메뉴 건너뛰기




Volumn 214, Issue , 1996, Pages 297-337

Hepatitis B virus morphogenesis

Author keywords

[No Author keywords available]

Indexed keywords

CORE PROTEIN; VITRONECTIN;

EID: 0030391205     PISSN: 0070217X     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-3-642-80145-7_10     Document Type: Review
Times cited : (68)

References (170)
  • 1
    • 0018835442 scopus 로고
    • Protein kinase activity in hepatitis B virus
    • Albin C, Robinson WS (1980) Protein kinase activity in hepatitis B virus. J Virol 34: 297-302
    • (1980) J Virol , vol.34 , pp. 297-302
    • Albin, C.1    Robinson, W.S.2
  • 2
    • 0028100649 scopus 로고
    • Is plasma membrane lipid composition defined in the exocytic or endocytic pathway?
    • Allan D, Kallen KJ (1994) Is plasma membrane lipid composition defined in the exocytic or endocytic pathway? Trends Cell Biol 4: 350-353
    • (1994) Trends Cell Biol , vol.4 , pp. 350-353
    • Allan, D.1    Kallen, K.J.2
  • 3
    • 0023971414 scopus 로고
    • A model for the hepatitis B virus core protein prediction of antigenic sites and relationship to RNA virus capsid proteins
    • Argos P, Fuller SD (1988) A model for the hepatitis B virus core protein prediction of antigenic sites and relationship to RNA virus capsid proteins. EMBO J 7: 819-824
    • (1988) EMBO J , vol.7 , pp. 819-824
    • Argos, P.1    Fuller, S.D.2
  • 4
    • 0026706346 scopus 로고
    • Hepadnaviral assembly is initiated by polymerase binding to the encapsidation signal in the viral RNA genome
    • Bartenschlager R, Schaller H (1992) Hepadnaviral assembly is initiated by polymerase binding to the encapsidation signal in the viral RNA genome EMBO J 11: 3413-3420
    • (1992) EMBO J , vol.11 , pp. 3413-3420
    • Bartenschlager, R.1    Schaller, H.2
  • 5
    • 0025026431 scopus 로고
    • The P gene product of hepatitis B virus is required as a structural component for genomic RNA encapsidation
    • Bartenschlager R, Junker-Niepmann M, Schaller H (1990) The P gene product of hepatitis B virus is required as a structural component for genomic RNA encapsidation J Virol 64 5324-5332
    • (1990) J Virol , vol.64 , pp. 5324-5332
    • Bartenschlager, R.1    Junker-Niepmann, M.2    Schaller, H.3
  • 6
    • 0024261645 scopus 로고
    • Roles of operator and nonoperator RNA sequences in bacteriophage R17 capsid assembly
    • Beckett D, Wu HN, Uhlenbeck, OC (1988) Roles of operator and nonoperator RNA sequences in bacteriophage R17 capsid assembly. J Mol Biol 204: 939-947
    • (1988) J Mol Biol , vol.204 , pp. 939-947
    • Beckett, D.1    Wu, H.N.2    Uhlenbeck, O.C.3
  • 8
    • 0025316017 scopus 로고
    • Hepatitis B virus nucleocapsid assembly: Primary structure requirements in the core protein
    • Birnbaum F, Nassal M (1990) Hepatitis B virus nucleocapsid assembly: primary structure requirements in the core protein J Virol 64: 3319-3330
    • (1990) J Virol , vol.64 , pp. 3319-3330
    • Birnbaum, F.1    Nassal, M.2
  • 9
    • 0027184227 scopus 로고
    • Hepatitis B virus, significance of naturally occurring mutants
    • Blum HE (1993) Hepatitis B virus, significance of naturally occurring mutants Intervirology 35: 40-50
    • (1993) Intervirology , vol.35 , pp. 40-50
    • Blum, H.E.1
  • 10
    • 76549181000 scopus 로고
    • A "new" antigen in leukemia sera
    • Blumberg BS, Alter HJ, Visnich S (1965) A "new" antigen in leukemia sera, JAMA 191: 541-546
    • (1965) JAMA , vol.191 , pp. 541-546
    • Blumberg, B.S.1    Alter, H.J.2    Visnich, S.3
  • 13
    • 0025770151 scopus 로고
    • Mutational analysis of hepatitis B surface antigen particle assembly and secretion
    • Bruss V, Ganem D (1991a) Mutational analysis of hepatitis B surface antigen particle assembly and secretion. J Virol 65: 3813-3820)
    • (1991) J Virol , vol.65 , pp. 3813-3820
    • Bruss, V.1    Ganem, D.2
  • 14
    • 0026034960 scopus 로고
    • The role of envelope proteins in hepatitis B virus assembly
    • Bruss V, Ganem D (1991b) The role of envelope proteins in hepatitis B virus assembly. Proc Natl Acad Sci USA 88: 1059-1063
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 1059-1063
    • Bruss, V.1    Ganem, D.2
  • 15
    • 0028013056 scopus 로고
    • Mapping a region of the large envelope protein required for hepatitis B virion maturation
    • Bruss V, Thomssen R (1994) Mapping a region of the large envelope protein required for hepatitis B virion maturation. J Virol 68: 1643-1650
    • (1994) J Virol , vol.68 , pp. 1643-1650
    • Bruss, V.1    Thomssen, R.2
  • 16
    • 0028236042 scopus 로고
    • Post-translational alterations in transmembrane topology of the hepatitis B virus large envelope protein
    • Bruss V, Lu X, Thomssen R, Gerlich WH (1994) Post-translational alterations in transmembrane topology of the hepatitis B virus large envelope protein. EMBO J 13: 2273-2279
    • (1994) EMBO J , vol.13 , pp. 2273-2279
    • Bruss, V.1    Lu, X.2    Thomssen, R.3    Gerlich, W.H.4
  • 17
    • 0022032391 scopus 로고
    • Transcripts and the putative RNA pregenome of duck hepatitis B virus: Implications for reverse transcription
    • Büscher M, Reiser W, Will H, Schaller H (1985) Transcripts and the putative RNA pregenome of duck hepatitis B virus: implications for reverse transcription. Cell 40: 717-724
    • (1985) Cell , vol.40 , pp. 717-724
    • Büscher, M.1    Reiser, W.2    Will, H.3    Schaller, H.4
  • 18
    • 0028274118 scopus 로고
    • Two regions of an avian hepadnavirus RNA pregenome are required in cis for encapsidation
    • Calvert J, Summers J (1994) Two regions of an avian hepadnavirus RNA pregenome are required in cis for encapsidation. J Virol 68: 2084-2090
    • (1994) J Virol , vol.68 , pp. 2084-2090
    • Calvert, J.1    Summers, J.2
  • 19
    • 0024593741 scopus 로고
    • Biosynthesis of the reverse transcriptase of hepatitis B viruses involves de novo translational initiation not ribosomal frameshifting
    • Chang LJ, Pryciak P, Ganem D, Varmus HE (1989) Biosynthesis of the reverse transcriptase of hepatitis B viruses involves de novo translational initiation not ribosomal frameshifting Nature 337: 364-368
    • (1989) Nature , vol.337 , pp. 364-368
    • Chang, L.J.1    Pryciak, P.2    Ganem, D.3    Varmus, H.E.4
  • 20
    • 0025350277 scopus 로고
    • Mechanism of translation of the hepadnaviral polymerase (P) gene
    • Chang LJ, Ganem D, Varmus HE (1990) Mechanism of translation of the hepadnaviral polymerase (P) gene. Proc Natl Acad Sci USA 87: 5158-5162
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 5158-5162
    • Chang, L.J.1    Ganem, D.2    Varmus, H.E.3
  • 21
    • 0028228462 scopus 로고
    • Phenotyptc mixing between different hepadnavirus nucleocapsid proteins reveals C protein dimerization to be cis preferential
    • Chang C, Zhou S, Ganem D, Standring DN (1994) Phenotyptc mixing between different hepadnavirus nucleocapsid proteins reveals C protein dimerization to be cis preferential. J Virol 68: 5225-5231
    • (1994) J Virol , vol.68 , pp. 5225-5231
    • Chang, C.1    Zhou, S.2    Ganem, D.3    Standring, D.N.4
  • 25
    • 0020316090 scopus 로고
    • Electron microscopy of hepatitis B core antigen synthesized in E coli
    • Cohen BJ, Richmond JE (1982) Electron microscopy of hepatitis B core antigen synthesized in E coli Nature 296: 677-678
    • (1982) Nature , vol.296 , pp. 677-678
    • Cohen, B.J.1    Richmond, J.E.2
  • 26
  • 28
    • 0027157736 scopus 로고
    • Folding and assembly of viral membrane proteins
    • Doms RW, Lamb RA, Rose JK, Helenius A (1993) Folding and assembly of viral membrane proteins. Virology 193: 545-562
    • (1993) Virology , vol.193 , pp. 545-562
    • Doms, R.W.1    Lamb, R.A.2    Rose, J.K.3    Helenius, A.4
  • 30
    • 0028928193 scopus 로고
    • Selection of peptide inhibitors of interactions involved in complex protein assemblies. association of the core and surface antigens of hepatitis B virus
    • Dyson MR, Murray K (1995) Selection of peptide inhibitors of interactions involved in complex protein assemblies. association of the core and surface antigens of hepatitis B virus. Proc Natl Acad Sci USA 92: 2194-2198
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 2194-2198
    • Dyson, M.R.1    Murray, K.2
  • 31
    • 0023428332 scopus 로고
    • Multiple topogenic sequences determine the transmembrane orientation of hepatitis B surface antigen
    • Eble BE, MacRae DR, Lingappa VR, Ganem D (1987) Multiple topogenic sequences determine the transmembrane orientation of hepatitis B surface antigen Mol Cell Biol 7: 2591-3601
    • (1987) Mol Cell Biol , vol.7 , pp. 2591-3601
    • Eble, B.E.1    MacRae, D.R.2    Lingappa, V.R.3    Ganem, D.4
  • 32
    • 0025219320 scopus 로고
    • The N-terminal (preS2) domain of a hepatitis B virus surface glycoprotein is translocated across membranes by downstream signal sequences
    • Eble BE, Lingappa VR, Ganem D (1990) The N-terminal (preS2) domain of a hepatitis B virus surface glycoprotein is translocated across membranes by downstream signal sequences. J Virol 64 1414-1419
    • (1990) J Virol , vol.64 , pp. 1414-1419
    • Eble, B.E.1    Lingappa, V.R.2    Ganem, D.3
  • 33
    • 0026008004 scopus 로고
    • Hepatitis B virus core antigen has two nuclear localization sequences in the arginine-rich carboxy terminus
    • Eckhardt SG, Milich DR, McLachlan A (1991) Hepatitis B virus core antigen has two nuclear localization sequences in the arginine-rich carboxy terminus. J Virol 65: 575-582
    • (1991) J Virol , vol.65 , pp. 575-582
    • Eckhardt, S.G.1    Milich, D.R.2    McLachlan, A.3
  • 34
    • 0027295660 scopus 로고
    • Infectious hepatitis B virus variant defective in preS2-expression in a chronic carrier
    • Fernholz D, Galle PR, Stemler M, Brunetto M, Bonino F, Will H (1993) Infectious hepatitis B virus variant defective in preS2-expression in a chronic carrier. Virology 194 137-148
    • (1993) Virology , vol.194 , pp. 137-148
    • Fernholz, D.1    Galle, P.R.2    Stemler, M.3    Brunetto, M.4    Bonino, F.5    Will, H.6
  • 35
    • 0027940713 scopus 로고
    • Specific incorporation of cyclophuin A into HIV-1 virions
    • Franke EK, Yuan HEH, Luban J (1994) Specific incorporation of cyclophuin A into HIV-1 virions Nature 372: 359-362
    • (1994) Nature , vol.372 , pp. 359-362
    • Franke, E.K.1    Yuan, H.E.H.2    Luban, J.3
  • 37
    • 0024474088 scopus 로고
    • A recombinant hepatitis B core antigen polypeptide with the protamine-like domain deleted self-assembles into capsid particles but fails to bind nucleic acids
    • Gallina A, Bonelli F, Zentilin L, Rindi G, Muttini M, Milanesi G (1989) A recombinant hepatitis B core antigen polypeptide with the protamine-like domain deleted self-assembles into capsid particles but fails to bind nucleic acids. J Virol 63 4645-4652
    • (1989) J Virol , vol.63 , pp. 4645-4652
    • Gallina, A.1    Bonelli, F.2    Zentilin, L.3    Rindi, G.4    Muttini, M.5    Milanesi, G.6
  • 38
    • 0025782903 scopus 로고    scopus 로고
    • Assembly of hepadnaviral virions and subviral particles
    • Mason WS, Seeger C (eds) Springer, Berlin Heidelberg New York
    • Ganem D (1991) Assembly of hepadnaviral virions and subviral particles. In: Mason WS, Seeger C (eds) Hepadnaviruses Molecular biology and pathogenesis. Springer, Berlin Heidelberg New York, pp 61-83 (Current topics in microbiology and immunology, vol 168)
    • (1991) Hepadnaviruses Molecular Biology and Pathogenesis , pp. 61-83
    • Ganem, D.1
  • 39
    • 0025782903 scopus 로고    scopus 로고
    • Ganem D (1991) Assembly of hepadnaviral virions and subviral particles. In: Mason WS, Seeger C (eds) Hepadnaviruses Molecular biology and pathogenesis. Springer, Berlin Heidelberg New York, pp 61-83 (Current topics in microbiology and immunology, vol 168)
    • Current Topics in Microbiology and Immunology , vol.168
  • 40
    • 0023080494 scopus 로고
    • The molecular biology of hepatitis B virus
    • Ganem D, Varmus HE (1987) The molecular biology of hepatitis B virus Annu Rev Biochem 56: 651-693
    • (1987) Annu Rev Biochem , vol.56 , pp. 651-693
    • Ganem, D.1    Varmus, H.E.2
  • 42
    • 0020265940 scopus 로고
    • Structure of hepatitis B surface antigen. Characterization of the lipid components and their association with the viral proteins
    • Gavilanes F, Gonzalez-Ros JM, Peterson DL (1982) Structure of hepatitis B surface antigen. Characterization of the lipid components and their association with the viral proteins J Biol Chem 257: 7770-7777
    • (1982) J Biol Chem , vol.257 , pp. 7770-7777
    • Gavilanes, F.1    Gonzalez-Ros, J.M.2    Peterson, D.L.3
  • 43
    • 0027333423 scopus 로고
    • Role of the major heat shock proteins as molecular chaperones
    • Georgopoulos C, Welch WJ (1993) Role of the major heat shock proteins as molecular chaperones. Annu Rev Cell Biol 9: 601-634
    • (1993) Annu Rev Cell Biol , vol.9 , pp. 601-634
    • Georgopoulos, C.1    Welch, W.J.2
  • 44
    • 0028833661 scopus 로고
    • Phenotypic mixing of rodent but not avian hepadnavirus surface proteins into human hepatitis B virus particles
    • Gerhardt E, Bruss V (1995) Phenotypic mixing of rodent but not avian hepadnavirus surface proteins into human hepatitis B virus particles. J Virol 69, 1201-1208
    • (1995) J Virol , vol.69 , pp. 1201-1208
    • Gerhardt, E.1    Bruss, V.2
  • 45
    • 0020072620 scopus 로고
    • Specificity and localization of the hepatitis B virus-associated kinase
    • Gerlich WH, Goldmann U, Muller R, Stibbe W, Wolff W (1982) Specificity and localization of the hepatitis B virus-associated kinase J Virol 42: 761-766
    • (1982) J Virol , vol.42 , pp. 761-766
    • Gerlich, W.H.1    Goldmann, U.2    Muller, R.3    Stibbe, W.4    Wolff, W.5
  • 46
    • 0028037170 scopus 로고
    • The large surface protein of duck hepatitis B virus is phosphorylated in the preS domain
    • Grgacic EVL, Anderson DA (1994) The large surface protein of duck hepatitis B virus is phosphorylated in the preS domain J Virol 68: 7344-7350
    • (1994) J Virol , vol.68 , pp. 7344-7350
    • Grgacic, E.V.L.1    Anderson, D.A.2
  • 47
    • 0026934552 scopus 로고
    • Cell biology of viruses that assemble along the biosynthetic pathway
    • Griffiths G, Rottier P (1992) Cell biology of viruses that assemble along the biosynthetic pathway Semin Cell Biol 3: 367-381
    • (1992) Semin Cell Biol , vol.3 , pp. 367-381
    • Griffiths, G.1    Rottier, P.2
  • 48
    • 0027221167 scopus 로고
    • Reproducible high level infection of cultured adult human hepatocytes by hepatitis B virus. effect of polyethylene glycol on adsorption and penetration
    • Gripon P, Diot C, Guguen-Guillouzo C (1993) Reproducible high level infection of cultured adult human hepatocytes by hepatitis B virus. effect of polyethylene glycol on adsorption and penetration Virology 192: 534-540
    • (1993) Virology , vol.192 , pp. 534-540
    • Gripon, P.1    Diot, C.2    Guguen-Guillouzo, C.3
  • 49
    • 0028822367 scopus 로고
    • Myristylation of the hepatitis B virus large surface protein is essential for viral infectivity
    • Gripon P, Le Seyec J, Rumin S, Guguen-Guillouzo C (1995) Myristylation of the hepatitis B virus large surface protein is essential for viral infectivity. Virology 213: 292-299
    • (1995) Virology , vol.213 , pp. 292-299
    • Gripon, P.1    Le Seyec, J.2    Rumin, S.3    Guguen-Guillouzo, C.4
  • 50
    • 0027966147 scopus 로고
    • Hepatitis B virus nucleocapsid particles do not cross the hepatocyte nuclear membrane in transgenic mice
    • Guidotti LG, Martinez V, Loh YT, Rogler CE, Chisari FV (1994) Hepatitis B virus nucleocapsid particles do not cross the hepatocyte nuclear membrane in transgenic mice J Virol 68: 5469-5475
    • (1994) J Virol , vol.68 , pp. 5469-5475
    • Guidotti, L.G.1    Martinez, V.2    Loh, Y.T.3    Rogler, C.E.4    Chisari, F.V.5
  • 51
    • 0026795429 scopus 로고
    • RNA- and DNA-binding activities in hepatitis B virus capsid protein: A model for their roles in viral replication
    • Hatton T, Zhou S, Standring DN (1992) RNA- and DNA-binding activities in hepatitis B virus capsid protein: a model for their roles in viral replication J Virol 66: 5232-5241
    • (1992) J Virol , vol.66 , pp. 5232-5241
    • Hatton, T.1    Zhou, S.2    Standring, D.N.3
  • 52
    • 0000523194 scopus 로고
    • Surface proteins of hepatitis B viruses
    • McLachlan A (ed) CRC Press, Boca Raton
    • Heermann KH, Gerlich WH (1991) Surface proteins of hepatitis B viruses In. McLachlan A (ed) Molecular biology of the hepatitis B virus CRC Press, Boca Raton, pp 145-169
    • (1991) Molecular Biology of the Hepatitis B Virus , pp. 145-169
    • Heermann, K.H.1    Gerlich, W.H.2
  • 54
    • 0028185738 scopus 로고
    • Compartments of the early secretory pathway
    • Maddy AH, Harris JR (eds) Plenum, New York
    • Hendriks RJM, Fuller SD (1993) Compartments of the early secretory pathway. In: Maddy AH, Harris JR (eds) Subcellular biochemistry: membrane biogenesis. Plenum, New York, 22: 101-149
    • (1993) Subcellular Biochemistry: Membrane Biogenesis , vol.22 , pp. 101-149
    • Hendriks, R.J.M.1    Fuller, S.D.2
  • 55
    • 0026909328 scopus 로고
    • Mechanisms that determine the transmembrane disposition of proteins
    • High S, Dobberstein B (1992) Mechanisms that determine the transmembrane disposition of proteins. Curr Opin Cell Biol 4: 581-586
    • (1992) Curr Opin Cell Biol , vol.4 , pp. 581-586
    • High, S.1    Dobberstein, B.2
  • 56
    • 0025764058 scopus 로고
    • Histone-DNA interactions and their modulation by phosphorylation of Ser-Pro-X-Lys/Arg motifs
    • Hill CS, Rimmer JM, Green BN, Finch JT, Thomas JO (1991) Histone-DNA interactions and their modulation by phosphorylation of Ser-Pro-X-Lys/Arg motifs. EMBO J 10: 1939-1948
    • (1991) EMBO J , vol.10 , pp. 1939-1948
    • Hill, C.S.1    Rimmer, J.M.2    Green, B.N.3    Finch, J.T.4    Thomas, J.O.5
  • 57
    • 0025238448 scopus 로고
    • Polymerase gene products of hepatitis B viruses are required for genomic RNA packaging as well as for reverse transcription
    • Hirsch RC, Lavine JE, Chang LJ, Varmus HE, Ganem D (1990) Polymerase gene products of hepatitis B viruses are required for genomic RNA packaging as well as for reverse transcription. Nature 344: 552-555
    • (1990) Nature , vol.344 , pp. 552-555
    • Hirsch, R.C.1    Lavine, J.E.2    Chang, L.J.3    Varmus, H.E.4    Ganem, D.5
  • 58
    • 0027484462 scopus 로고
    • High titers of retrovirus (vesicular stomatitis virus) pseudotypes, at last
    • Hopkins N (1993) High titers of retrovirus (vesicular stomatitis virus) pseudotypes, at last. Proc Natl Acad Sci USA 90 8759-8760
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 8759-8760
    • Hopkins, N.1
  • 59
    • 0030035038 scopus 로고    scopus 로고
    • Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase
    • Hu J, Seeger C (1996) Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase Proc Natl Acad Sci USA 93: 1060-1064
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1060-1064
    • Hu, J.1    Seeger, C.2
  • 60
    • 0026658183 scopus 로고
    • Hepatitis B surface antigen assembles in a post-ER, pre-Golgi compartment
    • Huovila AP, Eder AM, Fuller SD (1992) Hepatitis B surface antigen assembles in a post-ER, pre-Golgi compartment. J Cell Biol 118 1305-1320
    • (1992) J Cell Biol , vol.118 , pp. 1305-1320
    • Huovila, A.P.1    Eder, A.M.2    Fuller, S.D.3
  • 62
    • 0029078314 scopus 로고
    • The pre-S domain of the large viral envelope protein determines host range in avian hepatitis B viruses
    • Ishikawa T, Ganem D (1995) The pre-S domain of the large viral envelope protein determines host range in avian hepatitis B viruses Proc Natl Acad Sci USA 92: 6259-6263
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 6259-6263
    • Ishikawa, T.1    Ganem, D.2
  • 63
    • 0025045477 scopus 로고
    • A short cis-acting sequence is required for hepatitis B virus pregenome encapsidation and sufficient for packaging of foreign RNA
    • Junker-Niepmann M, Bartenschlager R, Schaller H (1990) A short cis-acting sequence is required for hepatitis B virus pregenome encapsidation and sufficient for packaging of foreign RNA. EMBO J 9: 3389-3396
    • (1990) EMBO J , vol.9 , pp. 3389-3396
    • Junker-Niepmann, M.1    Bartenschlager, R.2    Schaller, H.3
  • 64
    • 0028073177 scopus 로고
    • Effect of core protein phosphorylation by protein kinase C on encapsidation of RNA within core particles of hepatitis B virus
    • Kann M, Gerlich WH (1994) Effect of core protein phosphorylation by protein kinase C on encapsidation of RNA within core particles of hepatitis B virus J Virol 68: 7993-8000
    • (1994) J Virol , vol.68 , pp. 7993-8000
    • Kann, M.1    Gerlich, W.H.2
  • 65
    • 0029645618 scopus 로고
    • Conformational flexibility and evolutionary conservation sn the hepatitis B virus core structure
    • Kenney JM, von Bonsdorff C-H, Nassal M, Fuller SD (1995) Conformational flexibility and evolutionary conservation sn the hepatitis B virus core structure. Structure 3: 1009-1019
    • (1995) Structure , vol.3 , pp. 1009-1019
    • Kenney, J.M.1    Von Bonsdorff, C.-H.2    Nassal, M.3    Fuller, S.D.4
  • 67
    • 0027430748 scopus 로고
    • Hepadnavirus infection requires interaction between the viral pre-S domain and a specific hepatocellular receptor
    • Klingmüller U, Schaller H (1993) Hepadnavirus infection requires interaction between the viral pre-S domain and a specific hepatocellular receptor. J Virol 67: 7414-7422
    • (1993) J Virol , vol.67 , pp. 7414-7422
    • Klingmüller, U.1    Schaller, H.2
  • 68
    • 0027323570 scopus 로고
    • The encapsidation signal on the hepatitis B virus RNA pregenome forms a stem-loop structure that is critical for its function
    • Knaus T, Nassal M (1993) The encapsidation signal on the hepatitis B virus RNA pregenome forms a stem-loop structure that is critical for its function. Nucleic Acids Res 21: 3967-3975
    • (1993) Nucleic Acids Res , vol.21 , pp. 3967-3975
    • Knaus, T.1    Nassal, M.2
  • 69
    • 0027272784 scopus 로고
    • Analysis of the earliest steps of hepadnavirus replication: Genome repair after infectious entry into hepatocytes does not depend on viral polymerase activity
    • Kock J, Schlicht HJ (1993) Analysis of the earliest steps of hepadnavirus replication: genome repair after infectious entry into hepatocytes does not depend on viral polymerase activity J Virol 67: 4867-4874
    • (1993) J Virol , vol.67 , pp. 4867-4874
    • Kock, J.1    Schlicht, H.J.2
  • 70
    • 0028069572 scopus 로고
    • Characterization of the budding compartment of mouse hepatitis virus: Evidence that transport from the RER to the Golgi complex requires only one vesicular transport step
    • Krijnse-Locker J, Ericsson M, Rottier PJ, Griffiths G (1994) Characterization of the budding compartment of mouse hepatitis virus: evidence that transport from the RER to the Golgi complex requires only one vesicular transport step. J Cell Biol 124: 55-70
    • (1994) J Cell Biol , vol.124 , pp. 55-70
    • Krijnse-Locker, J.1    Ericsson, M.2    Rottier, P.J.3    Griffiths, G.4
  • 71
    • 0024431801 scopus 로고
    • Novel N-terminal amino acid sequence required for retention of a hepatitis B virus glycoprotein in the endoplasmic reticulum
    • Kuroki K, Russnack, Ganem D (1989) Novel N-terminal amino acid sequence required for retention of a hepatitis B virus glycoprotein in the endoplasmic reticulum. Mol Cell Biol 9 4459-4466
    • (1989) Mol Cell Biol , vol.9 , pp. 4459-4466
    • Kuroki, K.1    Russnack2    Ganem, D.3
  • 72
    • 0025265828 scopus 로고
    • Expression of hepatitis B virus core and precore antigens in insect cells and characterization of a core-associated kinase activity
    • Lanford RE, Notvall L (1990) Expression of hepatitis B virus core and precore antigens in insect cells and characterization of a core-associated kinase activity Virology 176 222-233
    • (1990) Virology , vol.176 , pp. 222-233
    • Lanford, R.E.1    Notvall, L.2
  • 73
    • 0024505906 scopus 로고
    • Expression and characterization of hepatitis B virus surface antigen polypeptides in insect cells with a baculovirus expression system
    • Lanford RE, Luckow V, Kennedy RC, Dreesman GR, Notvall L, Summers MD (1989) Expression and characterization of hepatitis B virus surface antigen polypeptides in insect cells with a baculovirus expression system J Virol 63 1549-1557
    • (1989) J Virol , vol.63 , pp. 1549-1557
    • Lanford, R.E.1    Luckow, V.2    Kennedy, R.C.3    Dreesman, G.R.4    Notvall, L.5    Summers, M.D.6
  • 74
    • 0028207631 scopus 로고
    • The stem-loop structure of the cis-encapsidation signal is highly conserved in naturally occurring hepatitis B virus variants
    • Laskus T, Rakela J, Persing DH (1994) The stem-loop structure of the cis-encapsidation signal is highly conserved in naturally occurring hepatitis B virus variants. Virology 200: 809-12
    • (1994) Virology , vol.200 , pp. 809-812
    • Laskus, T.1    Rakela, J.2    Persing, D.H.3
  • 75
    • 0027975956 scopus 로고
    • Recent developments in hepatitis delta research
    • Lazinski DW, Taylor JM (1994) Recent developments in hepatitis delta research. Adv Virus Res 43: 187-231
    • (1994) Adv Virus Res , vol.43 , pp. 187-231
    • Lazinski, D.W.1    Taylor, J.M.2
  • 76
    • 0028334395 scopus 로고
    • Coordinate regulation of replication and virus assembly by the large envelope protein of an avian hepadnavirus
    • Lenhoff RJ, Summers J (1994) Coordinate regulation of replication and virus assembly by the large envelope protein of an avian hepadnavirus. J Virol 68: 4565-4571
    • (1994) J Virol , vol.68 , pp. 4565-4571
    • Lenhoff, R.J.1    Summers, J.2
  • 77
    • 0026749913 scopus 로고
    • Evidence for involvement of a ribosomal leaky scanning mechanism in the translation of the hepatitis B virus pol gene from the viral pregenome RNA
    • Lin CG, Lo SJ (1992) Evidence for involvement of a ribosomal leaky scanning mechanism in the translation of the hepatitis B virus pol gene from the viral pregenome RNA Virology 188: 342-52
    • (1992) Virology , vol.188 , pp. 342-352
    • Lin, C.G.1    Lo, S.J.2
  • 78
    • 0028178379 scopus 로고
    • A eukaryotic cytosolic chaperonin is associated with a high molecular weight intermediate in the assembly of hepatitis B virus capsid, a multimeric particle
    • Lingappa JR, Martin RL, Wong ML, Ganem D, Welch WJ, Lingappa VR (1994) A eukaryotic cytosolic chaperonin is associated with a high molecular weight intermediate in the assembly of hepatitis B virus capsid, a multimeric particle. J Cell Biol 125: 99-111
    • (1994) J Cell Biol , vol.125 , pp. 99-111
    • Lingappa, J.R.1    Martin, R.L.2    Wong, M.L.3    Ganem, D.4    Welch, W.J.5    Lingappa, V.R.6
  • 79
    • 0025232841 scopus 로고
    • Microtubule-dependent retrograde transport of proteins into the ER in the presence of Brefeldin A suggests an ER recycling pathway
    • Lippincott-Schwartz J, Donaldson JG, Schweizer A, Berger EG, Hauri HP, Yuan LC, Klausner RD (1990) Microtubule-dependent retrograde transport of proteins into the ER in the presence of Brefeldin A suggests an ER recycling pathway. Cell 60: 821-836
    • (1990) Cell , vol.60 , pp. 821-836
    • Lippincott-Schwartz, J.1    Donaldson, J.G.2    Schweizer, A.3    Berger, E.G.4    Hauri, H.P.5    Yuan, L.C.6    Klausner, R.D.7
  • 80
    • 0028679793 scopus 로고
    • Treatment of chronic hepatitis B
    • Lok ASF (1994) Treatment of chronic hepatitis B. J Viral Hepatitis 1: 105-124
    • (1994) J Viral Hepatitis , vol.1 , pp. 105-124
    • Lok, A.S.F.1
  • 82
    • 0026013628 scopus 로고
    • Myristylation of a duck hepatitis B virus envelope protein is essential for infectivity but not for virus assembly
    • Macrae DR, Bruss V, Ganem D (1991) Myristylation of a duck hepatitis B virus envelope protein is essential for infectivity but not for virus assembly. Virology 181: 359-363
    • (1991) Virology , vol.181 , pp. 359-363
    • Macrae, D.R.1    Bruss, V.2    Ganem, D.3
  • 83
    • 0028176142 scopus 로고
    • Role of Pr160 gag-pol in mediating the selective incorporation of tRNA(Lys) into human immunodeficiency virus type 1 particles
    • Mak J, Jiang M, Wainberg MA, Hammarskjold ML, Rekosh D, Kleiman L (1994) Role of Pr160 gag-pol in mediating the selective incorporation of tRNA(Lys) into human immunodeficiency virus type 1 particles. J Virol 68: 2065-2072
    • (1994) J Virol , vol.68 , pp. 2065-2072
    • Mak, J.1    Jiang, M.2    Wainberg, M.A.3    Hammarskjold, M.L.4    Rekosh, D.5    Kleiman, L.6
  • 84
    • 0027293511 scopus 로고
    • Mutational analysis of the cysteine residues in the hepatitis B virus small envelope protein
    • Mangold CM, Streeck RE (1993) Mutational analysis of the cysteine residues in the hepatitis B virus small envelope protein J Virol 67: 4588-4597
    • (1993) J Virol , vol.67 , pp. 4588-4597
    • Mangold, C.M.1    Streeck, R.E.2
  • 85
    • 0028501438 scopus 로고
    • Molecular chaperones in cellular protein folding
    • Martin J, Hartl FU (1994) Molecular chaperones in cellular protein folding. Bioessays 16: 689-692
    • (1994) Bioessays , vol.16 , pp. 689-692
    • Martin, J.1    Hartl, F.U.2
  • 87
    • 12644267799 scopus 로고    scopus 로고
    • Mason WS, Seeger C (eds) (1991) Hepadnaviruses. Molecular biology and pathogenesis. Springer, Berlin Heidelberg New York (Current topics in microbiology and immunology, vol 168)
    • Current Topics in Microbiology and Immunology , vol.168
  • 90
    • 0027722382 scopus 로고
    • Hepatitis B virus C-gene variants
    • Miska S, Will H (1993) Hepatitis B virus C-gene variants. Arch Virol [Suppl] 8: 155-169
    • (1993) Arch Virol [Suppl] , vol.8 , pp. 155-169
    • Miska, S.1    Will, H.2
  • 91
    • 0026695732 scopus 로고
    • The Arg-rich domain of the HBV core protein is required for pregenome encapsidation and productive positive-strand DNA synthesis but not for virus assembly
    • Nassal M (1992) The Arg-rich domain of the HBV core protein is required for pregenome encapsidation and productive positive-strand DNA synthesis but not for virus assembly. J Virol 66: 4107-4116
    • (1992) J Virol , vol.66 , pp. 4107-4116
    • Nassal, M.1
  • 92
    • 0027201547 scopus 로고
    • Hepatitis B virus replication
    • Nassal M, Schaller H (1993a) Hepatitis B virus replication. Trends Microbiol 1: 221-226
    • (1993) Trends Microbiol , vol.1 , pp. 221-226
    • Nassal, M.1    Schaller, H.2
  • 93
    • 0004184629 scopus 로고
    • Hepatitis B virus nucleocapsid assembly
    • Dorfler W, Böhm P (eds) VCH, Weinheim
    • Nassal M, Schaller H (1993b) Hepatitis B virus nucleocapsid assembly. In: Dorfler W, Böhm P (eds) Virus strategies VCH, Weinheim, pp 41-75
    • (1993) Virus Strategies , pp. 41-75
    • Nassal, M.1    Schaller, H.2
  • 94
    • 0027264123 scopus 로고
    • An intramolecular disulfide bridge between Cys-7 and Cys61 determines the structure of the secretory core gene product (HBeAg) of hepatitis B virus
    • Nassal M, Rieger A (1993) An intramolecular disulfide bridge between Cys-7 and Cys61 determines the structure of the secretory core gene product (HBeAg) of hepatitis B virus. J Virol 67: 4307-4315
    • (1993) J Virol , vol.67 , pp. 4307-4315
    • Nassal, M.1    Rieger, A.2
  • 95
    • 0029940006 scopus 로고    scopus 로고
    • A bulged region of the hepatitis B virus RNA encapsidatton signal contains the replication origin for discontinuous first strand DNA synthesis
    • Nassal M, Rieger A (1996) A bulged region of the hepatitis B virus RNA encapsidatton signal contains the replication origin for discontinuous first strand DNA synthesis. J Virol 70: 2764-2773
    • (1996) J Virol , vol.70 , pp. 2764-2773
    • Nassal, M.1    Rieger, A.2
  • 96
    • 0025604455 scopus 로고
    • Translational inactivation of RNA function discrimination against a subset of genomic transcripts during HBV nucleocapsid assembly
    • Nassal M, Junker-Niepmann M, Schaller H (1990) Translational inactivation of RNA function discrimination against a subset of genomic transcripts during HBV nucleocapsid assembly Cell 63: 1357-1363
    • (1990) Cell , vol.63 , pp. 1357-1363
    • Nassal, M.1    Junker-Niepmann, M.2    Schaller, H.3
  • 97
    • 0026684254 scopus 로고
    • Topological analysis of the hepatitis B virus core particle by cysteine-cysteine crosslinking
    • Nassal M, Rieger A, Steinau O (1992) Topological analysis of the hepatitis B virus core particle by cysteine-cysteine crosslinking J Mol Biol 225: 1013-1025
    • (1992) J Mol Biol , vol.225 , pp. 1013-1025
    • Nassal, M.1    Rieger, A.2    Steinau, O.3
  • 98
    • 0028168882 scopus 로고
    • A carboxy-terminal portion of the PreS1 domain of hepatitis B virus (HBV) occasioned retention in endoplasmic reticulum of HBV envelope proteins expressed by recombinant vaccinia viruses
    • Nemeckova S, Kunke D, Press M, Nemecek V, Kutinova L (1994) A carboxy-terminal portion of the PreS1 domain of hepatitis B virus (HBV) occasioned retention in endoplasmic reticulum of HBV envelope proteins expressed by recombinant vaccinia viruses. Virology 202: 1024-1027
    • (1994) Virology , vol.202 , pp. 1024-1027
    • Nemeckova, S.1    Kunke, D.2    Press, M.3    Nemecek, V.4    Kutinova, L.5
  • 99
    • 0022538381 scopus 로고
    • Identification and chemical synthesis of a host cell receptor binding site on hepatitis B virus
    • Neurath AR, Kent SBH, Strick N, Parker K (1986) Identification and chemical synthesis of a host cell receptor binding site on hepatitis B virus. Cell 446: 429-436
    • (1986) Cell , vol.446 , pp. 429-436
    • Neurath, A.R.1    Kent, S.B.H.2    Strick, N.3    Parker, K.4
  • 100
    • 0026573138 scopus 로고
    • Search for hepatitis B virus cell receptors reveals binding sites for interleukin 6 on the virus envelope protein
    • Neurath AR, Strick N, Sproul P (1992) Search for hepatitis B virus cell receptors reveals binding sites for interleukin 6 on the virus envelope protein J Exp Med 175: 461-469
    • (1992) J Exp Med , vol.175 , pp. 461-469
    • Neurath, A.R.1    Strick, N.2    Sproul, P.3
  • 102
    • 0028201045 scopus 로고
    • Leeway and constraints in the forced evolution of a regulatory RNA helix
    • Olsthoorn RC, Licis N, van Duin J (1994) Leeway and constraints in the forced evolution of a regulatory RNA helix. EMBO J 13: 2660-2668
    • (1994) EMBO J , vol.13 , pp. 2660-2668
    • Olsthoorn, R.C.1    Licis, N.2    Van Duin, J.3
  • 103
    • 0019961608 scopus 로고
    • Electron microscopy of human hepatitis B virus cores by negative staining-carbon film technique
    • Onodera S, Ohori H, Yamaki M, Ishida N (1982) Electron microscopy of human hepatitis B virus cores by negative staining-carbon film technique J Med Virol 10: 147-155
    • (1982) J Med Virol , vol.10 , pp. 147-155
    • Onodera, S.1    Ohori, H.2    Yamaki, M.3    Ishida, N.4
  • 104
    • 0028265897 scopus 로고
    • A dramatic shift in the transmembrane topology of a viral envelope protein accompanies hepatitis B viral morphogenesis
    • Ostapchuk P, Hearing P, Ganem D (1994) A dramatic shift in the transmembrane topology of a viral envelope protein accompanies hepatitis B viral morphogenesis EMBO J 13: 1048-1057
    • (1994) EMBO J , vol.13 , pp. 1048-1057
    • Ostapchuk, P.1    Hearing, P.2    Ganem, D.3
  • 106
    • 0021237805 scopus 로고
    • Intracellular transport and secretion of hepatitis B surface antigen in mammalian cells
    • Patzer EJ, Nakamura GR, Yaffe A (1984) intracellular transport and secretion of hepatitis B surface antigen in mammalian cells. J Virol 51: 346-353
    • (1984) J Virol , vol.51 , pp. 346-353
    • Patzer, E.J.1    Nakamura, G.R.2    Yaffe, A.3
  • 107
    • 0022538396 scopus 로고
    • Intracellular assembly and packaging of hepatitis B surface antigen particles occur in the endoplasmic reticulum
    • Patzer EJ, Nakamura GR, Simonsen CC, Levinson AD, Brands R (1986) Intracellular assembly and packaging of hepatitis B surface antigen particles occur in the endoplasmic reticulum. J Virol 58: 884-892
    • (1986) J Virol , vol.58 , pp. 884-892
    • Patzer, E.J.1    Nakamura, G.R.2    Simonsen, C.C.3    Levinson, A.D.4    Brands, R.5
  • 108
    • 0027404265 scopus 로고
    • The RNA binding site of bacteriophage MS2 coat protein
    • Peabody DS (1993) The RNA binding site of bacteriophage MS2 coat protein EMBO J 12: 595-600
    • (1993) EMBO J , vol.12 , pp. 595-600
    • Peabody, D.S.1
  • 109
    • 0023007621 scopus 로고
    • Inhibition of secretion of hepatitis B surface antigen by a related presurface polypeptide
    • Persing DH, Varmus HE, Ganem D (1986) Inhibition of secretion of hepatitis B surface antigen by a related presurface polypeptide. Science 234: 1388-1391
    • (1986) Science , vol.234 , pp. 1388-1391
    • Persing, D.H.1    Varmus, H.E.2    Ganem, D.3
  • 110
    • 0023177636 scopus 로고
    • The preS1 protein of hepatitis B virus is acylated at its N-terminus with myristic acid
    • Persing DH, Varmus HE, Ganem D (1987) The preS1 protein of hepatitis B virus is acylated at its N-terminus with myristic acid. J Virol 61: 1672-1677
    • (1987) J Virol , vol.61 , pp. 1672-1677
    • Persing, D.H.1    Varmus, H.E.2    Ganem, D.3
  • 111
    • 0023353201 scopus 로고
    • The structure of hepatitis B surface antigen and its antigenic sites
    • Peterson DL (1987) The structure of hepatitis B surface antigen and its antigenic sites Bioessays 6 258-262
    • (1987) Bioessays , vol.6 , pp. 258-262
    • Peterson, D.L.1
  • 112
    • 0026076805 scopus 로고    scopus 로고
    • Protein localization and virus assembly at intracellular membranes
    • Compans RW (ed) Springer, Berlin Heidelberg New York
    • Petterson RF (1991) Protein localization and virus assembly at intracellular membranes In: Compans RW (ed) Protein traffic in eukaryotic cells. Selected reviews. Springer, Berlin Heidelberg New York, pp 67-107 (Current topics in microbiology and immunology, vol 170)
    • (1991) Protein Traffic in Eukaryotic Cells. Selected Reviews , pp. 67-107
    • Petterson, R.F.1
  • 113
    • 0026076805 scopus 로고    scopus 로고
    • Petterson RF (1991) Protein localization and virus assembly at intracellular membranes In: Compans RW (ed) Protein traffic in eukaryotic cells. Selected reviews. Springer, Berlin Heidelberg New York, pp 67-107 (Current topics in microbiology and immunology, vol 170)
    • Current Topics in Microbiology and Immunology , vol.170
  • 114
    • 0027167557 scopus 로고
    • An RNA stem-loop structure directs hepatitis B virus genomic RNA encapsidation
    • Pollack JR, Ganem D (1993) An RNA stem-loop structure directs hepatitis B virus genomic RNA encapsidation. J Virol 67: 3254-3263
    • (1993) J Virol , vol.67 , pp. 3254-3263
    • Pollack, J.R.1    Ganem, D.2
  • 115
    • 0028095240 scopus 로고
    • Site-specific RNA binding by a hepatitis B virus reverse transcriptase initiates two distinct reactions: RNA packaging and DNA synthesis
    • Pollack JR, Ganem D (1994) Site-specific RNA binding by a hepatitis B virus reverse transcriptase initiates two distinct reactions: RNA packaging and DNA synthesis. J Virol 68 5579-5587
    • (1994) J Virol , vol.68 , pp. 5579-5587
    • Pollack, J.R.1    Ganem, D.2
  • 117
    • 0028859149 scopus 로고
    • Novel transmembrane topology of the hepatitis B virus envelope proteins
    • Prange R, Streeck RE (1995) Novel transmembrane topology of the hepatitis B virus envelope proteins. EMBO J 14: 247-256
    • (1995) EMBO J , vol.14 , pp. 247-256
    • Prange, R.1    Streeck, R.E.2
  • 118
    • 0025864197 scopus 로고
    • Myristylation is involved in intracellular retention of hepatitis B virus envelope proteins
    • Prange R, Clemen A, Streeck RE (1991) Myristylation is involved in intracellular retention of hepatitis B virus envelope proteins. J Virol 65: 3919-3923
    • (1991) J Virol , vol.65 , pp. 3919-3923
    • Prange, R.1    Clemen, A.2    Streeck, R.E.3
  • 119
    • 0024635927 scopus 로고
    • Characterization of the major duck hepatitis B virus core particle protein
    • Pugh J, Zweidler A, Summers J (1989) Characterization of the major duck hepatitis B virus core particle protein J Virol 63: 1371-1376
    • (1989) J Virol , vol.63 , pp. 1371-1376
    • Pugh, J.1    Zweidler, A.2    Summers, J.3
  • 120
    • 0028142830 scopus 로고
    • Identification of hepatitis B virus core protein regions exposed or internalized at the surface of HBcAg particles by scanning with monoclonal antibodies
    • Pushko P, Sällberg M, Borisova G, Ruden U, Bichko V, Wahren B, Pumpens P, Magnius L (1994) Identification of hepatitis B virus core protein regions exposed or internalized at the surface of HBcAg particles by scanning with monoclonal antibodies Virology 202: 912-20
    • (1994) Virology , vol.202 , pp. 912-920
    • Pushko, P.1    Sällberg, M.2    Borisova, G.3    Ruden, U.4    Bichko, V.5    Wahren, B.6    Pumpens, P.7    Magnius, L.8
  • 121
    • 0025061039 scopus 로고
    • Mutational analysis of the hepatitis B virus P gene product. domain structure and RNase H activity
    • Radziwill G, Tucker W, Schaller H (1990) Mutational analysis of the hepatitis B virus P gene product. domain structure and RNase H activity. J Virol 64: 613-620
    • (1990) J Virol , vol.64 , pp. 613-620
    • Radziwill, G.1    Tucker, W.2    Schaller, H.3
  • 122
    • 0028842546 scopus 로고
    • Distinct requirements for primary sequence in the 5′-and 3′- part of a bulge in the hepatitis B virus RNA encapsidation signal revealed by a combined in vivo selection/in vitro amplification system
    • Rieger A, Nassal M (1995) Distinct requirements for primary sequence in the 5′-and 3′- part of a bulge in the hepatitis B virus RNA encapsidation signal revealed by a combined in vivo selection/in vitro amplification system. Nucl Acids Res 23 3309-3315
    • (1995) Nucl Acids Res , vol.23 , pp. 3309-3315
    • Rieger, A.1    Nassal, M.2
  • 123
    • 0029655242 scopus 로고    scopus 로고
    • Specific hepatitis B virus minus-strand DNA synthesis requires only the 5′-encapsidation signal and the 3′- proximal direct repeat DR1*
    • Rieger A, Nassal M (1996) Specific hepatitis B virus minus-strand DNA synthesis requires only the 5′-encapsidation signal and the 3′- proximal direct repeat DR1*. J Virol 70 585-589
    • (1996) J Virol , vol.70 , pp. 585-589
    • Rieger, A.1    Nassal, M.2
  • 124
    • 0026506254 scopus 로고
    • Duck hepatitis B virus infection of hepatocytes is not dependent on low pH
    • Rigg RJ, Schaller H (1992) Duck hepatitis B virus infection of hepatocytes is not dependent on low pH. J Virol 66: 2829-2836
    • (1992) J Virol , vol.66 , pp. 2829-2836
    • Rigg, R.J.1    Schaller, H.2
  • 126
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman JE (1994) Mechanisms of intracellular protein transport Nature 372: 55-63
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 127
    • 0027950659 scopus 로고
    • Pararetroviruses and retroviruses: A comparative review of viral structure and gene expression strategies
    • Rothnie HM, Chapdelaine Y, Hohn T (1994) Pararetroviruses and retroviruses: a comparative review of viral structure and gene expression strategies Adv Virus Res 44: 1-67
    • (1994) Adv Virus Res , vol.44 , pp. 1-67
    • Rothnie, H.M.1    Chapdelaine, Y.2    Hohn, T.3
  • 128
    • 0027294692 scopus 로고
    • Ribonucleoprotein complexes of hepatitis delta virus
    • Ryu WS, Netter HJ, Bayer M, Taylor J (1993) Ribonucleoprotein complexes of hepatitis delta virus J Virol 67: 3281-3287
    • (1993) J Virol , vol.67 , pp. 3281-3287
    • Ryu, W.S.1    Netter, H.J.2    Bayer, M.3    Taylor, J.4
  • 129
    • 0025872501 scopus 로고
    • Characterisation of a linear binding site for a monoclonal antibody to hepatitis B core antigen
    • Sällberg M, Ruden U, Magnius LO, Harthus HP, Noah M, Wahren B (1991) Characterisation of a linear binding site for a monoclonal antibody to hepatitis B core antigen J Med Virol 33: 248-252
    • (1991) J Med Virol , vol.33 , pp. 248-252
    • Sällberg, M.1    Ruden, U.2    Magnius, L.O.3    Harthus, H.P.4    Noah, M.5    Wahren, B.6
  • 130
    • 0024500103 scopus 로고
    • Antigenic determinants and functional domains in core antigen and e antigen from hepatitis B virus
    • Salfeld J, Pfaff E, Noah M, Schaller H (1989) Antigenic determinants and functional domains in core antigen and e antigen from hepatitis B virus. J Virol 63: 798-808
    • (1989) J Virol , vol.63 , pp. 798-808
    • Salfeld, J.1    Pfaff, E.2    Noah, M.3    Schaller, H.4
  • 131
    • 0025348681 scopus 로고
    • Lipid composition of hepatitis B virus surface antigen particles and the particle-producing human hepatoma cell lines
    • Satoh O, Umeda M, Imai H, Tunoo H, Inoue K (1990) Lipid composition of hepatitis B virus surface antigen particles and the particle-producing human hepatoma cell lines J Lipid Res 31 1293-1300
    • (1990) J Lipid Res , vol.31 , pp. 1293-1300
    • Satoh, O.1    Umeda, M.2    Imai, H.3    Tunoo, H.4    Inoue, K.5
  • 132
    • 0024381771 scopus 로고
    • The duck hepatitis B virus core protein contains a highly phosphorylated C terminus that is essential for replication but not for RNA packaging
    • Schlicht HJ, Bartenschlager R, Schaller H (1989a) The duck hepatitis B virus core protein contains a highly phosphorylated C terminus that is essential for replication but not for RNA packaging J Virol 63: 2995-3000
    • (1989) J Virol , vol.63 , pp. 2995-3000
    • Schlicht, H.J.1    Bartenschlager, R.2    Schaller, H.3
  • 133
    • 0024968115 scopus 로고
    • Synthesis and encapsidation of duck hepatitis B virus reverse transcriptase do not require formation of core-polymerase fusion proteins
    • Schlicht HJ, Radziwill G, Schaller H (1989b) Synthesis and encapsidation of duck hepatitis B virus reverse transcriptase do not require formation of core-polymerase fusion proteins. Cell 56: 85-92
    • (1989) Cell , vol.56 , pp. 85-92
    • Schlicht, H.J.1    Radziwill, G.2    Schaller, H.3
  • 135
    • 0027463464 scopus 로고
    • Structure of hepatitis B virus core and e-antigen. A single precore amino acid prevents nucleocapsid assembly
    • Schödel F, Peterson D, Zheng J, Jones JE, Hughes JL, Milich DR (1993) Structure of hepatitis B virus core and e-antigen. A single precore amino acid prevents nucleocapsid assembly. J Biol Chem 268: 1332-1337
    • (1993) J Biol Chem , vol.268 , pp. 1332-1337
    • Schödel, F.1    Peterson, D.2    Zheng, J.3    Jones, J.E.4    Hughes, J.L.5    Milich, D.R.6
  • 136
    • 0027164918 scopus 로고
    • Recombinant human hepatitis B virus reverse transcriptase is active in the absence of the nucleocapsid or the viral replication origin, DR1
    • Seifer M, Standring DN (1993) Recombinant human hepatitis B virus reverse transcriptase is active in the absence of the nucleocapsid or the viral replication origin, DR1. J Virol 67: 4513-4520
    • (1993) J Virol , vol.67 , pp. 4513-4520
    • Seifer, M.1    Standring, D.N.2
  • 137
    • 0028136709 scopus 로고
    • A protease-sensitve hinge linking the two domains of the hepatitis B virus core protein is exposed on the viral capsid surface
    • Seifer M, Standring DN (1994) A protease-sensitve hinge linking the two domains of the hepatitis B virus core protein is exposed on the viral capsid surface. J Virol 68: 5548-5555
    • (1994) J Virol , vol.68 , pp. 5548-5555
    • Seifer, M.1    Standring, D.N.2
  • 138
    • 0028821810 scopus 로고
    • Assembly and antigenicity of hepatitis B virus core particles
    • Seifer M, Standring DN (1995) Assembly and antigenicity of hepatitis B virus core particles. Intervirology 38: 47-62
    • (1995) Intervirology , vol.38 , pp. 47-62
    • Seifer, M.1    Standring, D.N.2
  • 139
    • 0027398488 scopus 로고
    • A micromolar pool of antigenically distinct precursors is required to initiate cooperative assembly of hepatitis B virus capsids in Xenopus oocytes
    • Seifer M, Zhou S, Standring DN (1993) A micromolar pool of antigenically distinct precursors is required to initiate cooperative assembly of hepatitis B virus capsids in Xenopus oocytes. J Virol 67: 249-257
    • (1993) J Virol , vol.67 , pp. 249-257
    • Seifer, M.1    Zhou, S.2    Standring, D.N.3
  • 140
    • 0026717490 scopus 로고
    • Preferential ribosomal scanning is involved in the differential synthesis of the hepatitis B viral surface antigens from subgenomic transcripts
    • Sheu SY, Lo SJ (1992) Preferential ribosomal scanning is involved in the differential synthesis of the hepatitis B viral surface antigens from subgenomic transcripts. Virology 188: 353-357
    • (1992) Virology , vol.188 , pp. 353-357
    • Sheu, S.Y.1    Lo, S.J.2
  • 141
    • 0024245271 scopus 로고
    • Secreted hepatitis B surface antigen polypeptides are derived from a transmembrane precursor
    • Simon K, Lingappa VR, Ganem D (1988) Secreted hepatitis B surface antigen polypeptides are derived from a transmembrane precursor. J Cell Biol 107 2163-2168
    • (1988) J Cell Biol , vol.107 , pp. 2163-2168
    • Simon, K.1    Lingappa, V.R.2    Ganem, D.3
  • 142
    • 0021924489 scopus 로고
    • Comparative sequence analysis of duck and human hepatitis B virus genomes
    • Sprengel R, Kuhn C, Will H, Schaller H (1985) Comparative sequence analysis of duck and human hepatitis B virus genomes. J Med Virol 15: 323-333
    • (1985) J Med Virol , vol.15 , pp. 323-333
    • Sprengel, R.1    Kuhn, C.2    Will, H.3    Schaller, H.4
  • 143
    • 0023803399 scopus 로고
    • Isolation and characterization of a hepatitis B virus endemic in herons
    • Sprengel R, Kaleta EF, Will H (1988) Isolation and characterization of a hepatitis B virus endemic in herons. J Virol 62: 3832-3839
    • (1988) J Virol , vol.62 , pp. 3832-3839
    • Sprengel, R.1    Kaleta, E.F.2    Will, H.3
  • 144
    • 0342372911 scopus 로고
    • The molecular biology of the hepatitis B virus core protein
    • McLachlan A (ed) CRC Press, Boca Raton
    • Standring DN (1991) The molecular biology of the hepatitis B virus core protein. In: McLachlan A (ed) Molecular biology of the hepatitis B virus. CRC Press, Boca Raton, pp 145-169
    • (1991) Molecular Biology of the Hepatitis B Virus , pp. 145-169
    • Standring, D.N.1
  • 145
    • 0026773810 scopus 로고
    • A topological model for hepatitis B surface antigen
    • Stirk HJ, Thornton JM, Howard CR (1992) A topological model for hepatitis B surface antigen. Intervirology 33 148-158
    • (1992) Intervirology , vol.33 , pp. 148-158
    • Stirk, H.J.1    Thornton, J.M.2    Howard, C.R.3
  • 146
    • 0019949367 scopus 로고
    • Replication of the genome of hepatitis B-like virus by reverse transcription of an RNA intermediate
    • Summers J, Mason WS (1982) Replication of the genome of hepatitis B-like virus by reverse transcription of an RNA intermediate. Cell 29: 403-415
    • (1982) Cell , vol.29 , pp. 403-415
    • Summers, J.1    Mason, W.S.2
  • 147
    • 0025334855 scopus 로고
    • Hepadnavirus envelope proteins regulate covatently closed circular DNA amplification
    • Summers J, Smith PM, Horwich AL (1990) Hepadnavirus envelope proteins regulate covatently closed circular DNA amplification. J Virol 64: 2819-2824
    • (1990) J Virol , vol.64 , pp. 2819-2824
    • Summers, J.1    Smith, P.M.2    Horwich, A.L.3
  • 148
    • 0025980689 scopus 로고
    • Morphogenetic and regulatory effects of mutations in the envelope proteins of an avian hepadnavirus
    • Summers J, Smith PM, Huang MJ, Yu MS (1991) Morphogenetic and regulatory effects of mutations in the envelope proteins of an avian hepadnavirus. J Virol 65: 1310-1317
    • (1991) J Virol , vol.65 , pp. 1310-1317
    • Summers, J.1    Smith, P.M.2    Huang, M.J.3    Yu, M.S.4
  • 149
    • 0028235728 scopus 로고
    • Incorporation of homologous and heterologous proteins into the envelope of Moloney murine leukemia virus
    • Suomalainen M, Garoff H (1994) Incorporation of homologous and heterologous proteins into the envelope of Moloney murine leukemia virus. J Virol 68: 4879-4889
    • (1994) J Virol , vol.68 , pp. 4879-4889
    • Suomalainen, M.1    Garoff, H.2
  • 150
    • 0027396860 scopus 로고
    • Role of the large hepatitis B virus envelope protein in infectivity of the hepatitis delta virion
    • Sureau C, Guerra B, Lanford R (1993) Role of the large hepatitis B virus envelope protein in infectivity of the hepatitis delta virion. J Virol 67:366-372
    • (1993) J Virol , vol.67 , pp. 366-372
    • Sureau, C.1    Guerra, B.2    Lanford, R.3
  • 151
    • 0027210553 scopus 로고
    • Expression of functional hepatitis B virus polymerase in yeast reveals it to be the sole viral protein required for correct initiation of reverse transcription
    • Tavis JE, Ganem D (1993) Expression of functional hepatitis B virus polymerase in yeast reveals it to be the sole viral protein required for correct initiation of reverse transcription. Proc Natl Acad Sci USA 90: 4107-4111
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 4107-4111
    • Tavis, J.E.1    Ganem, D.2
  • 153
    • 0023028191 scopus 로고
    • Formation of the pool of covalently closed circular viral DNA in hepadnavirus-infected cells
    • Tuttleman J, Pourcel C, Summers J (1986) Formation of the pool of covalently closed circular viral DNA in hepadnavirus-infected cells Cell 47 451-460
    • (1986) Cell , vol.47 , pp. 451-460
    • Tuttleman, J.1    Pourcel, C.2    Summers, J.3
  • 154
    • 0025879364 scopus 로고
    • Three envelope proteins of hepatitis B virus: Large S, middle S, and major S proteins needed for the formation of Dane particles
    • Ueda K, Tsurimoto T, Matsubara K (1991) Three envelope proteins of hepatitis B virus: large S, middle S, and major S proteins needed for the formation of Dane particles. J Virol 65: 3521-3529
    • (1991) J Virol , vol.65 , pp. 3521-3529
    • Ueda, K.1    Tsurimoto, T.2    Matsubara, K.3
  • 155
    • 0024448087 scopus 로고
    • Lipid traffic in animal cells
    • van Meer G (1989) Lipid traffic in animal cells Annu Rev Cell Biol 5: 247-275
    • (1989) Annu Rev Cell Biol , vol.5 , pp. 247-275
    • Van Meer, G.1
  • 156
    • 0026493753 scopus 로고
    • The reverse transcriptase of hepatitis B virus acts as a protein primer for viral DNA synthesis
    • Wang GH, Seeger C (1992) The reverse transcriptase of hepatitis B virus acts as a protein primer for viral DNA synthesis. Cell 71: 663-670
    • (1992) Cell , vol.71 , pp. 663-670
    • Wang, G.H.1    Seeger, C.2
  • 157
    • 0027494086 scopus 로고
    • Novel mechanism for reverse transcription in hepatitis B viruses
    • Wang GH, Seeger C (1993) Novel mechanism for reverse transcription in hepatitis B viruses J Virol 67: 6507-6512
    • (1993) J Virol , vol.67 , pp. 6507-6512
    • Wang, G.H.1    Seeger, C.2
  • 158
    • 0027141464 scopus 로고
    • The Mauriceville plasmid reverse transcriptase can initiate cDNA synthesis de novo and may be related to reverse transcriptase and DNA polymerase progenitor
    • Wang H, Lambowitz AM (1993) The Mauriceville plasmid reverse transcriptase can initiate cDNA synthesis de novo and may be related to reverse transcriptase and DNA polymerase progenitor. Cell 75: 1071-1081
    • (1993) Cell , vol.75 , pp. 1071-1081
    • Wang, H.1    Lambowitz, A.M.2
  • 159
    • 0027464971 scopus 로고
    • Relevance of cysteine residues for biosynthesis and antigenicity of human hepatitis B virus e protein
    • Wasenauer G, Köck J, Schlicht HJ (1993) Relevance of cysteine residues for biosynthesis and antigenicity of human hepatitis B virus e protein. J Virol 67: 1315-1321
    • (1993) J Virol , vol.67 , pp. 1315-1321
    • Wasenauer, G.1    Köck, J.2    Schlicht, H.J.3
  • 160
    • 0025329760 scopus 로고
    • In hepatocytes infected with duck hepatitis B virus, the template for viral RNA synthesis is amplified by an intracellular pathway
    • Wu TT, Coates L, Aldrich C, Summers J, Mason W (1990) In hepatocytes infected with duck hepatitis B virus, the template for viral RNA synthesis is amplified by an intracellular pathway. Virology 175: 255-261
    • (1990) Virology , vol.175 , pp. 255-261
    • Wu, T.T.1    Coates, L.2    Aldrich, C.3    Summers, J.4    Mason, W.5
  • 161
    • 0028012463 scopus 로고
    • Capsid assembly and involved function of twelve core protein mutants of duck hepatitis B virus
    • Yang W, Guo J, Ying Z, Hua S, Dong W, Chen H (1994) Capsid assembly and involved function of twelve core protein mutants of duck hepatitis B virus. J Virol 68: 338-345
    • (1994) J Virol , vol.68 , pp. 338-345
    • Yang, W.1    Guo, J.2    Ying, Z.3    Hua, S.4    Dong, W.5    Chen, H.6
  • 162
    • 0025251613 scopus 로고
    • The arginine-rich domain of hepatitits B virus core and precore proteins contains a signal for nuclear transport
    • Yeh CT, Liaw YF, Ou JH (1990) The arginine-rich domain of hepatitits B virus core and precore proteins contains a signal for nuclear transport. J Virol 64: 6141-6147
    • (1990) J Virol , vol.64 , pp. 6141-6147
    • Yeh, C.T.1    Liaw, Y.F.2    Ou, J.H.3
  • 163
    • 0027255244 scopus 로고
    • Cell cycle regulation of nuclear localization of hepatitis B virus core protein
    • Yeh CT, Wong SW, Fung YK, Ou JH (1993) Cell cycle regulation of nuclear localization of hepatitis B virus core protein. Proc Natl Acad Sci USA 90: 6459-6463
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 6459-6463
    • Yeh, C.T.1    Wong, S.W.2    Fung, Y.K.3    Ou, J.H.4
  • 164
    • 0025773026 scopus 로고
    • A domain of the hepadnavirus capsid protein is specifically required for DNA maturation and virus assembly
    • Yu M, Summers J (1991) A domain of the hepadnavirus capsid protein is specifically required for DNA maturation and virus assembly. J Virol 65: 2511-2517
    • (1991) J Virol , vol.65 , pp. 2511-2517
    • Yu, M.1    Summers, J.2
  • 165
    • 0028358552 scopus 로고
    • Multiple functions of capsid protein phosphorylation in duck hepatitis B virus replication
    • Yu M, Summers J (1994) Multiple functions of capsid protein phosphorylation in duck hepatitis B virus replication. J Virol 68: 4341-4348
    • (1994) J Virol , vol.68 , pp. 4341-4348
    • Yu, M.1    Summers, J.2
  • 166
    • 0026027726 scopus 로고
    • The C-terminal half of the preS1 region is essential for the secretion of human hepatitis B virus large S protein devoid of the N-terminal retention sequence
    • Yu XM (1991) The C-terminal half of the preS1 region is essential for the secretion of human hepatitis B virus large S protein devoid of the N-terminal retention sequence Virology 181: 386-389
    • (1991) Virology , vol.181 , pp. 386-389
    • Yu, X.M.1
  • 167
    • 0026090336 scopus 로고
    • Peptide mapping of neutralizing and nonneutralizing epitopes of duck hepatitis B virus pre-S polypeptide
    • Yuasa S, Cheung RC, Pham Q, Robinson WS, Marion PL (1991) Peptide mapping of neutralizing and nonneutralizing epitopes of duck hepatitis B virus pre-S polypeptide. Virology 181: 14-21
    • (1991) Virology , vol.181 , pp. 14-21
    • Yuasa, S.1    Cheung, R.C.2    Pham, Q.3    Robinson, W.S.4    Marion, P.L.5
  • 168
    • 0026793044 scopus 로고
    • The structure of hepadnaviral core antigens Identification of free thiols and determination of the disulfide bonding pattern
    • Zheng J, Schödel F, Peterson DL (1992) The structure of hepadnaviral core antigens Identification of free thiols and determination of the disulfide bonding pattern. J Biol Chem 267: 9422-942
    • (1992) J Biol Chem , vol.267 , pp. 9422-9942
    • Zheng, J.1    Schödel, F.2    Peterson, D.L.3
  • 169
    • 0026483273 scopus 로고
    • Hepatitis B virus capsids are assembled from core protein dimers
    • Zhou S, Standring DN (1992) Hepatitis B virus capsids are assembled from core protein dimers Proc Natl Acad Sci USA 89 10046-10050
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10046-10050
    • Zhou, S.1    Standring, D.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.