메뉴 건너뛰기




Volumn 56, Issue 7-8, 1999, Pages 580-603

Scaffolding proteins and their role in viral assembly

Author keywords

Assembly; Bacteriophage; Capsid; Chaperones; Morphogenesis; Virus

Indexed keywords

CHAPERONE; PHOSMET; STRUCTURAL PROTEIN; VIRUS PROTEIN;

EID: 0032712201     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s000180050455     Document Type: Review
Times cited : (119)

References (199)
  • 1
    • 0032489015 scopus 로고    scopus 로고
    • The cell as a collection of protein machines: Preparing the next generation of molecular biologists
    • 1 Alberts B. (1998) The cell as a collection of protein machines: preparing the next generation of molecular biologists. Cell 92: 291-294
    • (1998) Cell , vol.92 , pp. 291-294
    • Alberts, B.1
  • 2
    • 0013889480 scopus 로고
    • Morphogenesis of bacteriophage T4 in extracts of mutant-infected cells
    • 2 Edgar R. S. and Wood W. B. (1966) Morphogenesis of bacteriophage T4 in extracts of mutant-infected cells, Proc. Natl. Acad. Sci. USA 55: 498-505
    • (1966) Proc. Natl. Acad. Sci. USA , vol.55 , pp. 498-505
    • Edgar, R.S.1    Wood, W.B.2
  • 4
    • 0001446319 scopus 로고
    • Reconstitution of active tobacco mosaic virus from its inactive protein and nucleic acid components
    • 4 Fraenkel-Conrat H. and Williams R. C. (1955) Reconstitution of active tobacco mosaic virus from its inactive protein and nucleic acid components. Proc. Natl. Acad. Sci. USA 41: 690-698
    • (1955) Proc. Natl. Acad. Sci. USA , vol.41 , pp. 690-698
    • Fraenkel-Conrat, H.1    Williams, R.C.2
  • 5
    • 0000334168 scopus 로고
    • Regulation of structural protein interactions as revealed in phage morphogenesis
    • Goldberger R. F. (ed.), Plenum Press, New York
    • 5 King J. (1980) Regulation of structural protein interactions as revealed in phage morphogenesis. In: Biological Regulation and Development, pp. 101-132, Goldberger R. F. (ed.), Plenum Press, New York
    • (1980) Biological Regulation and Development , pp. 101-132
    • King, J.1
  • 6
    • 0017319012 scopus 로고
    • DNA viruses. Cooperativity and regulation through conformational changes of phage assembly
    • 6 Kellenberger E. (1976) DNA viruses. Cooperativity and regulation through conformational changes of phage assembly. Phil. Trans. Roy. Soc. London B 276: 3-13
    • (1976) Phil. Trans. Roy. Soc. London B , vol.276 , pp. 3-13
    • Kellenberger, E.1
  • 7
    • 0025297775 scopus 로고
    • Form determination of the heads of bacteriophages
    • 7 Kellenberger E. (1990) Form determination of the heads of bacteriophages. Eur. J. Biochem. 190: 233-248
    • (1990) Eur. J. Biochem. , vol.190 , pp. 233-248
    • Kellenberger, E.1
  • 8
    • 0027638730 scopus 로고
    • Conformational change an alternative energy source? exothermic phase transition in phage capsid maturation
    • 8 Steven A. C. (1993) Conformational change an alternative energy source? Exothermic phase transition in phage capsid maturation. Biophys J 65: 5-6
    • (1993) Biophys J , vol.65 , pp. 5-6
    • Steven, A.C.1
  • 9
    • 0015897898 scopus 로고
    • Mechanism of head assembly and DNA encapsulation in Salmonella phage P22. 11
    • 9 King J., Lenk E. V. and Botstein D. (1973) Mechanism of head assembly and DNA encapsulation in Salmonella phage P22. 11. Morphogenetic pathway. J. Mol. Biol. 80: 697-731
    • (1973) Morphogenetic Pathway. J. Mol. Biol. , vol.80 , pp. 697-731
    • King, J.1    Lenk, E.V.2    Botstein, D.3
  • 10
    • 0015808773 scopus 로고
    • Assembly core of bacteriophage T4: An intermediate in head formation
    • 10 Showe M. K. and Black L. W. (1973) Assembly core of bacteriophage T4: an intermediate in head formation. Nature New Biol. 242: 70-75
    • (1973) Nature New Biol. , vol.242 , pp. 70-75
    • Showe, M.K.1    Black, L.W.2
  • 11
    • 0019118785 scopus 로고
    • Scaffolding proteins and the genetic control of virus shell assembly
    • 11 King J., Griffin-Shea R. and Fuller M. T. (1980) Scaffolding proteins and the genetic control of virus shell assembly. Quart. Rev. Biol. 55: 369-393
    • (1980) Quart. Rev. Biol. , vol.55 , pp. 369-393
    • King, J.1    Griffin-Shea, R.2    Fuller, M.T.3
  • 12
    • 0002107186 scopus 로고
    • Control mechanisms in dsDNA bacteriophage assembly
    • Calendar R. (ed.), Plenum Press, New York
    • 12 Casjens S. and Hendrix R. (1988) Control mechanisms in dsDNA bacteriophage assembly. In: The Bacteriophages, pp. 15-91, Calendar R. (ed.), Plenum Press, New York
    • (1988) The Bacteriophages , pp. 15-91
    • Casjens, S.1    Hendrix, R.2
  • 15
    • 0018133425 scopus 로고
    • Head morphogenesis of complex double-stranded deoxyribonucleic acid bacteriophages
    • 15 Murialdo H. and Becker A. (1978) Head morphogenesis of complex double-stranded deoxyribonucleic acid bacteriophages. Microbiol. Rev. 42: 529-576
    • (1978) Microbiol. Rev. , vol.42 , pp. 529-576
    • Murialdo, H.1    Becker, A.2
  • 16
    • 0002917513 scopus 로고    scopus 로고
    • Principles of virion structure, function and assembly
    • Chiu W. (ed.), Oxford University Press, New York
    • 16 Casjens S. (1997) Principles of virion structure, function and assembly. In: Structural Biology of Viruses, pp. 3-37, Chiu W. (ed.), Oxford University Press, New York
    • (1997) Structural Biology of Viruses , pp. 3-37
    • Casjens, S.1
  • 17
    • 0002381715 scopus 로고
    • An introduction to virus structure and assembly
    • Casjens S. (ed.), Jones and Bartlett, Boston
    • 17 Casjens S. (1985) An introduction to virus structure and assembly. In: Virus Structure and Assembly, pp. 2-28, Casjens S. (ed.), Jones and Bartlett, Boston
    • (1985) Virus Structure and Assembly , pp. 2-28
    • Casjens, S.1
  • 20
    • 0032967636 scopus 로고    scopus 로고
    • The role of scaffolding proteins in the assembly of the small, single-stranded DNA virus φX174
    • 20 Dokland T., Bernal R. A., Durch A., Pletnev S., Fane B. A. and Rossmann M. G. (1999) The Role of scaffolding proteins in the assembly of the small, single-stranded DNA virus φX174. J. Mol. Biol. 288: 595-608
    • (1999) J. Mol. Biol. , vol.288 , pp. 595-608
    • Dokland, T.1    Bernal, R.A.2    Durch, A.3    Pletnev, S.4    Fane, B.A.5    Rossmann, M.G.6
  • 22
    • 1842317809 scopus 로고
    • Morphogenesis of the isometric phages
    • Denhardt D. T., Dressler D. and Ray D. S. (eds), Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
    • 22 Hayashi M. (1978) Morphogenesis of the isometric phages. In: The Single-Stranded DNA phages, pp. 531-547, Denhardt D. T., Dressler D. and Ray D. S. (eds), Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
    • (1978) The Single-stranded DNA Phages , pp. 531-547
    • Hayashi, M.1
  • 23
    • 0002410957 scopus 로고
    • Biology of the bacteriophage φX174
    • Calendar R. (ed.), Plenum Press, New York
    • 23 Hayashi M., Aoyoma A., Richardson D. Jr and Hayashi M. (1988) Biology of the bacteriophage φX174. In: The Bacteriophages, pp. 1-71, Calendar R. (ed.), Plenum Press, New York
    • (1988) The Bacteriophages , pp. 1-71
    • Hayashi, M.1    Aoyoma, A.2    Richardson D., Jr.3    Hayashi, M.4
  • 24
    • 0017346359 scopus 로고
    • Functions of gene C and gene D products of bacteriophage φX174
    • 24 Fujisawa H. and Hayashi M. (1977) Functions of gene C and gene D products of bacteriophage φX174. Virology 21: 506-515
    • (1977) Virology , vol.21 , pp. 506-515
    • Fujisawa, H.1    Hayashi, M.2
  • 25
    • 0017687352 scopus 로고
    • Two infectious forms of bacteriophage φX174
    • 25 Fujisawa H. and Hayashi M. (1977) Two infectious forms of bacteriophage φX174. J. Virol. 23: 439-442
    • (1977) J. Virol. , vol.23 , pp. 439-442
    • Fujisawa, H.1    Hayashi, M.2
  • 26
    • 0014944712 scopus 로고
    • Intermediates in the assembly of φX174
    • 26 Tonegawa S. and Hayashi M. (1970) Intermediates in the assembly of φX174. J. Mol. Biol. 48: 219-242
    • (1970) J. Mol. Biol. , vol.48 , pp. 219-242
    • Tonegawa, S.1    Hayashi, M.2
  • 27
    • 0016140571 scopus 로고
    • Role of the gene B product in bacteriophage φX174 development
    • 27 Siden E. J. and Hayashi M. (1974) Role of the gene B product in bacteriophage φX174 development. J. Mol. Biol. 89: 1-16
    • (1974) J. Mol. Biol. , vol.89 , pp. 1-16
    • Siden, E.J.1    Hayashi, M.2
  • 28
    • 0016281572 scopus 로고
    • A DNA-protein complex involved in bacteriophage φX174 particle formation
    • 28 Weisbeck P. J. and Sinsheimer R. L. (1974) A DNA-protein complex involved in bacteriophage φX174 particle formation. Proc. Natl. Acad. Sci. USA 71: 3054-3058
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 3054-3058
    • Weisbeck, P.J.1    Sinsheimer, R.L.2
  • 29
    • 0017238642 scopus 로고
    • Purification and properties of bacteriophage φX174 gene D product
    • 29 Farber M. B. (1976) Purification and properties of bacteriophage φX174 gene D product. J. Virol. 17: 1027-1037
    • (1976) J. Virol. , vol.17 , pp. 1027-1037
    • Farber, M.B.1
  • 30
    • 73649156890 scopus 로고
    • Physical principles in the construction of regular viruses
    • 30 Caspar D. L. D. and Klug A. (1962) Physical principles in the construction of regular viruses. Cold Spring Harb. Symp. Quant. Biol. 27: 1-24
    • (1962) Cold Spring Harb. Symp. Quant. Biol. , vol.27 , pp. 1-24
    • Caspar, D.L.D.1    Klug, A.2
  • 32
    • 0025663313 scopus 로고
    • Interactions between satellite bacteriophage P4 and its helpers
    • 32 Christie G. E. and Calendar R. (1990) Interactions between satellite bacteriophage P4 and its helpers. Annu. Rev. Genet. 24: 465-490
    • (1990) Annu. Rev. Genet. , vol.24 , pp. 465-490
    • Christie, G.E.1    Calendar, R.2
  • 33
    • 0002567358 scopus 로고
    • The P2-like phages and their parasite, P4
    • Calendar R. (ed.), Plenum Press, New York
    • 33 Bertani L. E. and Six E. (1988) The P2-like phages and their parasite, P4. In: The Bacteriophages, pp. 73 -143, Calendar R. (ed.), Plenum Press, New York
    • (1988) The Bacteriophages , pp. 73-143
    • Bertani, L.E.1    Six, E.2
  • 34
    • 0027208795 scopus 로고
    • Mechanisms of genome propagation and helper exploitation by satellite pliage P4
    • 34 Lindqvist B. H., Deho G. and Calendar R. (1993) Mechanisms of genome propagation and helper exploitation by satellite pliage P4. Microbiol. Rev. 57: 683-702
    • (1993) Microbiol. Rev. , vol.57 , pp. 683-702
    • Lindqvist, B.H.1    Deho, G.2    Calendar, R.3
  • 35
    • 0026579790 scopus 로고
    • Image reconstruction from cryo-electron micrographs reveals the morphopoietic mechanism in the P2-P4 bacteriophage system
    • 35 Dokland T. E., Lindqvist B. H. and Fuller S. D. (1992) Image reconstruction from cryo-electron micrographs reveals the morphopoietic mechanism in the P2-P4 bacteriophage system. EMBO J. 11: 839-846
    • (1992) EMBO J. , vol.11 , pp. 839-846
    • Dokland, T.E.1    Lindqvist, B.H.2    Fuller, S.D.3
  • 36
    • 0017139928 scopus 로고
    • Interactions between a satellite bacteriophage and its helper
    • 36 Barrett K. J., Marsh M. L. and Calendar R. (1976) Interactions between a satellite bacteriophage and its helper. J. Mol. Biol. 106: 683-707
    • (1976) J. Mol. Biol. , vol.106 , pp. 683-707
    • Barrett, K.J.1    Marsh, M.L.2    Calendar, R.3
  • 39
    • 0028331137 scopus 로고
    • Bacteriophage P2 and P4 assembly: Alternative scaffolding proteins regulate capsid size
    • 39 Marvik O. J., Sharma P., Dokland T. and Lindqvist B. H. (1994) Bacteriophage P2 and P4 assembly: alternative scaffolding proteins regulate capsid size. Virology 200: 702-714
    • (1994) Virology , vol.200 , pp. 702-714
    • Marvik, O.J.1    Sharma, P.2    Dokland, T.3    Lindqvist, B.H.4
  • 40
    • 0030012503 scopus 로고    scopus 로고
    • Mutational analysis of the bacteriophage P4 capsid-size-determining gene
    • 40 Nilssen Ø., Six E. W., Sunshine M. G. and Lindqvist B. H. (1996) Mutational analysis of the bacteriophage P4 capsid-size-determining gene. Virology 219: 432-442
    • (1996) Virology , vol.219 , pp. 432-442
    • Six, E.W.1    Sunshine, M.G.2    Lindqvist, B.H.3
  • 41
    • 0015841378 scopus 로고
    • Mechanism of head assembly and DNA encapsulation in Salmonella phage P22. I. Genes, proteins, structures and DNA maturation
    • 41 Botstein D., Waddell C. H. and King J. (1973) Mechanism of head assembly and DNA encapsulation in Salmonella phage P22. I. Genes, proteins, structures and DNA maturation. J. Mol. Biol. 80: 669-695
    • (1973) J. Mol. Biol. , vol.80 , pp. 669-695
    • Botstein, D.1    Waddell, C.H.2    King, J.3
  • 42
    • 0016312775 scopus 로고
    • Catalytic head assembling protein in virus morphogenesis
    • 42 King J. and Casjens S. (1974) Catalytic head assembling protein in virus morphogenesis. Nature 251: 112-119
    • (1974) Nature , vol.251 , pp. 112-119
    • King, J.1    Casjens, S.2
  • 44
    • 0023696277 scopus 로고
    • Scaffolding protein regulates the polymerization of P22 subunits into icosahedral shells in vitro
    • 44 Prevelige P., Thomas D. and King J. (1988) Scaffolding protein regulates the polymerization of P22 subunits into icosahedral shells in vitro. J. Mol. Biol. 202: 743-757
    • (1988) J. Mol. Biol. , vol.202 , pp. 743-757
    • Prevelige, P.1    Thomas, D.2    King, J.3
  • 45
    • 0027232759 scopus 로고
    • Nucleation and growth phases in the polymerization of coat and scaffolding subunits into icosahedral procapsid shells
    • 45 Prevelige P., Thomas D. and King J. (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, P.1    Thomas, D.2    King, J.3
  • 46
    • 0019075771 scopus 로고
    • Regulation of coat protein polymerization by the scaffolding protein of bacteriophage P22
    • 46 Fuller M. T. and King J. (1980) Regulation of coat protein polymerization by the scaffolding protein of bacteriophage P22. Biophys J. 32: 381-401
    • (1980) Biophys J. , vol.32 , pp. 381-401
    • Fuller, M.T.1    King, J.2
  • 47
    • 0018232414 scopus 로고
    • Structure of phage P22 coat protein aggregates formed in the absence of the scaffolding protein
    • 47 Earnshaw W. and King J. (1978) Structure of phage P22 coat protein aggregates formed in the absence of the scaffolding protein. J. Mol. Biol. 126: 721-747
    • (1978) J. Mol. Biol. , vol.126 , pp. 721-747
    • Earnshaw, W.1    King, J.2
  • 48
    • 0017118828 scopus 로고
    • Assembly of the head of bacteriophage P22: X-ray diffraction from heads, proheads and related structures
    • 48 Earnshaw W. C., Casjens S. and Harrison S. C. (1976) Assembly of the head of bacteriophage P22: X-ray diffraction from heads, proheads and related structures. J. Mol. Biol. 104: 387-410
    • (1976) J. Mol. Biol. , vol.104 , pp. 387-410
    • Earnshaw, W.C.1    Casjens, S.2    Harrison, S.C.3
  • 49
    • 0030570434 scopus 로고    scopus 로고
    • Three-dimensional structure of scaffolding-containing phage P22 procapsids by electron cryo-microscopy
    • 49 Thuman-Commike P. A., Greene B., Jakana J., Prasad B. V. V., King J., Prevelige P. E. et al. (1996) Three-dimensional structure of scaffolding-containing phage P22 procapsids by electron cryo-microscopy. J. Mol. Biol. 260: 85-98
    • (1996) J. Mol. Biol. , vol.260 , pp. 85-98
    • Thuman-Commike, P.A.1    Greene, B.2    Jakana, J.3    Prasad, B.V.V.4    King, J.5    Prevelige, P.E.6
  • 50
    • 18744429919 scopus 로고    scopus 로고
    • Bacteriophage P22 scaffolding protein forms oligomers in solution
    • 50 Parker M. H., Stafford W. F. and Prevelige P. E. (1997) Bacteriophage P22 scaffolding protein forms oligomers in solution. J. Mol. Biol. 268: 655-665
    • (1997) J. Mol. Biol. , vol.268 , pp. 655-665
    • Parker, M.H.1    Stafford, W.F.2    Prevelige, P.E.3
  • 51
    • 0032566932 scopus 로고    scopus 로고
    • Electrostatic interactions drive scaffolding/coat protein binding and procapsid maturation in bacteriophage P22
    • 51 Parker M. H. and Prevelige P. E. (1998) Electrostatic interactions drive scaffolding/coat protein binding and procapsid maturation in bacteriophage P22. Virology 250: 337-349
    • (1998) Virology , vol.250 , pp. 337-349
    • Parker, M.H.1    Prevelige, P.E.2
  • 52
    • 0030752503 scopus 로고    scopus 로고
    • Cloning, purification and preliminary characterization by circular dichroism and NMR of a carboxyl-terminal domain of the bacteriophage P22 scaffolding protein
    • 52 Parker M. H., Jablonsky M., Casjens S., Sampson L., Krishna N. R. and Prevelige P. E. (1997) Cloning, purification and preliminary characterization by circular dichroism and NMR of a carboxyl-terminal domain of the bacteriophage P22 scaffolding protein. Protein Science 6: 1583-1586
    • (1997) Protein Science , vol.6 , pp. 1583-1586
    • Parker, M.H.1    Jablonsky, M.2    Casjens, S.3    Sampson, L.4    Krishna, N.R.5    Prevelige, P.E.6
  • 53
    • 0032493783 scopus 로고    scopus 로고
    • Functional domains of bacteriophage P22 scaffolding protein
    • 53 Parker M. H., Casjens S. and Prevelige P. E. (1998) Functional domains of bacteriophage P22 scaffolding protein. J. Mol. Biol. 281: 69-79
    • (1998) J. Mol. Biol. , vol.281 , pp. 69-79
    • Parker, M.H.1    Casjens, S.2    Prevelige, P.E.3
  • 54
    • 0032493694 scopus 로고    scopus 로고
    • A helical coat protein recognition domain of the bacteriophage P22 scaffolding protein
    • 54 Tuma R., Parker M. H., Weigele P., Sampson L., Sun Y., Krishna N. R. et al. (1998) A helical coat protein recognition domain of the bacteriophage P22 scaffolding protein. J. Mol. Biol. 281: 81-94
    • (1998) J. Mol. Biol. , vol.281 , pp. 81-94
    • Tuma, R.1    Parker, M.H.2    Weigele, P.3    Sampson, L.4    Sun, Y.5    Krishna, N.R.6
  • 55
    • 0020483095 scopus 로고
    • Assembly in vitro of bacteriophage P22 procapsids from purified coat and scaffolding subunits
    • 55 Fuller M. T. and King J. (1982) Assembly in vitro of bacteriophage P22 procapsids from purified coat and scaffolding subunits. J. Mol. Biol. 156: 633-665
    • (1982) J. Mol. Biol. , vol.156 , pp. 633-665
    • Fuller, M.T.1    King, J.2
  • 56
    • 0019458559 scopus 로고
    • Purification of the coat and scaffolding proteins from procapsids of bacteriophage P22
    • 56 Fuller M. T. and King J. (1981) Purification of the coat and scaffolding proteins from procapsids of bacteriophage P22. Virology 112: 529-547
    • (1981) Virology , vol.112 , pp. 529-547
    • Fuller, M.T.1    King, J.2
  • 57
    • 0029864052 scopus 로고    scopus 로고
    • Structural transitions in the scaffolding and coat proteins of P22 virus during assembly and disassembly
    • 57 Tuma R., Prevelige P. E. and Thomas G. J. (1996) Structural transitions in the scaffolding and coat proteins of P22 virus during assembly and disassembly. Biochemistry 35: 4619-4627
    • (1996) Biochemistry , vol.35 , pp. 4619-4627
    • Tuma, R.1    Prevelige, P.E.2    Thomas, G.J.3
  • 58
    • 0025358014 scopus 로고
    • Conformational states of the bacteriophage p22 capsid subunit in relation to self-assembly
    • 58 Prevelige P. E., Thomas D., King J., Towse S. A. and Thomas G. J. (1990) Conformational states of the bacteriophage P22 capsid subunit in relation to self-assembly. Biochemistry 29: 5626-5633
    • (1990) Biochemistry , vol.29 , pp. 5626-5633
    • Prevelige, P.E.1    Thomas, D.2    King, J.3    Towse, S.A.4    Thomas, G.J.5
  • 59
    • 0027447982 scopus 로고
    • Subunit conformational changes accompanying bacteriophage P22 capsid maturation
    • 59 Prevelige P., Thomas D., Aubrey K. L., Towse S. A. and Thomas G. J. (1993) Subunit conformational changes accompanying bacteriophage P22 capsid maturation. Biochemistry 32: 537-543
    • (1993) Biochemistry , vol.32 , pp. 537-543
    • Prevelige, P.1    Thomas, D.2    Aubrey, K.L.3    Towse, S.A.4    Thomas, G.J.5
  • 60
    • 0031982564 scopus 로고    scopus 로고
    • Role of the scaffolding protein in P22 procapsid size determination suggested by T=4 and T=7 procapsid structures
    • 60 Thuman-Commike P. A., Greene B., Malinski J. A., King J. and Chiu W. (1998) Role of the scaffolding protein in P22 procapsid size determination suggested by T=4 and T=7 procapsid structures. Biophys. J. 74: 559-568
    • (1998) Biophys. J. , vol.74 , pp. 559-568
    • Thuman-Commike, P.A.1    Greene, B.2    Malinski, J.A.3    King, J.4    Chiu, W.5
  • 61
    • 0028130527 scopus 로고
    • Binding of scaffolding subunits within the P22 procapsid lattice
    • 61 Greene B. and King J. (1994) Binding of scaffolding subunits within the P22 procapsid lattice. Virology 205: 188-197
    • (1994) Virology , vol.205 , pp. 188-197
    • Greene, B.1    King, J.2
  • 62
    • 0023682381 scopus 로고
    • Initiation of P22 procapsid assembly in vivo
    • 62 Bazinet C. and King J. (1988) Initiation of P22 procapsid assembly in vivo. J. Mol. Biol. 202: 77-86
    • (1988) J. Mol. Biol. , vol.202 , pp. 77-86
    • Bazinet, C.1    King, J.2
  • 63
    • 0016290968 scopus 로고
    • Locations and amounts of the major structural proteins of bacteriophage lambda
    • 63 Casjens S. and Hendrix R. W. (1974) Locations and amounts of the major structural proteins of bacteriophage lambda. J. Mol. Biol. 88: 535-545
    • (1974) J. Mol. Biol. , vol.88 , pp. 535-545
    • Casjens, S.1    Hendrix, R.W.2
  • 64
    • 0027366430 scopus 로고
    • Structural transitions during maturation of bacteriophage lambda capsids
    • 64 Dokland T. and Murialdo H. (1993) Structural transitions during maturation of bacteriophage lambda capsids. J. Mol. Biol. 233: 682-694
    • (1993) J. Mol. Biol. , vol.233 , pp. 682-694
    • Dokland, T.1    Murialdo, H.2
  • 65
    • 0021033446 scopus 로고
    • Early intermediates in bacteriophage lambda prohead assembly. II. Identification of biologically active intermediates
    • 65 Kochan J. and Murialdo H. (1983) Early intermediates in bacteriophage lambda prohead assembly. II. Identification of biologically active intermediates. Virology 131: 100-115
    • (1983) Virology , vol.131 , pp. 100-115
    • Kochan, J.1    Murialdo, H.2
  • 66
    • 0016608755 scopus 로고
    • The role of gene Nu3 in bacteriophage lambda head morphogenesis
    • 66 Ray P. and Murialdo H. (1975) The role of gene Nu3 in bacteriophage lambda head morphogenesis. Virology 64: 247-263
    • (1975) Virology , vol.64 , pp. 247-263
    • Ray, P.1    Murialdo, H.2
  • 67
    • 0016770390 scopus 로고
    • Petit λ a family of particles from coliphage lambda infected cells
    • 67 Hohn T., Flick H. and Hohn B. (1975) Petit λ a family of particles from coliphage lambda infected cells. J. Mol. Biol. 98: 107-120
    • (1975) J. Mol. Biol. , vol.98 , pp. 107-120
    • Hohn, T.1    Flick, H.2    Hohn, B.3
  • 68
    • 0018748111 scopus 로고
    • Early intermediates in bacteriophage lambda prohead assembly
    • 68 Murialdo H. (1979) Early intermediates in bacteriophage lambda prohead assembly. Virology 96: 341-367
    • (1979) Virology , vol.96 , pp. 341-367
    • Murialdo, H.1
  • 69
    • 0018727424 scopus 로고
    • Structural studies of bacteriophage lambda heads and proheads by small angle X-ray diffraction
    • 69 Earnshaw W. C., Hendrix R. W. and King J. (1979) Structural studies of bacteriophage lambda heads and proheads by small angle X-ray diffraction. J. Mol. Biol. 134: 575-594
    • (1979) J. Mol. Biol. , vol.134 , pp. 575-594
    • Earnshaw, W.C.1    Hendrix, R.W.2    King, J.3
  • 70
    • 0017576679 scopus 로고
    • Assembly of biologically active proheads of bacteriophage lambda in vitro
    • 70 Murialdo H. and Becker A. (1977) Assembly of biologically active proheads of bacteriophage lambda in vitro. Proc. Natl. Acad. Sci. USA 74: 906-910
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 906-910
    • Murialdo, H.1    Becker, A.2
  • 72
    • 0021088696 scopus 로고
    • Structure and inherent properties of the bacteriophage lambda head shell. IV. Small-head mutants
    • 72 Katsura I. (1983) Structure and inherent properties of the bacteriophage lambda head shell. IV. Small-head mutants. J. Mol. Biol. 171: 297-317
    • (1983) J. Mol. Biol. , vol.171 , pp. 297-317
    • Katsura, I.1
  • 73
    • 0002120296 scopus 로고
    • The structure of bacteriophage T7
    • Viral Structure, Harris J. R. and Horne R. W. (eds), Academic Press, London
    • 73 Steven A. C. and Trus B. (1986) The structure of bacteriophage T7. In: Electron Microscopy of Proteins, vol. 5: Viral Structure, pp. 1-35, Harris J. R. and Horne R. W. (eds), Academic Press, London
    • (1986) Electron Microscopy of Proteins , vol.5 , pp. 1-35
    • Steven, A.C.1    Trus, B.2
  • 74
    • 0017102281 scopus 로고
    • Internal proteins of bacteriophage T7
    • 74 Serwer P. (1976) Internal proteins of bacteriophage T7. J. Mol. Biol. 107: 271-291
    • (1976) J. Mol. Biol. , vol.107 , pp. 271-291
    • Serwer, P.1
  • 75
    • 0020052944 scopus 로고
    • Function of an internal bacteriophage T7 core during assembly of a T7 procapsid
    • 75 Serwer P. and Watson R. H. (1982) Function of an internal bacteriophage T7 core during assembly of a T7 procapsid. J. Virol. 42: 595-601
    • (1982) J. Virol. , vol.42 , pp. 595-601
    • Serwer, P.1    Watson, R.H.2
  • 76
    • 0018561189 scopus 로고
    • Fibrous projections from the core of a bacteriophage T7 procapsid
    • 76 Serwer P. (1979) Fibrous projections from the core of a bacteriophage T7 procapsid. J. Supramol. Struct. 11: 321-326
    • (1979) J. Supramol. Struct. , vol.11 , pp. 321-326
    • Serwer, P.1
  • 77
    • 0029998659 scopus 로고    scopus 로고
    • Assembly of T7 capsids from independently expressed and purified head protein and scaffolding protein
    • 77 Cerritelli M. E. and Studier F. W. (1996) Assembly of T7 capsids from independently expressed and purified head protein and scaffolding protein. J. Mol. Biol. 258: 286-298
    • (1996) J. Mol. Biol. , vol.258 , pp. 286-298
    • Cerritelli, M.E.1    Studier, F.W.2
  • 78
    • 0001315638 scopus 로고
    • Structure and assembly of herpesviruses
    • 78 Rixon F. J. (1993) Structure and assembly of herpesviruses. Semin. Virol. 4: 135-144
    • (1993) Semin. Virol. , vol.4 , pp. 135-144
    • Rixon, F.J.1
  • 79
    • 0001860050 scopus 로고    scopus 로고
    • Herpesvirus capsid assembly and envelopment
    • Chiu W., Burnett R. M. and Garcia R. L. (eds), Oxford University Press, New York
    • 79 Steven A. C. and Spear P. G. (1997) Herpesvirus capsid assembly and envelopment. In: Structural Biology of Viruses, pp. 312-351, Chiu W., Burnett R. M. and Garcia R. L. (eds), Oxford University Press, New York
    • (1997) Structural Biology of Viruses , pp. 312-351
    • Steven, A.C.1    Spear, P.G.2
  • 80
    • 0025060289 scopus 로고
    • Three-dimensional structures of maturable and abortive capsids of equine herpesvirus I from cryoelectron microscopy
    • 80 Baker T. S., Newcomb W. W., Booy F. P., Brown J. C. and Steven A. C. (1990) Three-dimensional structures of maturable and abortive capsids of equine herpesvirus I from cryoelectron microscopy. J. Virol. 64: 563-573
    • (1990) J. Virol. , vol.64 , pp. 563-573
    • Baker, T.S.1    Newcomb, W.W.2    Booy, F.P.3    Brown, J.C.4    Steven, A.C.5
  • 81
    • 0026073819 scopus 로고
    • Liquid-crystalline, phage-like packing of encapsidated DNA in herpes simplex virus
    • 81 Booy F. P., Newcomb W. W., Trus B. L., Brown J. C., Baker T. S. and Steven A. C. (1991) Liquid-crystalline, phage-like packing of encapsidated DNA in herpes simplex virus. Cell 64: 1007-1015
    • (1991) Cell , vol.64 , pp. 1007-1015
    • Booy, F.P.1    Newcomb, W.W.2    Trus, B.L.3    Brown, J.C.4    Baker, T.S.5    Steven, A.C.6
  • 82
    • 0024552611 scopus 로고
    • Three-dimensional structure of the HSV1 nucleocapsid
    • 82 Schrag J. D., Prasad B. V. V., Rixon F. J. and Chiu W. (1989) Three-dimensional structure of the HSV1 nucleocapsid. Cell 56: 651-660
    • (1989) Cell , vol.56 , pp. 651-660
    • Schrag, J.D.1    Prasad, B.V.V.2    Rixon, F.J.3    Chiu, W.4
  • 83
    • 0027291013 scopus 로고
    • Structure of the herpes simplex virus capsid. Molecular composition of the pentons and the triplexes
    • 83 Newcomb W. W., Trus B. L., Booy F. P., Steven A. C., Wall J. S. and Brown J. C. (1993) Structure of the herpes simplex virus capsid. Molecular composition of the pentons and the triplexes. J. Mol. Biol. 232: 499-511
    • (1993) J. Mol. Biol. , vol.232 , pp. 499-511
    • Newcomb, W.W.1    Trus, B.L.2    Booy, F.P.3    Steven, A.C.4    Wall, J.S.5    Brown, J.C.6
  • 84
    • 0032029782 scopus 로고    scopus 로고
    • Capsids are formed in a mutant virus blocked at the maturation site of the UL26 and UL26.5 open reading frames of herpes simplex virus type 1 but are not formed in a null mutant of UL38 (VP19C)
    • 84 Person S. and Desai P. (1998) Capsids are formed in a mutant virus blocked at the maturation site of the UL26 and UL26.5 open reading frames of herpes simplex virus type 1 but are not formed in a null mutant of UL38 (VP19C). Virology 242: 193-203
    • (1998) Virology , vol.242 , pp. 193-203
    • Person, S.1    Desai, P.2
  • 85
    • 0032539811 scopus 로고    scopus 로고
    • Identification of the sites of interaction between the scaffold and outer shell in herpes simplex virus-1 capsids by difference electron imaging
    • 85 Zhou Z. H., Macnab S. J., Jakana J., Scott L. R., Chiu W. and Rixon F. J. (1998) Identification of the sites of interaction between the scaffold and outer shell in herpes simplex virus-1 capsids by difference electron imaging. Proc. Natl. Acad. Sci. USA 95: 2778-2783
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2778-2783
    • Zhou, Z.H.1    Macnab, S.J.2    Jakana, J.3    Scott, L.R.4    Chiu, W.5    Rixon, F.J.6
  • 86
    • 0028210056 scopus 로고
    • Localization of the herpes simplex virus type 1 major capsid protein VP5 in the cell nucleus requires the abundant scaffolding protein VP22a
    • 86 Nicholson P., Addison C., Cross A. M., Kennard J., Preston V. G. and Rixon F. J. (1994) Localization of the herpes simplex virus type 1 major capsid protein VP5 in the cell nucleus requires the abundant scaffolding protein VP22a. J. Gen. Virol. 75: 1091-1099
    • (1994) J. Gen. Virol. , vol.75 , pp. 1091-1099
    • Nicholson, P.1    Addison, C.2    Cross, A.M.3    Kennard, J.4    Preston, V.G.5    Rixon, F.J.6
  • 87
    • 0031060532 scopus 로고    scopus 로고
    • Human cytomegalovirus capsid assembly protein precursor (pUL80.5) interacts with itself and with the major capsid protein (pUL86) through two different domains
    • 87 Wood L. J., Baxter M. K., Plafker S. M. and Gibson W. (1997) Human cytomegalovirus capsid assembly protein precursor (pUL80.5) interacts with itself and with the major capsid protein (pUL86) through two different domains. J. Virol. 71: 179-190
    • (1997) J. Virol. , vol.71 , pp. 179-190
    • Wood, L.J.1    Baxter, M.K.2    Plafker, S.M.3    Gibson, W.4
  • 89
    • 0029840591 scopus 로고    scopus 로고
    • Multiple interactions control the intracellular localization of the herpes simplex virus type 1 capsid proteins
    • 89 Rixon F. J., Addison C., MacGregor A., Macnab S. J., Nicholson P., Preston V. G. et al. (1996) Multiple interactions control the intracellular localization of the herpes simplex virus type 1 capsid proteins. J. Gen. Virol. 77: 2251-2260
    • (1996) J. Gen. Virol. , vol.77 , pp. 2251-2260
    • Rixon, F.J.1    Addison, C.2    MacGregor, A.3    Macnab, S.J.4    Nicholson, P.5    Preston, V.G.6
  • 90
    • 0028256487 scopus 로고
    • Assembly of herpes simplex virus type 1 capsids using a panel of recombinant baculoviruses
    • 90 Tatman J. D., Preston V. G., Nicholson P., Elliott R. M. and Rixon F. J. (1994) Assembly of herpes simplex virus type 1 capsids using a panel of recombinant baculoviruses. J. Gen. Virol. 75: 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
  • 91
    • 0028345731 scopus 로고
    • Assembly of herpes simplex virus (HSV) intermediate capsids in insect cells infected with recombinant baculoviruses expressing HSV capsid proteins
    • 91 Thomsen D. R., Roof L. L. and Homa F. L. (1994) Assembly of herpes simplex virus (HSV) intermediate capsids in insect cells infected with recombinant baculoviruses expressing HSV capsid proteins. J. Virol. 68: 2442-2457
    • (1994) J. Virol. , vol.68 , pp. 2442-2457
    • Thomsen, D.R.1    Roof, L.L.2    Homa, F.L.3
  • 92
    • 0028031336 scopus 로고
    • Cell-free assembly of the herpes simplex virus capsid
    • 92 Newcomb W. W., Homa F. L., Thomsen D. R., Ye Z. and Brown J. C. (1994) Cell-free assembly of the herpes simplex virus capsid. J. Virol. 68: 6059-6063
    • (1994) J. Virol. , vol.68 , pp. 6059-6063
    • Newcomb, W.W.1    Homa, F.L.2    Thomsen, D.R.3    Ye, Z.4    Brown, J.C.5
  • 93
    • 0030298322 scopus 로고    scopus 로고
    • Assembly of the herpes simplex virus capsid: Characterization of intermediates observed during cell-free capsid formation
    • 93 Newcomb W. W., Homa F. L., Thomsen D. R., Booy F. P., Trus B. L., Steven A. C. et al. (1996) Assembly of the herpes simplex virus capsid: characterization of intermediates observed during cell-free capsid formation. J. Mol. Biol. 263: 432-446
    • (1996) J. Mol. Biol. , vol.263 , pp. 432-446
    • Newcomb, W.W.1    Homa, F.L.2    Thomsen, D.R.3    Booy, F.P.4    Trus, B.L.5    Steven, A.C.6
  • 94
    • 0031980307 scopus 로고    scopus 로고
    • Assembly of the herpes simplex virus capsid: Preformed triplexes bind to the nascent capsid
    • 94 Spencer J. V., Newcomb W. W., Thomsen D. R., Homa F. L. and Brown J. C. (1998) Assembly of the herpes simplex virus capsid: preformed triplexes bind to the nascent capsid. J. Virol. 72: 3944-3951
    • (1998) J. Virol. , vol.72 , pp. 3944-3951
    • Spencer, J.V.1    Newcomb, W.W.2    Thomsen, D.R.3    Homa, F.L.A.4    Brown, J.C.5
  • 95
    • 0028067308 scopus 로고
    • The size and symmetry of B capsids of herpes simplex virus type 1 are determined by the gene products of the UL26 open reading frame
    • 95 Desai P., Watkins S. C. and Person S. (1994) The size and symmetry of B capsids of herpes simplex virus type 1 are determined by the gene products of the UL26 open reading frame. J. Virol. 68: 5365-5374
    • (1994) J. Virol. , vol.68 , pp. 5365-5374
    • Desai, P.1    Watkins, S.C.2    Person, S.3
  • 96
    • 0023797055 scopus 로고
    • The products of herpes simplex virus type 1 gene UL26 which are involved in DNA packaging are strongly associated with empty but not with full capsids
    • 96 Rixon F. J., Cross A. M., Addison C. and Preston V. G. (1988) The products of herpes simplex virus type 1 gene UL26 which are involved in DNA packaging are strongly associated with empty but not with full capsids. J. Gen. Virol. 69: 2879-2891
    • (1988) J. Gen. Virol. , vol.69 , pp. 2879-2891
    • Rixon, F.J.1    Cross, A.M.2    Addison, C.3    Preston, V.G.4
  • 97
    • 0026098298 scopus 로고
    • Structure of the herpes simplex virus capsid: Effects of extraction with guanidine-HCI and partial reconstruction of extracted capsids
    • 97 Newcomb W. W. and Brown J. (1991) Structure of the herpes simplex virus capsid: effects of extraction with guanidine-HCI and partial reconstruction of extracted capsids. J. Virol. 65: 613-620
    • (1991) J. Virol. , vol.65 , pp. 613-620
    • Newcomb, W.W.1    Brown, J.2
  • 98
    • 0029908793 scopus 로고    scopus 로고
    • The herpes simplex virus procapsid: Structure, conformational changes upon maturation, and roles of the triplex proteins VP19c and VP23 in assembly
    • 98 Trus B. L., Booy F. P., Newcomb W. W., Brown J. C., Homa F. L., Thomsen D. R. et al. (1996) The herpes simplex virus procapsid: structure, conformational changes upon maturation, and roles of the triplex proteins VP19c and VP23 in assembly. J. Mol. Biol. 263: 447-462
    • (1996) J. Mol. Biol. , vol.263 , pp. 447-462
    • Trus, B.L.1    Booy, F.P.2    Newcomb, W.W.3    Brown, J.C.4    Homa, F.L.5    Thomsen, D.R.6
  • 99
    • 0029655959 scopus 로고    scopus 로고
    • Identification of a minimal Hydrophobic domain in the herpes simplex virus type 1 scaffolding protein which is required for interaction with the major capsid protein
    • 99 Hong Z., Beaudet-Miller M., Durkin J., Zhang R. and Kwong A. D. (1996) Identification of a minimal Hydrophobic domain in the herpes simplex virus type 1 scaffolding protein which is required for interaction with the major capsid protein. J. Virol. 70: 533-540
    • (1996) J. Virol. , vol.70 , pp. 533-540
    • Hong, Z.1    Beaudet-Miller, M.2    Durkin, J.3    Zhang, R.4    Kwong, A.D.5
  • 100
    • 0029843595 scopus 로고    scopus 로고
    • Virus-specific interaction between the human cytomegalovirus major capsid protein and the C terminus of the assembly protein precursor
    • 100 Beaudet-Miller M., Zhang R., Durkin J., Gibson W., Kwong A. D. and Hong Z. (1996) Virus-specific interaction between the human cytomegalovirus major capsid protein and the C terminus of the assembly protein precursor. J. Virol. 70: 8081-8088
    • (1996) J. Virol. , vol.70 , pp. 8081-8088
    • Beaudet-Miller, M.1    Zhang, R.2    Durkin, J.3    Gibson, W.4    Kwong, A.D.5    Hong, Z.6
  • 101
    • 0031026433 scopus 로고    scopus 로고
    • Assembly of herpes simplex virus capsids using the human cytomegalovirus scaffold protein: Critical role of the C terminus
    • 101 Oien N. L., Thomsen D. R., Wathen M. W., Newcomb W. W., Brown J. C. and Homa F. L. (1997) Assembly of herpes simplex virus capsids using the human cytomegalovirus scaffold protein: critical role of the C terminus. J. Virol. 71: 1281-1291
    • (1997) J. Virol. , vol.71 , pp. 1281-1291
    • Oien, N.L.1    Thomsen, D.R.2    Wathen, M.W.3    Newcomb, W.W.4    Brown, J.C.5    Homa, F.L.6
  • 102
    • 0030860067 scopus 로고    scopus 로고
    • Efficient herpes simplex virus type 1 (HSV-1) capsid formation directed by the varicella-zoster virus scaffolding protein requires the carboxy-terminal sequences from the HSV-1 homologue
    • 102 Preston V. G., Kennard J., Rixon F. J., Logan A. J., Mansfield R. W. and McDougall I. M. (1997) Efficient herpes simplex virus type 1 (HSV-1) capsid formation directed by the varicella-zoster virus scaffolding protein requires the carboxy-terminal sequences from the HSV-1 homologue. J. Gen. Virol. 78: 1633-1646
    • (1997) J. Gen. Virol. , vol.78 , pp. 1633-1646
    • Preston, V.G.1    Kennard, J.2    Rixon, F.J.3    Logan, A.J.4    Mansfield, R.W.5    McDougall, I.M.6
  • 103
    • 0028800285 scopus 로고
    • The bovine herpesvirus 1 maturational proteinase and scaffold proteins can substitute for the homologous herpes simplex virus type 1 proteins in the formation of hybrid type B capsids
    • 103 Haanes E. J., Thomsen D. R., Martin S., Homa F. L. and Lowery D. E. (1995) The bovine herpesvirus 1 maturational proteinase and scaffold proteins can substitute for the homologous herpes simplex virus type 1 proteins in the formation of hybrid type B capsids. J. Virol. 69: 7375-7379
    • (1995) J. Virol. , vol.69 , pp. 7375-7379
    • Haanes, E.J.1    Thomsen, D.R.2    Martin, S.3    Homa, F.L.4    Lowery, D.E.5
  • 104
    • 0030923354 scopus 로고    scopus 로고
    • Self-association of herpes simplex virus type 1 ICP35 is via coiled-coil interactions and promotes stable interaction with the major capsid protein
    • 104 Pelletier A., Do F., Brisebois J. J., Lagace L. and Cordingley M. G. (1997) Self-association of herpes simplex virus type 1 ICP35 is via coiled-coil interactions and promotes stable interaction with the major capsid protein. J. Virol. 71: 5197-5208
    • (1997) J. Virol. , vol.71 , pp. 5197-5208
    • Pelletier, A.1    Do, F.2    Brisebois, J.J.3    Lagace, L.4    Cordingley, M.G.5
  • 105
    • 0000956277 scopus 로고
    • Bacteriophage T4, Mathews C. K. (ed.), ASM Press, Washington, DC
    • 105 Black L. W., Showe M. K. and Steven A. C. (1995) Morphogenesis of the T4 head. In: Bacteriophage T4, pp. 218-258, Mathews C. K. (ed.), ASM Press, Washington, DC
    • (1995) Morphogenesis of the T4 Head , pp. 218-258
    • Black, L.W.1    Showe, M.K.2    Steven, A.C.3
  • 106
    • 0021336823 scopus 로고
    • Formation of the prohead core of bacteriophage T4 in vivo
    • 106 Traub F. and Maeder M. (1984) Formation of the prohead core of bacteriophage T4 in vivo. J. Virol. 49: 892-901
    • (1984) J. Virol. , vol.49 , pp. 892-901
    • Traub, F.1    Maeder, M.2
  • 107
    • 0021343670 scopus 로고
    • Isolation of the prohead core of bacteriophage T4 after cross-linking and determination of protein composition
    • 107 Traub F., Keller B., Kuhn A. and Maeder M. (1984) Isolation of the prohead core of bacteriophage T4 after cross-linking and determination of protein composition. J. Virol. 49: 902-908
    • (1984) J. Virol. , vol.49 , pp. 902-908
    • Traub, F.1    Keller, B.2    Kuhn, A.3    Maeder, M.4
  • 108
    • 0017881643 scopus 로고
    • Isolation and characterization of bacteriophage T4 mutant preheads
    • 108 Onorato L., Stirmer B. and Showe M. K. (1978) Isolation and characterization of bacteriophage T4 mutant preheads. J. Virol. 2: 409-426
    • (1978) J. Virol. , vol.2 , pp. 409-426
    • Onorato, L.1    Stirmer, B.2    Showe, M.K.3
  • 109
    • 0018936770 scopus 로고
    • Probable localization of the bacteriophage T4 prehead proteinase zymogen in the center of the prehead core
    • 109 van Driel R., Traub F. and Showe M. K. (1980) Probable localization of the bacteriophage T4 prehead proteinase zymogen in the center of the prehead core. J. Virol. 36: 220-223
    • (1980) J. Virol. , vol.36 , pp. 220-223
    • Van Driel, R.1    Traub, F.2    Showe, M.K.3
  • 110
    • 0019747519 scopus 로고
    • Bacteriophage T4 head assembly. In vivo characterisation of the morphopoietic core
    • 110 Traub F., Maeder M. and Kellenberger E. (1981) Bacteriophage T4 head assembly. In vivo characterisation of the morphopoietic core. Prog. Clin. Biol. Res. 64: 127-137
    • (1981) Prog. Clin. Biol. Res. , vol.64 , pp. 127-137
    • Traub, F.1    Maeder, M.2    Kellenberger, E.3
  • 111
    • 0018184953 scopus 로고
    • Assembly of bacteriophage T4 head-related structures. II. In vitro assembly of prehead-like structures
    • 111 van Driel R. and Couture E. (1978) Assembly of bacteriophage T4 head-related structures. II. In vitro assembly of prehead-like structures. J. Mol. Biol. 123: 115-128
    • (1978) J. Mol. Biol. , vol.123 , pp. 115-128
    • Van Driel, R.1    Couture, E.2
  • 112
    • 0018276730 scopus 로고
    • Assembly of the scaffolding core of bacteriophage T4 preheads
    • 112 van Driel R. and Couture E. (1978) Assembly of the scaffolding core of bacteriophage T4 preheads. J. Mol. Biol. 123: 713-719
    • (1978) J. Mol. Biol. , vol.123 , pp. 713-719
    • Van Driel, R.1    Couture, E.2
  • 113
    • 0014966072 scopus 로고
    • Studies on the morphopoiesis of the head of bacteriophage T-even. 8. Multilayered polyheads
    • 113 Yanagida M., Boy de la Tour E., Alff-Steinberger C, and Kellenberger E. (1970) Studies on the morphopoiesis of the head of bacteriophage T-even. 8. Multilayered polyheads. J. Mol. Biol. 50: 35-58
    • (1970) J. Mol. Biol. , vol.50 , pp. 35-58
    • Yanagida, M.1    Boy De La Tour, E.2    Alff-Steinberger, C.3    Kellenberger, E.4
  • 114
    • 0017756315 scopus 로고
    • Assembly of T4 head-related structures. Assembly of polyheads in vitro
    • 114 van Driel R. (1977) Assembly of T4 head-related structures. Assembly of polyheads in vitro. J. Mol. Biol. 114: 61-72
    • (1977) J. Mol. Biol. , vol.114 , pp. 61-72
    • Van Driel, R.1
  • 115
    • 0022495729 scopus 로고
    • Assembly and disassembly of bacteriophage T4 polyheads
    • 115 Caldentey J. and Kellenberger E. (1986) Assembly and disassembly of bacteriophage T4 polyheads. J. Mol. Biol. 188: 39-48
    • (1986) J. Mol. Biol. , vol.188 , pp. 39-48
    • Caldentey, J.1    Kellenberger, E.2
  • 116
    • 0023644971 scopus 로고
    • Isolation and reassembly of bacteriophage T4 core proteins
    • 116 Caldentey J., Lepault J. and Kellenberger E. (1987) Isolation and reassembly of bacteriophage T4 core proteins. J. Mol. Biol. 195: 637-647
    • (1987) J. Mol. Biol. , vol.195 , pp. 637-647
    • Caldentey, J.1    Lepault, J.2    Kellenberger, E.3
  • 117
    • 0031579251 scopus 로고    scopus 로고
    • Isolation of a gp20-complex and its role in in vitro assembly of both prohead and core of bacteriophage T4
    • 117 Kato H. and Baschong C. (1997) Isolation of a gp20-complex and its role in in vitro assembly of both prohead and core of bacteriophage T4, Virology 227: 400-408
    • (1997) Virology , vol.227 , pp. 400-408
    • Kato, H.1    Baschong, C.2
  • 118
    • 0017287393 scopus 로고
    • Head length determination in bacteriophage T4: The role of the core protein P22
    • 118 Paulson J. R., Lazaroff S. and Laemmli U. K. (1976) Head length determination in bacteriophage T4: the role of the core protein P22. J. Mol. Biol. 103: 155-174
    • (1976) J. Mol. Biol. , vol.103 , pp. 155-174
    • Paulson, J.R.1    Lazaroff, S.2    Laemmli, U.K.3
  • 119
    • 0022537299 scopus 로고
    • Amber mutants in gene 67 of phage T4. Effects on formation and shape determination of the head
    • 119 Keller B., Maeder M., Becker-Laburte C., Kellenberger E. and Bickle T. A. (1986) Amber mutants in gene 67 of phage T4. Effects on formation and shape determination of the head. J. Mol. Biol. 190: 83-95
    • (1986) J. Mol. Biol. , vol.190 , pp. 83-95
    • Keller, B.1    Maeder, M.2    Becker-Laburte, C.3    Kellenberger, E.4    Bickle, T.A.5
  • 120
    • 0023690367 scopus 로고
    • Length and shape variants of the bacteriophage T4 head: Mutations in the scaffolding core genes 68 and 22
    • 120 Keller B., Dubochet J., Adrian M., Maeder M., Wurtz M. and Kellenberger E. (1988) Length and shape variants of the bacteriophage T4 head: mutations in the scaffolding core genes 68 and 22. J. Virol. 62: 2960-2969
    • (1988) J. Virol. , vol.62 , pp. 2960-2969
    • Keller, B.1    Dubochet, J.2    Adrian, M.3    Maeder, M.4    Wurtz, M.5    Kellenberger, E.6
  • 121
    • 0025614822 scopus 로고
    • A proposed structure of bacteriophage T4 gene product 22 - A major prohead scaffolding core protein
    • 121 Mesyanzhinov V. V., Sobolev B. N., Marusich E. I. and Efimov V. P. (1990) A proposed structure of bacteriophage T4 gene product 22 - a major prohead scaffolding core protein. J. Struct. Biol. 104; 24-31
    • (1990) J. Struct. Biol. , vol.104 , pp. 24-31
    • Mesyanzhinov, V.V.1    Sobolev, B.N.2    Marusich, E.I.3    Efimov, V.P.4
  • 122
    • 0018862157 scopus 로고
    • Assembly of bacteriophage T4 head-related structures. IV. Isolation and association properties of T4 prehead proteins
    • 122 van Driel R. (1980) Assembly of bacteriophage T4 head-related structures. IV. Isolation and association properties of T4 prehead proteins. J. Mol. Biol. 138: 27-42
    • (1980) J. Mol. Biol. , vol.138 , pp. 27-42
    • Van Driel, R.1
  • 123
    • 0020158116 scopus 로고
    • A proposed structure of the prolate phage T4 prehead core. An electron microscopic study
    • 123 Engel A., van Driel R. and Driedonks R. (1982) A proposed structure of the prolate phage T4 prehead core. An electron microscopic study. J. Ultrastruct. Res. 80: 12-22
    • (1982) J. Ultrastruct. Res. , vol.80 , pp. 12-22
    • Engel, A.1    Van Driel, R.2    Driedonks, R.3
  • 124
    • 0017353813 scopus 로고
    • Morphogenetic core of the bacteriophage T4 head: Structure of the core in polyheads
    • 124 Paulson J. R. and Lacmmli U. K. (1977) Morphogenetic core of the bacteriophage T4 head: structure of the core in polyheads. J. Mol. Biol. 111: 459-485
    • (1977) J. Mol. Biol. , vol.111 , pp. 459-485
    • Paulson, J.R.1    Lacmmli, U.K.2
  • 125
    • 0031928582 scopus 로고    scopus 로고
    • On the structure of the scaffolding core of bacteriophage T4 and its role in head length determination
    • 125 Berger B. and Shor P. W. (1998) On the structure of the scaffolding core of bacteriophage T4 and its role in head length determination. J. Struct. Biol. 121: 285-294
    • (1998) J. Struct. Biol. , vol.121 , pp. 285-294
    • Berger, B.1    Shor, P.W.2
  • 126
    • 0019816862 scopus 로고
    • Gene 20 product of bacteriophage T4, its purification and structure
    • 126 Driedonks R. A., Engel A., ten Heggeler B. and van Driel R. (1981) Gene 20 product of bacteriophage T4, its purification and structure. J. Mol. Biol. 152: 641-662
    • (1981) J. Mol. Biol. , vol.152 , pp. 641-662
    • Driedonks, R.A.1    Engel, A.2    Ten Heggeler, B.A.3    Van Driel, R.4
  • 127
    • 0017231208 scopus 로고
    • Head morphologies in bacteriophage T4 head and internal protein mutant infections
    • 127 Black L. W. and Brown D. T. (1976) Head morphologies in bacteriophage T4 head and internal protein mutant infections. J. Virol. 17: 894-905
    • (1976) J. Virol. , vol.17 , pp. 894-905
    • Black, L.W.1    Brown, D.T.2
  • 128
    • 0017148706 scopus 로고
    • Bacteriophage T4 prehead proteinase. II. Its cleavage from the product of gene 21 and regulation in phage-infected cells
    • 128 Showe M. K., Isobe E. and Onorato L. (1976) Bacteriophage T4 prehead proteinase. II. Its cleavage from the product of gene 21 and regulation in phage-infected cells. J. Mol. Biol. 107: 55-69
    • (1976) J. Mol. Biol. , vol.107 , pp. 55-69
    • Showe, M.K.1    Isobe, E.2    Onorato, L.3
  • 129
    • 0017190085 scopus 로고
    • Bacteriophage T4 prehead proteinase. I. Purification and properties of a bacteriophage enzyme which cleaves the capsid precursor proteins
    • 129 Showe M. K., Isobe E. and Onorato L. (1976) Bacteriophage T4 prehead proteinase. I. Purification and properties of a bacteriophage enzyme which cleaves the capsid precursor proteins. J. Mol. Biol. 107: 35-54
    • (1976) J. Mol. Biol. , vol.107 , pp. 35-54
    • Showe, M.K.1    Isobe, E.2    Onorato, L.3
  • 130
    • 0013909852 scopus 로고
    • Structure of Bacillus subtilis bacteriophage φ29 and the length of φ29 deoxyribonulecic acid
    • 130 Anderson D. L., Hickman D. D. and Reilly B. E. (1966) Structure of Bacillus subtilis bacteriophage φ29 and the length of φ29 deoxyribonulecic acid. J Bacteriol. 91: 2081-2089
    • (1966) J Bacteriol. , vol.91 , pp. 2081-2089
    • Anderson, D.L.1    Hickman, D.D.2    Reilly, B.E.3
  • 132
    • 0032582665 scopus 로고    scopus 로고
    • Bacteriophage φ29: A complex biological machine studied by cryo-electron microscopy
    • 132 Tao Y., Olson N. H., Xu W., Anderson D. L., Rossmann M. G. and Baker T. S. (1998) Bacteriophage φ29: a complex biological machine studied by cryo-electron microscopy. Cell 95: 431-437
    • (1998) Cell , vol.95 , pp. 431-437
    • Tao, Y.1    Olson, N.H.2    Xu, W.3    Anderson, D.L.4    Rossmann, M.G.5    Baker, T.S.6
  • 133
    • 0017101218 scopus 로고
    • Morphogenesis of bacteriophage φ29 of Bacillus subtilis: Preliminary isolation and characterization of intermediate particles of the assembly pathway
    • 133 Nelson R. A., Reilly B. E. and Anderson D. L. (1976) Morphogenesis of bacteriophage φ29 of Bacillus subtilis: preliminary isolation and characterization of intermediate particles of the assembly pathway. J. Virol. 19: 518-532
    • (1976) J. Virol. , vol.19 , pp. 518-532
    • Nelson, R.A.1    Reilly, B.E.2    Anderson, D.L.3
  • 135
    • 0017594208 scopus 로고
    • Assembly of Bacillus subtilis phage φ29. I. Mutants in the cistrons coding for the structural proteins
    • 135 Camacho A., Jimenez F., De La Torre J., Carrascosa J. L., Mellado R. P., Vasquez, C. et al. (1977) Assembly of Bacillus subtilis phage φ29. I. Mutants in the cistrons coding for the structural proteins. Eur. J. Biochem. 73: 39-55
    • (1977) Eur. J. Biochem. , vol.73 , pp. 39-55
    • Camacho, A.1    Jimenez, F.2    De la Torre, J.3    Carrascosa, J.L.4    Mellado, R.P.5    Vasquez, C.6
  • 136
    • 0021894713 scopus 로고
    • Morphogenesis of bacteriophage φ29 of Bacillus subtilis: Prohead restoration for DNA-gp3 packaging and assembly
    • 136 Bjornsti M.-A., Reilly B. E. and Anderson D. L. (1985) Morphogenesis of bacteriophage φ29 of Bacillus subtilis: prohead restoration for DNA-gp3 packaging and assembly. J. Virol. 53: 858-861
    • (1985) J. Virol. , vol.53 , pp. 858-861
    • Bjornsti, M.-A.1    Reilly, B.E.2    Anderson, D.L.3
  • 137
    • 0025923286 scopus 로고
    • Regulation of phage φ29 prohead shape and size by the portal vertex
    • 137 Guo P., Erickson S., Xu W., Olson N., Baker T. S. and Anderson D. (1991) Regulation of phage φ29 prohead shape and size by the portal vertex. Virology 183: 366-373
    • (1991) Virology , vol.183 , pp. 366-373
    • Guo, P.1    Erickson, S.2    Xu, W.3    Olson, N.4    Baker, T.S.5    Anderson, D.6
  • 138
    • 0029078936 scopus 로고
    • In vitro assembly of infectious virions of ds-DNA phage φ29 from cloned gene products and synthetic nucleic acids
    • 138 Lee C. S. and Guo P. (1995) In vitro assembly of infectious virions of ds-DNA phage φ29 from cloned gene products and synthetic nucleic acids. J. Virol. 69: 5018-5023
    • (1995) J. Virol. , vol.69 , pp. 5018-5023
    • Lee, C.S.1    Guo, P.2
  • 139
    • 0029039737 scopus 로고
    • Sequential interactions of structural proteins in phage φ29 procapsid assembly
    • 139 Lee C. S. and Guo P. (1995) Sequential interactions of structural proteins in phage φ29 procapsid assembly. J. Virol. 69: 5024-5032
    • (1995) J. Virol. , vol.69 , pp. 5024-5032
    • Lee, C.S.1    Guo, P.2
  • 140
    • 0027965277 scopus 로고
    • A highly sensitive system for the assay of in vitro viral assembly of bacteriophage φ29 of Bacillus subtilis
    • 140 Lee C. S. and Guo P. (1994) A highly sensitive system for the assay of in vitro viral assembly of bacteriophage φ29 of Bacillus subtilis. Virology 202: 1039-1042
    • (1994) Virology , vol.202 , pp. 1039-1042
    • Lee, C.S.1    Guo, P.2
  • 141
    • 0015886707 scopus 로고
    • Bacteriophage P2 head morphogenesis: Cleavage of the major capsid protein
    • 141 Lengyel J. A., Goldstein R. N., Marsh M., Sunshine M. G. and Calendar R. (1973) Bacteriophage P2 head morphogenesis: cleavage of the major capsid protein. Virology 53: 1-23
    • (1973) Virology , vol.53 , pp. 1-23
    • Lengyel, J.A.1    Goldstein, R.N.2    Marsh, M.3    Sunshine, M.G.4    Calendar, R.5
  • 142
    • 0025271666 scopus 로고
    • Regulation of icosahedral virion capsid size by the in vitro activity of a cloned gene product
    • 142 Agarwal M., Arthur M., Arbeit R. D. and Goldstein R. (1990) Regulation of icosahedral virion capsid size by the in vitro activity of a cloned gene product. Proc. Nat. Acad. Sci. USA 87: 2428-2432
    • (1990) Proc. Nat. Acad. Sci. USA , vol.87 , pp. 2428-2432
    • Agarwal, M.1    Arthur, M.2    Arbeit, R.D.3    Goldstein, R.4
  • 143
    • 0028151705 scopus 로고
    • Bacteriophage P2 and P4 morphogenesis: Assembly precedes proteolylic processing of the capsid proteins
    • 143 Marvik O. J., Jacobsen E., Dokland T. and Lindqvist B. H. (1994) Bacteriophage P2 and P4 morphogenesis: assembly precedes proteolylic processing of the capsid proteins. Virology 205: 51-65
    • (1994) Virology , vol.205 , pp. 51-65
    • Marvik, O.J.1    Jacobsen, E.2    Dokland, T.3    Lindqvist, B.H.4
  • 144
    • 0028223884 scopus 로고
    • Bacteriophage P2 and P4 morphogenesis: Identification and characterization of the portal protein
    • 144 Rishovd S., Marvik O. J., Jacobsen E. and Lindqvist B. H. (1994) Bacteriophage P2 and P4 morphogenesis: identification and characterization of the portal protein. Virology 200: 744-751
    • (1994) Virology , vol.200 , pp. 744-751
    • Rishovd, S.1    Marvik, O.J.2    Jacobsen, E.3    Lindqvist, B.H.4
  • 145
    • 0032565727 scopus 로고    scopus 로고
    • Bacteriophage P2 nad P4 morphogenesis: Structure and function of the connector
    • 145 Rishovd S., Holzenburg A., Johansen B. V. and Lindqvist B. H. (1998) Bacteriophage P2 nad P4 morphogenesis: structure and function of the connector. Virology 245: 11-17
    • (1998) Virology , vol.245 , pp. 11-17
    • Rishovd, S.1    Holzenburg, A.2    Johansen, B.V.3    Lindqvist, B.H.4
  • 146
    • 0033548237 scopus 로고    scopus 로고
    • Cross-functional analysis of the microviridae internal scaffolding protein
    • 146 Burch A. D., Ta J. and Fane B. A. (1999) Cross-functional analysis of the Microviridae internal scaffolding protein. J. Mol. Biol. 286: 95-104
    • (1999) J. Mol. Biol. , vol.286 , pp. 95-104
    • Burch, A.D.1    Ta, J.2    Fane, B.A.3
  • 147
  • 149
    • 0001859172 scopus 로고    scopus 로고
    • The structure of adenovirus
    • Chiu W., Burnett R. M. and Garcia R. L. (eds), Oxford University Press, New York
    • 149 Burnett R. M. (1997) The structure of adenovirus. In: Structural Biology of Viruses, pp. 209-238, Chiu W., Burnett R. M. and Garcia R. L. (eds), Oxford University Press, New York
    • (1997) Structural Biology of Viruses , pp. 209-238
    • Burnett, R.M.1
  • 152
    • 0017805150 scopus 로고
    • Assembly intermediates among adenovirus type 5 temperature-sensitive mutants
    • 152 Edvardsson B., Ustacelebi S., Williams J. and Philipson L. (1978) Assembly intermediates among adenovirus type 5 temperature-sensitive mutants. J. Virol. 25: 641-651
    • (1978) J. Virol. , vol.25 , pp. 641-651
    • Edvardsson, B.1    Ustacelebi, S.2    Williams, J.3    Philipson, L.4
  • 153
    • 0017812369 scopus 로고
    • Temperature-sensitive mutant of adenovirus type 2 blocked in virion assembly: Accumulation of light intermediate particles
    • 153 D'Halluin J.-C., Milleville M., Boulanger P. A. and Martin G. R. (1978) Temperature-sensitive mutant of adenovirus type 2 blocked in virion assembly: accumulation of light intermediate particles. J. Virol. 26: 344-356
    • (1978) J. Virol. , vol.26 , pp. 344-356
    • D'Halluin, J.-C.1    Milleville, M.2    Boulanger, P.A.3    Martin, G.R.4
  • 154
    • 0017892996 scopus 로고
    • Adenovirus type 2 assembly analyzed by reversible cross-linking of labile intermediates
    • 154 D'Halluin J. C., Martin G. R., Torpier G. and Boulanger P. A. (1978) Adenovirus type 2 assembly analyzed by reversible cross-linking of labile intermediates. J. Virol. 26: 344-356
    • (1978) J. Virol. , vol.26 , pp. 344-356
    • D'Halluin, J.C.1    Martin, G.R.2    Torpier, G.3    Boulanger, P.A.4
  • 155
    • 0031660669 scopus 로고    scopus 로고
    • Encapsidation of viral DNA requires the adenovirus LI 52/55-kilodalton protein
    • 155 Gustin K. E. and Imperiale M. J. (1998) Encapsidation of viral DNA requires the adenovirus LI 52/55-kilodalton protein. J. Virol. 72: 7860-7870
    • (1998) J. Virol. , vol.72 , pp. 7860-7870
    • Gustin, K.E.1    Imperiale, M.J.2
  • 156
    • 0019787788 scopus 로고
    • Characterization of two temperature-sensitive mutants of type 5 adenovirus with mutations in the 100,000-Dalton protein gene
    • 156 Oosterom-Dragon E. A. and Ginsberg H. S. (1981) Characterization of two temperature-sensitive mutants of type 5 adenovirus with mutations in the 100,000-Dalton protein gene. J. Virol. 40: 491-500
    • (1981) J. Virol. , vol.40 , pp. 491-500
    • Oosterom-Dragon, E.A.1    Ginsberg, H.S.2
  • 157
    • 0021183942 scopus 로고
    • Morphogenesis of human adenovirus type 2: Sequence of entry of proteins into previral and viral particles
    • 157 Morin N. and Boulanger P. (1984) Morphogenesis of human adenovirus type 2: sequence of entry of proteins into previral and viral particles. Virology 136: 153-167
    • (1984) Virology , vol.136 , pp. 153-167
    • Morin, N.1    Boulanger, P.2
  • 158
    • 0022446817 scopus 로고
    • Hexon trimerization occuring in an assembly-defective, 100K temperature-sensitive mutant of adenovirus 2
    • 158 Morin N. and Boulanger P. (1986) Hexon trimerization occuring in an assembly-defective, 100K temperature-sensitive mutant of adenovirus 2. Virology 152: 11-31
    • (1986) Virology , vol.152 , pp. 11-31
    • Morin, N.1    Boulanger, P.2
  • 159
    • 0020678190 scopus 로고
    • Coliphage P1 morphogenesis: Analysis of mutants by electron microscopy
    • 159 Walker J. T. and Walker D. H. (1983) Coliphage P1 morphogenesis: analysis of mutants by electron microscopy. J. Virol. 45: 1118-1139
    • (1983) J. Virol. , vol.45 , pp. 1118-1139
    • Walker, J.T.1    Walker, D.H.2
  • 160
    • 0029978730 scopus 로고    scopus 로고
    • Bacteriophage Mu head assembly
    • 160 Grimaud R. (1996) Bacteriophage Mu head assembly. Virology 217: 200-210
    • (1996) Virology , vol.217 , pp. 200-210
    • Grimaud, R.1
  • 161
    • 0344863179 scopus 로고    scopus 로고
    • The complete nucleotide sequence and functional organization of Bacillus subtilis bacteriophage SPP1
    • 161 Alonso J. C., Luder G., Stiege A. C., Chai S., Weise F. and Trautner T. A. (1997) The complete nucleotide sequence and functional organization of Bacillus subtilis bacteriophage SPP1. Gene 204: 201-212
    • (1997) Gene , vol.204 , pp. 201-212
    • Alonso, J.C.1    Luder, G.2    Stiege, A.C.3    Chai, S.4    Weise, F.5    Trautner, T.A.6
  • 163
    • 0028927348 scopus 로고
    • Genetic basis of bacteriophage HK97 prohead assembly
    • 163 Duda R. L., Mertincic K. and Hendrix R. W. (1995) Genetic basis of bacteriophage HK97 prohead assembly. J. Mol. Biol. 247: 636-647
    • (1995) J. Mol. Biol. , vol.247 , pp. 636-647
    • Duda, R.L.1    Mertincic, K.2    Hendrix, R.W.3
  • 164
    • 0031950208 scopus 로고    scopus 로고
    • The major structural protein of African swine fever virus, p73, is packaged into large structures, indicative of viral capsid or matrix precursors, on the endoplasmatic reticulum
    • 164 Cobbold C. and Wileman T. (1998) The major structural protein of African swine fever virus, p73, is packaged into large structures, indicative of viral capsid or matrix precursors, on the endoplasmatic reticulum. J. Virol. 72: 5215-5223
    • (1998) J. Virol. , vol.72 , pp. 5215-5223
    • Cobbold, C.1    Wileman, T.2
  • 165
    • 0020062026 scopus 로고
    • In vitro reassembly of vesicular stomatitis virus skeletons
    • 165 Newcomb W. W., Tobin G. J., McGowan J. J. and Brown J. C. (1982) In vitro reassembly of vesicular stomatitis virus skeletons. J. Virol. 41: 1055-1062
    • (1982) J. Virol. , vol.41 , pp. 1055-1062
    • Newcomb, W.W.1    Tobin, G.J.2    McGowan, J.J.3    Brown, J.C.4
  • 166
    • 0027359282 scopus 로고
    • Vesicular stomatitis virus M protein may be inside the ribonucleocapsid coil
    • 166 Barge A., Gaudin Y., Coulon P. and Ruigrok R. W. (1993) Vesicular stomatitis virus M protein may be inside the ribonucleocapsid coil. J. Virol. 67: 7246-7253
    • (1993) J. Virol. , vol.67 , pp. 7246-7253
    • Barge, A.1    Gaudin, Y.2    Coulon, P.3    Ruigrok, R.W.4
  • 167
    • 0032889562 scopus 로고    scopus 로고
    • Matrix protein of rabies virus is responsible for the assembly and budding of bullet-shaped particles and interacts with the transmembrane spike glycoprotein G
    • 167 Mebatsion T., Weiland F. and Conzelmann K.-K. (1999) Matrix protein of rabies virus is responsible for the assembly and budding of bullet-shaped particles and interacts with the transmembrane spike glycoprotein G. J. Virol. 73: 242-250
    • (1999) J. Virol. , vol.73 , pp. 242-250
    • Mebatsion, T.1    Weiland, F.2    Conzelmann, K.-K.3
  • 168
    • 0028329280 scopus 로고
    • FlgD is a scaffolding protein needed for flagellar hook assembly in Salmonella typhimurium
    • 168 Ohnishi K., Ohio Y., Aizawa S., Macnab R. M. and Iino T. (1994) FlgD is a scaffolding protein needed for flagellar hook assembly in Salmonella typhimurium. J. Bacteriol. 176: 2272-2281
    • (1994) J. Bacteriol. , vol.176 , pp. 2272-2281
    • Ohnishi, K.1    Ohio, Y.2    Aizawa, S.3    Macnab, R.M.4    Iino, T.5
  • 172
    • 0028945057 scopus 로고
    • Microtubules and microtubule-associated proteins
    • 172 Mandelkow E. and Mandelkow E.-M. (1995) Microtubules and microtubule-associated proteins. Curr. Opin. Cell Biol. 7: 72-81
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 72-81
    • Mandelkow, E.1    Mandelkow, E.-M.2
  • 175
    • 0031718358 scopus 로고    scopus 로고
    • The role of preassembled cytoplasmic complexes in assembly of flagellar dynein subunits
    • 175 Fowkes M. L. and Mitchell D. R. (1998) The role of preassembled cytoplasmic complexes in assembly of flagellar dynein subunits. Mol. Biol. Cell 9: 2337-2347
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2337-2347
    • Fowkes, M.L.1    Mitchell, D.R.2
  • 176
    • 49249151121 scopus 로고
    • Conformational flexibility and its functional significance in some protein molecules
    • 176 Huber R. (1979) Conformational flexibility and its functional significance in some protein molecules. Trends Biochem. Sci. 4: 271-276
    • (1979) Trends Biochem. Sci. , vol.4 , pp. 271-276
    • Huber, R.1
  • 177
    • 0020647920 scopus 로고
    • Functional significance of flexibility in proteins
    • 177 Huber R. and Bennett W. S. (1983) Functional significance of flexibility in proteins. Biopolymers 22: 261-279
    • (1983) Biopolymers , vol.22 , pp. 261-279
    • Huber, R.1    Bennett, W.S.2
  • 178
    • 0003974942 scopus 로고    scopus 로고
    • R. G. Landes Company, Georgetown, TX
    • 178 Subbiah S. (1996) Protein Motions, R. G. Landes Company, Georgetown, TX
    • (1996) Protein Motions
    • Subbiah, S.1
  • 180
    • 0031616362 scopus 로고    scopus 로고
    • Protein disorder and the evolution of molecular recognition: Theory, predictions and observations
    • 180 Dunker A. K., Garner E., Guilliot S., Romero P., Albrecht K., Hart J. et al. (1998) Protein disorder and the evolution of molecular recognition: theory, predictions and observations, Pac. Symp. Biocomput. 473-484
    • (1998) Pac. Symp. Biocomput. , pp. 473-484
    • Dunker, A.K.1    Garner, E.2    Guilliot, S.3    Romero, P.4    Albrecht, K.5    Hart, J.6
  • 181
  • 182
    • 0032570318 scopus 로고    scopus 로고
    • The C-terminal half of the anti-sigma factor FlgM contains a dynamic equilibrium solution structure favoring helical conformations
    • 182 Daughdrill G. W., Hanely L. J. and Dahlquist F. W. (1998) The C-terminal half of the anti-sigma factor FlgM contains a dynamic equilibrium solution structure favoring helical conformations. Biochemistry 37: 1076-1082
    • (1998) Biochemistry , vol.37 , pp. 1076-1082
    • Daughdrill, G.W.1    Hanely, L.J.2    Dahlquist, F.W.3
  • 183
    • 0030980926 scopus 로고    scopus 로고
    • The C-terminal half of the anti-sigma factor, FlgM, becomes structured when bound to its target, sigma 28
    • 183 Daughdrill G. W., Chadsey M. S., Karlinsey J. E., Hughes K. T. and Dahlquist F. W. (1997) The C-terminal half of the anti-sigma factor, FlgM, becomes structured when bound to its target, sigma 28. Nature Struct. Biol. 4: 285-291
    • (1997) Nature Struct. Biol. , vol.4 , pp. 285-291
    • Daughdrill, G.W.1    Chadsey, M.S.2    Karlinsey, J.E.3    Hughes, K.T.4    Dahlquist, F.W.5
  • 187
    • 0027278758 scopus 로고
    • Three-dimensional transformation of capsids associated with genome packaging in a bacterial virus
    • 187 Prasad B. V. V., Prevelige P. E., Marietta E., Chen R. O., Thomas D., King J. et al. (1993) Three-dimensional transformation of capsids associated with genome packaging in a bacterial virus. J. Mol. Biol. 231: 65-74
    • (1993) J. Mol. Biol. , vol.231 , pp. 65-74
    • Prasad, B.V.V.1    Prevelige, P.E.2    Marietta, E.3    Chen, R.O.4    Thomas, D.5    King, J.6
  • 188
    • 0025908787 scopus 로고
    • The maturation-dependent conformational change of phage T4 capsid involves the translocation of specific epitopes between the inner and the outer capsid surfaces
    • 188 Steven A. C., Bauer A. C., Bisher M. E., Robey F. A. and Black L. W. (1991) The maturation-dependent conformational change of phage T4 capsid involves the translocation of specific epitopes between the inner and the outer capsid surfaces. J. Struct. Biol. 106: 221-236
    • (1991) J. Struct. Biol. , vol.106 , pp. 221-236
    • Steven, A.C.1    Bauer, A.C.2    Bisher, M.E.3    Robey, F.A.4    Black, L.W.5
  • 189
    • 0025297936 scopus 로고
    • The maturation-dependent conformational change of the major capsid protein of bacteriophage T4 involves a substantial change in secondary structure
    • 189 Steven A. C., Greenstone H., Bauer A. C. and Williams R. W. (1990) The maturation-dependent conformational change of the major capsid protein of bacteriophage T4 involves a substantial change in secondary structure. Biochemistry 29: 5556-5561
    • (1990) Biochemistry , vol.29 , pp. 5556-5561
    • Steven, A.C.1    Greenstone, H.2    Bauer, A.C.3    Williams, R.W.4
  • 190
    • 0031406242 scopus 로고    scopus 로고
    • Mechanisms of virus assembly probed by Raman spectroscopy: The icosahedral bacteriophage P22
    • 190 Tuma R. and Thomas G. J. (1997) Mechanisms of virus assembly probed by Raman spectroscopy: the icosahedral bacteriophage P22. Biophys. Chem. 68: 17-31
    • (1997) Biophys. Chem. , vol.68 , pp. 17-31
    • Tuma, R.1    Thomas, G.J.2
  • 191
    • 0033039372 scopus 로고    scopus 로고
    • Mechanism of scaffolding-directed virus assembly suggested by comparison of scaffolding-containing and scaffolding-lacking P22 procapsids
    • 191 Thuman-Commike P. A., Greene B., Malinski J. A., Burbea M., McGough A., Chin W. et al. (1999) Mechanism of scaffolding-directed virus assembly suggested by comparison of scaffolding-containing and scaffolding-lacking P22 procapsids. Biophys. J. 76: 3267-3277
    • (1999) Biophys. J. , vol.76 , pp. 3267-3277
    • Thuman-Commike, P.A.1    Greene, B.2    Malinski, J.A.3    Burbea, M.4    McGough, A.5    Chin, W.6
  • 192
    • 0032544102 scopus 로고    scopus 로고
    • Mechanism of capsid maturation in a double-stranded DNA virus, proc
    • 192 Tuma R., Prevelige P. E. and Thomas G. J. (1998) Mechanism of capsid maturation in a double-stranded DNA virus, Proc. Natl. Acad. Sci. USA 95: 9885-9890
    • (1998) Natl. Acad. Sci. USA , vol.95 , pp. 9885-9890
    • Tuma, R.1    Prevelige, P.E.2    Thomas, G.J.3
  • 194
    • 0028947765 scopus 로고
    • Cold denaturation of an icosahedral virus. The role of entropy in virus assembly
    • 194 da Poian A. T., Oliveira A. C. and Silva J. L. (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
  • 195
    • 0019889063 scopus 로고
    • Thermodynamics of protein association reactions: Forces contributing to stability
    • 195 Ross P. D. and Subramanian S. (1981) Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry 20: 3096-3102
    • (1981) Biochemistry , vol.20 , pp. 3096-3102
    • Ross, P.D.1    Subramanian, S.2
  • 196
    • 0019075292 scopus 로고
    • Movement and self-control in protein assemblies: Quasi-equivalence revisited
    • 196 Caspar D. L. D. (1980) Movement and self-control in protein assemblies: quasi-equivalence revisited. Biophys. J. 32: 108-138
    • (1980) Biophys. J. , vol.32 , pp. 108-138
    • Caspar, D.L.D.1
  • 197
    • 0015911961 scopus 로고
    • Assembly of bacterial ribosomes
    • 197 Nomura M. (1973) Assembly of bacterial ribosomes. Science 179: 864-873
    • (1973) Science , vol.179 , pp. 864-873
    • Nomura, M.1
  • 198
    • 0019099296 scopus 로고
    • Bacteriophage T4 morphogenesis as a model for assembly of subcellular structure
    • 198 Wood W. B. (1980) Bacteriophage T4 morphogenesis as a model for assembly of subcellular structure. Quart. Rev. Biol. 55: 353-367
    • (1980) Quart. Rev. Biol. , vol.55 , pp. 353-367
    • Wood, W.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.