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Volumn 89, Issue 5, 2015, Pages 2918-2930

Regulation of multiple stages of hepadnavirus replication by the carboxyl-terminal domain of viral core protein in trans

Author keywords

[No Author keywords available]

Indexed keywords

CORE PROTEIN; CYCLIN DEPENDENT KINASE 2; DOUBLE STRANDED DNA; KARYOPHERIN ALPHA; VIRUS DNA; CIRCULAR DNA; HEPATITIS B CORE ANTIGEN; MUTANT PROTEIN; PROTEIN BINDING; RECOMBINANT PROTEIN;

EID: 84923008599     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.03116-14     Document Type: Article
Times cited : (38)

References (51)
  • 1
    • 34547755447 scopus 로고    scopus 로고
    • Hepadnaviruses
    • Knipe DM, Howley PM (ed), Lippincott, Williams & Wilkins, Philadelphia, PA
    • Seeger C, Zoulim F, Mason WS. 2007. Hepadnaviruses, p 2977-3030. In Knipe DM, Howley PM (ed), Fields virology. Lippincott, Williams & Wilkins, Philadelphia, PA.
    • (2007) Fields virology , pp. 2977-3030
    • Seeger, C.1    Zoulim, F.2    Mason, W.S.3
  • 2
    • 0033152857 scopus 로고    scopus 로고
    • The crystal structure of the human hepatitis B virus capsid
    • Wynne SA, Crowther RA, Leslie AG. 1999. The crystal structure of the human hepatitis B virus capsid. Mol Cell 3:771-780. http://dx.doi.org/10.1016/S1097-2765(01)80009-5.
    • (1999) Mol Cell , vol.3 , pp. 771-780
    • Wynne, S.A.1    Crowther, R.A.2    Leslie, A.G.3
  • 3
    • 0030937751 scopus 로고    scopus 로고
    • Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy
    • Conway JF, Cheng N, Zlotnick A, Wingfield PT, Stahl SJ, Steven AC. 1997. Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy. Nature 386:91-94. http://dx.doi.org/10.1038/386091a0.
    • (1997) Nature , vol.386 , pp. 91-94
    • Conway, J.F.1    Cheng, N.2    Zlotnick, A.3    Wingfield, P.T.4    Stahl, S.J.5    Steven, A.C.6
  • 4
    • 0019949367 scopus 로고
    • Replication of the genome of a hepatitis B-like virus by reverse transcription of an RNA intermediate
    • Summers J, Mason WS. 1982. Replication of the genome of a hepatitis B-like virus by reverse transcription of an RNA intermediate. Cell 29:403-415. http://dx.doi.org/10.1016/0092-8674(82)90157-X.
    • (1982) Cell , vol.29 , pp. 403-415
    • Summers, J.1    Mason, W.S.2
  • 5
    • 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. http://dx.doi.org/10.1038/344552a0.
    • (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
  • 6
    • 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
  • 7
    • 84892451874 scopus 로고    scopus 로고
    • Hepatitis B virus reverse transcriptase: diverse functions as classical and emerging targets for antiviral intervention
    • Jones SA, Hu J. 2013. Hepatitis B virus reverse transcriptase: diverse functions as classical and emerging targets for antiviral intervention. Emerg Microbes Infect 2:e56. http://dx.doi.org/10.1038/emi.2013.56.
    • (2013) Emerg Microbes Infect , vol.2
    • Jones, S.A.1    Hu, J.2
  • 8
    • 0023028191 scopus 로고
    • Formation of the pool of covalently closed circular viral DNA in hepadnavirus-infected cells
    • Tuttleman JS, Pourcel C, Summers J. 1986. Formation of the pool of covalently closed circular viral DNA in hepadnavirus-infected cells. Cell 47:451-460. http://dx.doi.org/10.1016/0092-8674(86)90602-1.
    • (1986) Cell , vol.47 , pp. 451-460
    • Tuttleman, J.S.1    Pourcel, C.2    Summers, J.3
  • 9
    • 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 CE, Summers J, Mason WS. 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. http://dx.doi.org/10.1016/0042-6822(90)90206-7.
    • (1990) Virology , vol.175 , pp. 255-261
    • Wu, T.T.1    Coates, L.2    Aldrich, C.E.3    Summers, J.4    Mason, W.S.5
  • 10
    • 34249945560 scopus 로고    scopus 로고
    • Formation of hepatitis B virus covalently closed circular DNA: removal of genome-linked protein
    • Gao W, Hu J. 2007. Formation of hepatitis B virus covalently closed circular DNA: removal of genome-linked protein. J Virol 81:6164-6174. http://dx.doi.org/10.1128/JVI.02721-06.
    • (2007) J Virol , vol.81 , pp. 6164-6174
    • Gao, W.1    Hu, J.2
  • 11
    • 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
  • 12
    • 0026695732 scopus 로고
    • The arginine-rich domain of the hepatitis B virus core protein is required for pregenome encapsidation and productive viral positive-strand DNA synthesis but not for virus assembly
    • Nassal M. 1992. The arginine-rich domain of the hepatitis B virus core protein is required for pregenome encapsidation and productive viral 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
  • 13
    • 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. 1989. 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
  • 14
    • 0028355452 scopus 로고
    • Phosphorylation of the duck hepatitis B virus capsid protein associated with conformational changes in the C terminus
    • Yu M, Summers J. 1994. Phosphorylation of the duck hepatitis B virus capsid protein associated with conformational changes in the C terminus. J Virol 68:2965-2969.
    • (1994) J Virol , vol.68 , pp. 2965-2969
    • Yu, M.1    Summers, J.2
  • 15
    • 0028813109 scopus 로고
    • Phosphorylation and nuclear localization of the hepatitis B virus core protein: significance of serine in the three repeated SPRRR motifs
    • Liao W, Ou JH. 1995. Phosphorylation and nuclear localization of the hepatitis B virus core protein: significance of serine in the three repeated SPRRR motifs. J Virol 69:1025-1029.
    • (1995) J Virol , vol.69 , pp. 1025-1029
    • Liao, W.1    Ou, J.H.2
  • 16
    • 21144448515 scopus 로고    scopus 로고
    • Reverse transcription-associated dephosphorylation of hepadnavirus nucleocapsids
    • Perlman DH, Berg EA, O'Connor PB, Costello CE, Hu J. 2005. Reverse transcription-associated dephosphorylation of hepadnavirus nucleocapsids. Proc Natl Acad Sci USA 102:9020-9025. http://dx.doi.org/10.1073/pnas.0502138102.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 9020-9025
    • Perlman, D.H.1    Berg, E.A.2    O'Connor, P.B.3    Costello, C.E.4    Hu, J.5
  • 17
    • 84904876084 scopus 로고    scopus 로고
    • Phosphoacceptors threonine 162 and serines 170 and 178 within the carboxylterminal RRRS/T motif of the hepatitis B virus core protein make multiple contributions to hepatitis B virus replication
    • Jung J, Hwang SG, Chwae YJ, Park S, Shin HJ, Kim K. 2014. Phosphoacceptors threonine 162 and serines 170 and 178 within the carboxylterminal RRRS/T motif of the hepatitis B virus core protein make multiple contributions to hepatitis B virus replication. J Virol 88:8754-8767. http://dx.doi.org/10.1128/JVI.01343-14.
    • (2014) J Virol , vol.88 , pp. 8754-8767
    • Jung, J.1    Hwang, S.G.2    Chwae, Y.J.3    Park, S.4    Shin, H.J.5    Kim, K.6
  • 18
    • 0033526794 scopus 로고    scopus 로고
    • Roles of the three major phosphorylation sites of hepatitis B virus core protein in viral replication
    • Lan YT, Li J, Liao W, Ou J. 1999. Roles of the three major phosphorylation sites of hepatitis B virus core protein in viral replication. Virology 259:342-348. http://dx.doi.org/10.1006/viro.1999.9798.
    • (1999) Virology , vol.259 , pp. 342-348
    • Lan, Y.T.1    Li, J.2    Liao, W.3    Ou, J.4
  • 19
    • 79951903566 scopus 로고    scopus 로고
    • Serine phosphoacceptor sites within the core protein of hepatitis B virus contribute to genome replication pleiotropically
    • Lewellyn EB, Loeb DD. 2011. Serine phosphoacceptor sites within the core protein of hepatitis B virus contribute to genome replication pleiotropically. PLoS One 6:e17202. http://dx.doi.org/10.1371/journal.pone.0017202.
    • (2011) PLoS One , vol.6
    • Lewellyn, E.B.1    Loeb, D.D.2
  • 20
    • 0033999564 scopus 로고    scopus 로고
    • Core protein phosphorylation modulates pregenomic RNA encapsidation to different extents in human and duck hepatitis B viruses
    • Gazina EV, Fielding JE, Lin B, Anderson DA. 2000. Core protein phosphorylation modulates pregenomic RNA encapsidation to different extents in human and duck hepatitis B viruses. J Virol 74:4721-4728. http://dx.doi.org/10.1128/JVI.74.10.4721-4728.2000.
    • (2000) J Virol , vol.74 , pp. 4721-4728
    • Gazina, E.V.1    Fielding, J.E.2    Lin, B.3    Anderson, D.A.4
  • 21
    • 33846813972 scopus 로고    scopus 로고
    • Regulation of hepadnavirus reverse transcription by dynamic nucleocapsid phosphorylation
    • Basagoudanavar SH, Perlman DH, Hu J. 2007. Regulation of hepadnavirus reverse transcription by dynamic nucleocapsid phosphorylation. J Virol 81:1641-1649. http://dx.doi.org/10.1128/JVI.01671-06.
    • (2007) J Virol , vol.81 , pp. 1641-1649
    • Basagoudanavar, S.H.1    Perlman, D.H.2    Hu, J.3
  • 22
    • 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
  • 23
    • 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
  • 24
    • 0033526096 scopus 로고    scopus 로고
    • Phosphorylation-dependent binding of hepatitis B virus core particles to the nuclear pore complex
    • Kann M, Sodeik B, Vlachou A, Gerlich WH, Helenius A. 1999. Phosphorylation-dependent binding of hepatitis B virus core particles to the nuclear pore complex. J Cell Biol 145:45-55. http://dx.doi.org/10.1083/jcb.145.1.45.
    • (1999) J Cell Biol , vol.145 , pp. 45-55
    • Kann, M.1    Sodeik, B.2    Vlachou, A.3    Gerlich, W.H.4    Helenius, A.5
  • 25
    • 0036318795 scopus 로고    scopus 로고
    • Identification of SRPK1 and SRPK2 as the major cellular protein kinases phosphorylating hepatitis B virus core protein
    • Daub H, Blencke S, Habenberger P, Kurtenbach A, Dennenmoser J, Wissing J, Ullrich A, Cotten M. 2002. Identification of SRPK1 and SRPK2 as the major cellular protein kinases phosphorylating hepatitis B virus core protein. J Virol 76:8124-8137. http://dx.doi.org/10.1128/JVI.76.16.8124-8137.2002.
    • (2002) J Virol , vol.76 , pp. 8124-8137
    • Daub, H.1    Blencke, S.2    Habenberger, P.3    Kurtenbach, A.4    Dennenmoser, J.5    Wissing, J.6    Ullrich, A.7    Cotten, M.8
  • 26
    • 84869133121 scopus 로고    scopus 로고
    • Cyclin-dependent kinase 2 phosphorylates S/T-P sites in the hepadnavirus core protein C-terminal domain and is incorporated into viral capsids
    • Ludgate L, Ning X, Nguyen DH, Adams C, Mentzer L, Hu J. 2012. Cyclin-dependent kinase 2 phosphorylates S/T-P sites in the hepadnavirus core protein C-terminal domain and is incorporated into viral capsids. J Virol 86:12237-12250. http://dx.doi.org/10.1128/JVI.01218-12.
    • (2012) J Virol , vol.86 , pp. 12237-12250
    • Ludgate, L.1    Ning, X.2    Nguyen, D.H.3    Adams, C.4    Mentzer, L.5    Hu, J.6
  • 27
    • 0018835442 scopus 로고
    • Protein kinase activity in hepatitis B virus
    • Albin C, Robinson W. 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.2
  • 28
    • 84891552006 scopus 로고    scopus 로고
    • Maturation-associated destabilization of hepatitis B virus nucleocapsid
    • Cui X, Ludgate L, Ning X, Hu J. 2013. Maturation-associated destabilization of hepatitis B virus nucleocapsid. J Virol 87:11494-11503. http://dx.doi.org/10.1128/JVI.01912-13.
    • (2013) J Virol , vol.87 , pp. 11494-11503
    • Cui, X.1    Ludgate, L.2    Ning, X.3    Hu, J.4
  • 29
    • 36049013787 scopus 로고    scopus 로고
    • Characterization of the intracellular deproteinized relaxed circular DNA of hepatitis B virus: an intermediate of covalently closed circular DNA formation
    • Guo H, Jiang D, Zhou T, Cuconati A, Block TM, Guo JT. 2007. Characterization of the intracellular deproteinized relaxed circular DNA of hepatitis B virus: an intermediate of covalently closed circular DNA formation. J Virol 81:12472-12484. http://dx.doi.org/10.1128/JVI.01123-07.
    • (2007) J Virol , vol.81 , pp. 12472-12484
    • Guo, H.1    Jiang, D.2    Zhou, T.3    Cuconati, A.4    Block, T.M.5    Guo, J.T.6
  • 30
    • 0042692926 scopus 로고    scopus 로고
    • Nuclear import of hepatitis B virus capsids and release of the viral genome
    • Rabe B, Vlachou A, Pante N, Helenius A, Kann M. 2003. Nuclear import of hepatitis B virus capsids and release of the viral genome. Proc Natl Acad Sci USA 100:9849-9854. http://dx.doi.org/10.1073/pnas.1730940100.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 9849-9854
    • Rabe, B.1    Vlachou, A.2    Pante, N.3    Helenius, A.4    Kann, M.5
  • 32
    • 0026008004 scopus 로고
    • Hepatitis B virus core antigen has two nuclear localization sequences in the arginine-rich carboxyl terminus
    • Eckhardt SG, Milich DR, McLachlan A. 1991. Hepatitis B virus core antigen has two nuclear localization sequences in the arginine-rich carboxyl 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
  • 33
    • 0029120509 scopus 로고
    • A single serine mutation on the nuclear localization signal of hepatitis B virus core protein abolishes the inhibition of nuclear transport by surface proteins
    • Yeh CT, Chu CM, Liaw YF. 1995. A single serine mutation on the nuclear localization signal of hepatitis B virus core protein abolishes the inhibition of nuclear transport by surface proteins. Biochem Biophys Res Commun 213:1068-1074. http://dx.doi.org/10.1006/bbrc.1995.2236.
    • (1995) Biochem Biophys Res Commun , vol.213 , pp. 1068-1074
    • Yeh, C.T.1    Chu, C.M.2    Liaw, Y.F.3
  • 34
    • 0025251613 scopus 로고
    • The arginine-rich domain of hepatitis B virus precore and core proteins contains a signal for nuclear transport
    • Yeh CT, Liaw YF, Ou JH. 1990. The arginine-rich domain of hepatitis B virus precore and core 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
  • 35
    • 78449260869 scopus 로고    scopus 로고
    • Nuclear export and import of human hepatitis B virus capsid protein and particles
    • Li HC, Huang EY, Su PY, Wu SY, Yang CC, Lin YS, Chang WC, Shih C. 2010. Nuclear export and import of human hepatitis B virus capsid protein and particles. PLoS Pathog 6:e1001162. http://dx.doi.org/10.1371/journal.ppat.1001162.
    • (2010) PLoS Pathog , vol.6
    • Li, H.C.1    Huang, E.Y.2    Su, P.Y.3    Wu, S.Y.4    Yang, C.C.5    Lin, Y.S.6    Chang, W.C.7    Shih, C.8
  • 36
    • 0035132753 scopus 로고    scopus 로고
    • Signals for bidirectional nucleocytoplasmic transport in the duck hepatitis B virus capsid protein
    • Mabit H, Breiner KM, Knaust A, Zachmann-Brand B, Schaller H. 2001. Signals for bidirectional nucleocytoplasmic transport in the duck hepatitis B virus capsid protein. J Virol 75:1968-1977. http://dx.doi.org/10.1128/JVI.75.4.1968-1977.2001.
    • (2001) J Virol , vol.75 , pp. 1968-1977
    • Mabit, H.1    Breiner, K.M.2    Knaust, A.3    Zachmann-Brand, B.4    Schaller, H.5
  • 37
    • 84055207539 scopus 로고    scopus 로고
    • Phosphorylation state-dependent interactions of hepadnavirus core protein with host factors
    • Ludgate L, Adams C, Hu J. 2011. Phosphorylation state-dependent interactions of hepadnavirus core protein with host factors. PLoS One 6:e29566. http://dx.doi.org/10.1371/journal.pone.0029566.
    • (2011) PLoS One , vol.6
    • Ludgate, L.1    Adams, C.2    Hu, J.3
  • 38
    • 0025334855 scopus 로고
    • Hepadnavirus envelope proteins regulate covalently closed circular DNA amplification
    • Summers J, Smith PM, Horwich AL. 1990. Hepadnavirus envelope proteins regulate covalently 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
  • 39
    • 0037025366 scopus 로고    scopus 로고
    • Role of p50/CDC37 in hepadnavirus assembly and replication
    • Wang X, Grammatikakis N, Hu J. 2002. Role of p50/CDC37 in hepadnavirus assembly and replication. J Biol Chem 277:24361-24367. http://dx.doi.org/10.1074/jbc.M202198200.
    • (2002) J Biol Chem , vol.277 , pp. 24361-24367
    • Wang, X.1    Grammatikakis, N.2    Hu, J.3
  • 40
    • 0026579879 scopus 로고
    • Rapid resolution of duck hepatitis B virus infections occurs after massive hepatocellular involvement
    • Jilbert AR, Wu TT, England JM, Hall PM, Carp NZ, O'Connell AP, Mason WS. 1992. Rapid resolution of duck hepatitis B virus infections occurs after massive hepatocellular involvement. J Virol 66:1377-1388.
    • (1992) J Virol , vol.66 , pp. 1377-1388
    • Jilbert, A.R.1    Wu, T.T.2    England, J.M.3    Hall, P.M.4    Carp, N.Z.5    O'Connell, A.P.6    Mason, W.S.7
  • 41
    • 34247635482 scopus 로고    scopus 로고
    • Deamination-independent inhibition of hepatitis B virus reverse transcription by APOBEC3G
    • Nguyen DH, Gummuluru S, Hu J. 2007. Deamination-independent inhibition of hepatitis B virus reverse transcription by APOBEC3G. J Virol 81:4465-4472. http://dx.doi.org/10.1128/JVI.02510-06.
    • (2007) J Virol , vol.81 , pp. 4465-4472
    • Nguyen, D.H.1    Gummuluru, S.2    Hu, J.3
  • 42
    • 0014202537 scopus 로고
    • Selective extraction of polyoma DNA from infected mouse cell cultures
    • Hirt B. 1967. Selective extraction of polyoma DNA from infected mouse cell cultures. J Mol Biol 26:365-369. http://dx.doi.org/10.1016/0022-2836(67)90307-5.
    • (1967) J Mol Biol , vol.26 , pp. 365-369
    • Hirt, B.1
  • 43
    • 0037302268 scopus 로고    scopus 로고
    • Conditional replication of duck hepatitis B virus in hepatoma cells
    • Guo JT, Pryce M, Wang X, Barrasa MI, Hu J, Seeger C. 2003. Conditional replication of duck hepatitis B virus in hepatoma cells. J Virol 77: 1885-1893. http://dx.doi.org/10.1128/JVI.77.3.1885-1893.2003.
    • (2003) J Virol , vol.77 , pp. 1885-1893
    • Guo, J.T.1    Pryce, M.2    Wang, X.3    Barrasa, M.I.4    Hu, J.5    Seeger, C.6
  • 44
    • 8644249753 scopus 로고    scopus 로고
    • Requirement of heat shock protein 90 for human hepatitis B virus reverse transcriptase function
    • Hu J, Flores D, Toft D, Wang X, Nguyen D. 2004. Requirement of heat shock protein 90 for human hepatitis B virus reverse transcriptase function. J Virol 78:13122-13131. http://dx.doi.org/10.1128/JVI.78.23.13122-13131.2004.
    • (2004) J Virol , vol.78 , pp. 13122-13131
    • Hu, J.1    Flores, D.2    Toft, D.3    Wang, X.4    Nguyen, D.5
  • 45
    • 0037302481 scopus 로고    scopus 로고
    • Duck hepatitis B virus virion secretion requires a double-stranded DNA genome
    • Perlman D, Hu J. 2003. Duck hepatitis B virus virion secretion requires a double-stranded DNA genome. J Virol 77:2287-2294. http://dx.doi.org/10.1128/JVI.77.3.2287-2294.2003.
    • (2003) J Virol , vol.77 , pp. 2287-2294
    • Perlman, D.1    Hu, J.2
  • 46
    • 80053460800 scopus 로고    scopus 로고
    • Secretion of genome-free hepatitis B virus-single strand blocking model for virion morphogenesis of para-retrovirus
    • Ning X, Nguyen D, Mentzer L, Adams C, Lee H, Ashley R, Hafenstein S, Hu J. 2011. Secretion of genome-free hepatitis B virus-single strand blocking model for virion morphogenesis of para-retrovirus. PLoS Pathog 7:e1002255. http://dx.doi.org/10.1371/journal.ppat.1002255.
    • (2011) PLoS Pathog , vol.7
    • Ning, X.1    Nguyen, D.2    Mentzer, L.3    Adams, C.4    Lee, H.5    Ashley, R.6    Hafenstein, S.7    Hu, J.8
  • 47
    • 0031060322 scopus 로고    scopus 로고
    • Posttranscriptional regulation of hepatitis B virus replication by the precore protein
    • Scaglioni PP, Melegari M, Wands JR. 1997. Posttranscriptional regulation of hepatitis B virus replication by the precore protein. J Virol 71:345-353.
    • (1997) J Virol , vol.71 , pp. 345-353
    • Scaglioni, P.P.1    Melegari, M.2    Wands, J.R.3
  • 48
    • 0028145857 scopus 로고
    • Construction of avian hepadnavirus variants with enhanced replication and cytopathicity in primary hepatocytes
    • Lenhoff RJ, Summers J. 1994. Construction of avian hepadnavirus variants with enhanced replication and cytopathicity in primary hepatocytes. J Virol 68:5706-5713.
    • (1994) J Virol , vol.68 , pp. 5706-5713
    • Lenhoff, R.J.1    Summers, J.2
  • 49
    • 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
  • 50
    • 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
  • 51
    • 78149319907 scopus 로고    scopus 로고
    • Generation of covalently closed circular DNA of hepatitis B viruses via intracellular recycling is regulated in a virus specific manner
    • Kock J, Rosler C, Zhang JJ, Blum HE, Nassal M, Thoma C. 2010. Generation of covalently closed circular DNA of hepatitis B viruses via intracellular recycling is regulated in a virus specific manner. PLoS Pathog 6:e1001082. http://dx.doi.org/10.1371/journal.ppat.1001082.
    • (2010) PLoS Pathog , vol.6
    • Kock, J.1    Rosler, C.2    Zhang, J.J.3    Blum, H.E.4    Nassal, M.5    Thoma, C.6


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