메뉴 건너뛰기




Volumn 70, Issue 12, 1996, Pages 8382-8390

Involvement of the endoplasmic reticulum in the assembly and envelopment of African swine fever virus

Author keywords

[No Author keywords available]

Indexed keywords

BREFELDIN A; MEMBRANE PROTEIN; MONENSIN; STRUCTURAL PROTEIN;

EID: 0029861189     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.70.12.8382-8390.1996     Document Type: Article
Times cited : (73)

References (54)
  • 1
    • 0026456551 scopus 로고
    • Morphogenesis of African swine fever virus in monkey kidney cells after reversible inhibition of replication by cycloheximide
    • Arzuza, O., A. Urzainqui, J. R. Diaz-Ruiz, and E. Tabares. 1992. Morphogenesis of African swine fever virus in monkey kidney cells after reversible inhibition of replication by cycloheximide. Arch. Virol. 124:343-354.
    • (1992) Arch. Virol. , vol.124 , pp. 343-354
    • Arzuza, O.1    Urzainqui, A.2    Diaz-Ruiz, J.R.3    Tabares, E.4
  • 2
    • 0026596506 scopus 로고
    • Intracellular transport of rubella virus structural proteins expressed from cloned c-DNA
    • Baron, M. D., T. Ebel, and M. Suomalainen. 1992. Intracellular transport of rubella virus structural proteins expressed from cloned c-DNA. J. Gen. Virol. 73:1073-1086.
    • (1992) J. Gen. Virol. , vol.73 , pp. 1073-1086
    • Baron, M.D.1    Ebel, T.2    Suomalainen, M.3
  • 3
    • 0028241556 scopus 로고
    • African swine fever virus structural protein p72 contains a conformational neutralizing epitope
    • Borca, M. V., P. Irstua, C. Carrillo, C. L. Afonso, T. Burrage, and D. L. Rock. 1994. African swine fever virus structural protein p72 contains a conformational neutralizing epitope. Virology 201:413-418.
    • (1994) Virology , vol.201 , pp. 413-418
    • Borca, M.V.1    Irstua, P.2    Carrillo, C.3    Afonso, C.L.4    Burrage, T.5    Rock, D.L.6
  • 4
    • 0028292227 scopus 로고
    • An African swine fever virus gene with similarity to the T-lymphocyte surface antigen CD2 mediates hemadsorption
    • Borca, M. V., G. F. Kutish, C. L. Afonso, P. Irusta, C. Carrillo, A. Brun, M. Sussman, and D. Rock. 1994. An African swine fever virus gene with similarity to the T-lymphocyte surface antigen CD2 mediates hemadsorption. Virology 199:463-468.
    • (1994) Virology , vol.199 , pp. 463-468
    • Borca, M.V.1    Kutish, G.F.2    Afonso, C.L.3    Irusta, P.4    Carrillo, C.5    Brun, A.6    Sussman, M.7    Rock, D.8
  • 5
    • 0016631494 scopus 로고
    • Cross-linking of components of lactose synthetase with dimethylpimilidate
    • Brew, K., J. L. Shaper, K. W. Olsen, I. P. Trayer, and R. L. Hill. 1975. Cross-linking of components of lactose synthetase with dimethylpimilidate. J. Biol. Chem. 250:1434-1444.
    • (1975) J. Biol. Chem. , vol.250 , pp. 1434-1444
    • Brew, K.1    Shaper, J.L.2    Olsen, K.W.3    Trayer, I.P.4    Hill, R.L.5
  • 6
    • 0026093145 scopus 로고
    • Protein p22 of African swine fever virus: An early structural protein that is incorporated into the membrane of infected cells
    • Camacho, A., and E. Vinuela. 1991. Protein p22 of African swine fever virus: an early structural protein that is incorporated into the membrane of infected cells. Virology 181:251-257.
    • (1991) Virology , vol.181 , pp. 251-257
    • Camacho, A.1    Vinuela, E.2
  • 7
    • 0027161696 scopus 로고
    • Localization of African swine fever virus attachment protein p12 in the virus particle by immunoelectron microscopy
    • Carrascosa, A., I. Saastre, P. Gonzalez, and E. Vinuela. 1993. Localization of African swine fever virus attachment protein p12 in the virus particle by immunoelectron microscopy. Virology 193:460-465.
    • (1993) Virology , vol.193 , pp. 460-465
    • Carrascosa, A.1    Saastre, I.2    Gonzalez, P.3    Vinuela, E.4
  • 8
    • 0021844911 scopus 로고
    • Purification and properties of African swine fever virus
    • Carrascosa, A. L., M. del Val, J. F. Santaren, and E. Vinuela. 1985. Purification and properties of African swine fever virus. J. Virol. 54:337-344.
    • (1985) J. Virol. , vol.54 , pp. 337-344
    • Carrascosa, A.L.1    Del Val, M.2    Santaren, J.F.3    Vinuela, E.4
  • 11
    • 0029417216 scopus 로고
    • The African swine fever virus IAP homolog is a late structural protein
    • Chacon, M. R., F. Almazan, M. L. Nogal, E. Vinuela, and J. F. Rodriguez. 1995. The African swine fever virus IAP homolog is a late structural protein. Virology 214:670-674.
    • (1995) Virology , vol.214 , pp. 670-674
    • Chacon, M.R.1    Almazan, F.2    Nogal, M.L.3    Vinuela, E.4    Rodriguez, J.F.5
  • 12
    • 0026069627 scopus 로고
    • Brefeldin A arrests the maturation and egress of herpes simplex particles during infection
    • Cheung, P., B. W. Banfield, and F. Tufaro. 1991. Brefeldin A arrests the maturation and egress of herpes simplex particles during infection. J. Virol. 65:1893-1904.
    • (1991) J. Virol. , vol.65 , pp. 1893-1904
    • Cheung, P.1    Banfield, B.W.2    Tufaro, F.3
  • 13
    • 0026456803 scopus 로고
    • Expression in vivo and in vitro of the major structural protein (VP73) of African swine fever virus
    • Cistue, C., and E. Tabares. 1992. Expression in vivo and in vitro of the major structural protein (VP73) of African swine fever virus. Arch. Virol. 123:111-124.
    • (1992) Arch. Virol. , vol.123 , pp. 111-124
    • Cistue, C.1    Tabares, E.2
  • 14
    • 0023183656 scopus 로고
    • Glycosylated components induced in African swine fever virus-infected Vero cells
    • Del Val, M., and E. Vinuela. 1987. Glycosylated components induced in African swine fever virus-infected Vero cells. Virus Res. 7:297-308.
    • (1987) Virus Res. , vol.7 , pp. 297-308
    • Del Val, M.1    Vinuela, E.2
  • 15
    • 0028352137 scopus 로고
    • Nucleotide sequence of a 55kbp region from the right end of the genome of a pathogenic African swine fever virus isolate (Malawi LIL20/1)
    • Dixon, L. K., S. R. F. Twigg, S. A. Balis, S. Vydelingum, C. Bristow, J. M. Hammond, and G. L. Smith. 1994. Nucleotide sequence of a 55kbp region from the right end of the genome of a pathogenic African swine fever virus isolate (Malawi LIL20/1). J. Gen. Virol. 75:1655-1684.
    • (1994) J. Gen. Virol. , vol.75 , pp. 1655-1684
    • Dixon, L.K.1    Twigg, S.R.F.2    Balis, S.A.3    Vydelingum, S.4    Bristow, C.5    Hammond, J.M.6    Smith, G.L.7
  • 16
    • 0000233999 scopus 로고
    • Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase
    • Fuerst, T. R., E. G. Niles, W. F. Studier, and B. Moss. 1986. Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase. Proc. Natl. Acad. Sci. USA 83:8122-8126.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 8122-8126
    • Fuerst, T.R.1    Niles, E.G.2    Studier, W.F.3    Moss, B.4
  • 17
    • 0026708727 scopus 로고
    • Role of the host cell nucleus in the replication of African swine fever virus DNA
    • Garcea-Beato, M., L. Salas, E. Vinuela, and J. Salas. 1992. Role of the host cell nucleus in the replication of African swine fever virus DNA. Virology 188:637-649.
    • (1992) Virology , vol.188 , pp. 637-649
    • Garcea-Beato, M.1    Salas, L.2    Vinuela, E.3    Salas, J.4
  • 18
    • 0028106296 scopus 로고
    • Intracellular transport of newly synthesized varicella-zoster virus: Final envelopment by the trans-Golgi network
    • Gershon, A. A., D. L. Sherman, Z. Zhu, C. Gabel, R. T. Ambron, and M. D. Gershon, 1994. Intracellular transport of newly synthesized varicella-zoster virus: final envelopment by the trans-Golgi network. J. Virol. 68:6372-6390.
    • (1994) J. Virol. , vol.68 , pp. 6372-6390
    • Gershon, A.A.1    Sherman, D.L.2    Zhu, Z.3    Gabel, C.4    Ambron, R.T.5    Gershon, M.D.6
  • 19
    • 0017855848 scopus 로고
    • Macromolecular synthesis in cells infected by frog virus 3. VIII. The nucleus is a site of frog virus 3 DNA and RNA replication
    • Goorha, R., G. Murti, A. Granoff, and R. Tirey. 1978. Macromolecular synthesis in cells infected by frog virus 3. VIII. The nucleus is a site of frog virus 3 DNA and RNA replication. Virology 84:32-50.
    • (1978) Virology , vol.84 , pp. 32-50
    • Goorha, R.1    Murti, G.2    Granoff, A.3    Tirey, R.4
  • 20
    • 0026934552 scopus 로고
    • Cell biology of viruses that assemble along the biosynthetic pathway
    • Griffiths, G., and P. Rottier. 1992. Cell biology of viruses that assemble along the biosynthetic pathway. Semin. Cell Biol. 3:367-381.
    • (1992) Semin. Cell Biol. , vol.3 , pp. 367-381
    • Griffiths, G.1    Rottier, P.2
  • 21
    • 0026594934 scopus 로고
    • A ubiquitin-conjugating enzyme encoded by African swine fever virus
    • Hingamp, P. M., J. E. Arnold, R. J. Mayer, and L. K. Dixon. 1992. A ubiquitin-conjugating enzyme encoded by African swine fever virus. EMBO J. 11:361-366.
    • (1992) EMBO J. , vol.11 , pp. 361-366
    • Hingamp, P.M.1    Arnold, J.E.2    Mayer, R.J.3    Dixon, L.K.4
  • 22
    • 0028873461 scopus 로고
    • Characterization of a ubiquitinated protein which is externally located in African swine fever virus
    • Hingamp, P. M., M. L. Leyland, J. Webb, S. Twigger, R. J. Mayer, and L. K. Dixon. 1995. Characterization of a ubiquitinated protein which is externally located in African swine fever virus. J. Virol. 69:1785-1793.
    • (1995) J. Virol. , vol.69 , pp. 1785-1793
    • Hingamp, P.M.1    Leyland, M.L.2    Webb, J.3    Twigger, S.4    Mayer, R.J.5    Dixon, L.K.6
  • 23
    • 0027469910 scopus 로고
    • The rubella virus E2 and E1 spike glycoproteins are targeted to the Golgi complex
    • Hobmann, T. C., L. Woodward, and M. G. Farquar. 1993. The rubella virus E2 and E1 spike glycoproteins are targeted to the Golgi complex. J. Cell Biol. 121:269-281.
    • (1993) J. Cell Biol. , vol.121 , pp. 269-281
    • Hobmann, T.C.1    Woodward, L.2    Farquar, M.G.3
  • 24
    • 0019918329 scopus 로고
    • Monensin inhibits the processing of herpes simplex virus glycoproteins, their transport to the cell surface, and egress of virions from infected cells
    • Johnson, D. C., and P. G. Spear. 1982. Monensin inhibits the processing of herpes simplex virus glycoproteins, their transport to the cell surface, and egress of virions from infected cells. J. Virol. 43:1102-1112.
    • (1982) J. Virol. , vol.43 , pp. 1102-1112
    • Johnson, D.C.1    Spear, P.G.2
  • 25
    • 0022550932 scopus 로고
    • Oligomerization is essential for transport of VSV G protein to the cell surface
    • Kreis, T. E., and H. F. Lodish. 1986. Oligomerization is essential for transport of VSV G protein to the cell surface. Cell 46:929-937.
    • (1986) Cell , vol.46 , pp. 929-937
    • Kreis, T.E.1    Lodish, H.F.2
  • 26
    • 0028069572 scopus 로고
    • Characterization of the budding compartment of mouse hepatitis virus: Evidence that transport from the RER to the Golgi complex requires one vesicular step
    • Krijnse-Locker, J., M. Ericsson, P. J. M. Rottier, and G. Griffiths. 1994. Characterization of the budding compartment of mouse hepatitis virus: evidence that transport from the RER to the Golgi complex requires one vesicular step. J. Cell Biol. 124:55-70.
    • (1994) J. Cell Biol. , vol.124 , pp. 55-70
    • Krijnse-Locker, J.1    Ericsson, M.2    Rottier, P.J.M.3    Griffiths, G.4
  • 27
    • 0024591235 scopus 로고
    • Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin-A
    • Lippincott-Schwartz, J., L. C. Yuan, J. S. Bonifacino, and R. D. Klausner. 1989. Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin-A. Cell 56:801-813.
    • (1989) Cell , vol.56 , pp. 801-813
    • Lippincott-Schwartz, J.1    Yuan, L.C.2    Bonifacino, J.S.3    Klausner, R.D.4
  • 28
    • 0025308438 scopus 로고
    • Mapping and sequence of the gene coding for p72, the major capsid protein of African swine fever virus
    • Lopez-Otin, C., J. M. P. Freue, F. Parra, E. Mendez, and E. Vinuela. 1990. Mapping and sequence of the gene coding for p72, the major capsid protein of African swine fever virus. Virology 175:477-484.
    • (1990) Virology , vol.175 , pp. 477-484
    • Lopez-Otin, C.1    Freue, J.M.P.2    Parra, F.3    Mendez, E.4    Vinuela, E.5
  • 29
    • 0025049127 scopus 로고
    • The E1 glycoprotoin of an avian coronavirus is targeted to the cis-Golgi complex
    • Machamer, C. E., S. A. Mentone, J. K. Rose, and M. G. Farquhar. 1990. The E1 glycoprotoin of an avian coronavirus is targeted to the cis-Golgi complex. Proc. Natl. Acad. Sci. USA 87:6944-6948.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 6944-6948
    • Machamer, C.E.1    Mentone, S.A.2    Rose, J.K.3    Farquhar, M.G.4
  • 30
    • 0030006113 scopus 로고    scopus 로고
    • Cloning, sequence analysis and expression of the major capsid protein of the iridovirus frog three virus
    • Mao, J., N. Thamm, G. A. Gentry, A. Aubertin, and V. G. Chinchar. 1996. Cloning, sequence analysis and expression of the major capsid protein of the iridovirus frog three virus. Virology 216:431-436.
    • (1996) Virology , vol.216 , pp. 431-436
    • Mao, J.1    Thamm, N.2    Gentry, G.A.3    Aubertin, A.4    Chinchar, V.G.5
  • 31
    • 0016834916 scopus 로고
    • Ultrastructural study of African swine fever virus replication in cultures of swine bone marrow cells
    • Moura Nunes, J. F., J. D. Vigario, and A. M. Terrinha. 1975. Ultrastructural study of African swine fever virus replication in cultures of swine bone marrow cells. Arch. Virol. 49:59-66.
    • (1975) Arch. Virol. , vol.49 , pp. 59-66
    • Moura Nunes, J.F.1    Vigario, J.D.2    Terrinha, A.M.3
  • 32
    • 0022286208 scopus 로고
    • An unusual replication strategy of an animal iridovirus
    • Murti, K. G., R. Goorha, and A. Granoff. 1985. An unusual replication strategy of an animal iridovirus. Adv. Virus Res. 30:1-19.
    • (1985) Adv. Virus Res. , vol.30 , pp. 1-19
    • Murti, K.G.1    Goorha, R.2    Granoff, A.3
  • 33
    • 0027264124 scopus 로고
    • An African swine fever virus gene with similarity to the protooncogene bcl-22 and Epstein-Barr virus gene BHRFI
    • Neilan, J. G., Z. Lu, C. L. Afonso, G. F. Kutish, M. D. Sussman, and D. L. Rock. 1993. An African swine fever virus gene with similarity to the protooncogene bcl-22 and Epstein-Barr virus gene BHRFI. J. Virol. 67:4391-4393.
    • (1993) J. Virol. , vol.67 , pp. 4391-4393
    • Neilan, J.G.1    Lu, Z.2    Afonso, C.L.3    Kutish, G.F.4    Sussman, M.D.5    Rock, D.L.6
  • 35
    • 0026542277 scopus 로고
    • Genes homologous to ubiquitin-conjugating proteins and eukaryotic transcription factor S11 in African swine fever virus
    • Rodriguez, J. M., F. Almazan, E. Vinuela, and J. F. Rodriguez. 1992. Genes homologous to ubiquitin-conjugating proteins and eukaryotic transcription factor S11 in African swine fever virus. Virology 186:40-52.
    • (1992) Virology , vol.186 , pp. 40-52
    • Rodriguez, J.M.1    Almazan, F.2    Vinuela, E.3    Rodriguez, J.F.4
  • 36
    • 0027219595 scopus 로고
    • African swine fever virus encodes a CD2 homolog responsible for adhesion of erythrocytes to infected cells
    • Rodriguez, J. M., R. J. Yanez, F. Almazan, E. Vinuela, and J. F. Rodriguez. 1993. African swine fever virus encodes a CD2 homolog responsible for adhesion of erythrocytes to infected cells. J. Virol. 67:5312-5320.
    • (1993) J. Virol. , vol.67 , pp. 5312-5320
    • Rodriguez, J.M.1    Yanez, R.J.2    Almazan, F.3    Vinuela, E.4    Rodriguez, J.F.5
  • 37
    • 0022053407 scopus 로고
    • Monoclonal antibodies specific for African swine fever virus proteins
    • Sanz, A., B. Garcia-Barreno, M. L. Nogal, E. Vinuela, and L. Enjuanes. 1985. Monoclonal antibodies specific for African swine fever virus proteins. J. Virol. 54:199-206.
    • (1985) J. Virol. , vol.54 , pp. 199-206
    • Sanz, A.1    Garcia-Barreno, B.2    Nogal, M.L.3    Vinuela, E.4    Enjuanes, L.5
  • 38
    • 0026934508 scopus 로고
    • Pathways of protein sorting and membrane traffic between the rough endoplasmic reticulum and the Golgi complex
    • Saraste, J., and E. Kuismanen. 1992. Pathways of protein sorting and membrane traffic between the rough endoplasmic reticulum and the Golgi complex. Semin. Cell Biol. 3:343-355.
    • (1992) Semin. Cell Biol. , vol.3 , pp. 343-355
    • Saraste, J.1    Kuismanen, E.2
  • 39
    • 0028097957 scopus 로고
    • Assembly of vaccinia virus: The second wrapping cisterna is derived from the trans-Golgi network
    • Schmelz, M., B. Sodiek, 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    Sodiek, B.2    Ericsson, M.3    Wolffe, E.J.4    Shida, H.5    Hiller, G.6    Griffiths, G.7
  • 40
    • 0027180537 scopus 로고
    • Assembly of vaccinia virus: Role of the intermediate compartments between the endoplasmic reticulum and the Golgi stacks
    • Sodiek, B., R. W. Doms, M. Ericsson, G. Hiller, C. E. Machamer, W. van't Hof, G. van Meer, and G. Griffiths. 1993. Assembly of vaccinia virus: role of the intermediate compartments between the endoplasmic reticulum and the Golgi stacks. J. Cell Biol. 121:521-541.
    • (1993) J. Cell Biol. , vol.121 , pp. 521-541
    • Sodiek, B.1    Doms, R.W.2    Ericsson, M.3    Hiller, G.4    Machamer, C.E.5    Van't Hof, W.6    Van Meer, G.7    Griffiths, G.8
  • 41
    • 0027227704 scopus 로고
    • Polyprotein processing in African Swine Fever virus: A novel gene expression strategy for a DNA virus
    • Simon-Mateo, C., G. Andres, and E. Vinuela. 1993. Polyprotein processing in African Swine Fever virus: a novel gene expression strategy for a DNA virus. EMBO J. 12:2977-2987.
    • (1993) EMBO J. , vol.12 , pp. 2977-2987
    • Simon-Mateo, C.1    Andres, G.2    Vinuela, E.3
  • 42
    • 0028861662 scopus 로고
    • Mapping and sequence of the gene encoding protein p17, a major African swine fever protein
    • Simon-Mateo, C., J. M. Freue, G. Andres, C. Lopez-Otin, and E. Vinuela. 1995. Mapping and sequence of the gene encoding protein p17, a major African swine fever protein. Virology 206:1140-1144.
    • (1995) Virology , vol.206 , pp. 1140-1144
    • Simon-Mateo, C.1    Freue, J.M.2    Andres, G.3    Lopez-Otin, C.4    Vinuela, E.5
  • 43
    • 0029052884 scopus 로고
    • African swine fever virus gene j13L encodes a 25-27 kDa virion protein with variable numbers of amino acid repeats
    • Sun, H., S. Jacobs, G. L. Smith, L. K. Dixon, and R. M. E. Parkhouse. 1995. African swine fever virus gene j13L encodes a 25-27 kDa virion protein with variable numbers of amino acid repeats. J. Gen. Virol. 76:1117-1127.
    • (1995) J. Gen. Virol. , vol.76 , pp. 1117-1127
    • Sun, H.1    Jacobs, S.2    Smith, G.L.3    Dixon, L.K.4    Parkhouse, R.M.E.5
  • 44
    • 0020635123 scopus 로고
    • Perturbation of vesicular traffic with the carboxylic ionophore monensin
    • Tartakoff, A. M. 1983. Perturbation of vesicular traffic with the carboxylic ionophore monensin. Cell 32:1026-1028.
    • (1983) Cell , vol.32 , pp. 1026-1028
    • Tartakoff, A.M.1
  • 45
    • 0027530255 scopus 로고
    • Progeny vaccinia 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 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
  • 46
    • 0021322863 scopus 로고
    • Replication of coronavirus MHV-A59 in sac cells: Determination of the first site of budding of progeny virions
    • Tooze, J., S. A. Tooze, and G. Warren. 1984. Replication of coronavirus MHV-A59 in sac cells: determination of the first site of budding of progeny virions. Eur. J. Cell Biol. 33:281-293.
    • (1984) Eur. J. Cell Biol. , vol.33 , pp. 281-293
    • Tooze, J.1    Tooze, S.A.2    Warren, G.3
  • 47
    • 0023916548 scopus 로고
    • Site of addition of N-acetyl-galactosamine to the E1 glycoprotein of mouse hepatitis virus-A59
    • Tooze, J., S. A. Tooze, and G. Warren. 1988. Site of addition of N-acetyl-galactosamine to the E1 glycoprotein of mouse hepatitis virus-A59. J. Cell Biol. 106:1475-1487.
    • (1988) J. Cell Biol. , vol.106 , pp. 1475-1487
    • Tooze, J.1    Tooze, S.A.2    Warren, G.3
  • 49
    • 0026083301 scopus 로고
    • Effect of brefeldin A on alphaherpesvirus membrane protein glycosylation and virus egress
    • Whaley, M. E., J. P. Card, R. P. Meade, A. K. Robbins, and L. W. Enquist. 1991. Effect of brefeldin A on alphaherpesvirus membrane protein glycosylation and virus egress. J. Virol. 65:1066-1081.
    • (1991) J. Virol. , vol.65 , pp. 1066-1081
    • Whaley, M.E.1    Card, J.P.2    Meade, R.P.3    Robbins, A.K.4    Enquist, L.W.5
  • 50
    • 0027157153 scopus 로고
    • Associations between subunit ectodomains promote T-cell antigen receptor assembly and protect from degradation in the endoplasmic reticulum
    • Wileman, T., L. Kane, G. Carson, and C. Terhorst. 1993. Associations between subunit ectodomains promote T-cell antigen receptor assembly and protect from degradation in the endoplasmic reticulum. J. Cell Biol. 122:67-78.
    • (1993) J. Cell Biol. , vol.122 , pp. 67-78
    • Wileman, T.1    Kane, L.2    Carson, G.3    Terhorst, C.4
  • 51
    • 0002291865 scopus 로고
    • African swine fever virus
    • M. B. Pensaert (ed.), Elscvier, Amsterdam
    • Wilkinson, P. J. 1989. African swine fever virus, p. 17-35. In M. B. Pensaert (ed.), Virus infections of porcines. Elscvier, Amsterdam.
    • (1989) Virus Infections of Porcines , pp. 17-35
    • Wilkinson, P.J.1
  • 53
    • 0027257647 scopus 로고
    • Regulation of selective protein degradation in the endoplasmic reticulum by redox potential
    • Young, J., L. P. Kane, M. Exley, and T. Wileman. 1993. Regulation of selective protein degradation in the endoplasmic reticulum by redox potential. J. Biol. Chem. 268:19810-19818.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19810-19818
    • Young, J.1    Kane, L.P.2    Exley, M.3    Wileman, T.4
  • 54
    • 0028971193 scopus 로고
    • Envelopment of varicella-zoster: Targeting of viral glycoproteins to the trans-Golgi network
    • Zhu, Z., M. D. Gershon, Y. Hao, R. T. Ambron, C. Gabel, and A. A. Gershon. 1995. Envelopment of varicella-zoster: targeting of viral glycoproteins to the trans-Golgi network. J. Virol. 69:7951-7959.
    • (1995) J. Virol. , vol.69 , pp. 7951-7959
    • Zhu, Z.1    Gershon, M.D.2    Hao, Y.3    Ambron, R.T.4    Gabel, C.5    Gershon, A.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.