메뉴 건너뛰기




Volumn 80, Issue , 2005, Pages 135-168

Virus-Like Particles: Models for Assembly Studies and Foreign Epitope Carriers

Author keywords

[No Author keywords available]

Indexed keywords

DRUG CARRIER; EPITOPE; VIRUS PROTEIN;

EID: 33644693157     PISSN: 00796603     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0079-6603(05)80004-2     Document Type: Review
Times cited : (25)

References (163)
  • 1
    • 0029801019 scopus 로고    scopus 로고
    • Genetically engineered particulate virus-like structures and their use as vaccine delivery systems
    • Roy P. Genetically engineered particulate virus-like structures and their use as vaccine delivery systems. Intervirology 39 (1996) 62-71
    • (1996) Intervirology , vol.39 , pp. 62-71
    • Roy, P.1
  • 2
    • 0034884150 scopus 로고    scopus 로고
    • Use of the baculovirus expression system for the generation of virus-like particles
    • Casal J.I. Use of the baculovirus expression system for the generation of virus-like particles. Biotechnol. Genetic Engineering Rev. 18 (2001) 73-87
    • (2001) Biotechnol. Genetic Engineering Rev. , vol.18 , pp. 73-87
    • Casal, J.I.1
  • 3
    • 0034820497 scopus 로고    scopus 로고
    • Analysis of minimal sequences on JC virus VP1 required for capsid assembly
    • Ou W.C., Chen L.H., Wang M., Hseu T.H., and Chang D. Analysis of minimal sequences on JC virus VP1 required for capsid assembly. J. Neurovirol. 7 (2001) 298-301
    • (2001) J. Neurovirol. , vol.7 , pp. 298-301
    • Ou, W.C.1    Chen, L.H.2    Wang, M.3    Hseu, T.H.4    Chang, D.5
  • 4
    • 0034889864 scopus 로고    scopus 로고
    • HBV core particles as a carrier for B cell/T cell epitopes
    • Pumpens P., and Grens E. HBV core particles as a carrier for B cell/T cell epitopes. Intervirology 44 (2001) 98-114
    • (2001) Intervirology , vol.44 , pp. 98-114
    • Pumpens, P.1    Grens, E.2
  • 5
    • 0035405173 scopus 로고    scopus 로고
    • Papillomavirus-like particle based vaccines: Cervical cancer and beyond
    • Schiller J.T., and Lowy D.R. Papillomavirus-like particle based vaccines: Cervical cancer and beyond. Expert Opin. Biol. Therapy 1 (2001) 571-581
    • (2001) Expert Opin. Biol. Therapy , vol.1 , pp. 571-581
    • Schiller, J.T.1    Lowy, D.R.2
  • 7
    • 0034715825 scopus 로고    scopus 로고
    • Mechanism of capsid assembly for an icosahedral plant virus
    • Zlotnick A., Aldrich R., Johnson J.M., Ceres P., and Young M.J. Mechanism of capsid assembly for an icosahedral plant virus. Virology 277 (2000) 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
  • 8
    • 0026649563 scopus 로고
    • Expression, self-assembly, and antigenicity of the Norwalk virus capsid protein
    • Jiang X., Wang M., Graham D.Y., and Estes M.K. Expression, self-assembly, and antigenicity of the Norwalk virus capsid protein. J. Virol. 66 (1992) 6527-6532
    • (1992) J. Virol. , vol.66 , pp. 6527-6532
    • Jiang, X.1    Wang, M.2    Graham, D.Y.3    Estes, M.K.4
  • 9
    • 0027240069 scopus 로고
    • Comparison of the reactivities of baculovirus-expressed recombinant Norwalk virus capsid antigen with those of the native Norwalk virus antigen in serologic assays and some epidemiologic observations
    • Green K.Y., Lew J.F., Jiang X., Kapikian A.Z., and Estes M.K. Comparison of the reactivities of baculovirus-expressed recombinant Norwalk virus capsid antigen with those of the native Norwalk virus antigen in serologic assays and some epidemiologic observations. J. Clin. Microbiol. 31 (1993) 2185-2191
    • (1993) J. Clin. Microbiol. , vol.31 , pp. 2185-2191
    • Green, K.Y.1    Lew, J.F.2    Jiang, X.3    Kapikian, A.Z.4    Estes, M.K.5
  • 11
    • 0036199391 scopus 로고    scopus 로고
    • Structural requirements for the assembly of Norwalk virus-like particles
    • Bertolotti-Ciarlet A., White L.J., Chen R., Prasad B.V., and Estes M.K. Structural requirements for the assembly of Norwalk virus-like particles. J. Virol. 76 (2002) 4044-4055
    • (2002) J. Virol. , vol.76 , pp. 4044-4055
    • Bertolotti-Ciarlet, A.1    White, L.J.2    Chen, R.3    Prasad, B.V.4    Estes, M.K.5
  • 14
    • 0037334085 scopus 로고    scopus 로고
    • Two nonoverlapping domains on the Norwalk virus open reading frame 3 (ORF3) protein are involved in the formation of the phosphorylated 35K protein and in ORF3-capsid protein interactions
    • Glass P.J., Zeng C.Q., and Estes M.K. Two nonoverlapping domains on the Norwalk virus open reading frame 3 (ORF3) protein are involved in the formation of the phosphorylated 35K protein and in ORF3-capsid protein interactions. J. Virol. 77 (2003) 3569-3577
    • (2003) J. Virol. , vol.77 , pp. 3569-3577
    • Glass, P.J.1    Zeng, C.Q.2    Estes, M.K.3
  • 15
    • 0142060853 scopus 로고    scopus 로고
    • The 3′ end of Norwalk virus mRNA contains determinants that regulate the expression and stability of the viral capsid protein VP1: A novel function for the VP2 protein
    • Bertolotti-Ciarlet A., Crawford S.E., Hutson A.M., and Estes M.K. The 3′ end of Norwalk virus mRNA contains determinants that regulate the expression and stability of the viral capsid protein VP1: A novel function for the VP2 protein. J. Virol. 77 (2003) 11603-11615
    • (2003) J. Virol. , vol.77 , pp. 11603-11615
    • Bertolotti-Ciarlet, A.1    Crawford, S.E.2    Hutson, A.M.3    Estes, M.K.4
  • 16
    • 0037231935 scopus 로고    scopus 로고
    • Snow Mountain virus genome sequence and virus-like particle assembly
    • Lochridge V.P., and Hardy M.E. Snow Mountain virus genome sequence and virus-like particle assembly. Virus Genes 26 (2003) 71-82
    • (2003) Virus Genes , vol.26 , pp. 71-82
    • Lochridge, V.P.1    Hardy, M.E.2
  • 17
    • 0034086316 scopus 로고    scopus 로고
    • Protein requirements for assembly of virus-like particles of Junonia coenia densovirus in insect cells
    • Croizier L., Jousset F.X., Veyrunes J.C., Lopez-Ferber M., Bergoin M., and Croizier G. Protein requirements for assembly of virus-like particles of Junonia coenia densovirus in insect cells. J. Gen. Virol. 81 (2000) 1605-1613
    • (2000) J. Gen. Virol. , vol.81 , pp. 1605-1613
    • Croizier, L.1    Jousset, F.X.2    Veyrunes, J.C.3    Lopez-Ferber, M.4    Bergoin, M.5    Croizier, G.6
  • 19
    • 0030273361 scopus 로고    scopus 로고
    • Capsid proteins of cowpea mosaic virus transiently expressed in protoplasts form virus-like particles
    • Wellink J., Verver J., Van Lent J., and Van Kammen A. Capsid proteins of cowpea mosaic virus transiently expressed in protoplasts form virus-like particles. Virology 224 (1996) 352-355
    • (1996) Virology , vol.224 , pp. 352-355
    • Wellink, J.1    Verver, J.2    Van Lent, J.3    Van Kammen, A.4
  • 20
    • 0034529270 scopus 로고    scopus 로고
    • Coexpression of the capsid proteins of Cowpea mosaic virus in insect cells leads to the formation of virus-like particles
    • Shanks M., and Lomonossoff G.P. Coexpression of the capsid proteins of Cowpea mosaic virus in insect cells leads to the formation of virus-like particles. J. Gen. Virol. 81 (2000) 3093-3097
    • (2000) J. Gen. Virol. , vol.81 , pp. 3093-3097
    • Shanks, M.1    Lomonossoff, G.P.2
  • 21
    • 0030814904 scopus 로고    scopus 로고
    • Molecular cloning, sequencing, functional analysis, and expression in E. coli of major core protein gene (S3) of rice dwarf virus Chinese isolate
    • Zhang F., Li Y., Liu Y., An C., and Chen Z. Molecular cloning, sequencing, functional analysis, and expression in E. coli of major core protein gene (S3) of rice dwarf virus Chinese isolate. Acta Virologica 41 (1997) 161-168
    • (1997) Acta Virologica , vol.41 , pp. 161-168
    • Zhang, F.1    Li, Y.2    Liu, Y.3    An, C.4    Chen, Z.5
  • 22
    • 0033819795 scopus 로고    scopus 로고
    • Assembly of double-shelled, virus-like particles in transgenic rice plants expressing two major structural proteins of rice dwarf virus
    • Zheng H., Yu L., Wei C., Hu D., Shen Y., Chen Z., and Li Y. Assembly of double-shelled, virus-like particles in transgenic rice plants expressing two major structural proteins of rice dwarf virus. J. Virol. 74 (2000) 9808-9810
    • (2000) J. Virol. , vol.74 , pp. 9808-9810
    • Zheng, H.1    Yu, L.2    Wei, C.3    Hu, D.4    Shen, Y.5    Chen, Z.6    Li, Y.7
  • 23
    • 0037384087 scopus 로고    scopus 로고
    • Assembly of single-shelled cores and double-shelled virus-like particles after baculovirus expression of major structural proteins P3, P7, and P8 of Rice dwarf virus
    • Hagiwara K., Higashi T., Namba K., Uehara-Ichiki T., and Omura T. Assembly of single-shelled cores and double-shelled virus-like particles after baculovirus expression of major structural proteins P3, P7, and P8 of Rice dwarf virus. J. Gen. Virol. 84 (2003) 981-984
    • (2003) J. Gen. Virol. , vol.84 , pp. 981-984
    • Hagiwara, K.1    Higashi, T.2    Namba, K.3    Uehara-Ichiki, T.4    Omura, T.5
  • 24
    • 1542347737 scopus 로고    scopus 로고
    • The amino-terminal region of major capsid protein P3 is essential for self-assembly of single-shelled core-like particles of Rice dwarf virus
    • Hagiwara K., Higashi T., Miyazaki N., Naitow H., Cheng R.H., Nakagawa A., Mizuno H., Tsukihara T., and Omura T. The amino-terminal region of major capsid protein P3 is essential for self-assembly of single-shelled core-like particles of Rice dwarf virus. J. Virol. 78 (2004) 3145-3148
    • (2004) J. Virol. , vol.78 , pp. 3145-3148
    • Hagiwara, K.1    Higashi, T.2    Miyazaki, N.3    Naitow, H.4    Cheng, R.H.5    Nakagawa, A.6    Mizuno, H.7    Tsukihara, T.8    Omura, T.9
  • 26
    • 0035815102 scopus 로고    scopus 로고
    • Structural studies on the empty capsids of Physalis mottle virus
    • Krishna S.S., Sastri M., Savithri H.S., and Murthy M.R. Structural studies on the empty capsids of Physalis mottle virus. J. Mol. Biol. 307 (2001) 1035-1047
    • (2001) J. Mol. Biol. , vol.307 , pp. 1035-1047
    • Krishna, S.S.1    Sastri, M.2    Savithri, H.S.3    Murthy, M.R.4
  • 27
    • 0031551580 scopus 로고    scopus 로고
    • Assembly of physalis mottle virus capsid protein in Escherichia coli and the role of amino and carboxy termini in the formation of the icosahedral particles
    • Sastri M., Kekuda R., Gopinath K., Kumar C.T., Jagath J.R., and Savithri H.S. Assembly of physalis mottle virus capsid protein in Escherichia coli and the role of amino and carboxy termini in the formation of the icosahedral particles. J. Mol. Biol. 272 (1997) 541-552
    • (1997) J. Mol. Biol. , vol.272 , pp. 541-552
    • Sastri, M.1    Kekuda, R.2    Gopinath, K.3    Kumar, C.T.4    Jagath, J.R.5    Savithri, H.S.6
  • 28
    • 0032981431 scopus 로고    scopus 로고
    • Identification of a discrete intermediate in the assembly/disassembly of physalis mottle tymovirus through mutational analysis
    • Sastri M., Reddy D.S., Krishna S.S., Murthy M.R., and Savithri H.S. Identification of a discrete intermediate in the assembly/disassembly of physalis mottle tymovirus through mutational analysis. J. Mol. Biol. 289 (1999) 905-918
    • (1999) J. Mol. Biol. , vol.289 , pp. 905-918
    • Sastri, M.1    Reddy, D.S.2    Krishna, S.S.3    Murthy, M.R.4    Savithri, H.S.5
  • 29
    • 0037458571 scopus 로고    scopus 로고
    • Mutation of interfacial residues disrupts subunit folding and particle assembly of Physalis mottle tymovirus
    • Umashankar M., Murthy M.R., and Savithri H.S. Mutation of interfacial residues disrupts subunit folding and particle assembly of Physalis mottle tymovirus. J. Biol. Chem. 278 (2003) 6145-6152
    • (2003) J. Biol. Chem. , vol.278 , pp. 6145-6152
    • Umashankar, M.1    Murthy, M.R.2    Savithri, H.S.3
  • 30
    • 0023643240 scopus 로고
    • Site-directed mutation affecting polyomavirus capsid self-assembly in vitro
    • Garcea R.L., Salunke D.M., and Caspar D.L. Site-directed mutation affecting polyomavirus capsid self-assembly in vitro. Nature 329 (1987) 86-87
    • (1987) Nature , vol.329 , pp. 86-87
    • Garcea, R.L.1    Salunke, D.M.2    Caspar, D.L.3
  • 31
    • 0029937815 scopus 로고    scopus 로고
    • Purification, characterization, assembly, and crystallization of assembled alfalfa mosaic virus coat protein expressed in Escherichia coli
    • Yusibov V., Kumar A., North A., Johnson J.E., and Loesch-Fries L.S. Purification, characterization, assembly, and crystallization of assembled alfalfa mosaic virus coat protein expressed in Escherichia coli. J. Gen. Virol. 77 (1996) 567-573
    • (1996) J. Gen. Virol. , vol.77 , pp. 567-573
    • Yusibov, V.1    Kumar, A.2    North, A.3    Johnson, J.E.4    Loesch-Fries, L.S.5
  • 32
    • 0033587647 scopus 로고    scopus 로고
    • Effect of C-terminal mutations of alfalfa mosaic virus coat protein on dimer formation and assembly in vitro
    • Choi J., and Loesch-Fries L.S. Effect of C-terminal mutations of alfalfa mosaic virus coat protein on dimer formation and assembly in vitro. Virology 260 (1999) 182-189
    • (1999) Virology , vol.260 , pp. 182-189
    • Choi, J.1    Loesch-Fries, L.S.2
  • 33
    • 0029886822 scopus 로고    scopus 로고
    • Assembly of virus-like particles in insect cells infected with a baculovirus containing a modified coat protein gene of potato leafroll luteovirus
    • Lamb J.W., Duncan G.H., Reavy B., Gildow F.E., Mayo M.A., and Hay R.T. Assembly of virus-like particles in insect cells infected with a baculovirus containing a modified coat protein gene of potato leafroll luteovirus. J. Gen. Virol. 77 (1996) 1349-1358
    • (1996) J. Gen. Virol. , vol.77 , pp. 1349-1358
    • Lamb, J.W.1    Duncan, G.H.2    Reavy, B.3    Gildow, F.E.4    Mayo, M.A.5    Hay, R.T.6
  • 34
    • 0034751125 scopus 로고    scopus 로고
    • Alphavirus nucleocapsid protein contains a putative coiled coil alpha-helix important for core assembly
    • Perera R., Owen K.E., Tellinghuisen T.L., Gorbalenya A.E., and Kuhn R.J. Alphavirus nucleocapsid protein contains a putative coiled coil alpha-helix important for core assembly. J. Virol. 75 (2001) 1-10
    • (2001) J. Virol. , vol.75 , pp. 1-10
    • Perera, R.1    Owen, K.E.2    Tellinghuisen, T.L.3    Gorbalenya, A.E.4    Kuhn, R.J.5
  • 35
    • 0038447231 scopus 로고    scopus 로고
    • A heterologous coiled coil can substitute for helix I of the Sindbis virus capsid protein
    • Perera R., Navaratnarajah C., and Kuhn R.J. A heterologous coiled coil can substitute for helix I of the Sindbis virus capsid protein. J. Virol. 77 (2003) 8345-8353
    • (2003) J. Virol. , vol.77 , pp. 8345-8353
    • Perera, R.1    Navaratnarajah, C.2    Kuhn, R.J.3
  • 36
    • 0033614130 scopus 로고    scopus 로고
    • Self-assembly of tobacco mosaic virus: The role of an intermediate aggregate in generating both specificity and speed
    • Butler P.J. Self-assembly of tobacco mosaic virus: The role of an intermediate aggregate in generating both specificity and speed. Philosophical Transactions: Biological Sciences. The Royal Society London 354 (1999) 537-550
    • (1999) Philosophical Transactions: Biological Sciences. The Royal Society London , vol.354 , pp. 537-550
    • Butler, P.J.1
  • 37
    • 0028557224 scopus 로고
    • Expression of tobacco mosaic virus coat protein and assembly of pseudovirus particles in Escherichia coli
    • Hwang D.J., Roberts I.M., and Wilson T.M. Expression of tobacco mosaic virus coat protein and assembly of pseudovirus particles in Escherichia coli. Proc. Natl. Acad. Sci. USA 91 (1994) 9067-9071
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9067-9071
    • Hwang, D.J.1    Roberts, I.M.2    Wilson, T.M.3
  • 38
    • 0033971483 scopus 로고    scopus 로고
    • Virus-like particles assemble in plants and bacteria expressing the coat protein gene of Indian peanut clump virus
    • Bragard C., Duncan G.H., Wesley S.V., Naidu R.A., and Mayo M.A. Virus-like particles assemble in plants and bacteria expressing the coat protein gene of Indian peanut clump virus. J. Gen. Virol. 81 (2000) 267-272
    • (2000) J. Gen. Virol. , vol.81 , pp. 267-272
    • Bragard, C.1    Duncan, G.H.2    Wesley, S.V.3    Naidu, R.A.4    Mayo, M.A.5
  • 39
    • 0025772721 scopus 로고
    • Expression of potyvirus coat protein in Escherichia coli and yeast and its assembly into virus-like particles
    • Jagadish M.N., Ward C.W., Gough K.H., Tulloch P.A., Whittaker L.A., and Shukla D.D. Expression of potyvirus coat protein in Escherichia coli and yeast and its assembly into virus-like particles. J. Gen. Virol. 72 (1991) 1543-1550
    • (1991) J. Gen. Virol. , vol.72 , pp. 1543-1550
    • Jagadish, M.N.1    Ward, C.W.2    Gough, K.H.3    Tulloch, P.A.4    Whittaker, L.A.5    Shukla, D.D.6
  • 40
    • 0027210575 scopus 로고
    • Site-directed mutagenesis of a potyvirus coat protein and its assembly in Escherichia coli
    • Jagadish M.N., Huang D., and Ward C.W. Site-directed mutagenesis of a potyvirus coat protein and its assembly in Escherichia coli. J. Gen. Virol. 74 (1993) 893-896
    • (1993) J. Gen. Virol. , vol.74 , pp. 893-896
    • Jagadish, M.N.1    Huang, D.2    Ward, C.W.3
  • 42
    • 0032858731 scopus 로고    scopus 로고
    • Determination of 3′-terminal nucleotide sequence of pepper vein banding virus RNA and expression of its coat protein in Escherichia coli
    • Joseph J., and Savithri H.S. Determination of 3′-terminal nucleotide sequence of pepper vein banding virus RNA and expression of its coat protein in Escherichia coli. Arch. Virol. 144 (1999) 1679-1687
    • (1999) Arch. Virol. , vol.144 , pp. 1679-1687
    • Joseph, J.1    Savithri, H.S.2
  • 43
    • 0344982812 scopus 로고    scopus 로고
    • Surface-exposed amino- and carboxy-terminal residues are crucial for the initiation of assembly in Pepper vein banding virus: A flexuous rod-shaped virus
    • Anindya R., and Savithri H.S. Surface-exposed amino- and carboxy-terminal residues are crucial for the initiation of assembly in Pepper vein banding virus: A flexuous rod-shaped virus. Virology 316 (2003) 325-336
    • (2003) Virology , vol.316 , pp. 325-336
    • Anindya, R.1    Savithri, H.S.2
  • 44
    • 0034662748 scopus 로고    scopus 로고
    • Freedom and restraint: Themes in virus capsid assembly
    • Dokland T. Freedom and restraint: Themes in virus capsid assembly. Structure Folding Design 8 (2000) R157-R162
    • (2000) Structure Folding Design , vol.8
    • Dokland, T.1
  • 45
    • 0029019922 scopus 로고
    • Assembly of the herpes simplex virus capsid: Requirement for the carboxyl-terminal twenty-five amino acids of the proteins encoded by the UL26 and UL26.5 genes
    • Thomsen D.R., Newcomb W.W., Brown J.C., and Homa F.L. Assembly of the herpes simplex virus capsid: Requirement for the carboxyl-terminal twenty-five amino acids of the proteins encoded by the UL26 and UL26.5 genes. J. Virol. 69 (1995) 3690-3703
    • (1995) J. Virol. , vol.69 , pp. 3690-3703
    • Thomsen, D.R.1    Newcomb, W.W.2    Brown, J.C.3    Homa, F.L.4
  • 46
    • 0028256487 scopus 로고
    • Assembly of herpes simplex virus type 1 capsids using a panel of recombinant baculoviruses
    • Tatman J.D., Preston V.G., Nicholson P., Elliott R.M., and Rixon F.J. Assembly of herpes simplex virus type 1 capsids using a panel of recombinant baculoviruses. J. Gen. Virol. 75 (1994) 1101-1113
    • (1994) J. Gen. Virol. , vol.75 , pp. 1101-1113
    • Tatman, J.D.1    Preston, V.G.2    Nicholson, P.3    Elliott, R.M.4    Rixon, F.J.5
  • 47
    • 0029007025 scopus 로고
    • The 25 amino acid residues at the carboxy terminus of the herpes simplex virus type 1 UL26.5 protein are required for the formation of the capsid shell around the scaffold
    • Kennard J., Rixon F.J., McDougall I.M., Tatman J.D., and Preston V.G. The 25 amino acid residues at the carboxy terminus of the herpes simplex virus type 1 UL26.5 protein are required for the formation of the capsid shell around the scaffold. J. Gen. Virol. 76 (1995) 1611-1621
    • (1995) J. Gen. Virol. , vol.76 , pp. 1611-1621
    • Kennard, J.1    Rixon, F.J.2    McDougall, I.M.3    Tatman, J.D.4    Preston, V.G.5
  • 48
    • 0029015830 scopus 로고
    • The C-terminal 25 amino acids of the protease and its substrate ICP35 of herpes simplex virus type 1 are involved in the formation of sealed capsids
    • Matusick-Kumar L., Newcomb W.W., Brown J.C., McCann P.J., Hurlburt W., Weinheimer S.P., and Gao M. The C-terminal 25 amino acids of the protease and its substrate ICP35 of herpes simplex virus type 1 are involved in the formation of sealed capsids. J. Virol. 69 (1995) 4347-4356
    • (1995) J. Virol. , vol.69 , pp. 4347-4356
    • Matusick-Kumar, L.1    Newcomb, W.W.2    Brown, J.C.3    McCann, P.J.4    Hurlburt, W.5    Weinheimer, S.P.6    Gao, M.7
  • 49
    • 0034766951 scopus 로고    scopus 로고
    • The UL6 gene product forms the portal for the entry of DNA into the herpes simplex virus capsid
    • Newcomb W.W., Juhas R.N., Thomsen D.R., Homa F.L., Burch A.D., Weller S.K., and Brown J.C. The UL6 gene product forms the portal for the entry of DNA into the herpes simplex virus capsid. J. Virol. 75 (2001) 10923-10932
    • (2001) J. Virol. , vol.75 , pp. 10923-10932
    • Newcomb, W.W.1    Juhas, R.N.2    Thomsen, D.R.3    Homa, F.L.4    Burch, A.D.5    Weller, S.K.6    Brown, J.C.7
  • 50
    • 0028102107 scopus 로고
    • Characterization of virus-like particles produced by the expression of rotavirus capsid proteins in insect cells
    • Crawford S.E., Labbe M., Cohen J., Burroughs M.H., Zhou Y.J., and Estes M.K. Characterization of virus-like particles produced by the expression of rotavirus capsid proteins in insect cells. J. Virol. 68 (1994) 5945-5952
    • (1994) J. Virol. , vol.68 , pp. 5945-5952
    • Crawford, S.E.1    Labbe, M.2    Cohen, J.3    Burroughs, M.H.4    Zhou, Y.J.5    Estes, M.K.6
  • 51
    • 0030768785 scopus 로고    scopus 로고
    • Three-dimensional structural analysis of recombinant rotavirus-like particles with intact and amino-terminal-deleted VP2: Implications for the architecture of the VP2 capsid layer
    • Lawton J.A., Zeng C.Q.-Y., Mukherjee S.K., Cohen J., Estes M.K., and Venkataram Prasad B.V. Three-dimensional structural analysis of recombinant rotavirus-like particles with intact and amino-terminal-deleted VP2: Implications for the architecture of the VP2 capsid layer. J. Virol. 71 (1997) 7353-7360
    • (1997) J. Virol. , vol.71 , pp. 7353-7360
    • Lawton, J.A.1    Zeng, C.Q.-Y.2    Mukherjee, S.K.3    Cohen, J.4    Estes, M.K.5    Venkataram Prasad, B.V.6
  • 52
    • 0031964884 scopus 로고    scopus 로고
    • The N terminus of rotavirus VP2 is necessary for encapsidation of VP1 and VP3
    • Zeng C.Q., Estes M.K., Charpilienne A., and Cohen J. The N terminus of rotavirus VP2 is necessary for encapsidation of VP1 and VP3. J. Virol. 72 (1998) 201-208
    • (1998) J. Virol. , vol.72 , pp. 201-208
    • Zeng, C.Q.1    Estes, M.K.2    Charpilienne, A.3    Cohen, J.4
  • 53
    • 0033065426 scopus 로고    scopus 로고
    • Heterotypic protection and induction of a broad heterotypic neutralization response by rotavirus-like particles
    • Crawford S.E., Estes M.K., Ciarlet M., Barone C., O'Neal C.M., Cohen J., and Conner M.E. Heterotypic protection and induction of a broad heterotypic neutralization response by rotavirus-like particles. J. Virol. 73 (1999) 4813-4822
    • (1999) J. Virol. , vol.73 , pp. 4813-4822
    • Crawford, S.E.1    Estes, M.K.2    Ciarlet, M.3    Barone, C.4    O'Neal, C.M.5    Cohen, J.6    Conner, M.E.7
  • 54
    • 0036434259 scopus 로고    scopus 로고
    • Production of hybrid double- or triple-layered virus-like particles of group A and C rotaviruses using a baculovirus expression system
    • Kim Y., Chang K.O., Kim W.Y., and Saif L.J. Production of hybrid double- or triple-layered virus-like particles of group A and C rotaviruses using a baculovirus expression system. Virology 302 (2002) 1-8
    • (2002) Virology , vol.302 , pp. 1-8
    • Kim, Y.1    Chang, K.O.2    Kim, W.Y.3    Saif, L.J.4
  • 55
    • 0026646877 scopus 로고
    • Expression of the major capsid protein VP6 of group C rotavirus and synthesis of chimeric single-shelled particles by using recombinant baculovirus
    • Tosser G., Labbe M., Bremont M., and Cohen J. Expression of the major capsid protein VP6 of group C rotavirus and synthesis of chimeric single-shelled particles by using recombinant baculovirus. J. Virol. 66 (1992) 5825-5831
    • (1992) J. Virol. , vol.66 , pp. 5825-5831
    • Tosser, G.1    Labbe, M.2    Bremont, M.3    Cohen, J.4
  • 56
    • 0025215056 scopus 로고
    • Synthesis of bluetongue virus (BTV) core-like particles by a baculovirus expressing the two major structural proteins of BTV
    • French T.J., and Roy P. Synthesis of bluetongue virus (BTV) core-like particles by a baculovirus expressing the two major structural proteins of BTV. J. Virol. 64 (1990) 1530-1536
    • (1990) J. Virol. , vol.64 , pp. 1530-1536
    • French, T.J.1    Roy, P.2
  • 57
    • 0030985897 scopus 로고    scopus 로고
    • Baculovirus multigene expression vectors and their use for understanding the assembly process of architecturally complex virus particles
    • Roy P., Mikhailov M., and Bishop D.H. Baculovirus multigene expression vectors and their use for understanding the assembly process of architecturally complex virus particles. Gene 190 (1997) 119-129
    • (1997) Gene , vol.190 , pp. 119-129
    • Roy, P.1    Mikhailov, M.2    Bishop, D.H.3
  • 58
    • 0025225427 scopus 로고
    • Assembly of double-shelled, virus-like particles of bluetongue virus by the simultaneous expression of four structural proteins
    • French T.J., Marshall J.J., and Roy P. Assembly of double-shelled, virus-like particles of bluetongue virus by the simultaneous expression of four structural proteins. Virology 64 (1990) 5695-5700
    • (1990) Virology , vol.64 , pp. 5695-5700
    • French, T.J.1    Marshall, J.J.2    Roy, P.3
  • 59
    • 0033851585 scopus 로고    scopus 로고
    • Functional dissection of the major structural protein of bluetongue virus: Identification of key residues within VP7 essential for capsid assembly
    • Limn C.K., Staeuber N., Monastyrskaya K., Gouet P., and Roy P. Functional dissection of the major structural protein of bluetongue virus: Identification of key residues within VP7 essential for capsid assembly. J. Virol. 74 (2000) 8658-8669
    • (2000) J. Virol. , vol.74 , pp. 8658-8669
    • Limn, C.K.1    Staeuber, N.2    Monastyrskaya, K.3    Gouet, P.4    Roy, P.5
  • 60
    • 0028334968 scopus 로고
    • Identification of doman in bluetongue virus VP3 molecules essential for the assembly of virus cores
    • Tanaka S., and Roy P. Identification of doman in bluetongue virus VP3 molecules essential for the assembly of virus cores. J. Virol. 68 (1994) 2795-2802
    • (1994) J. Virol. , vol.68 , pp. 2795-2802
    • Tanaka, S.1    Roy, P.2
  • 61
    • 0141453603 scopus 로고    scopus 로고
    • Intermolecular interactions in a two-layered viral capsid that requires a complex symmetry mismatch
    • Limn C.K., and Roy P. Intermolecular interactions in a two-layered viral capsid that requires a complex symmetry mismatch. J. Virol. 77 (2003) 11114-11124
    • (2003) J. Virol. , vol.77 , pp. 11114-11124
    • Limn, C.K.1    Roy, P.2
  • 62
    • 1942486246 scopus 로고    scopus 로고
    • The C-terminal domain of the pVP2 precursor is essential for the interaction between VP2 and VP3, the capsid polypeptides of infectious bursal disease virus
    • Ona A., Luque D., Abaitua F., Maraver A., Caston J.R., and Rodriguez J.F. The C-terminal domain of the pVP2 precursor is essential for the interaction between VP2 and VP3, the capsid polypeptides of infectious bursal disease virus. Virology 322 (2004) 135-142
    • (2004) Virology , vol.322 , pp. 135-142
    • Ona, A.1    Luque, D.2    Abaitua, F.3    Maraver, A.4    Caston, J.R.5    Rodriguez, J.F.6
  • 63
    • 0037688319 scopus 로고    scopus 로고
    • The oligomerization domain of VP3, the scaffolding protein of infectious bursal disease virus, plays a critical role in capsid assembly
    • Maraver A., Ona A., Abaitua F., Gonzalez D., Clemente R., Ruiz-Diaz J.A., Caston J.R., Pazos F., and Rodriguez J.F. The oligomerization domain of VP3, the scaffolding protein of infectious bursal disease virus, plays a critical role in capsid assembly. J. Virol. 77 (2003) 6438-6449
    • (2003) J. Virol. , vol.77 , pp. 6438-6449
    • Maraver, A.1    Ona, A.2    Abaitua, F.3    Gonzalez, D.4    Clemente, R.5    Ruiz-Diaz, J.A.6    Caston, J.R.7    Pazos, F.8    Rodriguez, J.F.9
  • 64
    • 1842510044 scopus 로고    scopus 로고
    • The last C-terminal residue of VP3, glutamic acid 257, controls capsid assembly of infectious bursal disease virus
    • Chevalier C., Lepault J., Da Costa B., and Delmas B. The last C-terminal residue of VP3, glutamic acid 257, controls capsid assembly of infectious bursal disease virus. J. Virol. 78 (2004) 3296-3303
    • (2004) J. Virol. , vol.78 , pp. 3296-3303
    • Chevalier, C.1    Lepault, J.2    Da Costa, B.3    Delmas, B.4
  • 66
    • 0030042116 scopus 로고    scopus 로고
    • Hepatitis C virus: Detection of intracellular virus particles by electron microscopy
    • Shimizu Y.K., Feinstone S.M., Kohara M., Purcell R.H., and Yoshikura H. Hepatitis C virus: Detection of intracellular virus particles by electron microscopy. Hepatology 23 (1996) 205-209
    • (1996) Hepatology , vol.23 , pp. 205-209
    • Shimizu, Y.K.1    Feinstone, S.M.2    Kohara, M.3    Purcell, R.H.4    Yoshikura, H.5
  • 67
    • 0033133933 scopus 로고    scopus 로고
    • Ultrastructural and immunocytochemical evidences of core-particle formation in the methylotrophic Pichia pastoris yeast when expressing HCV structural proteins (core-E1)
    • Falcon V., Garcia C., de la Rosa M.C., Menandez I., Seoane J., and Grillo J.M. Ultrastructural and immunocytochemical evidences of core-particle formation in the methylotrophic Pichia pastoris yeast when expressing HCV structural proteins (core-E1). Tissue Cell 31 (1999) 117-125
    • (1999) Tissue Cell , vol.31 , pp. 117-125
    • Falcon, V.1    Garcia, C.2    de la Rosa, M.C.3    Menandez, I.4    Seoane, J.5    Grillo, J.M.6
  • 69
    • 0031977996 scopus 로고    scopus 로고
    • Hepatitis C virus structural proteins assemble into virus-like particles in insect cells
    • Baumert T.F., Ito S., Wong D.T., and Liang T.J. Hepatitis C virus structural proteins assemble into virus-like particles in insect cells. J. Virol. 72 (1998) 3827-3836
    • (1998) J. Virol. , vol.72 , pp. 3827-3836
    • Baumert, T.F.1    Ito, S.2    Wong, D.T.3    Liang, T.J.4
  • 71
    • 0035130118 scopus 로고    scopus 로고
    • Self-assembly of nucleocapsid-like particles from recombinant hepatitis C virus core protein
    • Kunkel M., Lornczi M., Rijnbrand R., Lemon S.M., and Watowich S.J. Self-assembly of nucleocapsid-like particles from recombinant hepatitis C virus core protein. J. Virol. 75 (2001) 2119-2129
    • (2001) J. Virol. , vol.75 , pp. 2119-2129
    • Kunkel, M.1    Lornczi, M.2    Rijnbrand, R.3    Lemon, S.M.4    Watowich, S.J.5
  • 72
    • 0036060096 scopus 로고    scopus 로고
    • A molecular switch in the capsid protein controls the particle polymorphism in an icosahedral virus
    • Lokesh G.L., Gowri T.D., Satheshkumar P.S., Murthy M.R., and Savithri H.S. A molecular switch in the capsid protein controls the particle polymorphism in an icosahedral virus. Virology 292 (2002) 211-223
    • (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
  • 75
    • 0037154257 scopus 로고    scopus 로고
    • tRNA elements mediate the assembly of an icosahedral RNA virus
    • Choi Y.G., Dreher T.W., and Rao A.L. tRNA elements mediate the assembly of an icosahedral RNA virus. Proc. Natl. Acad. Sci. USA 99 (2002) 655-660
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 655-660
    • Choi, Y.G.1    Dreher, T.W.2    Rao, A.L.3
  • 76
    • 0027535332 scopus 로고
    • Crystallization of virus-like particles assembled from flock house virus coat protein expressed in a baculovirus
    • Fisher J., McKinney B.R., Schneemann A., Rueckert R.R., and Johnson J.E. Crystallization of virus-like particles assembled from flock house virus coat protein expressed in a baculovirus. J. Virol. 67 (1993) 2950-2953
    • (1993) J. Virol. , vol.67 , pp. 2950-2953
    • Fisher, J.1    McKinney, B.R.2    Schneemann, A.3    Rueckert, R.R.4    Johnson, J.E.5
  • 77
    • 0027516461 scopus 로고
    • Use of recombinant baculoviruses in synthesis of morphologically distinct virus-like particles of flock house virus, a nodavirus
    • Schneemann A., Dasgupta R., Johnson J.E., and Rueckert R.R. Use of recombinant baculoviruses in synthesis of morphologically distinct virus-like particles of flock house virus, a nodavirus. J. Virol. 67 (1993) 2756-2763
    • (1993) J. Virol. , vol.67 , pp. 2756-2763
    • Schneemann, A.1    Dasgupta, R.2    Johnson, J.E.3    Rueckert, R.R.4
  • 78
    • 0031776460 scopus 로고    scopus 로고
    • Particle polymorphism caused by deletion of a peptide molecular switch in a quasiequivalent icosahedral virus
    • Dong X.F., Natarajan P., Tihova M., Johnson J.E., and Schneemann A. Particle polymorphism caused by deletion of a peptide molecular switch in a quasiequivalent icosahedral virus. J. Virol. 72 (1998) 6024-6033
    • (1998) J. Virol. , vol.72 , pp. 6024-6033
    • Dong, X.F.1    Natarajan, P.2    Tihova, M.3    Johnson, J.E.4    Schneemann, A.5
  • 79
    • 0035918974 scopus 로고    scopus 로고
    • Specific packaging of nodaviral RNA2 requires the N-terminus of the capsid protein
    • Marshall D., and Schneemann A. Specific packaging of nodaviral RNA2 requires the N-terminus of the capsid protein. Virology 285 (2001) 165-175
    • (2001) Virology , vol.285 , pp. 165-175
    • Marshall, D.1    Schneemann, A.2
  • 80
    • 0035841620 scopus 로고    scopus 로고
    • Characterization of virus-like particles assembled in a recombinant baculovirus system expressing the capsid protein of a fish nodavirus
    • Lin C.S., Lu M.W., Tang L., Liu W., Chao C.B., Lin C.J., Krishna N.K., Johnson J.E., and Schneemann A. Characterization of virus-like particles assembled in a recombinant baculovirus system expressing the capsid protein of a fish nodavirus. Virology 290 (2001) 50-58
    • (2001) Virology , vol.290 , pp. 50-58
    • Lin, C.S.1    Lu, M.W.2    Tang, L.3    Liu, W.4    Chao, C.B.5    Lin, C.J.6    Krishna, N.K.7    Johnson, J.E.8    Schneemann, A.9
  • 81
    • 0033028591 scopus 로고    scopus 로고
    • In vitro assembly of alphavirus cores by using nucleocapsid protein expressed in Escherichia coli
    • Tellinghuisen T.L., Hamburger A.E., Fisher B.R., Ostendorp R., and Kuhn R.J. In vitro assembly of alphavirus cores by using nucleocapsid protein expressed in Escherichia coli. J. Virol. 73 (1999) 5309-5319
    • (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
  • 82
    • 0033995285 scopus 로고    scopus 로고
    • Nucleic acid-dependent cross-linking of the nucleocapsid protein of Sindbis virus
    • Tellinghuisen T.L., and Kuhn R.J. Nucleic acid-dependent cross-linking of the nucleocapsid protein of Sindbis virus. J. Virol. 74 (2000) 4302-4309
    • (2000) J. Virol. , vol.74 , pp. 4302-4309
    • Tellinghuisen, T.L.1    Kuhn, R.J.2
  • 83
    • 0035128334 scopus 로고    scopus 로고
    • In vitro assembly of Sindbis virus core-like particles from cross-linked dimers of truncated and mutant capsid proteins
    • Tellinghuisen T.L., Perera R., and Kuhn R.J. In vitro assembly of Sindbis virus core-like particles from cross-linked dimers of truncated and mutant capsid proteins. J. Virol. 75 (2001) 2810-2817
    • (2001) J. Virol. , vol.75 , pp. 2810-2817
    • Tellinghuisen, T.L.1    Perera, R.2    Kuhn, R.J.3
  • 84
    • 0035123571 scopus 로고    scopus 로고
    • Characterization of Rous sarcoma virus Gag particles assembled in vitro
    • Yu F., Joshi S.M., Ma Y.M., Kingston R.L., Simon M.N., and Vogt V.M. Characterization of Rous sarcoma virus Gag particles assembled in vitro. J. Virol. 75 (2001) 2753-2764
    • (2001) J. Virol. , vol.75 , pp. 2753-2764
    • Yu, F.1    Joshi, S.M.2    Ma, Y.M.3    Kingston, R.L.4    Simon, M.N.5    Vogt, V.M.6
  • 85
    • 0036827828 scopus 로고    scopus 로고
    • Nucleic acid-independent retrovirus assembly can be driven by dimerization
    • Johnson M.C., Scobie H.M., Ma Y.M., and Vogt V.M. Nucleic acid-independent retrovirus assembly can be driven by dimerization. J. Virol. 76 (2002) 11177-11185
    • (2002) J. Virol. , vol.76 , pp. 11177-11185
    • Johnson, M.C.1    Scobie, H.M.2    Ma, Y.M.3    Vogt, V.M.4
  • 86
    • 0036091735 scopus 로고    scopus 로고
    • Rous sarcoma virus Gag protein-oligonucleotide interaction suggests a critical role for protein dimer formation in assembly
    • Ma Y.M., and Vogt V.M. Rous sarcoma virus Gag protein-oligonucleotide interaction suggests a critical role for protein dimer formation in assembly. J. Virol. 76 (2002) 5452-5462
    • (2002) J. Virol. , vol.76 , pp. 5452-5462
    • Ma, Y.M.1    Vogt, V.M.2
  • 87
    • 0344610289 scopus 로고    scopus 로고
    • Nucleic acid binding-induced Gag dimerization in the assembly of Rous sarcoma virus particles in vitro
    • Ma Y.M., and Vogt V.M. Nucleic acid binding-induced Gag dimerization in the assembly of Rous sarcoma virus particles in vitro. J. Virol. 78 (2004) 52-60
    • (2004) J. Virol. , vol.78 , pp. 52-60
    • Ma, Y.M.1    Vogt, V.M.2
  • 89
    • 0024429254 scopus 로고
    • Assembly and release of HIV-1 precursor Pr55gag virus-like particles from recombinant baculovirus-infected insect cells
    • Gheysen D., Jacobs E., de Foresta F., Thiriart C., Francotte M., Thines D., and De Wilde M. Assembly and release of HIV-1 precursor Pr55gag virus-like particles from recombinant baculovirus-infected insect cells. Cell 59 (1989) 103-112
    • (1989) Cell , vol.59 , pp. 103-112
    • Gheysen, D.1    Jacobs, E.2    de Foresta, F.3    Thiriart, C.4    Francotte, M.5    Thines, D.6    De Wilde, M.7
  • 90
    • 0024392730 scopus 로고
    • Human immunodeficiency virus-like particles produced by a vaccinia virus expression vector
    • Karacostas V., Nagashima K., Gonda M.A., and Moss B. Human immunodeficiency virus-like particles produced by a vaccinia virus expression vector. Proc. Natl. Acad. Sci. USA 86 (1989) 8964-8967
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 8964-8967
    • Karacostas, V.1    Nagashima, K.2    Gonda, M.A.3    Moss, B.4
  • 91
    • 0037062445 scopus 로고    scopus 로고
    • HIV type 1 Gag virus-like particle budding from spheroplasts of Saccharomyces cerevisiae
    • Sakuragi S., Goto T., Sano K., and Morikawa Y. HIV type 1 Gag virus-like particle budding from spheroplasts of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 99 (2002) 7956-7961
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7956-7961
    • Sakuragi, S.1    Goto, T.2    Sano, K.3    Morikawa, Y.4
  • 92
    • 0037320007 scopus 로고    scopus 로고
    • Foamy virus envelope glycoprotein is sufficient for particle budding and release
    • Shaw K.L., Lindemann D., Mulligan M.J., and Goepfert P.A. Foamy virus envelope glycoprotein is sufficient for particle budding and release. J. Virol. 77 (2003) 2338-2348
    • (2003) J. Virol. , vol.77 , pp. 2338-2348
    • Shaw, K.L.1    Lindemann, D.2    Mulligan, M.J.3    Goepfert, P.A.4
  • 93
    • 0028065160 scopus 로고
    • Assembly of rubella virus structural proteins into virus-like particles in transfected cells
    • Hobman T.C., Lundstrom M.L., Mauracher C.A., Woodward L., Gillam S., and Farquhar M.G. Assembly of rubella virus structural proteins into virus-like particles in transfected cells. Virology 202 (1994) 574-585
    • (1994) Virology , vol.202 , pp. 574-585
    • Hobman, T.C.1    Lundstrom, M.L.2    Mauracher, C.A.3    Woodward, L.4    Gillam, S.5    Farquhar, M.G.6
  • 94
    • 0344931714 scopus 로고    scopus 로고
    • Secretion of rubella virions and virus-like particles in cultured epithelial cells
    • Garbutt M., Chan H., and Hobman T.C. Secretion of rubella virions and virus-like particles in cultured epithelial cells. Virology 261 (1999) 340-346
    • (1999) Virology , vol.261 , pp. 340-346
    • Garbutt, M.1    Chan, H.2    Hobman, T.C.3
  • 95
    • 0028226159 scopus 로고
    • Expression and characterization of virus-like particles containing rubella virus structural proteins
    • Qiu Z., Ou D., Hobman T.C., and Gillam S. Expression and characterization of virus-like particles containing rubella virus structural proteins. J. Virol. 68 (1994) 4086-4091
    • (1994) J. Virol. , vol.68 , pp. 4086-4091
    • Qiu, Z.1    Ou, D.2    Hobman, T.C.3    Gillam, S.4
  • 96
    • 0032923868 scopus 로고    scopus 로고
    • Role of rubella virus glycoprotein domains in assembly of virus-like particles
    • Garbutt M., Law L.M., Chan H., and Hobman T.C. Role of rubella virus glycoprotein domains in assembly of virus-like particles. J. Virol. 73 (1999) 3524-3533
    • (1999) J. Virol. , vol.73 , pp. 3524-3533
    • Garbutt, M.1    Law, L.M.2    Chan, H.3    Hobman, T.C.4
  • 97
    • 0029933250 scopus 로고    scopus 로고
    • Nucleocapsid-independent assembly of coronavirus-like particles by coexpression of viral envelope protein genes
    • Vennema H., Godeke G.J., Rossen J.W., Voorhout W.F., Horzinek M.C., Opstelten D.J., and Rottier P.J. Nucleocapsid-independent assembly of coronavirus-like particles by coexpression of viral envelope protein genes. EMBO J. 15 (1996) 2020-2028
    • (1996) EMBO J. , vol.15 , pp. 2020-2028
    • Vennema, H.1    Godeke, G.J.2    Rossen, J.W.3    Voorhout, W.F.4    Horzinek, M.C.5    Opstelten, D.J.6    Rottier, P.J.7
  • 98
    • 0031950008 scopus 로고    scopus 로고
    • Coronavirus particle assembly: Primary structure requirements of the membrane protein
    • de Haan C.A., Kuo L., Masters P.S., Vennema H., and Rottier P.J. Coronavirus particle assembly: Primary structure requirements of the membrane protein. J. Virol. 72 (1998) 6838-6850
    • (1998) J. Virol. , vol.72 , pp. 6838-6850
    • de Haan, C.A.1    Kuo, L.2    Masters, P.S.3    Vennema, H.4    Rottier, P.J.5
  • 99
    • 0034067478 scopus 로고    scopus 로고
    • Assembly of the coronavirus envelope: Homotypic interactions between the M proteins
    • de Haan C.A., Vennema H., and Rottier P.J. Assembly of the coronavirus envelope: Homotypic interactions between the M proteins. J. Virol. 74 (2000) 4967-4978
    • (2000) J. Virol. , vol.74 , pp. 4967-4978
    • de Haan, C.A.1    Vennema, H.2    Rottier, P.J.3
  • 100
    • 0042167579 scopus 로고    scopus 로고
    • The cytoplasmic tails of infectious bronchitis virus E and M proteins mediate their interaction
    • Corse E., and Machamer C.E. The cytoplasmic tails of infectious bronchitis virus E and M proteins mediate their interaction. Virology 312 (2003) 25-34
    • (2003) Virology , vol.312 , pp. 25-34
    • Corse, E.1    Machamer, C.E.2
  • 101
    • 0034468745 scopus 로고    scopus 로고
    • Influenza virus matrix protein is the major driving force in virus budding
    • Gomez-Puertas P., Albo C., Perez-Pastrana E., Vivo A., and Portela A. Influenza virus matrix protein is the major driving force in virus budding. J. Virol. 74 (2000) 11538-11547
    • (2000) J. Virol. , vol.74 , pp. 11538-11547
    • Gomez-Puertas, P.1    Albo, C.2    Perez-Pastrana, E.3    Vivo, A.4    Portela, A.5
  • 102
    • 0032775721 scopus 로고    scopus 로고
    • Human parainfluenza virus type 1 matrix and nucleoprotein genes transiently expressed in mammalian cells induce the release of virus-like particles containing nucleocapsid like structures
    • Coronel C., Murti K.G., Takimoto T., and Portner A. Human parainfluenza virus type 1 matrix and nucleoprotein genes transiently expressed in mammalian cells induce the release of virus-like particles containing nucleocapsid like structures. J. Virol. 73 (1999) 7035-7038
    • (1999) J. Virol. , vol.73 , pp. 7035-7038
    • Coronel, C.1    Murti, K.G.2    Takimoto, T.3    Portner, A.4
  • 104
    • 0035031534 scopus 로고    scopus 로고
    • Ebola virus VP40-induced particle formation and association with the lipid bilayer
    • Jasenosky L.D., Neumann G., Lukashevich I., and Kawaoka Y. Ebola virus VP40-induced particle formation and association with the lipid bilayer. J. Virol. 75 (2001) 5205-5214
    • (2001) J. Virol. , vol.75 , pp. 5205-5214
    • Jasenosky, L.D.1    Neumann, G.2    Lukashevich, I.3    Kawaoka, Y.4
  • 105
    • 0036235725 scopus 로고    scopus 로고
    • Ebola virus VP40 drives the formation of virus-like filamentous particles along with GP
    • Noda T., Sagara H., Suzuki E., Takada A., Kida H., and Kawaoka Y. Ebola virus VP40 drives the formation of virus-like filamentous particles along with GP. J. Virol. 76 (2002) 4855-4865
    • (2002) J. Virol. , vol.76 , pp. 4855-4865
    • Noda, T.1    Sagara, H.2    Suzuki, E.3    Takada, A.4    Kida, H.5    Kawaoka, Y.6
  • 107
    • 0036194519 scopus 로고    scopus 로고
    • Requirements for budding of paramyxovirus simian virus 5 virus-like particles
    • Schmitt A.P., Leser G.P., Waning D.L., and Lamb R.A. Requirements for budding of paramyxovirus simian virus 5 virus-like particles. J. Virol. 76 (2002) 3952-3964
    • (2002) J. Virol. , vol.76 , pp. 3952-3964
    • Schmitt, A.P.1    Leser, G.P.2    Waning, D.L.3    Lamb, R.A.4
  • 108
    • 0022549499 scopus 로고
    • Self-assembly of purified polyomavirus capsid protein VP1
    • Salunke D.M., Caspar D.L., and Garcea R.L. Self-assembly of purified polyomavirus capsid protein VP1. Cell 46 (1986) 895-904
    • (1986) Cell , vol.46 , pp. 895-904
    • Salunke, D.M.1    Caspar, D.L.2    Garcea, R.L.3
  • 109
    • 0025955776 scopus 로고
    • Nuclear assembly of polyomavirus capsids in insect cells expressing the major capsid protein VP1
    • Montross L., Watkins S., Moreland R.B., Mamon H., Caspar D.L., and Garcea R.L. Nuclear assembly of polyomavirus capsids in insect cells expressing the major capsid protein VP1. J. Virol. 65 (1991) 4991-4998
    • (1991) J. Virol. , vol.65 , pp. 4991-4998
    • Montross, L.1    Watkins, S.2    Moreland, R.B.3    Mamon, H.4    Caspar, D.L.5    Garcea, R.L.6
  • 111
    • 0034749345 scopus 로고    scopus 로고
    • Roles of disulfide linkage and calcium ion-mediated interactions in assembly and disassembly of virus-like particles composed of simian virus 40 VP1 capsid protein
    • Ishizu K.I., Watanabe H., Han S.I., Kanesashi S.N., Hoque M., Yajima H., Kataoka K., and Handa H. Roles of disulfide linkage and calcium ion-mediated interactions in assembly and disassembly of virus-like particles composed of simian virus 40 VP1 capsid protein. J. Virol. 75 (2001) 61-72
    • (2001) J. Virol. , vol.75 , pp. 61-72
    • Ishizu, K.I.1    Watanabe, H.2    Han, S.I.3    Kanesashi, S.N.4    Hoque, M.5    Yajima, H.6    Kataoka, K.7    Handa, H.8
  • 112
    • 0035816403 scopus 로고    scopus 로고
    • Disulfide bonds stabilize JC virus capsid-like structure by protecting calcium ions from chelation
    • Chen P.-L., Wang M., Ou W.-C., Lii C.-K., Chen L.-S., and Chang D. Disulfide bonds stabilize JC virus capsid-like structure by protecting calcium ions from chelation. FEBS Lett. 500 (2001) 109-113
    • (2001) FEBS Lett. , vol.500 , pp. 109-113
    • Chen, P.-L.1    Wang, M.2    Ou, W.-C.3    Lii, C.-K.4    Chen, L.-S.5    Chang, D.6
  • 113
    • 4444242208 scopus 로고    scopus 로고
    • T = 1 capsid structures of Sesbania mosaic virus coat protein mutants: Determinants of T = 3 and T = 1 capsid assembly
    • Sangita V., Lokesh G.L., Satheshkumar P.S., Vijay C.S., Saravanan V., Savithri H.S., and Murthy M.R. T = 1 capsid structures of Sesbania mosaic virus coat protein mutants: Determinants of T = 3 and T = 1 capsid assembly. J. Mol. Biol. 342 (2004) 987-999
    • (2004) J. Mol. Biol. , vol.342 , pp. 987-999
    • Sangita, V.1    Lokesh, G.L.2    Satheshkumar, P.S.3    Vijay, C.S.4    Saravanan, V.5    Savithri, H.S.6    Murthy, M.R.7
  • 114
    • 4444284258 scopus 로고    scopus 로고
    • Role of metal ion-mediated interactions in the assembly and stability of Sesbania mosaic virus T = 3 and T = 1 capsids
    • Satheshkumar P.S., Lokesh G.L., Sangita V., Saravanan V., Vijay C.S., Murthy M.R., and Savithri H.S. Role of metal ion-mediated interactions in the assembly and stability of Sesbania mosaic virus T = 3 and T = 1 capsids. J. Mol. Biol. 342 (2004) 1001-1014
    • (2004) J. Mol. Biol. , vol.342 , pp. 1001-1014
    • Satheshkumar, P.S.1    Lokesh, G.L.2    Sangita, V.3    Saravanan, V.4    Vijay, C.S.5    Murthy, M.R.6    Savithri, H.S.7
  • 116
    • 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., and Streeck R.E. Organization of the major and minor capsid proteins in human papillomavirus type 33 virus-like particles. J. Gen. Virol. 76 (1995) 2407-2412
    • (1995) J. Gen. Virol. , vol.76 , pp. 2407-2412
    • Sapp, M.1    Volpers, C.2    Muller, M.3    Streeck, R.E.4
  • 117
    • 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., and Streeck R.E. Papillomavirus assembly requires trimerization of the major capsid protein by disulfides between two highly conserved cysteines. J. Virol. 72 (1998) 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
  • 118
    • 0036057763 scopus 로고    scopus 로고
    • Yeast coexpression of human papillomavirus types 6 and 16 capsid proteins
    • Buonamassa T., Greer C.E., Capo S., Yen T.S., Galeotti C.L., and Bensi G. Yeast coexpression of human papillomavirus types 6 and 16 capsid proteins. Virology 293 (2002) 335-344
    • (2002) Virology , vol.293 , pp. 335-344
    • Buonamassa, T.1    Greer, C.E.2    Capo, S.3    Yen, T.S.4    Galeotti, C.L.5    Bensi, G.6
  • 120
    • 0035155440 scopus 로고    scopus 로고
    • Analysis of the capsid processing strategy of Thosea asigna virus using baculovirus expression of virus-like particles
    • Pringle F.M., Kalmakoff J., and Ward V.K. Analysis of the capsid processing strategy of Thosea asigna virus using baculovirus expression of virus-like particles. J. Gen. Virol. 82 (2001) 259-266
    • (2001) J. Gen. Virol. , vol.82 , pp. 259-266
    • Pringle, F.M.1    Kalmakoff, J.2    Ward, V.K.3
  • 121
    • 0034630854 scopus 로고    scopus 로고
    • Rotavirus VP6 expressed by PVX vectors in Nicotiana benthamiana coats PVX rods and also assembles into virus-like particles
    • O'Brien G.J., Bryant C.J., Voogd C., Greenberg H.B., Gardner R.C., and Bellamy A.R. Rotavirus VP6 expressed by PVX vectors in Nicotiana benthamiana coats PVX rods and also assembles into virus-like particles. Virology 270 (2000) 444-453
    • (2000) Virology , vol.270 , pp. 444-453
    • O'Brien, G.J.1    Bryant, C.J.2    Voogd, C.3    Greenberg, H.B.4    Gardner, R.C.5    Bellamy, A.R.6
  • 122
    • 0036168067 scopus 로고    scopus 로고
    • The maturation process of pVP2 requires assembly of infectious bursal disease virus capsids
    • Chevalier J., Lepault J., Erk I., Da Costa B., and Delmas B. The maturation process of pVP2 requires assembly of infectious bursal disease virus capsids. J. Virol. 76 (2002) 2384-2392
    • (2002) J. Virol. , vol.76 , pp. 2384-2392
    • Chevalier, J.1    Lepault, J.2    Erk, I.3    Da Costa, B.4    Delmas, B.5
  • 123
    • 0035047146 scopus 로고    scopus 로고
    • PR domain of rous sarcoma virus Gag causes an assembly/budding defect in insect cells
    • Johnson M.C., Scobie H.M., and Vogt V.M. PR domain of rous sarcoma virus Gag causes an assembly/budding defect in insect cells. J. Virol. 75 (2000) 4407-4412
    • (2000) J. Virol. , vol.75 , pp. 4407-4412
    • Johnson, M.C.1    Scobie, H.M.2    Vogt, V.M.3
  • 124
    • 0034529206 scopus 로고    scopus 로고
    • Differential budding efficiencies of human T-cell leukemia virus type I (HTLV-I) Gag and Gag-Pro polyproteins from insect and mammalian cells
    • Bouamr F., Garnier L., Rayne F., Verna A., Rebeyrotte N., Cerutti M., and Mamoun R.Z. Differential budding efficiencies of human T-cell leukemia virus type I (HTLV-I) Gag and Gag-Pro polyproteins from insect and mammalian cells. Virology 278 (2000) 597-609
    • (2000) Virology , vol.278 , pp. 597-609
    • Bouamr, F.1    Garnier, L.2    Rayne, F.3    Verna, A.4    Rebeyrotte, N.5    Cerutti, M.6    Mamoun, R.Z.7
  • 125
    • 0345269268 scopus 로고    scopus 로고
    • Control of human immunodeficiency virus type-1 protease activity in insect cells expressing Gag-Pol rescues assembly of immature but not mature virus-like particles
    • Adamson C.S., Nermut M., and Jones I.M. Control of human immunodeficiency virus type-1 protease activity in insect cells expressing Gag-Pol rescues assembly of immature but not mature virus-like particles. Virology 308 (2003) 157-165
    • (2003) Virology , vol.308 , pp. 157-165
    • Adamson, C.S.1    Nermut, M.2    Jones, I.M.3
  • 126
    • 0035658023 scopus 로고    scopus 로고
    • HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress
    • Martin-Serrano J., Zang T., and Bieniasz P.D. HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress. Nat. Med. 7 (2001) 1313-1319
    • (2001) Nat. Med. , vol.7 , pp. 1313-1319
    • Martin-Serrano, J.1    Zang, T.2    Bieniasz, P.D.3
  • 127
    • 2442670346 scopus 로고    scopus 로고
    • Context-dependent effects of L domains and ubiquitination on viral budding
    • Martin-Serrano J., Perez-Caballero D., and Bieniasz P.D. Context-dependent effects of L domains and ubiquitination on viral budding. J. Virol. 78 (2004) 5554-5563
    • (2004) J. Virol. , vol.78 , pp. 5554-5563
    • Martin-Serrano, J.1    Perez-Caballero, D.2    Bieniasz, P.D.3
  • 129
    • 0042825878 scopus 로고    scopus 로고
    • Virus-like particles as immunogens
    • Noad R., and Roy P. Virus-like particles as immunogens. Trends Microbiol. 11 (2003) 438-444
    • (2003) Trends Microbiol. , vol.11 , pp. 438-444
    • Noad, R.1    Roy, P.2
  • 131
    • 0029865114 scopus 로고    scopus 로고
    • A new form of particulate single and multiple immunogen delivery system based on recombinant bluetongue virus-derived tubules
    • Mikhailov M., Monastyrskaya K., Bakker T., and Roy P. A new form of particulate single and multiple immunogen delivery system based on recombinant bluetongue virus-derived tubules. Virology 217 (1996) 323-331
    • (1996) Virology , vol.217 , pp. 323-331
    • Mikhailov, M.1    Monastyrskaya, K.2    Bakker, T.3    Roy, P.4
  • 132
    • 0034099316 scopus 로고    scopus 로고
    • Influence of three-dimensional structure on the immunogenicity of a peptide expressed on the surface of a plant virus
    • Taylor K.M., Lin T., Porta C., Mosser A.G., Giesing H.A., Lomonossoff G.P., and Johnson J.E. Influence of three-dimensional structure on the immunogenicity of a peptide expressed on the surface of a plant virus. J. Mol. Recognit. 13 (2000) 71-82
    • (2000) J. Mol. Recognit. , vol.13 , pp. 71-82
    • Taylor, K.M.1    Lin, T.2    Porta, C.3    Mosser, A.G.4    Giesing, H.A.5    Lomonossoff, G.P.6    Johnson, J.E.7
  • 135
    • 0026531008 scopus 로고
    • Canine parvovirus empty capsids produced by expression in a baculovirus vector: Use in analysis of viral properties and immunization of dogs
    • Saliki J.T., Mizak B., Flore H.P., Gettig R.R., Burand J.P., Carmichael L.E., Wood H.A., and Parrish C.R. Canine parvovirus empty capsids produced by expression in a baculovirus vector: Use in analysis of viral properties and immunization of dogs. J. Gen. Virol. 73 (1992) 369-374
    • (1992) J. Gen. Virol. , vol.73 , pp. 369-374
    • Saliki, J.T.1    Mizak, B.2    Flore, H.P.3    Gettig, R.R.4    Burand, J.P.5    Carmichael, L.E.6    Wood, H.A.7    Parrish, C.R.8
  • 136
    • 0030795494 scopus 로고    scopus 로고
    • Recombinant parvovirus-like particles as an antigen carrier: Novel nonreplicative exogenus antigen to elicit protective antiviral cytotoxic T-cells
    • Sedlik C., Saron M.-F., Sarraseca J., Casal I., and Leclerc C. Recombinant parvovirus-like particles as an antigen carrier: Novel nonreplicative exogenus antigen to elicit protective antiviral cytotoxic T-cells. Proc. Natl. Acad. Sci. USA 94 (1997) 7503-7508
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7503-7508
    • Sedlik, C.1    Saron, M.-F.2    Sarraseca, J.3    Casal, I.4    Leclerc, C.5
  • 137
    • 0029125373 scopus 로고
    • Immunogenicity of poliovirus B and T cell epitopes presented by hybrid porcine parvovirus particles
    • Sedlik C., Sarraseca J., Rueda P., Leclerc C., and Casal I. Immunogenicity of poliovirus B and T cell epitopes presented by hybrid porcine parvovirus particles. J. Gen. Virol. 76 (1995) 2361-2368
    • (1995) J. Gen. Virol. , vol.76 , pp. 2361-2368
    • Sedlik, C.1    Sarraseca, J.2    Rueda, P.3    Leclerc, C.4    Casal, I.5
  • 138
    • 0033543951 scopus 로고    scopus 로고
    • Minor displacements in the insertion site provoke major differences in the induction of antibody responses by chimeric parvovirus-like particles
    • Rueda P., Hurtado A., del Barrio M., Martinez-Torrecuadrada J.L., Kamstrup S., Leclerc C., and Casal J.I. Minor displacements in the insertion site provoke major differences in the induction of antibody responses by chimeric parvovirus-like particles. Virology 263 (1999) 89-99
    • (1999) Virology , vol.263 , pp. 89-99
    • Rueda, P.1    Hurtado, A.2    del Barrio, M.3    Martinez-Torrecuadrada, J.L.4    Kamstrup, S.5    Leclerc, C.6    Casal, J.I.7
  • 139
    • 0029900654 scopus 로고    scopus 로고
    • Identification of domains in canine parvovirus VP2 essential for the assembly of virus-like particles
    • Hurtado A., Rueda P., Nowicky J., Sarraseca J., and Casal J.I. Identification of domains in canine parvovirus VP2 essential for the assembly of virus-like particles. J. Virol. 70 (1996) 5422-5429
    • (1996) J. Virol. , vol.70 , pp. 5422-5429
    • Hurtado, A.1    Rueda, P.2    Nowicky, J.3    Sarraseca, J.4    Casal, J.I.5
  • 141
    • 0141459014 scopus 로고    scopus 로고
    • Mucosal immunization with virus-like particles of Simian immunodeficiency virus conjugated with cholera toxin subunit B
    • Kang S.-M., Yao Q., Guo L., and Compans R.W. Mucosal immunization with virus-like particles of Simian immunodeficiency virus conjugated with cholera toxin subunit B. J. Virol. 77 (2003) 9823-9830
    • (2003) J. Virol. , vol.77 , pp. 9823-9830
    • Kang, S.-M.1    Yao, Q.2    Guo, L.3    Compans, R.W.4
  • 142
    • 0041384562 scopus 로고    scopus 로고
    • Enhancement of mucosal immune response by chimeric influenza HA/SHIV virus-like particles
    • Guo L., Lu X., Kang S.-M., Chen C., Compans R.W., and Yao Q. Enhancement of mucosal immune response by chimeric influenza HA/SHIV virus-like particles. Virology 313 (2003) 502-513
    • (2003) Virology , vol.313 , pp. 502-513
    • Guo, L.1    Lu, X.2    Kang, S.-M.3    Chen, C.4    Compans, R.W.5    Yao, Q.6
  • 144
    • 0343279043 scopus 로고    scopus 로고
    • Packaging of up to 240 subunits of a 17 kDa nuclease into the interior of recombinant hepatitis B virus capsids
    • Beterams G., Bottcher B., and Nassal M. Packaging of up to 240 subunits of a 17 kDa nuclease into the interior of recombinant hepatitis B virus capsids. FEBS Lett. 481 (2000) 169-176
    • (2000) FEBS Lett. , vol.481 , pp. 169-176
    • Beterams, G.1    Bottcher, B.2    Nassal, M.3
  • 145
    • 0033514992 scopus 로고    scopus 로고
    • Native display of complete foreign protein domains on the surface of hepatitis B virus capsids
    • Kratz P.A., Bottcher B., and Nassal M. Native display of complete foreign protein domains on the surface of hepatitis B virus capsids. Proc. Natl. Acad. Sci. USA 96 (1999) 1915-1920
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1915-1920
    • Kratz, P.A.1    Bottcher, B.2    Nassal, M.3
  • 146
    • 0032874490 scopus 로고    scopus 로고
    • A universal influenza A vaccine based on the extracellular domain of the M2 protein
    • Neirynck S., Deroo T., Saelens X., Vanlandschoot P., Jou W.M., and Fiers W. A universal influenza A vaccine based on the extracellular domain of the M2 protein. Nat. Med. 5 (1999) 1157-1163
    • (1999) Nat. Med. , vol.5 , pp. 1157-1163
    • Neirynck, S.1    Deroo, T.2    Saelens, X.3    Vanlandschoot, P.4    Jou, W.M.5    Fiers, W.6
  • 149
    • 0027472081 scopus 로고
    • A single point mutation in the VP7 major core protein of bluetongue virus prevents the formation of core-like particles
    • Le Blois H., and Roy P. A single point mutation in the VP7 major core protein of bluetongue virus prevents the formation of core-like particles. J. Virol. 67 (1993) 353-359
    • (1993) J. Virol. , vol.67 , pp. 353-359
    • Le Blois, H.1    Roy, P.2
  • 150
    • 0026779473 scopus 로고
    • Presentation of hepatitis B virus preS2 epitope on bluetongue core-like particles
    • Belyaev A.S., and Roy P. Presentation of hepatitis B virus preS2 epitope on bluetongue core-like particles. Virology 190 (1992) 840-844
    • (1992) Virology , vol.190 , pp. 840-844
    • Belyaev, A.S.1    Roy, P.2
  • 151
    • 0036436785 scopus 로고    scopus 로고
    • Virus-derived tubular structure displaying foreign sequences on the surface elicit CD4+ Th cell and protective humoral responses
    • Ghosh M.K., Borca M.V., and Roy P. Virus-derived tubular structure displaying foreign sequences on the surface elicit CD4+ Th cell and protective humoral responses. Virology 302 (2002) 383-392
    • (2002) Virology , vol.302 , pp. 383-392
    • Ghosh, M.K.1    Borca, M.V.2    Roy, P.3
  • 153
    • 0034972583 scopus 로고    scopus 로고
    • Formation of wild-type and chimeric influenza virus-like particles following simultaneous expression of only four structural proteins
    • Latham T., and Galarza J.M. Formation of wild-type and chimeric influenza virus-like particles following simultaneous expression of only four structural proteins. J. Virol. 75 (2001) 6154-6165
    • (2001) J. Virol. , vol.75 , pp. 6154-6165
    • Latham, T.1    Galarza, J.M.2
  • 155
    • 0031827785 scopus 로고    scopus 로고
    • Expression of the potyvirus coat protein mediated by recombinant vaccinia virus and assembly of potyvirus-like particles in mammalian cells
    • Hammond J.M., Sproat K.W., Wise T.G., Hyatt A.D., Jagadish M.N., and Coupar B.E. Expression of the potyvirus coat protein mediated by recombinant vaccinia virus and assembly of potyvirus-like particles in mammalian cells. Arch. Virol. 143 (1998) 1433-1439
    • (1998) Arch. Virol. , vol.143 , pp. 1433-1439
    • Hammond, J.M.1    Sproat, K.W.2    Wise, T.G.3    Hyatt, A.D.4    Jagadish, M.N.5    Coupar, B.E.6
  • 156
    • 0035800739 scopus 로고    scopus 로고
    • Individual rotavirus-like particles containing 120 molecules of fluorescent protein are visible in living cells
    • Charpilienne A., Nejmeddine M., Berois M., Parez N., Neumann E., Hewat E., Trugnan G., and Cohen J. Individual rotavirus-like particles containing 120 molecules of fluorescent protein are visible in living cells. J. Biol. Chem. 276 (2001) 29361-29367
    • (2001) J. Biol. Chem. , vol.276 , pp. 29361-29367
    • Charpilienne, A.1    Nejmeddine, M.2    Berois, M.3    Parez, N.4    Neumann, E.5    Hewat, E.6    Trugnan, G.7    Cohen, J.8
  • 157
    • 0033431848 scopus 로고    scopus 로고
    • Changing the surface of a virus shell fusion of an enzyme to polyoma VP1
    • Gleiter S., Stubenrauch K., and Lilie H. Changing the surface of a virus shell fusion of an enzyme to polyoma VP1. Protein Sci. 8 (1999) 2562-2569
    • (1999) Protein Sci. , vol.8 , pp. 2562-2569
    • Gleiter, S.1    Stubenrauch, K.2    Lilie, H.3
  • 158
    • 0035875141 scopus 로고    scopus 로고
    • Conjugation of an antibody Fv fragment to a virus coat protein: Cell-specific targeting of recombinant polyoma-virus-like particles
    • Stubenrauch K., Gleiter S., Brinkmann U., Rudolph R., and Lilie H. Conjugation of an antibody Fv fragment to a virus coat protein: Cell-specific targeting of recombinant polyoma-virus-like particles. Biochem. J. 356 (2001) 867-873
    • (2001) Biochem. J. , vol.356 , pp. 867-873
    • Stubenrauch, K.1    Gleiter, S.2    Brinkmann, U.3    Rudolph, R.4    Lilie, H.5
  • 159
    • 0035993314 scopus 로고    scopus 로고
    • Assessment of cell type specific gene transfer of polyoma virus-like particles presenting a tumor-specific antibody Fv fragment
    • May T., Gleiter S., and Lilie H. Assessment of cell type specific gene transfer of polyoma virus-like particles presenting a tumor-specific antibody Fv fragment. J. Virol. Methods 105 (2002) 147-157
    • (2002) J. Virol. Methods , vol.105 , pp. 147-157
    • May, T.1    Gleiter, S.2    Lilie, H.3
  • 160
    • 0037298835 scopus 로고    scopus 로고
    • Cell-type specific targeting and gene expression using a variant of polyoma VP1 virus-like particles
    • Gleiter S., and Lilie H. Cell-type specific targeting and gene expression using a variant of polyoma VP1 virus-like particles. Biol. Chem. 384 (2003) 247-255
    • (2003) Biol. Chem. , vol.384 , pp. 247-255
    • Gleiter, S.1    Lilie, H.2
  • 162
    • 0034036079 scopus 로고    scopus 로고
    • Structures of virus and virus-like particles
    • Johnson J.E., and Chiu W. Structures of virus and virus-like particles. Curr. Opin. Struct. Biol. 10 (2000) 229-235
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 229-235
    • Johnson, J.E.1    Chiu, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.