메뉴 건너뛰기




Volumn 78, Issue 21, 2004, Pages 11879-11889

Essential function of the pseudorabies virus UL36 gene product is independent of its interaction with the UL37 protein

Author keywords

[No Author keywords available]

Indexed keywords

GENE PRODUCT; PROTEIN UL36; PROTEIN UL37; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 6344219960     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.78.21.11879-11889.2004     Document Type: Article
Times cited : (103)

References (53)
  • 1
    • 0020615188 scopus 로고
    • Characterization of the herpes simplex virion-associated factor responsible for the induction of alpha genes
    • Batterson, W., and B. Roizman. 1983. Characterization of the herpes simplex virion-associated factor responsible for the induction of alpha genes. J. Virol. 46:371-377.
    • (1983) J. Virol. , vol.46 , pp. 371-377
    • Batterson, W.1    Roizman, B.2
  • 2
    • 0020701819 scopus 로고
    • Molecular genetics of herpes simplex virus. VIII. Further characterization of a temperature-sensitive mutant defective in release of viral DNA and in other stages of the viral reproductive cycle
    • Batterson, W., D. Furlong, and B. Roizman. 1983. Molecular genetics of herpes simplex virus. VIII. Further characterization of a temperature-sensitive mutant defective in release of viral DNA and in other stages of the viral reproductive cycle. J. Virol. 45:397-407.
    • (1983) J. Virol. , vol.45 , pp. 397-407
    • Batterson, W.1    Furlong, D.2    Roizman, B.3
  • 3
    • 0034947771 scopus 로고    scopus 로고
    • Cytomegalovirus basic phosphoprotein (pUL32) binds to capsids in vitro through its amino one-third
    • Baxter, M. K., and W. Gibson. 2001. Cytomegalovirus basic phosphoprotein (pUL32) binds to capsids in vitro through its amino one-third. J. Virol. 75:6865-6873.
    • (2001) J. Virol. , vol.75 , pp. 6865-6873
    • Baxter, M.K.1    Gibson, W.2
  • 4
    • 0036149161 scopus 로고    scopus 로고
    • Hum. Cytomegalovirus UL47 tegument protein functions after entry and before immediate-early gene expression
    • Bechtel, J. T., and T. Shenk. 2002. Hum. Cytomegalovirus UL47 tegument protein functions after entry and before immediate-early gene expression. J. Virol. 76:1043-1050.
    • (2002) J. Virol. , vol.76 , pp. 1043-1050
    • Bechtel, J.T.1    Shenk, T.2
  • 5
    • 0033039489 scopus 로고    scopus 로고
    • Inhibition of virion maturation by simultaneous deletion of glycoproteins E, I, and M of pseudorabies virus
    • Brack, A. R., J. M. Dijkstra, H. Granzow, B. G. Klupp, and T. C. Mettenleiter. 1999. Inhibition of virion maturation by simultaneous deletion of glycoproteins E, I, and M of pseudorabies virus. J. Virol. 73:5364-5372.
    • (1999) J. Virol. , vol.73 , pp. 5364-5372
    • Brack, A.R.1    Dijkstra, J.M.2    Granzow, H.3    Klupp, B.G.4    Mettenleiter, T.C.5
  • 6
  • 7
    • 0021659654 scopus 로고
    • Identification of herpes simplex virus DNA sequences which encode a trans-acting polypeptide responsible for stimulation of immediate early transcription
    • Campbell, M. E., J. W. Palfreyman, and C. M. Preston. 1984. Identification of herpes simplex virus DNA sequences which encode a trans-acting polypeptide responsible for stimulation of immediate early transcription. J. Mol. Biol. 180:1-19.
    • (1984) J. Mol. Biol. , vol.180 , pp. 1-19
    • Campbell, M.E.1    Palfreyman, J.W.2    Preston, C.M.3
  • 8
    • 0033587536 scopus 로고    scopus 로고
    • Three-dimensional visualization of tegument/capsid interactions in the intact human cytomegalovirus
    • Chen, D. H., H. Jiang, M. Lee, F. Liu, and Z. H. Zhou. 1999. Three-dimensional visualization of tegument/capsid interactions in the intact human cytomegalovirus. Virology 260:10-16.
    • (1999) Virology , vol.260 , pp. 10-16
    • Chen, D.H.1    Jiang, H.2    Lee, M.3    Liu, F.4    Zhou, Z.H.5
  • 9
    • 0029065955 scopus 로고
    • R cassettes with the option of Flp-catalyzed excision of the antibiotic-resistance determinant
    • R cassettes with the option of Flp-catalyzed excision of the antibiotic-resistance determinant. Gene 158:9-14.
    • (1995) Gene , vol.158 , pp. 9-14
    • Cherepanov, P.P.1    Wackernagel, W.2
  • 10
    • 0017868338 scopus 로고
    • Empirical prediction of protein conformation
    • Chou, P. Y., and G. D. Fasman. 1978. Empirical prediction of protein conformation. Annu. Rev. Biochem. 47:251-276.
    • (1978) Annu. Rev. Biochem. , vol.47 , pp. 251-276
    • Chou, P.Y.1    Fasman, G.D.2
  • 11
    • 0024582526 scopus 로고
    • Characterization of DNA sequence-common and sequence-specific proteins binding to cis-acting sites for cleavage of the terminal a sequence of the herpes simplex virus 1 genome
    • Chou, J., and B. Roizman. 1993. Characterization of DNA sequence-common and sequence-specific proteins binding to cis-acting sites for cleavage of the terminal a sequence of the herpes simplex virus 1 genome. J. Virol. 63:1059-1068.
    • (1993) J. Virol. , vol.63 , pp. 1059-1068
    • Chou, J.1    Roizman, B.2
  • 12
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K. A., and B. L. Wanner. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. USA 97:6640-6645.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 13
    • 0036138814 scopus 로고    scopus 로고
    • The pseudorabies virus VP22 homologue (UL49) is dispensable for virus growth in vitro and has no effect on virulence and neuronal spread in rodents
    • del Rio, T., H. C. Werner, and L W. Enquist. 2002. The pseudorabies virus VP22 homologue (UL49) is dispensable for virus growth in vitro and has no effect on virulence and neuronal spread in rodents. J. Virol. 76:774-782.
    • (2002) J. Virol. , vol.76 , pp. 774-782
    • Rio, T.1    Werner, H.C.2    Enquist, L.W.3
  • 14
    • 0034466764 scopus 로고    scopus 로고
    • A null mutation in the UL36 gene of herpes simplex virus type 1 results in accumulation of unenveloped DNA-filled capsids in the cytoplasm of infected cells
    • Desai, P. 2000. A null mutation in the UL36 gene of herpes simplex virus type 1 results in accumulation of unenveloped DNA-filled capsids in the cytoplasm of infected cells. J. Virol. 74:1608-10618.
    • (2000) J. Virol. , vol.74 , pp. 1608-10618
    • Desai, P.1
  • 15
    • 0034785814 scopus 로고    scopus 로고
    • A null mutation in the gene encoding the UL37 polypeptide of herpes simplex virus type 1 abrogates virus maturation
    • Desai, P., G. Sexton, J. McCaffery, and S. Person. 2001. A null mutation in the gene encoding the UL37 polypeptide of herpes simplex virus type 1 abrogates virus maturation. J. Virol. 75:10259-10271.
    • (2001) J. Virol. , vol.75 , pp. 10259-10271
    • Desai, P.1    Sexton, G.2    McCaffery, J.3    Person, S.4
  • 16
    • 0036145852 scopus 로고    scopus 로고
    • Characterization of Marek's Disease Virus serotype 1 (MDV-1) deletion mutants that lack UL46 to UL49 genes: MDV-1 UL49, encoding VP22, is indispensable for virus growth
    • Dorange, F., B. K. Tischer, J. F. Vautherot, and N. Osterrieder. 2002. Characterization of Marek's Disease Virus serotype 1 (MDV-1) deletion mutants that lack UL46 to UL49 genes: MDV-1 UL49, encoding VP22, is indispensable for virus growth. J. Virol. 76:1959-1970.
    • (2002) J. Virol. , vol.76 , pp. 1959-1970
    • Dorange, F.1    Tischer, B.K.2    Vautherot, J.F.3    Osterrieder, N.4
  • 17
    • 0028849796 scopus 로고
    • VP16 interacts via its activation domain with VP22, a tegument protein of herpes simplex virus, and is relocated to a novel macromolecular assembly in coexpressing cells
    • Elliott, G., G. Mouzakitis, and P. O'Hare. 1995. VP16 interacts via its activation domain with VP22, a tegument protein of herpes simplex virus, and is relocated to a novel macromolecular assembly in coexpressing cells. J. Virol. 69:7932-7941.
    • (1995) J. Virol. , vol.69 , pp. 7932-7941
    • Elliott, G.1    Mouzakitis, G.2    O'Hare, P.3
  • 18
    • 0030011637 scopus 로고    scopus 로고
    • Identification and characterization of the pseudorabies virus UL3.5 protein, which is involved in virus egress
    • Fuchs, W., B. G. Klupp, H. Granzow, H. J. Rziha, and T. C. Mettenleiter. 1996. Identification and characterization of the pseudorabies virus UL3.5 protein, which is involved in virus egress. J. Virol. 70:3517-3527.
    • (1996) J. Virol. , vol.70 , pp. 3517-3527
    • Fuchs, W.1    Klupp, B.G.2    Granzow, H.3    Rziha, H.J.4    Mettenleiter, T.C.5
  • 19
    • 0036133234 scopus 로고    scopus 로고
    • The interacting UL31 and UL34 gene products of pseudorabies virus are involved in egress from the host-cell nucleus and represent components of primary enveloped but not mature virions
    • Fuchs, W., B. G. Klupp, H. Granzow, N. Osterrieder, and T. C. Mettenleiter. 2002. The interacting UL31 and UL34 gene products of pseudorabies virus are involved in egress from the host-cell nucleus and represent components of primary enveloped but not mature virions. J. Virol. 76:364-378.
    • (2002) J. Virol. , vol.76 , pp. 364-378
    • Fuchs, W.1    Klupp, B.G.2    Granzow, H.3    Osterrieder, N.4    Mettenleiter, T.C.5
  • 20
    • 0036278491 scopus 로고    scopus 로고
    • The UL48 tegument protein of pseudorabies virus is critical for intracytoplasmic assembly of infectious virions
    • Fuchs, W., H. Granzow, B. G. Klupp, M. Kopp, and T. C. Mettenleiter. 2002. The UL48 tegument protein of pseudorabies virus is critical for intracytoplasmic assembly of infectious virions. J. Virol. 76:6729-6742.
    • (2002) J. Virol. , vol.76 , pp. 6729-6742
    • Fuchs, W.1    Granzow, H.2    Klupp, B.G.3    Kopp, M.4    Mettenleiter, T.C.5
  • 21
    • 0036316146 scopus 로고    scopus 로고
    • Physical interaction between envelope glycoproteins E and M of pseudorabies virus and the major tegument protein UL49
    • Fuchs, W., B. G. Klupp, H. Granzow, A. Mundt, C. Hengartner, L. W. Enquist, and T. C. Mettenleiter. 2002. Physical interaction between envelope glycoproteins E and M of pseudorabies virus and the major tegument protein UL49. J. Virol. 76:8208-8217.
    • (2002) J. Virol. , vol.76 , pp. 8208-8217
    • Fuchs, W.1    Klupp, B.G.2    Granzow, H.3    Mundt, A.4    Hengartner, C.5    Enquist, L.W.6    Mettenleiter, T.C.7
  • 22
    • 0242660233 scopus 로고    scopus 로고
    • A pseudorabies virus recombinant simultaneously lacking the major tegument proteins encoded by the UL46, UL47, UL48, and UL49 genes is viable in cultured cells
    • Fuchs, W., H. Granzow, and T. C. Mettenleiter. 2003. A pseudorabies virus recombinant simultaneously lacking the major tegument proteins encoded by the UL46, UL47, UL48, and UL49 genes is viable in cultured cells. J. Virol. 77:12891-12900.
    • (2003) J. Virol. , vol.77 , pp. 12891-12900
    • Fuchs, W.1    Granzow, H.2    Mettenleiter, T.C.3
  • 23
    • 0028106296 scopus 로고
    • Intracellular transport of newly synthesized varicellazoster virus: Final envelopment in the trans-Golgi network
    • Gershon, A. A., D. L. Sherman, Z. Zhu, C. A. Gabel, R. T. Ambron, and M. D. Gershon. 1994. Intracellular transport of newly synthesized varicellazoster virus: final envelopment in 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.A.4    Ambron, R.T.5    Gershon, M.D.6
  • 24
    • 0015847039 scopus 로고
    • A new technique for the assay of infectivity of human adenovirus 5 DNA
    • Graham, F. L., and A. J. van der Eb. 1973. A new technique for the assay of infectivity of human adenovirus 5 DNA. Virology 52:456-467.
    • (1973) Virology , vol.52 , pp. 456-467
    • Graham, F.L.1    Van Der Eb, A.J.2
  • 26
    • 0000525742 scopus 로고
    • A comparison of herpes simplex and pseudorabies virus
    • Kaplan, A. S., and A. Vatter. 1959. A comparison of herpes simplex and pseudorabies virus. Virology 7:394-407.
    • (1959) Virology , vol.7 , pp. 394-407
    • Kaplan, A.S.1    Vatter, A.2
  • 27
    • 0033015078 scopus 로고    scopus 로고
    • Glycoprotein gL-independent infectivity of pseudorabies virus is mediated by a gD-gH fusion protein
    • Klupp, B. G., and T. C. Mettenleiter. 1999. Glycoprotein gL-independent infectivity of pseudorabies virus is mediated by a gD-gH fusion protein. J. Virol. 73:3014-3022.
    • (1999) J. Virol. , vol.73 , pp. 3014-3022
    • Klupp, B.G.1    Mettenleiter, T.C.2
  • 28
    • 0033775156 scopus 로고    scopus 로고
    • Primary envelopment of pseudorabies virus at the nuclear membrane requires the UL34 gene product
    • Klupp, B. G., H. Granzow, and T. C. Mettenleiter. 2000. Primary envelopment of pseudorabies virus at the nuclear membrane requires the UL34 gene product. J. Virol. 74:10063-10073.
    • (2000) J. Virol. , vol.74 , pp. 10063-10073
    • Klupp, B.G.1    Granzow, H.2    Mettenleiter, T.C.3
  • 29
    • 0034849764 scopus 로고    scopus 로고
    • Pseudorabies virus UL37 gene product is involved in secondary envelopment
    • Klupp, B. G., H. Granzow, E. Mundt, and T. C. Mettenleiter. 2001. Pseudorabies virus UL37 gene product is involved in secondary envelopment. J. Virol. 75:8927-8936.
    • (2001) J. Virol. , vol.75 , pp. 8927-8936
    • Klupp, B.G.1    Granzow, H.2    Mundt, E.3    Mettenleiter, T.C.4
  • 30
    • 0036191216 scopus 로고    scopus 로고
    • Pseudorabies virus UL36 tegument protein physically interacts with the UL37 protein
    • Klupp, B. G., W. Fuchs, H. Granzow, R. Nixdorf, and T. C. Mettenleiter. 2002. Pseudorabies virus UL36 tegument protein physically interacts with the UL37 protein. J. Virol. 76:3065-3071.
    • (2002) J. Virol. , vol.76 , pp. 3065-3071
    • Klupp, B.G.1    Fuchs, W.2    Granzow, H.3    Nixdorf, R.4    Mettenleiter, T.C.5
  • 31
  • 32
    • 0036337330 scopus 로고    scopus 로고
    • Identification and characterization of the pseudorabies virus tegument proteins UL46 and UL47: Role for UL47 in virion morphogenesis in the cytoplasm
    • Kopp, M., B. G. Klupp, H. Granzow, W. Fuchs, and T. C. Mettenleiter. 2002. Identification and characterization of the pseudorabies virus tegument proteins UL46 and UL47: role for UL47 in virion morphogenesis in the cytoplasm. J. Virol. 76:8820-8833.
    • (2002) J. Virol. , vol.76 , pp. 8820-8833
    • Kopp, M.1    Klupp, B.G.2    Granzow, H.3    Fuchs, W.4    Mettenleiter, T.C.5
  • 33
    • 0344080584 scopus 로고    scopus 로고
    • The pseudorabies virus UL11 protein is a virion component involved in secondary envelopment in the cytoplasm
    • Kopp, M., H. Granzow, W. Fuchs, B. G. Klupp, E. Mundt, A. Karger, and T. C. Mettenleiter. 2003. The pseudorabies virus UL11 protein is a virion component involved in secondary envelopment in the cytoplasm. J. Virol. 77:5339-5351.
    • (2003) J. Virol. , vol.77 , pp. 5339-5351
    • Kopp, M.1    Granzow, H.2    Fuchs, W.3    Klupp, B.G.4    Mundt, E.5    Karger, A.6    Mettenleiter, T.C.7
  • 34
    • 1542377535 scopus 로고    scopus 로고
    • Simultaneous deletion of pseudorabies virus tegument protein UL11 and glycoprotein M severely impairs secondary envelopment
    • Kopp, M., H. Granzow, W. Fuchs, B. G. Klupp, and T. C. Mettenleiter. 2004. Simultaneous deletion of pseudorabies virus tegument protein UL11 and glycoprotein M severely impairs secondary envelopment. J. Virol. 78:3024-3034.
    • (2004) J. Virol. , vol.78 , pp. 3024-3034
    • Kopp, M.1    Granzow, H.2    Fuchs, W.3    Klupp, B.G.4    Mettenleiter, T.C.5
  • 35
    • 0023866418 scopus 로고
    • Herpes simplex virus virion host shutoff function
    • Kwong, A. D., J. A. Kruper, and N. Frenkel. 1988. Herpes simplex virus virion host shutoff function. J. Virol. 62:912-921.
    • (1988) J. Virol. , vol.62 , pp. 912-921
    • Kwong, A.D.1    Kruper, J.A.2    Frenkel, N.3
  • 36
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 277:680-685.
    • (1970) Nature , vol.277 , pp. 680-685
    • Laemmli, U.K.1
  • 37
    • 0033997929 scopus 로고    scopus 로고
    • Bovine herpesvirus 1 UL3.5 interacts with bovine herpesvirus 1 alpha-transinducing factor
    • Lam, N., and G. J. Letchworth. 2000. Bovine herpesvirus 1 UL3.5 interacts with bovine herpesvirus 1 alpha-transinducing factor. J. Virol. 74:2876-2884.
    • (2000) J. Virol. , vol.74 , pp. 2876-2884
    • Lam, N.1    Letchworth, G.J.2
  • 38
    • 0021971623 scopus 로고
    • Demonstration of three major species of pseudorabies virus glycoproteins and identification of a disulfide-linked glycoprotein complex
    • Lukács, N., H.-J. Thiel, T. C. Mettenleiter, and H.-J. Rziha. 1985. Demonstration of three major species of pseudorabies virus glycoproteins and identification of a disulfide-linked glycoprotein complex. J. Virol. 53:166-173.
    • (1985) J. Virol. , vol.53 , pp. 166-173
    • Lukács, N.1    Thiel, H.-J.2    Mettenleiter, T.C.3    Rziha, H.-J.4
  • 40
    • 0026787060 scopus 로고
    • Characterization of the large tegument protein (ICP1/2) of herpes simplex virus type 1
    • McNabb, D. S., and R. J. Courtney. 1992. Characterization of the large tegument protein (ICP1/2) of herpes simplex virus type 1. Virology. 190:221-232.
    • (1992) Virology , vol.190 , pp. 221-232
    • McNabb, D.S.1    Courtney, R.J.2
  • 41
    • 0033631564 scopus 로고    scopus 로고
    • Aujeszky's disease (pseudorabies) virus: The virus and molecular pathogenesis-state of the art, June 1999
    • Mettenleiter, T. C. 2000. Aujeszky's disease (pseudorabies) virus: the virus and molecular pathogenesis-state of the art, June 1999. Vet. Res. 31:99-115.
    • (2000) Vet. Res. , vol.31 , pp. 99-115
    • Mettenleiter, T.C.1
  • 42
    • 0036148284 scopus 로고    scopus 로고
    • Herpesvirus assembly and egress
    • Mettenleiter, T. C. 2002. Herpesvirus assembly and egress. J. Virol. 76:1537-1547.
    • (2002) J. Virol. , vol.76 , pp. 1537-1547
    • Mettenleiter, T.C.1
  • 43
    • 0033919401 scopus 로고    scopus 로고
    • Evidence that herpes simplex virus VP16 is required for viral egress down-stream of the initial envelopment event
    • Mossman, K. L., R. Sherburne, C. Lavery, J. Duncan, and J. R. Smiley. 2000. Evidence that herpes simplex virus VP16 is required for viral egress down-stream of the initial envelopment event. J. Virol. 74:6287-6299.
    • (2000) J. Virol. , vol.74 , pp. 6287-6299
    • Mossman, K.L.1    Sherburne, R.2    Lavery, C.3    Duncan, J.4    Smiley, J.R.5
  • 44
    • 0037008483 scopus 로고    scopus 로고
    • Cytomegalovirus recruitment of a cellular kinase to dissolve the nuclear lamina
    • Muranyi, W., J. Haas, M. Wagner, G. Krohne, and U. H. Koszinowski. 2002. Cytomegalovirus recruitment of a cellular kinase to dissolve the nuclear lamina. Science 297:854-857.
    • (2002) Science , vol.297 , pp. 854-857
    • Muranyi, W.1    Haas, J.2    Wagner, M.3    Krohne, G.4    Koszinowski, U.H.5
  • 45
    • 0029690315 scopus 로고    scopus 로고
    • Retrieval of human cytomegalovirus glycoprotein B from the infected cell surface for virus envelopment
    • Radsak, K., M. Eickmann, T. Mockenhaupt, E. Bogner, H. Kern, A. Eis-Hubinger, and M. Reschke. 1996. Retrieval of human cytomegalovirus glycoprotein B from the infected cell surface for virus envelopment. Arch. Virol. 141:557-572.
    • (1996) Arch. Virol. , vol.141 , pp. 557-572
    • Radsak, K.1    Eickmann, M.2    Mockenhaupt, T.3    Bogner, E.4    Kern, H.5    Eis-Hubinger, A.6    Reschke, M.7
  • 46
    • 0034892972 scopus 로고    scopus 로고
    • UL31 and UL34 proteins of herpes simplex virus form a complex that accumulates at the nuclear rim and is required for envelopment of nucleocapsids
    • Reynolds, A., B. Ryckman, J. Haines, Y. Zhou, L. Liang, and R. Roller. 2001. UL31 and UL34 proteins of herpes simplex virus form a complex that accumulates at the nuclear rim and is required for envelopment of nucleocapsids. J. Virol. 75:8803-8817.
    • (2001) J. Virol. , vol.75 , pp. 8803-8817
    • Reynolds, A.1    Ryckman, B.2    Haines, J.3    Zhou, Y.4    Liang, L.5    Roller, R.6
  • 47
    • 0001142641 scopus 로고    scopus 로고
    • Herpes simplex viruses and their replication
    • D. M. Knipe and P. M. Howley (ed.), Lippincott Williams & Wilkins, Philadelphia, Pa.
    • Roizman, B., and D. M. Knipe. 2001. Herpes simplex viruses and their replication, p. 2399-2459. In D. M. Knipe and P. M. Howley (ed.), Fields virology. Lippincott Williams & Wilkins, Philadelphia, Pa.
    • (2001) Fields Virology , pp. 2399-2459
    • Roizman, B.1    Knipe, D.M.2
  • 48
    • 0001142642 scopus 로고    scopus 로고
    • The family Herpesviridae: A brief introduction
    • D. M. Knipe and P. M. Howley (ed.), Lippincott Williams & Wilkins, Philadelphia, Pa.
    • Roizman, B., and P. E. Pellet. 2001. The family Herpesviridae: a brief introduction, p. 2381-2397. In D. M. Knipe and P. M. Howley (ed.), Fields virology. Lippincott Williams & Wilkins, Philadelphia, Pa.
    • (2001) Fields Virology , pp. 2381-2397
    • Roizman, B.1    Pellet, P.E.2
  • 49
    • 0035024157 scopus 로고    scopus 로고
    • Herpes simplex virus nucleocapsids mature to progeny virions by an envelopment -> deenvelopment -> reenvelopment pathway
    • Skepper, J. N., A. Whiteley, H. Browne, and A. Minson. 2001. Herpes simplex virus nucleocapsids mature to progeny virions by an envelopment -> deenvelopment -> reenvelopment pathway. J. Virol. 75:5697-5702.
    • (2001) J. Virol. , vol.75 , pp. 5697-5702
    • Skepper, J.N.1    Whiteley, A.2    Browne, H.3    Minson, A.4
  • 50
    • 0033045991 scopus 로고    scopus 로고
    • Capsid structure of simian cytomegalovirus from cryoelectron microscopy: Evidence for tegument attachment sites
    • Trus, B. L., W. Gibson, N. Cheng, and A. C. Steven. 1999. Capsid structure of simian cytomegalovirus from cryoelectron microscopy: evidence for tegument attachment sites. J. Virol. 73:2181-2192.
    • (1999) J. Virol. , vol.73 , pp. 2181-2192
    • Trus, B.L.1    Gibson, W.2    Cheng, N.3    Steven, A.C.4
  • 51
    • 0026543979 scopus 로고
    • Deletion of the VP16 open reading frame of herpes simplex virus type 1
    • Weinheimer, S. P., B. A. Boyd, S. K. Durham, J. L. Resnick, and D. R. O'Boyle. 1992. Deletion of the VP16 open reading frame of herpes simplex virus type 1. J. Virol. 66:258-269.
    • (1992) J. Virol. , vol.66 , pp. 258-269
    • Weinheimer, S.P.1    Boyd, B.A.2    Durham, S.K.3    Resnick, J.L.4    O'Boyle, D.R.5
  • 52
    • 0026083301 scopus 로고
    • Effect of brefeldin a on alphaherpesvirus membrane protein glycosylation and virus egress
    • Whealy, 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
    • Whealy, M.E.1    Card, J.P.2    Meade, R.P.3    Robbins, A.K.4    Enquist, L.W.5
  • 53
    • 0345471494 scopus 로고    scopus 로고
    • Visualization of tegument-capsid interactions and DNA in intact herpes simplex virus type 1 virions
    • Zhou, Z. H., D. H. Chen, J. Jakana, F. J. Rixon, and W. Chiu. 1999. Visualization of tegument-capsid interactions and DNA in intact herpes simplex virus type 1 virions. J. Virol. 73:3210-3218.
    • (1999) J. Virol. , vol.73 , pp. 3210-3218
    • Zhou, Z.H.1    Chen, D.H.2    Jakana, J.3    Rixon, F.J.4    Chiu, W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.