메뉴 건너뛰기




Volumn 84, Issue 9, 2010, Pages 4782-4797

The length of and nonhydrophobic residues in the transmembrane domain of dengue virus envelope protein are critical for its retention and assembly in the endoplasmic reticulum

Author keywords

[No Author keywords available]

Indexed keywords

CD4 ANTIGEN; MEMBRANE PROTEIN; VIRUS ENVELOPE PROTEIN;

EID: 77950786716     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.01963-09     Document Type: Article
Times cited : (32)

References (74)
  • 1
    • 0032989258 scopus 로고    scopus 로고
    • Mapping of functional elements in the stem-anchor region of tick-borne encephalitis virus envelope protein E
    • Allison, S. L., K. Stiasny, K. Stadler, C. W. Mandl, and F. X. Heinz. 1999. Mapping of functional elements in the stem-anchor region of tick-borne encephalitis virus envelope protein E. J. Virol. 73:5605-5612.
    • (1999) J. Virol. , vol.73 , pp. 5605-5612
    • Allison, S.L.1    Stiasny, K.2    Stadler, K.3    Mandl, C.W.4    Heinz, F.X.5
  • 2
    • 0030979789 scopus 로고    scopus 로고
    • A retention signal necessary and sufficient for Golgi localization maps to the cytoplasmic tail of a Bunyaviridae (Uukuniemi virus) membrane glycoprotein
    • Andersson, A. M., L. Melin, A. Bean, and R. F. Pettersson. 1997. A retention signal necessary and sufficient for Golgi localization maps to the cytoplasmic tail of a Bunyaviridae (Uukuniemi virus) membrane glycoprotein. J. Virol. 71:4717-4727.
    • (1997) J. Virol. , vol.71 , pp. 4717-4727
    • Andersson, A.M.1    Melin, L.2    Bean, A.3    Pettersson, R.F.4
  • 3
    • 0026607683 scopus 로고
    • Golgi retention of a trans-Golgi membrane protein, galactosyltransferase, requires cysteine and histidine residues within the membrane-anchoring domain
    • Aoki, D., N. Lee, N. Yamaguchi, C. Dubois, and M. N. Fukuda. 1992. Golgi retention of a trans-Golgi membrane protein, galactosyltransferase, requires cysteine and histidine residues within the membrane-anchoring domain. Proc. Natl. Acad. Sci. USA 89:4319-4323.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4319-4323
    • Aoki, D.1    Lee, N.2    Yamaguchi, N.3    Dubois, C.4    Fukuda, M.N.5
  • 4
    • 0030939784 scopus 로고    scopus 로고
    • Intrinsic signals in the unique domain target p56(lck) to the plasma membrane independently of CD4
    • Bijlmakers, M. J., M. Isobe-Nakamura, L. J. Ruddock, and M. Marsh. 1997. Intrinsic signals in the unique domain target p56(lck) to the plasma membrane independently of CD4. J. Cell Biol. 137:1029-1040.
    • (1997) J. Cell Biol. , vol.137 , pp. 1029-1040
    • Bijlmakers, M.J.1    Isobe-Nakamura, M.2    Ruddock, L.J.3    Marsh, M.4
  • 5
    • 0031883267 scopus 로고    scopus 로고
    • Genetic determinants responsible for acquisition of dengue type 2 virus mouse neurovirulence
    • Bray, M., R. Men, I. Tokimatsu, and C. J. Lai. 1998. Genetic determinants responsible for acquisition of dengue type 2 virus mouse neurovirulence. J. Virol. 72:1647-1651. (Pubitemid 28116956)
    • (1998) Journal of Virology , vol.72 , Issue.2 , pp. 1647-1651
    • Bray, M.1    Men, R.2    Tokimatsu, I.3    Lai, C.-J.4
  • 6
    • 0027892019 scopus 로고
    • Cholesterol and the Golgi apparatus
    • Bretscher, M. S., and S. Munro. 1993. Cholesterol and the Golgi apparatus. Science 261:1280-1281.
    • (1993) Science , vol.261 , pp. 1280-1281
    • Bretscher, M.S.1    Munro, S.2
  • 8
    • 0034001808 scopus 로고    scopus 로고
    • A single intramuscular injection of recombinant plasmid DNA induces protective immunity and prevents Japanese encephalitis in mice
    • Chang, G. J., A. R. Hunt, and B. Davis. 2000. A single intramuscular injection of recombinant plasmid DNA induces protective immunity and prevents Japanese encephalitis in mice. J. Virol. 74:4244-4252.
    • (2000) J. Virol. , vol.74 , pp. 4244-4252
    • Chang, G.J.1    Hunt, A.R.2    Davis, B.3
  • 9
    • 0037294732 scopus 로고    scopus 로고
    • Enhancing biosynthesis and secretion of premembrane and envelope proteins by the chimeric plasmid of dengue virus type 2 and Japanese encephalitis virus
    • Chang, G. J., A. R. Hunt, D. A. Holmes, T. Springfield, T. S. Chiueh, J. T. Roehrig, and D. J. Gubler. 2003. Enhancing biosynthesis and secretion of premembrane and envelope proteins by the chimeric plasmid of dengue virus type 2 and Japanese encephalitis virus. Virology 306:170-180.
    • (2003) Virology , vol.306 , pp. 170-180
    • Chang, G.J.1    Hunt, A.R.2    Holmes, D.A.3    Springfield, T.4    Chiueh, T.S.5    Roehrig, J.T.6    Gubler, D.J.7
  • 10
    • 0033050645 scopus 로고    scopus 로고
    • The transmembrane domain of hepatitis C virus glycoprotein E1 is a signal for static retention in the endoplasmic reticulum
    • Cocquerel, L., S. Duvet, J. C. Meunier, A. Pillez, R. Cacan, C. Wychowski, and J. Dubuisson. 1999. The transmembrane domain of hepatitis C virus glycoprotein E1 is a signal for static retention in the endoplasmic reticulum. J. Virol. 73:2641-2649. (Pubitemid 29135648)
    • (1999) Journal of Virology , vol.73 , Issue.4 , pp. 2641-2649
    • Cocquerel, L.1    Duvet, S.2    Meunier, J.-C.3    Pillez, A.4    Cacan, R.5    Wychowski, C.6    Dubuisson, J.7
  • 11
    • 0031911782 scopus 로고    scopus 로고
    • A retention signal necessary and sufficient for endoplasmic reticulum localization maps to the transmembrane domain of hepatitis C virus glycoprotein E2
    • Cocquerel, L., J. C. Meunier, A. Pillez, C. Wychowski, and J. Dubuisson. 1998. A retention signal necessary and sufficient for endoplasmic reticulum localization maps to the transmembrane domain of hepatitis C virus glycoprotein E2. J. Virol. 72:2183-2191. (Pubitemid 28100775)
    • (1998) Journal of Virology , vol.72 , Issue.3 , pp. 2183-2191
    • Cocquerel, L.1    Meunier, J.-C.2    Pillez, A.3    Wychowski, C.4    Dubuisson, J.5
  • 12
    • 0034031173 scopus 로고    scopus 로고
    • Charged residues in the transmembrane domains of hepatitis C virus glycoproteins play a major role in the processing, subcellular localization, and assembly of these envelope proteins
    • DOI 10.1128/JVI.74.8.3623-3633.2000
    • Cocquerel, L., C. Wychowski, F. Minner, F. Penin, and J. Dubuisson. 2000. Charged residues in the transmembrane domains of hepatitis C virus glycoproteins play a major role in the processing, subcellular localization, and assembly of these envelope proteins. J. Virol. 74:3623-3633. (Pubitemid 30180306)
    • (2000) Journal of Virology , vol.74 , Issue.8 , pp. 3623-3633
    • Cocquerel, L.1    Wychowski, C.2    Minner, F.3    Penin, F.4    Dubuisson, J.5
  • 13
    • 0035051928 scopus 로고    scopus 로고
    • West Nile virus recombinant DNA vaccine protects mouse and horse from virus challenge and expresses in vitro a noninfectious recombinant antigen that can be used in enzyme-linked immunosorbent assays
    • Davis, B. S., G. J. Chang, B. Cropp, J. T. Roehrig, D. A. Martin, C. J. Mitchell, R. Bowen, and M. L. Bunning. 2001. West Nile virus recombinant DNA vaccine protects mouse and horse from virus challenge and expresses in vitro a noninfectious recombinant antigen that can be used in enzyme-linked immunosorbent assays. J. Virol. 75:4040-4047.
    • (2001) J. Virol. , vol.75 , pp. 4040-4047
    • Davis, B.S.1    Chang, G.J.2    Cropp, B.3    Roehrig, J.T.4    Martin, D.A.5    Mitchell, C.J.6    Bowen, R.7    Bunning, M.L.8
  • 14
    • 0033610886 scopus 로고    scopus 로고
    • Hepatitis C virus glycoprotein complex localization in the endoplasmic reticulum involves a determinant for retention and not retrieval
    • Duvet, S., L. Cocquerel, A. Pillez, R. Cacan, A. Verbert, D. Moradpour, C. Wychowski, and J. Dubuisson. 1998. Hepatitis C virus glycoprotein complex localization in the endoplasmic reticulum involves a determinant for retention and not retrieval. J. Biol. Chem. 273:32088-32095.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32088-32095
    • Duvet, S.1    Cocquerel, L.2    Pillez, A.3    Cacan, R.4    Verbert, A.5    Moradpour, D.6    Wychowski, C.7    Dubuisson, J.8
  • 15
    • 0025266306 scopus 로고
    • Molecular biology of the Bunyaviridae
    • Elliott, R. M. 1990. Molecular biology of the Bunyaviridae. J. Gen. Virol. 71(Pt 3):501-522.
    • (1990) J. Gen. Virol. , vol.71 , Issue.PART 3 , pp. 501-522
    • Elliott, R.M.1
  • 19
    • 0032771582 scopus 로고    scopus 로고
    • The C-terminal region of the hepatitis C virus E1 glycoprotein confers localization within the endoplasmic reticulum
    • Flint, M., and J. A. McKeating. 1999. The C-terminal region of the hepatitis C virus E1 glycoprotein confers localization within the endoplasmic reticulum. J. Gen. Virol. 80(Pt 8):1943-1947.
    • (1999) J. Gen. Virol. , vol.80 , Issue.PART 8 , pp. 1943-1947
    • Flint, M.1    McKeating, J.A.2
  • 20
    • 0029591306 scopus 로고
    • Differentiation of filoviruses by electron microscopy
    • Geisbert, T. W., and P. B. Jahrling. 1995. Differentiation of filoviruses by electron microscopy. Virus Res. 39:129-150.
    • (1995) Virus Res. , vol.39 , pp. 129-150
    • Geisbert, T.W.1    Jahrling, P.B.2
  • 21
    • 33748366332 scopus 로고    scopus 로고
    • Immunopathological mechanisms in dengue and dengue hemorrhagic fever
    • Green, S., and A. Rothman. 2006. Immunopathological mechanisms in dengue and dengue hemorrhagic fever. Curr. Opin. Infect. Dis. 19:429-436.
    • (2006) Curr. Opin. Infect. Dis. , vol.19 , pp. 429-436
    • Green, S.1    Rothman, A.2
  • 22
    • 0036468861 scopus 로고    scopus 로고
    • Epidemic dengue/dengue hemorrhagic fever as a public health, social and economic problem in the 21st century
    • Gubler, D. J. 2002. Epidemic dengue/dengue hemorrhagic fever as a public health, social and economic problem in the 21st century. Trends Microbiol. 10:100-103.
    • (2002) Trends Microbiol. , vol.10 , pp. 100-103
    • Gubler, D.J.1
  • 24
    • 0023818748 scopus 로고
    • Pathogenesis of dengue: Challenges to molecular biology
    • Halstead, S. B. 1988. Pathogenesis of dengue: challenges to molecular biology. Science 239:476-481.
    • (1988) Science , vol.239 , pp. 476-481
    • Halstead, S.B.1
  • 25
    • 0242660964 scopus 로고    scopus 로고
    • Deletions in the Transmembrane Domain of a Sindbis Virus Glycoprotein Alter Virus Infectivity, Stability, and Host Range
    • DOI 10.1128/JVI.77.23.12710-12719.2003
    • Hernandez, R., C. Sinodis, M. Horton, D. Ferreira, C. Yang, and D. T. Brown. 2003. Deletions in the transmembrane domain of a sindbis virus glycoprotein alter virus infectivity, stability, and host range. J. Virol. 77: 12710-12719. (Pubitemid 37430666)
    • (2003) Journal of Virology , vol.77 , Issue.23 , pp. 12710-12719
    • Hernandez, R.1    Sinodis, C.2    Horton, M.3    Ferreira, D.4    Yang, C.5    Brown, D.T.6
  • 26
    • 0032516841 scopus 로고    scopus 로고
    • Retention of cytochrome b5 in the endoplasmic reticulum is transmembrane and luminal domain-dependent
    • Honsho, M., J. Y. Mitoma, and A. Ito. 1998. Retention of cytochrome b5 in the endoplasmic reticulum is transmembrane and luminal domain-dependent. J. Biol. Chem. 273:20860-20866.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20860-20866
    • Honsho, M.1    Mitoma, J.Y.2    Ito, A.3
  • 27
    • 43049109558 scopus 로고    scopus 로고
    • A strong endoplasmic reticulum retention signal in the stem-anchor region of envelope glycoprotein of dengue virus type 2 affects the production of virus-like particles
    • Hsieh, S. C., I. J. Liu, C. C. King, G. J. Chang, and W. K. Wang. 2008. A strong endoplasmic reticulum retention signal in the stem-anchor region of envelope glycoprotein of dengue virus type 2 affects the production of virus-like particles. Virology 374:338-350.
    • (2008) Virology , vol.374 , pp. 338-350
    • Hsieh, S.C.1    Liu, I.J.2    King, C.C.3    Chang, G.J.4    Wang, W.K.5
  • 28
    • 35548932391 scopus 로고    scopus 로고
    • Characterization of retrovirus-based reporter viruses pseudotyped with the precursor membrane and envelope glycoproteins of four serotypes of dengue viruses
    • Hu, H. P., S. C. Hsieh, C. C. King, and W. K. Wang. 2007. Characterization of retrovirus-based reporter viruses pseudotyped with the precursor membrane and envelope glycoproteins of four serotypes of dengue viruses. Virology 368:376-387.
    • (2007) Virology , vol.368 , pp. 376-387
    • Hu, H.P.1    Hsieh, S.C.2    King, C.C.3    Wang, W.K.4
  • 29
    • 0034900171 scopus 로고    scopus 로고
    • A recombinant particulate antigen of Japanese encephalitis virus produced in stably-transformed cells is an effective noninfectious antigen and subunit immunogen
    • Hunt, A. R., C. B. Cropp, and G. J. Chang. 2001. A recombinant particulate antigen of Japanese encephalitis virus produced in stably-transformed cells is an effective noninfectious antigen and subunit immunogen. J. Virol. Methods 97:133-149.
    • (2001) J. Virol. Methods , vol.97 , pp. 133-149
    • Hunt, A.R.1    Cropp, C.B.2    Chang, G.J.3
  • 30
    • 77950838917 scopus 로고    scopus 로고
    • Virus assembly
    • In D. M. Knipe, P. M.Howley, and D. E. Griffin (ed.), Lippincott William & Wilkins, Philadelphia, PA
    • Hunter, E. 2007. Virus assembly, p. 141-168. In D. M. Knipe, P. M.Howley, and D. E. Griffin (ed.), Fields virology. Lippincott William & Wilkins, Philadelphia, PA.
    • (2007) Fields Virology , pp. 141-168
    • Hunter, E.1
  • 31
    • 0023864758 scopus 로고
    • Morphogenesis of yellow fever virus 17D in infected cell cultures
    • Ishak, R., D. G. Tovey, and C. R. Howard. 1988. Morphogenesis of yellow fever virus 17D in infected cell cultures. J. Gen. Virol. 69(Pt 2):325-335.
    • (1988) J. Gen. Virol. , vol.69 , Issue.PART 2 , pp. 325-335
    • Ishak, R.1    Tovey, D.G.2    Howard, C.R.3
  • 33
    • 1642374106 scopus 로고    scopus 로고
    • Sequence determination of the Crimean-Congo hemorrhagic fever virus L segment
    • DOI 10.1016/j.virol.2003.09.046, PII S0042682203007359
    • Kinsella, E., S. G. Martin, A. Grolla, M. Czub, H. Feldmann, and R. Flick. 2004. Sequence determination of the Crimean-Congo hemorrhagic fever virus L segment. Virology 321:23-28. (Pubitemid 38368099)
    • (2004) Virology , vol.321 , Issue.1 , pp. 23-28
    • Kinsella, E.1    Martin, S.G.2    Grolla, A.3    Czub, M.4    Feldmann, H.5    Flick, R.6
  • 34
    • 0037081397 scopus 로고    scopus 로고
    • Dengue type 2 virus subviral extracellular particles produced by a stably transfected mammalian cell line and their evaluation for a subunit vaccine
    • DOI 10.1016/S0264-410X(01)00446-7, PII S0264410X01004467
    • Konishi, E., and A. Fujii. 2002. Dengue type 2 virus subviral extracellular particles produced by a stably transfected mammalian cell line and their evaluation for a subunit vaccine. Vaccine 20:1058-1067. (Pubitemid 34135941)
    • (2002) Vaccine , vol.20 , Issue.7-8 , pp. 1058-1067
    • Konishi, E.1    Fujii, A.2
  • 35
    • 0035983231 scopus 로고    scopus 로고
    • Murray Valley encephalitis virus recombinant subviral particles protect mice from lethal challenge with virulent wild-type virus
    • Kroeger, M. A., and P. C. McMinn. 2002. Murray Valley encephalitis virus recombinant subviral particles protect mice from lethal challenge with virulent wild-type virus. Arch. Virol. 147:1155-1172.
    • (2002) Arch. Virol. , vol.147 , pp. 1155-1172
    • Kroeger, M.A.1    McMinn, P.C.2
  • 36
    • 0035907388 scopus 로고    scopus 로고
    • The missing link in coronavirus assembly. Retention of the avian coronavirus infectious bronchitis virus envelope protein in the pre-Golgi compartments and physical interaction between the envelope and membrane proteins
    • Lim, K. P., and D. X. Liu. 2001. The missing link in coronavirus assembly. Retention of the avian coronavirus infectious bronchitis virus envelope protein in the pre-Golgi compartments and physical interaction between the envelope and membrane proteins. J. Biol. Chem. 276:17515-17523.
    • (2001) J. Biol. Chem. , vol.276 , pp. 17515-17523
    • Lim, K.P.1    Liu, D.X.2
  • 37
    • 20744452745 scopus 로고    scopus 로고
    • Histidine at residue 99 and the transmembrane region of the precursor membrane PrM protein are important for the PrM-E heterodimeric complex formation of Japanese encephalitis virus
    • Lin, Y. J., and S. C. Wu. 2005. Histidine at residue 99 and the transmembrane region of the precursor membrane PrM protein are important for the PrM-E heterodimeric complex formation of Japanese encephalitis virus. J. Virol. 79:8535-8544.
    • (2005) J. Virol. , vol.79 , pp. 8535-8544
    • Lin, Y.J.1    Wu, S.C.2
  • 38
    • 34748873170 scopus 로고    scopus 로고
    • Flaviviridae: The viruses and their replication
    • In D. M. Knipe and P. M. Howley (ed.), Lippincott William & Wilkins, Philadelphia, PA
    • Lindenbach, B. D., H. J. Thiel, and C. M. Rice. 2007. Flaviviridae: the viruses and their replication, p. 1101-1152. In D. M. Knipe and P. M. Howley (ed.), Fields virology. Lippincott William & Wilkins, Philadelphia, PA.
    • (2007) Fields Virology , pp. 1101-1152
    • Lindenbach, B.D.1    Thiel, H.J.2    Rice, C.M.3
  • 39
    • 0027640284 scopus 로고
    • Targeting and retention of Golgi membrane proteins
    • Machamer, C. E. 1993. Targeting and retention of Golgi membrane proteins. Curr. Opin. Cell Biol. 5:606-612.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 606-612
    • Machamer, C.E.1
  • 40
    • 0034767341 scopus 로고    scopus 로고
    • Assembly and maturation of the flavivirus Kunjin virus appear to occur in the rough endoplasmic reticulum and along the secretory pathway, respectively
    • Mackenzie, J. M., and E. G. Westaway. 2001. Assembly and maturation of the flavivirus Kunjin virus appear to occur in the rough endoplasmic reticulum and along the secretory pathway, respectively. J. Virol. 75:10787-10799.
    • (2001) J. Virol. , vol.75 , pp. 10787-10799
    • Mackenzie, J.M.1    Westaway, E.G.2
  • 42
    • 0347503527 scopus 로고    scopus 로고
    • Lentiviral vectors pseudotyped with minimal filovirus envelopes increased gene transfer in murine lung
    • Medina, M. F., G. P. Kobinger, J. Rux, M. Gasmi, D. J. Looney, P. Bates, and J. M. Wilson. 2003. Lentiviral vectors pseudotyped with minimal filovirus envelopes increased gene transfer in murine lung. Mol. Ther. 8:777-789.
    • (2003) Mol. Ther. , vol.8 , pp. 777-789
    • Medina, M.F.1    Kobinger, G.P.2    Rux, J.3    Gasmi, M.4    Looney, D.J.5    Bates, P.6    Wilson, J.M.7
  • 43
    • 0025973898 scopus 로고
    • Carboxy-terminally truncated dengue virus envelope glycoproteins expressed on the cell surface and secreted extracellularly exhibit increased immunogenicity in mice
    • Men, R. H., M. Bray, and C. J. Lai. 1991. Carboxy-terminally truncated dengue virus envelope glycoproteins expressed on the cell surface and secreted extracellularly exhibit increased immunogenicity in mice. J. Virol. 65:1400-1407.
    • (1991) J. Virol. , vol.65 , pp. 1400-1407
    • Men, R.H.1    Bray, M.2    Lai, C.J.3
  • 44
    • 30944461855 scopus 로고    scopus 로고
    • Hide and run. Arginine-based endoplasmic-reticulum-sorting motifs in the assembly of heteromultimeric membrane proteins
    • Michelsen, K., H. Yuan, and B. Schwappach. 2005. Hide and run. Arginine-based endoplasmic-reticulum-sorting motifs in the assembly of heteromultimeric membrane proteins. EMBO Rep. 6:717-722.
    • (2005) EMBO Rep. , vol.6 , pp. 717-722
    • Michelsen, K.1    Yuan, H.2    Schwappach, B.3
  • 45
    • 0037495036 scopus 로고    scopus 로고
    • A ligand-binding pocket in the dengue virus envelope glycoprotein
    • Modis, Y., S. Ogata, D. Clements, and S. C. Harrison. 2003. A ligand-binding pocket in the dengue virus envelope glycoprotein. Proc. Natl. Acad. Sci. USA 100:6986-6991.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6986-6991
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 46
    • 11144244755 scopus 로고    scopus 로고
    • Variable surface epitopes in the crystal structure of dengue virus type 3 envelope glycoprotein
    • DOI 10.1128/JVI.79.2.1223-1231.2005
    • Modis, Y., S. Ogata, D. Clements, and S. C. Harrison. 2005. Variable surface epitopes in the crystal structure of dengue virus type 3 envelope glycoprotein. J. Virol. 79:1223-1231. (Pubitemid 40053904)
    • (2005) Journal of Virology , vol.79 , Issue.2 , pp. 1223-1231
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 48
    • 0029165107 scopus 로고
    • An investigation of the role of transmembrane domains in Golgi protein retention
    • Munro, S. 1995. An investigation of the role of transmembrane domains in Golgi protein retention. EMBO J. 14:4695-4704.
    • (1995) EMBO J. , vol.14 , pp. 4695-4704
    • Munro, S.1
  • 49
    • 0015909549 scopus 로고
    • Bunyaviridae: Morphologic and morphogenetic similarities of Bunyamwera serologic supergroup viruses and several other arthropod-borne viruses
    • Murphy, F. A., A. K. Harrison, and S. G. Whitfield. 1973. Bunyaviridae: morphologic and morphogenetic similarities of Bunyamwera serologic supergroup viruses and several other arthropod-borne viruses. Intervirology 1:297-316.
    • (1973) Intervirology , vol.1 , pp. 297-316
    • Murphy, F.A.1    Harrison, A.K.2    Whitfield, S.G.3
  • 50
    • 0027530821 scopus 로고
    • Processing of the dengue virus type 2 proteins prM and C-prM
    • Murray, J. M., J. G. Aaskov, and P. J. Wright. 1993. Processing of the dengue virus type 2 proteins prM and C-prM. J. Gen. Virol. 74(Pt 2):175-182.
    • (1993) J. Gen. Virol. , vol.74 , Issue.PART 2 , pp. 175-182
    • Murray, J.M.1    Aaskov, J.G.2    Wright, P.J.3
  • 51
    • 0026072695 scopus 로고
    • The membrane spanning domain of beta-1,4-galactosyltransferase specifies trans Golgi localization
    • Nilsson, T., J. M. Lucocq, D. Mackay, and G. Warren. 1991. The membrane spanning domain of beta-1,4-galactosyltransferase specifies trans Golgi localization. EMBO J. 10:3567-3575. (Pubitemid 21905382)
    • (1991) EMBO Journal , vol.10 , Issue.12 , pp. 3567-3575
    • Nilsson, T.1    Lucocq, J.M.2    Mackay, D.3    Warren, G.4
  • 52
    • 0027318045 scopus 로고
    • Kin recognition. a model for the retention of Golgi enzymes
    • Nilsson, T., P. Slusarewicz, M. H. Hoe, and G. Warren. 1993. Kin recognition. A model for the retention of Golgi enzymes. FEBS Lett. 330:1-4.
    • (1993) FEBS Lett. , vol.330 , pp. 1-4
    • Nilsson, T.1    Slusarewicz, P.2    Hoe, M.H.3    Warren, G.4
  • 53
    • 0037219512 scopus 로고    scopus 로고
    • Role of the transmembrane domains of prM and e proteins in the formation of yellow fever virus envelope
    • DOI 10.1128/JVI.77.2.813-820.2003
    • Op De Beeck, A., R. Molenkamp, M. Caron, A. Ben Younes, P. Bredenbeek, and J. Dubuisson. 2003. Role of the transmembrane domains of prM and E proteins in the formation of yellow fever virus envelope. J. Virol. 77:813-820. (Pubitemid 36055503)
    • (2003) Journal of Virology , vol.77 , Issue.2 , pp. 813-820
    • Op De Beeck, A.O.1    Molenkamp, R.2    Caron, M.3    Younes, A.B.4    Bredenbeek, P.5    Dubuisson, J.6
  • 54
    • 7644232918 scopus 로고    scopus 로고
    • The transmembrane domains of the prM and e proteins of yellow fever virus are endoplasmic reticulum localization signals
    • Op De Beeck, A., Y. Rouille, M. Caron, S. Duvet, and J. Dubuisson. 2004. The transmembrane domains of the prM and E proteins of yellow fever virus are endoplasmic reticulum localization signals. J. Virol. 78:12591-12602.
    • (2004) J. Virol. , vol.78 , pp. 12591-12602
    • Op De Beeck, A.1    Rouille, Y.2    Caron, M.3    Duvet, S.4    Dubuisson, J.5
  • 55
    • 33845439886 scopus 로고    scopus 로고
    • Construction and mutagenesis of an artificial bicistronic tick-borne encephalitis virus genome reveals an essential function of the second transmembrane region of protein e in flavivirus assembly
    • Orlinger, K. K., V. M. Hoenninger, R. M. Kofler, and C. W. Mandl. 2006. Construction and mutagenesis of an artificial bicistronic tick-borne encephalitis virus genome reveals an essential function of the second transmembrane region of protein E in flavivirus assembly. J. Virol. 80:12197-12208.
    • (2006) J. Virol. , vol.80 , pp. 12197-12208
    • Orlinger, K.K.1    Hoenninger, V.M.2    Kofler, R.M.3    Mandl, C.W.4
  • 56
    • 0029163053 scopus 로고
    • Sorting and retrieval between the endoplasmic reticulum and Golgi apparatus
    • Pelham, H. R. 1995. Sorting and retrieval between the endoplasmic reticulum and Golgi apparatus. Curr. Opin. Cell Biol. 7:530-535.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 530-535
    • Pelham, H.R.1
  • 57
    • 13844275217 scopus 로고    scopus 로고
    • Secretion of noninfectious dengue virus-like particles and identification of amino acids in the stem region involved in intracellular retention of envelope protein
    • Purdy, D. E., and G. J. Chang. 2005. Secretion of noninfectious dengue virus-like particles and identification of amino acids in the stem region involved in intracellular retention of envelope protein. Virology 333:239-250.
    • (2005) Virology , vol.333 , pp. 239-250
    • Purd, D.E.1    Chang, G.J.2
  • 58
    • 5444259738 scopus 로고    scopus 로고
    • Noninfectious recombinant antigen for detection of St. Louis encephalitis virus-specific antibodies in serum by enzyme-linked immunosorbent assay
    • Purdy, D. E., A. J. Noga, and G. J. Chang. 2004. Noninfectious recombinant antigen for detection of St. Louis encephalitis virus-specific antibodies in serum by enzyme-linked immunosorbent assay. J. Clin. Microbiol. 42:4709-4717.
    • (2004) J. Clin. Microbiol. , vol.42 , pp. 4709-4717
    • Purdy, D.E.1    Noga, A.J.2    Chang, G.J.3
  • 59
    • 0025064269 scopus 로고
    • Acidotropic amines inhibit proteolytic processing of flavivirus prM protein
    • Randolph, V. B., G. Winkler, and V. Stollar. 1990. Acidotropic amines inhibit proteolytic processing of flavivirus prM protein. Virology 174:450-458.
    • (1990) Virology , vol.174 , pp. 450-458
    • Randolph, V.B.1    Winkler, G.2    Stollar, V.3
  • 60
    • 0030945486 scopus 로고    scopus 로고
    • Transmembrane domain-dependent sorting of proteins to the ER and plasma membrane in yeast
    • Rayner, J. C., and H. R. Pelham. 1997. Transmembrane domain-dependent sorting of proteins to the ER and plasma membrane in yeast. EMBO J. 16:1832-1841.
    • (1997) EMBO J. , vol.16 , pp. 1832-1841
    • Rayner, J.C.1    Pelham, H.R.2
  • 61
    • 0029014434 scopus 로고
    • The envelope glycoprotein from tick-borne encephalitis virus at 2 a resolution
    • Rey, F. A., F. X. Heinz, C. Mandl, C. Kunz, and S. C. Harrison. 1995. The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution. Nature 375:291-298.
    • (1995) Nature , vol.375 , pp. 291-298
    • Rey, F.A.1    Heinz, F.X.2    Mandl, C.3    Kunz, C.4    Harrison, S.C.5
  • 62
    • 0029888374 scopus 로고    scopus 로고
    • Recombinant subviral particles from tick-borne encephalitis virus are fusogenic and provide a model system for studying flavivirus envelope glycoprotein functions
    • Schalich, J., S. L. Allison, K. Stiasny, C. W. Mandl, C. Kunz, and F. X. Heinz. 1996. Recombinant subviral particles from tick-borne encephalitis virus are fusogenic and provide a model system for studying flavivirus envelope glycoprotein functions. J. Virol. 70:4549-4557. (Pubitemid 26187453)
    • (1996) Journal of Virology , vol.70 , Issue.7 , pp. 4549-4557
    • Schalich, J.1    Allison, S.L.2    Stiasny, K.3    Mandl, C.W.4    Kunz, C.5    Heinz, F.X.6
  • 63
    • 0030804183 scopus 로고    scopus 로고
    • Interaction of influenza virus haemagglutinin with sphingolipid- cholesterol membrane domains via its transmembrane domain
    • DOI 10.1093/emboj/16.18.5501
    • Scheiffele, P., M. G. Roth, and K. Simons. 1997. Interaction of influenza virus haemagglutinin with sphingolipid-cholesterol membrane domains via its transmembrane domain. EMBO J. 16:5501-5508. (Pubitemid 27399842)
    • (1997) EMBO Journal , vol.16 , Issue.18 , pp. 5501-5508
    • Scheiffele, P.1    Roth, M.G.2    Simons, K.3
  • 64
    • 0025981099 scopus 로고
    • Signals for retention of transmembrane proteins in the endoplasmic reticulum studied with CD4 truncation mutants
    • Shin, J., R. L. Dunbrack, Jr., S. Lee, and J. L. Strominger. 1991. Signals for retention of transmembrane proteins in the endoplasmic reticulum studied with CD4 truncation mutants. Proc. Natl. Acad. Sci. USA 88:1918-1922.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 1918-1922
    • Shin, J.1    Dunbrack Jr., R.L.2    Lee, S.3    Strominger, J.L.4
  • 65
    • 0030764780 scopus 로고    scopus 로고
    • Proteolytic activation of tick-borne encephalitis virus by furin
    • Stadler, K., S. L. Allison, J. Schalich, and F. X. Heinz. 1997. Proteolytic activation of tick-borne encephalitis virus by furin. J. Virol. 71:8475-8481. (Pubitemid 27446428)
    • (1997) Journal of Virology , vol.71 , Issue.11 , pp. 8475-8481
    • Stadler, K.1    Allison, S.L.2    Schalich, J.3    Heinz, F.X.4
  • 67
    • 0021893229 scopus 로고
    • Infection of AtT20 murine pituitary tumour cells by mouse hepatitis virus strain A59: Virus budding is restricted to the Golgi region
    • Tooze, J., and S. A. Tooze. 1985. Infection of AtT20 murine pituitary tumour cells by mouse hepatitis virus strain A59: virus budding is restricted to the Golgi region. Eur. J. Cell Biol. 37:203-212.
    • (1985) Eur. J. Cell Biol. , vol.37 , pp. 203-212
    • Tooze, J.1    Tooze, S.A.2
  • 68
    • 0031564073 scopus 로고    scopus 로고
    • Ultrastructure and localization of e proteins in cultured neuron cells infected with Japanese encephalitis virus
    • Wang, J. J., C. L. Liao, Y. W. Chiou, C. T. Chiou, Y. L. Huang, and L. K. Chen. 1997. Ultrastructure and localization of E proteins in cultured neuron cells infected with Japanese encephalitis virus. Virology 238:30-39.
    • (1997) Virology , vol.238 , pp. 30-39
    • Wang, J.J.1    Liao, C.L.2    Chiou, Y.W.3    Chiou, C.T.4    Huang, Y.L.5    Chen, L.K.6
  • 69
    • 0033053594 scopus 로고    scopus 로고
    • PrM- And cell-binding domains of the dengue virus e protein
    • Wang, S., R. He, and R. Anderson. 1999. PrM- and cell-binding domains of the dengue virus E protein. J. Virol. 73:2547-2551. (Pubitemid 29098163)
    • (1999) Journal of Virology , vol.73 , Issue.3 , pp. 2547-2551
    • Wang, S.1    He, R.2    Anderson, R.3
  • 72
    • 0031028166 scopus 로고    scopus 로고
    • The transmembrane domain of a carboxyl-terminal anchored protein determines localization to the endoplasmic reticulum
    • Yang, M., J. Ellenberg, J. S. Bonifacino, and A. M. Weissman. 1997. The transmembrane domain of a carboxyl-terminal anchored protein determines localization to the endoplasmic reticulum. J. Biol. Chem. 272:1970-1975.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1970-1975
    • Yang, M.1    Ellenberg, J.2    Bonifacino, J.S.3    Weissman, A.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.