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Volumn 4, Issue 4, 2003, Pages 309-319

The structural biology of type I viral membrane fusion

Author keywords

[No Author keywords available]

Indexed keywords

ENVELOPE PROTEIN; HEMAGGLUTININ;

EID: 0037381269     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrm1076     Document Type: Review
Times cited : (398)

References (97)
  • 1
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • Skehel, J. J. & Wiley, D. C. Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu. Rev. Biochem. 69, 531-569 (2000). A comprehensive review of the known properties of the influenza virus haemagglutinin and the structural basis of these properties.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 2
    • 0027517462 scopus 로고
    • A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion
    • Sollner, T., Bennett, M. K., Whiteheart, S. W., Scheller, R. H. & Rothman, J. E. A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion. Cell 75, 409-418 (1993).
    • (1993) Cell , vol.75 , pp. 409-418
    • Sollner, T.1    Bennett, M.K.2    Whiteheart, S.W.3    Scheller, R.H.4    Rothman, J.E.5
  • 3
    • 0032902197 scopus 로고    scopus 로고
    • Structural basis for membrane fusion by enveloped viruses
    • Weissenhorn, W. et al. Structural basis for membrane fusion by enveloped viruses. Mol. Membr. Biol. 16, 3-9 (1999).
    • (1999) Mol. Membr. Biol. , vol.16 , pp. 3-9
    • Weissenhorn, W.1
  • 4
    • 0034567567 scopus 로고    scopus 로고
    • Structures and mechanisms in flavivirus fusion
    • Heinz, F. X. & Allison, S. L. Structures and mechanisms in flavivirus fusion. Adv. Virus Res. 55, 231-269 (2000).
    • (2000) Adv. Virus Res. , vol.55 , pp. 231-269
    • Heinz, F.X.1    Allison, S.L.2
  • 5
    • 0033762350 scopus 로고    scopus 로고
    • Crystal structure of the multifunctional paramyxovirus hemagglutinin-neuraminidase
    • Crennell, S., Takimoto, T., Portner, A. & Taylor, G. Crystal structure of the multifunctional paramyxovirus hemagglutinin-neuraminidase. Nature Struct. Biol. 7, 1068-1074 (2000). This paper presents the structure of the HN attachment protein of NDV and provides a basis for interpreting data that link this protein to the fusion activity of the F protein.
    • (2000) Nature Struct. Biol. , vol.7 , pp. 1068-1074
    • Crennell, S.1    Takimoto, T.2    Portner, A.3    Taylor, G.4
  • 6
    • 0035083470 scopus 로고    scopus 로고
    • The structure of the fusion glycoprotein of Newcastle disease virus suggests a novel paradigm for the molecular mechanism of membrane fusion
    • Chen, L. et al. The structure of the fusion glycoprotein of Newcastle disease virus suggests a novel paradigm for the molecular mechanism of membrane fusion. Structure 9, 255-266 (2001). Together with influenza HA, the structure presented in this paper is one of only two that provide information on the pre-fusion conformation of a type I viral fusion protein.
    • (2001) Structure , vol.9 , pp. 255-266
    • Chen, L.1
  • 7
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 (tm) resolution
    • Wilson, I. A., Skehel, J. J. & Wiley, D. C. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 (tm) resolution. Nature 289, 366-373 (1981).
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 8
    • 18844470928 scopus 로고    scopus 로고
    • Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation
    • Chen, J. et al. Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation. Cell 95, 409-417 (1998).
    • (1998) Cell , vol.95 , pp. 409-417
    • Chen, J.1
  • 9
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough, P. A., Hughson, F. M., Skehel, J. J. & Wiley, D. C. Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 371, 37-43 (1994).
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 10
    • 0033529752 scopus 로고    scopus 로고
    • N- and C-terminal residues combine in the fusion-pH influenza hemagglutinin HA(2) subunit to form an N cap that terminates the triple-stranded coiled coil
    • Chen, J., Skehel, J. J. & Wiley, D. C. N- and C-terminal residues combine in the fusion-pH influenza hemagglutinin HA(2) subunit to form an N cap that terminates the triple-stranded coiled coil. Proc. Natl Acad. Sci. USA 96, 8967-8972 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 8967-8972
    • Chen, J.1    Skehel, J.J.2    Wiley, D.C.3
  • 11
    • 0030010945 scopus 로고    scopus 로고
    • 2 amino-terminal fusion peptide but not the coiled coil region
    • 2 amino-terminal fusion peptide but not the coiled coil region. J. Biol. Chem. 271, 13417-13421 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 13417-13421
    • Durrer, P.1
  • 12
    • 0020035202 scopus 로고
    • Changes in the conformation of influenza virus hemagglutinin at the pH optimum of virus-mediated membrane fusion
    • Skehel, J. J. et al. Changes in the conformation of influenza virus hemagglutinin at the pH optimum of virus-mediated membrane fusion. Proc. Natl Acad. Sci. USA 79, 968-972 (1982).
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 968-972
    • Skehel, J.J.1
  • 13
    • 0031678678 scopus 로고    scopus 로고
    • A mechanism of protein-mediated fusion: Coupling between refolding of the influenza hemagglutinin and lipid rearrangements
    • Kozlov, M. M. & Chernomordik, L. V. A mechanism of protein-mediated fusion: coupling between refolding of the influenza hemagglutinin and lipid rearrangements. Biophys. J. 75, 1384-1396 (1998).
    • (1998) Biophys. J. , vol.75 , pp. 1384-1396
    • Kozlov, M.M.1    Chernomordik, L.V.2
  • 14
    • 0034120341 scopus 로고    scopus 로고
    • Membrane fusion mediated by coiled coils: A hypothesis
    • Bentz, J. Membrane fusion mediated by coiled coils: a hypothesis. Biophys. J. 78, 886-900 (2000).
    • (2000) Biophys. J. , vol.78 , pp. 886-900
    • Bentz, J.1
  • 15
    • 0036231335 scopus 로고    scopus 로고
    • New insights into the spring-loaded conformational change of influenza virus hemagglutinin
    • Gruenke, J. A., Armstrong, R. T., Newcomb, W. W., Brown, J. C. & White, J. M. New insights into the spring-loaded conformational change of influenza virus hemagglutinin. J. Virol. 76, 4456-4466 (2002).
    • (2002) J. Virol. , vol.76 , pp. 4456-4466
    • Gruenke, J.A.1    Armstrong, R.T.2    Newcomb, W.W.3    Brown, J.C.4    White, J.M.5
  • 16
    • 0026560161 scopus 로고
    • Introduction of intersubunit disulfide bonds in the membrane-distal region of the influenza hemagglutinin abolishes membrane fusion activity
    • Godley, L. et al. Introduction of intersubunit disulfide bonds in the membrane-distal region of the influenza hemagglutinin abolishes membrane fusion activity. Cell 68, 635-645. (1992).
    • (1992) Cell , vol.68 , pp. 635-645
    • Godley, L.1
  • 17
    • 0022657187 scopus 로고
    • Studies of influenza haemagglutinin-mediated membrane fusion
    • Wharton, S. A., Skehel, J. J. & Wiley, D. C. Studies of influenza haemagglutinin-mediated membrane fusion. Virology 149, 27-35 (1986).
    • (1986) Virology , vol.149 , pp. 27-35
    • Wharton, S.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 18
    • 0022886353 scopus 로고
    • Conformational changes in the hemagglutinin of influenza virus which accompany heat-induced fusion of virus with liposomes
    • Ruigrok, R. W. H. et al. Conformational changes in the hemagglutinin of influenza virus which accompany heat-induced fusion of virus with liposomes. Virology 155, 484-497 (1986).
    • (1986) Virology , vol.155 , pp. 484-497
    • Ruigrok, R.W.H.1
  • 19
    • 0002506954 scopus 로고
    • ed. Bentz, J. CRC Press, Boca Raton, Florida, USA
    • Stegmann, T. & Helenius, A. in Viral Fusion Mechanisms (ed. Bentz, J.) 89-111 (CRC Press, Boca Raton, Florida, USA, 1993).
    • (1993) Viral Fusion Mechanisms , pp. 89-111
    • Stegmann, T.1    Helenius, A.2
  • 20
    • 0019051305 scopus 로고
    • Influenza virus haemagglutinin. Structural predictions suggest that the fibrillar appearance is due to the presence of a coiled-coil
    • Ward, C. W. & Dopheide, T. A. Influenza virus haemagglutinin. Structural predictions suggest that the fibrillar appearance is due to the presence of a coiled-coil. Aust. J. Biol. Sci. 33, 441-447 (1980).
    • (1980) Aust. J. Biol. Sci. , vol.33 , pp. 441-447
    • Ward, C.W.1    Dopheide, T.A.2
  • 21
    • 0024968289 scopus 로고
    • Leucine zipper motif extends
    • Buckland, R. & Wild, F. Leucine zipper motif extends. Nature 338, 547 (1989).
    • (1989) Nature , vol.338 , pp. 547
    • Buckland, R.1    Wild, F.2
  • 22
    • 0025678671 scopus 로고
    • Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins
    • Chambers, P., Pringle, C. R. & Easton, A. J. Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins. J. Gen. Virol. 71, 3075-3080 (1990).
    • (1990) J. Gen. Virol. , vol.71 , pp. 3075-3080
    • Chambers, P.1    Pringle, C.R.2    Easton, A.J.3
  • 23
    • 0035950928 scopus 로고    scopus 로고
    • Cloning, expression, and crystallization of the fusion protein of Newcastle disease virus
    • Chen, L. et al. Cloning, expression, and crystallization of the fusion protein of Newcastle disease virus. Virology 290, 290-299 (2001).
    • (2001) Virology , vol.290 , pp. 290-299
    • Chen, L.1
  • 24
    • 0343618590 scopus 로고    scopus 로고
    • Electron microscopy of the human respiratory syncytial virus fusion protein and complexes that t forms with monoclonal antibodies
    • Calder, L. J. et al. Electron microscopy of the human respiratory syncytial virus fusion protein and complexes that t forms with monoclonal antibodies. Virology 271, 122-131 (2000).
    • (2000) Virology , vol.271 , pp. 122-131
    • Calder, L.J.1
  • 25
    • 0035264638 scopus 로고    scopus 로고
    • Paramyxovirus fusion (F) protein: A conformational change on cleavage activation
    • Dutch, R. E., Hagglund, R. N., Nagel, M. A., Paterson, R. G. & Lamb, R. A. Paramyxovirus fusion (F) protein: a conformational change on cleavage activation. Virology 281, 138-150 (2001).
    • (2001) Virology , vol.281 , pp. 138-150
    • Dutch, R.E.1    Hagglund, R.N.2    Nagel, M.A.3    Paterson, R.G.4    Lamb, R.A.5
  • 26
    • 0034712879 scopus 로고    scopus 로고
    • Fusion protein of the paramyxoviros SV5: Destabilizing and stabilizing mutants of fusion activation
    • Paterson, R. G., Russell, C. J. & Lamb, R. A. Fusion protein of the paramyxoviros SV5: destabilizing and stabilizing mutants of fusion activation. Virology 270, 17-30 (2000).
    • (2000) Virology , vol.270 , pp. 17-30
    • Paterson, R.G.1    Russell, C.J.2    Lamb, R.A.3
  • 27
    • 0034713246 scopus 로고    scopus 로고
    • Temperature dependence of fusion by Sendai virus
    • Wharton, S. A., Skehel, J. J. & Wiley, D. C. Temperature dependence of fusion by Sendai virus. Virology 271, 71-78 (2000).
    • (2000) Virology , vol.271 , pp. 71-78
    • Wharton, S.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 28
    • 0027430672 scopus 로고
    • Paramyxovirus fusion: A hypothesis for changes
    • Lamb, R. A. Paramyxovirus fusion: a hypothesis for changes. Virology 197, 1-11 (1993).
    • (1993) Virology , vol.197 , pp. 1-11
    • Lamb, R.A.1
  • 29
    • 0028076285 scopus 로고
    • Regions on the hemagglutinin-neuraminidase proteins of human parainfluenza virus type-1 and Sendai virus important for membrane fusion
    • Bousse, T., Takimoto, T., Gorman, W. L., Takahashi, T. & Portner, A. Regions on the hemagglutinin-neuraminidase proteins of human parainfluenza virus type-1 and Sendai virus important for membrane fusion. Virology 204, 506-514 (1994).
    • (1994) Virology , vol.204 , pp. 506-514
    • Bousse, T.1    Takimoto, T.2    Gorman, W.L.3    Takahashi, T.4    Portner, A.5
  • 30
    • 0029836433 scopus 로고    scopus 로고
    • Functional interaction of paramyxovirus glycoproteins: Identification of a domain in Sendai virus HN which promotes cell fusion
    • Tanabayashi, K. & Compans, R. W. Functional interaction of paramyxovirus glycoproteins: identification of a domain in Sendai virus HN which promotes cell fusion. Virology 70, 6112-6118 (1996).
    • (1996) Virology , vol.70 , pp. 6112-6118
    • Tanabayashi, K.1    Compans, R.W.2
  • 31
    • 0032899490 scopus 로고    scopus 로고
    • Mutational analysis of heptad repeats in the membrane-proximal region of Newcastle disease virus HN protein
    • Stone-Hulslander, J. & Morrison, T. G. Mutational analysis of heptad repeats in the membrane-proximal region of Newcastle disease virus HN protein. J. Virol. 73, 3630-3637 (1999).
    • (1999) J. Virol. , vol.73 , pp. 3630-3637
    • Stone-Hulslander, J.1    Morrison, T.G.2
  • 32
    • 0029036804 scopus 로고
    • A single amino acid change enhances the fusion promotion activity of human parainfluenza virus type 1 hemagglutinin-neuraminidase glycoprotein
    • Bousse, T., Takimoto, T. & Portner, A. A single amino acid change enhances the fusion promotion activity of human parainfluenza virus type 1 hemagglutinin-neuraminidase glycoprotein. Virology 209, 654-657 (1995).
    • (1995) Virology , vol.209 , pp. 654-657
    • Bousse, T.1    Takimoto, T.2    Portner, A.3
  • 33
    • 0033524341 scopus 로고    scopus 로고
    • Mutations in the Newcastle disease virus hemagglutinin-neuraminidase protein that interfere with its ability to interact with the homologous F protein in the promotion of fusion
    • Deng, R. et al. Mutations in the Newcastle disease virus hemagglutinin-neuraminidase protein that interfere with its ability to interact with the homologous F protein in the promotion of fusion. Virology 253, 43-54 (1999).
    • (1999) Virology , vol.253 , pp. 43-54
    • Deng, R.1
  • 34
    • 0036891868 scopus 로고    scopus 로고
    • Role of the hemagglutinin-neuraminidase protein in the mechanism of paramyxovirus-cell membrane fusion
    • Takimoto, T., Taylor, G. L., Connaris, H. C., Crennell, S. J. & Portner, A. Role of the hemagglutinin-neuraminidase protein in the mechanism of paramyxovirus-cell membrane fusion. J. Virol. 76, 13028-13033 (2002).
    • (2002) J. Virol. , vol.76 , pp. 13028-13033
    • Takimoto, T.1    Taylor, G.L.2    Connaris, H.C.3    Crennell, S.J.4    Portner, A.5
  • 35
    • 0031060164 scopus 로고    scopus 로고
    • Association of the parainfluenza virus fusion and hemagglutinin-neuraminidase glycoproteins on cell surfaces
    • Yao, Q., Hu, X. & Compans, R. W. Association of the parainfluenza virus fusion and hemagglutinin-neuraminidase glycoproteins on cell surfaces. J. Virol. 71, 650-656 (1997).
    • (1997) J. Virol. , vol.71 , pp. 650-656
    • Yao, Q.1    Hu, X.2    Compans, R.W.3
  • 36
    • 0030761711 scopus 로고    scopus 로고
    • Detection of an interaction between the HN and F proteins in Newcastle disease virus-infected cells
    • Stone-Hulslander, J. & Morrison, T. G. Detection of an interaction between the HN and F proteins in Newcastle disease virus-infected cells. J. Virol. 71, 6287-6295 (1997).
    • (1997) J. Virol. , vol.71 , pp. 6287-6295
    • Stone-Hulslander, J.1    Morrison, T.G.2
  • 37
    • 0030997127 scopus 로고    scopus 로고
    • Epitope map of human immunodeficiency virus type 1 gp41 derived from 47 monoclonal antibodies produced by immunization with oligomeric envelope protein
    • Earl, P. L., Broder, C. C., Doms, R. W. & Moss, B. Epitope map of human immunodeficiency virus type 1 gp41 derived from 47 monoclonal antibodies produced by immunization with oligomeric envelope protein. J. Virol. 71, 2674-2684 (1997).
    • (1997) J. Virol. , vol.71 , pp. 2674-2684
    • Earl, P.L.1    Broder, C.C.2    Doms, R.W.3    Moss, B.4
  • 38
    • 0028355456 scopus 로고
    • Native oligomeric human immunodeficiency virus type 1 envelope glycoprotein elicits diverse monoclonal antibody reactivities
    • Earl, P. L. et al. Native oligomeric human immunodeficiency virus type 1 envelope glycoprotein elicits diverse monoclonal antibody reactivities. J. Virol. 68, 3015-3026 (1994).
    • (1994) J. Virol. , vol.68 , pp. 3015-3026
    • Earl, P.L.1
  • 39
    • 0032899496 scopus 로고    scopus 로고
    • Functional dissection of CCR5 coreceptor function through the use of CD4-independent simian immunodeficiency virus strains
    • Edinger, A. L. et al. Functional dissection of CCR5 coreceptor function through the use of CD4-independent simian immunodeficiency virus strains. J. Virol. 73, 4062-4073 (1999).
    • (1999) J. Virol. , vol.73 , pp. 4062-4073
    • Edinger, A.L.1
  • 40
    • 0025572710 scopus 로고
    • Dissociation of gp120 from HIV-1 virions induced by soluble CD4
    • Moore, J. P., McKeating, J. A., Weiss, R. A. & Sattentau, Q. J. Dissociation of gp120 from HIV-1 virions induced by soluble CD4. Science 250, 1130-1142 (1990).
    • (1990) Science , vol.250 , pp. 1130-1142
    • Moore, J.P.1    McKeating, J.A.2    Weiss, R.A.3    Sattentau, Q.J.4
  • 41
    • 0030023304 scopus 로고    scopus 로고
    • Neutralizing antibodies to human immunodeficiency virus type-1 gp120 induce envelope glycoprotein subunit dissociation
    • Poignard, P., Fouts, T., Naniche, D., Moore, J. P. & Sattentau, Q. J. Neutralizing antibodies to human immunodeficiency virus type-1 gp120 induce envelope glycoprotein subunit dissociation. J. Exp. Med. 183, 473-484 (1996).
    • (1996) J. Exp. Med. , vol.183 , pp. 473-484
    • Poignard, P.1    Fouts, T.2    Naniche, D.3    Moore, J.P.4    Sattentau, Q.J.5
  • 42
    • 0030987357 scopus 로고    scopus 로고
    • Assembly of a rod-shaped chimera of a trimeric GCN4 zipper and the HIV-1 gp41 ectodomain expressed in Escherichia coli
    • Weissenhorn, W. et al. Assembly of a rod-shaped chimera of a trimeric GCN4 zipper and the HIV-1 gp41 ectodomain expressed in Escherichia coli. Proc. Natl Acad. Sci. USA 94, 6065-6069 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6065-6069
    • Weissenhorn, W.1
  • 44
    • 0033563698 scopus 로고    scopus 로고
    • The crystal structure of the SIV gp41 ectodomain at 1.47 (tm) resolution
    • Yang, Z. N. et al. The crystal structure of the SIV gp41 ectodomain at 1.47 (tm) resolution. J. Struct. Biol. 126, 131-144 (1999). This paper describes a high-resolution study of the fusion-core structure of simian immunodeficiency virus (SIV), which expands on the information that has been reported in parallel studies of HIV.
    • (1999) J. Struct. Biol. , vol.126 , pp. 131-144
    • Yang, Z.N.1
  • 45
    • 0026792879 scopus 로고
    • Lack of correlation between soluble CD4-induced shedding of the human immunodeficiency virus type 1 exterior envelope glycoprotein and subsequent membrane fusion events
    • Thali, M., Furman, C., Helseth, E., Repke, H. & Sodroski, J. Lack of correlation between soluble CD4-induced shedding of the human immunodeficiency virus type 1 exterior envelope glycoprotein and subsequent membrane fusion events. J. Virol. 66, 5516-5524 (1992).
    • (1992) J. Virol. , vol.66 , pp. 5516-5524
    • Thali, M.1    Furman, C.2    Helseth, E.3    Repke, H.4    Sodroski, J.5
  • 46
    • 0025866185 scopus 로고
    • Conformational changes induced in the human immunodeficiency virus envelope glycoproteins by soluble CD4 binding
    • Sattentau, Q. J. & Moore, J. P. Conformational changes induced in the human immunodeficiency virus envelope glycoproteins by soluble CD4 binding. J. Exp. Med. 174, 407-415 (1991).
    • (1991) J. Exp. Med. , vol.174 , pp. 407-415
    • Sattentau, Q.J.1    Moore, J.P.2
  • 47
    • 0027256814 scopus 로고
    • Characterization of human immunodeficiency virus type 1 (HIV-1) gp120 neutralization epitopes exposed upon gp120-CD4 binding
    • Thali, M. et al. Characterization of human immunodeficiency virus type 1 (HIV-1) gp120 neutralization epitopes exposed upon gp120-CD4 binding. J. Virol. 67, 3978-3988 (1993).
    • (1993) J. Virol. , vol.67 , pp. 3978-3988
    • Thali, M.1
  • 48
    • 0027488547 scopus 로고
    • Conformational changes induced in the envelope glycoproteins of the human and simian immunodeficiency viruses by soluble receptor binding
    • Sattentau, Q. J., Moore, J. P., Vignaux, F., Traincard, F. & Poignard, P. Conformational changes induced in the envelope glycoproteins of the human and simian immunodeficiency viruses by soluble receptor binding. J. Virol. 67, 7383-7393 (1993).
    • (1993) J. Virol. , vol.67 , pp. 7383-7393
    • Sattentau, Q.J.1    Moore, J.P.2    Vignaux, F.3    Traincard, F.4    Poignard, P.5
  • 49
    • 0034255034 scopus 로고    scopus 로고
    • Energetics of the HIV gp120-CD4 binding reaction
    • Myszka, D. G. et al. Energetics of the HIV gp120-CD4 binding reaction. Proc. Natl Acad. Sci. USA 97, 9026-9031 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9026-9031
    • Myszka, D.G.1
  • 50
    • 0037069682 scopus 로고    scopus 로고
    • HIV-1 evades antibody-mediated neutralization through conformational masking of receptor-binding sites
    • Kwong, P. D. et al. HIV-1 evades antibody-mediated neutralization through conformational masking of receptor-binding sites. Nature 420, 678-682 (2002). This article describes a thermodynamic study of the binding of gp120 to CD4, which indicates that very large conformational changes accompany the binding event.
    • (2002) Nature , vol.420 , pp. 678-682
    • Kwong, P.D.1
  • 51
    • 0033985999 scopus 로고    scopus 로고
    • A recombinant human immunodeficiency virus type 1 envelope glycoprotein complex stabilized by an intermolecular disulfide bond between the gp120 and gp41 subunits is an antigenic mimic of the trimeric virion-associated structure
    • Binley, J. M. et al. A recombinant human immunodeficiency virus type 1 envelope glycoprotein complex stabilized by an intermolecular disulfide bond between the gp120 and gp41 subunits is an antigenic mimic of the trimeric virion-associated structure. J. Virol. 74, 627-643 (2000).
    • (2000) J. Virol. , vol.74 , pp. 627-643
    • Binley, J.M.1
  • 52
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan, D. C., Fass, D., Berger, J. M. & Kim, P. S. Core structure of gp41 from the HIV envelope glycoprotein. Cell 89, 263-273 (1997).
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 53
    • 0033919404 scopus 로고    scopus 로고
    • Oligomeric modeling and electrostatic analysis of the gp120 envelope glycoprotein of human immunodeficiency virus
    • Kwong, P. D., Wyatt, R., Sattentau, Q. J., Sodroski, J. & Hendrickson, W. A. Oligomeric modeling and electrostatic analysis of the gp120 envelope glycoprotein of human immunodeficiency virus. J. Virol. 74, 1961-1972 (2000).
    • (2000) J. Virol. , vol.74 , pp. 1961-1972
    • Kwong, P.D.1    Wyatt, R.2    Sattentau, Q.J.3    Sodroski, J.4    Hendrickson, W.A.5
  • 54
    • 0032543307 scopus 로고    scopus 로고
    • Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
    • Kwong, P. D. et al. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 393, 648-659 (1998).
    • (1998) Nature , vol.393 , pp. 648-659
    • Kwong, P.D.1
  • 55
    • 0026465468 scopus 로고
    • A synthetic peptide inhibitor of human immunodeficiency virus replication: Correlation between solution structure and viral inhibition
    • Wild, C., Oas, T., McDanal, C., Bolognesi, D. & Matthews, T. A synthetic peptide inhibitor of human immunodeficiency virus replication: correlation between solution structure and viral inhibition. Proc. Natl Acad. Sci. USA 89, 10537-10541 (1992).
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10537-10541
    • Wild, C.1    Oas, T.2    McDanal, C.3    Bolognesi, D.4    Matthews, T.5
  • 56
    • 0027959493 scopus 로고
    • Peptides corresponding to a predictive α-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection
    • Wild, C. T., Shugars, D. C., Greenwell, T. K., McDanal, C. B. & Matthews, T. J. Peptides corresponding to a predictive α-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection. Proc. Natl Acad. Sci. USA 91, 9770-9774 (1994).
    • (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
  • 57
    • 0028864218 scopus 로고
    • A synthetic peptide corresponding to a conserved heptad repeat domain is a potent inhibitor of Sendai virus-cell fusion: An emerging similarity with functional domains of other viruses
    • Rapaport, D., Ovadia, M. & Shai, Y. A synthetic peptide corresponding to a conserved heptad repeat domain is a potent inhibitor of Sendai virus-cell fusion: an emerging similarity with functional domains of other viruses. EMBO J. 14, 5524-5531 (1995).
    • (1995) EMBO J. , vol.14 , pp. 5524-5531
    • Rapaport, D.1    Ovadia, M.2    Shai, Y.3
  • 58
    • 9044234408 scopus 로고    scopus 로고
    • Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion
    • Lambert, D. M. et al. Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion. Proc. Natl Acad. Sci. USA 93, 2186-2191 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2186-2191
    • Lambert, D.M.1
  • 59
    • 0030245704 scopus 로고    scopus 로고
    • Peptides corresponding to the heptad repeat sequence of human parainfluenza virus fusion protein are potent inhibitors of virus infection
    • Yao, Q. & Compans, R. W. Peptides corresponding to the heptad repeat sequence of human parainfluenza virus fusion protein are potent inhibitors of virus infection. Virology 223, 103-112 (1996).
    • (1996) Virology , vol.223 , pp. 103-112
    • Yao, Q.1    Compans, R.W.2
  • 60
    • 0028834461 scopus 로고
    • A trimeric structural domain of the HIV-1 transmembrane glycoprotein
    • Lu, M., Blacklow, S. C. & Kim, P. S. A trimeric structural domain of the HIV-1 transmembrane glycoprotein. Nature Struct. Biol. 2, 1075-1082 (1995).
    • (1995) Nature Struct. Biol. , vol.2 , pp. 1075-1082
    • Lu, M.1    Blacklow, S.C.2    Kim, P.S.3
  • 61
    • 0031729823 scopus 로고    scopus 로고
    • Potent suppression of HIV-1 replication in humans by T-20, a peptide inhibitor of gp41-mediated virus entry
    • Kilby, J. M. et al. Potent suppression of HIV-1 replication in humans by T-20, a peptide inhibitor of gp41-mediated virus entry. Nature Med. 4, 1302-1307 (1998). This work describes early clinical data, which indicate that new medicines might emerge from our growing understanding of the molecular basis of viral membrane fusion.
    • (1998) Nature Med. , vol.4 , pp. 1302-1307
    • Kilby, J.M.1
  • 62
    • 0031883832 scopus 로고    scopus 로고
    • Determinants of human immunodeficiency virus type 1 resistance to gp41-derived inhibitory peptides
    • Rimsky, L. T., Shugars, D. C. & Matthews, T. J. Determinants of human immunodeficiency virus type 1 resistance to gp41-derived inhibitory peptides. J. Virol. 72, 986-993 (1998).
    • (1998) J. Virol. , vol.72 , pp. 986-993
    • Rimsky, L.T.1    Shugars, D.C.2    Matthews, T.J.3
  • 63
    • 0032433685 scopus 로고    scopus 로고
    • Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target
    • Chan, D. C., Chutkowski, C. T. & Kim, P. S. Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target. Proc. Natl Acad. Sci. USA 95, 15613-15617 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 15613-15617
    • Chan, D.C.1    Chutkowski, C.T.2    Kim, P.S.3
  • 64
    • 0033214895 scopus 로고    scopus 로고
    • Inhibiting HIV-1 entry: Discovery of D-peptide inhibitors that target the gp41 coiled-coil pocket
    • Eckert, D. M., Malashkevich, V. N., Hong, L. H., Carr, P. A. & Kim, P. S. Inhibiting HIV-1 entry: discovery of D-peptide inhibitors that target the gp41 coiled-coil pocket. Cell 99, 103-115 (1999).
    • (1999) Cell , vol.99 , pp. 103-115
    • Eckert, D.M.1    Malashkevich, V.N.2    Hong, L.H.3    Carr, P.A.4    Kim, P.S.5
  • 65
    • 0035421959 scopus 로고    scopus 로고
    • Membrane fusion machines of paramyxoviruses: Capture of intermediates of fusion
    • Russell, C. J., Jardetzky, T. S. & Lamb, R. A. Membrane fusion machines of paramyxoviruses: capture of intermediates of fusion. EMBO J. 20, 4024-4034 (2001). This paper decribes an important study of conformational changes in the F protein, which were probed using the inhibitory effects of N- and C-peptides.
    • (2001) EMBO J. , vol.20 , pp. 4024-4034
    • Russell, C.J.1    Jardetzky, T.S.2    Lamb, R.A.3
  • 66
    • 0033064154 scopus 로고    scopus 로고
    • Interaction of peptides with sequences from the Newcastle disease virus fusion protein heptad repeat regions
    • Young, J. K., Li, D., Abramowitz, M. C. & Morrison, T. G. Interaction of peptides with sequences from the Newcastle disease virus fusion protein heptad repeat regions. J. Virol. 73, 5945-5956 (1999).
    • (1999) J. Virol. , vol.73 , pp. 5945-5956
    • Young, J.K.1    Li, D.2    Abramowitz, M.C.3    Morrison, T.G.4
  • 67
    • 0031959601 scopus 로고    scopus 로고
    • Capture of an early fusion-active conformation of HIV-1 gp41
    • Furuta, R. A., Wild, C. T., Weng, Y. & Weiss, C. D. Capture of an early fusion-active conformation of HIV-1 gp41. Nature Struct. Biol. 5, 276-279 (1998).
    • (1998) Nature Struct. Biol. , vol.5 , pp. 276-279
    • Furuta, R.A.1    Wild, C.T.2    Weng, Y.3    Weiss, C.D.4
  • 68
    • 0034675886 scopus 로고    scopus 로고
    • Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion
    • Melikyan, G. B. et al. Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion. J. Cell Biol. 151, 413-423 (2000).
    • (2000) J. Cell Biol. , vol.151 , pp. 413-423
    • Melikyan, G.B.1
  • 69
    • 0034675998 scopus 로고    scopus 로고
    • HIV-1 membrane fusion: Targets of opportunity
    • Doms, R. W. & Moore, J. P. HIV-1 membrane fusion: targets of opportunity. J. Cell Biol. 151, F9-F14 (2000).
    • (2000) J. Cell Biol. , vol.151
    • Doms, R.W.1    Moore, J.P.2
  • 70
    • 0037470227 scopus 로고    scopus 로고
    • The prefusogenic intermediate of HIV-1 gp41 contains exposed C-peptide regions
    • Koshiba, T. & Chan, D. C. The prefusogenic intermediate of HIV-1 gp41 contains exposed C-peptide regions. J. Biol. Chem. 278, 7573-7579 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 7573-7579
    • Koshiba, T.1    Chan, D.C.2
  • 71
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 72
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt, E. A. & Bacon, D. J. Raster3D: photorealistic molecular graphics. Meth. Enzymol. 277, 505-524 (1997).
    • (1997) Meth. Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 73
    • 0000732609 scopus 로고
    • GRASP: Graphical representation and analysis of surface properties
    • Nicholls, A. GRASP: graphical representation and analysis of surface properties. Biophys. J. 64, A116 (1993).
    • (1993) Biophys. J. , vol.64
    • Nicholls, A.1
  • 74
    • 0026058342 scopus 로고
    • Measles virus: Both the haemagglutinin and fusion glycoproteins are required for fusion
    • Wild, T. F., Malvoisin, E. & Buckland, R. Measles virus: both the haemagglutinin and fusion glycoproteins are required for fusion. J. Gen. Virol. 72, 439-442 (1991).
    • (1991) J. Gen. Virol. , vol.72 , pp. 439-442
    • Wild, T.F.1    Malvoisin, E.2    Buckland, R.3
  • 75
    • 0025769866 scopus 로고
    • The fusion and hemagglutinin-neuraminidase glycoproteins of human parainfluenza virus 3 are both required for fusion
    • Ebata, S. N., Cote, M.-J., Yong Kang, C. & Dimock, K. The fusion and hemagglutinin-neuraminidase glycoproteins of human parainfluenza virus 3 are both required for fusion. Virology 183, 437-441 (1991).
    • (1991) Virology , vol.183 , pp. 437-441
    • Ebata, S.N.1    Cote, M.-J.2    Yong Kang, C.3    Dimock, K.4
  • 76
    • 0026525004 scopus 로고
    • Functional interactions between the fusion protein and hemagglutinin-neuraminidase of human parainfluenza viruses
    • Hu, X., Ray, R. & Compans, R. W. Functional interactions between the fusion protein and hemagglutinin-neuraminidase of human parainfluenza viruses. J. Virol. 66, 1528-1534 (1992).
    • (1992) J. Virol. , vol.66 , pp. 1528-1534
    • Hu, X.1    Ray, R.2    Compans, R.W.3
  • 77
    • 0028883780 scopus 로고
    • Quantitative measurement of paramyxovirus fusion: Differences in requirements of glycoproteins between simian virus 5 and human parainfluenxza virus 3 or Newcastle disease virus
    • Bagai, S. & Lamb, R. A. Quantitative measurement of paramyxovirus fusion: differences in requirements of glycoproteins between simian virus 5 and human parainfluenxza virus 3 or Newcastle disease virus. J. Virol. 69, 6712-6719 (1995).
    • (1995) J. Virol. , vol.69 , pp. 6712-6719
    • Bagai, S.1    Lamb, R.A.2
  • 78
    • 0030775365 scopus 로고    scopus 로고
    • 2 subunit in syncytium formation
    • 2 subunit in syncytium formation. J. Virol. 71, 9855-9858 (1997).
    • (1997) J. Virol. , vol.71 , pp. 9855-9858
    • Ito, M.1
  • 79
    • 0033953651 scopus 로고    scopus 로고
    • An amino acid in the heptad repeat 1 domain is important for the haemagglutinin-neuraminidase-independent fusing activity of simian virus 5 fusion protein
    • Ito, M., Nishio, M., Komada, H., Ito, Y. & Tsurudome, M. An amino acid in the heptad repeat 1 domain is important for the haemagglutinin-neuraminidase-independent fusing activity of simian virus 5 fusion protein. J. Gen. Virol. 81, 719-727 (2000).
    • (2000) J. Gen. Virol. , vol.81 , pp. 719-727
    • Ito, M.1    Nishio, M.2    Komada, H.3    Ito, Y.4    Tsurudome, M.5
  • 80
    • 0034853335 scopus 로고    scopus 로고
    • Hemagglutinin-neuraminidase-independent fusion activity of simian virus 5 fusion (F) protein: Difference in conformation between fusogenic and nonfusogenic F proteins on the cell surface
    • Tsurudome, M. et al. Hemagglutinin-neuraminidase-independent fusion activity of simian virus 5 fusion (F) protein: difference in conformation between fusogenic and nonfusogenic F proteins on the cell surface. J. Virol. 75, 8999-9009 (2001).
    • (2001) J. Virol. , vol.75 , pp. 8999-9009
    • Tsurudome, M.1
  • 81
    • 0034024481 scopus 로고    scopus 로고
    • A single amino acid change in the Newcastle disease virus fusion protein alters the requirement for HN protein in fusion
    • Sergel, T. A., McGinnes, L. W. & Morrison, T. G. A single amino acid change in the Newcastle disease virus fusion protein alters the requirement for HN protein in fusion. J. Virol. 74, 5101-5107 (2000).
    • (2000) J. Virol. , vol.74 , pp. 5101-5107
    • Sergel, T.A.1    McGinnes, L.W.2    Morrison, T.G.3
  • 82
    • 0037213923 scopus 로고    scopus 로고
    • Mutations in the cytoplasmic domain of a paramyxovirus fusion glycoprotein rescue syncytium formation and eliminate the hemagglutinin-neuraminidase protein requirement for membrane fusion
    • Seth, S., Vincent, A. & Compans, R. W. Mutations in the cytoplasmic domain of a paramyxovirus fusion glycoprotein rescue syncytium formation and eliminate the hemagglutinin-neuraminidase protein requirement for membrane fusion. J. Virol. 77, 167-178 (2003).
    • (2003) J. Virol. , vol.77 , pp. 167-178
    • Seth, S.1    Vincent, A.2    Compans, R.W.3
  • 83
    • 0037301459 scopus 로고    scopus 로고
    • Evidence for mixed membrane topology of the Newcastle disease virus fusion protein
    • McGinnes, L. W., Reitter, J. N., Gravel, K. & Morrison, T. G. Evidence for mixed membrane topology of the Newcastle disease virus fusion protein. J. Virol. 77, 1951-1963 (2003).
    • (2003) J. Virol. , vol.77 , pp. 1951-1963
    • McGinnes, L.W.1    Reitter, J.N.2    Gravel, K.3    Morrison, T.G.4
  • 84
    • 0032054629 scopus 로고    scopus 로고
    • CL387626 exhibits marked and unusual antiviral activity against respiratory syncytial virus in tissue culture and in cotton rats
    • Wyde, P. R. et al. CL387626 exhibits marked and unusual antiviral activity against respiratory syncytial virus in tissue culture and in cotton rats. Antiviral Res. 38, 31-42 (1998).
    • (1998) Antiviral Res. , vol.38 , pp. 31-42
    • Wyde, P.R.1
  • 85
    • 0034102408 scopus 로고    scopus 로고
    • Inhibition of respiratory syncytial virus by a new class of chemotherapeutic agents
    • Aulabaugh, A. et al. Inhibition of respiratory syncytial virus by a new class of chemotherapeutic agents. Drugs of the Future 25, 287-294 (2000).
    • (2000) Drugs of the Future , vol.25 , pp. 287-294
    • Aulabaugh, A.1
  • 86
    • 4243335062 scopus 로고    scopus 로고
    • R170591, a new antiviral with picomolar activity against respiratory syncytial virus
    • Andries, K. et al. R170591, a new antiviral with picomolar activity against respiratory syncytial virus. Antiviral Res. 50, S1-S94 (2001).
    • (2001) Antiviral Res. , vol.50
    • Andries, K.1
  • 87
    • 0033607028 scopus 로고    scopus 로고
    • Structure-based identification of small molecule antiviral compounds targeted to the gp41 core structure of the human immunodeficiency virus type 1
    • Debnath, A. K., Radigan, L. & Jiang, S. Structure-based identification of small molecule antiviral compounds targeted to the gp41 core structure of the human immunodeficiency virus type 1. J. Med. Chem. 42, 3203-3209 (1999).
    • (1999) J. Med. Chem. , vol.42 , pp. 3203-3209
    • Debnath, A.K.1    Radigan, L.2    Jiang, S.3
  • 88
    • 0036223198 scopus 로고    scopus 로고
    • Peptide and non-peptide HIV fusion inhibitors
    • Jiang, S., Zhao, Q. & Debnath, A. K. Peptide and non-peptide HIV fusion inhibitors. Curr. Pharm. Des. 8, 563-580 (2002).
    • (2002) Curr. Pharm. Des. , vol.8 , pp. 563-580
    • Jiang, S.1    Zhao, Q.2    Debnath, A.K.3
  • 89
    • 17944384967 scopus 로고    scopus 로고
    • The structure of an HIV-1 specific cell entry inhibitor in complex with the HIV-1 gp41 trimeric core
    • Zhou, G. et al. The structure of an HIV-1 specific cell entry inhibitor in complex with the HIV-1 gp41 trimeric core. Bioorg. Med. Chem. 8, 2219-2227 (2000).
    • (2000) Bioorg. Med. Chem. , vol.8 , pp. 2219-2227
    • Zhou, G.1
  • 90
    • 0036268548 scopus 로고    scopus 로고
    • Modelling the structure of the fusion protein from human respiratory syncytial virus
    • Smith, B. J., Lawrence, M. C. & Colman, P. M. Modelling the structure of the fusion protein from human respiratory syncytial virus. Protein Eng. 15, 365-371 (2002).
    • (2002) Protein Eng. , vol.15 , pp. 365-371
    • Smith, B.J.1    Lawrence, M.C.2    Colman, P.M.3
  • 91
    • 0030053758 scopus 로고    scopus 로고
    • Generation and characterization of variants of NWS/G70C influenza virus after in vitro passage in 4-amino-Neu5Ac2en and 4-guanidino-Neu 5Ac2en
    • McKimm-Breschkin, J. L. et al. Generation and characterization of variants of NWS/G70C influenza virus after in vitro passage in 4-amino-Neu5Ac2en and 4-guanidino-Neu5Ac2en. Antimicrob. Agents Chemother. 40, 40-46 (1996).
    • (1996) Antimicrob. Agents Chemother. , vol.40 , pp. 40-46
    • McKimm-Breschkin, J.L.1
  • 92
    • 0029585928 scopus 로고
    • Generation and characterization of an influenza virus neuraminidase variant with decreased sensitivity to the neuraminidase-specific inhibitor 4-guanidino-Neu 5Ac2en
    • Blick, T. J. et al. Generation and characterization of an influenza virus neuraminidase variant with decreased sensitivity to the neuraminidase-specific inhibitor 4-guanidino-Neu5Ac2en. Virology 214, 475-484 (1995).
    • (1995) Virology , vol.214 , pp. 475-484
    • Blick, T.J.1
  • 93
    • 0028113435 scopus 로고
    • Influenza virus neuraminidase: Structure, antibodies, and inhibitors
    • Colman, P. M. Influenza virus neuraminidase: structure, antibodies, and inhibitors. Protein Sci. 3, 1687-1696 (1994).
    • (1994) Protein Sci. , vol.3 , pp. 1687-1696
    • Colman, P.M.1
  • 94
    • 0034469926 scopus 로고    scopus 로고
    • The anti-influenza virus agent 4-GU-DANA (zanamivir) inhibits cell fusion mediated by human parainfluenza virus and influenza virus HA
    • Greengard, O., Poltoratskaia, N., Leikina, E., Zimmerberg, J. & Moscona, A. The anti-influenza virus agent 4-GU-DANA (zanamivir) inhibits cell fusion mediated by human parainfluenza virus and influenza virus HA. J. Virol 74, 11108-11114 (2000).
    • (2000) J. Virol , vol.74 , pp. 11108-11114
    • Greengard, O.1    Poltoratskaia, N.2    Leikina, E.3    Zimmerberg, J.4    Moscona, A.5
  • 95
    • 2942622122 scopus 로고    scopus 로고
    • Anti-HIV-1 activity of cellulose acetate phthalate: Synergy with soluble CD4 and induction of 'dead-end' gp41 six-helix bundles
    • Neurath, A. R., Strick, N., Jiang, S., Li, Y. Y. & Debnath, A. K. Anti-HIV-1 activity of cellulose acetate phthalate: synergy with soluble CD4 and induction of 'dead-end' gp41 six-helix bundles. BMC Infect. Dis. 2, 6 (2002).
    • (2002) BMC Infect. Dis. , vol.2 , pp. 6
    • Neurath, A.R.1    Strick, N.2    Jiang, S.3    Li, Y.Y.4    Debnath, A.K.5
  • 96
    • 0033106334 scopus 로고    scopus 로고
    • Structural basis for paramyxovirus-mediated membrane fusion
    • Baker, K. A., Dutch, R. E., Lamb, R. A. & Jardetzky, T. S. Structural basis for paramyxovirus-mediated membrane fusion. Mol. Cell 3, 309-319 (1999). This paper describes the structure of the complex of N- and C-peptides from the paramyxovirus F protein and links this family of viruses to HIV.
    • (1999) Mol. Cell , vol.3 , pp. 309-319
    • Baker, K.A.1    Dutch, R.E.2    Lamb, R.A.3    Jardetzky, T.S.4
  • 97
    • 0034687711 scopus 로고    scopus 로고
    • Structural characterization of the human respiratory syncytial virus fusion protein core
    • Zhao, X., Singh, M., Malashkevich, V. N. & Kim, P. S. Structural characterization of the human respiratory syncytial virus fusion protein core. Proc. Natl Acad. Sci. USA 97, 14172-14177 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 14172-14177
    • Zhao, X.1    Singh, M.2    Malashkevich, V.N.3    Kim, P.S.4


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