol. Methods (1999) 80:77–84.
   PubMedGoogle Scholar
• LIU Y, KATI W, CHEN CM et al.: Effect correction. Anal. Biochem. (1999) 267:331–335.
   PubMed Web of Science ®Google Scholar
• CERRETANI M, DI RENZO L, SERAFINI S et al.: A high-throughput radiometric assay for hepatitis C virus N53 protease. Anal. Biochem. (1999) 266:192–197.
   PubMedGoogle Scholar
• CHUM, MIERZWA R, HE L et al: Isolation and structure of SCH 351633: a novel hepatitis C virus (HCV) NS3 protease inhibitor from the fungus Penicllium griseo-fulvum. Biorg. Med. Chem. Letters (1999) 9:1949–1952.
   PubMedGoogle Scholar
• ATTVVOOD MR, BENNETT JM, CAMPBELL AD: The design and synthesis of potent inhibitors of hepatitis C virus N53-4A proteinase. Antiviral Chem. Chemother. (1999) 10:259–273.
   PubMed Web of Science ®Google Scholar
• DI MARCO S, RIZZI M, VOLPARI C et al: Inhibition of thehepatitis C Virus N53/4A protease. J Biol. Chem. (2000) 275:7152–7157.
   PubMed Web of Science ®Google Scholar
• NARJES F, BRUNETTI M, COLARUSSO S et al: a-Ketoacids are potent slow binding Inhibitors of the hepatitis C virus protease. Biochemistry (2000) 39:1849–1861.
   PubMed Web of Science ®Google Scholar
• MARCHETTI A, ONTONORIA JM, MATASSA VG: Synthesis of two novel diphenyl ether analogs of an inhibitor of HCV NS3 protease. Synlett (1999):1000–1002.
   Google Scholar
• MARTIN F, STEINKCJHLER C, BRUNETTI M: A loop-mimetic inhibitor of the HCV-N53 protease derived from a minibody. Protein Eng. (1999) 12:1005–1011.
   PubMedGoogle Scholar
• VOCERO-AKBANI AM, VANDERHEYDEN N, LISSY A et al.: Killing HIV-infected cells by transduction with an HIV protease-activated caspase-3 protein. Nature Md. (1999) 5:29–33.
   PubMed Web of Science ®Google Scholar
• KWONG AD, KIM JL, LIN C: Structure and function of hepatitis C virus NS3 helicase. Curr. Top. Microbiol Immunol. (2000) 242:171–196.
   PubMed Web of Science ®Google Scholar
• LIN C, KIM JL: Structure-based mutagenesis study of hepatitis C virus N53 helicase. J. Viral (1999) 73:8789–8807.
   Google Scholar
• YAO N, HESSON M, HONG Z et al.: Structure of the hepatitis C virus RNA helicase domain. Nat. Struct. Biol. (1997) 4:463–467.
   PubMedGoogle Scholar
• KIM JL, MORGENSTERN KA, GRIFFITH JP et al.: Hepatitis virus N53 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding. Structure (1998) 6:89–100.
   PubMed Web of Science ®Google Scholar
• PORTER DJT, PREUGSCHAT F: Strand-separating activity of hepatitis C virus helicase in the absence of ATP. Biochemistry (2000) 39:5166–5173.
   PubMedGoogle Scholar
• BOROWSKI P, KUEHL R, MUELLER 0 et al.: Biochemical properties of a minimal functional domain with ATP-binding activity of the NTPase/helicase of hepatitis C virus. Eur. j Biochem. (1999) 266:715–723.
   Google Scholar
• WARDELL AD, ERRINGTON W, CIARAMELLA G et al.: Characterization and mutational analysis of the and NIPase activities of hepatitis C virus full-length NS3 protein. J. Gen. Virol. (1999) 80:701–709.
   PubMed Web of Science ®Google Scholar
• HESSON T, MANNARINO A, CABLE M: Probing the relationship between RNA-stimulated ATPase and helicase activities of HCV NS3 using 2'-0-methyl RNA substrates. Biochemistry (2000) 39:2619–2625.
   PubMedGoogle Scholar
• PREUGSCHAT F, DANGER DP, CARTER LH et al: Kinetic analysis of the effects of mutagenesis of W501 and V432 of the hepatitis C virus NS3 helicase domain on ATPase and strand-separating activity. Biochemistry (2000) 39:5174–5183.
   PubMedGoogle Scholar
• LEVIN MK, PATEL SS: The helicase from hepatitis C virus is active as an oligomer. J. Biol. Chem. (1999) 274:31839–31846.
   PubMedGoogle Scholar
• SOULTANAS P, DILLINGHAM MS, VELANKAR SS et al:DNA binding mediated conformational changes and metal ion coordination in the active site of PcrA helicase. j Mol Biol. (1999) 290:137–148.
   PubMedGoogle Scholar
• SPECTOR FC, LIANG L, GIORDANO H et al: Inhibition of herpes simplex virus replication by a 2-amino thiazole via interactions with the helicase component of the U1S-ULS-U1.52 complex. J. Virology (1998) 72:6979–6987.
   PubMed Web of Science ®Google Scholar
• WITHERELL GW, KNAP AK, GLUCHOWSKI C: Hepatitis C virus non-structural 5Aprotein as a therapeutic target. Curr. Opin. Antilnfect. Invest. Drugs (1999) 1:565–573.
   Web of Science ®Google Scholar
• MURAKAMI T, ENOMOTO N, KUROSAKI M et al.: Mutations in nonstructural protein 5A gene and response to interferon in hepatitis C virus genotype 2 infection. Hepatology (1999) 30:1045–1053.
   PubMed Web of Science ®Google Scholar
• NAKANO I, FUKUDA Y, KATANO Y et al: Why is the interferon sensitivity-determining region (ISDR) system useful in Japan? J. Hepatol. (1999) 30:1014–1022.
   Google Scholar
• CHUNG RT, MONTO A, DIENSTAG JL et al.: Mutations in the NS5A region do not predict interferon-responsiveness in American patients infected with genotype lb hepatitis C virus. J. Med. Virol. (1999) 58:353–358.
   PubMedGoogle Scholar
• SQUADRITO G, ORLANDO ME, CACCIOLA I et al.: Long-term response to interferon alpha is unrelated to 'interferon sensitivity determining region' variability in patients with chronic hepatitis C virus-1 B infection.. (1999) 30:1023–1027.
   Google Scholar
• KOCH JO, BARTENSCHLAGER R: Modulation of hepatitis virus NS5A hyperphosphorylation by nonstructural proteins NS3, NS4A and NS4B. J. Virology (1999) 73:7138–7146.
   PubMedGoogle Scholar
• NEDDERMAN P, CLEMENTI A, DE FRANCESCO R: Hyperphosphorylation of the hepatitis C virus NS5A protein requires an active NS3 protease, NS4A, NS4B and NS5A encoded on the same polyprotein. J. Virology (1999) 73:9984–9991.
   PubMedGoogle Scholar
• KIM J, LEE D, J CHOE: Hepatitis C virus NS5A protein is phosphorylated by casein kinase II. Biochem. Biophys. Res. Commun. (1999) 257:777–781.
   PubMedGoogle Scholar
• REED KE, RICE CM: Identification of the major phosphorylation site of the hepatitis C virus H strain5A protein as serine 2321. J. Biol. Chem. (1999) 274:28011–28018.
   PubMed Web of Science ®Google Scholar
• KORTH MJ, KATZE MG: Evading the interferonresponse: hepatitis C virus and the interferon-induced protein kinase, PKR. Curr. Top. Microbiol. Immunol (2000) 242:197–224.
   PubMedGoogle Scholar
• SONG J, FUJII M, WANG F et al.: The NS5A protein ofhepatitis C virus partially inhibits the antiviral activity of interferon. J. Gen. Vim]. (1999) 80:879–886.
   PubMedGoogle Scholar
• KOJI I, TANAKA Y, YAP CC et al.: Expression of hepatitis virus NS5B protein: characterization of its RNA polymerase activity and RNA binding. Hepatology (1999) 29:1227–1235.
   PubMedGoogle Scholar
• HAGEDORN CH, VAN BEERS EH, DE STAERCKE C: Hepatitis C virus RNA-dependent RNA polymerase (NS5B polymerase). Curr. Top. Microbiol. Immunol. (2000) 242:225–260.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• FERRARI E, WRIGHT-MINOGUE J, FANG JWS et al.: Characterization of soluble hepatitis C virus RNA-dependent RNA polymerase expressed in Escherichia coli. J. Virology (1999) 7:1649–1655.
   Google Scholar
• LESBURG CA, CABLE MB, FERRARI E et al.: Crystal structure of the RNA-dependent RNApolymerase from hepatitis C reveals a fully encircled active site. Nat. Struct. Biol. (1999) 6:937–943.
   PubMedGoogle Scholar
• ••This paper (and the following two) describe the crystalstructure of the NS5B polymerase which should prove very useful for structure-aided drug design.
   Google Scholar
• AGO H, ADACHI T, YOSHIDA A etal.: Crystal structure of the RNA-dependent RNA polymerase of hepatitis C virus. Structure (1999) 7:1417–1426.
   Google Scholar
• BRESSANELLI S, TOMEI L, ROUSSEL A et al.: Crystal structure of the RNA-dependent RNA polymerase of hepatitis C virus. Proc. Natl. Acad. Sci. USA (1999) 96:13034–13039.
   PubMed Web of Science ®Google Scholar
• LUO G, HAMATAKE RK, MATHIS DM et al: De novoinitia-tion of RNA synthesis by the RNA-dependent RNA polymerase (NS5B) of hepatitis C virus. j Vim/. (2000) 74:851–863.
   Google Scholar
• SUN XL, JOHNSON RB, HOCKMAN MA et al: De novo RNA synthesis catalyzed by HCV RNA-dependent RNA polymerase. Biochem. Biophys. Res. Commun. (2000) 268:798–803.
   PubMed Web of Science ®Google Scholar
• CHENG JC, CHANG MF, CHANG SC: Specific interaction between the hepatitis C virus NS5B RNA polymerase and the 3' end of the viral RNA. j Vim/. (1999) 73:7044–7049.
   Web of Science ®Google Scholar
• TU H, GAO L, SHI ST et al.: Hepatitis C virus RNA polymerase and NS5A complex with a SNARE-like protein. Virology (1999) 263:30–41.
   PubMed Web of Science ®Google Scholar
• PARK KJ, CHOI SH, MOON S et al: Identification of a cellular protein interacting with RNA polymerase of hepatitis C virus. J. Biochem. Mol. Biol. (2000) 33:59–62.
   Google Scholar
• ALBERTI A: Interferon alfacon-1: a novel interferon for the treatment of chronic hepatitis C. BioDrugs (1999) 12:343–357.
   PubMedGoogle Scholar
• DAVIS GL: Combination therapy with interferon alfa and ribavirin as retreatment of interferon relapse in chronic hepatitis C. Sem. Liver Dis. (1999) 19:49–55.
   PubMedGoogle Scholar
• MCHUTCHINSON JG, POYNARD T: Combination therapy with interferon plus ribavirin for the initial treatment of chronic hepatitis C. Sem. Liver Dis. (1999) 19:57–65.
   PubMedGoogle Scholar
• TAM RC, PAI B, BARD J et al.: Ribavirin polarizes human T cell responses towards a Type I cytokine profile. J Hepatol. (1999) 30:376–382.
   PubMed Web of Science ®Google Scholar
• MARKLAND W, MCQUAID TJ, JAIN J et al.: Broad-spectrum antiviral activity of the IMP dehydrogenase inhibitor VX-497: a comparison with ribavirin and demonstrations of antivral additivity with alpha interferon. Antimirob. Agents Chemother. (20 0 0) 44 :859–866.
   Google Scholar
• MARTIN J, NAVAS S, FERNANDEZ M et al.: In vitro effect of amantidine and interferon alpha-2a on hepatitis C virus markers in cultured peripheral blood mononu-clear cells from hepatitis C virus-infected patients. Antiviral Res. (1999) 42:59–70.
   PubMedGoogle Scholar
• JUBIN R, MURRAY MG, HOWE AYM et al.: Arnantadine and rimantidine have no direct inhibitory effects against hepatitis C viral protease, helicase, ATPase, polymerase and internal ribosomal entry site-mediated translation. J. Infect. Dis. (2000) 181:331–334.
   PubMedGoogle Scholar
• LOOK MP, GERARD A, RAO GS et al.: Interferon/antioxi-dant combination therapy for chronic hepatitis C - a controlled pilot trial. Antiviral Res. (1999) 43:113–122.
   PubMed Web of Science ®Google Scholar
• GIAMBARTOLOMEI S, ARTINI M, ALMERIGHI C et al.: Nonsteroidal anti-inflammatory drug metabolism potentiates interferon alfa signaling by increasing STAT1 phophorylation. Hepatology (1999) 30:510–516.
   PubMedGoogle Scholar
• HEIM MH, MORADPOUR D, BLUM HE: Expression of hepatitis C virus proteins inhibits signal transduction through the Jak-STAT pathway. J. Virology (1999) 73 :8469–8475.
   PubMed Web of Science ®Google Scholar
• NAYLOR PH: Zadaxin (thymosin alpha 1) for the treatment of viral hepatitis. Expert Opin. Invest. Drugs (1999) 8:281–287.
   PubMedGoogle Scholar
• MCHUTCHINSON JG, GIANELLI G, NYBERG L et al: A pilot study of daily subcutaneous interleukin-10 in patients with chronic hepatitis C. J. Interferon Cytokine Res. (1999) 19:1265–1270.
   PubMedGoogle Scholar
• LEE JH, TEUBER G, VON WAGNER M et al.: Antiviral effect of human recombinant interleukin-12 in patients infected with hepatitis C virus. J Med. Virol. (2000) 60:264–268.
   Google Scholar
• MEHTA A, ZITZMANN N, RUDD PM et al: a-Glucosidase inhibitors as potential broad based anti-viral agents. FEBS Letters (1998) 430:17–22.
   PubMed Web of Science ®Google Scholar
• SCHINAZI RF, ILAN E, BLACK PL et al.: Cell-based and animal models for hepatitis B and C viruses. Antiviral Chem. Chemother. (1999) 10:99–114.
   PubMed Web of Science ®Google Scholar
• KATO N, SHIMOTOHNO K: Systems to culture hepatitis virus. Curr. Top. Microbiol. Immunol. (2 0 0 0) 242:261–278.
   Google Scholar
• LOHMANN V, KORNER F, KOCH JO: Replication of subgenomic hepatitis C virus RNAs in a hepatoma cell line. Science (1999) 285:110–113.
   PubMed Web of Science ®Google Scholar
• ••This work by Bartenschlager et al. may provide the firstreproducible, practical cell-culture system for HCV.
   Google Scholar