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Volumn 79, Issue 19, 2005, Pages 12132-12147

Stoichiometry of envelope glycoprotein trimers in the entry of human immunodeficiency virus type 1

Author keywords

[No Author keywords available]

Indexed keywords

CD4 ANTIGEN; CHEMOKINE RECEPTOR CCR5; CHEMOKINE RECEPTOR CXCR4; VIRUS ENVELOPE PROTEIN; VIRUS GLYCOPROTEIN; VIRUS HEMAGGLUTININ;

EID: 25144500649     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.79.19.12132-12147.2005     Document Type: Article
Times cited : (139)

References (128)
  • 1
    • 0030018156 scopus 로고    scopus 로고
    • CC CKR5: A RANTES, MIP-1alpha, MIP-1beta receptor as a fusion cofactor for macrophage-tropic HIV-1
    • Alkhatib, G., C. Combadiere, C. C. Broder, Y. Feng, P. E. Kennedy, P. M. Murphy, and E. A. Berger. 1996. CC CKR5: a RANTES, MIP-1alpha, MIP-1beta receptor as a fusion cofactor for macrophage-tropic HIV-1. Science 272:1955-1958.
    • (1996) Science , vol.272 , pp. 1955-1958
    • Alkhatib, G.1    Combadiere, C.2    Broder, C.C.3    Feng, Y.4    Kennedy, P.E.5    Murphy, P.M.6    Berger, E.A.7
  • 2
    • 0034120341 scopus 로고    scopus 로고
    • Membrane fusion mediated by coiled coils: A hypothesis
    • Bentz, J. 2000. Membrane fusion mediated by coiled coils: a hypothesis. Biophys. J. 78:886-900.
    • (2000) Biophys. J. , vol.78 , pp. 886-900
    • Bentz, J.1
  • 3
    • 0034031590 scopus 로고    scopus 로고
    • Minimal aggregate size and minimal fusion unit for the first fusion pore of influenza hemagglutinin-mediated membrane fusion
    • Bentz, J. 2000. Minimal aggregate size and minimal fusion unit for the first fusion pore of influenza hemagglutinin-mediated membrane fusion. Biophys. J. 78:227-245.
    • (2000) Biophys. J. , vol.78 , pp. 227-245
    • Bentz, J.1
  • 4
    • 0038148746 scopus 로고    scopus 로고
    • Architecture of the influenza hemagglutinin membrane fusion site
    • Bentz, J., and A. Mittal. 2003. Architecture of the influenza hemagglutinin membrane fusion site. Biochim. Biophys. Acta 1614:24-35.
    • (2003) Biochim. Biophys. Acta , vol.1614 , pp. 24-35
    • Bentz, J.1    Mittal, A.2
  • 5
  • 6
    • 0029823936 scopus 로고    scopus 로고
    • Dilation of the influenza hemagglutinin fusion pore revealed by the kinetics of individual cell-cell fusion events
    • Blumenthal, R., D. P. Sarkar, S. Durell, D. E. Howard, and S. J. Morris. 1996. Dilation of the influenza hemagglutinin fusion pore revealed by the kinetics of individual cell-cell fusion events. J. Cell Biol. 135:63-71.
    • (1996) J. Cell Biol. , vol.135 , pp. 63-71
    • Blumenthal, R.1    Sarkar, D.P.2    Durell, S.3    Howard, D.E.4    Morris, S.J.5
  • 7
    • 0023868788 scopus 로고
    • Posttranslational oligomerization and cooperative acid activation of fixed influenza hemagglutinin trimers
    • Boulay, F., R. W. Doms, R. G. Webster, and A. Helenius. 1988. Posttranslational oligomerization and cooperative acid activation of fixed influenza hemagglutinin trimers. J. Cell Biol. 106:629-639.
    • (1988) J. Cell Biol. , vol.106 , pp. 629-639
    • Boulay, F.1    Doms, R.W.2    Webster, R.G.3    Helenius, A.4
  • 8
    • 0028372046 scopus 로고
    • The ratio of defective HIV-1 particles to replication-competent infectious virions
    • Bourinbaiar, A. S. 1994. The ratio of defective HIV-1 particles to replication-competent infectious virions. Acta Virol. 38:59-61.
    • (1994) Acta Virol. , vol.38 , pp. 59-61
    • Bourinbaiar, A.S.1
  • 9
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough, P. A., F. M. Hughson, J. J. Skehel, and D. C. Wiley. 1994. Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 371:37-43.
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 10
    • 2942720886 scopus 로고    scopus 로고
    • HIV-1 assembly and maturation
    • Bukrinskaya, A. G. 2004. HIV-1 assembly and maturation. Arch. Virol. 149:1067-1082.
    • (2004) Arch. Virol. , vol.149 , pp. 1067-1082
    • Bukrinskaya, A.G.1
  • 11
    • 0028300968 scopus 로고
    • Changes in the cytopathic effects of human immunodeficiency virus type 1 associated with a single amino acid alteration in the ectodomain of the gp41 transmembrane glycoprotein
    • Cao, J., B. Vasir, and J. G. Sodroski. 1994. Changes in the cytopathic effects of human immunodeficiency virus type 1 associated with a single amino acid alteration in the ectodomain of the gp41 transmembrane glycoprotein. J. Virol. 68:4662-4668.
    • (1994) J. Virol. , vol.68 , pp. 4662-4668
    • Cao, J.1    Vasir, B.2    Sodroski, J.G.3
  • 12
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan, D. C., D. Fass, J. M. Berger, and P. S. Kim. 1997. Core structure of gp41 from the HIV envelope glycoprotein. Cell 89:263-273.
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 13
    • 0032577550 scopus 로고    scopus 로고
    • HIV entry and its inhibition
    • Chan, D. C., and P. S. Kim. 1998. HIV entry and its inhibition. Cell 93:681-684.
    • (1998) Cell , vol.93 , pp. 681-684
    • Chan, D.C.1    Kim, P.S.2
  • 14
    • 0032559801 scopus 로고    scopus 로고
    • The pathway of membrane fusion catalyzed by influenza hemagglutinin: Restriction of lipids, hemifusion, and lipidic fusion pore formation
    • Chernomordik, L. V., V. A. Frolov, E. Leikina, P. Bronk, and J. Zimmerberg. 1998. The pathway of membrane fusion catalyzed by influenza hemagglutinin: restriction of lipids, hemifusion, and lipidic fusion pore formation. J. Cell Biol. 140:1369-1382.
    • (1998) J. Cell Biol. , vol.140 , pp. 1369-1382
    • Chernomordik, L.V.1    Frolov, V.A.2    Leikina, E.3    Bronk, P.4    Zimmerberg, J.5
  • 15
    • 0036091692 scopus 로고    scopus 로고
    • Envelope glycoprotein incorporation, not shedding of surface envelope glycoprotein (gp120/SU), is the primary determinant of SU content of purified human immunodeficiency virus type 1 and simian immunodeficiency virus
    • Chertova, E., J. W. Bess Jr., Jr., B. J. Crise, I. R. Sowder, T. M. Schaden, J. M. Hilburn, J. A. Hoxie, R. E. Benveniste, J. D. Lifson, L. E. Henderson, and L. O. Arthur. 2002. Envelope glycoprotein incorporation, not shedding of surface envelope glycoprotein (gp120/SU), is the primary determinant of SU content of purified human immunodeficiency virus type 1 and simian immunodeficiency virus. J. Virol. 76:5315-5325.
    • (2002) J. Virol. , vol.76 , pp. 5315-5325
    • Chertova, E.1    Bess Jr., J.W.2    Crise, B.J.3    Sowder, I.R.4    Schaden, T.M.5    Hilburn, J.M.6    Hoxie, J.A.7    Benveniste, R.E.8    Lifson, J.D.9    Henderson, L.E.10    Arthur, L.O.11
  • 16
    • 0030980295 scopus 로고    scopus 로고
    • The amphotropic murine leukemia virus receptor gene encodes a 71-kilodalton protein that is induced by phosphate depletion
    • Chien, M. L., J. L. Foster, J. L. Douglas, and J. V. Garcia. 1997. The amphotropic murine leukemia virus receptor gene encodes a 71-kilodalton protein that is induced by phosphate depletion. J. Virol. 71:4564-4570.
    • (1997) J. Virol. , vol.71 , pp. 4564-4570
    • Chien, M.L.1    Foster, J.L.2    Douglas, J.L.3    Garcia, J.V.4
  • 18
    • 0037381269 scopus 로고    scopus 로고
    • The structural biology of type I viral membrane fusion
    • Colman, P. M., and M. C. Lawrence. 2003. The structural biology of type I viral membrane fusion. Nat. Rev. Mol. Cell Biol. 4:309-319.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 309-319
    • Colman, P.M.1    Lawrence, M.C.2
  • 19
    • 0021751840 scopus 로고
    • The CD4 (T4) antigen is an essential component of the receptor for the AIDS retrovirus
    • Dalgleish, A. G., P. C. Beverley, P. R. Clapham, D. H. Crawford, M. F. Greaves, and R. A. Weiss. 1984. The CD4 (T4) antigen is an essential component of the receptor for the AIDS retrovirus. Nature 312:763-767.
    • (1984) Nature , vol.312 , pp. 763-767
    • Dalgleish, A.G.1    Beverley, P.C.2    Clapham, P.R.3    Crawford, D.H.4    Greaves, M.F.5    Weiss, R.A.6
  • 20
    • 0029898564 scopus 로고    scopus 로고
    • Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers
    • Danieli, T, S. L. Pelletier, Y. I. Henis, and J. M. White. 1996. Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers. J. Cell Biol. 133:559-569.
    • (1996) J. Cell Biol. , vol.133 , pp. 559-569
    • Danieli, T.1    Pelletier, S.L.2    Henis, Y.I.3    White, J.M.4
  • 22
    • 1842612607 scopus 로고    scopus 로고
    • Virus entry: Molecular mechanisms and biomedical applications
    • Dimitrov, D. S. 2004. Virus entry: molecular mechanisms and biomedical applications. Nat. Rev. Microbiol. 2:109-122.
    • (2004) Nat. Rev. Microbiol. , vol.2 , pp. 109-122
    • Dimitrov, D.S.1
  • 23
    • 0025286391 scopus 로고
    • Human immunodeficiency virus types 1 and 2 and simian immunodeficiency virus env proteins possess a functionally conserved assembly domain
    • Doms, R. W., P. L. Earl, S. Chakrabarti, and B. Moss. 1990. Human immunodeficiency virus types 1 and 2 and simian immunodeficiency virus env proteins possess a functionally conserved assembly domain. J. Virol. 64:3537-3540.
    • (1990) J. Virol. , vol.64 , pp. 3537-3540
    • Doms, R.W.1    Earl, P.L.2    Chakrabarti, S.3    Moss, B.4
  • 24
    • 0023033443 scopus 로고
    • Quaternary structure of influenza virus hemagglutinin after acid treatment
    • Doms, R. W., and A. Helenius. 1986. Quaternary structure of influenza virus hemagglutinin after acid treatment. J. Virol. 60:833-839.
    • (1986) J. Virol. , vol.60 , pp. 833-839
    • Doms, R.W.1    Helenius, A.2
  • 25
    • 0030604727 scopus 로고    scopus 로고
    • A dual-tropic primary HIV-1 isolate that uses fusin and the beta-chemokine receptors CKR-5, CKR-3, and CKR-2b as fusion cofactors
    • Doranz, B. J., J. Rucker, Y. Yi, R. J. Smyth, M. Samson, S. C. Peiper, M. Parmentier, R. G. Collman, and R. W. Doms. 1996. A dual-tropic primary HIV-1 isolate that uses fusin and the beta-chemokine receptors CKR-5, CKR-3, and CKR-2b as fusion cofactors. Cell 85:1149-1158.
    • (1996) Cell , vol.85 , pp. 1149-1158
    • Doranz, B.J.1    Rucker, J.2    Yi, Y.3    Smyth, R.J.4    Samson, M.5    Peiper, S.C.6    Parmentier, M.7    Collman, R.G.8    Doms, R.W.9
  • 26
    • 0029015314 scopus 로고
    • Analysis of the cleavage site of the human immunodeficiency virus type 1 glycoprotein: Requirement of precursor cleavage for glycoprotein incorporation
    • Dubay, J. W., S. R. Dubay, H. J. Shin, and E. Hunter. 1995. Analysis of the cleavage site of the human immunodeficiency virus type 1 glycoprotein: requirement of precursor cleavage for glycoprotein incorporation. J. Virol. 69:4675-4682.
    • (1995) J. Virol. , vol.69 , pp. 4675-4682
    • Dubay, J.W.1    Dubay, S.R.2    Shin, H.J.3    Hunter, E.4
  • 27
    • 0031664797 scopus 로고    scopus 로고
    • Membrane fusion promoted by increasing surface densities of the paramyxovirus F and HN proteins: Comparison of fusion reactions mediated by simian virus 5 F, human parainfluenza virus type 3 F, and influenza virus HA
    • Dutch, R. E., S. B. Joshi, and R. A. Lamb. 1998. Membrane fusion promoted by increasing surface densities of the paramyxovirus F and HN proteins: comparison of fusion reactions mediated by simian virus 5 F, human parainfluenza virus type 3 F, and influenza virus HA. J. Virol. 72:7745-7753.
    • (1998) J. Virol. , vol.72 , pp. 7745-7753
    • Dutch, R.E.1    Joshi, S.B.2    Lamb, R.A.3
  • 28
    • 0026029621 scopus 로고
    • Folding, interaction with GRP78-BiP, assembly, and transport of the human immunodeficiency virus type 1 envelope protein
    • Earl, P. L., B. Moss, and R. W. Doms. 1991. Folding, interaction with GRP78-BiP, assembly, and transport of the human immunodeficiency virus type 1 envelope protein. J. Virol. 65:2047-2055.
    • (1991) J. Virol. , vol.65 , pp. 2047-2055
    • Earl, P.L.1    Moss, B.2    Doms, R.W.3
  • 29
    • 0037370724 scopus 로고    scopus 로고
    • The avian retrovirus avian sarcoma/leukosis virus subtype a reaches the lipid mixing stage of fusion at neutral pH
    • Earp, L. J., S. E. Delos, R. C. Netter, P. Bates, and J. M. White. 2003. The avian retrovirus avian sarcoma/leukosis virus subtype A reaches the lipid mixing stage of fusion at neutral pH. J. Virol. 77:3058-3066.
    • (2003) J. Virol. , vol.77 , pp. 3058-3066
    • Earp, L.J.1    Delos, S.E.2    Netter, R.C.3    Bates, P.4    White, J.M.5
  • 31
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • Eckert, D. M., and P. S. Kim. 2001. Mechanisms of viral membrane fusion and its inhibition. Annu. Rev. Biochem. 70:777-810.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 32
    • 0025109728 scopus 로고
    • Fusion of influenza hemagglutinin-expressing fibroblasts with glycophorin-bearing liposomes: Role of hemagglutinin surface density
    • Ellens, H., J. Bentz, D. Mason, F. Zhang, and J. M. White. 1990. Fusion of influenza hemagglutinin-expressing fibroblasts with glycophorin-bearing liposomes: role of hemagglutinin surface density. Biochemistry 29:9697-9707.
    • (1990) Biochemistry , vol.29 , pp. 9697-9707
    • Ellens, H.1    Bentz, J.2    Mason, D.3    Zhang, F.4    White, J.M.5
  • 33
    • 0030002637 scopus 로고    scopus 로고
    • HIV-1 entry cofactor: Functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor
    • Feng, Y., C. C. Broder, P. E. Kennedy, and E. A. Berger. 1996. HIV-1 entry cofactor: functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor. Science 272:872-877.
    • (1996) Science , vol.272 , pp. 872-877
    • Feng, Y.1    Broder, C.C.2    Kennedy, P.E.3    Berger, E.A.4
  • 34
    • 0030894767 scopus 로고    scopus 로고
    • Host-derived ICAM-1 glycoproteins incorporated on human immunodeficiency virus type 1 are biologically active and enhance viral infectivity
    • Fortin, J. F., R. Cantin, G. Lamontagne, and M. Tremblay. 1997. Host-derived ICAM-1 glycoproteins incorporated on human immunodeficiency virus type 1 are biologically active and enhance viral infectivity. J. Virol. 71:3588-3596.
    • (1997) J. Virol. , vol.71 , pp. 3588-3596
    • Fortin, J.F.1    Cantin, R.2    Lamontagne, G.3    Tremblay, M.4
  • 35
    • 0026544416 scopus 로고
    • A mutation in the human immunodeficiency virus type 1 transmembrane glycoprotein gp41 dominantly interferes with fusion and infectivity
    • Freed, E. O., E. L. Delwart, G. L. Buchschacher, Jr., and A. T. Panganiban. 1992. A mutation in the human immunodeficiency virus type 1 transmembrane glycoprotein gp41 dominantly interferes with fusion and infectivity. Proc. Natl. Acad. Sci. USA 89:70-74.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 70-74
    • Freed, E.O.1    Delwart, E.L.2    Buchschacher Jr., G.L.3    Panganiban, A.T.4
  • 36
    • 0028819071 scopus 로고
    • Virion incorporation of envelope glycoproteins with long but not short cytoplasmic tails is blocked by specific, single amino acid substitutions in the human immunodeficiency virus type 1 matrix
    • Freed, E. O., and M. A. Martin. 1995. Virion incorporation of envelope glycoproteins with long but not short cytoplasmic tails is blocked by specific, single amino acid substitutions in the human immunodeficiency virus type 1 matrix. J. Virol. 69:1984-1989.
    • (1995) J. Virol. , vol.69 , pp. 1984-1989
    • Freed, E.O.1    Martin, M.A.2
  • 37
    • 0024435050 scopus 로고
    • Mutational analysis of the cleavage sequence of the human immunodeficiency virus type 1 envelope glycoprotein precursor gp160
    • Freed, E. O., D. J. Myers, and R. Risser. 1989. Mutational analysis of the cleavage sequence of the human immunodeficiency virus type 1 envelope glycoprotein precursor gp160. J. Virol. 63:4670-4675.
    • (1989) J. Virol. , vol.63 , pp. 4670-4675
    • Freed, E.O.1    Myers, D.J.2    Risser, R.3
  • 38
    • 0026755725 scopus 로고
    • Effects of deletions in the cytoplasmic domain on biological functions of human immunodeficiency virus type 1 envelope glycoproteins
    • Gabuzda, D. H., A. Lever, E. Terwilliger, and J. Sodroski. 1992. Effects of deletions in the cytoplasmic domain on biological functions of human immunodeficiency virus type 1 envelope glycoproteins. J. Virol. 66:3306-3315.
    • (1992) J. Virol. , vol.66 , pp. 3306-3315
    • Gabuzda, D.H.1    Lever, A.2    Terwilliger, E.3    Sodroski, J.4
  • 39
    • 0025904765 scopus 로고
    • Assembly and morphology of HIV: Potential effect of structure on viral function
    • Gelderblom, H. R. 1991. Assembly and morphology of HIV: potential effect of structure on viral function. AIDS 5:617-637.
    • (1991) AIDS , vol.5 , pp. 617-637
    • Gelderblom, H.R.1
  • 40
    • 0023099283 scopus 로고
    • Fine structure of human immunodeficiency virus (HIV) and immunolocalization of structural proteins
    • Gelderblom, H. R., E. H. Hausmann, M. Ozel, G. Pauli, and M. A. Koch. 1987. Fine structure of human immunodeficiency virus (HIV) and immunolocalization of structural proteins. Virology 156:171-176.
    • (1987) Virology , vol.156 , pp. 171-176
    • Gelderblom, H.R.1    Hausmann, E.H.2    Ozel, M.3    Pauli, G.4    Koch, M.A.5
  • 42
    • 0034977654 scopus 로고    scopus 로고
    • The role of the antibody response in influenza virus infection
    • Gerhard, W. 2001. The role of the antibody response in influenza virus infection. Curr. Top. Microbiol. Immunol. 260:171-190.
    • (2001) Curr. Top. Microbiol. Immunol. , vol.260 , pp. 171-190
    • Gerhard, W.1
  • 43
    • 0028871747 scopus 로고
    • Receptor-induced conformational changes in the subgroup a avian leukosis and sarcoma virus envelope glycoprotein
    • Gilbert, J. M., L. D. Hernandez, J. W. Balliet, P. Bates, and J. M. White. 1995. Receptor-induced conformational changes in the subgroup A avian leukosis and sarcoma virus envelope glycoprotein. J. Virol. 69:7410-7415.
    • (1995) J. Virol. , vol.69 , pp. 7410-7415
    • Gilbert, J.M.1    Hernandez, L.D.2    Balliet, J.W.3    Bates, P.4    White, J.M.5
  • 44
    • 0025225331 scopus 로고
    • Antifusion activity in sera from persons infected with human immunodeficiency virus type 1
    • Graham, B. S., J. M. Rowland, A. Modliszewski, and D. C. Monteflori. 1990. Antifusion activity in sera from persons infected with human immunodeficiency virus type 1. J. Clin. Microbiol. 28:2608-2611.
    • (1990) J. Clin. Microbiol. , vol.28 , pp. 2608-2611
    • Graham, B.S.1    Rowland, J.M.2    Modliszewski, A.3    Monteflori, D.C.4
  • 45
    • 0343621483 scopus 로고    scopus 로고
    • Role of hemagglutinin surface density in the initial stages of influenza virus fusion: Lack of evidence for cooperativity
    • Gunther-Ausborn, S., P. Schoen, I. Bartoldus, J. Wilschut, and T. Stegmann. 2000. Role of hemagglutinin surface density in the initial stages of influenza virus fusion: lack of evidence for cooperativity. J. Virol. 74:2714-2720.
    • (2000) J. Virol. , vol.74 , pp. 2714-2720
    • Gunther-Ausborn, S.1    Schoen, P.2    Bartoldus, I.3    Wilschut, J.4    Stegmann, T.5
  • 47
    • 0027524129 scopus 로고
    • Morphometric analysis of envelope glycoprotein gp120 distribution on HIV-1 virions
    • Hart, T. K., A. M. Klinkner, J. Ventre, and P. J. Bugelski. 1993. Morphometric analysis of envelope glycoprotein gp120 distribution on HIV-1 virions. J. Histochem. Cytochem. 41:265-271.
    • (1993) J. Histochem. Cytochem. , vol.41 , pp. 265-271
    • Hart, T.K.1    Klinkner, A.M.2    Ventre, J.3    Bugelski, P.J.4
  • 48
    • 0031440116 scopus 로고    scopus 로고
    • Activation of a retroviral membrane fusion protein: Soluble receptor-induced liposome binding of the ALSV envelope glycoprotein
    • Hernandez, L. D., R. J. Peters, S. E. Delos, J. A. Young, D. A. Agard, and J. M. White. 1997. Activation of a retroviral membrane fusion protein: soluble receptor-induced liposome binding of the ALSV envelope glycoprotein. J. Cell Biol. 139:1455-1464.
    • (1997) J. Cell Biol. , vol.139 , pp. 1455-1464
    • Hernandez, L.D.1    Peters, R.J.2    Delos, S.E.3    Young, J.A.4    Agard, D.A.5    White, J.M.6
  • 49
    • 0037223708 scopus 로고    scopus 로고
    • Nonneutralizing antibodies to the CD4-binding site on the gp120 subunit of human immunodeficiency virus type 1 do not interfere with the activity of a neutralizing antibody against the same site
    • Herrera, C., C. Spenlehauer, M. S. Fung, D. R. Burton, S. Beddows, and J. P. Moore. 2003. Nonneutralizing antibodies to the CD4-binding site on the gp120 subunit of human immunodeficiency virus type 1 do not interfere with the activity of a neutralizing antibody against the same site. J. Virol. 77:1084-1091.
    • (2003) J. Virol. , vol.77 , pp. 1084-1091
    • Herrera, C.1    Spenlehauer, C.2    Fung, M.S.3    Burton, D.R.4    Beddows, S.5    Moore, J.P.6
  • 51
    • 0037459076 scopus 로고    scopus 로고
    • Membrane fusion
    • Jahn, R., T. Lang, and T. C. Sudhof. 2003. Membrane fusion. Cell 112: 519-533.
    • (2003) Cell , vol.112 , pp. 519-533
    • Jahn, R.1    Lang, T.2    Sudhof, T.C.3
  • 52
    • 0026075572 scopus 로고
    • Oligomerization and transport of the envelope protein of Moloney murine leukemia virus-TB and of ts1, a neurovirulent temperature-sensitive mutant of MoMuLV-TB
    • Kamps, C. A., Y. C. Lin, and P. K. Wong. 1991. Oligomerization and transport of the envelope protein of Moloney murine leukemia virus-TB and of ts1, a neurovirulent temperature-sensitive mutant of MoMuLV-TB. Virology 184:687-694.
    • (1991) Virology , vol.184 , pp. 687-694
    • Kamps, C.A.1    Lin, Y.C.2    Wong, P.K.3
  • 53
    • 0025779468 scopus 로고
    • Single cell fusion events induced by influenza hemagglutinin: Studies with rapid-flow, quantitative fluorescence microscopy
    • Kaplan, D., J. Zimmerberg, A. Puri, D. P. Sarkar, and R. Blumenthal. 1991. Single cell fusion events induced by influenza hemagglutinin: studies with rapid-flow, quantitative fluorescence microscopy. Exp. Cell Res. 195:137-144.
    • (1991) Exp. Cell Res. , vol.195 , pp. 137-144
    • Kaplan, D.1    Zimmerberg, J.2    Puri, A.3    Sarkar, D.P.4    Blumenthal, R.5
  • 54
    • 0026562720 scopus 로고
    • Detection of replication-competent and pseudotyped human immunodeficiency virus with a sensitive cell line on the basis of activation of an integrated beta-galactosidase gene
    • Kimpton, J., and M. Emerman. 1992. Detection of replication-competent and pseudotyped human immunodeficiency virus with a sensitive cell line on the basis of activation of an integrated beta-galactosidase gene. J. Virol. 66:2232-2239.
    • (1992) J. Virol. , vol.66 , pp. 2232-2239
    • Kimpton, J.1    Emerman, M.2
  • 56
    • 0019822341 scopus 로고
    • Immunoelectron microscopic study of the detection of the glycoproteins of influenza and Sendai viruses in infected cells by the immunoperoxidase method
    • Kohama, M. T., J. M. Cardenas, and J. T. Seto. 1981. Immunoelectron microscopic study of the detection of the glycoproteins of influenza and Sendai viruses in infected cells by the immunoperoxidase method. J. Virol. Methods 3:293-301.
    • (1981) J. Virol. Methods , vol.3 , pp. 293-301
    • Kohama, M.T.1    Cardenas, J.M.2    Seto, J.T.3
  • 57
    • 0026444130 scopus 로고
    • Clonal dominance: Cause for a limited and failing immune response to HIV-1 infection and vaccination
    • Kohler, H., J. Goudsmit, and P. Nara. 1992. Clonal dominance: cause for a limited and failing immune response to HIV-1 infection and vaccination. J. Acquir. Immune Defic. Syndr. 5:1158-1168.
    • (1992) J. Acquir. Immune Defic. Syndr. , vol.5 , pp. 1158-1168
    • Kohler, H.1    Goudsmit, J.2    Nara, P.3
  • 58
    • 0001720445 scopus 로고    scopus 로고
    • Numbering positions in HIV relative to HXBc2
    • B. K. Korber, C. Foley, F. Hahn, B. McCutchan, F. Mellor, and J. Sodroski (ed.). Los Alamos National Laboratories, Los Alamos, N. Mex.
    • Korber, B. F., F. Kuiken, C. Pillai, S. Sodroksi, J. 1998. Numbering positions in HIV relative to HXBc2, p. II-A-54-II-A-69. In B. K. Korber, C. Foley, F. Hahn, B. McCutchan, F. Mellor, and J. Sodroski (ed.), Human retroviruses and AIDS. Los Alamos National Laboratories, Los Alamos, N. Mex.
    • (1998) Human Retroviruses and AIDS
    • Korber, B.F.1    Kuiken, F.2    Pillai, C.3    Sodroksi, S.4
  • 59
    • 0028148319 scopus 로고
    • The World Health Organization Global Programme on AIDS proposal for standardization of HIV sequence nomenclature
    • W.H.O. Network for HIV Isolation and Characterization
    • Korber, B. T., S. Osmanov, J. Esparza, and G. Myers. 1994. The World Health Organization Global Programme on AIDS proposal for standardization of HIV sequence nomenclature. W.H.O. Network for HIV Isolation and Characterization. AIDS Res. Hum. Retrovir. 10:1355-1358.
    • (1994) AIDS Res. Hum. Retrovir. , vol.10 , pp. 1355-1358
    • Korber, B.T.1    Osmanov, S.2    Esparza, J.3    Myers, G.4
  • 60
    • 0033941573 scopus 로고    scopus 로고
    • Cooperatively of multiple CCR5 coreceptors is required for infections by human immunodeficiency virus type 1
    • Kuhmann, S. E., E. J. Platt, S. L. Kozak, and D. Kabat. 2000. Cooperatively of multiple CCR5 coreceptors is required for infections by human immunodeficiency virus type 1. J. Virol. 74:7005-7015.
    • (2000) J. Virol. , vol.74 , pp. 7005-7015
    • Kuhmann, S.E.1    Platt, E.J.2    Kozak, S.L.3    Kabat, D.4
  • 62
    • 0024030790 scopus 로고
    • The human immunodeficiency virus and its pathogenesis
    • Levy, J. A. 1988. The human immunodeficiency virus and its pathogenesis. Infect. Dis. Clin. N. Am. 2:285-297.
    • (1988) Infect. Dis. Clin. N. Am. , vol.2 , pp. 285-297
    • Levy, J.A.1
  • 63
    • 0037176950 scopus 로고    scopus 로고
    • Use of pseudotyped retroviral vectors to analyze the receptor-binding pocket of hemagglutinin from a pathogenic avian influenza A virus (H7 subtype)
    • Lin, A. H., and P. M. Cannon. 2002. Use of pseudotyped retroviral vectors to analyze the receptor-binding pocket of hemagglutinin from a pathogenic avian influenza A virus (H7 subtype). Virus Res. 83:43-56.
    • (2002) Virus Res. , vol.83 , pp. 43-56
    • Lin, A.H.1    Cannon, P.M.2
  • 64
    • 0033920211 scopus 로고    scopus 로고
    • Functional implications of the human T-lymphotropic virus type 1 transmembrane glycoprotein helical hairpin structure
    • Maerz, A. L., R. J. Center, B. E. Kemp, B. Kobe, and P. Poumbourios. 2000. Functional implications of the human T-lymphotropic virus type 1 transmembrane glycoprotein helical hairpin structure. J. Virol. 74:6614-6621.
    • (2000) J. Virol. , vol.74 , pp. 6614-6621
    • Maerz, A.L.1    Center, R.J.2    Kemp, B.E.3    Kobe, B.4    Poumbourios, P.5
  • 65
    • 0030900512 scopus 로고    scopus 로고
    • Truncation of the human immunodeficiency virus type 1 envelope glycoprotein allows efficient pseudotyping of Moloney murine leukemia virus particles and gene transfer into CD4+ cells
    • Mammano, F., F. Salvatori, S. Indraccolo, A. De Rossi, L. Chieco-Bianchi, and H. G. Gottlinger. 1997. Truncation of the human immunodeficiency virus type 1 envelope glycoprotein allows efficient pseudotyping of Moloney murine leukemia virus particles and gene transfer into CD4+ cells. J. Virol. 71:3341-3345.
    • (1997) J. Virol. , vol.71 , pp. 3341-3345
    • Mammano, F.1    Salvatori, F.2    Indraccolo, S.3    De Rossi, A.4    Chieco-Bianchi, L.5    Gottlinger, H.G.6
  • 66
    • 0035956421 scopus 로고    scopus 로고
    • Synchronized activation and refolding of influenza hemagglutinin in multimeric fusion machines
    • Markovic, I., E. Leikina, M. Zhukovsky, J. Zimmerberg, and L. V. Chernomordik. 2001. Synchronized activation and refolding of influenza hemagglutinin in multimeric fusion machines. J. Cell Biol. 155:833-844.
    • (2001) J. Cell Biol. , vol.155 , pp. 833-844
    • Markovic, I.1    Leikina, E.2    Zhukovsky, M.3    Zimmerberg, J.4    Chernomordik, L.V.5
  • 67
    • 3242713988 scopus 로고    scopus 로고
    • Sequential roles of receptor binding and low pH in forming prehairpin and hairpin conformations of a retroviral envelope glycoprotein
    • Matsuyama, S., S. E. Delos, and J. M. White. 2004. Sequential roles of receptor binding and low pH in forming prehairpin and hairpin conformations of a retroviral envelope glycoprotein. J. Virol. 78:8201-8209.
    • (2004) J. Virol. , vol.78 , pp. 8201-8209
    • Matsuyama, S.1    Delos, S.E.2    White, J.M.3
  • 68
    • 0023921610 scopus 로고
    • Endoproteolytic cleavage of gp160 is required for the activation of human immunodeficiency virus
    • McCune, J. M., L. B. Rabin, M. B. Feinberg, M. Lieberman, J. C. Kosek, G. R. Reyes, and I. L. Weissman. 1988. Endoproteolytic cleavage of gp160 is required for the activation of human immunodeficiency virus. Cell 53: 55-67.
    • (1988) Cell , vol.53 , pp. 55-67
    • McCune, J.M.1    Rabin, L.B.2    Feinberg, M.B.3    Lieberman, M.4    Kosek, J.C.5    Reyes, G.R.6    Weissman, I.L.7
  • 69
    • 0031012358 scopus 로고    scopus 로고
    • Predominance of detrimental humoral immune responses to HIV-1 in AIDS patients with CD4 lymphocyte counts less than 400/mm3
    • McDougall, B., M. H. Nymark, G. Landucci, D. Forthal, and W. E. Robinson, Jr. 1997. Predominance of detrimental humoral immune responses to HIV-1 in AIDS patients with CD4 lymphocyte counts less than 400/mm3. Scand. J. Immunol. 45:103-111.
    • (1997) Scand. J. Immunol. , vol.45 , pp. 103-111
    • McDougall, B.1    Nymark, M.H.2    Landucci, G.3    Forthal, D.4    Robinson Jr., W.E.5
  • 70
    • 0026098303 scopus 로고
    • Differential loss of envelope glycoprotein gp120 from virions of human immunodeficiency virus type 1 isolates: Effects on infectivity and neutralization
    • McKeating, J. A., A. McKnight, and J. P. Moore. 1991. Differential loss of envelope glycoprotein gp120 from virions of human immunodeficiency virus type 1 isolates: effects on infectivity and neutralization. J. Virol. 65:852-860.
    • (1991) J. Virol. , vol.65 , pp. 852-860
    • McKeating, J.A.1    McKnight, A.2    Moore, J.P.3
  • 71
    • 0027395736 scopus 로고
    • Host cell membrane proteins on human immunodeficiency virus type 1 after in vitro infection of H9 cells and blood mononuclear cells. An immunoelectron microscopic study
    • Meerloo, T., M. A. Sheikh, A. C. Bloem, A. de Ronde, M. Schutten, C. A. van Els, P. J. Roholl, P. Joling, J. Goudsmit, and H. J. Schuurman. 1993. Host cell membrane proteins on human immunodeficiency virus type 1 after in vitro infection of H9 cells and blood mononuclear cells. An immunoelectron microscopic study. J. Gen. Virol. 74:129-135.
    • (1993) J. Gen. Virol. , vol.74 , pp. 129-135
    • Meerloo, T.1    Sheikh, M.A.2    Bloem, A.C.3    De Ronde, A.4    Schutten, M.5    Van Els, C.A.6    Roholl, P.J.7    Joling, P.8    Goudsmit, J.9    Schuurman, H.J.10
  • 72
    • 0028783783 scopus 로고
    • The fusion kinetics of influenza hemagglutinin expressing cells to planar bilayer membranes is affected by HA density and host cell surface
    • Melikyan, G. B., W. D. Niles, and F. S. Cohen. 1995. The fusion kinetics of influenza hemagglutinin expressing cells to planar bilayer membranes is affected by HA density and host cell surface. J. Gen. Physiol. 106:783-802.
    • (1995) J. Gen. Physiol. , vol.106 , pp. 783-802
    • Melikyan, G.B.1    Niles, W.D.2    Cohen, F.S.3
  • 73
    • 0035063938 scopus 로고    scopus 로고
    • Chemokine signaling and functional responses: The role of receptor dimerization and TK pathway activation
    • Mellado, M., J. M. Rodriguez-Frade, S. Manes, and A. C. Martinez. 2001. Chemokine signaling and functional responses: the role of receptor dimerization and TK pathway activation. Annu. Rev. Immunol. 19:397-421.
    • (2001) Annu. Rev. Immunol. , vol.19 , pp. 397-421
    • Mellado, M.1    Rodriguez-Frade, J.M.2    Manes, S.3    Martinez, A.C.4
  • 74
    • 0036841564 scopus 로고    scopus 로고
    • Measuring pKa of activation and pKi of inactivation for influenza hemagglutinin from kinetics of membrane fusion of virions and of HA expressing cells
    • Mittal, A., T. Shangguan, and J. Bentz. 2002. Measuring pKa of activation and pKi of inactivation for influenza hemagglutinin from kinetics of membrane fusion of virions and of HA expressing cells. Biophys. J. 83:2652-2666.
    • (2002) Biophys. J. , vol.83 , pp. 2652-2666
    • Mittal, A.1    Shangguan, T.2    Bentz, J.3
  • 75
    • 0017640103 scopus 로고
    • Analysis of precursors to the envelope glycoproteins of avian RNA tumor viruses in chicken and quail cells
    • Moelling, K., and M. Hayami. 1977. Analysis of precursors to the envelope glycoproteins of avian RNA tumor viruses in chicken and quail cells. J. Virol. 22:598-607.
    • (1977) J. Virol. , vol.22 , pp. 598-607
    • Moelling, K.1    Hayami, M.2
  • 76
    • 0030987291 scopus 로고    scopus 로고
    • HIV type 1 coreceptors, neutralization serotypes, and vaccine development
    • Moore, J., and A. Trkola. 1997. HIV type 1 coreceptors, neutralization serotypes, and vaccine development. AIDS Res. Hum. Retrovir. 13:733-736.
    • (1997) AIDS Res. Hum. Retrovir. , vol.13 , pp. 733-736
    • Moore, J.1    Trkola, A.2
  • 77
    • 0025572710 scopus 로고
    • Dissociation of gp120 from HIV-1 virions induced by soluble CD4
    • Moore, J. P., J. A. McKeating, R. A. Weiss, and Q. J. Sattentau. 1990. Dissociation of gp120 from HIV-1 virions induced by soluble CD4. Science 250:1139-1142.
    • (1990) Science , vol.250 , pp. 1139-1142
    • Moore, J.P.1    McKeating, J.A.2    Weiss, R.A.3    Sattentau, Q.J.4
  • 78
    • 0037810998 scopus 로고    scopus 로고
    • Structure and function of a paramyxovirus fusion protein
    • Morrison, T. G. 2003. Structure and function of a paramyxovirus fusion protein. Biochim. Biophys. Acta 1614:73-84.
    • (2003) Biochim. Biophys. Acta , vol.1614 , pp. 73-84
    • Morrison, T.G.1
  • 79
    • 0033697734 scopus 로고    scopus 로고
    • Retroviral entry mediated by receptor priming and low pH triggering of an envelope glycoprotein
    • Mothes, W., A. L. Boerger, S. Narayan, J. M. Cunningham, and J. A. Young. 2000. Retroviral entry mediated by receptor priming and low pH triggering of an envelope glycoprotein. Cell 103:679-689.
    • (2000) Cell , vol.103 , pp. 679-689
    • Mothes, W.1    Boerger, A.L.2    Narayan, S.3    Cunningham, J.M.4    Young, J.A.5
  • 80
    • 0022643192 scopus 로고
    • Distribution of hemagglutinin and neuraminidase on influenza virions as revealed by immunoelectron microscopy
    • Murti, K. G., and R. G. Webster. 1986. Distribution of hemagglutinin and neuraminidase on influenza virions as revealed by immunoelectron microscopy. Virology 149:36-43.
    • (1986) Virology , vol.149 , pp. 36-43
    • Murti, K.G.1    Webster, R.G.2
  • 81
    • 0023853928 scopus 로고
    • Quantitative infectivity assay for HIV-1 and -2
    • Nara, P. L., and P. J. Fischinger. 1988. Quantitative infectivity assay for HIV-1 and -2. Nature 332:469-470.
    • (1988) Nature , vol.332 , pp. 469-470
    • Nara, P.L.1    Fischinger, P.J.2
  • 82
    • 2442680451 scopus 로고    scopus 로고
    • Reverse genetics systems for the generation of segmented negative-sense RNA viruses entirely from cloned cDNA
    • Neumann, G., and Y. Kawaoka. 2004. Reverse genetics systems for the generation of segmented negative-sense RNA viruses entirely from cloned cDNA Curr. Top. Microbiol. Immunol. 283:43-60.
    • (2004) Curr. Top. Microbiol. Immunol. , vol.283 , pp. 43-60
    • Neumann, G.1    Kawaoka, Y.2
  • 83
    • 0019990290 scopus 로고
    • Processing of the env gene products of Moloney murine leukaemia virus
    • Ng, V. L., T. G. Wood, and R. B. Arlinghaus. 1982. Processing of the env gene products of Moloney murine leukaemia virus. J. Gen. Virol. 59:329-343.
    • (1982) J. Gen. Virol. , vol.59 , pp. 329-343
    • Ng, V.L.1    Wood, T.G.2    Arlinghaus, R.B.3
  • 85
    • 0036310245 scopus 로고    scopus 로고
    • Novel monoclonal antibody directed at the receptor binding site on the avian sarcoma and leukosis virus Env complex
    • Ochsenbauer-Jambor, C., S. E. Delos, M. A. Accavitti, J. M. White, and E. Hunter. 2002. Novel monoclonal antibody directed at the receptor binding site on the avian sarcoma and leukosis virus Env complex. J. Virol. 76:7518-7527.
    • (2002) J. Virol. , vol.76 , pp. 7518-7527
    • Ochsenbauer-Jambor, C.1    Delos, S.E.2    Accavitti, M.A.3    White, J.M.4    Hunter, E.5
  • 86
    • 0034834565 scopus 로고    scopus 로고
    • Receptors and entry cofactors for retroviruses include single and multiple transmembrane-spanning proteins as well as newly described glycophosphatidylinositol-anchored and secreted proteins
    • Overbaugh, J., A. D. Miller, and M. V. Eiden. 2001. Receptors and entry cofactors for retroviruses include single and multiple transmembrane-spanning proteins as well as newly described glycophosphatidylinositol-anchored and secreted proteins. Microbiol. Mol. Biol. Rev. 65:371-389.
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 371-389
    • Overbaugh, J.1    Miller, A.D.2    Eiden, M.V.3
  • 87
  • 89
    • 0028924022 scopus 로고
    • Amphotericin B derivative blocks human immunodeficiency virus type 1 entry after CD4 binding: Effect on virus-cell fusion but not on cell-cell fusion
    • Pleskoff, O., M. Seman, and M. Alizon. 1995. Amphotericin B derivative blocks human immunodeficiency virus type 1 entry after CD4 binding: effect on virus-cell fusion but not on cell-cell fusion. J. Virol. 69:570-574.
    • (1995) J. Virol. , vol.69 , pp. 570-574
    • Pleskoff, O.1    Seman, M.2    Alizon, M.3
  • 90
    • 0037213278 scopus 로고    scopus 로고
    • Heterogeneity of envelope molecules expressed on primary human immunodeficiency virus type 1 particles as probed by the binding of neutralizing and nonneutralizing antibodies
    • Poignard, P., M. Moulard, E. Golez, V. Vivona, M. Franti, S. Venturini, M. Wang, P. W. Parren, and D. R. Burton. 2003. Heterogeneity of envelope molecules expressed on primary human immunodeficiency virus type 1 particles as probed by the binding of neutralizing and nonneutralizing antibodies. J. Virol. 77:353-365.
    • (2003) J. Virol. , vol.77 , pp. 353-365
    • Poignard, P.1    Moulard, M.2    Golez, E.3    Vivona, V.4    Franti, M.5    Venturini, S.6    Wang, M.7    Parren, P.W.8    Burton, D.R.9
  • 91
    • 0032578032 scopus 로고    scopus 로고
    • The influenza virus hemagglutinin: A model protein in the study of membrane fusion
    • Ramalho-Santos, J., and M. C. de Lima. 1998. The influenza virus hemagglutinin: a model protein in the study of membrane fusion. Biochim. Biophys. Acta 1376:147-154.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 147-154
    • Ramalho-Santos, J.1    De Lima, M.C.2
  • 92
    • 0032079344 scopus 로고    scopus 로고
    • Efficient HIV-1 replication can occur in the absence of the viral matrix protein
    • Reil, H., A. A. Bukovsky, H. R. Gelderblom, and H. G. Gottlinger. 1998. Efficient HIV-1 replication can occur in the absence of the viral matrix protein. EMBO J. 17:2699-2708.
    • (1998) EMBO J. , vol.17 , pp. 2699-2708
    • Reil, H.1    Bukovsky, A.A.2    Gelderblom, H.R.3    Gottlinger, H.G.4
  • 93
    • 0030962180 scopus 로고    scopus 로고
    • Contribution of virion ICAM-1 to human immunodeficiency virus infectivity and sensitivity to neutralization
    • Rizzuto, C. D., and J. G. Sodroski. 1997. Contribution of virion ICAM-1 to human immunodeficiency virus infectivity and sensitivity to neutralization. J. Virol. 71:4847-4851.
    • (1997) J. Virol. , vol.71 , pp. 4847-4851
    • Rizzuto, C.D.1    Sodroski, J.G.2
  • 95
    • 0029034834 scopus 로고
    • Analysis of the subgroup a avian sarcoma and leukosis virus receptor: The 40-residue, cysteine-rich, low-density lipoprotein receptor repeat motif of TVa is sufficient to mediate viral entry
    • Rong, L., and P. Bates. 1995. Analysis of the subgroup A avian sarcoma and leukosis virus receptor: the 40-residue, cysteine-rich, low-density lipoprotein receptor repeat motif of TVa is sufficient to mediate viral entry. J. Virol. 69:4847-4853.
    • (1995) J. Virol. , vol.69 , pp. 4847-4853
    • Rong, L.1    Bates, P.2
  • 96
    • 0033749617 scopus 로고    scopus 로고
    • Cooperative subunit interactions within the oligomeric envelope glycoprotein of HIV-1: Functional complementation of specific defects in gp120 and gp41
    • Salzwedel, K., and E. A. Berger. 2000. Cooperative subunit interactions within the oligomeric envelope glycoprotein of HIV-1: functional complementation of specific defects in gp120 and gp41. Proc. Natl. Acad. Sci. USA 97:12794-12799.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12794-12799
    • Salzwedel, K.1    Berger, E.A.2
  • 97
    • 0036682935 scopus 로고    scopus 로고
    • Lentiviral vectors pseudotyped with a modified RD114 envelope glycoprotein show increased stability in sera and augmented transduction of primary lymphocytes and CD34+ cells derived from human and nonhuman primates
    • Sandrin, V., B. Boson, P. Salmon, W. Gay, D. Negre, R. Le Grand, D. Trono, and F. L. Cosset. 2002. Lentiviral vectors pseudotyped with a modified RD114 envelope glycoprotein show increased stability in sera and augmented transduction of primary lymphocytes and CD34+ cells derived from human and nonhuman primates. Blood 100:823-832.
    • (2002) Blood , vol.100 , pp. 823-832
    • Sandrin, V.1    Boson, B.2    Salmon, P.3    Gay, W.4    Negre, D.5    Le Grand, R.6    Trono, D.7    Cosset, F.L.8
  • 98
    • 0033485553 scopus 로고    scopus 로고
    • Host cyclophilin a mediates HIV-1 attachment to target cells via heparans
    • Saphire, A. C., M. D. Bobardt, and P. A. Gallay. 1999. Host cyclophilin A mediates HIV-1 attachment to target cells via heparans. EMBO J. 18:6771-6785.
    • (1999) EMBO J. , vol.18 , pp. 6771-6785
    • Saphire, A.C.1    Bobardt, M.D.2    Gallay, P.A.3
  • 99
    • 0023005485 scopus 로고
    • Shedding and interspecies type sero-reactivity of the envelope glycopolypeptide gp120 of the human immunodeficiency virus
    • Schneider, J., O. Kaaden, T. D. Copeland, S. Oroszlan, and G. Hunsmann. 1986. Shedding and interspecies type sero-reactivity of the envelope glycopolypeptide gp120 of the human immunodeficiency virus. J. Gen. Virol. 67:2533-2538.
    • (1986) J. Gen. Virol. , vol.67 , pp. 2533-2538
    • Schneider, J.1    Kaaden, O.2    Copeland, T.D.3    Oroszlan, S.4    Hunsmann, G.5
  • 100
    • 0032850727 scopus 로고    scopus 로고
    • Stoichiometry of monoclonal antibody neutralization of T-cell line-adapted human immunodeficiency virus type 1
    • Schonning, K., O. Lund, O. S. Lund, and J. E. Hansen. 1999. Stoichiometry of monoclonal antibody neutralization of T-cell line-adapted human immunodeficiency virus type 1. J. Virol. 73:8364-8370.
    • (1999) J. Virol. , vol.73 , pp. 8364-8370
    • Schonning, K.1    Lund, O.2    Lund, O.S.3    Hansen, J.E.4
  • 101
    • 0029918812 scopus 로고    scopus 로고
    • Influenza-virus-liposome lipid mixing is leaky and largely insensitive to the material properties of the target membrane
    • Shangguan, T., D. Alford, and J. Bentz. 1996. Influenza-virus-liposome lipid mixing is leaky and largely insensitive to the material properties of the target membrane. Biochemistry 35:4956-4965.
    • (1996) Biochemistry , vol.35 , pp. 4956-4965
    • Shangguan, T.1    Alford, D.2    Bentz, J.3
  • 102
  • 103
    • 0037348281 scopus 로고    scopus 로고
    • Effects of HIV type 1 envelope glycoprotein proteolytic processing on antigenicity
    • Si, Z., N. Phan, E. Kiprilov, and J. Sodroski. 2003. Effects of HIV type 1 envelope glycoprotein proteolytic processing on antigenicity. AIDS Res. Hum. Retrovir. 19:217-226.
    • (2003) AIDS Res. Hum. Retrovir. , vol.19 , pp. 217-226
    • Si, Z.1    Phan, N.2    Kiprilov, E.3    Sodroski, J.4
  • 104
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • Skehel, J. J., and D. C. Wiley. 2000. Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu. Rev. Biochem. 69:531-569.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 105
    • 0023886862 scopus 로고
    • Formation of mixed hemagglutinin trimers in the course of double infection with influenza viruses belonging to different subtypes
    • Sklyanskaya, E. I., M. Shie, Y. S. Komarov, S. S. Yamnikova, and N. V. Kaverin. 1988. Formation of mixed hemagglutinin trimers in the course of double infection with influenza viruses belonging to different subtypes. Virus Res. 10:153-165.
    • (1988) Virus Res. , vol.10 , pp. 153-165
    • Sklyanskaya, E.I.1    Shie, M.2    Komarov, Y.S.3    Yamnikova, S.S.4    Kaverin, N.V.5
  • 106
    • 1842534392 scopus 로고    scopus 로고
    • How viruses enter animal cells
    • Smith, A. E., and A. Helenius. 2004. How viruses enter animal cells. Science 304:237-242.
    • (2004) Science , vol.304 , pp. 237-242
    • Smith, A.E.1    Helenius, A.2
  • 107
    • 0346373694 scopus 로고    scopus 로고
    • The mature avian leukosis virus subgroup a envelope glycoprotein is metastable, and refolding induced by the synergistic effects of receptor binding and low pH is coupled to infection
    • Smith, J. G., W. Mothes, S. C. Blacklow, and J. M. Cunningham. 2004. The mature avian leukosis virus subgroup A envelope glycoprotein is metastable, and refolding induced by the synergistic effects of receptor binding and low pH is coupled to infection. J. Virol. 78:1403-1410.
    • (2004) J. Virol. , vol.78 , pp. 1403-1410
    • Smith, J.G.1    Mothes, W.2    Blacklow, S.C.3    Cunningham, J.M.4
  • 108
    • 0032499531 scopus 로고    scopus 로고
    • Cell-specific viral targeting mediated by a soluble retroviral receptor-ligand fusion protein
    • Snitkovsky, S., and J. A. Young. 1998. Cell-specific viral targeting mediated by a soluble retroviral receptor-ligand fusion protein. Proc. Natl. Acad. Sci. USA 95:7063-7068.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7063-7068
    • Snitkovsky, S.1    Young, J.A.2
  • 109
    • 0034252567 scopus 로고    scopus 로고
    • Membrane fusion mechanisms: The influenza hemagglutinin paradigm and its implications for intracellular fusion
    • Stegmann, T. 2000. Membrane fusion mechanisms: the influenza hemagglutinin paradigm and its implications for intracellular fusion. Traffic 1:598-604.
    • (2000) Traffic , vol.1 , pp. 598-604
    • Stegmann, T.1
  • 110
    • 0025266354 scopus 로고
    • Intracellular processing of the gp160 HIV-1 envelope precursor. Endoproteolytic cleavage occurs in a cis or medial compartment of the Golgi complex
    • Stein, B. S., and E. G. Engleman. 1990. Intracellular processing of the gp160 HIV-1 envelope precursor. Endoproteolytic cleavage occurs in a cis or medial compartment of the Golgi complex. J. Biol. Chem. 265:2640-2649.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2640-2649
    • Stein, B.S.1    Engleman, E.G.2
  • 111
    • 0029020970 scopus 로고
    • Replicative function and neutralization sensitivity of envelope glycoproteins from primary and T-cell line-passaged human immunodeficiency virus type 1 isolates
    • Sullivan, N., Y. Sun, J. Li, W. Hofmann, and J. Sodroski. 1995. Replicative function and neutralization sensitivity of envelope glycoproteins from primary and T-cell line-passaged human immunodeficiency virus type 1 isolates. J. Virol. 69:4413-4422.
    • (1995) J. Virol. , vol.69 , pp. 4413-4422
    • Sullivan, N.1    Sun, Y.2    Li, J.3    Hofmann, W.4    Sodroski, J.5
  • 112
    • 0030780614 scopus 로고    scopus 로고
    • Atomic structure of a thermostable subdomain of HIV-1 gp41
    • Tan, K., J. Liu, J. Wang, S. Shen, and M. Lu. 1997. Atomic structure of a thermostable subdomain of HIV-1 gp41. Proc. Natl. Acad. Sci. USA 94: 12303-12308.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12303-12308
    • Tan, K.1    Liu, J.2    Wang, J.3    Shen, S.4    Lu, M.5
  • 113
    • 0023391217 scopus 로고
    • Quantitative relationships between an influenza virus and neutralizing antibody
    • Taylor, H. P., S. J. Armstrong, and N. J. Dimmock. 1987. Quantitative relationships between an influenza virus and neutralizing antibody. Virology 159:288-298.
    • (1987) Virology , vol.159 , pp. 288-298
    • Taylor, H.P.1    Armstrong, S.J.2    Dimmock, N.J.3
  • 115
    • 0026748702 scopus 로고
    • Hemagglutinin activation of pathogenic avian influenza viruses of serotype H7 requires the protease recognition motif R-X-K/R-R
    • Vey, M., M. Orlich, S. Adler, H. D. Klenk, R. Rott, and W. Garten. 1992. Hemagglutinin activation of pathogenic avian influenza viruses of serotype H7 requires the protease recognition motif R-X-K/R-R. Virology 188:408-413.
    • (1992) Virology , vol.188 , pp. 408-413
    • Vey, M.1    Orlich, M.2    Adler, S.3    Klenk, H.D.4    Rott, R.5    Garten, W.6
  • 117
    • 0025734320 scopus 로고
    • Cell-surface receptor for ecotropic murine retroviruses is a basic amino-acid transporter
    • Wang, H., M. P. Kavanaugh, R. A. North, and D. Rabat. 1991. Cell-surface receptor for ecotropic murine retroviruses is a basic amino-acid transporter. Nature 352:729-731.
    • (1991) Nature , vol.352 , pp. 729-731
    • Wang, H.1    Kavanaugh, M.P.2    North, R.A.3    Rabat, D.4
  • 118
    • 0032568634 scopus 로고    scopus 로고
    • The central structural feature of the membrane fusion protein subunit from the Ebola virus glycoprotein is a long triple-stranded coiled coil
    • Weissenhorn, W., L. J. Calder, S. A. Wharton, J. J. Skehel, and D. C. Wiley. 1998. The central structural feature of the membrane fusion protein subunit from the Ebola virus glycoprotein is a long triple-stranded coiled coil. Proc. Natl. Acad. Sci. USA 95:6032-6036.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6032-6036
    • Weissenhorn, W.1    Calder, L.J.2    Wharton, S.A.3    Skehel, J.J.4    Wiley, D.C.5
  • 120
    • 0027959493 scopus 로고
    • Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection
    • Wild, C. T., D. C. Shugars, T. K. Greenwell, C. B. McDanal, and T. J. Matthews. 1994. Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection. Proc. Natl. Acad. Sci. USA 91:9770-9774.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9770-9774
    • Wild, C.T.1    Shugars, D.C.2    Greenwell, T.K.3    McDanal, C.B.4    Matthews, T.J.5
  • 121
    • 0010296944 scopus 로고
    • Biosynthesis, cleavage, and degradation of the human immunodeficiency virus 1 envelope glycoprotein gp160
    • Willey, R. L., J. S. Bonifacino, B. J. Potts, M. A. Martin, and R. D. Klausner. 1988. Biosynthesis, cleavage, and degradation of the human immunodeficiency virus 1 envelope glycoprotein gp160. Proc. Natl. Acad. Sci. USA 85:9580-9584.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 9580-9584
    • Willey, R.L.1    Bonifacino, J.S.2    Potts, B.J.3    Martin, M.A.4    Klausner, R.D.5
  • 122
    • 0018347043 scopus 로고
    • Electron microscopy of influenza virus
    • Wrigley, N. G. 1979. Electron microscopy of influenza virus. Br. Med. Bull. 35:35-38.
    • (1979) Br. Med. Bull. , vol.35 , pp. 35-38
    • Wrigley, N.G.1
  • 123
    • 0032546844 scopus 로고    scopus 로고
    • The HIV-1 envelope glycoproteins: Fusogens, antigens, and immunogens
    • Wyatt, R., and J. Sodroski. 1998. The HIV-1 envelope glycoproteins: fusogens, antigens, and immunogens. Science 280:1884-1888.
    • (1998) Science , vol.280 , pp. 1884-1888
    • Wyatt, R.1    Sodroski, J.2
  • 124
    • 0034004321 scopus 로고    scopus 로고
    • Modifications that stabilize human immunodeficiency virus envelope glycoprotein trimers in solution
    • Yang, X., L. Florin, M. Farzan, P. Kolchinsky, P. D. Kwong, J. Sodroski, and R. Wyatt. 2000. Modifications that stabilize human immunodeficiency virus envelope glycoprotein trimers in solution. J. Virol. 74:4746-4754.
    • (2000) J. Virol. , vol.74 , pp. 4746-4754
    • Yang, X.1    Florin, L.2    Farzan, M.3    Kolchinsky, P.4    Kwong, P.D.5    Sodroski, J.6    Wyatt, R.7
  • 125
    • 14744269583 scopus 로고    scopus 로고
    • Stoichiometry of antibody neutralization of human immunodeficiency virus type 1
    • Yang, X., S. Kurteva, S. Lee, and J. Sodroski. 2005. Stoichiometry of antibody neutralization of human immunodeficiency virus type 1. J. Virol. 79:3500-3508.
    • (2005) J. Virol. , vol.79 , pp. 3500-3508
    • Yang, X.1    Kurteva, S.2    Lee, S.3    Sodroski, J.4
  • 126
    • 0042389489 scopus 로고    scopus 로고
    • Role of the gp120 inner domain beta-sandwich in the interaction between the human immunodeficiency virus envelope glycoprotein subunits
    • Yang, X., E. Mahony, G. H. Holm, A. Kassa, and J. Sodroski. 2003. Role of the gp120 inner domain beta-sandwich in the interaction between the human immunodeficiency virus envelope glycoprotein subunits. Virology 313: 117-125.
    • (2003) Virology , vol.313 , pp. 117-125
    • Yang, X.1    Mahony, E.2    Holm, G.H.3    Kassa, A.4    Sodroski, J.5
  • 127
    • 2942661340 scopus 로고    scopus 로고
    • Modulation of Env content in virions of simian immunodeficiency virus: Correlation with cell surface expression and virion infectivity
    • Yuste, E., J. D. Reeves, R. W. Doms, and R. C. Desrosiers. 2004. Modulation of Env content in virions of simian immunodeficiency virus: correlation with cell surface expression and virion infectivity. J. Virol. 78:6775-6785.
    • (2004) J. Virol. , vol.78 , pp. 6775-6785
    • Yuste, E.1    Reeves, J.D.2    Doms, R.W.3    Desrosiers, R.C.4


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