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Volumn 72, Issue 12, 1998, Pages 9924-9933

Vaccinia virus induces Ca2+-independent cell-matrix adhesion during the motile phase of infection

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; COLLAGEN; CYCLOHEXIMIDE; CYTARABINE; EDETIC ACID; EGTAZIC ACID; FIBRONECTIN; HEPARIN; KISTRIN; LAMININ; TRYPSIN; VITRONECTIN;

EID: 0031775224     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.72.12.9924-9933.1998     Document Type: Article
Times cited : (18)

References (58)
  • 1
    • 0026646637 scopus 로고
    • A soluble receptor for interleukin-1β encoded by vaccinia virus: A novel mechanism of virus modulation of the host response to infection
    • Alcamí, A., and G. L. Smith. 1992. A soluble receptor for interleukin-1β encoded by vaccinia virus: a novel mechanism of virus modulation of the host response to infection. Cell 71:153-167.
    • (1992) Cell , vol.71 , pp. 153-167
    • Alcamí, A.1    Smith, G.L.2
  • 2
    • 0018143346 scopus 로고
    • Studies on the mechanisms of vaccinia virus cytopathic effects. II. Early cell rounding is associated with virus polypeptide synthesis
    • Bablanian, R., B. Baxt, J. A. Sonnabend, and M. Esteban. 1978. Studies on the mechanisms of vaccinia virus cytopathic effects. II. Early cell rounding is associated with virus polypeptide synthesis. J. Gen. Virol. 39:403-413.
    • (1978) J. Gen. Virol. , vol.39 , pp. 403-413
    • Bablanian, R.1    Baxt, B.2    Sonnabend, J.A.3    Esteban, M.4
  • 3
    • 0019501236 scopus 로고
    • Inhibition of protein synthesis by vaccinia virus. IV. The role of low-molecular-weight viral RNA in the inhibition of protein synthesis
    • Bablanian, R., G. Coppola, S. Scribani, and M. Esteban. 1981. Inhibition of protein synthesis by vaccinia virus. IV. The role of low-molecular-weight viral RNA in the inhibition of protein synthesis. Virology 112:13-24.
    • (1981) Virology , vol.112 , pp. 13-24
    • Bablanian, R.1    Coppola, G.2    Scribani, S.3    Esteban, M.4
  • 4
    • 0026039370 scopus 로고
    • Extracellular vaccinia virus formation and cell-to-cell virus transmission are prevented by deletion of the gene encoding the 37,000-dalton outer envelope protein
    • Blasco, R., and B. Moss. 1991. Extracellular vaccinia virus formation and cell-to-cell virus transmission are prevented by deletion of the gene encoding the 37,000-dalton outer envelope protein. J. Virol. 65:5910-5920.
    • (1991) J. Virol. , vol.65 , pp. 5910-5920
    • Blasco, R.1    Moss, B.2
  • 5
    • 0026625607 scopus 로고
    • Role of cell-associated enveloped vaccinia virus in cell-to-cell spread
    • Blasco, R., and B. Moss. 1992. Role of cell-associated enveloped vaccinia virus in cell-to-cell spread. J. Virol. 66:4170-4179.
    • (1992) J. Virol. , vol.66 , pp. 4170-4179
    • Blasco, R.1    Moss, B.2
  • 6
    • 0022977603 scopus 로고
    • Integrin (the CSAT antigen): Functionality requires oligomeric integrity
    • Buck, C. A., E. Shea, K. Duggan, and A. F. Horwitz. 1986. Integrin (the CSAT antigen): functionality requires oligomeric integrity. J. Cell Biol. 103: 2421-2428.
    • (1986) J. Cell Biol. , vol.103 , pp. 2421-2428
    • Buck, C.A.1    Shea, E.2    Duggan, K.3    Horwitz, A.F.4
  • 7
    • 0026669346 scopus 로고
    • An ovarian tumor marker with homology to vaccinia virus contains an IgV-like region and multiple transmembrane domains
    • Campbell, I. G., P. S. Freemont, W. Foulkes, and J. Trowsdale. 1992. An ovarian tumor marker with homology to vaccinia virus contains an IgV-like region and multiple transmembrane domains. Cancer Res. 52:5416-5420.
    • (1992) Cancer Res. , vol.52 , pp. 5416-5420
    • Campbell, I.G.1    Freemont, P.S.2    Foulkes, W.3    Trowsdale, J.4
  • 8
    • 0020049591 scopus 로고
    • Modification of membrane permeability in vaccinia virus-infected cells
    • Carrasco, L., and M. Esteban. 1982. Modification of membrane permeability in vaccinia virus-infected cells. Virology 117:62-69.
    • (1982) Virology , vol.117 , pp. 62-69
    • Carrasco, L.1    Esteban, M.2
  • 9
    • 0023601045 scopus 로고
    • An Arg-Gly-Asp-directed receptor on the surface of human melanoma cells exists in a divalent cation-dependent functional complex with the disialoganglioside GD2
    • Cheresh, D. A., R. Pytela, M. D. Pierschbacher, F. G. Klier, E. Ruoslahti, and R. A. Reisfeld. 1987. An Arg-Gly-Asp-directed receptor on the surface of human melanoma cells exists in a divalent cation-dependent functional complex with the disialoganglioside GD2. J. Cell Biol. 105:1163-1173.
    • (1987) J. Cell Biol. , vol.105 , pp. 1163-1173
    • Cheresh, D.A.1    Pytela, R.2    Pierschbacher, M.D.3    Klier, F.G.4    Ruoslahti, E.5    Reisfeld, R.A.6
  • 10
    • 0028918040 scopus 로고
    • Actin-based bacterial motility
    • Cossart, P. 1995. Actin-based bacterial motility. Curr. Opin. Cell. Biol. 7:94-101.
    • (1995) Curr. Opin. Cell. Biol. , vol.7 , pp. 94-101
    • Cossart, P.1
  • 11
    • 0028112027 scopus 로고
    • The actin-based motility of the facultative intracellular pathogen Listeria monocytogenes
    • Cossart, P., and C. Kocks. 1994. The actin-based motility of the facultative intracellular pathogen Listeria monocytogenes. Mol. Microbiol. 13:395-402.
    • (1994) Mol. Microbiol. , vol.13 , pp. 395-402
    • Cossart, P.1    Kocks, C.2
  • 12
    • 0028866712 scopus 로고
    • Actin-based motility of vaccinia virus
    • Cudmore, S., P. Cossart, G. Griffiths, and M. Way. 1995. Actin-based motility of vaccinia virus. Nature 378:636-638.
    • (1995) Nature , vol.378 , pp. 636-638
    • Cudmore, S.1    Cossart, P.2    Griffiths, G.3    Way, M.4
  • 13
    • 0029888696 scopus 로고    scopus 로고
    • Vaccinia virus: A model system for actin-membrane interactions
    • Cudmore, S., I. Reckmann, G. Griffiths, and M. Way 1996. Vaccinia virus: a model system for actin-membrane interactions. J. Cell Sci. 109:1739-1747.
    • (1996) J. Cell Sci. , vol.109 , pp. 1739-1747
    • Cudmore, S.1    Reckmann, I.2    Griffiths, G.3    Way, M.4
  • 14
    • 0026576331 scopus 로고
    • Identification and characterization of an extracellular envelope glycoprotein affecting vaccinia virus egress
    • Duncan, S. A., and G. L. Smith. 1992. Identification and characterization of an extracellular envelope glycoprotein affecting vaccinia virus egress. J. Virol. 66:1610-1621.
    • (1992) J. Virol. , vol.66 , pp. 1610-1621
    • Duncan, S.A.1    Smith, G.L.2
  • 15
    • 0023359506 scopus 로고
    • A major difference between serum and fibronectin in the divalent cation requirement for adhesion and spreading of BHK21 cells
    • Edwards, J. G., R. T. Robson, and G. Campbell. 1987. A major difference between serum and fibronectin in the divalent cation requirement for adhesion and spreading of BHK21 cells. J. Cell Sci. 87:657-665.
    • (1987) J. Cell Sci. , vol.87 , pp. 657-665
    • Edwards, J.G.1    Robson, R.T.2    Campbell, G.3
  • 16
    • 0026655115 scopus 로고
    • A constitutively expressed vaccinia virus gene encodes a 42-kDa glycoprotein related to complement control factors that forms part of the extracellular virus envelope
    • Engelstad, M., S. T. Howard, and G. L. Smith. 1992. A constitutively expressed vaccinia virus gene encodes a 42-kDa glycoprotein related to complement control factors that forms part of the extracellular virus envelope. Virology 188:801-810.
    • (1992) Virology , vol.188 , pp. 801-810
    • Engelstad, M.1    Howard, S.T.2    Smith, G.L.3
  • 17
    • 0030451424 scopus 로고    scopus 로고
    • TGN38-green fluorescent protein hybrid proteins expressed in stably transfected eukaryotic cells provide a tool for the real time, in vivo study of membrane traffic pathways and suggest a possible role for rat TGN38
    • Girotti, M., and G. Banting. 1996. TGN38-green fluorescent protein hybrid proteins expressed in stably transfected eukaryotic cells provide a tool for the real time, in vivo study of membrane traffic pathways and suggest a possible role for rat TGN38. J. Cell Sci. 109:2915-2926.
    • (1996) J. Cell Sci. , vol.109 , pp. 2915-2926
    • Girotti, M.1    Banting, G.2
  • 18
    • 0028142840 scopus 로고
    • Integrin-ligand interactions: A year in review
    • Haas, T. A., and E. F. Plow. 1994. Integrin-ligand interactions: a year in review. Curr. Opin. Cell Biol. 6:652-662.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 652-662
    • Haas, T.A.1    Plow, E.F.2
  • 19
    • 2642647850 scopus 로고    scopus 로고
    • Functional analysis of vaccinia virus B5R protein: Essential role in virus envelopment is independent of a large portion of the extracellular domain
    • Herrera, E., M. del Mar Lorenzo, R. Blasco, and S. N. Isaacs. 1998. Functional analysis of vaccinia virus B5R protein: essential role in virus envelopment is independent of a large portion of the extracellular domain. J. Virol. 72:294-302.
    • (1998) J. Virol. , vol.72 , pp. 294-302
    • Herrera, E.1    Del Mar Lorenzo, M.2    Blasco, R.3    Isaacs, S.N.4
  • 20
    • 0018679460 scopus 로고
    • Interaction of assembled progeny pox viruses with the cellular cytoskeleton
    • Hiller, G., K. Weber, L. Schneider, C. Parajsz, and C. Jungwirth. 1979. Interaction of assembled progeny pox viruses with the cellular cytoskeleton. Virology 98:142-153.
    • (1979) Virology , vol.98 , pp. 142-153
    • Hiller, G.1    Weber, K.2    Schneider, L.3    Parajsz, C.4    Jungwirth, C.5
  • 21
    • 0022495556 scopus 로고
    • Localization and fine structure of a vaccinia virus gene encoding an envelope antigen
    • Hirt, P., G. Hiller, and R. Wittek. 1986. Localization and fine structure of a vaccinia virus gene encoding an envelope antigen. J. Virol. 58:757-764.
    • (1986) J. Virol. , vol.58 , pp. 757-764
    • Hirt, P.1    Hiller, G.2    Wittek, R.3
  • 22
    • 0022342663 scopus 로고
    • The cell substrate attachment (CSAT) antigen has properties of a receptor for laminin and fibronectin
    • Horwitz, A. F., K. Duggan, R. Greggs, C. Decker, and C. Buck. 1985. The cell substrate attachment (CSAT) antigen has properties of a receptor for laminin and fibronectin. J. Cell Biol. 101:2134-2144.
    • (1985) J. Cell Biol. , vol.101 , pp. 2134-2144
    • Horwitz, A.F.1    Duggan, K.2    Greggs, R.3    Decker, C.4    Buck, C.5
  • 23
    • 0004043397 scopus 로고
    • Springer-Verlag, New York, N.Y.
    • Hynes, R. O. 1990. Fibronectin. Springer-Verlag, New York, N.Y.
    • (1990) Fibronectin
    • Hynes, R.O.1
  • 24
    • 0023666065 scopus 로고
    • Integrins: A family of cell surface receptors
    • Hynes, R. O. 1987. Integrins: a family of cell surface receptors. Cell 48:549-554.
    • (1987) Cell , vol.48 , pp. 549-554
    • Hynes, R.O.1
  • 25
    • 0026454214 scopus 로고
    • Characterization of a vaccinia virus-encoded 42-kilodalton class I membrane glycoprotein component of the extracellular virus envelope
    • Isaacs, S. N., E. J. Wolffe, L. G. Payne, and B. Moss. 1992. Characterization of a vaccinia virus-encoded 42-kilodalton class I membrane glycoprotein component of the extracellular virus envelope. J. Virol. 66:7217-7224.
    • (1992) J. Virol. , vol.66 , pp. 7217-7224
    • Isaacs, S.N.1    Wolffe, E.J.2    Payne, L.G.3    Moss, B.4
  • 26
    • 0029867915 scopus 로고    scopus 로고
    • Ligand occupancy of the αVβ3 integrin is necessary for muscle cells to migrate in response to insulin-like growth factor I
    • Jones, J. I., T. Prevette, A. Gockerman, and D. R. Clemmons. 1996. Ligand occupancy of the αVβ3 integrin is necessary for muscle cells to migrate in response to insulin-like growth factor I. Proc. Natl. Acad. Sci. USA 93:2482-2487.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2482-2487
    • Jones, J.I.1    Prevette, T.2    Gockerman, A.3    Clemmons, D.R.4
  • 28
    • 0026327658 scopus 로고
    • Avian neural crest cell attachment to laminin: Involvement of divalent cation dependent and independent integrins
    • Lallier, T., and M. Bronner-Fraser. 1991. Avian neural crest cell attachment to laminin: involvement of divalent cation dependent and independent integrins. Development 113:1069-1084.
    • (1991) Development , vol.113 , pp. 1069-1084
    • Lallier, T.1    Bronner-Fraser, M.2
  • 29
    • 0026482459 scopus 로고
    • Cranial and trunk neural crest cells use different mechanisms for attachment to extracellular matrices
    • Lallier, T., G. Leblanc, K. B. Artinger, and M. Bronner-Fraser. 1992. Cranial and trunk neural crest cells use different mechanisms for attachment to extracellular matrices. Development 116:531-541.
    • (1992) Development , vol.116 , pp. 531-541
    • Lallier, T.1    Leblanc, G.2    Artinger, K.B.3    Bronner-Fraser, M.4
  • 30
    • 0026764576 scopus 로고
    • Requirement of the integrin β3 subunit for carcinoma cell spreading or migration on vitronectin and fibronectin
    • Leavesley, D. I., G. D. Ferguson, E. A. Wayner, and D. A. Cheresh. 1992. Requirement of the integrin β3 subunit for carcinoma cell spreading or migration on vitronectin and fibronectin. J. Cell Biol. 117:1101-1107.
    • (1992) J. Cell Biol. , vol.117 , pp. 1101-1107
    • Leavesley, D.I.1    Ferguson, G.D.2    Wayner, E.A.3    Cheresh, D.A.4
  • 33
    • 0031911650 scopus 로고    scopus 로고
    • The extracellular domain of vaccinia virus protein B5R affects plaque formation, EEV release, and intracellular actin tail formation
    • Mathew, E., C. M. Sanderson, M. Hollinshead, and G. L. Smith. 1998. The extracellular domain of vaccinia virus protein B5R affects plaque formation, EEV release, and intracellular actin tail formation. J. Virol. 72:2429-2438.
    • (1998) J. Virol. , vol.72 , pp. 2429-2438
    • Mathew, E.1    Sanderson, C.M.2    Hollinshead, M.3    Smith, G.L.4
  • 34
    • 0029655645 scopus 로고    scopus 로고
    • Vaccinia virus glycoprotein A34R is required for infectivity of extracellular enveloped virus
    • McIntosh, A. A. G., and G. L. Smith. 1996. Vaccinia virus glycoprotein A34R is required for infectivity of extracellular enveloped virus. J. Virol. 70:272-281.
    • (1996) J. Virol. , vol.70 , pp. 272-281
    • McIntosh, A.A.G.1    Smith, G.L.2
  • 35
    • 0000557448 scopus 로고    scopus 로고
    • Poxviridae: The viruses and their replication
    • B. N. Fields, D. M. Knipe, and P. M. Howley (ed.). Lippincott Raven Press, New York, N.Y.
    • Moss, B. 1996. Poxviridae: the viruses and their replication, p. 2637-2671. In B. N. Fields, D. M. Knipe, and P. M. Howley (ed.), Fields virology, vol. 2. Lippincott Raven Press, New York, N.Y.
    • (1996) Fields Virology , vol.2 , pp. 2637-2671
    • Moss, B.1
  • 36
    • 0025312949 scopus 로고
    • Regulation of vaccinia virus transcription
    • Moss, B. 1990. Regulation of vaccinia virus transcription. Annu. Rev. Biochem. 59:661-668.
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 661-668
    • Moss, B.1
  • 37
    • 0028802984 scopus 로고
    • The vaccinia virus A38L gene product is a 33-kDa integral membrane glycoprotein
    • Parkinson, J. E., C. M. Sanderson, and G. L. Smith. 1995. The vaccinia virus A38L gene product is a 33-kDa integral membrane glycoprotein. Virology 214:177-188.
    • (1995) Virology , vol.214 , pp. 177-188
    • Parkinson, J.E.1    Sanderson, C.M.2    Smith, G.L.3
  • 38
    • 0027980628 scopus 로고
    • r 43-50K protein on the surface of extracellular enveloped virus
    • r 43-50K protein on the surface of extracellular enveloped virus. Virology 204:376-390.
    • (1994) Virology , vol.204 , pp. 376-390
    • Parkinson, J.E.1    Smith, G.L.2
  • 39
    • 0022647829 scopus 로고
    • Isolation of cowpox virus A-type inclusions and characterization of their major protein component
    • Patel, D. D., D. J. Pickup, and W. K. Joklik. 1986. Isolation of cowpox virus A-type inclusions and characterization of their major protein component. Virology 149:174-189.
    • (1986) Virology , vol.149 , pp. 174-189
    • Patel, D.D.1    Pickup, D.J.2    Joklik, W.K.3
  • 40
    • 0017159846 scopus 로고
    • Presence of haemagglutinin in the envelope of extracellular vaccinia virus particles
    • Payne, L. G., and E. Norrby. 1976. Presence of haemagglutinin in the envelope of extracellular vaccinia virus particles. J. Gen. Virol. 32:63-72.
    • (1976) J. Gen. Virol. , vol.32 , pp. 63-72
    • Payne, L.G.1    Norrby, E.2
  • 41
    • 0025001946 scopus 로고
    • IPTG-dependent vaccinia virus: Identification of a virus protein enabling virion envelopment by Golgi membrane and egress
    • Rodriguez, J. F., and G. L. Smith. 1990. IPTG-dependent vaccinia virus: identification of a virus protein enabling virion envelopment by Golgi membrane and egress. Nucleic Acids Res. 18:5347-5351.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 5347-5351
    • Rodriguez, J.F.1    Smith, G.L.2
  • 42
    • 0029994032 scopus 로고    scopus 로고
    • Extracellular vaccinia virus envelope glycoprotein encoded by the A33R gene
    • Roper, R. L., L. G. Payne, and B. Moss. 1996. Extracellular vaccinia virus envelope glycoprotein encoded by the A33R gene. J. Virol. 70:3753-3762.
    • (1996) J. Virol. , vol.70 , pp. 3753-3762
    • Roper, R.L.1    Payne, L.G.2    Moss, B.3
  • 43
    • 0031958096 scopus 로고    scopus 로고
    • The envelope protein encoded by the A33R gene is required for formation of actin-containing microvilli and efficient cell-to-cell spread of vaccinia virus
    • Roper, R. L., E. J. Wolffe, A. Weisberg, and B. Moss. 1998. The envelope protein encoded by the A33R gene is required for formation of actin-containing microvilli and efficient cell-to-cell spread of vaccinia virus. J. Virol. 72:4192-4204.
    • (1998) J. Virol. , vol.72 , pp. 4192-4204
    • Roper, R.L.1    Wolffe, E.J.2    Weisberg, A.3    Moss, B.4
  • 44
    • 0023637601 scopus 로고
    • New perspectives in cell adhesion: RGD and integrins
    • Ruoslahti, E., and M. Pierschbacher. 1987. New perspectives in cell adhesion: RGD and integrins. Science 238:491-497.
    • (1987) Science , vol.238 , pp. 491-497
    • Ruoslahti, E.1    Pierschbacher, M.2
  • 45
    • 0031806239 scopus 로고    scopus 로고
    • Roles of vaccinia virus EEV-specific proteins in intracellular actin tail formation and low pH-induced cell-cell fusion
    • Sanderson, C. M., F. Frischknecht, M. Way, M. Hollinshead, and G. L. Smith. 1998. Roles of vaccinia virus EEV-specific proteins in intracellular actin tail formation and low pH-induced cell-cell fusion. J. Gen. Virol. 79:1415-1425.
    • (1998) J. Gen. Virol. , vol.79 , pp. 1415-1425
    • Sanderson, C.M.1    Frischknecht, F.2    Way, M.3    Hollinshead, M.4    Smith, G.L.5
  • 47
    • 0031906414 scopus 로고    scopus 로고
    • Virus-induced cell motility
    • Sanderson, C. M., M. Way, and G. L. Smith. 1998. Virus-induced cell motility. J. Virol. 72:1235-1243.
    • (1998) J. Virol. , vol.72 , pp. 1235-1243
    • Sanderson, C.M.1    Way, M.2    Smith, G.L.3
  • 49
    • 0028097957 scopus 로고
    • Assembly of vaccinia virus: The second wrapping cisterna is derived from the trans Golgi network
    • Schmelz, M., B. Sodeik, M. Ericsson, E. J. Wolffe, H. Shida, G. Hiller, and G. Griffiths. 1994. Assembly of vaccinia virus: the second wrapping cisterna is derived from the trans Golgi network. J. Virol. 68:130-147.
    • (1994) J. Virol. , vol.68 , pp. 130-147
    • Schmelz, M.1    Sodeik, B.2    Ericsson, M.3    Wolffe, E.J.4    Shida, H.5    Hiller, G.6    Griffiths, G.7
  • 50
    • 0022625330 scopus 로고
    • Nucleotide sequence of the vaccinia virus hemagglutinin gene
    • Shida, H. 1986. Nucleotide sequence of the vaccinia virus hemagglutinin gene. Virology 150:451-462.
    • (1986) Virology , vol.150 , pp. 451-462
    • Shida, H.1
  • 51
    • 0024230916 scopus 로고
    • The Arg-Gly-Asp binding domain of the vitronectin receptor. Photoaffinity cross-linking implicates amino acid residues 61-203 of the β subunit
    • Smith, J. W., and D. A. Cheresh. 1988. The Arg-Gly-Asp binding domain of the vitronectin receptor. Photoaffinity cross-linking implicates amino acid residues 61-203 of the β subunit. J. Biol. Chem. 263:18726-18731.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18726-18731
    • Smith, J.W.1    Cheresh, D.A.2
  • 52
    • 0027316090 scopus 로고
    • The wily ways of a parasite: Induction of actin assembly by Listeria
    • Tilney, L. G., and M. S. Tilney. 1993. The wily ways of a parasite: induction of actin assembly by Listeria. Trends Microbiol. 1:25-31.
    • (1993) Trends Microbiol. , vol.1 , pp. 25-31
    • Tilney, L.G.1    Tilney, M.S.2
  • 53
    • 0023813318 scopus 로고
    • Purification and characterization of mammalian integrins expressed by a rat neural cell line (PC12): Evidence that they function as alpha/beta heterodimeric receptors for laminin and type II collagen
    • Tomaselli, K. J., C. H. Damskyl, and F. Reichardt. 1988. Purification and characterization of mammalian integrins expressed by a rat neural cell line (PC12): evidence that they function as alpha/beta heterodimeric receptors for laminin and type II collagen. J. Cell Biol. 107:1241-1252.
    • (1988) J. Cell Biol. , vol.107 , pp. 1241-1252
    • Tomaselli, K.J.1    Damskyl, C.H.2    Reichardt, F.3
  • 54
    • 0027530255 scopus 로고
    • Progeny vaccinia viruses and human cytomegalovirus particles utilize early endosomal cisternae for their envelopes
    • Tooze, J., M. Hollinshead, B. Reis, K. Radsak, and H. Kern. 1993. Progeny vaccinia viruses and human cytomegalovirus particles utilize early endosomal cisternae for their envelopes. Eur. J. Cell Biol. 60:163-178.
    • (1993) Eur. J. Cell Biol. , vol.60 , pp. 163-178
    • Tooze, J.1    Hollinshead, M.2    Reis, B.3    Radsak, K.4    Kern, H.5
  • 55
    • 0032560578 scopus 로고    scopus 로고
    • Extracellular enveloped vaccinia virus is resistant to complement because of incorporation of cellular complement control proteins into its envelope
    • Vanderplasschen, A., M. Hollinshead, E. Mathew, R. B. Sim, and G. L. Smith. 1998. Extracellular enveloped vaccinia virus is resistant to complement because of incorporation of cellular complement control proteins into its envelope. Proc. Natl. Acad. Sci. USA 95:7544-7549.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7544-7549
    • Vanderplasschen, A.1    Hollinshead, M.2    Mathew, E.3    Sim, R.B.4    Smith, G.L.5
  • 56
    • 0024117029 scopus 로고
    • Derepression of a novel class of vaccinia virus genes upon DNA replication
    • Vos, J. C., and H. G. Stunnenberg. 1988. Derepression of a novel class of vaccinia virus genes upon DNA replication. EMBO J. 7:3487-3492.
    • (1988) EMBO J. , vol.7 , pp. 3487-3492
    • Vos, J.C.1    Stunnenberg, H.G.2
  • 57
    • 0031000689 scopus 로고    scopus 로고
    • The A34R glycoprotein gene is required for induction of specialized actin-contaming microvilli and efficient cell-to-cell transmission of vaccinia virus
    • Wolffe, E., E. Katz, A. Weisberg, and B. Moss. 1997. The A34R glycoprotein gene is required for induction of specialized actin-contaming microvilli and efficient cell-to-cell transmission of vaccinia virus. J. Virol. 71:3905-3915.
    • (1997) J. Virol. , vol.71 , pp. 3905-3915
    • Wolffe, E.1    Katz, E.2    Weisberg, A.3    Moss, B.4
  • 58
    • 0032565358 scopus 로고    scopus 로고
    • Role for the vaccinia virus A36R outer envelope protein in the formation of virus-lipped actin-containing microvilli and cell-to-cell virus spread
    • Wolffe, E. J., A. S. Weisberg, and B. Moss. 1998. Role for the vaccinia virus A36R outer envelope protein in the formation of virus-lipped actin-containing microvilli and cell-to-cell virus spread. Virology 244:20-26.
    • (1998) Virology , vol.244 , pp. 20-26
    • Wolffe, E.J.1    Weisberg, A.S.2    Moss, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.