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Journal of Virology
Volumn 89, Issue 6, 2015, Pages 3275-3284
The interface between hepatitis B virus capsid proteins affects self- assembly, pregenomic RNA packaging, and reverse transcription
Author keywords

[No Author keywords available]
Indexed keywords

CAPSID PROTEIN; PREGENOMIC RNA; RNA; UNCLASSIFIED DRUG; RNA DIRECTED DNA POLYMERASE; VIRAL PROTEIN; VIRUS RNA;
EID: 84923163857     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.03545-14     Document Type: Article
Times cited : (83)
References (63)
  • 1
    • 84923158242 scopus 로고    scopus 로고
    • July 2004. Hepatitis B. Fact sheet no. 204
    • WHO. July 2004. Hepatitis B. Fact sheet no. 204. http://www.who.int/mediacentre/factsheets/fs204/en/.
  • 2
    • 33846555643 scopus 로고    scopus 로고
    • Antiviral therapy and resistance with hepatitis B virus infection
    • Tillmann HL. 2007. Antiviral therapy and resistance with hepatitis B virus infection. World J Gastroenterol 13:125-140. http://dx.doi.org/10.3748/wjg.v13.i1.125.
    • (2007) World J Gastroenterol , vol.13 , pp. 125-140
    • Tillmann, H.L.1
  • 3
    • 84885095261 scopus 로고    scopus 로고
    • Unraveling the complexity of hepatitis B virus: from molecular understanding to therapeutic strategy in 50 years
    • Liu B, Wen X, Huang C, Wei Y. 2013. Unraveling the complexity of hepatitis B virus: from molecular understanding to therapeutic strategy in 50 years. Int J Biochem Cell Biol 45:1987-1996. http://dx.doi.org/10.1016/j.biocel.2013.06.017.
    • (2013) Int J Biochem Cell Biol , vol.45 , pp. 1987-1996
    • Liu, B.1    Wen, X.2    Huang, C.3    Wei, Y.4
  • 4
    • 43049117085 scopus 로고    scopus 로고
    • Hepatitis B viruses: reverse transcription a different way
    • Nassal M. 2008. Hepatitis B viruses: reverse transcription a different way. Virus Res 134:235-249. http://dx.doi.org/10.1016/j.virusres.2007.12.024.
    • (2008) Virus Res , vol.134 , pp. 235-249
    • Nassal, M.1
  • 5
    • 33846514081 scopus 로고    scopus 로고
    • Hepatitis B virus replication
    • Beck J, Nassal M. 2007. Hepatitis B virus replication. World J Gastroenterol 13:48-64. http://dx.doi.org/10.3748/wjg.v13.i1.48.
    • (2007) World J Gastroenterol , vol.13 , pp. 48-64
    • Beck, J.1    Nassal, M.2
  • 6
    • 77953747864 scopus 로고    scopus 로고
    • Full-length hepatitis B virus core protein packages viral and heterologous RNA with similarly high levels of cooperativity
    • Porterfield JZ, Dhason MS, Loeb DD, Nassal M, Stray SJ, Zlotnick A. 2010. Full-length hepatitis B virus core protein packages viral and heterologous RNA with similarly high levels of cooperativity. J Virol 84:7174-7184. http://dx.doi.org/10.1128/JVI.00586-10.
    • (2010) J Virol , vol.84 , pp. 7174-7184
    • Porterfield, J.Z.1    Dhason, M.S.2    Loeb, D.D.3    Nassal, M.4    Stray, S.J.5    Zlotnick, A.6
  • 7
    • 67649393359 scopus 로고    scopus 로고
    • Electrostatic regulation of genome packaging in human hepatitis B virus
    • Jiang T, Wang ZG, Wu J. 2009. Electrostatic regulation of genome packaging in human hepatitis B virus. Biophys J 96:3065-3073. http://dx .doi.org/10.1016/j.bpj.2009.01.009.
    • (2009) Biophys J , vol.96 , pp. 3065-3073
    • Jiang, T.1    Wang, Z.G.2    Wu, J.3
  • 8
    • 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
  • 9
    • 1542316127 scopus 로고    scopus 로고
    • Hepatitis B virus infection-natural history and clinical consequences
    • Ganem D, Prince AM. 2004. Hepatitis B virus infection-natural history and clinical consequences. N Engl J Med 350:1118-1129. http://dx.doi .org/10.1056/NEJMra031087.
    • (2004) N Engl J Med , vol.350 , pp. 1118-1129
    • Ganem, D.1    Prince, A.M.2
  • 10
    • 84905665941 scopus 로고    scopus 로고
    • Encapsidated hepatitis B virus reverse transcriptase is poised on an ordered RNA lattice
    • Wang JC-Y, Nickens DG, Lentz TB, Loeb DD, Zlotnick A. 2014. Encapsidated hepatitis B virus reverse transcriptase is poised on an ordered RNA lattice. Proc Natl Acad Sci U S A 111:11329-11334. http://dx .doi.org/10.1073/pnas.1321424111.
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 11329-11334
    • Wang, J.C.-Y.1    Nickens, D.G.2    Lentz, T.B.3    Loeb, D.D.4    Zlotnick, A.5
  • 11
    • 77954489756 scopus 로고    scopus 로고
    • Control of hepatitis B virus at the level of transcription
    • Quasdorff M, Protzer U. 2010. Control of hepatitis B virus at the level of transcription. J Viral Hepat 17:527-536. http://dx.doi.org/10.1111/j.1365-2893.2010.01315.x.
    • (2010) J Viral Hepat , vol.17 , pp. 527-536
    • Quasdorff, M.1    Protzer, U.2
  • 13
    • 33646205969 scopus 로고    scopus 로고
    • Base pairing between the 5' half of epsilon and a cis-acting sequence, phi, makes a contribution to the synthesis of minus-strand DNA for human hepatitis B virus
    • Abraham TM, Loeb DD. 2006. Base pairing between the 5' half of epsilon and a cis-acting sequence, phi, makes a contribution to the synthesis of minus-strand DNA for human hepatitis B virus. J Virol 80:4380-4387. http://dx.doi.org/10.1128/JVI.80.9.4380-4387.2006.
    • (2006) J Virol , vol.80 , pp. 4380-4387
    • Abraham, T.M.1    Loeb, D.D.2
  • 14
    • 33750380899 scopus 로고    scopus 로고
    • Sequence identity of the direct repeats, DR1 and DR2, contributes to the discrimination between primer translocation and in situ priming during replication of the duck hepatitis B virus
    • Habig JW, Loeb DD. 2006. Sequence identity of the direct repeats, DR1 and DR2, contributes to the discrimination between primer translocation and in situ priming during replication of the duck hepatitis B virus. J Mol Biol 364:32-43. http://dx.doi.org/10.1016/j.jmb.2006.08.095.
    • (2006) J Mol Biol , vol.364 , pp. 32-43
    • Habig, J.W.1    Loeb, D.D.2
  • 15
    • 35448984203 scopus 로고    scopus 로고
    • The topology of hepatitis B virus pregenomic RNA promotes its replication
    • Abraham TM, Loeb DD. 2007. The topology of hepatitis B virus pregenomic RNA promotes its replication. J Virol 81:11577-11584. http://dx .doi.org/10.1128/JVI.01414-07.
    • (2007) J Virol , vol.81 , pp. 11577-11584
    • Abraham, T.M.1    Loeb, D.D.2
  • 16
    • 34250213863 scopus 로고    scopus 로고
    • The sequence of the RNA primer and the DNA template influence the initiation of plus-strand DNA synthesis in hepatitis B virus
    • Haines KM, Loeb DD. 2007. The sequence of the RNA primer and the DNA template influence the initiation of plus-strand DNA synthesis in hepatitis B virus. J Mol Biol 370:471-480. http://dx.doi.org/10.1016/j.jmb .2007.04.057.
    • (2007) J Mol Biol , vol.370 , pp. 471-480
    • Haines, K.M.1    Loeb, D.D.2
  • 17
    • 34249934195 scopus 로고    scopus 로고
    • Base pairing between cis-acting sequences contributes to template switching during plus-strand DNA synthesis in human hepatitis B virus
    • Lewellyn EB, Loeb DD. 2007. Base pairing between cis-acting sequences contributes to template switching during plus-strand DNA synthesis in human hepatitis B virus. J Virol 81:6207-6215. http://dx.doi.org/10.1128/JVI.00210-07.
    • (2007) J Virol , vol.81 , pp. 6207-6215
    • Lewellyn, E.B.1    Loeb, D.D.2
  • 18
    • 78649427977 scopus 로고    scopus 로고
    • cis-Acting sequences that contribute to synthesis of minus-strand DNA are not conserved between hepadnaviruses
    • Maguire ML, Loeb DD. 2010. cis-Acting sequences that contribute to synthesis of minus-strand DNA are not conserved between hepadnaviruses. J Virol 84:12824-12831. http://dx.doi.org/10.1128/JVI.01487-10.
    • (2010) J Virol , vol.84 , pp. 12824-12831
    • Maguire, M.L.1    Loeb, D.D.2
  • 19
    • 0018728482 scopus 로고
    • Morphological irregularities in Dane particle cores
    • Stannard LM, Hodgkiss M. 1979. Morphological irregularities in Dane particle cores. J Gen Virol 45:509-514. http://dx.doi.org/10.1099/0022-1317-45-2-509.
    • (1979) J Gen Virol , vol.45 , pp. 509-514
    • Stannard, L.M.1    Hodgkiss, M.2
  • 20
    • 0029950758 scopus 로고    scopus 로고
    • Dimorphism of hepatitis B virus capsids is strongly influenced by the C-terminus of the capsid protein
    • Zlotnick A, Cheng N, Conway JF, Booy FP, Steven AC, Stahl SJ, Wingfield PT. 1996. Dimorphism of hepatitis B virus capsids is strongly influenced by the C-terminus of the capsid protein. Biochemistry 35: 7412-7421. http://dx.doi.org/10.1021/bi9604800.
    • (1996) Biochemistry , vol.35 , pp. 7412-7421
    • Zlotnick, A.1    Cheng, N.2    Conway, J.F.3    Booy, F.P.4    Steven, A.C.5    Stahl, S.J.6    Wingfield, P.T.7
  • 21
    • 0029645618 scopus 로고
    • Evolutionary conservation in the hepatitis B virus core structure: comparison of human and duck cores
    • Kenney JM, von Bonsdorff CH, Nassal M, Fuller SD. 1995. Evolutionary conservation in the hepatitis B virus core structure: comparison of human and duck cores. Structure 3:1009-1019. http://dx.doi.org/10.1016/S0969-2126(01)00237-4.
    • (1995) Structure , vol.3 , pp. 1009-1019
    • Kenney, J.M.1    von Bonsdorff, C.H.2    Nassal, M.3    Fuller, S.D.4
  • 22
    • 0028307177 scopus 로고
    • Three-dimensional structure of hepatitis B virus core particles determined by electron cryomicroscopy
    • Crowther RA, Kiselev NA, Bottcher B, Berriman JA, Borisova GP, Ose V, Pumpens P. 1994. Three-dimensional structure of hepatitis B virus core particles determined by electron cryomicroscopy. Cell 77:943-950. http://dx.doi.org/10.1016/0092-8674(94)90142-2.
    • (1994) Cell , vol.77 , pp. 943-950
    • Crowther, R.A.1    Kiselev, N.A.2    Bottcher, B.3    Berriman, J.A.4    Borisova, G.P.5    Ose, V.6    Pumpens, P.7
  • 23
    • 0033105535 scopus 로고    scopus 로고
    • Separation and crystallization of T=3 and T=4 icosahedral complexes of the hepatitis B virus core protein
    • Zlotnick A, Palmer I, Stahl SJ, Steven AC, Wingfield PT. 1999. Separation and crystallization of T=3 and T=4 icosahedral complexes of the hepatitis B virus core protein. Acta Crystallogr D Biol Crystallogr 55:717-720. http://dx.doi.org/10.1107/S090744499801350X.
    • (1999) Acta Crystallogr D Biol Crystallogr , vol.55 , pp. 717-720
    • Zlotnick, A.1    Palmer, I.2    Stahl, S.J.3    Steven, A.C.4    Wingfield, P.T.5
  • 24
    • 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
  • 25
    • 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
  • 26
    • 78651384693 scopus 로고    scopus 로고
    • The arginine clusters of the carboxyterminal domain of the core protein of hepatitis B virus make pleiotropic contributions to genome replication
    • Lewellyn EB, Loeb DD. 2011. The arginine clusters of the carboxyterminal domain of the core protein of hepatitis B virus make pleiotropic contributions to genome replication. J Virol 85:1298-1309. http://dx.doi .org/10.1128/JVI.01957-10.
    • (2011) J Virol , vol.85 , pp. 1298-1309
    • Lewellyn, E.B.1    Loeb, D.D.2
  • 27
    • 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
  • 28
    • 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
  • 29
    • 22544476234 scopus 로고    scopus 로고
    • Hepatitis B virus DNA replication is coordinated by core protein serine phosphorylation and HBx expression
    • Melegari M, Wolf SK, Schneider RJ. 2005. Hepatitis B virus DNA replication is coordinated by core protein serine phosphorylation and HBx expression. J Virol 79:9810-9820. http://dx.doi.org/10.1128/JVI.79.15 .9810-9820.2005.
    • (2005) J Virol , vol.79 , pp. 9810-9820
    • Melegari, M.1    Wolf, S.K.2    Schneider, R.J.3
  • 30
    • 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 U S A 102:9020-9025. http://dx.doi.org/10.1073/pnas.0502138102.
    • (2005) Proc Natl Acad Sci U S A , 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
  • 31
    • 0036786867 scopus 로고    scopus 로고
    • Weak protein-protein interactions are sufficient to drive assembly of hepatitis B virus capsids
    • Ceres P, Zlotnick A. 2002. Weak protein-protein interactions are sufficient to drive assembly of hepatitis B virus capsids. Biochemistry 41: 11525-11531. http://dx.doi.org/10.1021/bi0261645.
    • (2002) Biochemistry , vol.41 , pp. 11525-11531
    • Ceres, P.1    Zlotnick, A.2
  • 32
    • 0035997081 scopus 로고    scopus 로고
    • Model-based analysis of assembly kinetics for virus capsids or other spherical polymers
    • Endres D, Zlotnick A. 2002. Model-based analysis of assembly kinetics for virus capsids or other spherical polymers. Biophys J 83:1217-1230. http://dx.doi.org/10.1016/S0006-3495(02)75245-4.
    • (2002) Biophys J , vol.83 , pp. 1217-1230
    • Endres, D.1    Zlotnick, A.2
  • 33
    • 0033517792 scopus 로고    scopus 로고
    • A theoretical model successfully identifies features of hepatitis B virus capsid assembly
    • Zlotnick A, Johnson JM, Wingfield PW, Stahl SJ, Endres D. 1999. A theoretical model successfully identifies features of hepatitis B virus capsid assembly. Biochemistry 38:14644-14652. http://dx.doi.org/10 .1021/bi991611a.
    • (1999) Biochemistry , vol.38 , pp. 14644-14652
    • Zlotnick, A.1    Johnson, J.M.2    Wingfield, P.W.3    Stahl, S.J.4    Endres, D.5
  • 34
    • 73949118464 scopus 로고    scopus 로고
    • Conformational changes in the hepatitis B virus core protein are consistent with a role for allostery in virus assembly
    • Packianathan C, Katen SP, Dann CE, III, Zlotnick A. 2010. Conformational changes in the hepatitis B virus core protein are consistent with a role for allostery in virus assembly. J Virol 84:1607-1615. http://dx.doi.org/10.1128/JVI.02033-09.
    • (2010) J Virol , vol.84 , pp. 1607-1615
    • Packianathan, C.1    Katen, S.P.2    Dann, C.E.3    Zlotnick, A.4
  • 35
    • 36549046150 scopus 로고    scopus 로고
    • Conformational equilibria and rates of localized motion within hepatitis B virus capsids
    • Hilmer JK, Zlotnick A, Bothner B. 2008. Conformational equilibria and rates of localized motion within hepatitis B virus capsids. J Mol Biol 375: 581-594. http://dx.doi.org/10.1016/j.jmb.2007.10.044.
    • (2008) J Mol Biol , vol.375 , pp. 581-594
    • Hilmer, J.K.1    Zlotnick, A.2    Bothner, B.3
  • 36
    • 84872128220 scopus 로고    scopus 로고
    • One protein, at least three structures, and many functions
    • Zlotnick A, Tan Z, Selzer L. 2013. One protein, at least three structures, and many functions. Structure 21:6-8. http://dx.doi.org/10.1016/j.str .2012.12.003.
    • (2013) Structure , vol.21 , pp. 6-8
    • Zlotnick, A.1    Tan, Z.2    Selzer, L.3
  • 37
    • 64349101502 scopus 로고    scopus 로고
    • A mutant hepatitis B virus core protein mimics inhibitors of icosahedral capsid self-assembly
    • Bourne CR, Katen SP, Fulz MR, Packianathan C, Zlotnick A. 2009. A mutant hepatitis B virus core protein mimics inhibitors of icosahedral capsid self-assembly. Biochemistry 48:1736-1742. http://dx.doi.org/10 .1021/bi801814y.
    • (2009) Biochemistry , vol.48 , pp. 1736-1742
    • Bourne, C.R.1    Katen, S.P.2    Fulz, M.R.3    Packianathan, C.4    Zlotnick, A.5
  • 38
    • 4143143115 scopus 로고    scopus 로고
    • Hepatitis B virus capsid assembly is enhanced by naturally occurring mutation F97L
    • Ceres P, Stray SJ, Zlotnick A. 2004. Hepatitis B virus capsid assembly is enhanced by naturally occurring mutation F97L. J Virol 78:9538-9543. http://dx.doi.org/10.1128/JVI.78.17.9538-9543.2004.
    • (2004) J Virol , vol.78 , pp. 9538-9543
    • Ceres, P.1    Stray, S.J.2    Zlotnick, A.3
  • 39
    • 0033064976 scopus 로고    scopus 로고
    • The mechanism of an immature secretion phenotype of a highly frequent nat-urally occurring missense mutation at codon 97 of human hepatitis B virus core antigen
    • Yuan TT, Sahu GK, Whitehead WE, Greenberg R, Shih C. 1999. The mechanism of an immature secretion phenotype of a highly frequent nat-urally occurring missense mutation at codon 97 of human hepatitis B virus core antigen. J Virol 73:5731-5740.
    • (1999) J Virol , vol.73 , pp. 5731-5740
    • Yuan, T.T.1    Sahu, G.K.2    Whitehead, W.E.3    Greenberg, R.4    Shih, C.5
  • 40
    • 20444421508 scopus 로고    scopus 로고
    • A heteroaryldihydropyrimidine activates and can misdirect hepatitis B virus capsid assembly
    • Stray SJ, Bourne CR, Punna S, Lewis WG, Finn MG, Zlotnick A. 2005. A heteroaryldihydropyrimidine activates and can misdirect hepatitis B virus capsid assembly. Proc Natl Acad Sci U S A 102:8138-8143. http://dx .doi.org/10.1073/pnas.0409732102.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 8138-8143
    • Stray, S.J.1    Bourne, C.R.2    Punna, S.3    Lewis, W.G.4    Finn, M.G.5    Zlotnick, A.6
  • 41
    • 33750704335 scopus 로고    scopus 로고
    • Global structural changes in hepatitis B capsids induced by the assembly effector HAP1
    • Bourne C, Finn MG, Zlotnick A. 2006. Global structural changes in hepatitis B capsids induced by the assembly effector HAP1. J Virol 80: 11055-11061. http://dx.doi.org/10.1128/JVI.00933-06.
    • (2006) J Virol , vol.80 , pp. 11055-11061
    • Bourne, C.1    Finn, M.G.2    Zlotnick, A.3
  • 42
    • 53749103127 scopus 로고    scopus 로고
    • Small-molecule effectors of hepatitis B virus capsid assembly give insight into virus life cycle
    • Bourne C, Lee S, Venkataiah B, Lee A, Korba B, Finn MG, Zlotnick A. 2008. Small-molecule effectors of hepatitis B virus capsid assembly give insight into virus life cycle. J Virol 82:10262-10270. http://dx.doi.org/10 .1128/JVI.01360-08.
    • (2008) J Virol , vol.82 , pp. 10262-10270
    • Bourne, C.1    Lee, S.2    Venkataiah, B.3    Lee, A.4    Korba, B.5    Finn, M.G.6    Zlotnick, A.7
  • 43
    • 78650580448 scopus 로고    scopus 로고
    • Trapping of hepatitis B virus capsid assembly intermediates by phenylpropenamide assembly accelerators
    • Katen SP, Chirapu SR, Finn MG, Zlotnick A. 2010. Trapping of hepatitis B virus capsid assembly intermediates by phenylpropenamide assembly accelerators. ACS Chem Biol 5:1125-1136. http://dx.doi.org/10.1021/cb100275b.
    • (2010) ACS Chem Biol , vol.5 , pp. 1125-1136
    • Katen, S.P.1    Chirapu, S.R.2    Finn, M.G.3    Zlotnick, A.4
  • 44
    • 84881478439 scopus 로고    scopus 로고
    • Assemblydirected antivirals differentially bind quasiequivalent pockets to modify hepatitis B virus capsid tertiary and quaternary structure
    • Katen SP, Tan Z, Chirapu SR, Finn MG, Zlotnick A. 2013. Assemblydirected antivirals differentially bind quasiequivalent pockets to modify hepatitis B virus capsid tertiary and quaternary structure. Structure 21: 1406-1416. http://dx.doi.org/10.1016/j.str.2013.06.013.
    • (2013) Structure , vol.21 , pp. 1406-1416
    • Katen, S.P.1    Tan, Z.2    Chirapu, S.R.3    Finn, M.G.4    Zlotnick, A.5
  • 45
    • 84874698351 scopus 로고    scopus 로고
    • Genetically altering the thermodynamics and kinetics of hepatitis B virus capsid assembly has profound effects on virus replication in cell culture
    • Tan Z, Maguire ML, Loeb DD, Zlotnick A. 2013. Genetically altering the thermodynamics and kinetics of hepatitis B virus capsid assembly has profound effects on virus replication in cell culture. J Virol 87:3208-3216. http://dx.doi.org/10.1128/JVI.03014-12.
    • (2013) J Virol , vol.87 , pp. 3208-3216
    • Tan, Z.1    Maguire, M.L.2    Loeb, D.D.3    Zlotnick, A.4
  • 47
    • 81755187190 scopus 로고    scopus 로고
    • A kinase chaperones hepatitis B virus capsid assembly and captures capsid dynamics in vitro
    • Chen C, Wang JC-Y, Zlotnick A. 2011. A kinase chaperones hepatitis B virus capsid assembly and captures capsid dynamics in vitro. PLoS Pathog 7:e1002388. http://dx.doi.org/10.1371/journal.ppat.1002388.
    • (2011) PLoS Pathog , vol.7
    • Chen, C.1    Wang, J.C.-Y.2    Zlotnick, A.3
  • 48
    • 0032311808 scopus 로고    scopus 로고
    • Prediction of binding energetics from structure using empirical parameterization
    • Baker BM, Murphy KP. 1998. Prediction of binding energetics from structure using empirical parameterization. Methods Enzymol 295:294-315. http://dx.doi.org/10.1016/S0076-6879(98)95045-5.
    • (1998) Methods Enzymol , vol.295 , pp. 294-315
    • Baker, B.M.1    Murphy, K.P.2
  • 49
    • 0022596727 scopus 로고
    • Solvation energy in protein folding and binding
    • Eisenberg D, McLachlan AD. 1986. Solvation energy in protein folding and binding. Nature 319:199-203. http://dx.doi.org/10.1038/319199a0.
    • (1986) Nature , vol.319 , pp. 199-203
    • Eisenberg, D.1    McLachlan, A.D.2
  • 50
    • 61849163979 scopus 로고    scopus 로고
    • Thermodynamics of virus capsid assembly
    • Katen SP, Zlotnick A. 2009. Thermodynamics of virus capsid assembly. Methods Enzymol 455:395-417. http://dx.doi.org/10.1016/S0076-6879 (08)04214-6.
    • (2009) Methods Enzymol , vol.455 , pp. 395-417
    • Katen, S.P.1    Zlotnick, A.2
  • 51
    • 33645992810 scopus 로고    scopus 로고
    • Classical nucleation theory of virus capsids
    • Zandi R, van der Schoot P, Reguera D, Kegel W, Reiss H. 2006. Classical nucleation theory of virus capsids. Biophys J 90:1939-1948. http://dx.doi .org/10.1529/biophysj.105.072975.
    • (2006) Biophys J , vol.90 , pp. 1939-1948
    • Zandi, R.1    van der Schoot, P.2    Reguera, D.3    Kegel, W.4    Reiss, H.5
  • 52
    • 0032568540 scopus 로고    scopus 로고
    • Free energy of burying hydrophobic residues in the interface between protein subunits
    • Vallone B, Miele AE, Vecchini P, Chiancone E, Brunori M. 1998. Free energy of burying hydrophobic residues in the interface between protein subunits. Proc Natl Acad Sci U S A 95:6103-6107. http://dx.doi.org/10 .1073/pnas.95.11.6103.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 6103-6107
    • Vallone, B.1    Miele, A.E.2    Vecchini, P.3    Chiancone, E.4    Brunori, M.5
  • 53
    • 84869068058 scopus 로고    scopus 로고
    • Binding efficiency of proteinprotein complexes
    • Day ES, Cote SM, Whitty A. 2012. Binding efficiency of proteinprotein complexes. Biochemistry 51:9124-9136. http://dx.doi.org/10 .1021/bi301039t.
    • (2012) Biochemistry , vol.51 , pp. 9124-9136
    • Day, E.S.1    Cote, S.M.2    Whitty, A.3
  • 54
    • 33845868485 scopus 로고    scopus 로고
    • BAY 41-4109 has multiple effects on hepatitis B virus capsid assembly
    • Stray SJ, Zlotnick A. 2006. BAY 41-4109 has multiple effects on hepatitis B virus capsid assembly. J Mol Recognit 19:542-548. http://dx.doi.org/10 .1002/jmr.801.
    • (2006) J Mol Recognit , vol.19 , pp. 542-548
    • Stray, S.J.1    Zlotnick, A.2
  • 55
    • 0344585939 scopus 로고    scopus 로고
    • Antivirals interacting with hepatitis B virus core protein and core mutations may misdirect capsid assembly in a similar fashion
    • Hacker HJ, Deres K, Mildenberger M, Schroder CH. 2003. Antivirals interacting with hepatitis B virus core protein and core mutations may misdirect capsid assembly in a similar fashion. Biochem Pharmacol 66: 2273-2279. http://dx.doi.org/10.1016/j.bcp.2003.08.001.
    • (2003) Biochem Pharmacol , vol.66 , pp. 2273-2279
    • Hacker, H.J.1    Deres, K.2    Mildenberger, M.3    Schroder, C.H.4
  • 56
    • 34548641466 scopus 로고    scopus 로고
    • The phenylpropenamide derivative AT-130 blocks HBV replication at the level of viral RNA packaging
    • Feld JJ, Colledge D, Sozzi V, Edwards R, Littlejohn M, Locarnini SA. 2007. The phenylpropenamide derivative AT-130 blocks HBV replication at the level of viral RNA packaging. Antiviral Res 76:168-177. http://dx .doi.org/10.1016/j.antiviral.2007.06.014.
    • (2007) Antiviral Res , vol.76 , pp. 168-177
    • Feld, J.J.1    Colledge, D.2    Sozzi, V.3    Edwards, R.4    Littlejohn, M.5    Locarnini, S.A.6
  • 57
    • 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
  • 58
    • 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
  • 59
    • 84866941201 scopus 로고    scopus 로고
    • Structural organization of pregenomic RNA and the carboxy-terminal domain of the capsid protein of hepatitis B virus
    • Wang JC, Dhason MS, Zlotnick A. 2012. Structural organization of pregenomic RNA and the carboxy-terminal domain of the capsid protein of hepatitis B virus. PLoS Pathog 8:e1002919. http://dx.doi.org/10.1371/journal.ppat.1002919.
    • (2012) PLoS Pathog , vol.8
    • Wang, J.C.1    Dhason, M.S.2    Zlotnick, A.3
  • 60
    • 84896717309 scopus 로고    scopus 로고
    • Nucleic acid chaperone activity associated with the arginine-rich domain of human hepatitis B virus core protein
    • Chu TH, Liou AT, Su PY, Wu HN, Shih C. 2014. Nucleic acid chaperone activity associated with the arginine-rich domain of human hepatitis B virus core protein. J Virol 88:2530-2543. http://dx.doi.org/10.1128/JVI .03235-13.
    • (2014) J Virol , vol.88 , pp. 2530-2543
    • Chu, T.H.1    Liou, A.T.2    Su, P.Y.3    Wu, H.N.4    Shih, C.5
  • 61
    • 84898993517 scopus 로고    scopus 로고
    • The ensemble nature of allostery
    • Motlagh HN, Wrabl JO, Li J, Hilser VJ. 2014. The ensemble nature of allostery. Nature 508:331-339. http://dx.doi.org/10.1038/nature13001.
    • (2014) Nature , vol.508 , pp. 331-339
    • Motlagh, H.N.1    Wrabl, J.O.2    Li, J.3    Hilser, V.J.4
  • 63
    • 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

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