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Volumn , Issue , 2010, Pages 131-158

An overview of capsid assembly kinetics

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EID: 85000856674     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1142/9781848164666_0006     Document Type: Chapter
Times cited : (11)

References (96)
  • 3
    • 0014905804 scopus 로고
    • The self-assembly of spherical plant viruses
    • J. B. Bancroft. The self-assembly of spherical plant viruses. Adv. Virus Res. 16: 99-134 (1970).
    • (1970) Adv. Virus Res , vol.16 , pp. 99-134
    • Bancroft, J.B.1
  • 4
    • 0014096331 scopus 로고
    • Formation of an infectious nucleoprotein from protein and nucleic acid isolated from a small spherical virus
    • J. B. Bancroft and E. Hiebert. Formation of an infectious nucleoprotein from protein and nucleic acid isolated from a small spherical virus. Virology 32: 354-356 (1967).
    • (1967) Virology , vol.32 , pp. 354-356
    • Bancroft, J.B.1    Hiebert, E.2
  • 6
    • 0025316017 scopus 로고
    • Hepatitis B virus nucleocapsid assembly: Primary structure requirements in the core protein
    • F. Birnbaum and M. Nassal. Hepatitis B virus nucleocapsid assembly: primary structure requirements in the core protein. J. Virol. 64: 3319-3330 (1990).
    • (1990) J. Virol , vol.64 , pp. 3319-3330
    • Birnbaum, F.1    Nassal, M.2
  • 7
    • 33750704335 scopus 로고    scopus 로고
    • Global structural changes in hepatitis B capsids induced by the assembly effector HAP1
    • C. Bourne, M. G. Finn and A. Zlotnick. Global structural changes in hepatitis B capsids induced by the assembly effector HAP1. J Virol. 80: 11055-11061 (2006).
    • (2006) J Virol , vol.80 , pp. 11055-11061
    • Bourne, C.1    Finn, M.G.2    Zlotnick, A.3
  • 8
    • 53749103127 scopus 로고    scopus 로고
    • Small-molecule effectors of hepatitis B virus capsid assembly give insight into virus life cycle
    • C. Bourne, S. Lee, B. Venkataiah, A. Lee, B. Korba, M. G. Finn and A. Zlotnick. Small-molecule effectors of hepatitis B virus capsid assembly give insight into virus life cycle. J. Virol. 82: 10262-10270 (2008).
    • (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
  • 10
    • 3142634785 scopus 로고    scopus 로고
    • In vitro papillomavirus capsid assembly analyzed by light scattering
    • G. L. Casini, D. Graham, D. Heine, R. L. Garcea and D. T. Wu. In vitro papillomavirus capsid assembly analyzed by light scattering. Virology 325: 320-327 (2004).
    • (2004) Virology , vol.325 , pp. 320-327
    • Casini, G.L.1    Graham, D.2    Heine, D.3    Garcea, R.L.4    Wu, D.T.5
  • 11
    • 0021931593 scopus 로고
    • Assembly-controlled autogenous modulation of bacteriophage P22 scaffolding protein gene expression
    • S. Casjens, M. B. Adams, C. Hall and J. King. Assembly-controlled autogenous modulation of bacteriophage P22 scaffolding protein gene expression. J. Virol. 53: 174-179 (1985).
    • (1985) J. Virol , vol.53 , pp. 174-179
    • Casjens, S.1    Adams, M.B.2    Hall, C.3    King, J.4
  • 12
    • 4143143115 scopus 로고    scopus 로고
    • Hepatitis B Virus Capsid Assembly is Enhanced by Naturally Occurring Mutation F97L
    • P. Ceres, S. J. Stray and A. Zlotnick. Hepatitis B Virus Capsid Assembly is Enhanced by Naturally Occurring Mutation F97L. J. Virol. 78: 9538-9543 (2004).
    • (2004) J. Virol , vol.78 , pp. 9538-9543
    • Ceres, P.1    Stray, S.J.2    Zlotnick, A.3
  • 13
    • 0036786867 scopus 로고    scopus 로고
    • Weak protein-protein interactions are sufficient to drive assembly of hepatitis B virus capsids
    • P. Ceres and A. Zlotnick. Weak protein-protein interactions are sufficient to drive assembly of hepatitis B virus capsids. Biochemistry 41: 11525-11531 (2002).
    • (2002) Biochemistry , vol.41 , pp. 11525-11531
    • Ceres, P.1    Zlotnick, A.2
  • 14
    • 36549086082 scopus 로고    scopus 로고
    • Incorporation of scaffolding protein gpO in bacteriophages P2 and P4
    • J. R. Chang, A. Poliakov, P. E. Prevelige, J. A. Mobley and T. Dokland. Incorporation of scaffolding protein gpO in bacteriophages P2 and P4. Virology 370: 352-361 (2008).
    • (2008) Virology , vol.370 , pp. 352-361
    • Chang, J.R.1    Poliakov, A.2    Prevelige, P.E.3    Mobley, J.A.4    Dokland, T.5
  • 15
    • 54249158841 scopus 로고    scopus 로고
    • Self-Assembly of Brome Mosaic Virus Capsids: Insights from Shorter Time-Scale Experiments
    • C. Chen, C. Kao and B. Dragnea. Self-Assembly of Brome Mosaic Virus Capsids: Insights from Shorter Time-Scale Experiments. J. Phys. Chem. A112: 9405-9412 (2008).
    • (2008) J. Phys. Chem. A , vol.112 , pp. 9405-9412
    • Chen, C.1    Kao, C.2    Dragnea, B.3
  • 17
    • 0035896012 scopus 로고    scopus 로고
    • Papillomavirus capsid protein expression in Escherichia coli: Purification and assembly of HPV11 and HPV16 L1
    • X. S. Chen, G. Casini, S. C. Harrison and R. L. Garcea. Papillomavirus capsid protein expression in Escherichia coli: purification and assembly of HPV11 and HPV16 L1. J. Mol. Biol. 307: 173-182 (2001).
    • (2001) J. Mol. Biol , vol.307 , pp. 173-182
    • Chen, X.S.1    Casini, G.2    Harrison, S.C.3    Garcea, R.L.4
  • 18
    • 36949077319 scopus 로고
    • The structure of small viruses
    • F. H. C. Crick and J. D. Watson. The structure of small viruses. Nature 177: 473-475 (1956).
    • (1956) Nature , vol.177 , pp. 473-475
    • Crick, F.H.C.1    Watson, J.D.2
  • 19
    • 0021103686 scopus 로고
    • Self-assembly of brome mosaic virus capsids. Kinetic study using neutron and X-ray solution scattering
    • M. Cuillel, C. Berthet-Colominas, B. Krop, A. Tardieu, P. Vachette and B. Jacrot. Self-assembly of brome mosaic virus capsids. Kinetic study using neutron and X-ray solution scattering. J. Mol. Biol. 164: 645-650 (1983).
    • (1983) J. Mol. Biol , vol.164 , pp. 645-650
    • Cuillel, M.1    Berthet-Colominas, C.2    Krop, B.3    Tardieu, A.4    Vachette, P.5    Jacrot, B.6
  • 22
    • 33646578826 scopus 로고    scopus 로고
    • Viruses: Making friends with old foes
    • T. Douglas and M. Young. Viruses: making friends with old foes. Science 312: 873-875 (2006).
    • (2006) Science , vol.312 , pp. 873-875
    • Douglas, T.1    Young, M.2
  • 23
    • 22444445178 scopus 로고    scopus 로고
    • A reaction landscape identifies the intermediates critical for self-assembly of virus capsids and other polyhedral structures
    • D. Endres, M. Miyahara, P. Moisant and A. Zlotnick. A reaction landscape identifies the intermediates critical for self-assembly of virus capsids and other polyhedral structures. Protein Science 14: 1518-1525 (2005).
    • (2005) Protein Science , vol.14 , pp. 1518-1525
    • Endres, D.1    Miyahara, M.2    Moisant, P.3    Zlotnick, A.4
  • 24
    • 0035997081 scopus 로고    scopus 로고
    • Model-based Analysis of Assembly Kinetics for Virus Capsids or Other Spherical Polymers
    • D. Endres and A. Zlotnick. Model-based Analysis of Assembly Kinetics for Virus Capsids or Other Spherical Polymers. Biophys. J. 83: 1217-1230 (2002).
    • (2002) Biophys. J , vol.83 , pp. 1217-1230
    • Endres, D.1    Zlotnick, A.2
  • 25
    • 0042326090 scopus 로고    scopus 로고
    • Mechanism of scaffolding-assisted viral assembly
    • W. Chiu and J.E. Johnson (eds.), Academic Press, San Diego
    • B. A. Fane and P. E. Prevelige, Jr. Mechanism of scaffolding-assisted viral assembly. InW. Chiu and J. E. Johnson (eds.), Virus Structure. Academic Press, San Diego, 64: 259-299 (2003).
    • (2003) Virus Structure , vol.64 , pp. 259-299
    • Fane, B.A.1    Prevelige, P.E.2
  • 26
    • 0031945831 scopus 로고    scopus 로고
    • Expression of ORF A1 of infectious bursal disease virus results in the formation of virus-like particles
    • A. Fernandez-Arias, C. Risco, S. Martinez, J. P. Albar and J. F. Rodriguez. Expression of ORF A1 of infectious bursal disease virus results in the formation of virus-like particles. J. Gen. Virol. 79(Pt 5): 1047-1054 (1998).
    • (1998) J. Gen. Virol , vol.79 , pp. 1047-1054
    • Fernandez-Arias, A.1    Risco, C.2    Martinez, S.3    Albar, J.P.4    Rodriguez, J.F.5
  • 27
    • 0001446319 scopus 로고
    • Reconstitution of Active Tobacco Mosaic Virus from Its Inactive Protein and Nucleic Acid Components
    • H. Fraenkel-Conrat and R. C. Williams. Reconstitution of Active Tobacco Mosaic Virus from Its Inactive Protein and Nucleic Acid Components. Proc. Natl. Acad. Sci. USA 41: 690-698 (1955).
    • (1955) Proc. Natl. Acad. Sci. USA , vol.41 , pp. 690-698
    • Fraenkel-Conrat, H.1    Williams, R.C.2
  • 28
    • 1542316127 scopus 로고    scopus 로고
    • Hepatitis B virus infection-natural history and clinical consequences
    • D. Ganem and A. M. Prince. Hepatitis B virus infection-natural history and clinical consequences. N. Engl. J. Med. 350: 1118-1129 (2004).
    • (2004) N. Engl. J. Med , vol.350 , pp. 1118-1129
    • Ganem, D.1    Prince, A.M.2
  • 30
    • 0344585939 scopus 로고    scopus 로고
    • Antivirals interacting with hepatitis B virus core protein and core mutations may misdirect capsid assembly in a similar fashion
    • H. J. Hacker, K. Deres, M. Mildenberger and C. H. Schroder. Antivirals interacting with hepatitis B virus core protein and core mutations may misdirect capsid assembly in a similar fashion. Biochem. Pharmacol. 66: 2273-2279 (2003).
    • (2003) Biochem. Pharmacol , vol.66 , pp. 2273-2279
    • Hacker, H.J.1    Deres, K.2    Mildenberger, M.3    Schroder, C.H.4
  • 32
    • 33745787907 scopus 로고    scopus 로고
    • Dynamic pathways for viral capsid assembly
    • M. F. Hagan and D. Chandler. Dynamic pathways for viral capsid assembly. Biophys. J. 91: 42-54 (2006).
    • (2006) Biophys. J , vol.91 , pp. 42-54
    • Hagan, M.F.1    Chandler, D.2
  • 33
    • 0027087369 scopus 로고
    • Calculation of the free energy of association for protein complexes
    • N. Horton and M. Lewis. Calculation of the free energy of association for protein complexes. Protein Sci. 1: 169-181 (1992).
    • (1992) Protein Sci , vol.1 , pp. 169-181
    • Horton, N.1    Lewis, M.2
  • 37
    • 33645282189 scopus 로고    scopus 로고
    • Master equation approach to the assembly of viral capsids
    • T. Keef, C. Micheletti and R. Twarock. Master equation approach to the assembly of viral capsids. J. Theor. Biol. 242: 713-721 (2006).
    • (2006) J. Theor. Biol , vol.242 , pp. 713-721
    • Keef, T.1    Micheletti, C.2    Twarock, R.3
  • 40
    • 0035793215 scopus 로고    scopus 로고
    • Probing the kinetics of formation of the bacteriophage MS2 translational operator complex: Identification of a protein conformer unable to bind RNA
    • H. Lago, A. M. Parrott, T. Moss, N. J. Stonehouse and P. G. Stockley. Probing the kinetics of formation of the bacteriophage MS2 translational operator complex: identification of a protein conformer unable to bind RNA. J. Mol. Biol. 305: 1131-1144 (2001).
    • (2001) J. Mol. Biol , vol.305 , pp. 1131-1144
    • Lago, H.1    Parrott, A.M.2    Moss, T.3    Stonehouse, N.J.4    Stockley, P.G.5
  • 41
    • 0004062555 scopus 로고
    • P. DeBrunner, J. Tsibris and E. Munck (eds.), University of Illinois Press, Allerton House, Monticello, IL
    • C. Levinthal. In P. DeBrunner, J. Tsibris and E. Munck (eds.), Mossbauer spectroscopy in biological systems. University of Illinois Press, Allerton House, Monticello, IL, p. 22 (1969).
    • (1969) Mossbauer spectroscopy in biological systems
    • Levinthal, C.1
  • 43
    • 0036060096 scopus 로고    scopus 로고
    • A molecular switch in the capsid protein controls the particle polymorphism in an icosahedral virus
    • G. L. Lokesh, T. D. Gowri, P. S. Satheshkumar, M. R. Murthy and H. S. Savithri. A molecular switch in the capsid protein controls the particle polymorphism in an icosahedral virus. Virology 292: 211-223 (2002).
    • (2002) Virology , vol.292 , pp. 211-223
    • Lokesh, G.L.1    Gowri, T.D.2    Satheshkumar, P.S.3    Murthy, M.R.4    Savithri, H.S.5
  • 44
    • 17844372452 scopus 로고    scopus 로고
    • Micelle formation and crystallization as paradigms for virus assembly
    • A. McPherson. Micelle formation and crystallization as paradigms for virus assembly. Bioessays 27: 447-458 (2005).
    • (2005) Bioessays , vol.27 , pp. 447-458
    • McPherson, A.1
  • 45
    • 46649083183 scopus 로고    scopus 로고
    • A quantitative description of in vitro assembly of human papillomavirus 16 viruslike particles
    • S. Mukherjee, M. V. Thorsteinsson, L. B. Johnston, P. DePhillips and A. Zlotnick. A quantitative description of in vitro assembly of human papillomavirus 16 viruslike particles. J. Mol. Biol. 381: 229-237 (2008).
    • (2008) J. Mol. Biol , vol.381 , pp. 229-237
    • Mukherjee, S.1    Thorsteinsson, M.V.2    Johnston, L.B.3    DePhillips, P.4    Zlotnick, A.5
  • 46
    • 0032899606 scopus 로고    scopus 로고
    • Assembly of the herpes simplex virus procapsid from purified components and identification of small complexes containing the major capsid and scaffolding proteins
    • W. W. Newcomb, F. L. Homa, D. R. Thomsen, B. L. Trus, N. Cheng, A. Steven, F. Booy and J. C. Brown. Assembly of the herpes simplex virus procapsid from purified components and identification of small complexes containing the major capsid and scaffolding proteins. J. Virol. 73: 4239-4250 (1999).
    • (1999) J. Virol , vol.73 , pp. 4239-4250
    • Newcomb, W.W.1    Homa, F.L.2    Thomsen, D.R.3    Trus, B.L.4    Cheng, N.5    Steven, A.6    Booy, F.7    Brown, J.C.8
  • 47
    • 61649113957 scopus 로고    scopus 로고
    • Generalized Structural Polymorphism in Self-Assembled Viral Particles
    • H. D. Nguyen and C. L. Brooks 3rd. Generalized Structural Polymorphism in Self-Assembled Viral Particles. Nano Lett. 8: 4574-4581 (2008).
    • (2008) Nano Lett , vol.8 , pp. 4574-4581
    • Nguyen, H.D.1    Brooks, C.L.2
  • 48
    • 33847712647 scopus 로고    scopus 로고
    • Deciphering the kinetic mechanism of spontaneous self-assembly of icosahedral capsids
    • H. D. Nguyen, V. S. Reddy and C. L. Brooks, 3rd. Deciphering the kinetic mechanism of spontaneous self-assembly of icosahedral capsids. Nano Lett. 7: 338-344 (2007).
    • (2007) Nano Lett , vol.7 , pp. 338-344
    • Nguyen, H.D.1    Reddy, V.S.2    Brooks, C.L.3
  • 49
    • 38049150832 scopus 로고    scopus 로고
    • Chemical mimicry of viral capsid selfassembly
    • A. J. Olson, Y. H. Hu and E. Keinan. Chemical mimicry of viral capsid selfassembly. Proc. Natl. Acad. Sci. USA 104: 20731-20736 (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 20731-20736
    • Olson, A.J.1    Hu, Y.H.2    Keinan, E.3
  • 50
    • 23944439447 scopus 로고    scopus 로고
    • Electrostatic interactions govern both nucleation and elongation during phage P22 procapsid assembly
    • K. N. Parent, S. M. Doyle, E. Anderson and C. M. Teschke. Electrostatic interactions govern both nucleation and elongation during phage P22 procapsid assembly. Virology 340: 33-45 (2005).
    • (2005) Virology , vol.340 , pp. 33-45
    • Parent, K.N.1    Doyle, S.M.2    Anderson, E.3    Teschke, C.M.4
  • 51
    • 33751545279 scopus 로고    scopus 로고
    • Phage P22 procapsids equilibrate with free coat protein subunits
    • K. N. Parent, M. M. Suhanovsky and C. M. Teschke. Phage P22 procapsids equilibrate with free coat protein subunits. J. Mol. Biol. 365: 513-522 (2006a).
    • (2006) J. Mol. Biol , vol.365 , pp. 513-522
    • Parent, K.N.1    Suhanovsky, M.M.2    Teschke, C.M.3
  • 52
    • 33744802678 scopus 로고    scopus 로고
    • Quantitative analysis of multicomponent spherical virus assembly: Scaffolding protein contributes to the global stability of phage P22 procapsids
    • K. N. Parent, A. Zlotnick and C. M. Teschke. Quantitative analysis of multicomponent spherical virus assembly: scaffolding protein contributes to the global stability of phage P22 procapsids. J. Mol. Biol. 359: 1097-1106 (2006b).
    • (2006) J. Mol. Biol , vol.359 , pp. 1097-1106
    • Parent, K.N.1    Zlotnick, A.2    Teschke, C.M.3
  • 53
    • 0023696277 scopus 로고
    • Scaffolding protein regulates the polymerization of P22 coat subunits into icosahedral shells in vitro
    • J. Prevelige, D. Thomas and J. King. Scaffolding protein regulates the polymerization of P22 coat subunits into icosahedral shells in vitro. J. Mol. Biol. 202: 743-757 (1988).
    • (1988) J. Mol. Biol , vol.202 , pp. 743-757
    • Prevelige, J.1    Thomas, D.2    King, J.3
  • 54
    • 0027232759 scopus 로고
    • Nucleation and growth phases in the polymerization of coat and scaffolding subunits into icosahedral procapsid shells
    • P. E. Prevelige, D. Thomas and J. King. Nucleation and growth phases in the polymerization of coat and scaffolding subunits into icosahedral procapsid shells. Biophys. J. 64: 824-835 (1993).
    • (1993) Biophys. J , vol.64 , pp. 824-835
    • Prevelige, P.E.1    Thomas, D.2    King, J.3
  • 55
    • 0032007554 scopus 로고    scopus 로고
    • Inhibiting virus-capsid assembly by altering the polymerisation pathway
    • P. E. J. Prevelige. Inhibiting virus-capsid assembly by altering the polymerisation pathway. Trends Biotech. 16: 61-65 (1998).
    • (1998) Trends Biotech , vol.16 , pp. 61-65
    • Prevelige, P.E.J.1
  • 56
  • 57
    • 55149103754 scopus 로고    scopus 로고
    • Role of reversibility in viral capsid growth: A paradigm for selfassembly
    • D. C. Rapaport. Role of reversibility in viral capsid growth: a paradigm for selfassembly. Phys. Rev. Lett. 101: 186101 (2008).
    • (2008) Phys. Rev. Lett , vol.101
    • Rapaport, D.C.1
  • 58
    • 0033184831 scopus 로고    scopus 로고
    • Supramolecular self-assembly: Molecular dynamics modeling of polyhedral shell formation
    • D. C. Rapaport, J. E. Johnson and J. Skolnick. Supramolecular self-assembly: Molecular dynamics modeling of polyhedral shell formation. Comp. Phys. Comm. 121: 231-235 (1999).
    • (1999) Comp. Phys. Comm , vol.121 , pp. 231-235
    • Rapaport, D.C.1    Johnson, J.E.2    Skolnick, J.3
  • 59
    • 0031961961 scopus 로고    scopus 로고
    • Energetics of quasiequivalence: Computational analysis of protein-protein interactions in icosahedral viruses
    • V. S. Reddy, H. A. Giesing, R. T. Morton, A. Kumar, C. B. Post, C. L. Brooks, 3rd and J. E. Johnson. Energetics of quasiequivalence: computational analysis of protein-protein interactions in icosahedral viruses. Biophys. J. 74: 546-558 (1998).
    • (1998) Biophys. J , vol.74 , pp. 546-558
    • Reddy, V.S.1    Giesing, H.A.2    Morton, R.T.3    Kumar, A.4    Post, C.B.5    Brooks, C.L.6    Johnson, J.E.7
  • 60
    • 0025821080 scopus 로고
    • A comparison ofWIN51711 andR78206 as stabilizers of poliovirus virions and procapsids
    • B. Rombaut, K. Andries and A. Boeye. A comparison ofWIN51711 andR78206 as stabilizers of poliovirus virions and procapsids. J. Gen. Virol. 72: 2153-2157 (1991a).
    • (1991) J. Gen. Virol , vol.72 , pp. 2153-2157
    • Rombaut, B.1    Andries, K.2    Boeye, A.3
  • 61
    • 0026032983 scopus 로고
    • In vitro assembly of poliovirus 14 S subunits: Identification of the assembly promoting activity of infected cell extracts
    • B. Rombaut, A. Foriers and A. Boeye. In vitro assembly of poliovirus 14 S subunits: identification of the assembly promoting activity of infected cell extracts. Virology 180: 781-787 (1991b).
    • (1991) Virology , vol.180 , pp. 781-787
    • Rombaut, B.1    Foriers, A.2    Boeye, A.3
  • 62
    • 0000327130 scopus 로고    scopus 로고
    • Picornaviridae: The viruses and their replication
    • B.N. Fields, D.M. Knipe, P.M. Howley, R.M. Chanock, J.L. Melnick, T.P. Monath, B. Roizman and S.E. Straus (eds.), Lippincott-Raven, Philadelphia
    • R. R. Rueckert. Picornaviridae: The viruses and their replication. In B. N. Fields, D. M. Knipe, P. M. Howley, R. M. Chanock, J. L. Melnick, T. P. Monath, B. Roizman and S. E. Straus (eds.), Fields Virology. Lippincott-Raven, Philadelphia, pp. 609-654 (1996).
    • (1996) Fields Virology , pp. 609-654
    • Rueckert, R.R.1
  • 64
    • 0034653972 scopus 로고    scopus 로고
    • "Local rules" theory applied to polyomavirus polymorphic capsid assemblies
    • R. Schwartz, R. L. Garcea and B. Berger. "Local rules" theory applied to polyomavirus polymorphic capsid assemblies. Virology 268: 461-470 (2000).
    • (2000) Virology , vol.268 , pp. 461-470
    • Schwartz, R.1    Garcea, R.L.2    Berger, B.3
  • 65
    • 0031737889 scopus 로고    scopus 로고
    • Local rules simulation of the kinetics of virus capsid self-assembly
    • R. Schwartz, P. W. Shor, P. E. J. Prevelige and B. Berger. Local rules simulation of the kinetics of virus capsid self-assembly. Biophys. J. 75: 2626-2636 (1998).
    • (1998) Biophys. J , vol.75 , pp. 2626-2636
    • Schwartz, R.1    Shor, P.W.2    Prevelige, P.E.J.3    Berger, B.4
  • 66
    • 0037705348 scopus 로고    scopus 로고
    • Observed hysteresis of virus capsid disassembly is implicit in kinetic models of assembly
    • S. Singh and A. Zlotnick. Observed hysteresis of virus capsid disassembly is implicit in kinetic models of assembly. J. Biol. Chem. 278: 18249-18255 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 18249-18255
    • Singh, S.1    Zlotnick, A.2
  • 68
    • 0029643791 scopus 로고
    • Structures of the native and swollen forms of cowpea chlorotic mottle virus determined by X-ray crystallography and cryo-electron microscopy
    • J. A. Speir, S. Munshi, G. Wang, T. S. Baker and J. E. Johnson. Structures of the native and swollen forms of cowpea chlorotic mottle virus determined by X-ray crystallography and cryo-electron microscopy. Structure 3: 63-78 (1995).
    • (1995) Structure , vol.3 , pp. 63-78
    • Speir, J.A.1    Munshi, S.2    Wang, G.3    Baker, T.S.4    Johnson, J.E.5
  • 69
    • 0030584124 scopus 로고    scopus 로고
    • The structure of simian virus 40 refined at 3. 1 A resolution
    • T. Stehle, S. J. Gamblin, Y. Yan and S. C. Harrison. The structure of simian virus 40 refined at 3. 1 A resolution. Structure 4: 165-182 (1996).
    • (1996) Structure , vol.4 , pp. 165-182
    • Stehle, T.1    Gamblin, S.J.2    Yan, Y.3    Harrison, S.C.4
  • 71
  • 72
    • 3543096838 scopus 로고    scopus 로고
    • Zinc ions trigger conformational change and oligomerization of hepatitis B virus capsid protein
    • S. J. Stray, P. Ceres and A. Zlotnick. Zinc ions trigger conformational change and oligomerization of hepatitis B virus capsid protein. Biochemistry 43: 9989-9998 (2004).
    • (2004) Biochemistry , vol.43 , pp. 9989-9998
    • Stray, S.J.1    Ceres, P.2    Zlotnick, A.3
  • 73
    • 33644855448 scopus 로고    scopus 로고
    • An in vitro fluorescence screen to identify antivirals that disrupt hepatitis B virus capsid assembly
    • S. J. Stray, J. M. Johnson, B. G. Kopek and A. Zlotnick. An in vitro fluorescence screen to identify antivirals that disrupt hepatitis B virus capsid assembly. Nat. Biotechnol. 24: 358-362 (2006).
    • (2006) Nat. Biotechnol , vol.24 , pp. 358-362
    • Stray, S.J.1    Johnson, J.M.2    Kopek, B.G.3    Zlotnick, A.4
  • 74
    • 33845868485 scopus 로고    scopus 로고
    • BAY 41-4109 has multiple effects on Hepatitis B virus capsid assembly
    • S. J. Stray and A. Zlotnick. BAY 41-4109 has multiple effects on Hepatitis B virus capsid assembly. J. Mol. Recognit. 19: 542-548 (2006).
    • (2006) J. Mol. Recognit , vol.19 , pp. 542-548
    • Stray, S.J.1    Zlotnick, A.2
  • 75
    • 0036889379 scopus 로고    scopus 로고
    • Replication advantage and host factor-independent phenotypes attributable to a common naturally occurring capsid mutation (I97L) in human hepatitis B virus
    • F. M. Suk, M. H. Lin, M. Newman, S. Pan, S. H. Chen, J. D. Liu and C. Shih. Replication advantage and host factor-independent phenotypes attributable to a common naturally occurring capsid mutation (I97L) in human hepatitis B virus. J. Virol. 76: 12069-12077 (2002).
    • (2002) J. Virol , vol.76 , pp. 12069-12077
    • Suk, F.M.1    Lin, M.H.2    Newman, M.3    Pan, S.4    Chen, S.H.5    Liu, J.D.6    Shih, C.7
  • 77
    • 0033605211 scopus 로고    scopus 로고
    • Two distinct segments of the hepatitis B virus surface antigen contribute synergistically to its association with the viral core particles
    • W. S. Tan, M. R. Dyson and K. Murray. Two distinct segments of the hepatitis B virus surface antigen contribute synergistically to its association with the viral core particles. J. Mol. Biol. 286: 797-808 (1999).
    • (1999) J. Mol. Biol , vol.286 , pp. 797-808
    • Tan, W.S.1    Dyson, M.R.2    Murray, K.3
  • 78
    • 0033028591 scopus 로고    scopus 로고
    • In vitro assembly of alphavirus cores by using nucleocapsid protein expressed in Escherichia. coli
    • T. L. Tellinghuisen, A. E. Hamburger, B. R. Fisher, R. Ostendorp and R. J. Kuhn. In vitro assembly of alphavirus cores by using nucleocapsid protein expressed in Escherichia. coli. J. Virol. 73: 5309-5319 (1999).
    • (1999) J. Virol , vol.73 , pp. 5309-5319
    • Tellinghuisen, T.L.1    Hamburger, A.E.2    Fisher, B.R.3    Ostendorp, R.4    Kuhn, R.J.5
  • 79
    • 26944455601 scopus 로고    scopus 로고
    • The HIV-1 capsid protein C-terminal domain in complex with a virus assembly inhibitor
    • F. Ternois, J. Sticht, S. Duquerroy, H. G. Krausslich and F. A. Rey. The HIV-1 capsid protein C-terminal domain in complex with a virus assembly inhibitor. Nat. Struct. Mol. Biol. 12: 678-682 (2005).
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 678-682
    • Ternois, F.1    Sticht, J.2    Duquerroy, S.3    Krausslich, H.G.4    Rey, F.A.5
  • 80
    • 0027364215 scopus 로고
    • Inhibition of viral capsid assembly by 1, 1-bi(4-anilinonaphthalene-5-sulfonic acid)
    • C. M. Teschke, J. King and P. E. Prevelige, Jr. Inhibition of viral capsid assembly by 1, 1-bi(4-anilinonaphthalene-5-sulfonic acid). Biochemistry 32: 10658-10665 (1993).
    • (1993) Biochemistry , vol.32 , pp. 10658-10665
    • Teschke, C.M.1    King, J.2    Prevelige, P.E.3
  • 81
    • 48749094694 scopus 로고    scopus 로고
    • Detection of intermediates and kinetic control during assembly of bacteriophage P22 procapsid
    • R. Tuma, H. Tsuruta, K. H. French and P. E. Prevelige. Detection of intermediates and kinetic control during assembly of bacteriophage P22 procapsid. J. Mol. Biol. 381: 1395-1406 (2008).
    • (2008) J. Mol. Biol , vol.381 , pp. 1395-1406
    • Tuma, R.1    Tsuruta, H.2    French, K.H.3    Prevelige, P.E.4
  • 82
  • 83
    • 0034665442 scopus 로고    scopus 로고
    • In vitro assembly of bacteriophage P4 procapsids from purified capsid and scaffolding proteins
    • S. Wang, P. Palasingam, R. H. Nokling, B. H. Lindqvist and T. Dokland. In vitro assembly of bacteriophage P4 procapsids from purified capsid and scaffolding proteins. Virology 275: 133-144 (2000).
    • (2000) Virology , vol.275 , pp. 133-144
    • Wang, S.1    Palasingam, P.2    Nokling, R.H.3    Lindqvist, B.H.4    Dokland, T.5
  • 87
    • 0028953769 scopus 로고
    • Hepatitis core antigen produced in Escherichia coli: Subunit composition, conformational analysis, and in vitro capsid assembly
    • P. T. Wingfield, S. J. Stahl, R. W. Williams and A. C. Steven. Hepatitis core antigen produced in Escherichia coli: subunit composition, conformational analysis, and in vitro capsid assembly. Biochemistry 34: 4919-4932 (1995).
    • (1995) Biochemistry , vol.34 , pp. 4919-4932
    • Wingfield, P.T.1    Stahl, S.J.2    Williams, R.W.3    Steven, A.C.4
  • 88
    • 0033152857 scopus 로고    scopus 로고
    • The crystal structure of the human hepatitis B virus capsid
    • S. A. Wynne, R. A. Crowther and A. G. Leslie. The crystal structure of the human hepatitis B virus capsid. Mol. Cell 3: 771-780 (1999).
    • (1999) Mol. Cell , vol.3 , pp. 771-780
    • Wynne, S.A.1    Crowther, R.A.2    Leslie, A.G.3
  • 89
    • 0033064976 scopus 로고    scopus 로고
    • The mechanism of an immature secretion phenotype of a highly frequent naturally occurring missense mutation at codon 97 of human hepatitis B virus core antigen
    • T. T. Yuan, G. K. Sahu, W. E. Whitehead, R. Greenberg and C. Shih. The mechanism of an immature secretion phenotype of a highly frequent naturally occurring missense mutation at codon 97 of human hepatitis B virus core antigen. J. Virol. 73: 5731-5740 (1999a).
    • (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
  • 90
    • 0141834247 scopus 로고    scopus 로고
    • Subtype-independent immature secretion and subtype-dependent replication deficiency of a highly frequent, naturally occurring mutation of human hepatitis B virus core antigen
    • T. T. Yuan, P. C. Tai and C. Shih. Subtype-independent immature secretion and subtype-dependent replication deficiency of a highly frequent, naturally occurring mutation of human hepatitis B virus core antigen. J. Virol. 73: 10122-10128 (1999b).
    • (1999) J. Virol , vol.73 , pp. 10122-10128
    • Yuan, T.T.1    Tai, P.C.2    Shih, C.3
  • 92
    • 33646150440 scopus 로고    scopus 로고
    • Simulation study of the contribution of oligomer/oligomer binding to capsid assembly kinetics
    • T. Zhang and R. Schwartz. Simulation study of the contribution of oligomer/oligomer binding to capsid assembly kinetics. Biophys. J. 90: 57-64 (2006).
    • (2006) Biophys. J , vol.90 , pp. 57-64
    • Zhang, T.1    Schwartz, R.2
  • 93
    • 0028059187 scopus 로고
    • To build a virus capsid. An equilibrium model of the self assembly of polyhedral protein complexes
    • A. Zlotnick. To build a virus capsid. An equilibrium model of the self assembly of polyhedral protein complexes. J. Mol. Biol. 241: 59-67 (1994).
    • (1994) J. Mol. Biol , vol.241 , pp. 59-67
    • Zlotnick, A.1
  • 94
    • 0034715825 scopus 로고    scopus 로고
    • Mechanism of Capsid Assembly for an Icosahedral Plant Virus
    • A. Zlotnick, R. Aldrich, J. M. Johnson, P. Ceres and M. J. Young. Mechanism of Capsid Assembly for an Icosahedral Plant Virus. Virology 277: 450-456 (2000).
    • (2000) Virology , vol.277 , pp. 450-456
    • Zlotnick, A.1    Aldrich, R.2    Johnson, J.M.3    Ceres, P.4    Young, M.J.5
  • 95
    • 0036242046 scopus 로고    scopus 로고
    • A small molecule inhibits and misdirects assembly of hepatitis B virus capsids
    • A. Zlotnick, P. Ceres, S. Singh and J. M. Johnson. A small molecule inhibits and misdirects assembly of hepatitis B virus capsids. J. Virol. 76: 4848-4854 (2002).
    • (2002) J. Virol , vol.76 , pp. 4848-4854
    • Zlotnick, A.1    Ceres, P.2    Singh, S.3    Johnson, J.M.4
  • 96
    • 0033517792 scopus 로고    scopus 로고
    • A theoretical model successfully identifies features of hepatitis B virus capsid assembly
    • A. Zlotnick, J. M. Johnson, P. W. Wingfield, S. J. Stahl and D. Endres. A theoretical model successfully identifies features of hepatitis B virus capsid assembly. Biochemistry 38: 14644-14652 (1999).
    • (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


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