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Volumn 85, Issue 10, 2011, Pages 5159-5171

The helical domains of the stem region of dengue virus envelope protein are involved in both virus assembly and entry

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ENVELOPE PROTEIN; PROLINE;

EID: 79955417646     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02099-10     Document Type: Article
Times cited : (49)

References (61)
  • 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
    • 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.
    • (1998) J. Virol. , vol.72 , pp. 1647-1651
    • Bray, M.1    Men, R.2    Tokimatsu, I.3    Lai, C.J.4
  • 3
    • 1842526097 scopus 로고    scopus 로고
    • Structure of a flavivirus envelope glycoprotein in its low-pH-induced membrane fusion conformation
    • Bressanelli, S., et al. 2004. Structure of a flavivirus envelope glycoprotein in its low-pH-induced membrane fusion conformation. EMBO J. 23:728-738.
    • (2004) EMBO J , vol.23 , pp. 728-738
    • Bressanelli, S.1
  • 4
    • 0037294732 scopus 로고    scopus 로고
    • Enhancing biosynthesis and secretion of premem-brane and envelope proteins by the chimeric plasmid of dengue virus type 2 and Japanese encephalitis virus
    • Chang, G. J., et al. 2003. Enhancing biosynthesis and secretion of premem-brane 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
  • 5
    • 0034812854 scopus 로고    scopus 로고
    • Cellular membrane-binding ability of the C-terminal cytoplasmic domain of human immunodeficiency virus type 1 envelope transmembrane protein gp41
    • Chen, S. S., S. F. Lee, and C. T. Wang. 2001. Cellular membrane-binding ability of the C-terminal cytoplasmic domain of human immunodeficiency virus type 1 envelope transmembrane protein gp41. J. Virol. 75:9925-9938.
    • (2001) J. Virol. , vol.75 , pp. 9925-9938
    • Chen, S.S.1    Lee, S.F.2    Wang, C.T.3
  • 6
    • 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., et al. 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
  • 7
    • 0035265843 scopus 로고    scopus 로고
    • Molecular organization of a recombinant subviral particle from tick-borne encephalitis virus
    • Ferlenghi, I., et al. 2001. Molecular organization of a recombinant subviral particle from tick-borne encephalitis virus. Mol. Cell 7:593-602.
    • (2001) Mol. Cell , vol.7 , pp. 593-602
    • Ferlenghi, I.1
  • 8
    • 0042709368 scopus 로고    scopus 로고
    • Incorporation of tick-borne encephalitis virus repli-cons into virus-like particles by a packaging cell line
    • Gehrke, R., et al. 2003. Incorporation of tick-borne encephalitis virus repli-cons into virus-like particles by a packaging cell line. J. Virol. 77:8924-8933.
    • (2003) J. Virol. , vol.77 , pp. 8924-8933
    • Gehrke, R.1
  • 9
    • 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
  • 10
    • 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
  • 11
    • 0027169938 scopus 로고
    • Selection and partial characterization of dengue 2 virus mutants that induce fusion at elevated pH
    • Guirakhoo, F., A. R. Hunt, J. G. Lewis, and J. T. Roehrig. 1993. Selection and partial characterization of dengue 2 virus mutants that induce fusion at elevated pH. Virology 194:219-223.
    • (1993) Virology , vol.194 , pp. 219-223
    • Guirakhoo, F.1    Hunt, A.R.2    Lewis, J.G.3    Roehrig, J.T.4
  • 13
    • 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
  • 14
    • 23744446349 scopus 로고    scopus 로고
    • Peptide inhibitors of dengue virus and West Nile virus infectivity
    • Hrobowski, Y. M., R. F. Garry, and S. F. Michael. 2005. Peptide inhibitors of dengue virus and West Nile virus infectivity. Virol. J. 2:49.
    • (2005) Virol. J. , vol.2 , pp. 49
    • Hrobowski, Y.M.1    Garry, R.F.2    Michael, S.F.3
  • 15
    • 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
  • 16
    • 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
  • 17
    • 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
  • 18
    • 11344251060 scopus 로고    scopus 로고
    • Construction and applications of yellow fever virus replicons
    • Jones, C. T., C. G. Patkar, and R. J. Kuhn. 2005. Construction and applications of yellow fever virus replicons. Virology 331:247-259.
    • (2005) Virology , vol.331 , pp. 247-259
    • Jones, C.T.1    Patkar, C.G.2    Kuhn, R.J.3
  • 19
    • 73549095327 scopus 로고    scopus 로고
    • Capturing a flavivirus pre-fusion intermediate
    • Kaufmann, B., et al. 2009. Capturing a flavivirus pre-fusion intermediate. PLoS Pathog. 5:e1000672.
    • (2009) PLoS Pathog , vol.5
    • Kaufmann, B.1
  • 20
    • 10744223893 scopus 로고    scopus 로고
    • Alterations of pr-M cleavage and virus export in pr-M junction chimeric dengue viruses
    • Keelapang, P., et al. 2004. Alterations of pr-M cleavage and virus export in pr-M junction chimeric dengue viruses. J. Virol. 78:2367-2381.
    • (2004) J. Virol. , vol.78 , pp. 2367-2381
    • Keelapang, P.1
  • 21
    • 0031798576 scopus 로고    scopus 로고
    • Encapsidation of the flavivirus Kunjin replicon RNA by using a complementation system providing Kunjin virus structural proteins in trans
    • Khromykh, A. A., A. N. Varnavski, and E. G. Westaway. 1998. Encapsidation of the flavivirus Kunjin replicon RNA by using a complementation system providing Kunjin virus structural proteins in trans. J. Virol. 72:5967-5977.
    • (1998) J. Virol. , vol.72 , pp. 5967-5977
    • Khromykh, A.A.1    Varnavski, A.N.2    Westaway, E.G.3
  • 22
    • 31344432402 scopus 로고    scopus 로고
    • Virus membrane-fusion proteins: More than one way to make a hairpin
    • Kielian, M., and F. A. Rey. 2006. Virus membrane-fusion proteins: more than one way to make a hairpin. Nat. Rev. Microbiol. 4:67-76.
    • (2006) Nat. Rev. Microbiol. , vol.4 , pp. 67-76
    • Kielian, M.1    Rey, F.A.2
  • 23
    • 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
    • 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.
    • (2002) Vaccine , vol.20 , pp. 1058-1067
    • Konishi, E.1    Fujii, A.2
  • 24
    • 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
  • 25
    • 26444506252 scopus 로고    scopus 로고
    • Domain III from class II fusion proteins function as a dominant-negative inhibitor of virus membrane fusion
    • Liao, M., and M. Kielian. 2005. Domain III from class II fusion proteins function as a dominant-negative inhibitor of virus membrane fusion. J. Cell Biol. 171:111-120.
    • (2005) J. Cell Biol. , vol.171 , pp. 111-120
    • Liao, M.1    Kielian, M.2
  • 26
    • 34748873170 scopus 로고    scopus 로고
    • Flaviviridae: The viruses and their replication
    • D. M. Knipe and P. M. Howley (ed.), Lippincott Williams & 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 Williams & Wilkins, Philadelphia, PA.
    • (2007) Fields virology , pp. 1101-1152
    • Lindenbach, B.D.1    Thiel, H.J.2    Rice, C.M.3
  • 27
    • 0141570502 scopus 로고    scopus 로고
    • Functional analysis of mosquito-borne flavivirus conserved sequence elements within 3' untranslated region of West Nile virus by use of a reporting replicon that differentiates between viral translation and RNA replication
    • Lo, M. K., M. Tilgner, K. A. Bernard, and P. Y. Shi. 2003. Functional analysis of mosquito-borne flavivirus conserved sequence elements within 3' untranslated region of West Nile virus by use of a reporting replicon that differentiates between viral translation and RNA replication. J. Virol. 77:10004-10014.
    • (2003) J. Virol. , vol.77 , pp. 10004-10014
    • Lo, M.K.1    Tilgner, M.2    Bernard, K.A.3    Shi, P.Y.4
  • 28
    • 0037378495 scopus 로고    scopus 로고
    • Intracellular assembly and secretion of recombinant subviral particles from tick-borne encephalitis virus
    • Lorenz, I. C, et al. 2003. Intracellular assembly and secretion of recombinant subviral particles from tick-borne encephalitis virus. J. Virol. 77:4370-4382.
    • (2003) J. Virol. , vol.77 , pp. 4370-4382
    • Lorenz, I.C.1
  • 29
    • 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
  • 30
    • 39149128276 scopus 로고    scopus 로고
    • A West Nile virus DNA vaccine induces neutralizing antibody in healthy adults during a phase 1 clinical trial
    • Martin, J. E., et al. 2007. A West Nile virus DNA vaccine induces neutralizing antibody in healthy adults during a phase 1 clinical trial. J. Infect. Dis. 196:1732-1740.
    • (2007) J. Infect. Dis. , vol.196 , pp. 1732-1740
    • Martin, J.E.1
  • 32
    • 1642499388 scopus 로고    scopus 로고
    • Structure of the dengue virus envelope protein after membrane fusion
    • Modis, Y., S. Ogata, D. Clements, and S. C. Harrison. 2004. Structure of the dengue virus envelope protein after membrane fusion. Nature 427:313-319.
    • (2004) Nature , vol.427 , pp. 313-319
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 33
    • 11144244755 scopus 로고    scopus 로고
    • Variable surface epitopes in the crystal structure of dengue virus type 3 envelope glycoprotein
    • 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.
    • (2005) J. Virol. , vol.79 , pp. 1223-1231
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 35
    • 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
  • 36
    • 0037219512 scopus 로고    scopus 로고
    • Role of the transmembrane domains of prM and E proteins in the formation of yellow fever virus envelope
    • Op De Beeck, A., et al. 2003. Role of the transmembrane domains of prM and E proteins in the formation of yellow fever virus envelope. J. Virol. 77:813-820.
    • (2003) J. Virol. , vol.77 , pp. 813-820
    • Op De Beeck, A.1
  • 37
    • 33845439886 scopus 로고    scopus 로고
    • Construction and mutagenesis of an artificial bicistronic tick-borne encephalitis virus genome reveals an essential function of the second transmem-brane 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 transmem-brane 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
  • 38
    • 32844457056 scopus 로고    scopus 로고
    • A rapid and quantitative assay for measuring antibody-mediated neutralization of West Nile virus infection
    • Pierson, T. C., et al. 2006. A rapid and quantitative assay for measuring antibody-mediated neutralization of West Nile virus infection. Virology 346: 53-65.
    • (2006) Virology , vol.346 , pp. 53-65
    • Pierson, T.C.1
  • 39
    • 70449521008 scopus 로고    scopus 로고
    • A small molecule fusion inhibitor of dengue virus
    • Poh, M. K., et al. 2009. A small molecule fusion inhibitor of dengue virus. Antiviral Res. 84:260-266.
    • (2009) Antiviral Res , vol.84 , pp. 260-266
    • Poh, M.K.1
  • 40
    • 28844486636 scopus 로고    scopus 로고
    • High-throughput assays using luciferase-expressing replicon, virus-like particle, and full-length virus for West Nile virus drug discovery
    • Puig-Basagoiti, F., et al. 2005. High-throughput assays using luciferase-expressing replicon, virus-like particle, and full-length virus for West Nile virus drug discovery. Antimicrob. Agents Chemother. 49:4980-4988.
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 4980-4988
    • Puig-Basagoiti, F.1
  • 41
    • 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
  • 42
    • 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
    • Purdy, D.E.1    Chang, G.J.2
  • 43
    • 77951298609 scopus 로고    scopus 로고
    • A high-throughput assay using dengue-1 virus-like particles for drug discovery
    • Qing, M., W. Liu, Z. Yuan, F. Gu, and P. Y. Shi. 2010. A high-throughput assay using dengue-1 virus-like particles for drug discovery. Antiviral Res. 86:163-171.
    • (2010) Antiviral Res , vol.86 , pp. 163-171
    • Qing, M.1    Liu, W.2    Yuan, Z.3    Gu, F.4    Shi, P.Y.5
  • 44
    • 0025030596 scopus 로고
    • Low pH-induced cell fusion in flavi-virus-infected Aedes albopictus cell cultures
    • Randolph, V. B., and V. Stollar. 1990. Low pH-induced cell fusion in flavi-virus-infected Aedes albopictus cell cultures. J. Gen. Virol. 71:1845-1850.
    • (1990) J. Gen. Virol. , vol.71 , pp. 1845-1850
    • Randolph, V.B.1    Stollar, V.2
  • 45
    • 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
  • 46
    • 0002315081 scopus 로고
    • Chemical and antigenic structure of flaviviruses
    • R. W. Schlesinger (ed.), Academic Press, New York, NY
    • Russell, P. K., W. E. Brandt, and J. M. Dalrymple. 1980. Chemical and antigenic structure of flaviviruses, p. 503-529. In R. W. Schlesinger (ed.), The togaviruses. Academic Press, New York, NY.
    • (1980) The togaviruses , pp. 503-529
    • Russell, P.K.1    Brandt, W.E.2    Dalrymple, J.M.3
  • 47
    • 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., et al. 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.
    • (1996) J. Virol. , vol.70 , pp. 4549-4557
    • Schalich, J.1
  • 48
    • 77954044356 scopus 로고    scopus 로고
    • Peptide inhibitors of dengue-virus entry target a late-stage fusion intermediate
    • Schmidt, A. G., P. L. Yang, and S. C. Harrison. 2010. Peptide inhibitors of dengue-virus entry target a late-stage fusion intermediate. PLoS Pathog. 6:e1000851.
    • (2010) PLoS Pathog , vol.6
    • Schmidt, A.G.1    Yang, P.L.2    Harrison, S.C.3
  • 49
    • 6344284698 scopus 로고    scopus 로고
    • Trans-packaged West Nile virus-like particles: Infectious properties in vitro and in infected mosquito vectors
    • Scholle, F., Y. A. Girard, Q. Zhao, S. Higgs, and P. W. Mason. 2004. Trans-packaged West Nile virus-like particles: infectious properties in vitro and in infected mosquito vectors. J. Virol. 78:11605-11614.
    • (2004) J. Virol. , vol.78 , pp. 11605-11614
    • Scholle, F.1    Girard, Y.A.2    Zhao, Q.3    Higgs, S.4    Mason, P.W.5
  • 50
    • 0036107695 scopus 로고    scopus 로고
    • Infectious cDNA clone of the epidemic West Nile virus from New York City
    • Shi, P. Y., M. Tilgner, M. K. Lo, K. A. Kent, and K. A. Bernard. 2002. Infectious cDNA clone of the epidemic West Nile virus from New York City. J. Virol. 76:5847-5856.
    • (2002) J. Virol. , vol.76 , pp. 5847-5856
    • Shi, P.Y.1    Tilgner, M.2    Lo, M.K.3    Kent, K.A.4    Bernard, K.A.5
  • 51
    • 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. U. S. A. 88:1918-1922.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 1918-1922
    • Shin, J.1    Dunbrack Jr., R.L.2    Lee, S.3    Strominger, J.L.4
  • 52
    • 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.
    • (1997) J. Virol. , vol.71 , pp. 8475-8481
    • Stadler, K.1    Allison, S.L.2    Schalich, J.3    Heinz, F.X.4
  • 53
    • 0029795282 scopus 로고    scopus 로고
    • Structural requirements for low-pH-induced rearrangements in the envelope glycoprotein of tick-borne encephalitis virus
    • Stiasny, K., S. L. Allison, A. Marchler-Bauer, C. Kunz, and F. X. Heinz. 1996. Structural requirements for low-pH-induced rearrangements in the envelope glycoprotein of tick-borne encephalitis virus. J. Virol. 70:8142- 8147.
    • (1996) J. Virol. , vol.70 , pp. 8142-8147
    • Stiasny, K.1    Allison, S.L.2    Marchler-Bauer, A.3    Kunz, C.4    Heinz, F.X.5
  • 54
    • 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.
    • (1999) J. Virol. , vol.73 , pp. 2547-2551
    • Wang, S.1    He, R.2    Anderson, R.3
  • 55
    • 33750295473 scopus 로고    scopus 로고
    • Slower rates of clearance of viral load and virus-containing immune complexes in patients with dengue hemorrhagic fever
    • Wang, W. K., et al. 2006. Slower rates of clearance of viral load and virus-containing immune complexes in patients with dengue hemorrhagic fever. Clin. Infect. Dis. 43:1023-1030.
    • (2006) Clin. Infect. Dis. , vol.43 , pp. 1023-1030
    • Wang, W.K.1
  • 56
    • 64649097038 scopus 로고    scopus 로고
    • Composition and three-dimensional architecture of the dengue virus replication and assembly sites
    • Welsch, S., et al. 2009. Composition and three-dimensional architecture of the dengue virus replication and assembly sites. Cell Host Microbe 5:365- 375.
    • (2009) Cell Host Microbe , vol.5 , pp. 365-375
    • Welsch, S.1
  • 57
    • 0012615362 scopus 로고    scopus 로고
    • World Health Organization, Fact sheet no. 117. World Health Organization, Geneva, Switzerland
    • World Health Organization. 2009. Dengue and dengue hemorrhagic fever. Fact sheet no. 117. World Health Organization, Geneva, Switzerland. http://www.who.int/mediacentre/factsheets/fs117/en.
    • (2009) Dengue and dengue hemorrhagic fever
  • 58
    • 0030974503 scopus 로고    scopus 로고
    • Formation of intracellular particles by hepatitis B virus large surface protein
    • Xu, Z., V. Bruss, and T. S. Yen. 1997. Formation of intracellular particles by hepatitis B virus large surface protein. J. Virol. 71:5487-5494.
    • (1997) J. Virol. , vol.71 , pp. 5487-5494
    • Xu, Z.1    Bruss, V.2    Yen, T.S.3
  • 59
    • 41349112304 scopus 로고    scopus 로고
    • Structure of the immature dengue virus at low pH primes proteolytic maturation
    • Yu, I. M., et al. 2008. Structure of the immature dengue virus at low pH primes proteolytic maturation. Science 319:1834-1837.
    • (2008) Science , vol.319 , pp. 1834-1837
    • Yu, I.M.1
  • 60
    • 0242574743 scopus 로고    scopus 로고
    • Visualization of membrane protein domains by cryo-electron microscopy of dengue virus
    • Zhang, W., et al. 2003. Visualization of membrane protein domains by cryo-electron microscopy of dengue virus. Nat. Struct. Biol. 10:907-912.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 907-912
    • Zhang, W.1
  • 61
    • 4444338894 scopus 로고    scopus 로고
    • Conformational changes of the flavivirus E glycoprotein
    • Zhang, Y., et al. 2004. Conformational changes of the flavivirus E glycoprotein. Structure 12:1607-1618.
    • (2004) Structure , vol.12 , pp. 1607-1618
    • Zhang, Y.1


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