Bibliography
- CHOO QL, KUO G, WEINER AJ etal.: Isolation of a cDNA clone derived from a blood-borne non-A, non-B viral hepatitis genome. Science (1989) 24:359–362.
- ••Original report describing the firstmolecular cloning of HCV.
- CORNBERG M, WEDEMEYER H, MANNS MP: Treatment of chronic hepatitis C with PEGylated interferon and ribavirin. Carr. Gastroenteral. Rep. (2002) 4:23–30.
- MANNS MP, MCHUTCHISON JG, GORDON SC et Peginterferon alfa-2b plus ribavirin compared with interferon alfa-2b plus ribavirin for initial treatment of chronic hepatitis C: a randomised trial. Lancet (2001) 358:958–965.
- ••References 2 and 3 describe the mostefficacious treatment combination presently available.
- BAZAN JF, FLETTERICK RJ: Detectionof a trypsin-like serine protease motif in flaviviruses and pestiviruses. Virology (1989) 171:637–639.
- MILLER RH, PURCELL RH: Hepatitis Cvirus shares amino acid sequence similarity with pestiviruses and flaviviruses as well as members of two plant virus supergroups. Proc. Natl. Acad. Sci. USA (1990) 87:2057–2061.
- LOHMANN V, KOCH JO, BARTENSCHLAGER R: Processing pathways of the hepatitis C virus j Hepatal. (1996) 24:11–19.
- BARTENSCHLAGER R, AHLBORN-LAAKE L, MOUS J et al.: Kinetic and structural analyses of hepatitis C virus polyprotein processing. j Viral. (1994) 68:5045–5055.
- FAILLA C, TOMEI L, DE FRANCESCOR: Both N53 and NS4A are required for proteolytic processing of hepatitis C virus nonstructural proteins. j Viral. (1994) 68:3753–3760.
- GRAKOUI A, MCCOURT DW, WYCHOWSKI C et al.: A second hepatitis C virus-encoded proteinase. Proc. Nati Acad. Sci. USA (1993) 90:10583–10587.
- HIJIKATA M, MIZUSHIMA H, AKAGI T: Two distinct proteinase activities required for the processing of a putative nonstructural precursor protein of hepatitis C virus. j Viral. (1993) 67:4665–4675.
- 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 Viral. (2000) 74:2046–2051.
- •First demonstration that HCV proteases are essential for infectivity.
- PALLAORO M, LAHM A, BIASIOL G et al.: Characterization of the hepatitis C virus N52/3 processing reaction using a purified precursor protein. I Viral. (2001) 75:9939–9946.
- WHITNEY M, STACK JH, DARKE PL et al.: A collaborative screening program for the discovery of inhibitors of HCV N52/3 is-cleaving protease activity. J. Biomol. Screen. (2002) 7:149–154.
- LOHMANN V, KORNER F, KOCH JO et al: Replication of subgenomic hepatitis C virus RNAs in a hepatoma cell line. Science (1999) 285:110–113.
- ••First cell culture system of HCVreplication.
- BARTENSCHLAGER R: Hepatitis C virus replicons: potential role for drug development. Nature Rev. Drug Discov. (2002) 1:911–916.
- KOLYKHALOV AA, AGAPOV EV, BLIGHT KJ etal.: Transmission of hepatitis C by intrahepatic inoculation with transcribed RNA. Science (1997) 277:570–574.
- ••First demonstration of infection by amolecular clone of the HCV genome.
- MERCER DE SCHILLER DE, ELLIOTT JF et al: Hepatitis C virus replication in mice with chimeric human livers. Nat. Med. (2001) 7:927–933.
- ILAN E, ARAZI J, NUSSBAUM O etal.: The hepatitis C virus (HCV)-Trimera mouse: a model for evaluation of agents against HCV. j Infect Dis. (2002) 185:153–161.
- KIM JL, MORGENSTERN KA, LIN C et al: Crystal structure of the hepatitis virus NS3 proteinase domain complexed with a syntehtic NS4A cofactor peptide. Cell (1996) 87:343–355.
- LOVE RA, PARGE HE, WICKERSHAM JA etal.: 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.
- YAN Y, LI Y, MUNSHI S et al: Complex ofNS3 protease and NS4A peptide of BK strain hepatitis C virus: A 2.2 A resolution structure in a hexagonal crystal form. Protein Li. (1998) 7:837–847.
- BARBATO G, CICERO DO, NARDI C 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. Mal Biol. (1999) 289:371–384.
- YAO N, REICHERT P, TAREMI SS et al: Molecular views of viral polyprotein processing revealed by the crystal structure of the hepatitis C virus bifunctional protease-helicase. Structure Fold Des. (1999) 15:1353–1563.
- ••References 19–23, describing X-ray and NMR structures, give insight into the mechanisms of activation of the NS3 protease by its cofactor and into the mechanisms and consequences of product inhibition.
- PIZZI E, TRAMONTANO A, TOMEI L etal.: Molecular model of the specificity pocket of the hepatitis C virus proteinase: implications for substrate recognition. Proc. Natl. Acad. Sci. USA (1994) 91:888–892.
- •A homology model of the Si pocket of the NS3 protease was used to predict its P1 specificity.
- FAILLA C, PIZZI E, DE FRANCESCO R etal.: Redesigning the substrate specificity of the hepatitis C virus protease. Folding Design (1996) 1:35–42.
- KOCH JO, BARTENSCHLAGER R: Determinants of substrate specificity in the NS3 serine proteinase of the hepatitis C virus. Virology (1997) 237:78–88.
- BARTENSCHLAGER R, AHLBORN-LAAKE L, YASARGIL K et al: Substrate determinants for cleavage in cis and in trans by the hepatitis C virus N53 proteinase. Viral (1995) 69:198–205.
- STEINKUHLER C, BIASIOL G, BRUNETTI M et al: Product inhibition of the hepatitis C virus N53 protease. Biochemistry (1998) 37:8899–8905.
- LLINAS-BRUNET M, BAILEY M, FAZAL G et al.: Peptide based inhibitors of the hepatitis C virus serine protease. Bioorg. Med. Chem. Lett.(1998) 8:1713–1718.
- INGALLINELLA P, ALTAMURA S, BIANCHI E et al.: Potent peptide inhibitors of human hepatitis C virus NS3 protease are obtained by optimising the cleavage products. Biochemistry (1998) 37:8906–8914.
- ••References 28–30 describe thephenomenon of product inhibition of the N53 protease and how this feature can be used to develop potent peptide inhibitors.
- URBANI A, BIANCHI E, NARJES F etal.: Substrate specificity of the hepatitis C virus serine protease N53. J. Biol. Chem. (1997) 272:9204–9209.
- ZHANG R, DURKIN J, WINDSOR WT etal.: Probing the substrate specificity of hepatitis C virus NS3 serine protease by using synthetic peptides. j Viral (1997) 71:6208–6213.
- PACINI L, VITELLI A, FILOCAMO G etal.: In vivo selection of protease cleavage sites by using chimeric sindbis virus libraries. J. Viral (2000) 74:10563–10570.
- KIM SY, PARK KW, LEE YJ et al: In vivo determination of substrate specificity of hepatitis C virus N53 protease: genetic assay for site-specific proteolysis. Anal. Biochem. (2000) 15:42–48.
- KOCH U, BIASIOL G, BRUNETTI M et al.: Role of charged residues in the catalytic mechanism of hepatitis C virus N53 protease: electrostatic precollision guidance and transition state stabilization. Biochemistry (2001) 40:631–640.
- PERNI RB: NS3.4A protease as a target for interfering with hepatitis C virus replication. Drug News Perspect. (2000) 13:69–77.
- DYMOCK BW, JONES PS, WILSON FX:Novel approaches to the treatment of hepatitis C virus infection. Antiviral Chem. Chemother. (2000) 11:79–96.
- STEINKOHLER C, KOCH U, NARJES F et al.: Hepatitis C virus serine protease inhibitors: current progress and future challenges. Cum: Med. Chem. (2001) 8:919–932.
- BEAULIEU PL, LLINAS-BRUNET M: Therapies for hepatitis C infection: targeting the non-structural proteins of HCV. Curr. Med. Chem.: Anti-Infective Agents (2002) 1:163–176.
- BIANCHI E, PESSI A: Inhibiting viral proteases: Challenges and opportunities. Biopolymers (2002) 66:101–114.
- TAN SL, PAUSE A, SHI Y: Hepatitis C virus therapeutics: Current status and emerging strategies. Nat. Rev Drug Discov. (2002) 1:867–881.
- WEST ML, FAIRLIE DP: Targeting HIV protease: a test of drug design methodologies. Trends Pharmacol Sci. (1995) 16:67–75.
- JOHANSSON A, HUBATSCH I, AKERBLOM E et al.: Inhibition of hepatitis C virus N53 protease activity by product-based peptides is dependent on helicase domain. Bioorg. Med. Chem. Lett. (2001) 11:203–206.
- JOHANSSON A, POLIAKOV A, AKERBLOM E et al.: Tetrapeptides as potent protease inhibitors of hepatitis C virus full-Length N53 (protease-helicasei NTPase). Bioorg. Med. Chem. (2002) 10:3915–3922.
- POUPART MA, CAMERON DR, CHABOT C etal.: Solid phase synthesis ofpeptidomimetic inhibitors for the hepatitis C virus protease. j Org. Chem. (2001) 66:4743–4751.
- LLINAS-BRUNET M, BAILEY M, BORDELEAU J et al.: Discovery of novel tri-peptide inhibitors of the Hepatitis C virus serine protease. Abstr. Pap. Am. Chem. Soc. (2000) 220:MEDI–018.
- •First report on tripeptide inhibitors of the NS3 protease with cell-based activity.
- LLINAS-BRUNET M: NS3 serine protease inhibitors as potential antiviral agents for the treatment of hepatitis C virus infections. 3rd International Antiviral & Vaccine Discovery & Development Summit, Princeton, NJ, USA (2002).
- LLINAS-BRUNET M: XVIIth International Medicinal Chemistry Symposium, Barcelona, Spain (2002).
- EDE NJ, EAGLE SN, WICKHAM G et al.: Solid phase synthesis of peptide aldehyde protease inhibitors. Probing the proteolytic sites of hepatitis C virus polyprotein. j Pept. Li. (2000) 6:11–18.
- PRIESTLEY ES, DE LUCCA I, GHAVIMI B et al.: P1 Phenethyl peptide boronic acid inhibitors of HCV N53 protease. Bioorg. Med. Chem. Lett. (2002) 12:3199–3202.
- NARJES F, KOEHLER KF, KOCH U et al: A designed P1 cysteine mimetic for covalent and non-covalent inhibitors of HCV N53 protease. Bioorg. Med. Chem. Lett. (2002) 12:701–704.
- NARJES E BRUNETTI M, COLARUSSO S et al: Alpha-ketoacids are potent slow binding inhibitors of the Hepatitis C virus N53 protease. Biochemistry (2000) 39: 1849-1861.
- •References 51 and 52 describe the rational design of a cysteine mimetic and its successful incorporation into mechanism-based inhibitors.
- COLARUSSO S, GERLACH B, KOCH U et al.: Evolution, synthesis and SAR of tripeptide lalphal-ketoacid Inhibitors of the hepatitis C virus N53/NS4A serine protease. Bioorg. Med. Chem. Lett. (2002) 12:705–708.
- NIZI E, KOCH U, PONZI S et al.: Capped dipeptide lalphal-Ketoacid inhibitors of the HCV N53 protease. Bioorg. Med. Chem. Lett. (2002) 12:3325–3328.
- BEEVERS R, CARR MG, JONES PS et al.:Solution and solid-Phase synthesis of potent inhibitors of hepatitis C Virus N53 proteinase. Bioorg. Med. Chem. Lett. (2002) 12:641–643.
- BENNETT JM, CAMPBELL AD, CAMPBELL AJ et al: The identification of a-ketoamides as potent inhibitors of Hepatitis C virus N53-4A Proteinase. Bioorg. Med. Chem. Lett. (2001) 11:355–357.
- COLARUSSO S, GERLACH B, KOCH U et al: Solid phase synthesis of novel non-covalent amide inhibitors of the hepatitis C virus serine protease.Drugs Future (2002) 27(Suppl. A):179.
- INGALLINELLA P, FATTORI D, ALTAMURA S et al.: Prime site binding inhibitors of a serine protease: NS3/4A of hepatitis C virus. Biochemistry (2002) 41:5483–5492.
- •First report on inhibitors binding exclusively to the prime site of a serine protease.
- SING WT, LEE CL, YEO SL et al.: Arylalkylidene rhodanine with bulky and hydrophobic functional group as selective HCV N53 protease inhibitor. Bioorg. Med. Chem. Lett. (2001) 11:91–94.
- SPERANDIO D, GANGLOFF AR, LITVAK J et al.: Highly potent non-peptidic inhibitors of the HCV N53/4A serine protease. Bioorg. Med. Chem. Lett. (2002) 12:3129–3133.
Websites
- http://www.cdc.gov/ncidod/diseases/ hepatitis/slideset/hep_c/ hcv_epi_for_distrib_000925.pdf HEPATITIS BRANCH: CDC- Centers for Disease Control and Prevention Report (2000).
- http://consensus.nih.gov/cons/116/ Hepc091202.pdf NIH Consensus Development conference statement.