메뉴 건너뛰기




Volumn 225, Issue 1, 1996, Pages 82-96

Scaffolding mutants identifying domains required for P22 procapsid assembly and maturation

Author keywords

[No Author keywords available]

Indexed keywords

CAPSID PROTEIN;

EID: 0030296886     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1996.0577     Document Type: Article
Times cited : (51)

References (63)
  • 1
    • 0024294288 scopus 로고
    • Purification and organization of the gene 1 portal protein required for phage P22 DNA packaging
    • Bazinet, C., Benbasat, J., King, J., Carazo, J. M., and Carrascosa, J. L. (1988). Purification and organization of the gene 1 portal protein required for phage P22 DNA packaging. Biochemistry 27, 1849-1856.
    • (1988) Biochemistry , vol.27 , pp. 1849-1856
    • Bazinet, C.1    Benbasat, J.2    King, J.3    Carazo, J.M.4    Carrascosa, J.L.5
  • 2
    • 0023682381 scopus 로고
    • Initiation of P22 procapsid assembly in vivo
    • 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
  • 4
    • 0024452966 scopus 로고
    • DNA packaging in dsDNA bacteriophages
    • Black, L. W. (1989). DNA packaging in dsDNA bacteriophages. Annu. Rev. Microbiol. 43, 267-292.
    • (1989) Annu. Rev. Microbiol. , vol.43 , pp. 267-292
    • Black, L.W.1
  • 5
    • 0015369489 scopus 로고
    • Genetics of bacteriophage P22. II. Gene order and gene function
    • Botstein, D., Chan, R. K., and Waddell, C. H. (1972). Genetics of bacteriophage P22. II. Gene order and gene function. Virology 49, 268-282.
    • (1972) Virology , vol.49 , pp. 268-282
    • Botstein, D.1    Chan, R.K.2    Waddell, C.H.3
  • 6
    • 0015841378 scopus 로고
    • Mechanism of head assembly and DNA encapsulation in Salmonella phage P22. I. Genes, proteins, structures and DNA maturation
    • 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
  • 7
    • 0021637494 scopus 로고
    • DNA injection proteins are targets of acridine-sensitized photoinactivation of bacteriophage P22
    • Bryant, J. L., Jr., and King, J. (1984). DNA injection proteins are targets of acridine-sensitized photoinactivation of bacteriophage P22. J. Mol. Biol. 180, 837-863.
    • (1984) J. Mol. Biol. , vol.180 , pp. 837-863
    • Bryant J.L., Jr.1    King, J.2
  • 8
    • 0025899372 scopus 로고
    • Fine structure genetic and physical map of the gene 3 to 10 regions of the bacteriophage P22 chromosome
    • Casjens, S., Eppler, K., Sampson, L., Parr, R., and Wyckhoff, E. (1991). Fine structure genetic and physical map of the gene 3 to 10 regions of the bacteriophage P22 chromosome. Genetics 127, 637-647.
    • (1991) Genetics , vol.127 , pp. 637-647
    • Casjens, S.1    Eppler, K.2    Sampson, L.3    Parr, R.4    Wyckhoff, E.5
  • 9
    • 0002107186 scopus 로고
    • Control mechanisms in dsDNA bacteriophage assembly
    • (R Calendar, Ed.), Plenum, New York
    • Casjens, S., and Hendrix, R. (1988). Control mechanisms in dsDNA bacteriophage assembly. In "The Bacteriophages" (R Calendar, Ed.), Vol. 1, pp. 15-91. Plenum, New York.
    • (1988) The Bacteriophages , vol.1 , pp. 15-91
    • Casjens, S.1    Hendrix, R.2
  • 10
    • 0016370643 scopus 로고
    • P22 morphogenesis I: Catalytic scaffolding protein in capsid assembly
    • Casjens, S., and King, J. (1974). P22 morphogenesis I: Catalytic scaffolding protein in capsid assembly. J. Supramol. Struct. 2, 202-224.
    • (1974) J. Supramol. Struct. , vol.2 , pp. 202-224
    • Casjens, S.1    King, J.2
  • 11
    • 0028099585 scopus 로고
    • Stabilizing and destabilizing effects of placing β-branched amino acids in protein α-helices
    • Cornish, V. W., Kaplan, M. I., Veenstra, D. L., Kollman, P. A., and Schultz, P. G. (1994). Stabilizing and destabilizing effects of placing β-branched amino acids in protein α-helices. Biochemistry 33, 12022-12031.
    • (1994) Biochemistry , vol.33 , pp. 12022-12031
    • Cornish, V.W.1    Kaplan, M.I.2    Veenstra, D.L.3    Kollman, P.A.4    Schultz, P.G.5
  • 12
    • 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
    • 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
  • 13
    • 0017892996 scopus 로고
    • Adenovirus type 2 assembly analysed by reversible cross-linking of labile intermediates
    • D'Halluin, J-C. M., Martin, G. R., Torpier, G., and Boulanger, P. (1978). Adenovirus type 2 assembly analysed by reversible cross-linking of labile intermediates. J. Virol. 26, 357-363.
    • (1978) J. Virol. , vol.26 , pp. 357-363
    • D'Halluin, J.-C.M.1    Martin, G.R.2    Torpier, G.3    Boulanger, P.4
  • 14
    • 0018932980 scopus 로고
    • DNA packaging by the double-stranded DNA bacteriophages
    • Earnshaw, W., and Casjens, S. (1980). DNA packaging by the double-stranded DNA bacteriophages. Cell 21, 319-331.
    • (1980) Cell , vol.21 , pp. 319-331
    • Earnshaw, W.1    Casjens, S.2
  • 15
    • 0018232414 scopus 로고
    • Structure of phage P22 coat protein aggregates formed in the absence of the scaffolding protein
    • 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
  • 17
    • 0025770720 scopus 로고
    • Nucleotide sequence of the bacteriophage P22 genes required for DNA packaging
    • Eppler, K., Wyckhoff, E., Goates, J., Parr, R., and Casjens, S. (1991). Nucleotide sequence of the bacteriophage P22 genes required for DNA packaging. Virology 183, 519-538.
    • (1991) Virology , vol.183 , pp. 519-538
    • Eppler, K.1    Wyckhoff, E.2    Goates, J.3    Parr, R.4    Casjens, S.5
  • 18
    • 0019458559 scopus 로고
    • Purification of the coat and scaffolding proteins from procapsids of bacteriophage P22
    • 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
  • 19
    • 0020483095 scopus 로고
    • Assembly in vitro of bacteriophage P22 procapsids from purified coat and scaffolding subunits
    • 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
  • 20
    • 0027320418 scopus 로고
    • Conformational transformations in the protein lattice of phage P22 procapsids
    • Galisteo, M. L., and King, J. (1993). Conformational transformations in the protein lattice of phage P22 procapsids. Biophys. J. 65, 227-235.
    • (1993) Biophys. J. , vol.65 , pp. 227-235
    • Galisteo, M.L.1    King, J.2
  • 21
    • 0027210999 scopus 로고
    • Temperature-sensitive mutations in the phage P22 coat protein which interfere with polypeptide chain folding
    • Gordon, C. L., and King, J. (1993). Temperature-sensitive mutations in the phage P22 coat protein which interfere with polypeptide chain folding. J. Biol. Chem. 268, 9358-9368.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9358-9368
    • Gordon, C.L.1    King, J.2
  • 22
    • 0028040190 scopus 로고
    • Genetic properties of temperature-sensitive folding mutants of the coat protein of phage P22
    • Gordon, C. L., and King, J. (1994). Genetic properties of temperature-sensitive folding mutants of the coat protein of phage P22. Genetics 136, 427-438.
    • (1994) Genetics , vol.136 , pp. 427-438
    • Gordon, C.L.1    King, J.2
  • 23
    • 0028130527 scopus 로고
    • Binding of scaffolding subunits within the P22 procapsid lattice
    • 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
  • 24
    • 0025923286 scopus 로고
    • Regulation of the phage Φ29 prohead shape and size by the portal vertex
    • Guo, P., Erickson, S, Xu, W., Olson, N., Baker, T. S., and Anderson, D. (1991). Regulation of the 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
  • 25
    • 0023883586 scopus 로고
    • Formation of aggregates from a thermolabile in vivo folding intermediate in P22 tailspike maturation
    • Haase-Pettingell, C., and King, J. (1988). Formation of aggregates from a thermolabile in vivo folding intermediate in P22 tailspike maturation. J. Biol. Chem. 263, 4977-4983.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4977-4983
    • Haase-Pettingell, C.1    King, J.2
  • 26
    • 0003025772 scopus 로고
    • DNA injection apparatus of phage P22
    • Hartweig, E., Bazinet, C., and King, J. (1986). DNA injection apparatus of phage P22. Biophys. J. 49, 24-26.
    • (1986) Biophys. J. , vol.49 , pp. 24-26
    • Hartweig, E.1    Bazinet, C.2    King, J.3
  • 27
    • 0002836341 scopus 로고
    • Shape determination in virus assembly: The bacteriophage example
    • (S. Casjens, Ed.), Jones and Bartlett, Boston
    • Hendrix, R. W. (1985). Shape determination in virus assembly: The bacteriophage example. In "Virus Structure and Assembly" (S. Casjens, Ed.), pp. 169-203. Jones and Bartlett, Boston.
    • (1985) Virus Structure and Assembly , pp. 169-203
    • Hendrix, R.W.1
  • 28
    • 0016753519 scopus 로고
    • Bacteriophage P22 virion protein which performs an essential early function. I. Analysis of 16-ts mutants
    • Hoffman, B., and Levine, M. (1975a). Bacteriophage P22 virion protein which performs an essential early function. I. Analysis of 16-ts mutants. J. Virol. 16, 1536-1546.
    • (1975) J. Virol. , vol.16 , pp. 1536-1546
    • Hoffman, B.1    Levine, M.2
  • 29
    • 0016809125 scopus 로고
    • Bacteriophage P22 virion protein which performs an essential early function. II. Characterization of the gene 16 function
    • Hoffman, B., and Levine, M. (1975b). Bacteriophage P22 virion protein which performs an essential early function. II. Characterization of the gene 16 function. J. Virol. 16, 1547-1559.
    • (1975) J. Virol. , vol.16 , pp. 1547-1559
    • Hoffman, B.1    Levine, M.2
  • 30
    • 0015801657 scopus 로고
    • A genetic method for determining the order of events in a biological pathway
    • Jarvik, J., and Botstein, D. (1973). A genetic method for determining the order of events in a biological pathway. Proc. Natl. Acad. Sci. USA 70, 2046-2050.
    • (1973) Proc. Natl. Acad. Sci. USA , vol.70 , pp. 2046-2050
    • Jarvik, J.1    Botstein, D.2
  • 31
    • 0009404164 scopus 로고
    • Conditional-lethal mutations that suppress genetic defects in morphogenesis by altering structural proteins
    • Jarvik, J., and Botstein, D. (1975). Conditional-lethal mutations that suppress genetic defects in morphogenesis by altering structural proteins. Proc. Natl. Acad. Sci. USA 72, 2738-2742.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 2738-2742
    • Jarvik, J.1    Botstein, D.2
  • 32
    • 0025297775 scopus 로고
    • Form determination of the heads of bacteriophages
    • 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
  • 33
    • 0023690367 scopus 로고
    • Length and shape variants of the bacteriophage T4 head: Mutations in the scaffolding core genes 68 and 22
    • 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
  • 34
    • 0002608842 scopus 로고
    • The procapsid to capsid transition in double-stranded DNA bacteriophages
    • (W. Chiu, R. Burnett, and R. Garcea, Eds.), Oxford Univ. Press, New York
    • King, J., and Chiu, W. (1995). The procapsid to capsid transition in double-stranded DNA bacteriophages. In "Structural Biology of Viruses" (W. Chiu, R. Burnett, and R. Garcea, Eds.), Oxford Univ. Press, New York.
    • (1995) Structural Biology of Viruses
    • King, J.1    Chiu, W.2
  • 35
    • 0019118785 scopus 로고
    • Scaffolding proteins and the genetic control of virus shell assembly
    • 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
  • 36
    • 0015897898 scopus 로고
    • Mechanism of head assembly and DNA encapsulation in Salmonella phage P22 II. Morphogenetic pathway
    • King, J., Lenk, E. V., and Botstein, D. (1973). Mechanism of head assembly and DNA encapsulation in Salmonella phage P22 II. Morphogenetic pathway. J. Mol. Biol. 80, 697-731.
    • (1973) J. Mol. Biol. , vol.80 , pp. 697-731
    • King, J.1    Lenk, E.V.2    Botstein, D.3
  • 37
    • 0021033446 scopus 로고
    • Early intermediates in bacteriophage lambda prohead assembly. II. Identification of biologically active intermediates
    • 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
  • 38
    • 0014944824 scopus 로고
    • Form-determining function of the genes required for the assembly of the head of bacteriophage T4
    • Laemmli, U. K., Molbert, E., Showe, M., and Kellenberger, E. (1970). Form-determining function of the genes required for the assembly of the head of bacteriophage T4. J. Mol. Biol. 49, 99-113.
    • (1970) J. Mol. Biol. , vol.49 , pp. 99-113
    • Laemmli, U.K.1    Molbert, E.2    Showe, M.3    Kellenberger, E.4
  • 39
    • 0023811818 scopus 로고
    • Primate cytomegalovirus assembly: Evidence that DNA packaging occurs subsequent to B capsid assembly
    • Lee, J. Y., Irmiere, A., and Gibson, W. (1988). Primate cytomegalovirus assembly: Evidence that DNA packaging occurs subsequent to B capsid assembly. Virology 167, 87-96.
    • (1988) Virology , vol.167 , pp. 87-96
    • Lee, J.Y.1    Irmiere, A.2    Gibson, W.3
  • 40
  • 41
    • 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. (1995). 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, 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
  • 42
    • 0025614822 scopus 로고
    • A proposed structure of bacteriophage T4 gene product 22 - A major prohead scaffolding core protein
    • Mesyanzhinov, V. V., Sobolev, B. N., Marusich, E. I., Prilipov, A. G., 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    Prilipov, A.G.4    Efimov, V.P.5
  • 43
    • 0018748111 scopus 로고
    • Early intermediates in bacteriophage lambda prohead assembly
    • Murialdo, H. (1979). Early intermediates in bacteriophage lambda prohead assembly. Virology 96, 341-367.
    • (1979) Virology , vol.96 , pp. 341-367
    • Murialdo, H.1
  • 44
    • 0018133425 scopus 로고
    • Head morphogenesis of complex double-stranded deoxyribonucleic acid bacteriophages
    • Murialdo, H., and Becker, A. (1978a). 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
  • 45
    • 0018121711 scopus 로고
    • A genetic analysis of bacteriophage lambda prohead assembly in vitro
    • Murialdo, H., and Becker, A. (1978b). A genetic analysis of bacteriophage lambda prohead assembly in vitro. J. Mol. Biol. 125, 57-74.
    • (1978) J. Mol. Biol. , vol.125 , pp. 57-74
    • Murialdo, H.1    Becker, A.2
  • 46
    • 0026098298 scopus 로고
    • Structure of the herpes simplex virus capsid: Effects of extraction with guanidine hydrochloride and partial reconstitution of extracted capsids
    • Newcomb, W. W., and Brown, J. C. (1991). Structure of the herpes simplex virus capsid: Effects of extraction with guanidine hydrochloride and partial reconstitution of extracted capsids. J. Virol. 65, 613-620.
    • (1991) J. Virol. , vol.65 , pp. 613-620
    • Newcomb, W.W.1    Brown, J.C.2
  • 47
    • 0028266837 scopus 로고
    • Diverse essential functions revealed by complementing yeast calmodulin mutants
    • Ohya, Y., and Botstein, D. (1994). Diverse essential functions revealed by complementing yeast calmodulin mutants. Science 263, 963-966.
    • (1994) Science , vol.263 , pp. 963-966
    • Ohya, Y.1    Botstein, D.2
  • 48
    • 0018750052 scopus 로고
    • Encapsulation of phage P22 DNA in vitro
    • Poteete, A. R., Jarvik, V., and Botstein, D. (1979). Encapsulation of phage P22 DNA in vitro. Virology 95, 550-564.
    • (1979) Virology , vol.95 , pp. 550-564
    • Poteete, A.R.1    Jarvik, V.2    Botstein, D.3
  • 49
    • 0027278758 scopus 로고
    • Three-dimensional structure transition from precursor to mature capsid in a bacterial virus
    • Prasad, B. V. V., Prevelige, P. E., Marietta, E., Chen, R. O., Thomas, D., King, J., and Chiu, W. (1993). Three-dimensional structure transition from precursor to mature capsid 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    Chiu, W.7
  • 50
    • 0028048246 scopus 로고
    • The herpes simplex virus gene UL26 proteinase in the presence of the UL 26.5 gene product promotes the formation of scaffold-like structures
    • Preston, V. G., Al-Kobaisi, M. F., McDougall, I. M., and Rixon, F. J.(1994). The herpes simplex virus gene UL26 proteinase in the presence of the UL 26.5 gene product promotes the formation of scaffold-like structures. J. Gen. Virol. 75, 2355-2366.
    • (1994) J. Gen. Virol. , vol.75 , pp. 2355-2366
    • Preston, V.G.1    Al-Kobaisi, M.F.2    McDougall, I.M.3    Rixon, F.J.4
  • 51
    • 0020678189 scopus 로고
    • Identification and characterization of a herpes simplex virus gene product required for encapsidation of virus DNA
    • Preston, V. G., Coates, J. A., and Rixon, F. J. (1983). Identification and characterization of a herpes simplex virus gene product required for encapsidation of virus DNA. J. Virol. 45, 1056-1064.
    • (1983) J. Virol. , vol.45 , pp. 1056-1064
    • Preston, V.G.1    Coates, J.A.2    Rixon, F.J.3
  • 52
    • 0027232759 scopus 로고
    • Nucleation and growth phases in the polymerization of coat and scaffolding subunits into icosahedral procapsid shells
    • Prevelige, P. E., Jr., 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.E., Jr.1    Thomas, D.2    King, J.3
  • 53
    • 0023696277 scopus 로고
    • Scaffolding protein regulates the polymerization of P22 coat subunits into icosahedral shells in vitro
    • Prevelige, P., Thomas, D., and King, J. (1988). Scaffolding protein regulates the polymerization of P22 coat 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
  • 54
    • 0016608755 scopus 로고
    • The role of gene Nu3 in bacteriophage lambda head morphogenesis
    • 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
  • 55
    • 0023986450 scopus 로고
    • Characterization of intranuclear capsids made by ts morphogenetic mutants of HSV-1
    • Sherman, G., and Bachenheimer, S. L. (1988). Characterization of intranuclear capsids made by ts morphogenetic mutants of HSV-1. Virology 163, 471-480.
    • (1988) Virology , vol.163 , pp. 471-480
    • Sherman, G.1    Bachenheimer, S.L.2
  • 56
    • 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. (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
  • 57
    • 0025726316 scopus 로고
    • A pilot protein participates in the initiation of P22 procapsid assembly
    • Thomas, D., and Prevelige, P. (1991). A pilot protein participates in the initiation of P22 procapsid assembly. Virology 182, 673-681.
    • (1991) Virology , vol.182 , pp. 673-681
    • Thomas, D.1    Prevelige, P.2
  • 58
    • 0029019922 scopus 로고
    • Assembly of the herpes simplex virus capsid: Requirement for the carboxyl-terminal twenty-five amino acids of the protein encoded by the UL26 and UL26.5 genes
    • Thomsen, D. R., Newcomb, W. W., Brown, J. C., and Homa, F. L. (1995). Assembly of the herpes simplex virus capsid: Requirement for the carboxyl-terminal twenty-five amino acids of the protein encoded by the UL26 and UL26.5 genes. J. Virol. 69, 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
  • 59
    • 0028345731 scopus 로고
    • Assembly of herpes simplex virus (HSV) intermediate capsids in insect cells infected with recombinant baculoviruses expressing HSV capsid proteins
    • 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
  • 60
    • 0021336823 scopus 로고
    • Formation of the prohead core of bacteriophage T4 in vivo
    • 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
  • 61
    • 0018184953 scopus 로고
    • Assembly of bacteriophage T4 head-related structures. II. In vitro assembly of prehead-like structures
    • van Driel, R., and Couture, E. (1978a). 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
  • 62
    • 0018276730 scopus 로고
    • Assembly of the scaffolding core of bacteriophage T4 preheads
    • van Driel, R., and Couture, E. (1978b). 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
  • 63
    • 0018412538 scopus 로고
    • Characterization of amber and ochre suppressors in Salmonella typhimurium
    • Winston, F., Botstein, D., and Miller, J. H. (1979). Characterization of amber and ochre suppressors in Salmonella typhimurium. J. Bacteriol. 137, 433-439.
    • (1979) J. Bacteriol. , vol.137 , pp. 433-439
    • Winston, F.1    Botstein, D.2    Miller, J.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.