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Volumn 22, Issue 2, 2006, Pages 554-560

Assembly of human papillomavirus type-16 virus-like particles: Multifactorial study of assembly and competing aggregation

Author keywords

[No Author keywords available]

Indexed keywords

AGGLOMERATION; CRYSTALLIZATION; ESCHERICHIA COLI; FLUORESCENCE; SPECTROSCOPIC ANALYSIS; VIRUSES;

EID: 33646065318     PISSN: 87567938     EISSN: None     Source Type: Journal    
DOI: 10.1021/bp0502781     Document Type: Article
Times cited : (36)

References (23)
  • 1
    • 0035888074 scopus 로고    scopus 로고
    • Estimating the world cancer burden: GLOBOCAN 2000
    • Parkin, D. M.; Bray, F.; Ferlay, J.; Pisani, P. Estimating the world cancer burden: GLOBOCAN 2000. Int. J. Cancer 2001, 94, 153-156.
    • (2001) Int. J. Cancer , vol.94 , pp. 153-156
    • Parkin, D.M.1    Bray, F.2    Ferlay, J.3    Pisani, P.4
  • 5
    • 8444249386 scopus 로고    scopus 로고
    • Efficacy of a bivalent L1 virus-like particle vaccine in prevention of infection with human papillomavirus types 16 and 18 in young women: A randomised controlled trial
    • Harper, D. M.; Franco, E. L.; Wheeler, C.; Ferris, D. G.; Jenkins, D.; Schuind, A.; Zahaf, T.; Innis, B.; Naud, P.; De Carvalho, N. S. Efficacy of a bivalent L1 virus-like particle vaccine in prevention of infection with human papillomavirus types 16 and 18 in young women: a randomised controlled trial. Lancet 2004, 364, 1757-1765.
    • (2004) Lancet , vol.364 , pp. 1757-1765
    • Harper, D.M.1    Franco, E.L.2    Wheeler, C.3    Ferris, D.G.4    Jenkins, D.5    Schuind, A.6    Zahaf, T.7    Innis, B.8    Naud, P.9    De Carvalho, N.S.10
  • 6
    • 0026329210 scopus 로고
    • Structures of bovine and human papillomaviruses - Analysis by cryoelectron microscopy and 3-dimensional image-reconstruction
    • Baker, T. S.; Newcomb, W. W.; Olson, N. H.; Cowsert, L. M.; Olson, C.; Brown, J. C. Structures of bovine and human papillomaviruses - Analysis by cryoelectron microscopy and 3-dimensional image-reconstruction. Biophys. J. 1991, 60, 1445-1456.
    • (1991) Biophys. J. , vol.60 , pp. 1445-1456
    • Baker, T.S.1    Newcomb, W.W.2    Olson, N.H.3    Cowsert, L.M.4    Olson, C.5    Brown, J.C.6
  • 7
    • 0031936604 scopus 로고    scopus 로고
    • Intercapsomeric disulfide bonds in papillomavirus assembly and disassembly
    • Li, M. L.; Beard, P.; Estes, P. A.; Lyon, M. K.; Garcea, R. L. Intercapsomeric disulfide bonds in papillomavirus assembly and disassembly. J. Virol. 1998, 72, 2160-2167.
    • (1998) J. Virol. , vol.72 , pp. 2160-2167
    • Li, M.L.1    Beard, P.2    Estes, P.A.3    Lyon, M.K.4    Garcea, R.L.5
  • 8
    • 0031777693 scopus 로고    scopus 로고
    • Papillomavirus assembly requires trimerization of the major capsid protein by disulfides between two highly conserved cysteines
    • Sapp, M.; Fligge, C.; Petzak, I.; Harris, J. R.; Streeck, R. E. Papillomavirus assembly requires trimerization of the major capsid protein by disulfides between two highly conserved cysteines. J. Virol. 1998, 72, 6186-6189.
    • (1998) J. Virol. , vol.72 , pp. 6186-6189
    • Sapp, M.1    Fligge, C.2    Petzak, I.3    Harris, J.R.4    Streeck, R.E.5
  • 9
    • 0037119997 scopus 로고    scopus 로고
    • Atomic model of the papillomavirus capsid
    • Modis, Y.; Trus, B. L.; Harrison, S. C. Atomic model of the papillomavirus capsid. EMBO J. 2002, 21, 4754-4762.
    • (2002) EMBO J. , vol.21 , pp. 4754-4762
    • Modis, Y.1    Trus, B.L.2    Harrison, S.C.3
  • 10
    • 0033696899 scopus 로고    scopus 로고
    • Structure of small virus-like particles assembled from the L1 protein of human papillomavirus 16
    • Chen, X. J. S.; Garcea, R. L.; Goldberg, I.; Casini, G.; Harrison, S. C. Structure of small virus-like particles assembled from the L1 protein of human papillomavirus 16. Mol. Cell 2000, 5, 557-567.
    • (2000) Mol. Cell , vol.5 , pp. 557-567
    • Chen, X.J.S.1    Garcea, R.L.2    Goldberg, I.3    Casini, G.4    Harrison, S.C.5
  • 11
    • 0029112188 scopus 로고
    • Organization of the major and minor capsid proteins in human papillomavirus type-33 virus-like particles
    • Sapp, M.; Volpers, C.; Muller, M.; Streeck, R. E. Organization of the major and minor capsid proteins in human papillomavirus type-33 virus-like particles. J. Gen. Virol. 1995, 76, 2407-2412.
    • (1995) J. Gen. Virol. , vol.76 , pp. 2407-2412
    • Sapp, M.1    Volpers, C.2    Muller, M.3    Streeck, R.E.4
  • 12
    • 0031974862 scopus 로고    scopus 로고
    • Quantitative disassembly and reassembly of human papillomavirus type 11 viruslike particles in vitro
    • McCarthy, M. P.; White, W. I.; PalmerHill, F.; Koenig, S.; Suzich, J. A. Quantitative disassembly and reassembly of human papillomavirus type 11 viruslike particles in vitro. J. Virol. 1998, 72, 32-41.
    • (1998) J. Virol. , vol.72 , pp. 32-41
    • McCarthy, M.P.1    White, W.I.2    Palmerhill, F.3    Koenig, S.4    Suzich, J.A.5
  • 13
    • 0031900355 scopus 로고    scopus 로고
    • Calcium is required in reassembly of bovine papillomavirus in vitro
    • Paintsil, J.; Muller, M.; Picken, M.; Gissmann, L.; Zhou, J. Calcium is required in reassembly of bovine papillomavirus in vitro. J. Gen. Virol. 1998, 79, 1133-1141.
    • (1998) J. Gen. Virol. , vol.79 , pp. 1133-1141
    • Paintsil, J.1    Muller, M.2    Picken, M.3    Gissmann, L.4    Zhou, J.5
  • 14
    • 0035896012 scopus 로고    scopus 로고
    • Papillomavirus capsid protein expression in Escherichia coli: Purification and assembly of HPV11 and HPV16 L1
    • Chen, X. J. S.; Casini, G.; Harrison, S. C.; Garcea, R. L. Papillomavirus capsid protein expression in Escherichia coli: Purification and assembly of HPV11 and HPV16 L1. J. Mol. Biol. 2001, 307, 173-182.
    • (2001) J. Mol. Biol. , vol.307 , pp. 173-182
    • Chen, X.J.S.1    Casini, G.2    Harrison, S.C.3    Garcea, R.L.4
  • 16
    • 0030245737 scopus 로고    scopus 로고
    • Surface conformational and linear epitopes on HPV-16 and HPV-18 L1 virus-like particles as defined by monoclonal antibodies
    • Christensen, N. D.; Dillner, J.; Eklund, C.; Carter, J. J.; Wipf, G. C.; Reed, C. A.; Cladel, N. M.; Galloway, D. A. Surface conformational and linear epitopes on HPV-16 and HPV-18 L1 virus-like particles as defined by monoclonal antibodies. Virology 1996, 223, 174-184.
    • (1996) Virology , vol.223 , pp. 174-184
    • Christensen, N.D.1    Dillner, J.2    Eklund, C.3    Carter, J.J.4    Wipf, G.C.5    Reed, C.A.6    Cladel, N.M.7    Galloway, D.A.8
  • 18
    • 0014937559 scopus 로고
    • Formation of three-dimensional structures in proteins. Rapid nonenzymic reactivation of reduced lysozyme
    • Saxena, V. P.; Wetlaufer, D. B. Formation of three-dimensional structures in proteins. Rapid nonenzymic reactivation of reduced lysozyme. Biochemistry 1970, 9, 5015-5022.
    • (1970) Biochemistry , vol.9 , pp. 5015-5022
    • Saxena, V.P.1    Wetlaufer, D.B.2
  • 19
    • 0032867418 scopus 로고    scopus 로고
    • Folding dynamics of the B1 domain of protein C explored by ultrarapid mixing
    • Park, S. H.; Shastry, M. C. R.; Roder, H. Folding dynamics of the B1 domain of protein C explored by ultrarapid mixing. Nat. Struct. Biol. 1999, 6, 943-947.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 943-947
    • Park, S.H.1    Shastry, M.C.R.2    Roder, H.3
  • 20
    • 0034680784 scopus 로고    scopus 로고
    • Multisite fluorescence in proteins with multiple tryptophan residues - Apomyoglobin natural variants and site-directed mutants
    • Tcherkasskaya, O.; Bychkova, V. E.; Uversky, V. N.; Gronenborn, A. M. Multisite fluorescence in proteins with multiple tryptophan residues - Apomyoglobin natural variants and site-directed mutants. J. Biol Chem. 2000, 275, 36285-36294.
    • (2000) J. Biol Chem. , vol.275 , pp. 36285-36294
    • Tcherkasskaya, O.1    Bychkova, V.E.2    Uversky, V.N.3    Gronenborn, A.M.4
  • 21
    • 0035028745 scopus 로고    scopus 로고
    • Mechanisms of tryptophan fluorescence shifts in proteins
    • Vivian, J. T.; Callis, P. R. Mechanisms of tryptophan fluorescence shifts in proteins. Biophys. J. 2001, 80, 2093-2109.
    • (2001) Biophys. J. , vol.80 , pp. 2093-2109
    • Vivian, J.T.1    Callis, P.R.2
  • 22
    • 1942469376 scopus 로고    scopus 로고
    • Stopped-flow fluorescence analysis of the conformational changes in the GroEL apical domain - Relationships between movements in the apical domain and the quaternary structure of GroEL
    • Taniguchi, M.; Yoshimi, T.; Kongo, K.; Mizobata, T.; Kawata, Y. Stopped-flow fluorescence analysis of the conformational changes in the GroEL apical domain - Relationships between movements in the apical domain and the quaternary structure of GroEL. J. Biol. Chem. 2004, 279, 16368-16376.
    • (2004) J. Biol. Chem. , vol.279 , pp. 16368-16376
    • Taniguchi, M.1    Yoshimi, T.2    Kongo, K.3    Mizobata, T.4    Kawata, Y.5
  • 23
    • 3142634785 scopus 로고    scopus 로고
    • In vitro papillomavirus capsid assembly analyzed by light scattering
    • Accepted for publication December 14, 2005
    • Casini, G. L.; Graham, D.; Heine, D.; Garcea, R. L.; Wu, D. T. In vitro papillomavirus capsid assembly analyzed by light scattering. Virology 2004, 325, 320-327. Accepted for publication December 14, 2005.
    • (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.