메뉴 건너뛰기




Volumn 107, Issue 3, 2010, Pages 550-560

Modeling the competition between aggregation and self-assembly during virus-like particle processing

Author keywords

Aggregation; Critical concentration; Modeling; Self assembly; Virus like particles

Indexed keywords

AGGREGATION; AGGREGATION BEHAVIOR; BIO-MOLECULAR; BIOTHERAPEUTICS; CONCENTRATION DEPENDENCE; CRITICAL CONCENTRATION; EFFICIENT METHOD; LOW COSTS; MODELING; NON-NATIVE; PHARMACEUTICAL PROTEIN; PRODUCT YIELDS; PROTEIN AGGREGATION; PROTEIN SUBUNITS; QUALITY CONSISTENCY; REALISTIC MODEL; SCALE-UP; SECOND ORDERS; SELF-ASSEMBLING; VIRUS ASSEMBLY; VIRUS-LIKE PARTICLES;

EID: 78651478069     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.22821     Document Type: Article
Times cited : (45)

References (69)
  • 3
    • 0042367744 scopus 로고    scopus 로고
    • A new kinetic scheme for lysozyme refolding and aggregation
    • Buswell AM, Middelberg APJ. 2003. A new kinetic scheme for lysozyme refolding and aggregation. Biotechnol Bioeng 83(5):567-577.
    • (2003) Biotechnol Bioeng , vol.83 , Issue.5 , pp. 567-577
    • Buswell, A.M.1    Middelberg, A.P.J.2
  • 4
    • 3142634785 scopus 로고    scopus 로고
    • In vitro papillomavirus capsid assembly analyzed by light scattering
    • Casini GL, Graham D, Heine D, Garcea RL, Wu DT. 2004. In vitro papillomavirus capsid assembly analyzed by light scattering. Virology 325(2):320-327.
    • (2004) Virology , vol.325 , Issue.2 , pp. 320-327
    • Casini, G.L.1    Graham, D.2    Heine, D.3    Garcea, R.L.4    Wu, D.T.5
  • 5
    • 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(39): 11525-11531.
    • (2002) Biochemistry , vol.41 , Issue.39 , pp. 11525-11531
    • Ceres, P.1    Zlotnick, A.2
  • 6
    • 0141567459 scopus 로고    scopus 로고
    • Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation
    • Chi EY, Krishnan S, Randolph TW, Carpenter JF. 2003. Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation. Pharm Res 20(9):1325-1336.
    • (2003) Pharm Res , vol.20 , Issue.9 , pp. 1325-1336
    • Chi, E.Y.1    Krishnan, S.2    Randolph, T.W.3    Carpenter, J.F.4
  • 7
    • 41049116335 scopus 로고    scopus 로고
    • Quantitative analysis of virus-like particle size and distribution by field-flow fractionation
    • Chuan YP, Fan YY, Lua LHL, Middelberg APJ. 2008a. Quantitative analysis of virus-like particle size and distribution by field-flow fractionation. Biotechnol Bioeng 99(6):1425-1433.
    • (2008) Biotechnol Bioeng , vol.99 , Issue.6 , pp. 1425-1433
    • Chuan, Y.P.1    Fan, Y.Y.2    Lua, L.H.L.3    Middelberg, A.P.J.4
  • 8
    • 39649100408 scopus 로고    scopus 로고
    • High-level expression of soluble viral structural protein in Escherichia coli
    • Chuan YP, Lua LHL, Middelberg APJ. 2008b. High-level expression of soluble viral structural protein in Escherichia coli. J Biotechnol 134(1-2):64-71.
    • (2008) J Biotechnol , vol.134 , Issue.1-2 , pp. 64-71
    • Chuan, Y.P.1    Lua, L.H.L.2    Middelberg, A.P.J.3
  • 9
    • 76049094891 scopus 로고    scopus 로고
    • 2+- triggered switch in the thermodynamic attraction between structural protein capsomeres
    • 2+- triggered switch in the thermodynamic attraction between structural protein capsomeres. J R Soc Interface 7(44):409-421.
    • (2010) J R Soc Interface , vol.7 , Issue.44 , pp. 409-421
    • Chuan, Y.P.1    Fan, Y.Y.2    Lua, L.H.L.3    Middelberg, A.P.J.4
  • 10
    • 0025671869 scopus 로고
    • Refolding and aggregation of bovine carbonic anhydrase-B: Quasi-elastic light-scattering analysis
    • Cleland JL, Wang DIC. 1990. Refolding and aggregation of bovine carbonic anhydrase-B: Quasi-elastic light-scattering analysis. Biochemistry 29(50):11072-11078.
    • (1990) Biochemistry , vol.29 , Issue.50 , pp. 11072-11078
    • Cleland, J.L.1    Wang, D.I.C.2
  • 11
    • 0031776460 scopus 로고    scopus 로고
    • Particle polymorphism caused by deletion of a peptide molecular switch in a quasiequivalent icosahedral virus
    • Dong XF, Natarajan P, Tihova M, Johnson JE, Schneemann A. 1998. Particle polymorphism caused by deletion of a peptide molecular switch in a quasiequivalent icosahedral virus. J Virol 72(7):6024-6033.
    • (1998) J Virol , vol.72 , Issue.7 , pp. 6024-6033
    • Dong, X.F.1    Natarajan, P.2    Tihova, M.3    Johnson, J.E.4    Schneemann, A.5
  • 12
    • 38349042010 scopus 로고    scopus 로고
    • Protein phase behavior in aqueous solutions: Crystallization, liquid-liquid phase separation, gels, and aggregates
    • Dumetz AC, Chockla AM, Kaler EW, Lenhoff AM. 2008. Protein phase behavior in aqueous solutions: Crystallization, liquid-liquid phase separation, gels, and aggregates. Biophys J 94(2):570-583.
    • (2008) Biophys J , vol.94 , Issue.2 , pp. 570-583
    • Dumetz, A.C.1    Chockla, A.M.2    Kaler, E.W.3    Lenhoff, A.M.4
  • 14
    • 23344441590 scopus 로고    scopus 로고
    • Virus-like particle vaccine conferred complete protection against a lethal influenza virus challenge
    • Galarza JM, Latham T, Cupo A. 2005. Virus-like particle vaccine conferred complete protection against a lethal influenza virus challenge. Viral Immunol 18(2):365-372.
    • (2005) Viral Immunol , vol.18 , Issue.2 , pp. 365-372
    • Galarza, J.M.1    Latham, T.2    Cupo, A.3
  • 16
    • 0029511317 scopus 로고
    • Crystallogenesis of biological macromolecules. Biological, microgravity and other physicochemical aspects
    • Giege R, Drenth J, Ducruix A, McPherson A, Saenger W. 1995. Crystallogenesis of biological macromolecules. Biological, microgravity and other physicochemical aspects. Prog Cryst Growth Charact Mater 30(4):237-281.
    • (1995) Prog Cryst Growth Charact Mater , vol.30 , Issue.4 , pp. 237-281
    • Giege, R.1    Drenth, J.2    Ducruix, A.3    McPherson, A.4    Saenger, W.5
  • 17
    • 0000461539 scopus 로고    scopus 로고
    • The protein-water phase diagram and the growth of protein crystals from aqueous solution
    • Haas C, Drenth J. 1998. The protein-water phase diagram and the growth of protein crystals from aqueous solution. J Phys Chem B 102(21):4226-4232.
    • (1998) J Phys Chem B , vol.102 , Issue.21 , pp. 4226-4232
    • Haas, C.1    Drenth, J.2
  • 18
    • 33646065318 scopus 로고    scopus 로고
    • Assembly of human papillomavirus type-16 virus-like particles: Multifactorial study of assembly and competing aggregation
    • Hanslip SJ, Zaccai NR, Middelberg APJ, Falconer RJ. 2006. Assembly of human papillomavirus type-16 virus-like particles: Multifactorial study of assembly and competing aggregation. Biotechnol Prog 22(2):554-560.
    • (2006) Biotechnol Prog , vol.22 , Issue.2 , pp. 554-560
    • Hanslip, S.J.1    Zaccai, N.R.2    Middelberg, A.P.J.3    Falconer, R.J.4
  • 19
    • 57749205392 scopus 로고    scopus 로고
    • Influenza-pseudotyped Gag virus-like particle vaccines provide broad protection against highly pathogenic avian influenza challenge
    • Haynes JR, Dokken L, Wiley JA, Cawthon AG, Bigger J, Harmsen AG, Richardson C. 2009. Influenza-pseudotyped Gag virus-like particle vaccines provide broad protection against highly pathogenic avian influenza challenge. Vaccine 27(4):530-541.
    • (2009) Vaccine , vol.27 , Issue.4 , pp. 530-541
    • Haynes, J.R.1    Dokken, L.2    Wiley, J.A.3    Cawthon, A.G.4    Bigger, J.5    Harmsen, A.G.6    Richardson, C.7
  • 20
    • 1842410676 scopus 로고    scopus 로고
    • Oxidative renaturation of lysozyme at high concentrations
    • Hevehan DL, Clark ED. 1997. Oxidative renaturation of lysozyme at high concentrations. Biotechnol Bioeng 54(3):221-230.
    • (1997) Biotechnol Bioeng , vol.54 , Issue.3 , pp. 221-230
    • Hevehan, D.L.1    Clark, E.D.2
  • 21
    • 24644454633 scopus 로고    scopus 로고
    • Role of specific hemagglutinin amino acids in the immunogenicity and protection of H5N1 influenza virus vaccines
    • Hoffmann E, Lipatov AS, Webby RJ, Govorkova EA, Webster RG. 2005. Role of specific hemagglutinin amino acids in the immunogenicity and protection of H5N1 influenza virus vaccines. Proc Natl Acad Sci USA 102(36):12915-12920.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.36 , pp. 12915-12920
    • Hoffmann, E.1    Lipatov, A.S.2    Webby, R.J.3    Govorkova, E.A.4    Webster, R.G.5
  • 22
    • 67349253093 scopus 로고    scopus 로고
    • Molecular-assisted refolding: Study of two different ionic forms of recombinant human fibroblast growth factors
    • Huang ZF, Leong SSJ. 2009. Molecular-assisted refolding: Study of two different ionic forms of recombinant human fibroblast growth factors. J Biotechnol 142(2):157-163.
    • (2009) J Biotechnol , vol.142 , Issue.2 , pp. 157-163
    • Huang, Z.F.1    Leong, S.S.J.2
  • 24
    • 2942662201 scopus 로고    scopus 로고
    • Competing hydrophobic and screened-Coulomb interactions in hepatitis B virus capsid assembly
    • Kegel WK, van der Schoot P. 2004. Competing hydrophobic and screened-Coulomb interactions in hepatitis B virus capsid assembly. Biophys J 86(6):3905-3913.
    • (2004) Biophys J , vol.86 , Issue.6 , pp. 3905-3913
    • Kegel, W.K.1    van der Schoot, P.2
  • 26
    • 14744271625 scopus 로고
    • Protein aggregation in vitro and in vivo: A quantitative model of the kinetic competition between folding and aggregation
    • Kiefhaber T, Rudolph R, Kohler HH, Buchner J. 1991. Protein aggregation in vitro and in vivo: A quantitative model of the kinetic competition between folding and aggregation. Biotechnology 9(9):825-829.
    • (1991) Biotechnology , vol.9 , Issue.9 , pp. 825-829
    • Kiefhaber, T.1    Rudolph, R.2    Kohler, H.H.3    Buchner, J.4
  • 27
    • 4844220670 scopus 로고    scopus 로고
    • SV40 pseudovirions as highly efficient vectors for gene transfer and their potential application in cancer therapy
    • Kimchi-Sarfaty C, Gottesman MM. 2004. SV40 pseudovirions as highly efficient vectors for gene transfer and their potential application in cancer therapy. Curr Pharm Biotechnol 5(5):451-458.
    • (2004) Curr Pharm Biotechnol , vol.5 , Issue.5 , pp. 451-458
    • Kimchi-Sarfaty, C.1    Gottesman, M.M.2
  • 30
    • 0037359309 scopus 로고    scopus 로고
    • Interaction of papillomavirus virus-like particles with human myeloid antigen-presenting cells
    • Lenz P, Thompson CD, Day PM, Bacot SM, Lowy DR, Schiller JT. 2003. Interaction of papillomavirus virus-like particles with human myeloid antigen-presenting cells. Clin Immunol 106(3):231-237.
    • (2003) Clin Immunol , vol.106 , Issue.3 , pp. 231-237
    • Lenz, P.1    Thompson, C.D.2    Day, P.M.3    Bacot, S.M.4    Lowy, D.R.5    Schiller, J.T.6
  • 31
    • 38949210239 scopus 로고    scopus 로고
    • Preparing recombinant single chain antibodies
    • Leong SSJ, Chen WN. 2008. Preparing recombinant single chain antibodies. Chem Eng Sci 63(6):1401-1414.
    • (2008) Chem Eng Sci , vol.63 , Issue.6 , pp. 1401-1414
    • Leong, S.S.J.1    Chen, W.N.2
  • 32
    • 42049122813 scopus 로고    scopus 로고
    • Quaternary size distribution of soluble aggregates of glutathione-S-transferase-purified viral protein as determined by asymmetrical flow field flow fractionation and dynamic light scattering
    • Lipin DI, Lua LHL, Middelberg APJ. 2008. Quaternary size distribution of soluble aggregates of glutathione-S-transferase-purified viral protein as determined by asymmetrical flow field flow fractionation and dynamic light scattering. J Chromatogr A 1190(1-2):204-214.
    • (2008) J Chromatogr A , vol.1190 , Issue.1-2 , pp. 204-214
    • Lipin, D.I.1    Lua, L.H.L.2    Middelberg, A.P.J.3
  • 33
    • 1642587771 scopus 로고    scopus 로고
    • Cloud-point temperature and liquid-liquid phase separation of supersaturated lysozyme solution
    • Lu J, Carpenter K, Li RJ, Wang XJ, Ching CB. 2004. Cloud-point temperature and liquid-liquid phase separation of supersaturated lysozyme solution. Biophys Chem 109(1):105-112.
    • (2004) Biophys Chem , vol.109 , Issue.1 , pp. 105-112
    • Lu, J.1    Carpenter, K.2    Li, R.J.3    Wang, X.J.4    Ching, C.B.5
  • 34
    • 0001002352 scopus 로고
    • Conformation changes of proteins
    • Lumry R, Eyring H. 1954. Conformation changes of proteins. J Phys Chem 58(2):110-120.
    • (1954) J Phys Chem , vol.58 , Issue.2 , pp. 110-120
    • Lumry, R.1    Eyring, H.2
  • 36
    • 0031974862 scopus 로고    scopus 로고
    • Quantitative disassembly and reassembly of human papillomavirus type 11 viruslike particles in vitro
    • McCarthy MP, White WI, Palmer-Hill F, Koenig S, Suzich JA. 1998. Quantitative disassembly and reassembly of human papillomavirus type 11 viruslike particles in vitro. J Virol 72(1):32-41.
    • (1998) J Virol , vol.72 , Issue.1 , pp. 32-41
    • McCarthy, M.P.1    White, W.I.2    Palmer-Hill, F.3    Koenig, S.4    Suzich, J.A.5
  • 37
    • 33644653105 scopus 로고    scopus 로고
    • Redirecting the coat protein of a spherical virus to assemble into tubular nanostructures
    • Mukherjee S, Pfeifer CM, Johnson JM, Liu J, Zlotnick A. 2006. Redirecting the coat protein of a spherical virus to assemble into tubular nanostructures. J Am Chem Soc 128(8):2538-2539.
    • (2006) J Am Chem Soc , vol.128 , Issue.8 , pp. 2538-2539
    • Mukherjee, S.1    Pfeifer, C.M.2    Johnson, J.M.3    Liu, J.4    Zlotnick, A.5
  • 38
    • 0031559476 scopus 로고    scopus 로고
    • Liquid-liquid phase separation in supersaturated lysozyme solutions and associated precipitate formation/ crystallization
    • Muschol M, Rosenberger F. 1997. Liquid-liquid phase separation in supersaturated lysozyme solutions and associated precipitate formation/ crystallization. J Chem Phys 107(6):1953-1962.
    • (1997) J Chem Phys , vol.107 , Issue.6 , pp. 1953-1962
    • Muschol, M.1    Rosenberger, F.2
  • 39
    • 67749130949 scopus 로고    scopus 로고
    • Invariant polymorphism in virus capsid assembly
    • Nguyen HD, Reddy VS, Brooks CL. 2009. Invariant polymorphism in virus capsid assembly. J Am Chem Soc 131(7):2606-2614.
    • (2009) J Am Chem Soc , vol.131 , Issue.7 , pp. 2606-2614
    • Nguyen, H.D.1    Reddy, V.S.2    Brooks, C.L.3
  • 41
    • 33744802678 scopus 로고    scopus 로고
    • Quantitative analysis of multicomponent spherical virus assembly: Scaffolding protein contributes to the global stability of phage P22 procapsids
    • Parent KN, Zlotnick A, Teschke CM. 2006. Quantitative analysis of multicomponent spherical virus assembly: Scaffolding protein contributes to the global stability of phage P22 procapsids. J Mol Biol 359(4):1097-1106.
    • (2006) J Mol Biol , vol.359 , Issue.4 , pp. 1097-1106
    • Parent, K.N.1    Zlotnick, A.2    Teschke, C.M.3
  • 42
    • 60349103484 scopus 로고    scopus 로고
    • Quantitative characterization of virus-like particles by asymmetrical flow field flow fractionation, electrospray differential mobility analysis, and transmission electron microscopy
    • Pease LF, Lipin DI, Tsai DH, Zachariah MR, Lua LHL, Tarlov MJ, Middelberg APJ. 2009. Quantitative characterization of virus-like particles by asymmetrical flow field flow fractionation, electrospray differential mobility analysis, and transmission electron microscopy. Biotechnol Bioeng 102(3):845-855.
    • (2009) Biotechnol Bioeng , vol.102 , Issue.3 , pp. 845-855
    • Pease, L.F.1    Lipin, D.I.2    Tsai, D.H.3    Zachariah, M.R.4    Lua, L.H.L.5    Tarlov, M.J.6    Middelberg, A.P.J.7
  • 43
    • 0027232759 scopus 로고
    • Nucleation and growth phases in the polymerization of coat and scaffolding subunits into icosahedral procapsid shells
    • Prevelige PE, Thomas D, King J. 1993. Nucleation and growth phases in the polymerization of coat and scaffolding subunits into icosahedral procapsid shells. Biophys J 64(3):824-835.
    • (1993) Biophys J , vol.64 , Issue.3 , pp. 824-835
    • Prevelige, P.E.1    Thomas, D.2    King, J.3
  • 45
    • 33947410779 scopus 로고    scopus 로고
    • Virus-like particle vaccine induces protective immunity against homologous and heterologous strains of influenza virus
    • Quan FS, Huang CZ, Compans RW, Kang SM. 2007. Virus-like particle vaccine induces protective immunity against homologous and heterologous strains of influenza virus. J Virol 81(7):3514-3524.
    • (2007) J Virol , vol.81 , Issue.7 , pp. 3514-3524
    • Quan, F.S.1    Huang, C.Z.2    Compans, R.W.3    Kang, S.M.4
  • 46
    • 38349040438 scopus 로고    scopus 로고
    • Self-assembly of polyhedral shells: A molecular dynamics study
    • Rapaport DC. 2004. Self-assembly of polyhedral shells: A molecular dynamics study. Phys Rev E 70(5):051905.
    • (2004) Phys Rev E , vol.70 , Issue.5 , pp. 051905
    • Rapaport, D.C.1
  • 47
    • 0020031457 scopus 로고
    • Polyomavirus capsid structure at 22.5Å resolution
    • Rayment I, Baker TS, Caspar DLD, Murakami WT. 1982. Polyomavirus capsid structure at 22.5Å resolution. Nature 295(5845):110-115.
    • (1982) Nature , vol.295 , Issue.5845 , pp. 110-115
    • Rayment, I.1    Baker, T.S.2    Caspar, D.L.D.3    Murakami, W.T.4
  • 48
    • 0035194351 scopus 로고    scopus 로고
    • Virus Particle Explorer (VIPER): A website for virus capsid structures and their computational analyses
    • Reddy VS, Natarajan P, Okerberg B, Li K, Damodaran KV, Morton RT, Brooks C, Johnson JE. 2001. Virus Particle Explorer (VIPER): A website for virus capsid structures and their computational analyses. J Virol 75(24):11943-11947.
    • (2001) J Virol , vol.75 , Issue.24 , pp. 11943-11947
    • Reddy, V.S.1    Natarajan, P.2    Okerberg, B.3    Li, K.4    Damodaran, K.V.5    Morton, R.T.6    Brooks, C.7    Johnson, J.E.8
  • 49
    • 67650330245 scopus 로고    scopus 로고
    • A trivalent virus-like particle vaccine elicits protective immune responses against seasonal influenza strains in mice and ferrets
    • Ross TM, Mahmood K, Crevar CJ, Schneider-Ohrum K, Heaton PM, Bright RA. 2009. A trivalent virus-like particle vaccine elicits protective immune responses against seasonal influenza strains in mice and ferrets. PLoS ONE 4(6):e6032.
    • (2009) PLoS ONE , vol.4 , Issue.6
    • Ross, T.M.1    Mahmood, K.2    Crevar, C.J.3    Schneider-Ohrum, K.4    Heaton, P.M.5    Bright, R.A.6
  • 50
    • 0022549499 scopus 로고
    • Self-assembly of purified polyomavirus capsid protein VP1
    • Salunke DM, Caspar DLD, Garcea RL. 1986. Self-assembly of purified polyomavirus capsid protein VP1. Cell 46(6):895-904.
    • (1986) Cell , vol.46 , Issue.6 , pp. 895-904
    • Salunke, D.M.1    Caspar, D.L.D.2    Garcea, R.L.3
  • 51
    • 0024761528 scopus 로고
    • Polymorphism in the assembly of polyomavirus capsid protein VP1
    • Salunke DM, Caspar DLD, Garcea RL. 1989. Polymorphism in the assembly of polyomavirus capsid protein VP1. Biophys J 56(5):887-900.
    • (1989) Biophys J , vol.56 , Issue.5 , pp. 887-900
    • Salunke, D.M.1    Caspar, D.L.D.2    Garcea, R.L.3
  • 52
    • 33644864036 scopus 로고    scopus 로고
    • Crystal gazing: Biotech's financial outlook
    • Schmidt E, Strupp DJ. 2006. Crystal gazing: Biotech's financial outlook. Nat Biotechnol 24(3):261-264.
    • (2006) Nat Biotechnol , vol.24 , Issue.3 , pp. 261-264
    • Schmidt, E.1    Strupp, D.J.2
  • 53
    • 0031737889 scopus 로고    scopus 로고
    • Local rules simulation of the kinetics of virus capsid self-assembly
    • Schwartz R, Shor PW, Prevelige PE, Berger B. 1998. Local rules simulation of the kinetics of virus capsid self-assembly. Biophys J 75(6):2626-2636.
    • (1998) Biophys J , vol.75 , Issue.6 , pp. 2626-2636
    • Schwartz, R.1    Shor, P.W.2    Prevelige, P.E.3    Berger, B.4
  • 54
    • 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 SL, 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(1):249-257.
    • (1993) J Virol , vol.67 , Issue.1 , pp. 249-257
    • Seifer, M.1    Zhou, S.L.2    Standring, D.N.3
  • 56
    • 0028303852 scopus 로고
    • Structure of murine polyomavirus complexed with an oligosaccharide receptor fragment
    • Stehle T, Yan YW, Benjamin TL, Harrison SC. 1994. Structure of murine polyomavirus complexed with an oligosaccharide receptor fragment. Nature 369(6476):160-163.
    • (1994) Nature , vol.369 , Issue.6476 , pp. 160-163
    • Stehle, T.1    Yan, Y.W.2    Benjamin, T.L.3    Harrison, S.C.4
  • 58
    • 0030806177 scopus 로고    scopus 로고
    • Enhancement of protein crystal nucleation by critical density fluctuations
    • tenWolde PR, Frenkel D. 1997. Enhancement of protein crystal nucleation by critical density fluctuations. Science 277(5334):1975-1978.
    • (1997) Science , vol.277 , Issue.5334 , pp. 1975-1978
    • tenWolde, P.R.1    Frenkel, D.2
  • 59
    • 48749094694 scopus 로고    scopus 로고
    • Detection of intermediates and kinetic control during assembly of bacteriophage P22 procapsid
    • Tuma R, Tsuruta H, French KH, Prevelige PE. 2008. Detection of intermediates and kinetic control during assembly of bacteriophage P22 procapsid. J Mol Biol 381(5):1395-1406.
    • (2008) J Mol Biol , vol.381 , Issue.5 , pp. 1395-1406
    • Tuma, R.1    Tsuruta, H.2    French, K.H.3    Prevelige, P.E.4
  • 60
    • 33845629453 scopus 로고    scopus 로고
    • Mathematical virology: A novel approach to the structure and assembly of viruses
    • Twarock R. 2006. Mathematical virology: A novel approach to the structure and assembly of viruses. Phil Trans R Soc Lond A Math Phys Eng Sci 364(1849):3357-3373.
    • (2006) Phil Trans R Soc Lond A Math Phys Eng Sci , vol.364 , Issue.1849 , pp. 3357-3373
    • Twarock, R.1
  • 61
    • 38049161762 scopus 로고    scopus 로고
    • Kinetic theory of virus capsid assembly
    • van der Schoot P, Zandi R. 2007. Kinetic theory of virus capsid assembly. Phys Biol 4(4):296-304.
    • (2007) Phys Biol , vol.4 , Issue.4 , pp. 296-304
    • van der Schoot, P.1    Zandi, R.2
  • 64
    • 0018788361 scopus 로고
    • Reconstitution of lacticdehydrogenase: Non-covalent aggregation vs reactivation. 1. Physical properties and kinetics of aggregation
    • Zettlmeissl G, Rudolph R, Jaenicke R. 1979. Reconstitution of lacticdehydrogenase: Non-covalent aggregation vs reactivation. 1. Physical properties and kinetics of aggregation. Biochemistry 18(25):5567-5571.
    • (1979) Biochemistry , vol.18 , Issue.25 , pp. 5567-5571
    • Zettlmeissl, G.1    Rudolph, R.2    Jaenicke, R.3
  • 66
    • 0028059187 scopus 로고
    • To build a virus capsid: An equilibrium model of the selfassembly of polyhedral protein complexes
    • Zlotnick A. 1994. To build a virus capsid: An equilibrium model of the selfassembly of polyhedral protein complexes. J Mol Biol 241(1):59-67.
    • (1994) J Mol Biol , vol.241 , Issue.1 , pp. 59-67
    • Zlotnick, A.1
  • 67
    • 27744467626 scopus 로고    scopus 로고
    • Theoretical aspects of virus capsid assembly
    • Zlotnick A. 2005. Theoretical aspects of virus capsid assembly. J Mol Recognit 18(6):479-490.
    • (2005) J Mol Recognit , vol.18 , Issue.6 , pp. 479-490
    • Zlotnick, A.1
  • 68
    • 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(44):14644-14652.
    • (1999) Biochemistry , vol.38 , Issue.44 , pp. 14644-14652
    • Zlotnick, A.1    Johnson, J.M.2    Wingfield, P.W.3    Stahl, S.J.4    Endres, D.5
  • 69
    • 0034715825 scopus 로고    scopus 로고
    • Mechanismof capsid assembly for an icosahedral plant virus
    • Zlotnick A, Aldrich R, Johnson JM, Ceres P, Young MJ. 2000. Mechanismof capsid assembly for an icosahedral plant virus. Virology 277(2):450-456.
    • (2000) Virology , vol.277 , Issue.2 , pp. 450-456
    • Zlotnick, A.1    Aldrich, R.2    Johnson, J.M.3    Ceres, P.4    Young, M.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.