메뉴 건너뛰기




Volumn 64, Issue , 2005, Pages 231-261

Mechanism of Membrane Fusion by Viral Envelope Proteins

Author keywords

[No Author keywords available]

Indexed keywords

VIRUS ENVELOPE PROTEIN; VIRUS RECEPTOR;

EID: 26944466459     PISSN: 00653527     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0065-3527(05)64007-9     Document Type: Review
Times cited : (160)

References (85)
  • 1
    • 0036118329 scopus 로고    scopus 로고
    • The fusion peptide of Semliki Forest virus associates with sterol-rich membrane domains
    • Ahn A., Gibbons D.L., and Kielian M. The fusion peptide of Semliki Forest virus associates with sterol-rich membrane domains. J. Virol. 76 (2002) 3267-3275
    • (2002) J. Virol. , vol.76 , pp. 3267-3275
    • Ahn, A.1    Gibbons, D.L.2    Kielian, M.3
  • 3
    • 0035051804 scopus 로고    scopus 로고
    • Mutational evidence for an internal fusion peptide in flavivirus envelope protein E
    • Allison S.L., Schalich J., Stiasny K., Mandl C.W., and Heinz F.X. Mutational evidence for an internal fusion peptide in flavivirus envelope protein E. J. Virol. 75 (2001) 4268-4275
    • (2001) J. Virol. , vol.75 , pp. 4268-4275
    • Allison, S.L.1    Schalich, J.2    Stiasny, K.3    Mandl, C.W.4    Heinz, F.X.5
  • 4
    • 0028815675 scopus 로고
    • Oligomeric rearrangement of tick-borne encephalitis virus envelope proteins induced by an acidic pH
    • Allison S.L., Schalich J., Stiasny K., Mandl C.W., Kunz C., and Heinz F.X. Oligomeric rearrangement of tick-borne encephalitis virus envelope proteins induced by an acidic pH. J. Virol. 69 (1995) 695-700
    • (1995) J. Virol. , vol.69 , pp. 695-700
    • Allison, S.L.1    Schalich, J.2    Stiasny, K.3    Mandl, C.W.4    Kunz, C.5    Heinz, F.X.6
  • 5
    • 0032989258 scopus 로고    scopus 로고
    • Mapping of functional elements in the stem-anchor region of tick-borne encephalitis virus envelope protein E
    • Allison S.L., Stiasny K., Stadler K., Mandl C.W., and Heinz F.X. Mapping of functional elements in the stem-anchor region of tick-borne encephalitis virus envelope protein E. J. Virol. 73 (1999) 5605-5612
    • (1999) J. Virol. , vol.73 , pp. 5605-5612
    • Allison, S.L.1    Stiasny, K.2    Stadler, K.3    Mandl, C.W.4    Heinz, F.X.5
  • 6
    • 0034676041 scopus 로고    scopus 로고
    • The transmembrane domain of influenza hemagglutinin exhibits a stringent length requirement to support the hemifusion to fusion transition
    • Armstrong R.T., Kushnir A.S., and White J.M. The transmembrane domain of influenza hemagglutinin exhibits a stringent length requirement to support the hemifusion to fusion transition. J. Cell Biol. 151 (2000) 425-437
    • (2000) J. Cell Biol. , vol.151 , pp. 425-437
    • Armstrong, R.T.1    Kushnir, A.S.2    White, J.M.3
  • 7
    • 0028864614 scopus 로고
    • A trimeric subdomain of the simian immunodeficiency virus envelope glycoprotein
    • Blacklow S.C., Lu M., and Kim P.S. A trimeric subdomain of the simian immunodeficiency virus envelope glycoprotein. Biochemistry 34 (1995) 14955-14962
    • (1995) Biochemistry , vol.34 , pp. 14955-14962
    • Blacklow, S.C.1    Lu, M.2    Kim, P.S.3
  • 9
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough P.A., Hughson F.M., Skehel J.J., and Wiley D.C. Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 371 (1994) 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
  • 11
    • 0027253445 scopus 로고
    • A spring-loaded mechanism for the conformational change of influenza hemagglutinin
    • Carr C.M., and Kim P.S. A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell 73 (1993) 823-832
    • (1993) Cell , vol.73 , pp. 823-832
    • Carr, C.M.1    Kim, P.S.2
  • 12
    • 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., and 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 (1998) 15613-15617
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 15613-15617
    • Chan, D.C.1    Chutkowski, C.T.2    Kim, P.S.3
  • 13
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan D.C., Fass D., Berger J.M., and Kim P.S. Core structure of gp41 from the HIV envelope glycoprotein. Cell 89 (1997) 263-273
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 14
    • 0033529752 scopus 로고    scopus 로고
    • 2 subunit to form an N cap that terminates the triple-stranded coiled coil
    • 2 subunit to form an N cap that terminates the triple-stranded coiled coil. Proc. Natl. Acad. Sci. USA 96 (1999) 8967-8972
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 8967-8972
    • Chen, J.1    Skehel, J.J.2    Wiley, D.C.3
  • 15
    • 0038468973 scopus 로고    scopus 로고
    • The process of membrane fusion: Nipples, hemifusion, pores, and pore growth
    • Cohen F.S., Markosyan R.M., and Melikyan G.B. The process of membrane fusion: Nipples, hemifusion, pores, and pore growth. Curr. Top. Membr. 52 (2002) 501-529
    • (2002) Curr. Top. Membr. , vol.52 , pp. 501-529
    • Cohen, F.S.1    Markosyan, R.M.2    Melikyan, G.B.3
  • 17
    • 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., Pelletier S.L., Henis Y.I., and White J.M. Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers. J. Cell Biol. 133 (1996) 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
  • 19
    • 0035037386 scopus 로고    scopus 로고
    • Deletion of the cytoplasmic tail of the fusion protein of the paramyxovirus simian virus 5 affects fusion pore enlargement
    • Dutch R.E., and Lamb R.A. Deletion of the cytoplasmic tail of the fusion protein of the paramyxovirus simian virus 5 affects fusion pore enlargement. J. Virol. 75 (2001) 5363-5369
    • (2001) J. Virol. , vol.75 , pp. 5363-5369
    • Dutch, R.E.1    Lamb, R.A.2
  • 20
    • 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., and Kim P.S. Inhibiting HIV-1 entry: Discovery of D-peptide inhibitors that target the gp41 coiled-coil pocket. Cell 99 (1999) 103-115
    • (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
  • 21
    • 0029914299 scopus 로고    scopus 로고
    • Retrovirus envelope domain at 1.7 Å resolution
    • Fass D., Harrison S.C., and Kim P.S. Retrovirus envelope domain at 1.7 Å resolution. Nat. Struct. Biol. 3 (1996) 465-469
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 465-469
    • Fass, D.1    Harrison, S.C.2    Kim, P.S.3
  • 22
    • 0030002637 scopus 로고    scopus 로고
    • HIV-1 entry cofactor: Functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor
    • Feng Y., Broder C.C., Kennedy P.E., and Berger E.A. HIV-1 entry cofactor: Functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor. Science 272 (1996) 872-877
    • (1996) Science , vol.272 , pp. 872-877
    • Feng, Y.1    Broder, C.C.2    Kennedy, P.E.3    Berger, E.A.4
  • 24
    • 0031959601 scopus 로고    scopus 로고
    • Capture of an early fusion-active conformation of HIV-1 gp41
    • Furuta R.A., Wild C.T., Weng Y., and Weiss C.D. Capture of an early fusion-active conformation of HIV-1 gp41. Nat. Struct. Biol. 5 (1998) 276-279
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 276-279
    • Furuta, R.A.1    Wild, C.T.2    Weng, Y.3    Weiss, C.D.4
  • 25
    • 1842457801 scopus 로고    scopus 로고
    • Multistep regulation of membrane insertion of the fusion peptide of Semliki Forest virus
    • Gibbons D.L., Ahn A., Liao M., Hammar L., Cheng R.H., and Kielian M. Multistep regulation of membrane insertion of the fusion peptide of Semliki Forest virus. J. Virol. 78 (2004) 3312-3318
    • (2004) J. Virol. , vol.78 , pp. 3312-3318
    • Gibbons, D.L.1    Ahn, A.2    Liao, M.3    Hammar, L.4    Cheng, R.H.5    Kielian, M.6
  • 26
    • 0141429172 scopus 로고    scopus 로고
    • Visualization of the target-membrane-inserted fusion protein of Semliki Forest virus by combined electron microscopy and crystallography
    • Gibbons D.L., Erk I., Reilly B., Navaza J., Kielian M., Rey F.A., and Lepault J. Visualization of the target-membrane-inserted fusion protein of Semliki Forest virus by combined electron microscopy and crystallography. Cell 114 (2003) 573-583
    • (2003) Cell , vol.114 , pp. 573-583
    • Gibbons, D.L.1    Erk, I.2    Reilly, B.3    Navaza, J.4    Kielian, M.5    Rey, F.A.6    Lepault, J.7
  • 27
    • 1642540249 scopus 로고    scopus 로고
    • Conformational change and protein-protein interactions of the fusion protein of Semliki Forest virus
    • Gibbons D.L., Vaney M.C., Roussel A., Vigouroux A., Reilly B., Lepault J., Kielian M., and Rey F.A. Conformational change and protein-protein interactions of the fusion protein of Semliki Forest virus. Nature 427 (2004) 320-325
    • (2004) Nature , vol.427 , pp. 320-325
    • Gibbons, D.L.1    Vaney, M.C.2    Roussel, A.3    Vigouroux, A.4    Reilly, B.5    Lepault, J.6    Kielian, M.7    Rey, F.A.8
  • 28
    • 0034892952 scopus 로고    scopus 로고
    • Membrane structure and fusion-triggering conformational change of the fusion domain from influenza hemagglutinin
    • Han X., Bushweller J.H., Cafiso D.S., and Tamm L.K. Membrane structure and fusion-triggering conformational change of the fusion domain from influenza hemagglutinin. Nat. Struct. Biol. 8 (2001) 715-720
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 715-720
    • Han, X.1    Bushweller, J.H.2    Cafiso, D.S.3    Tamm, L.K.4
  • 29
    • 0026094713 scopus 로고
    • The flavivirus envelope protein E: Isolation of a soluble form from tick-borne encephalitis virus and its crystallization
    • Heinz F.X., Mandl C.W., Holzmann H., Kunz C., Harris B.A., Rey F., and Harrison S.C. The flavivirus envelope protein E: Isolation of a soluble form from tick-borne encephalitis virus and its crystallization. J. Virol. 65 (1991) 5579-5583
    • (1991) J. Virol. , vol.65 , pp. 5579-5583
    • Heinz, F.X.1    Mandl, C.W.2    Holzmann, H.3    Kunz, C.4    Harris, B.A.5    Rey, F.6    Harrison, S.C.7
  • 30
    • 0028278395 scopus 로고
    • Structural changes and functional control of the tick-borne encephalitis virus glycoprotein E by the heterodimeric association with protein prM
    • Heinz F.X., Stiasny K., Puschner-Auer G., Holzmann H., Allison S.L., Mandl C.W., and Kunz C. Structural changes and functional control of the tick-borne encephalitis virus glycoprotein E by the heterodimeric association with protein prM. Virology 198 (1994) 109-117
    • (1994) Virology , vol.198 , pp. 109-117
    • Heinz, F.X.1    Stiasny, K.2    Puschner-Auer, G.3    Holzmann, H.4    Allison, S.L.5    Mandl, C.W.6    Kunz, C.7
  • 31
    • 0037459076 scopus 로고    scopus 로고
    • Membrane fusion
    • Jahn R., Lang T., and Sudhof T.C. Membrane fusion. Cell 112 (2003) 519-533
    • (2003) Cell , vol.112 , pp. 519-533
    • Jahn, R.1    Lang, T.2    Sudhof, T.C.3
  • 33
    • 0031962175 scopus 로고    scopus 로고
    • Conformational changes in cell surface HIV-1 envelope glycoproteins are triggered by cooperation between cell surface CD4 and co-receptors
    • Jones P.L., Korte T., and Blumenthal R. Conformational changes in cell surface HIV-1 envelope glycoproteins are triggered by cooperation between cell surface CD4 and co-receptors. J. Biol. Chem. 273 (1998) 404-409
    • (1998) J. Biol. Chem. , vol.273 , pp. 404-409
    • Jones, P.L.1    Korte, T.2    Blumenthal, R.3
  • 34
    • 0028179011 scopus 로고
    • Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion
    • Kemble G.W., Danieli T., and White J.M. Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion. Cell 76 (1994) 383-391
    • (1994) Cell , vol.76 , pp. 383-391
    • Kemble, G.W.1    Danieli, T.2    White, J.M.3
  • 35
    • 0038187684 scopus 로고    scopus 로고
    • Novel therapies based on mechanisms of HIV-1 cell entry
    • Kilby J.M., and Eron J.J. Novel therapies based on mechanisms of HIV-1 cell entry. N. Engl. J. Med. 348 (2003) 2228-2238
    • (2003) N. Engl. J. Med. , vol.348 , pp. 2228-2238
    • Kilby, J.M.1    Eron, J.J.2
  • 37
    • 0028152964 scopus 로고
    • Membrane and protein interactions of a soluble form of the Semliki Forest virus fusion protein
    • Klimjack M.R., Jeffrey S., and Kielian M. Membrane and protein interactions of a soluble form of the Semliki Forest virus fusion protein. J. Virol. 68 (1994) 6940-6946
    • (1994) J. Virol. , vol.68 , pp. 6940-6946
    • Klimjack, M.R.1    Jeffrey, S.2    Kielian, M.3
  • 41
    • 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., Wyatt R., Robinson J., Sweet R.W., Sodroski J., and Hendrickson W.A. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 393 (1998) 648-659
    • (1998) Nature , vol.393 , pp. 648-659
    • Kwong, P.D.1    Wyatt, R.2    Robinson, J.3    Sweet, R.W.4    Sodroski, J.5    Hendrickson, W.A.6
  • 42
    • 0035815282 scopus 로고    scopus 로고
    • The fusion glycoprotein shell of Semliki Forest virus: An icosahedral assembly primed for fusogenic activation at endosomal pH
    • Lescar J., Roussel A., Wien M.W., Navaza J., Fuller S.D., Wengler G., and Rey F.A. The fusion glycoprotein shell of Semliki Forest virus: An icosahedral assembly primed for fusogenic activation at endosomal pH. Cell 105 (2001) 137-148
    • (2001) Cell , vol.105 , pp. 137-148
    • Lescar, J.1    Roussel, A.2    Wien, M.W.3    Navaza, J.4    Fuller, S.D.5    Wengler, G.6    Rey, F.A.7
  • 43
    • 0028834461 scopus 로고
    • A trimeric structural domain of the HIV-1 transmembrane glycoprotein
    • Lu M., Blacklow S.C., and Kim P.S. A trimeric structural domain of the HIV-1 transmembrane glycoprotein. Nat. Struct. Biol. 2 (1995) 1075-1082
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 1075-1082
    • Lu, M.1    Blacklow, S.C.2    Kim, P.S.3
  • 45
    • 0028865392 scopus 로고
    • GPI-anchored influenza hemagglutinin induces hemifusion to both red blood cell and planar bilayer membranes
    • Melikyan G.B., White J.M., and Cohen F.S. GPI-anchored influenza hemagglutinin induces hemifusion to both red blood cell and planar bilayer membranes. J. Cell Biol. 131 (1995) 679-691
    • (1995) J. Cell Biol. , vol.131 , pp. 679-691
    • Melikyan, G.B.1    White, J.M.2    Cohen, F.S.3
  • 46
  • 47
    • 1642499388 scopus 로고    scopus 로고
    • Structure of the dengue virus envelope protein after membrane fusion
    • Modis Y., Ogata S., Clements D., and Harrison S.C. Structure of the dengue virus envelope protein after membrane fusion. Nature 427 (2004) 313-319
    • (2004) Nature , vol.427 , pp. 313-319
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 48
    • 0025572710 scopus 로고
    • Dissociation of gp120 from HIV-1 virions induced by soluble CD4
    • Moore J.P., McKeating J.A., Weiss R.A., and Sattentau Q.J. Dissociation of gp120 from HIV-1 virions induced by soluble CD4. Science 250 (1990) 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
  • 49
    • 0343365487 scopus 로고    scopus 로고
    • Role of the membrane-proximal domain in the initial stages of human immunodeficiency virus type 1 envelope glycoprotein-mediated membrane fusion
    • Munoz-Barroso I., Salzwedel K., Hunter E., and Blumenthal R. Role of the membrane-proximal domain in the initial stages of human immunodeficiency virus type 1 envelope glycoprotein-mediated membrane fusion. J. Virol. 73 (1999) 6089-6092
    • (1999) J. Virol. , vol.73 , pp. 6089-6092
    • Munoz-Barroso, I.1    Salzwedel, K.2    Hunter, E.3    Blumenthal, R.4
  • 52
    • 0026567492 scopus 로고
    • Truncated variants of gp120 bind CD4 with high affinity and suggest a minimum CD4 binding region
    • Pollard S.R., Rosa M.D., Rosa J.J., and Wiley D.C. Truncated variants of gp120 bind CD4 with high affinity and suggest a minimum CD4 binding region. EMBO J. 11 (1992) 585-591
    • (1992) EMBO J. , vol.11 , pp. 585-591
    • Pollard, S.R.1    Rosa, M.D.2    Rosa, J.J.3    Wiley, D.C.4
  • 53
    • 0032812477 scopus 로고    scopus 로고
    • A specific point mutant at position 1 of the influenza hemagglutinin fusion peptide displays a hemifusion phenotype
    • Qiao H., Armstrong R.T., Melikyan G.B., Cohen F.S., and White J.M. A specific point mutant at position 1 of the influenza hemagglutinin fusion peptide displays a hemifusion phenotype. Mol. Biol. Cell 10 (1999) 2759-2769
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2759-2769
    • Qiao, H.1    Armstrong, R.T.2    Melikyan, G.B.3    Cohen, F.S.4    White, J.M.5
  • 54
    • 0029014434 scopus 로고
    • The envelope glycoprotein from tick-borne encephalitis virus at 2 Å resolution
    • Rey F.A., Heinz F.X., Mandl C., Kunz C., and Harrison S.C. The envelope glycoprotein from tick-borne encephalitis virus at 2 Å resolution. Nature 375 (1995) 291-298
    • (1995) Nature , vol.375 , pp. 291-298
    • Rey, F.A.1    Heinz, F.X.2    Mandl, C.3    Kunz, C.4    Harrison, S.C.5
  • 55
    • 0031883832 scopus 로고    scopus 로고
    • Determinants of human immunodeficiency virus type-I resistance to gp41-derived inhibitory peptides
    • Rimsky L.T., Shugars D.C., and Matthews T.J. Determinants of human immunodeficiency virus type-I resistance to gp41-derived inhibitory peptides. J. Virol. 72 (1998) 986-993
    • (1998) J. Virol. , vol.72 , pp. 986-993
    • Rimsky, L.T.1    Shugars, D.C.2    Matthews, T.J.3
  • 57
    • 0021833513 scopus 로고
    • Characterization of envelope and core structural gene products of HTLV-III with sera from AIDS patients
    • Robey W.G., Safai B., Oroszlan S., Arthur L.O., Gonda M.A., Gallo R.C., and Fischinger P.J. Characterization of envelope and core structural gene products of HTLV-III with sera from AIDS patients. Science 228 (1985) 593-595
    • (1985) Science , vol.228 , pp. 593-595
    • Robey, W.G.1    Safai, B.2    Oroszlan, S.3    Arthur, L.O.4    Gonda, M.A.5    Gallo, R.C.6    Fischinger, P.J.7
  • 58
    • 0035793406 scopus 로고    scopus 로고
    • Protein design of an HIV-1 entry inhibitor
    • Root M.J., Kay M.S., and Kim P.S. Protein design of an HIV-1 entry inhibitor. Science 291 (2001) 884-888
    • (2001) Science , vol.291 , pp. 884-888
    • Root, M.J.1    Kay, M.S.2    Kim, P.S.3
  • 60
    • 0036892508 scopus 로고    scopus 로고
    • Effects of membrane potential and sphingolipid structures on fusion of Semliki Forest virus
    • Samsonov A.V., Chatterjee P.K., Razinkob V.I., Eng C.H., Kielian M., and Cohen F.S. Effects of membrane potential and sphingolipid structures on fusion of Semliki Forest virus. J. Virol. 76 (2002) 12691-12702
    • (2002) J. Virol. , vol.76 , pp. 12691-12702
    • Samsonov, A.V.1    Chatterjee, P.K.2    Razinkob, V.I.3    Eng, C.H.4    Kielian, M.5    Cohen, F.S.6
  • 61
    • 0025866185 scopus 로고
    • Conformational changes induced in the human immunodeficiency virus envelope glycoprotein by soluble CD4 binding
    • Sattentau Q.J., and Moore J.P. Conformational changes induced in the human immunodeficiency virus envelope glycoprotein by soluble CD4 binding. J. Exp. Med. 174 (1991) 407-415
    • (1991) J. Exp. Med. , vol.174 , pp. 407-415
    • Sattentau, Q.J.1    Moore, J.P.2
  • 62
    • 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., and Poignard P. Conformational changes induced in the envelope glycoproteins of the human and simian immunodeficiency viruses by soluble receptor binding. J. Virol. 67 (1993) 7383-7393
    • (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
  • 63
    • 0027362739 scopus 로고
    • Energetics of intermediates in membrane fusion: Comparison of stalk and inverted micellar intermediate mechanisms
    • Siegel D.P. Energetics of intermediates in membrane fusion: Comparison of stalk and inverted micellar intermediate mechanisms. Biophys. J. 65 (1993) 2124-2140
    • (1993) Biophys. J. , vol.65 , pp. 2124-2140
    • Siegel, D.P.1
  • 64
    • 0032431055 scopus 로고    scopus 로고
    • Coiled coils in both intracellular vesicle and viral membrane fusion
    • Skehel J.J., and Wiley D.C. Coiled coils in both intracellular vesicle and viral membrane fusion. Cell 95 (1998) 871-874
    • (1998) Cell , vol.95 , pp. 871-874
    • Skehel, J.J.1    Wiley, D.C.2
  • 65
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • Skehel J.J., and Wiley D.C. Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin. Annu. Rev. Biochem. 69 (2000) 531-569
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 66
    • 0028824850 scopus 로고
    • Studies of the membrane fusion activities of fusion peptide mutants of influenza virus hemagglutinin
    • Steinhauer D.A., Wharton S.A., Skehel J.J., and Wiley D.C. Studies of the membrane fusion activities of fusion peptide mutants of influenza virus hemagglutinin. J. Virol. 69 (1995) 6643-6651
    • (1995) J. Virol. , vol.69 , pp. 6643-6651
    • Steinhauer, D.A.1    Wharton, S.A.2    Skehel, J.J.3    Wiley, D.C.4
  • 67
    • 0036198006 scopus 로고    scopus 로고
    • Membrane interactions of the tick-borne encephalitis virus fusion protein E at low pH
    • Stiasny K., Allison S.L., Schalich J., and Heinz F.X. Membrane interactions of the tick-borne encephalitis virus fusion protein E at low pH. J. Virol. 76 (2002) 3784-3790
    • (2002) J. Virol. , vol.76 , pp. 3784-3790
    • Stiasny, K.1    Allison, S.L.2    Schalich, J.3    Heinz, F.X.4
  • 68
    • 1542347705 scopus 로고    scopus 로고
    • Characterization of a membrane-associated trimeric low-pH induced form of the class II viral fusion protein E from tick-borne encephalitis virus and its crystallization
    • Stiasny K., Bressanelli S., Lepault J., Rey F.A., and Heinz F.X. Characterization of a membrane-associated trimeric low-pH induced form of the class II viral fusion protein E from tick-borne encephalitis virus and its crystallization. J. Virol. 78 (2004) 3178-3183
    • (2004) J. Virol. , vol.78 , pp. 3178-3183
    • Stiasny, K.1    Bressanelli, S.2    Lepault, J.3    Rey, F.A.4    Heinz, F.X.5
  • 69
    • 0030780614 scopus 로고    scopus 로고
    • Atomic structure of a thermostable subdomain of HIV-1 gp41
    • Tan K., Liu J., Wang J., Shen S., and Lu M. Atomic structure of a thermostable subdomain of HIV-1 gp41. Proc. Natl. Acad. Sci. USA 94 (1997) 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
  • 72
    • 0031919431 scopus 로고    scopus 로고
    • A single point mutation controls the cholesterol dependence of Semliki Forest virus entry and exit
    • Vashishtha M., Phalen T., Marquardt M.T., Ryu J.S., Ng A.C., and Kielian M. A single point mutation controls the cholesterol dependence of Semliki Forest virus entry and exit. J. Cell Biol. 140 (1998) 91-99
    • (1998) J. Cell Biol. , vol.140 , pp. 91-99
    • Vashishtha, M.1    Phalen, T.2    Marquardt, M.T.3    Ryu, J.S.4    Ng, A.C.5    Kielian, M.6
  • 73
    • 0022352075 scopus 로고
    • Characterization of gp41 as the transmembrane protein coded by the HTLV-III/LAV envelope gene
    • Veronese F.D., DeVico A.L., Copeland T.D., Oroszlan S., Gallo R.C., and Sarngadharan M.G. Characterization of gp41 as the transmembrane protein coded by the HTLV-III/LAV envelope gene. Science 229 (1985) 1402-1405
    • (1985) Science , vol.229 , pp. 1402-1405
    • Veronese, F.D.1    DeVico, A.L.2    Copeland, T.D.3    Oroszlan, S.4    Gallo, R.C.5    Sarngadharan, M.G.6
  • 74
    • 0024455501 scopus 로고
    • The heterodimeric association between the membrane proteins of Semliki Forest virus changes its sensitivity to low pH during virus maturation
    • Wahlberg J.M., Boere W.A., and Garoff H. The heterodimeric association between the membrane proteins of Semliki Forest virus changes its sensitivity to low pH during virus maturation. J. Virol. 63 (1989) 4991-4997
    • (1989) J. Virol. , vol.63 , pp. 4991-4997
    • Wahlberg, J.M.1    Boere, W.A.2    Garoff, H.3
  • 75
    • 0026495818 scopus 로고
    • Membrane fusion of Semliki Forest virus involves homotrimers of the fusion protein
    • Wahlberg J.M., Bron R., Wilschut J., and Garoff H. Membrane fusion of Semliki Forest virus involves homotrimers of the fusion protein. J. Virol. 66 (1992) 7309-7318
    • (1992) J. Virol. , vol.66 , pp. 7309-7318
    • Wahlberg, J.M.1    Bron, R.2    Wilschut, J.3    Garoff, H.4
  • 76
    • 0033771310 scopus 로고    scopus 로고
    • Functional importance of the coiled-coil of the Ebola virus glycoprotein
    • Watanabe S., Takada A., Watanabe T., Ito H., Kida H., and Kawaoka Y. Functional importance of the coiled-coil of the Ebola virus glycoprotein. J. Virol. 74 (2000) 10194-10201
    • (2000) J. Virol. , vol.74 , pp. 10194-10201
    • Watanabe, S.1    Takada, A.2    Watanabe, T.3    Ito, H.4    Kida, H.5    Kawaoka, Y.6
  • 77
    • 0032214714 scopus 로고    scopus 로고
    • Crystal structure of the Ebola virus membrane fusion subunit, GP2, from the envelope glycoprotein ectodomain
    • Weissenhorn W., Carfi A., Lee K.H., Skehel J.J., and Wiley D.C. Crystal structure of the Ebola virus membrane fusion subunit, GP2, from the envelope glycoprotein ectodomain. Mol. Cell 2 (1998) 605-616
    • (1998) Mol. Cell , vol.2 , pp. 605-616
    • Weissenhorn, W.1    Carfi, A.2    Lee, K.H.3    Skehel, J.J.4    Wiley, D.C.5
  • 79
    • 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., and Matthews T. A synthetic peptide inhibitor of human immunodeficiency virus replication: Correlation between solution structure and viral inhibition. Proc. Natl. Acad. Sci. USA 89 (1992) 10537-10541
    • (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
  • 80
    • 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., and 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 (1994) 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.