메뉴 건너뛰기




Volumn 90, Issue 6, 2006, Pages 1939-1948

Classical nucleation theory of virus capsids

Author keywords

[No Author keywords available]

Indexed keywords

CAPSID PROTEIN; MULTIPROTEIN COMPLEX;

EID: 33645992810     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.105.072975     Document Type: Article
Times cited : (175)

References (48)
  • 1
    • 0014905804 scopus 로고
    • The self-assembly of spherical plant viruses
    • Bancroft, J. B. 1970. The self-assembly of spherical plant viruses. Adv. Virus Res. 16:99-134.
    • (1970) Adv. Virus Res. , vol.16 , pp. 99-134
    • Bancroft, J.B.1
  • 3
    • 77956721435 scopus 로고
    • Assembly and stability of the Tobacco Mosaic Virus particle
    • Caspar, D. L. D. 1963. Assembly and stability of the Tobacco Mosaic Virus particle. Adv. Protein Chem. 18:37-121.
    • (1963) Adv. Protein Chem. , vol.18 , pp. 37-121
    • Caspar, D.L.D.1
  • 4
    • 0036786867 scopus 로고    scopus 로고
    • Weak protein-protein interactions are sufficient to drive assembly of Hepatitis B virus capsids
    • Ceres, P., and A. Zlotnick. 2002. Weak protein-protein interactions are sufficient to drive assembly of Hepatitis B virus capsids. Biochemistry. 41:11525-11531.
    • (2002) Biochemistry , vol.41 , pp. 11525-11531
    • Ceres, P.1    Zlotnick, A.2
  • 6
    • 17844372452 scopus 로고    scopus 로고
    • Micelle formation and crystallization as paradigms for virus assembly
    • McPherson, A. 2005. Micelle formation and crystallization as paradigms for virus assembly. Bioessays. 27:447-458.
    • (2005) Bioessays , vol.27 , pp. 447-458
    • McPherson, A.1
  • 8
    • 27244438043 scopus 로고    scopus 로고
    • Mechanical properties of viral capsids
    • Zandi, R., and D. Reguera. 2005. Mechanical properties of viral capsids. Phys. Rev. E. 72:021917-1-021917-12.
    • (2005) Phys. Rev. E , vol.72 , pp. 219171-2191712
    • Zandi, R.1    Reguera, D.2
  • 10
    • 3142634785 scopus 로고    scopus 로고
    • In vitro Papillomavirus capsid assembly analyzed by light scattering
    • Casini, G. L., D. Graham, D. Heine, R. L. Garcea, and D. T. Wu. 2004. In vitro Papillomavirus capsid assembly analyzed by light scattering. Virology. 325:320-327.
    • (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
    • 0014259486 scopus 로고
    • The assembly in vitro of some small spherical viruses, hybrid viruses and other nucleoproteins
    • Hiebert, E., J. B. Bancroft, and C. E. Bracker. 1968. The assembly in vitro of some small spherical viruses, hybrid viruses and other nucleoproteins. Virology. 34:492-508.
    • (1968) Virology , vol.34 , pp. 492-508
    • Hiebert, E.1    Bancroft, J.B.2    Bracker, C.E.3
  • 12
    • 0028947765 scopus 로고
    • Cold denaturation of an icosahedral virus. The role of entropy in virus assembly
    • Da Poian, A. T., A. C. Oliveira, and J. L. Silva. 1995. Cold denaturation of an icosahedral virus. The role of entropy in virus assembly. Biochemistry. 34:2672-2677.
    • (1995) Biochemistry , vol.34 , pp. 2672-2677
    • Da Poian, A.T.1    Oliveira, A.C.2    Silva, J.L.3
  • 13
    • 0033614097 scopus 로고    scopus 로고
    • The Tobacco Mosaic Virus particle: Structure and assembly
    • Klug, A. 1999. The Tobacco Mosaic Virus particle: structure and assembly. Phil. Trans. Roy. Soc. London B. 354:531-535.
    • (1999) Phil. Trans. Roy. Soc. London B , vol.354 , pp. 531-535
    • Klug, A.1
  • 14
    • 0028953769 scopus 로고
    • Hepatitis core antigen produced in Escherichia coli: Subunit composition, conformational analysis, and in vitro capsid assembly
    • Wingfield, P. T., S. J. Stahl, R. W. Williams, and A. C. Steven. 1995. Hepatitis core antigen produced in Escherichia coli: subunit composition, conformational analysis, and in vitro capsid assembly. Biochemistry. 34:4919-4932.
    • (1995) Biochemistry , vol.34 , pp. 4919-4932
    • Wingfield, P.T.1    Stahl, S.J.2    Williams, R.W.3    Steven, A.C.4
  • 15
    • 2942662201 scopus 로고    scopus 로고
    • Competing hydrophobic and screened-Coulomb interactions in Hepatitis B virus capsid assembly
    • Kegel, W. K., and P. van der Schoot. 2004. Competing hydrophobic and screened-Coulomb interactions in Hepatitis B virus capsid assembly. Biophys. J. 86:3905-3913.
    • (2004) Biophys. J. , vol.86 , pp. 3905-3913
    • Kegel, W.K.1    Van Der Schoot, P.2
  • 16
    • 0014118741 scopus 로고
    • Polymerization-depolymerization of Tobacco Mosaic Virus protein VI: Light scattering studies
    • Smith, C. E., and M. A. Lauffer. 1967. Polymerization-depolymerization of Tobacco Mosaic Virus protein VI: light scattering studies. Biochemistry. 6:2457-2465.
    • (1967) Biochemistry , vol.6 , pp. 2457-2465
    • Smith, C.E.1    Lauffer, M.A.2
  • 17
    • 0019828231 scopus 로고
    • Scanning calorimetric investigation of the polymerization of the coat proteins of tobacco mosaic virus
    • Sturtevant, J. M., G. Velicelebi, R. Jaenike, and M. A. Lauffer. 1981. Scanning calorimetric investigation of the polymerization of the coat proteins of tobacco mosaic virus. Biochemistry. 20:3792-3800.
    • (1981) Biochemistry , vol.20 , pp. 3792-3800
    • Sturtevant, J.M.1    Velicelebi, G.2    Jaenike, R.3    Lauffer, M.A.4
  • 18
    • 1842405464 scopus 로고    scopus 로고
    • Studies of protein-protein interfaces: A statistical analysis of the hydrophobic effect
    • Tsai, C.-J., S. L. Lin, H. J. Wolfson, and R. Nussinov. 1997. Studies of protein-protein interfaces: a statistical analysis of the hydrophobic effect. Protein Sci. 6:53-64.
    • (1997) Protein Sci. , vol.6 , pp. 53-64
    • Tsai, C.-J.1    Lin, S.L.2    Wolfson, H.J.3    Nussinov, R.4
  • 19
    • 21244433239 scopus 로고    scopus 로고
    • Electrostatic contributions to the kinetics and thermodynamics of protein assembly
    • Dell'Orco, D., W.-F. Xue, and S. Linse. 2005. Electrostatic contributions to the kinetics and thermodynamics of protein assembly. Biophys. J. 88:1991-2000.
    • (2005) Biophys.J. , vol.88 , pp. 1991-2000
    • Dell'Orco, D.1    Xue, W.-F.2    Linse, S.3
  • 20
    • 27944504802 scopus 로고    scopus 로고
    • Electrostatics of an RNA virus
    • van der Schoot, P., and R. Bruinsma. 2005. Electrostatics of an RNA virus. Phys. Rev. E. 70:61928-1-61928-12.
    • (2005) Phys. Rev. E , vol.70 , pp. 619281-6192812
    • Van Der Schoot, P.1    Bruinsma, R.2
  • 21
    • 0029643791 scopus 로고
    • Structures of the native and swollen forms of CCMV determined by x-ray crystallography and cryo-electron microscopy
    • Speir, J. A., S. Mushi, G. Wang, T. S. Baker, and J. E. Johnson. 1995. Structures of the native and swollen forms of CCMV determined by x-ray crystallography and cryo-electron microscopy. Structure. 3:63-78.
    • (1995) Structure , vol.3 , pp. 63-78
    • Speir, J.A.1    Mushi, S.2    Wang, G.3    Baker, T.S.4    Johnson, J.E.5
  • 22
    • 0031962061 scopus 로고    scopus 로고
    • Caspar carboxylates: The structural basis of Tabomovirus disassembly
    • Wang, H., A. Planchart, and G. Stubbs. 1997. Caspar carboxylates: the structural basis of Tabomovirus disassembly. Biophys. J. 74:633-638.
    • (1997) Biophys. J. , vol.74 , pp. 633-638
    • Wang, H.1    Planchart, A.2    Stubbs, G.3
  • 23
    • 0142154217 scopus 로고    scopus 로고
    • Are weak protein-protein interactions the general rule in capsid assembly?
    • Zlotnick, A. 2003. Are weak protein-protein interactions the general rule in capsid assembly? Virology. 315:269-274.
    • (2003) Virology , vol.315 , pp. 269-274
    • Zlotnick, A.1
  • 24
    • 0034715825 scopus 로고    scopus 로고
    • Mechanism of capsid assembly for an icosahedral plant virus
    • Zlotnick, A., R. Aldrich, J. M. Johnson, P. Ceres, and M. J. Young. 2000. Mechanism of capsid assembly for an icosahedral plant virus. Virology. 277:450-456.
    • (2000) Virology , vol.277 , pp. 450-456
    • Zlotnick, A.1    Aldrich, R.2    Johnson, J.M.3    Ceres, P.4    Young, M.J.5
  • 25
    • 0033517792 scopus 로고    scopus 로고
    • A theoretical model successfully identifies features of Hepatitis B Virus capsid assembly
    • Zlotnick, A., J. M. Johnson, P. W. Wingfield, S. J. Strahl, and D. Andres. 1999. A theoretical model successfully identifies features of Hepatitis B Virus capsid assembly. Biochemistry. 38:14644-14652.
    • (1999) Biochemistry , vol.38 , pp. 14644-14652
    • Zlotnick, A.1    Johnson, J.M.2    Wingfield, P.W.3    Strahl, S.J.4    Andres, D.5
  • 26
    • 0027232759 scopus 로고
    • Nucleation and growth phases in the polymerization of coat and scaffolding subunits into icosahedral procapsid shells
    • Prevelige, P. E., Jr., D. Thomas, and J. King. 1993. Nucleation and growth phases in the polymerization of coat and scaffolding subunits into icosahedral procapsid shells. Biophys. J. 64:824-835.
    • (1993) Biophys. J. , vol.64 , pp. 824-835
    • Prevelige Jr., P.E.1    Thomas, D.2    King, J.3
  • 27
    • 0035997081 scopus 로고    scopus 로고
    • Model-based analysis of assembly kinetics for virus capsids or other spherical polymers
    • Endres, D., and A. Zlotnick. 2002. Model-based analysis of assembly kinetics for virus capsids or other spherical polymers. Biophys. J. 83:1217-1230
    • (2002) Biophys. J. , vol.83 , pp. 1217-1230
    • Endres, D.1    Zlotnick, A.2
  • 28
    • 38349040438 scopus 로고    scopus 로고
    • Self-assembly of polyhedral shells: A molecular dynamics study
    • Rapaport, D. C. 2004. Self-assembly of polyhedral shells: a molecular dynamics study. Phys. Rev. E. 70:051905, 1-13.
    • (2004) Phys. Rev. E , vol.70 , pp. 051905
    • Rapaport, D.C.1
  • 29
    • 0031737889 scopus 로고    scopus 로고
    • Local rules simulation of the kinetics of virus capsid self-assembly
    • Schwartz, R., P. W. Schorr, P. E. Prevelige, Jr., and B. Berger. 1998. Local rules simulation of the kinetics of virus capsid self-assembly. Biophys. J. 75:2626-2636.
    • (1998) Biophys. J. , vol.75 , pp. 2626-2636
    • Schwartz, R.1    Schorr, P.W.2    Prevelige Jr., P.E.3    Berger, B.4
  • 30
    • 3342900950 scopus 로고
    • On the kinetics of step-wise micelle association
    • Aniansson, E. A. G., and S. N. Wall. 1974. On the kinetics of step-wise micelle association. J. Phys. Chem. 78:1024-1030.
    • (1974) J. Phys. Chem. , vol.78 , pp. 1024-1030
    • Aniansson, E.A.G.1    Wall, S.N.2
  • 31
    • 0006628246 scopus 로고    scopus 로고
    • Butterworth-Heinemann, Oxford, UK
    • Kashchiev, D. 2000. Nucleation. Butterworth-Heinemann, Oxford, UK.
    • (2000) Nucleation
    • Kashchiev, D.1
  • 32
    • 77956674927 scopus 로고    scopus 로고
    • Nucleation theory
    • Wu, D. T. 1997. Nucleation theory. Solid State Phys. 50:37-187.
    • (1997) Solid State Phys. , vol.50 , pp. 37-187
    • Wu, D.T.1
  • 33
    • 12944264524 scopus 로고    scopus 로고
    • The energy landscape as a unifying theme in molecular science
    • Wales, D. J. 2005. The energy landscape as a unifying theme in molecular science. Phil. Trans. Roy. Soc. A. 363:357-377.
    • (2005) Phil. Trans. Roy. Soc. A , vol.363 , pp. 357-377
    • Wales, D.J.1
  • 34
    • 0032007554 scopus 로고    scopus 로고
    • Inhibiting virus-capsid assembly by altering the polymerisation pathway
    • Prevelige, P. E. 1998. Inhibiting virus-capsid assembly by altering the polymerisation pathway. Trends Biotechnol. 16:61-65.
    • (1998) Trends Biotechnol. , vol.16 , pp. 61-65
    • Prevelige, P.E.1
  • 35
    • 0037705348 scopus 로고    scopus 로고
    • Observed hysteresis of virus capsid assembly is implicit in kinetic models of assembly
    • Singh, S., and A. Zlotnick. 2003. Observed hysteresis of virus capsid assembly is implicit in kinetic models of assembly. J. Biol. Chem. 278:18249-18255.
    • (2003) J. Biol. Chem. , vol.278 , pp. 18249-18255
    • Singh, S.1    Zlotnick, A.2
  • 36
    • 0028059187 scopus 로고
    • To build a virus capsid. An equilibrium model of the self-assembly of polyhedral protein complexes
    • Zlotnick, A. 1994. To build a virus capsid. An equilibrium model of the self-assembly of polyhedral protein complexes. J. Mol. Biol. 241:59-67.
    • (1994) J. Mol. Biol. , vol.241 , pp. 59-67
    • Zlotnick, A.1
  • 37
    • 22444445178 scopus 로고    scopus 로고
    • A reaction landscape identifies the intermediates critical for self-assembly of virus capsids and other polyhedral structures
    • Endres, D., M. Miyahara, P. Moisant, and A. Zlotnick. 2005. A reaction landscape identifies the intermediates critical for self-assembly of virus capsids and other polyhedral structures. Protein Sci. 6:1518-1525.
    • (2005) Protein Sci. , vol.6 , pp. 1518-1525
    • Endres, D.1    Miyahara, M.2    Moisant, P.3    Zlotnick, A.4
  • 40
    • 33646181737 scopus 로고    scopus 로고
    • Theory of supramolecular polymerization
    • A. Ciferri, editor. CRC Press, Boca Raton, FL
    • van der Schoot, P. 2005. Theory of supramolecular polymerization. In Supramolecular Polymers, 2nd Ed. A. Ciferri, editor. CRC Press, Boca Raton, FL.
    • (2005) Supramolecular Polymers, 2nd Ed.
    • Van Der Schoot, P.1
  • 41
    • 0036467249 scopus 로고    scopus 로고
    • Potential of mean force for protein-protein interaction studies
    • Jiang, L., Y. Gao, R. Mao, Z. Lia, and L. Lai. 2002. Potential of mean force for protein-protein interaction studies. Proteins Struct. Funct. Gen. 46:190-196.
    • (2002) Proteins Struct. Funct. Gen. , vol.46 , pp. 190-196
    • Jiang, L.1    Gao, Y.2    Mao, R.3    Lia, Z.4    Lai, L.5
  • 43
    • 33646908249 scopus 로고    scopus 로고
    • Length scale for configurational entropy in microemulsions
    • Reiss, H., W. K. Kegel, and J. Groenewold. 1996. Length scale for configurational entropy in microemulsions. Ber. Bunsenges. Phys. Chem. 100:279-295.
    • (1996) Ber. Bunsenges. Phys. Chem. , vol.100 , pp. 279-295
    • Reiss, H.1    Kegel, W.K.2    Groenewold, J.3
  • 45
    • 0346366811 scopus 로고    scopus 로고
    • Interaction with capsid protein alters RNA structure and the pathway for in vitro assembly of Cowpea Chlorotic Mottle virus
    • Johnson, J. M., D. A. Willits, M. J. Young, and A. Zlotnick. 2004. Interaction with capsid protein alters RNA structure and the pathway for in vitro assembly of Cowpea Chlorotic Mottle virus. J. Mol. Biol. 335:455-464.
    • (2004) J. Mol. Biol. , vol.335 , pp. 455-464
    • Johnson, J.M.1    Willits, D.A.2    Young, M.J.3    Zlotnick, A.4
  • 46
    • 12344263557 scopus 로고    scopus 로고
    • Calcium ions affect the HBV core assembly
    • Choi, Y., S. G. Park, J. Yoo, and G. Jung. 2005. Calcium ions affect the HBV core assembly. Virology. 332:454-463.
    • (2005) Virology , vol.332 , pp. 454-463
    • Choi, Y.1    Park, S.G.2    Yoo, J.3    Jung, G.4
  • 47
    • 3543096838 scopus 로고    scopus 로고
    • Zinc ions trigger conformational change and oligomerization of Hepatitis B Virus capsid protein
    • Stray, S. J., P. Ceres, and A. Zlotnick. 2004. Zinc ions trigger conformational change and oligomerization of Hepatitis B Virus capsid protein. Biochemistry. 43:9989-9998.
    • (2004) Biochemistry , vol.43 , pp. 9989-9998
    • Stray, S.J.1    Ceres, P.2    Zlotnick, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.