메뉴 건너뛰기




Volumn 369, Issue , 2013, Pages 113-142

Hepatitis C virus proteins: From structure to function

Author keywords

[No Author keywords available]

Indexed keywords

CORE PROTEIN; GLYCOPROTEIN E1; GLYCOPROTEIN E2; NONSTRUCTURAL PROTEIN 4B; NONSTRUCTURAL PROTEIN 5A; NS2 PROTEASE; NS3 4A PROTEIN; P7 VIROPORIN; PHOSPHOPROTEIN; RNA DIRECTED RNA POLYMERASE; RNA HELICASE; STRUCTURAL PROTEIN; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 84876520299     PISSN: 0070217X     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-3-642-27340-7_5     Document Type: Article
Times cited : (281)

References (135)
  • 2
    • 84856947208 scopus 로고    scopus 로고
    • Conserved glycine 33 residue in flexible domain i of hepatitis C virus core protein is critical for virus infectivity
    • Angus AG, Loquet A, Stack SJ, Dalrymple D, Gatherer D, Penin F, Patel AH (2012) Conserved glycine 33 residue in flexible domain I of hepatitis C virus core protein is critical for virus infectivity. J Virol 86:679-6900
    • (2012) J Virol , vol.86 , pp. 679-6900
    • Angus, A.G.1    Loquet, A.2    Stack, S.J.3    Dalrymple, D.4    Gatherer, D.5    Penin, F.6    Patel, A.H.7
  • 3
    • 13944263525 scopus 로고    scopus 로고
    • Mutational analysis of hepatitis C virus nonstructural protein 5A: Potential role of differential phosphorylation in RNA replication and identification of a genetically flexible domain
    • Appel N, Pietschmann T, Bartenschlager R (2005) Mutational analysis of hepatitis C virus nonstructural protein 5A: potential role of differential phosphorylation in RNA replication and identification of a genetically flexible domain. J Virol 79:3187-31944
    • (2005) J Virol , vol.79 , pp. 3187-31944
    • Appel, N.1    Pietschmann, T.2    Bartenschlager, R.3
  • 5
    • 72849147739 scopus 로고    scopus 로고
    • Crystal structure of a novel conformational state of the flavivirus NS3 protein: Implications for polyprotein processing and viral replication
    • Assenberg R, Mastrangelo E, Walter TS, Verma A, Milani M, Owens RJ, Stuart DI, Grimes JM, Mancini EJ (2009) Crystal structure of a novel conformational state of the flavivirus NS3 protein: implications for polyprotein processing and viral replication. J Virol 83:12895-129066
    • (2009) J Virol , vol.83 , pp. 12895-129066
    • Assenberg, R.1    Mastrangelo, E.2    Walter, T.S.3    Verma, A.4    Milani, M.5    Owens, R.J.6    Stuart, D.I.7    Grimes, J.M.8    Mancini, E.J.9
  • 7
    • 0030051777 scopus 로고    scopus 로고
    • Identification and properties of the RNAdependent RNA polymerase of hepatitis C virus
    • Behrens S-E, Tomei L, De Francesco R (1996) Identification and properties of the RNAdependent RNA polymerase of hepatitis C virus. EMBO J 15:12-222
    • (1996) EMBO J , vol.15 , pp. 12-222
    • Behrens, S.-E.1    Tomei, L.2    De Francesco, R.3
  • 8
    • 63149134943 scopus 로고    scopus 로고
    • The NS4A protein of hepatitis C virus promotes RNA-coupled ATP hydrolysis by the NS3 helicase
    • Beran RK, Lindenbach BD, Pyle AM (2009) The NS4A protein of hepatitis C virus promotes RNA-coupled ATP hydrolysis by the NS3 helicase. J Virol 83:3268-32755
    • (2009) J Virol , vol.83 , pp. 3268-32755
    • Beran, R.K.1    Lindenbach, B.D.2    Pyle, A.M.3
  • 9
    • 80052284074 scopus 로고    scopus 로고
    • Hepatitis C virus stimulates the phosphatidylinositol 4-kinase IIIα-dependent phosphatidylinositol 4-phosphate production that is essential for its replication
    • Berger KL, Kelly SM, Jordan TX, Tartell MA, Randall G (2011) Hepatitis C virus stimulates the phosphatidylinositol 4-kinase IIIα-dependent phosphatidylinositol 4-phosphate production that is essential for its replication. J Virol 85:8870-88833
    • (2011) J Virol , vol.85 , pp. 8870-88833
    • Berger, K.L.1    Kelly, S.M.2    Jordan, T.X.3    Tartell, M.A.4    Randall, G.5
  • 10
    • 0034623816 scopus 로고    scopus 로고
    • Efficient initiation of HCV RNA replication in cell culture
    • Blight KJ, Kolykhalov AA, Rice CM (2000) Efficient initiation of HCV RNA replication in cell culture. Science 290:1972-19744
    • (2000) Science , vol.290 , pp. 1972-19744
    • Blight, K.J.1    Kolykhalov, A.A.2    Rice, C.M.3
  • 11
    • 79960951066 scopus 로고    scopus 로고
    • A concerted action of hepatitis C virus p7 and nonstructural protein 2 regulates core localization at the endoplasmic reticulum and virus assembly
    • Boson B, Granio O, Bartenschlager R, Cosset FL (2011) A concerted action of hepatitis C virus p7 and nonstructural protein 2 regulates core localization at the endoplasmic reticulum and virus assembly. PLoS Pathog 7:e10021444
    • (2011) PLoS Pathog , vol.7
    • Boson, B.1    Granio, O.2    Bartenschlager, R.3    Cosset, F.L.4
  • 12
    • 23844530172 scopus 로고    scopus 로고
    • Hepatitis C virus core protein is a dimeric α-helical protein exhibiting membrane protein features
    • Boulant S, Vanbelle C, Ebel C, Penin F, Lavergne JP (2005) Hepatitis C virus core protein is a dimeric α-helical protein exhibiting membrane protein features. J Virol 79:11353-113655
    • (2005) J Virol , vol.79 , pp. 11353-113655
    • Boulant, S.1    Vanbelle, C.2    Ebel, C.3    Penin, F.4    Lavergne, J.P.5
  • 14
    • 34547592075 scopus 로고    scopus 로고
    • Disrupting the association of hepatitis C virus core protein with lipid droplets correlates with a loss in production of infectious virus
    • Ulant S, Targett-Adams P, McLauchlan J (2007) Disrupting the association of hepatitis C virus core protein with lipid droplets correlates with a loss in production of infectious virus. J Gen Virol 88:2204-22133
    • (2007) J Gen Virol , vol.88 , pp. 2204-22133
    • Ulant, S.1    Targett-Adams, P.2    McLauchlan, J.3
  • 15
    • 14644415892 scopus 로고    scopus 로고
    • The hepatitis C virus alternate reading frame and its family of novel products: The alternate reading frame protein/F-protein, the double-frameshift protein, and others
    • Branch AD, Stump DD, Gutierrez JA, Eng F, Walewski JL (2005) The hepatitis C virus alternate reading frame and its family of novel products: the alternate reading frame protein/F-protein, the double-frameshift protein, and others. Semin Liver Dis 25:105-1177
    • (2005) Semin Liver Dis , vol.25 , pp. 105-1177
    • Branch, A.D.1    Stump, D.D.2    Gutierrez, J.A.3    Eng, F.4    Walewski, J.L.5
  • 16
    • 55749102288 scopus 로고    scopus 로고
    • Structural determinants for membrane association and dynamic organization of the hepatitis C virus NS3-4A complex
    • Brass V, Berke JM, Montserret R, Blum HE, Penin F, Moradpour D (2008) Structural determinants for membrane association and dynamic organization of the hepatitis C virus NS3-4A complex. Proc Natl Acad Sci USA 105:14545-145500
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 14545-145500
    • Brass, V.1    Berke, J.M.2    Montserret, R.3    Blum, H.E.4    Penin, F.5    Moradpour, D.6
  • 18
    • 0036120573 scopus 로고    scopus 로고
    • Structural analysis of the hepatitis C virus RNA polymerase in complex with ribonucleotides
    • Bressanelli S, Tomei L, Rey FA, De Francesco R (2002) Structural analysis of the hepatitis C virus RNA polymerase in complex with ribonucleotides. J Virol 76:3482-34922
    • (2002) J Virol , vol.76 , pp. 3482-34922
    • Bressanelli, S.1    Tomei, L.2    Rey, F.A.3    De Francesco, R.4
  • 20
    • 84866943211 scopus 로고    scopus 로고
    • The p7 protein of hepatitis C virus forms structurally plastic, minimalist ion channels
    • Chandler DE, Penin F, Schulten K, Chipot C (2012) The p7 protein of hepatitis C virus forms structurally plastic, minimalist ion channels. PLoS Comp Biol 8:e10027022
    • (2012) PLoS Comp Biol , vol.8
    • Chandler, D.E.1    Penin, F.2    Schulten, K.3    Chipot, C.4
  • 22
    • 33846005485 scopus 로고    scopus 로고
    • Evidence for the formation of a heptameric ion channel complex by the hepatitis C virus p7 protein in vitro
    • Clarke D, Griffin S, Beales L, Gelais CS, Burgess S, Harris M, Rowlands D (2006) Evidence for the formation of a heptameric ion channel complex by the hepatitis C virus p7 protein in vitro. J Biol Chem 281:37057-370688
    • (2006) J Biol Chem , vol.281 , pp. 37057-370688
    • Clarke, D.1    Griffin, S.2    Beales, L.3    Gelais, C.S.4    Burgess, S.5    Harris, M.6    Rowlands, D.7
  • 26
    • 80055073369 scopus 로고    scopus 로고
    • Trafficking of hepatitis C virus core protein during virus particle assembly
    • Counihan NA, Rawlinson SM, Lindenbach BD (2011) Trafficking of hepatitis C virus core protein during virus particle assembly. PLoS Pathog 7:e10023022
    • (2011) PLoS Pathog , vol.7
    • Counihan, N.A.1    Rawlinson, S.M.2    Lindenbach, B.D.3
  • 27
    • 3042576370 scopus 로고    scopus 로고
    • The hepatitis C virus core protein is a potent nucleic acid chaperone that directs dimerization of the viral (+) strand RNA in vitro
    • Cristofari G, Ivanyi-Nagy R, Gabus C, Boulant S, Lavergne JP, Penin F, Darlix JL (2004) The hepatitis C virus core protein is a potent nucleic acid chaperone that directs dimerization of the viral (+) strand RNA in vitro. Nucleic Acids Res 32:2623-26311
    • (2004) Nucleic Acids Res , vol.32 , pp. 2623-26311
    • Cristofari, G.1    Ivanyi-Nagy, R.2    Gabus, C.3    Boulant, S.4    Lavergne, J.P.5    Penin, F.6    Darlix, J.L.7
  • 29
    • 0033992657 scopus 로고    scopus 로고
    • Structure and function of the hepatitis C virus NS3-NS4A serine protease
    • de Francesco R, Steinkuhler C (2000) Structure and function of the hepatitis C virus NS3-NS4A serine protease. Curr Top Microbiol Immunol 242:149-1699
    • (2000) Curr Top Microbiol Immunol , vol.242 , pp. 149-1699
    • De Francesco, R.1    Steinkuhler, C.2
  • 31
    • 79955383686 scopus 로고    scopus 로고
    • Unmasking the active helicase conformation of nonstructural protein 3 from hepatitis C virus
    • Ding SC, Kohlway AS, Pyle AM (2011) Unmasking the active helicase conformation of nonstructural protein 3 from hepatitis C virus. J Virol 85:4343-43533
    • (2011) J Virol , vol.85 , pp. 4343-43533
    • Ding, S.C.1    Kohlway, A.S.2    Pyle, A.M.3
  • 32
    • 0036100578 scopus 로고    scopus 로고
    • Expression of hepatitis C virus proteins induces distinct membrane alterations including a candidate viral replication complex
    • Egger D, Wolk B, Gosert R, Bianchi L, Blum HE, Moradpour D, Bienz K (2002) Expression of hepatitis C virus proteins induces distinct membrane alterations including a candidate viral replication complex. J Virol 76:5974-59844
    • (2002) J Virol , vol.76 , pp. 5974-59844
    • Egger, D.1    Wolk, B.2    Gosert, R.3    Bianchi, L.4    Blum, H.E.5    Moradpour, D.6    Bienz, K.7
  • 33
    • 4644222500 scopus 로고    scopus 로고
    • A nucleotide binding motif in hepatitis C virus (HCV) NS4B mediates HCV RNA replication
    • Einav S, Elazar M, Danieli T, Glenn JS (2004) A nucleotide binding motif in hepatitis C virus (HCV) NS4B mediates HCV RNA replication. J Virol 78:11288-112955
    • (2004) J Virol , vol.78 , pp. 11288-112955
    • Einav, S.1    Elazar, M.2    Danieli, T.3    Glenn, J.S.4
  • 35
    • 63149086110 scopus 로고    scopus 로고
    • Internal initiation stimulates production of p8 minicore, a member of a newly discovered family of hepatitis C virus core protein isoforms
    • Eng FJ, Walewski JL, Klepper AL, Fishman SL, Desai SM, McMullan LK, Evans MJ, Rice CM, Branch AD (2009) Internal initiation stimulates production of p8 minicore, a member of a newly discovered family of hepatitis C virus core protein isoforms. J Virol 83:3104-31144
    • (2009) J Virol , vol.83 , pp. 3104-31144
    • Eng, F.J.1    Walewski, J.L.2    Klepper, A.L.3    Fishman, S.L.4    Desai, S.M.5    McMullan, L.K.6    Evans, M.J.7    Rice, C.M.8    Branch, A.D.9
  • 37
    • 4444377616 scopus 로고    scopus 로고
    • Phosphorylation of hepatitis C virus nonstructural protein 5A modulates its protein interactions and viral RNA replication
    • Evans MJ, Rice CM, Goff SP (2004) Phosphorylation of hepatitis C virus nonstructural protein 5A modulates its protein interactions and viral RNA replication. Proc Natl Acad Sci USA 101:13038-130433
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 13038-130433
    • Evans, M.J.1    Rice, C.M.2    Goff, S.P.3
  • 40
    • 0345144016 scopus 로고    scopus 로고
    • Identification of the hepatitis C virus RNA replication complex in Huh-7 cells harboring subgenomic replicons
    • Gosert R, Egger D, Lohmann V, Bartenschlager R, Blum HE, Bienz K, Moradpour D (2003) Identification of the hepatitis C virus RNA replication complex in Huh-7 cells harboring subgenomic replicons. J Virol 77:5487-54922
    • (2003) J Virol , vol.77 , pp. 5487-54922
    • Gosert, R.1    Egger, D.2    Lohmann, V.3    Bartenschlager, R.4    Blum, H.E.5    Bienz, K.6    Moradpour, D.7
  • 43
    • 70350330475 scopus 로고    scopus 로고
    • An amphipathic α-helix at the C terminus of NS4B mediates membrane association
    • Gouttenoire J, Montserret R, Kennel A, Penin F, Moradpour D (2009b) An amphipathic α-helix at the C terminus of NS4B mediates membrane association. J Virol 51:11378-113844
    • (2009) J Virol , vol.51 , pp. 11378-113844
    • Gouttenoire, J.1    Montserret, R.2    Kennel, A.3    Penin, F.4    Moradpour, D.5
  • 44
    • 77649175920 scopus 로고    scopus 로고
    • Hepatitis C virus nonstructural protein 4B: A journey into unexplored territory
    • Gouttenoire J, Penin F, Moradpour D (2010a) Hepatitis C virus nonstructural protein 4B: a journey into unexplored territory. Rev Med Virol 20:117-1299
    • (2010) Rev Med Virol , vol.20 , pp. 117-1299
    • Gouttenoire, J.1    Penin, F.2    Moradpour, D.3
  • 45
    • 78649398569 scopus 로고    scopus 로고
    • Amphipathic α-helix AH2 is a major determinant for the oligomerization of hepatitis C virus nonstructural protein 4B
    • Gouttenoire J, Roingeard P, Penin F, Moradpour D (2010b) Amphipathic α-helix AH2 is a major determinant for the oligomerization of hepatitis C virus nonstructural protein 4B. J Virol 84:12529-125377
    • (2010) J Virol , vol.84 , pp. 12529-125377
    • Gouttenoire, J.1    Roingeard, P.2    Penin, F.3    Moradpour, D.4
  • 46
    • 76249111702 scopus 로고    scopus 로고
    • Three conformational snapshots of the hepatitis C virus NS3 helicase reveal a ratchet translocation mechanism
    • Gu M, Rice CM (2010) Three conformational snapshots of the hepatitis C virus NS3 helicase reveal a ratchet translocation mechanism. Proc Natl Acad Sci USA 107:521-5288
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 521-5288
    • Gu, M.1    Rice, C.M.2
  • 47
    • 79958830099 scopus 로고    scopus 로고
    • Hepatitis C virus resistance to protease inhibitors
    • Halfon P, Locarnini S (2011) Hepatitis C virus resistance to protease inhibitors. J Hepatol 55:192-2066
    • (2011) J Hepatol , vol.55 , pp. 192-2066
    • Halfon, P.1    Locarnini, S.2
  • 50
    • 84855272666 scopus 로고    scopus 로고
    • Increasing rate of cleavage at boundary between non-structural proteins 4B and 5A inhibits replication of hepatitis C virus
    • Herod MR, Jones DM, McLauchlan J, McCormick CJ (2012) Increasing rate of cleavage at boundary between non-structural proteins 4B and 5A inhibits replication of hepatitis C virus. J Biol Chem 287:568-5800
    • (2012) J Biol Chem , vol.287 , pp. 568-5800
    • Herod, M.R.1    Jones, D.M.2    McLauchlan, J.3    McCormick, C.J.4
  • 51
    • 80052281413 scopus 로고    scopus 로고
    • Mitochondrial-associated endoplasmic reticulum membranes (MAM) form innate immune synapses and are targeted by hepatitis C virus
    • Horner SM, Liu HM, Park HS, Briley J, Gale Jr. M. (2011) Mitochondrial-associated endoplasmic reticulum membranes (MAM) form innate immune synapses and are targeted by hepatitis C virus. Proc Natl Acad Sci USA 108:14590-145955
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 14590-145955
    • Horner, S.M.1    Liu, H.M.2    Park, H.S.3    Briley, J.4    Gale Jr., M.5
  • 52
    • 34249664478 scopus 로고    scopus 로고
    • Phosphorylation of hepatitis C virus NS5A nonstructural protein: A new paradigm for phosphorylation-dependent viral RNA replication?
    • Huang Y, Staschke K, De Francesco R, Tan SL (2007) Phosphorylation of hepatitis C virus NS5A nonstructural protein: a new paradigm for phosphorylation-dependent viral RNA replication? Virology 364:1-99
    • (2007) Virology , vol.364 , pp. 1-99
    • Huang, Y.1    Staschke, K.2    De Francesco, R.3    Tan, S.L.4
  • 53
    • 78649430973 scopus 로고    scopus 로고
    • Hepatitis C virus nonstructural protein 5A: Biochemical characterization of a novel structural class of RNA-binding proteins
    • Hwang J, Huang L, Cordek DG, Vaughan R, Reynolds SL, Kihara G, Raney KD, Kao CC, Cameron CE (2010) Hepatitis C virus nonstructural protein 5A: biochemical characterization of a novel structural class of RNA-binding proteins. J Virol 84:12480-124911
    • (2010) J Virol , vol.84 , pp. 12480-124911
    • Hwang, J.1    Huang, L.2    Cordek, D.G.3    Vaughan, R.4    Reynolds, S.L.5    Kihara, G.6    Raney, K.D.7    Kao, C.C.8    Cameron, C.E.9
  • 56
    • 78651252353 scopus 로고    scopus 로고
    • Structural and functional studies of nonstructural protein 2 of the hepatitis C virus reveal its key role as organizer of virion assembly
    • Jirasko V, Montserret R, Lee JY, Gouttenoire J, Moradpour D, Penin F, Bartenschlager R (2010) Structural and functional studies of nonstructural protein 2 of the hepatitis C virus reveal its key role as organizer of virion assembly. PLoS Pathog 6:e10012333
    • (2010) PLoS Pathog , vol.6
    • Jirasko, V.1    Montserret, R.2    Lee, J.Y.3    Gouttenoire, J.4    Moradpour, D.5    Penin, F.6    Bartenschlager, R.7
  • 58
    • 60049083503 scopus 로고    scopus 로고
    • The hepatitis C virus NS4B protein can trans-complement viral RNA replication and modulates production of infectious virus
    • Jones DM, Patel AH, Targett-Adams P, McLauchlan J (2009) The hepatitis C virus NS4B protein can trans-complement viral RNA replication and modulates production of infectious virus. J Virol 83:2163-21777
    • (2009) J Virol , vol.83 , pp. 2163-21777
    • Jones, D.M.1    Patel, A.H.2    Targett-Adams, P.3    McLauchlan, J.4
  • 62
    • 31344432402 scopus 로고    scopus 로고
    • Virus membrane-fusion proteins: More than one way to make a hairpin
    • Kielian M, Rey FA (2006) Virus membrane-fusion proteins: more than one way to make a hairpin. Nat Rev Microbiol 4:67-766
    • (2006) Nat Rev Microbiol , vol.4 , pp. 67-766
    • Kielian, M.1    Rey, F.A.2
  • 63
    • 80052066409 scopus 로고    scopus 로고
    • Regulation of the production of infectious genotype 1a hepatitis C virus by NS5A domain III
    • Kim S, Welsch C, Yi M, Lemon SM (2011) Regulation of the production of infectious genotype 1a hepatitis C virus by NS5A domain III. J Virol 85:6645-66566
    • (2011) J Virol , vol.85 , pp. 6645-66566
    • Kim, S.1    Welsch, C.2    Yi, M.3    Lemon, S.M.4
  • 64
    • 75449084143 scopus 로고    scopus 로고
    • Genetic analysis of the carboxy-terminal region of the hepatitis C virus core protein
    • Kopp M, Murray CL, Jones CT, Rice CM (2010) Genetic analysis of the carboxy-terminal region of the hepatitis C virus core protein. J Virol 84:1666-16733
    • (2010) J Virol , vol.84 , pp. 1666-16733
    • Kopp, M.1    Murray, C.L.2    Jones, C.T.3    Rice, C.M.4
  • 66
    • 77956041471 scopus 로고    scopus 로고
    • A disulfide-bonded dimer of the core protein of hepatitis C virus is important for virus-like particle production
    • Kushima Y, Wakita T, Hijikata M (2010) A disulfide-bonded dimer of the core protein of hepatitis C virus is important for virus-like particle production. J Virol 84:9118-91277
    • (2010) J Virol , vol.84 , pp. 9118-91277
    • Kushima, Y.1    Wakita, T.2    Hijikata, M.3
  • 67
    • 0032876683 scopus 로고    scopus 로고
    • Crystal structure of the RNA-dependent RNA polymerase from hepatitis C virus reveals a fully encircled active site
    • Lesburg CA, Cable MB, Ferrari E, Hong Z, Mannarino AF, Weber PC (1999) Crystal structure of the RNA-dependent RNA polymerase from hepatitis C virus reveals a fully encircled active site. Nat Struct Biol 6:937-9433
    • (1999) Nat Struct Biol , vol.6 , pp. 937-9433
    • Lesburg, C.A.1    Cable, M.B.2    Ferrari, E.3    Hong, Z.4    Mannarino, A.F.5    Weber, P.C.6
  • 69
    • 35348891616 scopus 로고    scopus 로고
    • Domain 2 of nonstructural protein 5A (NS5A) of hepatitis C virus is natively unfolded
    • Liang Y, Ye H, Kang CB, Yoon HS (2007) Domain 2 of nonstructural protein 5A (NS5A) of hepatitis C virus is natively unfolded. Biochemistry 46:11550-115588
    • (2007) Biochemistry , vol.46 , pp. 11550-115588
    • Liang, Y.1    Ye, H.2    Kang, C.B.3    Yoon, H.S.4
  • 70
    • 79953221885 scopus 로고    scopus 로고
    • Hepatitis C virus NS5A protein interacts with phosphatidylinositol 4-kinase type III alpha and regulates viral propagation
    • Lim YS, Hwang SB (2011) Hepatitis C virus NS5A protein interacts with phosphatidylinositol 4-kinase type III alpha and regulates viral propagation. J Biol Chem 286:11290-112988
    • (2011) J Biol Chem , vol.286 , pp. 11290-112988
    • Lim, Y.S.1    Hwang, S.B.2
  • 71
    • 34548188701 scopus 로고    scopus 로고
    • The C-terminus of hepatitis C virus NS4A encodes an electrostatic switch that regulates NS5A hyperphosphorylation and viral replication
    • Lindenbach BD, Pragai BM, Montserret R, Beran RK, Pyle AM, Penin F, Rice CM (2007) The C-terminus of hepatitis C virus NS4A encodes an electrostatic switch that regulates NS5A hyperphosphorylation and viral replication. J Virol 81:8905-89188
    • (2007) J Virol , vol.81 , pp. 8905-89188
    • Lindenbach, B.D.1    Pragai, B.M.2    Montserret, R.3    Beran, R.K.4    Pyle, A.M.5    Penin, F.6    Rice, C.M.7
  • 72
    • 84885695869 scopus 로고    scopus 로고
    • Flaviviridae: The viruses and their replication
    • Knipe DM et al. (eds) Lippincott Williams and Wilkins, New York (in press)
    • Lindenbach BD, Murray CL, Thiel H-J, Rice CM (2013) Flaviviridae: the viruses and their replication. In: Knipe DM et al. (eds) Fields Virology. Lippincott Williams and Wilkins, New York (in press)
    • (2013) Fields Virology
    • Lindenbach, B.D.1    Murray, C.L.2    Thiel, H.-J.3    Rice, C.M.4
  • 73
    • 67449093865 scopus 로고    scopus 로고
    • Critical role of cyclophilin A and its prolyl-peptidyl isomerase activity in the structure and function of the hepatitis C virus replication complex
    • Liu Z, Yang F, Robotham JM, Tang H (2009) Critical role of cyclophilin A and its prolyl-peptidyl isomerase activity in the structure and function of the hepatitis C virus replication complex. J Virol 83:6554-65655
    • (2009) J Virol , vol.83 , pp. 6554-65655
    • Liu, Z.1    Yang, F.2    Robotham, J.M.3    Tang, H.4
  • 74
    • 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, Korner F, Herian U, Bartenschlager R (1997) Biochemical properties of hepatitis C virus NS5B RNA-dependent RNA polymerase and identification of amino acid sequence motifs essential for enzymatic activity. J Virol 71:8416-84288
    • (1997) J Virol , vol.71 , pp. 8416-84288
    • Lohmann, V.1    Korner, F.2    Herian, U.3    Bartenschlager, R.4
  • 75
    • 33747452685 scopus 로고    scopus 로고
    • Structure of the catalytic domain of the hepatitis C virus NS2-3 protease
    • Lorenz IC, Marcotrigiano J, Dentzer TG, Rice CM (2006) Structure of the catalytic domain of the hepatitis C virus NS2-3 protease. Nature 442:831-8355
    • (2006) Nature , vol.442 , pp. 831-8355
    • Lorenz, I.C.1    Marcotrigiano, J.2    Dentzer, T.G.3    Rice, C.M.4
  • 76
    • 66149115122 scopus 로고    scopus 로고
    • Crystal structure of a novel dimeric form of NS5A domain i protein from hepatitis C virus
    • Love RA, Brodsky O, Hickey MJ, Wells PA, Cronin CN (2009) Crystal structure of a novel dimeric form of NS5A domain I protein from hepatitis C virus. J Virol 83:4395-44033
    • (2009) J Virol , vol.83 , pp. 4395-44033
    • Love, R.A.1    Brodsky, O.2    Hickey, M.J.3    Wells, P.A.4    Cronin, C.N.5
  • 78
    • 0344373790 scopus 로고    scopus 로고
    • Topology of the membraneassociated hepatitis C virus protein NS4B
    • Lundin M, Monne M, Widell A, Von Heijne G, Persson MA (2003) Topology of the membraneassociated hepatitis C virus protein NS4B. J Virol 77:5428-54388
    • (2003) J Virol , vol.77 , pp. 5428-54388
    • Lundin, M.1    Monne, M.2    Widell, A.3    Von Heijne, G.4    Persson, M.A.5
  • 79
    • 33750249579 scopus 로고    scopus 로고
    • Dual topology of the processed hepatitis C virus protein NS4B is influenced by the NS5A protein
    • Lundin M, Lindstrom H, Gronwall C, Persson MA (2006) Dual topology of the processed hepatitis C virus protein NS4B is influenced by the NS5A protein. J Gen Virol 87:3263-32722
    • (2006) J Gen Virol , vol.87 , pp. 3263-32722
    • Lundin, M.1    Lindstrom, H.2    Gronwall, C.3    Persson, M.A.4
  • 80
    • 77953306294 scopus 로고    scopus 로고
    • Flexibility between the protease and helicase domains of the dengue virus NS3 protein conferred by the linker region and its functional implications
    • Luo D, Wei N, Doan DN, Paradkar PN, Chong Y, Davidson AD, Kotaka M, Lescar J, Vasudevan SG (2010) Flexibility between the protease and helicase domains of the dengue virus NS3 protein conferred by the linker region and its functional implications. J Biol Chem 285:18817-188277
    • (2010) J Biol Chem , vol.285 , pp. 18817-188277
    • Luo, D.1    Wei, N.2    Doan, D.N.3    Paradkar, P.N.4    Chong, Y.5    Davidson, A.D.6    Kotaka, M.7    Lescar, J.8    Vasudevan, S.G.9
  • 81
    • 47749092840 scopus 로고    scopus 로고
    • NS3 helicase domains involved in infectious intracellular hepatitis C virus particle assembly
    • Ma Y, Yates J, Liang Y, Lemon SM, Yi M (2008) NS3 helicase domains involved in infectious intracellular hepatitis C virus particle assembly. J Virol 82:7624-76399
    • (2008) J Virol , vol.82 , pp. 7624-76399
    • Ma, Y.1    Yates, J.2    Liang, Y.3    Lemon, S.M.4    Yi, M.5
  • 82
    • 78650062692 scopus 로고    scopus 로고
    • Hepatitis C virus NS2 protein serves as a scaffold for virus assembly by interacting with both structural and nonstructural proteins
    • Ma Y, Anantpadma M, Timpe JM, Shanmugam S, Singh SM, Lemon SM, Yi M (2011) Hepatitis C virus NS2 protein serves as a scaffold for virus assembly by interacting with both structural and nonstructural proteins. J Virol 85:86-977
    • (2011) J Virol , vol.85 , pp. 86-977
    • Ma, Y.1    Anantpadma, M.2    Timpe, J.M.3    Shanmugam, S.4    Singh, S.M.5    Lemon, S.M.6    Yi, M.7
  • 83
    • 4544336360 scopus 로고    scopus 로고
    • Hepatitis C virus NS5A: Tales of a promiscuous protein
    • Macdonald A, Harris M (2004) Hepatitis C virus NS5A: tales of a promiscuous protein. J Gen Virol 85:2485-25022
    • (2004) J Gen Virol , vol.85 , pp. 2485-25022
    • Macdonald, A.1    Harris, M.2
  • 85
    • 78651244199 scopus 로고    scopus 로고
    • The variable regions of hepatitis C virus glycoprotein E2 have an essential structural role in glycoprotein assembly and virion infectivity
    • McCaffrey K, Gouklani H, Boo I, Poumbourios P, Drummer HE (2011) The variable regions of hepatitis C virus glycoprotein E2 have an essential structural role in glycoprotein assembly and virion infectivity. J Gen Virol 92:112-1211
    • (2011) J Gen Virol , vol.92 , pp. 112-1211
    • McCaffrey, K.1    Gouklani, H.2    Boo, I.3    Poumbourios, P.4    Drummer, H.E.5
  • 86
    • 0036683052 scopus 로고    scopus 로고
    • Intramembrane proteolysis promotes trafficking of hepatitis C virus core protein to lipid droplets
    • McLauchlan J, Lemberg MK, Hope G, Martoglio B (2002) Intramembrane proteolysis promotes trafficking of hepatitis C virus core protein to lipid droplets. EMBO J 21:3980-39888
    • (2002) EMBO J , vol.21 , pp. 3980-39888
    • McLauchlan, J.1    Lemberg, M.K.2    Hope, G.3    Martoglio, B.4
  • 87
    • 27144440476 scopus 로고    scopus 로고
    • Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus
    • Meylan E, Curran J, Hofmann K, Moradpour D, Binder M, Bartenschlager R, Tschopp J (2005) Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus. Nature 437:1167-11722
    • (2005) Nature , vol.437 , pp. 1167-11722
    • Meylan, E.1    Curran, J.2    Hofmann, K.3    Moradpour, D.4    Binder, M.5    Bartenschlager, R.6    Tschopp, J.7
  • 88
    • 42349086670 scopus 로고    scopus 로고
    • Modification of intracellular membrane structures for virus replication
    • Miller S, Krijnse-Locker J (2008) Modification of intracellular membrane structures for virus replication. Nat Rev Microbiol 6:363-3744
    • (2008) Nat Rev Microbiol , vol.6 , pp. 363-3744
    • Miller, S.1    Krijnse-Locker, J.2
  • 89
    • 0346118919 scopus 로고    scopus 로고
    • Hepatitis C virus non-structural proteins in the probable membranous compartment function in viral RNA replication
    • Miyanari Y, Hijikata M, Yamaji M, Hosaka M, Takahashi H, Shimotohno K (2003) Hepatitis C virus non-structural proteins in the probable membranous compartment function in viral RNA replication. J Biol Chem 278:50301-503088
    • (2003) J Biol Chem , vol.278 , pp. 50301-503088
    • Miyanari, Y.1    Hijikata, M.2    Yamaji, M.3    Hosaka, M.4    Takahashi, H.5    Shimotohno, K.6
  • 93
    • 3142764760 scopus 로고    scopus 로고
    • Insertion of green fluorescent protein into nonstructural protein 5A allows direct visualization of functional hepatitis C virus replication complexes
    • Moradpour D, Evans MJ, Gosert R, Yuan ZH, Blum HE, Goff SP, Lindenbach BD, Rice CM (2004b) Insertion of green fluorescent protein into nonstructural protein 5A allows direct visualization of functional hepatitis C virus replication complexes. J Virol 78:7400-74099
    • (2004) J Virol , vol.78 , pp. 7400-74099
    • Moradpour, D.1    Evans, M.J.2    Gosert, R.3    Zh, Y.4    Blum, H.E.5    Goff, S.P.6    Lindenbach, B.D.7    Rice, C.M.8
  • 94
    • 24144438257 scopus 로고    scopus 로고
    • Function follows form: The structure of the N-terminal domain of HCV NS5A
    • Moradpour D, Brass V, Penin F (2005) Function follows form: the structure of the N-terminal domain of HCV NS5A. Hepatology 42:732-7355
    • (2005) Hepatology , vol.42 , pp. 732-7355
    • Moradpour, D.1    Brass, V.2    Penin, F.3
  • 98
    • 49649102821 scopus 로고    scopus 로고
    • Architects of assembly: Roles of Flaviviridae non-structural proteins in virion morphogenesis
    • Murray CL, Jones CT, Rice CM (2008) Architects of assembly: roles of Flaviviridae non-structural proteins in virion morphogenesis. Nat Rev Microbiol 6:699-7088
    • (2008) Nat Rev Microbiol , vol.6 , pp. 699-7088
    • Murray, C.L.1    Jones, C.T.2    Rice, C.M.3
  • 99
    • 84858232188 scopus 로고    scopus 로고
    • Nature outlook: Hepatitis C
    • Nature Outlook: Hepatitis C (2011). Nature 474:S1-S211
    • (2011) Nature , vol.474
  • 100
    • 8644290077 scopus 로고    scopus 로고
    • Reduction of hepatitis C virus NS5A hyperphosphorylation by selective inhibition of cellular kinases activates viral RNA replication in cell culture
    • Neddermann P, Quintavalle M, Di Pietro C, Clementi A, Cerretani M, Altamura S, Bartholomew L, De Francesco R (2004) Reduction of hepatitis C virus NS5A hyperphosphorylation by selective inhibition of cellular kinases activates viral RNA replication in cell culture. J Virol 78:13306-133144
    • (2004) J Virol , vol.78 , pp. 13306-133144
    • Neddermann, P.1    Quintavalle, M.2    Di Pietro, C.3    Clementi, A.4    Cerretani, M.5    Altamura, S.6    Bartholomew, L.7    De Francesco, R.8
  • 101
    • 84864391185 scopus 로고    scopus 로고
    • Structural analysis of hepatitis C virus core-E1 signal peptide and requirements for cleavage of the genotype 3a signal sequence by signal peptide peptidase
    • Oehler V, Filipe A, Montserret R, da Costa D, Brown G, Penin F, McLauchlan J (2012) Structural analysis of hepatitis C virus core-E1 signal peptide and requirements for cleavage of the genotype 3a signal sequence by signal peptide peptidase. J Virol 86:7818-78288
    • (2012) J Virol , vol.86 , pp. 7818-78288
    • Oehler, V.1    Filipe, A.2    Montserret, R.3    Da Costa, D.4    Brown, G.5    Penin, F.6    McLauchlan, J.7
  • 102
    • 50149086906 scopus 로고    scopus 로고
    • Intramembrane processing by signal peptide peptidase regulates the membrane localization of hepatitis C virus core protein and viral propagation
    • Okamoto K, Mori Y, Komoda Y, Okamoto T, Okochi M, Takeda M, Suzuki T, Moriishi K, Matsuura Y (2008) Intramembrane processing by signal peptide peptidase regulates the membrane localization of hepatitis C virus core protein and viral propagation. J Virol 82:8349-83611
    • (2008) J Virol , vol.82 , pp. 8349-83611
    • Okamoto, K.1    Mori, Y.2    Komoda, Y.3    Okamoto, T.4    Okochi, M.5    Takeda, M.6    Suzuki, T.7    Moriishi, K.8    Matsuura, Y.9
  • 103
    • 79960406328 scopus 로고    scopus 로고
    • NS4B self-interaction through conserved C-terminal elements is required for the establishment of functional hepatitis C virus replication complexes
    • Paul D, Romero-Brey I, Gouttenoire J, Stoitsova S, Krijnse-Locker J, Moradpour D, Bartenschlager R (2011) NS4B self-interaction through conserved C-terminal elements is required for the establishment of functional hepatitis C virus replication complexes. J Virol 85:6963-69766
    • (2011) J Virol , vol.85 , pp. 6963-69766
    • Paul, D.1    Romero-Brey, I.2    Gouttenoire, J.3    Stoitsova, S.4    Krijnse-Locker, J.5    Moradpour, D.6    Bartenschlager, R.7
  • 104
    • 0035000935 scopus 로고    scopus 로고
    • Conservation of the conformation and positive charges of hepatitis C virus E2 envelope glycoprotein hypervariable region 1 points to a role in cell attachment
    • Penin F, Combet C, Germanidis G, Frainais PO, Deleage G, Pawlotsky JM (2001) Conservation of the conformation and positive charges of hepatitis C virus E2 envelope glycoprotein hypervariable region 1 points to a role in cell attachment. J Virol 75:5703-57100
    • (2001) J Virol , vol.75 , pp. 5703-57100
    • Penin, F.1    Combet, C.2    Germanidis, G.3    Frainais, P.O.4    Deleage, G.5    Pawlotsky, J.M.6
  • 106
    • 78651399012 scopus 로고    scopus 로고
    • The acidic domain of hepatitis C virus NS4A contributes to RNA replication and virus particle assembly
    • Phan T, Kohlway A, Dimberu P, Pyle AM, Lindenbach BD (2011) The acidic domain of hepatitis C virus NS4A contributes to RNA replication and virus particle assembly. J Virol 85:1193-12044
    • (2011) J Virol , vol.85 , pp. 1193-12044
    • Phan, T.1    Kohlway, A.2    Dimberu, P.3    Pyle, A.M.4    Lindenbach, B.D.5
  • 107
    • 0035148546 scopus 로고    scopus 로고
    • Characterization of cell lines carrying self-replicating hepatitis C virus RNAs
    • Pietschmann T, Lohmann V, Rutter G, Kurpanek K, Bartenschlager R (2001) Characterization of cell lines carrying self-replicating hepatitis C virus RNAs. J Virol 75:1252-12644
    • (2001) J Virol , vol.75 , pp. 1252-12644
    • Pietschmann, T.1    Lohmann, V.2    Rutter, G.3    Kurpanek, K.4    Bartenschlager, R.5
  • 110
    • 27144513392 scopus 로고    scopus 로고
    • Quantitative analysis of the hepatitis C virus replication complex
    • Quinkert D, Bartenschlager R, Lohmann V (2005) Quantitative analysis of the hepatitis C virus replication complex. J Virol 79:13594-136055
    • (2005) J Virol , vol.79 , pp. 13594-136055
    • Quinkert, D.1    Bartenschlager, R.2    Lohmann, V.3
  • 111
    • 34247117377 scopus 로고    scopus 로고
    • Hepatitis C virus NS5A is a direct substrate of casein kinase I-alpha, a cellular kinase identified by inhibitor affinity chromatography using specific NS5A hyperphosphorylation inhibitors
    • Quintavalle M, Sambucini S, Summa V, Orsatti L, Talamo F, De Francesco R, Neddermann P (2007) Hepatitis C virus NS5A is a direct substrate of casein kinase I-alpha, a cellular kinase identified by inhibitor affinity chromatography using specific NS5A hyperphosphorylation inhibitors. J Biol Chem 282:5536-55444
    • (2007) J Biol Chem , vol.282 , pp. 5536-55444
    • Quintavalle, M.1    Sambucini, S.2    Summa, V.3    Orsatti, L.4    Talamo, F.5    De Francesco, R.6    Neddermann, P.7
  • 112
    • 79955647061 scopus 로고    scopus 로고
    • New opportunities in anti-hepatitis C virus drug discovery: Targeting NS4B
    • Rai R, Deval J (2011) New opportunities in anti-hepatitis C virus drug discovery: targeting NS4B. Antiviral Res 90:93-1011
    • (2011) Antiviral Res , vol.90 , pp. 93-1011
    • Rai, R.1    Deval, J.2
  • 113
    • 77954931489 scopus 로고    scopus 로고
    • Hepatitis C virus non-structural protein 3: A multifunctional antiviral target
    • Raney KD, Sharma SD, Moustafa IM, Cameron CE (2010) Hepatitis C virus non-structural protein 3: a multifunctional antiviral target. J Biol Chem 285:22725-227311
    • (2010) J Biol Chem , vol.285 , pp. 22725-227311
    • Raney, K.D.1    Sharma, S.D.2    Moustafa, I.M.3    Cameron, C.E.4
  • 114
    • 0033600812 scopus 로고    scopus 로고
    • Identification of the major phosphorylation site of the hepatitis C virus H strain NS5A protein as serine 2321
    • Reed K, Rice CM (1999) Identification of the major phosphorylation site of the hepatitis C virus H strain NS5A protein as serine 2321. J Biol Chem 274:28011-280188
    • (1999) J Biol Chem , vol.274 , pp. 28011-280188
    • Reed, K.1    Rice, C.M.2
  • 116
    • 0028233530 scopus 로고
    • Biosynthesis and biochemical properties of the hepatitis C virus core protein
    • Santolini E, Migliaccio G, La Monica N (1994) Biosynthesis and biochemical properties of the hepatitis C virus core protein. J Virol 68:3631-36411
    • (1994) J Virol , vol.68 , pp. 3631-36411
    • Santolini, E.1    Migliaccio, G.2    La Monica, N.3
  • 117
  • 118
  • 119
    • 65249157102 scopus 로고    scopus 로고
    • Hepatitis C virus NS2 is a protease stimulated by cofactor domains in NS3
    • Schregel V, Jacobi S, Penin F, Tautz N (2009) Hepatitis C virus NS2 is a protease stimulated by cofactor domains in NS3. Proc Natl Acad Sci USA 106:5342-53477
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 5342-53477
    • Schregel, V.1    Jacobi, S.2    Penin, F.3    Tautz, N.4
  • 120
    • 37549005607 scopus 로고    scopus 로고
    • The lipid droplet binding domain of hepatitis C virus core protein is a major determinant for efficient virus assembly
    • Shavinskaya A, Boulant S, Penin F, McLauchlan J, Bartenschlager R (2007) The lipid droplet binding domain of hepatitis C virus core protein is a major determinant for efficient virus assembly. J Biol Chem 282:37158-371699
    • (2007) J Biol Chem , vol.282 , pp. 37158-371699
    • Shavinskaya, A.1    Boulant, S.2    Penin, F.3    McLauchlan, J.4    Bartenschlager, R.5
  • 122
    • 78951472458 scopus 로고    scopus 로고
    • Hepatitis C virus NS2 coordinates virus particle assembly through physical interactions with the E1-E2 glycoprotein and NS3-NS4A enzyme complexes
    • Stapleford KA, Lindenbach BD (2011) Hepatitis C virus NS2 coordinates virus particle assembly through physical interactions with the E1-E2 glycoprotein and NS3-NS4A enzyme complexes. J Virol 85:1706-17177
    • (2011) J Virol , vol.85 , pp. 1706-17177
    • Stapleford, K.A.1    Lindenbach, B.D.2
  • 123
    • 79952131523 scopus 로고    scopus 로고
    • Hepatitis C virus p7-A viroporin crucial for virus assembly and an emerging target for antiviral therapy
    • Steinmann E, Pietschmann T (2010) Hepatitis C virus p7-a viroporin crucial for virus assembly and an emerging target for antiviral therapy. Viruses 2:2078-20955
    • (2010) Viruses , vol.2 , pp. 2078-20955
    • Steinmann, E.1    Pietschmann, T.2
  • 125
    • 19644393931 scopus 로고    scopus 로고
    • Structure of the zinc-binding domain of an essential replicase component of hepatitis C virus reveals a novel fold
    • Tellinghuisen TL, Marcotrigiano J, Rice CM (2005) Structure of the zinc-binding domain of an essential replicase component of hepatitis C virus reveals a novel fold. Nature 435:375-3799
    • (2005) Nature , vol.435 , pp. 375-3799
    • Tellinghuisen, T.L.1    Marcotrigiano, J.2    Rice, C.M.3
  • 126
    • 42949145532 scopus 로고    scopus 로고
    • Regulation of hepatitis C virion production via phosphorylation of the NS5A protein
    • Tellinghuisen TL, Foss KL, Treadaway J (2008) Regulation of hepatitis C virion production via phosphorylation of the NS5A protein. PLoS Pathog 4:e10000322
    • (2008) PLoS Pathog , vol.4
    • Tellinghuisen, T.L.1    Foss, K.L.2    Treadaway, J.3
  • 127
    • 61449111949 scopus 로고    scopus 로고
    • Biochemical characterization of recombinant hepatitis C virus nonstructural protein 4B: Evidence for ATP/GTP hydrolysis and adenylate kinase activity
    • Thompson AA, Zou A, Yan J, Duggal R, Hao W, Molina D, Cronin CN, Wells PA (2009) Biochemical characterization of recombinant hepatitis C virus nonstructural protein 4B: evidence for ATP/GTP hydrolysis and adenylate kinase activity. Biochemistry 48:906-9166
    • (2009) Biochemistry , vol.48 , pp. 906-9166
    • Thompson, A.A.1    Zou, A.2    Yan, J.3    Duggal, R.4    Hao, W.5    Molina, D.6    Cronin, C.N.7    Wells, P.A.8
  • 129
    • 77956832815 scopus 로고    scopus 로고
    • Characterization of the envelope glycoproteins associated with infectious hepatitis C virus
    • Vieyres G, Thomas X, Descamps V, Duverlie G, Patel AH, Dubuisson J (2010) Characterization of the envelope glycoproteins associated with infectious hepatitis C virus. J Virol 84:10159-101688
    • (2010) J Virol , vol.84 , pp. 10159-101688
    • Vieyres, G.1    Thomas, X.2    Descamps, V.3    Duverlie, G.4    Patel, A.H.5    Dubuisson, J.6
  • 130
    • 4344583055 scopus 로고    scopus 로고
    • Functional hepatitis C virus envelope glycoproteins
    • Voisset C, Dubuisson J (2004) Functional hepatitis C virus envelope glycoproteins. Biol Cell 96:413-4200
    • (2004) Biol Cell , vol.96 , pp. 413-4200
    • Voisset, C.1    Dubuisson, J.2
  • 132
    • 0242456017 scopus 로고    scopus 로고
    • Subcellular localization, stability and trans-cleavage competence of the hepatitis C virus NS3-NS4A complex expressed in tetracycline-regulated cell lines
    • Wolk B, Sansonno D, Krausslich H-G, Dammacco F, Rice CM, Blum HE, Moradpour D (2000) Subcellular localization, stability and trans-cleavage competence of the hepatitis C virus NS3-NS4A complex expressed in tetracycline-regulated cell lines. J Virol 74:2293-23044
    • (2000) J Virol , vol.74 , pp. 2293-23044
    • Wolk, B.1    Sansonno, D.2    Krausslich, H.-G.3    Dammacco, F.4    Rice, C.M.5    Blum, H.E.6    Moradpour, D.7
  • 133
    • 78149341400 scopus 로고    scopus 로고
    • Intracellular proton conductance of the hepatitis C virus p7 protein and its contribution to infectious virus production
    • Wozniak AL, Griffin S, Rowlands D, Harris M, Yi M, Lemon SM, Weinman SA (2010) Intracellular proton conductance of the hepatitis C virus p7 protein and its contribution to infectious virus production. PLoS Pathog 6:e10010877
    • (2010) PLoS Pathog , vol.6
    • Wozniak, A.L.1    Griffin, S.2    Rowlands, D.3    Harris, M.4    Yi, M.5    Lemon, S.M.6    Weinman, S.A.7
  • 134
    • 0033571623 scopus 로고    scopus 로고
    • Molecular views of viral polyprotein processing revealed by the crystal structure of the hepatitis C virus bifunctional protease- helicase
    • Yao N, Reichert P, Taremi SS, Prosise WW, Weber PC (1999) Molecular views of viral polyprotein processing revealed by the crystal structure of the hepatitis C virus bifunctional protease- helicase. Structure Fold Des 7:1353-13633
    • (1999) Structure Fold des , vol.7 , pp. 1353-13633
    • Yao, N.1    Reichert, P.2    Taremi, S.S.3    Prosise, W.W.4    Weber, P.C.5
  • 135
    • 33744921881 scopus 로고    scopus 로고
    • Palmitoylation and polymerization of hepatitis C virus NS4B protein
    • Yu GY, Lee KJ, Gao L, Lai MM (2006) Palmitoylation and polymerization of hepatitis C virus NS4B protein. J Virol 80:6013-60233
    • (2006) J Virol , vol.80 , pp. 6013-60233
    • Yu, G.Y.1    Lee, K.J.2    Gao, L.3    Lai, M.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.