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Volumn 14, Issue 3, 1997, Pages 97-112

What studies of fusion peptides tell us about viral envelope glycoprotein-mediated membrane fusion

Author keywords

Fusion; Haemagglutinin; HIV; Membranes; Viruses

Indexed keywords

FLUORESCENT DYE; MEMBRANE LIPID; SYNTHETIC PEPTIDE; VIRUS ENVELOPE PROTEIN; VIRUS FUSION PROTEIN; VIRUS GLYCOPROTEIN; VIRUS HEMAGGLUTININ;

EID: 0030682144     PISSN: 09687688     EISSN: None     Source Type: Journal    
DOI: 10.3109/09687689709048170     Document Type: Review
Times cited : (192)

References (149)
  • 1
    • 0025284844 scopus 로고
    • Transmitter release from synapses: Does a preassembled fusion pore initiate exocytosis
    • Almers, W. and Tse, F. W. (1990) Transmitter release from synapses: Does a preassembled fusion pore initiate exocytosis. Neuron, 4, 813-818.
    • (1990) Neuron , vol.4 , pp. 813-818
    • Almers, W.1    Tse, F.W.2
  • 2
    • 0026562263 scopus 로고
    • The SWISS-PROT protein sequence data bank
    • Bairoch, A. and Boeckmann, B. (1992) The SWISS-PROT protein sequence data bank. Nucleic Acids Research, 20, 2019-2022.
    • (1992) Nucleic Acids Research , vol.20 , pp. 2019-2022
    • Bairoch, A.1    Boeckmann, B.2
  • 3
    • 0002282242 scopus 로고
    • Architecture of the influenza hemagglutinin membrane fusion site
    • J. Bentz, ed (CRC Press, Boca Raton, Ann Arbor, London & Tokyo)
    • Bentz, J., Ellens, H. and Alford, D. (1993) Architecture of the influenza hemagglutinin membrane fusion site. In Viral Fusion Mechanisms, J. Bentz, ed (CRC Press, Boca Raton, Ann Arbor, London & Tokyo), pp. 163-199.
    • (1993) Viral Fusion Mechanisms , pp. 163-199
    • Bentz, J.1    Ellens, H.2    Alford, D.3
  • 4
    • 0031583329 scopus 로고    scopus 로고
    • The viral mousetrap
    • Binley, J. and Moore, J. P. (1997) The viral mousetrap. Nature, 387, 346-348.
    • (1997) Nature , vol.387 , pp. 346-348
    • Binley, J.1    Moore, J.P.2
  • 5
    • 0003110115 scopus 로고    scopus 로고
    • Membrane fusion
    • J. F. Hoffman and J. C. Jamieson, eds (Oxford University Press, New York)
    • Blumenthal, R. and Dimitrov, D. S. (1997) Membrane fusion. In Handbook of Physiology, J. F. Hoffman and J. C. Jamieson, eds (Oxford University Press, New York), pp. 569-604.
    • (1997) Handbook of Physiology , pp. 569-604
    • Blumenthal, R.1    Dimitrov, D.S.2
  • 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., Sarkar, D. P., Durell, S., Howard, D. E. and Morris, S. J. (1996) Dilation of the influenza hemagglutinin fusion pore revealed by the kinetics of individual cell-cell fusion events. Journal of Cell Biology, 135, 63-71.
    • (1996) Journal of Cell Biology , vol.135 , pp. 63-71
    • Blumenthal, R.1    Sarkar, D.P.2    Durell, S.3    Howard, D.E.4    Morris, S.J.5
  • 7
    • 0002832464 scopus 로고
    • Cryoelectron microscopy
    • J. Bentz, ed (CRC Press, Boca Raton, Ann Arbor, London & Tokyo)
    • Booy, F. P. (1993) Cryoelectron microscopy. In Viral Fusion Mechanisms, J. Bentz, ed (CRC Press, Boca Raton, Ann Arbor, London & Tokyo), pp. 21-54.
    • (1993) Viral Fusion Mechanisms , pp. 21-54
    • Booy, F.P.1
  • 9
    • 0025054302 scopus 로고
    • Orientation into the lipid bilayer of an asymmetric amphipathic helical peptide located at the N-terminus of viral fusion proteins
    • Brasseur R., Vandenbranden, M., Cornet, B., Burny, A. and Ruysschaert, J.-M. (1990) Orientation into the lipid bilayer of an asymmetric amphipathic helical peptide located at the N-terminus of viral fusion proteins. Biochimica et Biophysica Acta, 1029, 267-273.
    • (1990) Biochimica et Biophysica Acta , vol.1029 , pp. 267-273
    • Brasseur, R.1    Vandenbranden, M.2    Cornet, B.3    Burny, A.4    Ruysschaert, J.-M.5
  • 10
    • 0030451267 scopus 로고    scopus 로고
    • HIV and the 7-transmembrane-domain receptors
    • Broder, C. C. and Dimitrov, D. S. (1996) HIV and the 7-transmembrane-domain receptors. Pathobiology, 64, 171-179.
    • (1996) Pathobiology , vol.64 , pp. 171-179
    • Broder, C.C.1    Dimitrov, D.S.2
  • 11
    • 0024836427 scopus 로고
    • Testing topological models for the membrane penetration of the fusion peptide of influenza virus hemagglutinin
    • Brunner, J. (1989) Testing topological models for the membrane penetration of the fusion peptide of influenza virus hemagglutinin. FEBS Letters, 257, 369-372.
    • (1989) FEBS Letters , vol.257 , pp. 369-372
    • Brunner, J.1
  • 12
    • 0027203297 scopus 로고
    • New photolabeling and crosslinking methods
    • Brunner, J. (1993) New photolabeling and crosslinking methods. Annual Review of Biochemistry, 62, 483-514.
    • (1993) Annual Review of Biochemistry , vol.62 , pp. 483-514
    • Brunner, J.1
  • 13
    • 0002345765 scopus 로고
    • Fusion-protein membrane interactions as studied by hydrophobic photolabeling
    • J. Bentz, ed (CRC Press, Boca Raton, Ann Arbor, London & Tokyo)
    • Brunner, J. and Tsurudome, M. (1993) Fusion-protein membrane interactions as studied by hydrophobic photolabeling. In Viral Fusion Mechanisms, J. Bentz, ed (CRC Press, Boca Raton, Ann Arbor, London & Tokyo), pp. 67-88.
    • (1993) Viral Fusion Mechanisms , pp. 67-88
    • Brunner, J.1    Tsurudome, M.2
  • 14
    • 0025793208 scopus 로고
    • Fusion activity of influenza virus PR8/34 correlates with a temperature-induced conformational change within the hemagglutinin ectodomain detected by photochemical labeling
    • Brunner, J., Zugliani C. and Mischler, R. (1991) Fusion activity of influenza virus PR8/34 correlates with a temperature-induced conformational change within the hemagglutinin ectodomain detected by photochemical labeling. Biochemistry, 30, 2432-2438.
    • (1991) Biochemistry , vol.30 , pp. 2432-2438
    • Brunner, J.1    Zugliani, C.2    Mischler, R.3
  • 15
    • 0026744238 scopus 로고
    • A leucine zipper structure present in the measles virus fusion protein is not required for its tetramerization but is essential for fusion
    • Buckland, R., Malvoisin, E., Beauverger, P. and Wild, F. (1992) A leucine zipper structure present in the measles virus fusion protein is not required for its tetramerization but is essential for fusion. Journal of General Virology, 73, 1703-1707.
    • (1992) Journal of General Virology , vol.73 , pp. 1703-1707
    • Buckland, R.1    Malvoisin, E.2    Beauverger, P.3    Wild, F.4
  • 16
    • 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. (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
  • 17
    • 0025853752 scopus 로고
    • The interaction of synthetic analogs of the N-terminal fusion sequence of influenza virus with a lipid monolayer. Comparison of fusion-active and fusion-defective analogs
    • Burger, K. N., Wharton, S. A., Demel, R. A. and Verkleij, A. J. (1991) The interaction of synthetic analogs of the N-terminal fusion sequence of influenza virus with a lipid monolayer. Comparison of fusion-active and fusion-defective analogs. Biochimica et Biophysica Acta, 1065, 121-129.
    • (1991) Biochimica et Biophysica Acta , vol.1065 , pp. 121-129
    • Burger, K.N.1    Wharton, S.A.2    Demel, R.A.3    Verkleij, A.J.4
  • 18
    • 0027253445 scopus 로고
    • A spring-loaded mechanism for the conformational change of influenza hemagglutinin
    • Carr, C. M. and Kim, P. S. (1993). A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell, 73, 823-832.
    • (1993) Cell , vol.73 , pp. 823-832
    • Carr, C.M.1    Kim, P.S.2
  • 19
    • 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. (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
  • 20
    • 0018644692 scopus 로고
    • Membrane fusion during secretion: Cortical granule exocytosis in sex urchin eggs as studied by quick-freezing and freeze-fracture
    • Chandler, D. E. and Heuser, J. (1979) Membrane fusion during secretion: cortical granule exocytosis in sex urchin eggs as studied by quick-freezing and freeze-fracture. Journal of Cell Biology, 83, 91-108.
    • (1979) Journal of Cell Biology , vol.83 , pp. 91-108
    • Chandler, D.E.1    Heuser, J.2
  • 23
    • 0025816519 scopus 로고
    • Delay time for influenza virus hemagglutinin-induced membrane fusion depends on hemagglutinin surface density
    • Clague, M. J., Schoch, C. and Blumenthal, R. (1991) Delay time for influenza virus hemagglutinin-induced membrane fusion depends on hemagglutinin surface density. Journal of Virology, 65, 2402-2407.
    • (1991) Journal of Virology , vol.65 , pp. 2402-2407
    • Clague, M.J.1    Schoch, C.2    Blumenthal, R.3
  • 24
    • 0006353327 scopus 로고
    • Toward a dissection of the influenza hemagglutinin-mediated membrane fusion pathway
    • J. Bentz, ed (CRC Press, Boca Raton, Ann Arbor, London & Tokyo)
    • Clague, M. J., Schoch, C. and Blumenthal, R. (1993) Toward a dissection of the influenza hemagglutinin-mediated membrane fusion pathway. In Viral Fusion Mechanisms, J. Bentz, ed (CRC Press, Boca Raton, Ann Arbor, London & Tokyo), pp. 113-132.
    • (1993) Viral Fusion Mechanisms , pp. 113-132
    • Clague, M.J.1    Schoch, C.2    Blumenthal, R.3
  • 25
    • 0030041468 scopus 로고    scopus 로고
    • Structural study of the interaction between the SIV fusion peptide and model membranes
    • Colotto, A., Martin, I., Ruysschaert, J.-M., Sen, A., Hui, S. W. and Epand, R. M. (1996) Structural study of the interaction between the SIV fusion peptide and model membranes. Biochemistry, 35, 980-989.
    • (1996) Biochemistry , vol.35 , pp. 980-989
    • Colotto, A.1    Martin, I.2    Ruysschaert, J.-M.3    Sen, A.4    Hui, S.W.5    Epand, R.M.6
  • 26
    • 0026485306 scopus 로고
    • Role of transmembrane domain interactions in the assembly of class II MHC molecules
    • Cosson, P. and Bonifacino, J. S. (1992) Role of transmembrane domain interactions in the assembly of class II MHC molecules. Science, 258, 659-662.
    • (1992) Science , vol.258 , pp. 659-662
    • Cosson, P.1    Bonifacino, J.S.2
  • 27
    • 0000920828 scopus 로고
    • The packing of α-helices: Simple coiled-coils
    • Crick, F. H. C. (1953) The packing of α-helices: simple coiled-coils. Acta Crystallography, 6, 689-697.
    • (1953) Acta Crystallography , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 28
    • 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. (1996) Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers. Journal of Cell Biology, 133, 559-569.
    • (1996) Journal of Cell Biology , vol.133 , pp. 559-569
    • Danieli, T.1    Pelletier, S.L.2    Henis, Y.I.3    White, J.M.4
  • 30
    • 0029968695 scopus 로고    scopus 로고
    • Mutational analysis of the fusion peptide of the human immunodeficiency virus type 1: Identification of critical glycine residues
    • Delahunty, M. D., Rhee, I., Freed, E. O. and Bonifacino, J. S. (1996). Mutational analysis of the fusion peptide of the human immunodeficiency virus type 1: identification of critical glycine residues. Virology, 218, 94-102.
    • (1996) Virology , vol.218 , pp. 94-102
    • Delahunty, M.D.1    Rhee, I.2    Freed, E.O.3    Bonifacino, J.S.4
  • 31
    • 0026779508 scopus 로고
    • Analysis of HIV-1 envelope mutants and pseudotyping of replication-defective HIV-1 vectors by genetic complementation
    • Delwart, E. L., Buchschacher, Jr., G. L., Freed, E. O. and Panganiban, A. T. (1992) Analysis of HIV-1 envelope mutants and pseudotyping of replication-defective HIV-1 vectors by genetic complementation. Aids Research and Human Retroviruses, 8, 1669-1677.
    • (1992) Aids Research and Human Retroviruses , vol.8 , pp. 1669-1677
    • Delwart, E.L.1    Buchschacher Jr., G.L.2    Freed, E.O.3    Panganiban, A.T.4
  • 32
  • 34
    • 0027157736 scopus 로고
    • Folding and assembly of viral membrane proteins
    • Doms, R. W., Lamb, R. A., Rose, J. K. and Helenius, A. (1993) Folding and assembly of viral membrane proteins. Virology, 193, 545-562.
    • (1993) Virology , vol.193 , pp. 545-562
    • Doms, R.W.1    Lamb, R.A.2    Rose, J.K.3    Helenius, A.4
  • 35
    • 0026652457 scopus 로고
    • Mutations in the leucine zipper of the human immunodeficiency virus type 1 transmembrane glycoprotein affect fusion and infectivity
    • Dubay, J. W., Roberts, S. J., Brody, B. and Hunter, E. (1992) Mutations in the leucine zipper of the human immunodeficiency virus type 1 transmembrane glycoprotein affect fusion and infectivity. Journal of Virology, 66, 4748-4756.
    • (1992) Journal of Virology , vol.66 , pp. 4748-4756
    • Dubay, J.W.1    Roberts, S.J.2    Brody, B.3    Hunter, E.4
  • 36
    • 0030010945 scopus 로고    scopus 로고
    • H+-induced membrane insertion of influenza virus hemagglutinin involves the HA2 amino-terminal fusion peptide but not the coiled coil region
    • Durrer, P., Galli, C., Hoenke, S., Corti, C., Gluck, R., Vorherr, T. and Brunner, J. (1996) H+-induced membrane insertion of influenza virus hemagglutinin involves the HA2 amino-terminal fusion peptide but not the coiled coil region. Journal of Biological Chemistry, 271, 13417-13421.
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 13417-13421
    • Durrer, P.1    Galli, C.2    Hoenke, S.3    Corti, C.4    Gluck, R.5    Vorherr, T.6    Brunner, J.7
  • 37
    • 0029143629 scopus 로고
    • Photolabeling identifies a putative fusion domain in the envelope glycoprotein of rabies and vesicular stomatitis viruses
    • Durrer, P., Gaudin, Y., Ruigrok, R. W., Graf, R. and Brunner, J. (1995) Photolabeling identifies a putative fusion domain in the envelope glycoprotein of rabies and vesicular stomatitis viruses. Journal of Biological Chemistry, 270, 17575-17581.
    • (1995) Journal of Biological Chemistry , vol.270 , pp. 17575-17581
    • Durrer, P.1    Gaudin, Y.2    Ruigrok, R.W.3    Graf, R.4    Brunner, J.5
  • 38
    • 0023838935 scopus 로고
    • Membrane action of synthetic Nterminal peptides of influenza virus hemagglutinin and its mutants
    • Duzgunes, N. and Gambale, F. (1988) Membrane action of synthetic Nterminal peptides of influenza virus hemagglutinin and its mutants. FEBS Letters, 227, 110-114.
    • (1988) FEBS Letters , vol.227 , pp. 110-114
    • Duzgunes, N.1    Gambale, F.2
  • 39
    • 0025109728 scopus 로고
    • Fusion of influenza hemagglutinin-expressing fibroblasts with glycophorin-bearing liposomes: Role of hemagglutinin surface density
    • Ellens, H., Bentz, J., Mason, D., Zhang, F. and White, J. M. (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
  • 40
    • 0028477923 scopus 로고
    • A trans-dominant mutation in human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein gp41 inhibits membrane fusion when expressed in target cells
    • Elson, H. F., Dimitrov, D. S. and Blumenthal, R. (1994) A trans-dominant mutation in human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein gp41 inhibits membrane fusion when expressed in target cells. Molecular Membrane Biology, 11, 165-169.
    • (1994) Molecular Membrane Biology , vol.11 , pp. 165-169
    • Elson, H.F.1    Dimitrov, D.S.2    Blumenthal, R.3
  • 41
    • 0022418382 scopus 로고
    • Diacylglycerols, lysolecithin, or hydrocarbons markedly alter the bilayer to hexagonal phase transition temperature of phosphatidylethanolamines
    • Epand, R. M. (1985) Diacylglycerols, lysolecithin, or hydrocarbons markedly alter the bilayer to hexagonal phase transition temperature of phosphatidylethanolamines. Biochemistry, 24, 7092-7095.
    • (1985) Biochemistry , vol.24 , pp. 7092-7095
    • Epand, R.M.1
  • 42
    • 0028023386 scopus 로고
    • Relationship between the infectivity of influenza virus and the ability of its fusion peptide to perturb bilayers
    • Epand, R. M. and Epand, R. F. (1994) Relationship between the infectivity of influenza virus and the ability of its fusion peptide to perturb bilayers. Biochemical and Biophysical Research Communications, 202, 1420-1425.
    • (1994) Biochemical and Biophysical Research Communications , vol.202 , pp. 1420-1425
    • Epand, R.M.1    Epand, R.F.2
  • 43
    • 0026061765 scopus 로고
    • Promotion of hexagonal phase formation and lipid mixing by fatty acids with varying degrees of unsaturation
    • Epand, R. M., Epand, R. F., Ahmed, N. and Chen, R. (1991) Promotion of hexagonal phase formation and lipid mixing by fatty acids with varying degrees of unsaturation. Chemistry and Physics of Lipids, 57, 75-80.
    • (1991) Chemistry and Physics of Lipids , vol.57 , pp. 75-80
    • Epand, R.M.1    Epand, R.F.2    Ahmed, N.3    Chen, R.4
  • 44
    • 0028576923 scopus 로고
    • Membrane orientation of the SIV fusion peptide determines its effect on bilayer stability and ability to promote membrane fusion
    • Epand, R. F., Martin, I., Ruysschaert, J.-M. and Epand, R. M. (1994) Membrane orientation of the SIV fusion peptide determines its effect on bilayer stability and ability to promote membrane fusion. Biochemical and Biophysical Research Communications, 205, 1938-1943.
    • (1994) Biochemical and Biophysical Research Communications , vol.205 , pp. 1938-1943
    • Epand, R.F.1    Martin, I.2    Ruysschaert, J.-M.3    Epand, R.M.4
  • 45
  • 47
    • 0028796347 scopus 로고
    • Vesicular stomatitis virus glycoprotein mutations that affect membrane fusion activity and abolish virus infectivity
    • Fredericksen, B. L. and Whitt, M. A. (1995) Vesicular stomatitis virus glycoprotein mutations that affect membrane fusion activity and abolish virus infectivity. Journal of Virology, 69, 1435-1443.
    • (1995) Journal of Virology , vol.69 , pp. 1435-1443
    • Fredericksen, B.L.1    Whitt, M.A.2
  • 48
    • 0026544416 scopus 로고
    • A mutation in the human immunodeficiency virus type 1 transmembrane glycoprotein gp41 dominantly interferes with fusion and infectivity
    • Freed, E. O., Delwart, E. L., Buchschacher, Jr., G. L. and Panganiban, A. T. (1992) A mutation in the human immunodeficiency virus type 1 transmembrane glycoprotein gp41 dominantly interferes with fusion and infectivity. Proceedings of the National Academy of Sciences, USA, 89, 70-74.
    • (1992) Proceedings of the National Academy of Sciences, USA , vol.89 , pp. 70-74
    • Freed, E.O.1    Delwart, E.L.2    Buchschacher Jr., G.L.3    Panganiban, A.T.4
  • 49
    • 0025297179 scopus 로고
    • Characterization of the fusion domain of the human immunodeficiency virus type 1 envelope glycoprotein gp41
    • Freed, E. O., Myers, D. J. and Risser, R. (1990) Characterization of the fusion domain of the human immunodeficiency virus type 1 envelope glycoprotein gp41. Proceedings of the National Academy of Sciences, USA, 87, 4650-4654.
    • (1990) Proceedings of the National Academy of Sciences, USA , vol.87 , pp. 4650-4654
    • Freed, E.O.1    Myers, D.J.2    Risser, R.3
  • 50
    • 0019479713 scopus 로고
    • Infrared membrane spectroscopy
    • E. Grell, ed. (Springer-Verlag, Berlin, New York)
    • Fringeli, U. R. and Günthard, M. H. (1981) Infrared membrane spectroscopy. In Membrane Spectroscopy, E. Grell, ed. (Springer-Verlag, Berlin, New York), pp. 270-332.
    • (1981) Membrane Spectroscopy , pp. 270-332
    • Fringeli, U.R.1    Günthard, M.H.2
  • 51
    • 0023669119 scopus 로고
    • Detection of a fusion peptide sequence in the transmembrane protein of human immunodeficiency virus
    • Gallaher W. R. (1987) Detection of a fusion peptide sequence in the transmembrane protein of human immunodeficiency virus. Cell, 50, 327-328.
    • (1987) Cell , vol.50 , pp. 327-328
    • Gallaher, W.R.1
  • 53
    • 0026758352 scopus 로고
    • Are fusion peptides really 'sided' insertional helices?
    • Gallaher, W. R., Segrest, J. P. and Hunter, E. (1992) Are fusion peptides really 'sided' insertional helices? Cell, 70, 531-532.
    • (1992) Cell , vol.70 , pp. 531-532
    • Gallaher, W.R.1    Segrest, J.P.2    Hunter, E.3
  • 54
    • 0029022681 scopus 로고
    • Low-pH induced conformational changes in viral fusion proteins: Implications for the fusion mechanism
    • Gaudin, Y., Ruigrok, R. W. H. and Brunner, J. (1995) Low-pH induced conformational changes in viral fusion proteins: implications for the fusion mechanism. Journal of General Virology, 76, 1541-1556.
    • (1995) Journal of General Virology , vol.76 , pp. 1541-1556
    • Gaudin, Y.1    Ruigrok, R.W.H.2    Brunner, J.3
  • 55
    • 0027378261 scopus 로고
    • Structural characterization, membrane interaction, and specific assembly within phospholipid membranes of hydrophobic segments from Bacillus thuringiensis var. israelensis cytolytic toxin
    • Gazit, E. and Shai, Y. (1993) Structural characterization, membrane interaction, and specific assembly within phospholipid membranes of hydrophobic segments from Bacillus thuringiensis var. israelensis cytolytic toxin. Biochemistry, 32, 12363-12371.
    • (1993) Biochemistry , vol.32 , pp. 12363-12371
    • Gazit, E.1    Shai, Y.2
  • 56
    • 0022619527 scopus 로고
    • Studies on the mechanism of membrane fusion: Site-specific mutagenesis of hemagglutinin of influenza virus
    • Gething, M. J., Doms, R. W., York, D. and White, J. (1986) Studies on the mechanism of membrane fusion: site-specific mutagenesis of hemagglutinin of influenza virus. Journal of Cell Biology, 102, 11-23.
    • (1986) Journal of Cell Biology , vol.102 , pp. 11-23
    • Gething, M.J.1    Doms, R.W.2    York, D.3    White, J.4
  • 57
    • 0023603605 scopus 로고
    • Sequence similarities between human immunodeficiency virus gp41 and paramyxovirus fusion proteins
    • Gonzalez-Scarano, F., Waxham, M. N., Ross, A. M. and Hoxie, J. A. (1987) Sequence similarities between human immunodeficiency virus gp41 and paramyxovirus fusion proteins. AIDS Research and Human Retroviruses, 3, 245-252.
    • (1987) AIDS Research and Human Retroviruses , vol.3 , pp. 245-252
    • Gonzalez-Scarano, F.1    Waxham, M.N.2    Ross, A.M.3    Hoxie, J.A.4
  • 58
    • 0025005940 scopus 로고
    • Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier-transform infrared spectroscopy on hydrated film
    • Goormaghtigh, E., Cabiaux, V. and Ruysschaert, J.-M. (1990) Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier-transform infrared spectroscopy on hydrated film. European Journal of Biochemistry, 193, 409-420.
    • (1990) European Journal of Biochemistry , vol.193 , pp. 409-420
    • Goormaghtigh, E.1    Cabiaux, V.2    Ruysschaert, J.-M.3
  • 59
    • 0028709475 scopus 로고
    • Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy
    • Goormaghtigh, E., Cabiaux, V. and Ruysschaert, J.-M. (1995). Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. Subcellular Biochemistry, 23, 405-450.
    • (1995) Subcellular Biochemistry , vol.23 , pp. 405-450
    • Goormaghtigh, E.1    Cabiaux, V.2    Ruysschaert, J.-M.3
  • 62
    • 0026743982 scopus 로고
    • The amino-terminal peptide of HIV-1 glycoprotein 41 interacts with human erythrocyte membranes: Peptide conformation, orientation and aggregation
    • Gordon, L. M., Curtain, C. C., Zhong, Y. C., Kirkpatrick, A., Mobley, P. W. and Waring, A. J. (1992) The amino-terminal peptide of HIV-1 glycoprotein 41 interacts with human erythrocyte membranes: peptide conformation, orientation and aggregation. Biochimica et Biophysica Acta, 1139, 257-274.
    • (1992) Biochimica et Biophysica Acta , vol.1139 , pp. 257-274
    • Gordon, L.M.1    Curtain, C.C.2    Zhong, Y.C.3    Kirkpatrick, A.4    Mobley, P.W.5    Waring, A.J.6
  • 63
    • 0030012221 scopus 로고    scopus 로고
    • Effect of the N-terminal glycine on the secondary structure, orientation, and interaction of the influenza hemagglutinin fusion peptide with lipid bilayers
    • Gray, C., Tatulian, S. A., Wharton, S. A. and Tamm, L. K. (1996) Effect of the N-terminal glycine on the secondary structure, orientation, and interaction of the influenza hemagglutinin fusion peptide with lipid bilayers. Biophysical Journal, 70, 2275-2286.
    • (1996) Biophysical Journal , vol.70 , pp. 2275-2286
    • Gray, C.1    Tatulian, S.A.2    Wharton, S.A.3    Tamm, L.K.4
  • 64
    • 0028249545 scopus 로고
    • Using sequence homology to analyze the structure and function of voltage-gated ion channel proteins
    • Society of General Physiologists, 47th Annual Symposium, D. M. Fambrough, ed (Rockefeller Univ. Press, New York)
    • Guy, H. R. and Durell, S. R. (1994) Using sequence homology to analyze the structure and function of voltage-gated ion channel proteins. In Molecular Evolution of Physiological Processes, Society of General Physiologists, 47th Annual Symposium, D. M. Fambrough, ed (Rockefeller Univ. Press, New York), pp. 197-212.
    • (1994) Molecular Evolution of Physiological Processes , pp. 197-212
    • Guy, H.R.1    Durell, S.R.2
  • 65
    • 0029690882 scopus 로고    scopus 로고
    • Developing three-dimensional models of ion channel proteins
    • T. Narahashi, ed (Plenum Press, New York)
    • Guy, H. R. and Durell, S. R. (1996) Developing three-dimensional models of ion channel proteins. In Ion Channels, Vol. 4, T. Narahashi, ed (Plenum Press, New York), pp. 1-40.
    • (1996) Ion Channels , vol.4 , pp. 1-40
    • Guy, H.R.1    Durell, S.R.2
  • 66
    • 0023899125 scopus 로고
    • Hydrophobic photolabeling identifies BHA2 as the subunit mediating the interaction of bromelain-solubilized influenza virus hemagglutinin with liposomes at low pH
    • Harter, C., Bachi, T., Semenza, G. and Brunner, J. (1988) Hydrophobic photolabeling identifies BHA2 as the subunit mediating the interaction of bromelain-solubilized influenza virus hemagglutinin with liposomes at low pH. Biochemistry, 27, 1856-1864.
    • (1988) Biochemistry , vol.27 , pp. 1856-1864
    • Harter, C.1    Bachi, T.2    Semenza, G.3    Brunner, J.4
  • 67
    • 0024564217 scopus 로고
    • Hydrophobic binding of the ectodomain of influenza hemagglutinin to membranes occurs through the 'fusion peptide'
    • Harter, C., James, P., Bachi, T., Semenza, G. and Brunner, J. (1989) Hydrophobic binding of the ectodomain of influenza hemagglutinin to membranes occurs through the 'fusion peptide'. Journal of Biological Chemistry, 264, 6459-6464.
    • (1989) Journal of Biological Chemistry , vol.264 , pp. 6459-6464
    • Harter, C.1    James, P.2    Bachi, T.3    Semenza, G.4    Brunner, J.5
  • 68
    • 0019874170 scopus 로고
    • Initiation of fusion and disassembly of Sendai virus membrane into liposomes
    • Haywood A. M. and Boyer, B. P. (1981) Initiation of fusion and disassembly of Sendai virus membrane into liposomes. Biochimica et Biophysica Acta, 646, 31-35.
    • (1981) Biochimica et Biophysica Acta , vol.646 , pp. 31-35
    • Haywood, A.M.1    Boyer, B.P.2
  • 70
    • 0026558240 scopus 로고
    • Studies on the fusion peptide of a paramyxovirus fusion glycoprotein: Roles of conserved residues in cell fusion
    • Horvath, C. M. and Lamb, R. A. (1992) Studies on the fusion peptide of a paramyxovirus fusion glycoprotein: roles of conserved residues in cell fusion. Journal of Virology, 66, 2443-2455.
    • (1992) Journal of Virology , vol.66 , pp. 2443-2455
    • Horvath, C.M.1    Lamb, R.A.2
  • 71
    • 0029257245 scopus 로고
    • Structural characterization of viral fusion proteins
    • Hughson, F. M. (1995) Structural characterization of viral fusion proteins. Current Biology, 5, 265-274.
    • (1995) Current Biology , vol.5 , pp. 265-274
    • Hughson, F.M.1
  • 72
    • 0027484593 scopus 로고
    • Orientation of fusionactive synthetic peptides in phospholipid bilayers: Determination by Fourier transform infrared spectroscopy
    • Ishiguro, R., Kimura, N. and Takahashi, S. (1993) Orientation of fusionactive synthetic peptides in phospholipid bilayers: determination by Fourier transform infrared spectroscopy. Biochemistry, 32, 9792-9797.
    • (1993) Biochemistry , vol.32 , pp. 9792-9797
    • Ishiguro, R.1    Kimura, N.2    Takahashi, S.3
  • 73
    • 0029915994 scopus 로고    scopus 로고
    • Interaction of fusogenic synthetic peptide with phospholipid bilayers: Orientation of the peptide alpha-helix and binding isotherm
    • Ishiguro, R., Matsumoto, M. and Takahashi, S. (1996) Interaction of fusogenic synthetic peptide with phospholipid bilayers: orientation of the peptide alpha-helix and binding isotherm. Biochemistry, 35, 4976-4983.
    • (1996) Biochemistry , vol.35 , pp. 4976-4983
    • Ishiguro, R.1    Matsumoto, M.2    Takahashi, S.3
  • 74
    • 0028179011 scopus 로고
    • Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion
    • Kemble, G. W., Danieli, T. and White, J. M. (1994) Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion. Cell, 76, 383-391.
    • (1994) Cell , vol.76 , pp. 383-391
    • Kemble, G.W.1    Danieli, T.2    White, J.M.3
  • 75
    • 0031010455 scopus 로고    scopus 로고
    • Fusion peptides derived from the HIV type I glycoprotein 41 associate within phospholipid membranes and inhibit cell-cell fusion: Structure-function study
    • Kliger, Y., Aharoni, A., Rapaport, D., Jones, P., Blumenthal, R. and Shai, Y. (1997) Fusion peptides derived from the HIV type I glycoprotein 41 associate within phospholipid membranes and inhibit cell-cell fusion: structure-function study. Journal of Biological Chemistry, 272, 13496-13505.
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 13496-13505
    • Kliger, Y.1    Aharoni, A.2    Rapaport, D.3    Jones, P.4    Blumenthal, R.5    Shai, Y.6
  • 76
    • 0023654706 scopus 로고
    • Membrane binding and conformational properties of peptides representing the NH2 terminus of influenza HA-2
    • Lear, J. D. and DeGrado, W. F. (1987) Membrane binding and conformational properties of peptides representing the NH2 terminus of influenza HA-2. Journal of Biological Chemistry, 262, 6500-6505.
    • (1987) Journal of Biological Chemistry , vol.262 , pp. 6500-6505
    • Lear, J.D.1    DeGrado, W.F.2
  • 77
    • 0027050182 scopus 로고
    • Sequence specificity in the dimerization of transmembrane α-helices
    • Lemmon, M. A., Flanagan, J. M., Treutlein, H. R., Zhang, J. and Engelman, D. M. (1992) Sequence specificity in the dimerization of transmembrane α-helices. Biochemistry, 31, 12719-12725.
    • (1992) Biochemistry , vol.31 , pp. 12719-12725
    • Lemmon, M.A.1    Flanagan, J.M.2    Treutlein, H.R.3    Zhang, J.4    Engelman, D.M.5
  • 78
    • 0029156059 scopus 로고
    • Structure and function of fusion pores in exocytosis and ectoplasmic membrane fusion
    • Lindau, M. and Almers, W. (1995) Structure and function of fusion pores in exocytosis and ectoplasmic membrane fusion. Current Opinion in Cell Biology, 7, 509-517.
    • (1995) Current Opinion in Cell Biology , vol.7 , pp. 509-517
    • Lindau, M.1    Almers, W.2
  • 84
    • 0027955142 scopus 로고
    • Correlation between fusogenicity of synthetic modified peptides corresponding to the NH2-terminal extremity of simian immunodeficiency virus gp32 and their mode of insertion into the lipid bilayer: An infrared spectroscopy study
    • Martin, I., Dubois, M. C., Defrise-Quertain, F., Saermark, T., Burny, A., Brasseur, R. and Ruysschaert, J.-M. (1994) Correlation between fusogenicity of synthetic modified peptides corresponding to the NH2-terminal extremity of simian immunodeficiency virus gp32 and their mode of insertion into the lipid bilayer: an infrared spectroscopy study. Journal of Virology, 68, 1139-1148.
    • (1994) Journal of Virology , vol.68 , pp. 1139-1148
    • Martin, I.1    Dubois, M.C.2    Defrise-Quertain, F.3    Saermark, T.4    Burny, A.5    Brasseur, R.6    Ruysschaert, J.-M.7
  • 85
    • 0029655419 scopus 로고    scopus 로고
    • Lipid membrane fusion induced by the human immunodeficiency virus type 1 gp41 N-terminal extremity is determined by its orientation in the lipid bilayer
    • Martin, I., Schaal, H., Scheid, A. and Ruysschaert, J.-M. (1996) Lipid membrane fusion induced by the human immunodeficiency virus type 1 gp41 N-terminal extremity is determined by its orientation in the lipid bilayer. Journal of Virology, 70, 298-304.
    • (1996) Journal of Virology , vol.70 , pp. 298-304
    • Martin, I.1    Schaal, H.2    Scheid, A.3    Ruysschaert, J.-M.4
  • 86
    • 0027740001 scopus 로고
    • Influenza virus hemagglutinin-induced cell-planar bilayer fusion: Quantitative dissection of fusion pore kinetics into stages
    • Melikyan, G. B., Niles, W. D. and Cohen, F. S. (1993a) Influenza virus hemagglutinin-induced cell-planar bilayer fusion: quantitative dissection of fusion pore kinetics into stages. Journal of General Physiology, 102, 1151-1170.
    • (1993) Journal of General Physiology , vol.102 , pp. 1151-1170
    • Melikyan, G.B.1    Niles, W.D.2    Cohen, F.S.3
  • 87
    • 0027715108 scopus 로고
    • Influenza hemagglutinin-mediated fusion pores connecting cells to planar membranes: Flickering to final expansion
    • Melikyan, G. B., Niles, W. D., Peeples, M. E. and Cohen, F. S. (1993b) Influenza hemagglutinin-mediated fusion pores connecting cells to planar membranes: flickering to final expansion. Journal of General Physiology, 102, 1131-1149.
    • (1993) Journal of General Physiology , vol.102 , pp. 1131-1149
    • Melikyan, G.B.1    Niles, W.D.2    Peeples, M.E.3    Cohen, F.S.4
  • 88
    • 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. (1995) GPI-anchored influenza hemagglutinin induces hemifusion to both red blood cell and planar bilayer membranes. Journal of Cell Biology, 131, 679-691.
    • (1995) Journal of Cell Biology , vol.131 , pp. 679-691
    • Melikyan, G.B.1    White, J.M.2    Cohen, F.S.3
  • 90
    • 0030222281 scopus 로고    scopus 로고
    • The fusion pore and mechanisms of biological membrane fusion
    • Monck, J. R. and Fernandez, J. M. (1996) The fusion pore and mechanisms of biological membrane fusion. Current Opinion in Cell Biology, 8, 524-533.
    • (1996) Current Opinion in Cell Biology , vol.8 , pp. 524-533
    • Monck, J.R.1    Fernandez, J.M.2
  • 91
    • 0000476294 scopus 로고
    • The HIV-cell fusion reaction
    • J. Bentz, ed (CRC Press, Boca Raton, Ann Arbor, London & Tokyo)
    • Moore, J. P., Jameson, B. A., Weiss, R. A. and Sattentau, Q. (1993). The HIV-cell fusion reaction. In Viral Fusion Mechanisms, J. Bentz, ed (CRC Press, Boca Raton, Ann Arbor, London & Tokyo), pp. 21-54.
    • (1993) Viral Fusion Mechanisms , pp. 21-54
    • Moore, J.P.1    Jameson, B.A.2    Weiss, R.A.3    Sattentau, Q.4
  • 92
    • 0009601848 scopus 로고
    • Hemagglutinin-catalyzed cell-cell fusion: Kinetics of initial pore formation from video rate, multi-wavelength fluorescence microscopy
    • Morris., S. J., Howard, D. E., Chang, T. H., Sarkar, D. P. and Blumenthal, R. (1995) Hemagglutinin-catalyzed cell-cell fusion: kinetics of initial pore formation from video rate, multi-wavelength fluorescence microscopy. Journal of the Microscopy Society of America, 1, 47-54.
    • (1995) Journal of the Microscopy Society of America , vol.1 , pp. 47-54
    • Morris, S.J.1    Howard, D.E.2    Chang, T.H.3    Sarkar, D.P.4    Blumenthal, R.5
  • 93
    • 0023423183 scopus 로고
    • pH-Dependent membrane fusion activity of a synthetic twenty amino acid peptide with the same sequence as that of the hydrophobic segment of influenza virus hemagglutinin
    • Murata, M., Sugahara, Y., Takahashi, S. and Ohnishi, S.-I. (1987) pH-Dependent membrane fusion activity of a synthetic twenty amino acid peptide with the same sequence as that of the hydrophobic segment of influenza virus hemagglutinin. Journal of Biochemistry, 102, 957-962.
    • (1987) Journal of Biochemistry , vol.102 , pp. 957-962
    • Murata, M.1    Sugahara, Y.2    Takahashi, S.3    Ohnishi, S.-I.4
  • 94
    • 0026766291 scopus 로고
    • pH-Dependent membrane fusion and vesiculation of phospholipid large unilamellar vesicles induced by amphiphilic anionic and cationic peptides
    • Murata, M., Takahashi, S., Kagiwada, S., Suzuki, A. and Ohnishi, S.-I. (1992) pH-Dependent membrane fusion and vesiculation of phospholipid large unilamellar vesicles induced by amphiphilic anionic and cationic peptides. Biochemistry, 31, 1986-1992.
    • (1992) Biochemistry , vol.31 , pp. 1986-1992
    • Murata, M.1    Takahashi, S.2    Kagiwada, S.3    Suzuki, A.4    Ohnishi, S.-I.5
  • 95
    • 0013657423 scopus 로고
    • Discrete changes of cell membrane capacitance observed under conditions of enhanced secretion in bovine adrenal chromaffin cells
    • Neher, E. and Marty, A. (1982) Discrete changes of cell membrane capacitance observed under conditions of enhanced secretion in bovine adrenal chromaffin cells. Proceedings of the National Academy of Sciences, USA, 79, 6712-6716.
    • (1982) Proceedings of the National Academy of Sciences, USA , vol.79 , pp. 6712-6716
    • Neher, E.1    Marty, A.2
  • 96
    • 0028218423 scopus 로고
    • Interaction of the HIV-1 fusion peptide with phospholipid vesicles: Different structural requirements for fusion and leakage
    • Nieva, J. L., Nir, S., Muga, A., Goni, F. M. and Wilschut, J. (1994) Interaction of the HIV-1 fusion peptide with phospholipid vesicles: different structural requirements for fusion and leakage. Biochemistry, 33, 3201-3209.
    • (1994) Biochemistry , vol.33 , pp. 3201-3209
    • Nieva, J.L.1    Nir, S.2    Muga, A.3    Goni, F.M.4    Wilschut, J.5
  • 97
  • 98
    • 0028110074 scopus 로고
    • Thermolysin activation mutants with changes in the fusogenic region of an influenza virus hemagglutinin
    • Orlich, M. and Rott, R. (1994) Thermolysin activation mutants with changes in the fusogenic region of an influenza virus hemagglutinin. Journal of Virology, 68, 7537-7539.
    • (1994) Journal of Virology , vol.68 , pp. 7537-7539
    • Orlich, M.1    Rott, R.2
  • 100
    • 0028934164 scopus 로고
    • Liposome destabilization induced by the HIV-1 fusion peptide effect of a single amino acid substitution
    • Pereira, F. B., Goni, F. M. and Nieva, J. L. (1995) Liposome destabilization induced by the HIV-1 fusion peptide effect of a single amino acid substitution. FEBS Letters, 362, 243-246.
    • (1995) FEBS Letters , vol.362 , pp. 243-246
    • Pereira, F.B.1    Goni, F.M.2    Nieva, J.L.3
  • 101
    • 0025279843 scopus 로고
    • Conformational changes and fusion activity of influenza virus hemagglutinin of the H2 and H3 subtypes: Effects of acid pretreatment
    • Puri, A., Booy, F. P., Doms, R. W., White, J. M. and Blumenthal, R. (1990) Conformational changes and fusion activity of influenza virus hemagglutinin of the H2 and H3 subtypes: effects of acid pretreatment. Journal of Virology, 64, 3824-3832.
    • (1990) Journal of Virology , vol.64 , pp. 3824-3832
    • Puri, A.1    Booy, F.P.2    Doms, R.W.3    White, J.M.4    Blumenthal, R.5
  • 102
    • 0025050505 scopus 로고
    • Phospholipid interactions of synthetic peptides representing the N-terminus of HIV gp41
    • Rafalski, M., Lear, J. D. and DeGrado, W. F. (1990) Phospholipid interactions of synthetic peptides representing the N-terminus of HIV gp41. Biochemistry, 29, 7917-7922.
    • (1990) Biochemistry , vol.29 , pp. 7917-7922
    • Rafalski, M.1    Lear, J.D.2    DeGrado, W.F.3
  • 103
    • 0025719093 scopus 로고
    • Membrane fusion activity of the influenza virus hemagglutinin: Interaction of HA2 N-terminal peptides with phospholipid vesicles
    • Rafalski, M., Ortiz, A., Rockwell, A., van Ginkel, L. C., Lear, J. D., DeGrado, W. F. and Wilschult, J. (1991) Membrane fusion activity of the influenza virus hemagglutinin: interaction of HA2 N-terminal peptides with phospholipid vesicles. Biochemistry, 30, 10211-10220.
    • (1991) Biochemistry , vol.30 , pp. 10211-10220
    • Rafalski, M.1    Ortiz, A.2    Rockwell, A.3    Van Ginkel, L.C.4    Lear, J.D.5    DeGrado, W.F.6    Wilschult, J.7
  • 104
    • 0028306273 scopus 로고
    • Interaction of fluorescently labeled analogues of the amino-terminal fusion peptide of Sendai virus with phospholipid membranes
    • Rapaport, D. and Shai, Y. (1994) Interaction of fluorescently labeled analogues of the amino-terminal fusion peptide of Sendai virus with phospholipid membranes. Journal of Biological Chemistry, 269, 15124-15131.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 15124-15131
    • Rapaport, D.1    Shai, Y.2
  • 105
    • 0028977999 scopus 로고
    • Orientation of the lipid domains and of the apolipophorin-III in the insect apolipophorin-III-dimyristoylphosphatidylcholine complexes
    • Raussens. V., Goormaghtigh, E., Ryan, R. O. and Ruysschaert, J.-M. (1995) Orientation of the lipid domains and of the apolipophorin-III in the insect apolipophorin-III-dimyristoylphosphatidylcholine complexes. Journal of Biological Chemistry, 270, 12542-12547.
    • (1995) Journal of Biological Chemistry , vol.270 , pp. 12542-12547
    • Raussens, V.1    Goormaghtigh, E.2    Ryan, R.O.3    Ruysschaert, J.-M.4
  • 106
    • 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. (1995) The envelope glycoprotein from tick-borne encephalitis virus at 2 Å resolution. Nature, 375, 291-298.
    • (1995) Nature , vol.375 , pp. 291-298
    • Rey, F.A.1    Heinz, F.X.2    Mandl, C.3    Kunz, C.4    Harrison, S.C.5
  • 107
    • 0021068591 scopus 로고
    • Oligopeptides that specifically inhibit membrane fusion by paramyxoviruses: Studies on the site of action
    • Richardson, C. D. and Choppin, P. W. (1983) Oligopeptides that specifically inhibit membrane fusion by paramyxoviruses: studies on the site of action. Virology, 131, 518-532.
    • (1983) Virology , vol.131 , pp. 518-532
    • Richardson, C.D.1    Choppin, P.W.2
  • 109
    • 0024406233 scopus 로고
    • Initial stages of influenza hemagglutinin-induced cell fusion monitored simultaneously by two fluorescent events: Cytoplasmic continuity and lipid mixing
    • Sarkar, D. P., Morris, S. J., Eidelman, O., Zimmerberg, J. and Blumenthal, R. (1989) Initial stages of influenza hemagglutinin-induced cell fusion monitored simultaneously by two fluorescent events: cytoplasmic continuity and lipid mixing. Journal of Cell Biology, 109, 113-122.
    • (1989) Journal of Cell Biology , vol.109 , pp. 113-122
    • Sarkar, D.P.1    Morris, S.J.2    Eidelman, O.3    Zimmerberg, J.4    Blumenthal, R.5
  • 110
    • 0029062097 scopus 로고
    • Requirement of N-terminal amino acid residues of gp41 for human immunodeficiency virus type 1-mediated cell fusion
    • Schaal, H., Klein, M., Gehrmann, P., Adams, O. and Scheid, A. (1995) Requirement of N-terminal amino acid residues of gp41 for human immunodeficiency virus type 1-mediated cell fusion. Journal of Virology, 69, 3308-3314.
    • (1995) Journal of Virology , vol.69 , pp. 3308-3314
    • Schaal, H.1    Klein, M.2    Gehrmann, P.3    Adams, O.4    Scheid, A.5
  • 111
    • 0027190432 scopus 로고
    • Role of the fusion peptide sequence in initial stages of influenza hemagglutinin-induced cell fusion
    • Schoch, C. and Blumenthal, R. (1993) Role of the fusion peptide sequence in initial stages of influenza hemagglutinin-induced cell fusion. Journal of Biological Chemistry, 268, 9267-9274.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 9267-9274
    • Schoch, C.1    Blumenthal, R.2
  • 112
    • 0028788193 scopus 로고
    • Molecular recognition between membrane-spanning polypeptides
    • Shai, Y. (1995) Molecular recognition between membrane-spanning polypeptides. Trends in Biochemical Sciences, 20, 460-464.
    • (1995) Trends in Biochemical Sciences , vol.20 , pp. 460-464
    • Shai, Y.1
  • 113
    • 0027362739 scopus 로고
    • Energetics of intermediates in membrane fusion: Comparison of stalk and inverted micellar intermediate mechanisms
    • Siegel, D. P. (1993a) Energetics of intermediates in membrane fusion: comparison of stalk and inverted micellar intermediate mechanisms. Biophysical Journal, 65, 2124-2140.
    • (1993) Biophysical Journal , vol.65 , pp. 2124-2140
    • Siegel, D.P.1
  • 114
    • 0001835372 scopus 로고
    • Modeling protein-induced fusion mechanisms: Insights from the relative stability of lipidic structures
    • J. Bentz, ed (CRC Press, Boca Raton, Ann Arbor, London & Tokyo)
    • Siegel, D. P. (1993b) Modeling protein-induced fusion mechanisms: insights from the relative stability of lipidic structures. In Viral Fusion Mechanisms, J. Bentz, ed (CRC Press, Boca Raton, Ann Arbor, London & Tokyo), pp. 475-512.
    • (1993) Viral Fusion Mechanisms , pp. 475-512
    • Siegel, D.P.1
  • 115
    • 0025875216 scopus 로고
    • The first milliseconds of the pore formed by a fusogenic viral envelope protein during membrane fusion
    • Spruce, A. E., Iwata, A. and Almers, W. (1991) The first milliseconds of the pore formed by a fusogenic viral envelope protein during membrane fusion. Proceedings of the National Academy of Sciences, USA, 88, 3623-3627.
    • (1991) Proceedings of the National Academy of Sciences, USA , vol.88 , pp. 3623-3627
    • Spruce, A.E.1    Iwata, A.2    Almers, W.3
  • 116
    • 0024331657 scopus 로고
    • Patch clamp studies of single cell-fusion events mediated by a viral fusion protein
    • Spruce, A. E., Iwata, A., White, J. M. and Almers, W. (1989) Patch clamp studies of single cell-fusion events mediated by a viral fusion protein. Nature, 342, 555-558.
    • (1989) Nature , vol.342 , pp. 555-558
    • Spruce, A.E.1    Iwata, A.2    White, J.M.3    Almers, W.4
  • 117
    • 0026735967 scopus 로고
    • Role of the fusogenic peptide sequence in syncytium induction and infectivity of human immunodeficiency virus type 2
    • Steffy, K. R., Kraus, G., Looney, D. J. and Wong-Staal, F. (1992) Role of the fusogenic peptide sequence in syncytium induction and infectivity of human immunodeficiency virus type 2. Journal of Virology, 66, 4532-4535.
    • (1992) Journal of Virology , vol.66 , pp. 4532-4535
    • Steffy, K.R.1    Kraus, G.2    Looney, D.J.3    Wong-Staal, F.4
  • 118
    • 0028448430 scopus 로고
    • Anchors aweigh
    • Stegmann, T. (1994) Anchors aweigh. Current Biology, 4, 551-554.
    • (1994) Current Biology , vol.4 , pp. 551-554
    • Stegmann, T.1
  • 119
    • 0026062948 scopus 로고
    • The HA2 subunit of influenza hemagglutin inserts into the target membrane prior to fusion
    • Stegmann, T., Delfino, J. M., Richards, F. M., Helenius, A. (1991) The HA2 subunit of influenza hemagglutin inserts into the target membrane prior to fusion. Journal of Biological Chemistry, 266, 18404-18410.
    • (1991) Journal of Biological Chemistry , vol.266 , pp. 18404-18410
    • Stegmann, T.1    Delfino, J.M.2    Richards, F.M.3    Helenius, A.4
  • 121
    • 0002506954 scopus 로고
    • Influenza virus fusion: From models toward a mechanism
    • J. Bentz, ed (CRC Press, Boca Raton, Ann Arbor, London & Tokyo)
    • Stegmann, T. and Helenius, A. (1993) Influenza virus fusion: from models toward a mechanism. In Viral Fusion Mechanisms, J. Bentz, ed (CRC Press, Boca Raton, Ann Arbor, London & Tokyo), pp. 89-111.
    • (1993) Viral Fusion Mechanisms , pp. 89-111
    • Stegmann, T.1    Helenius, A.2
  • 122
    • 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. (1995) Studies of the membrane fusion activities of fusion peptide mutants of influenza virus hemagglutinin. Journal of Virology, 69, 6643-6651.
    • (1995) Journal of Virology , vol.69 , pp. 6643-6651
    • Steinhauer, D.A.1    Wharton, S.A.2    Skehel, J.J.3    Wiley, D.C.4
  • 123
    • 0025369546 scopus 로고
    • Conformation of membrane fusion-active 20 residues peptides with or without lipid bilayers. Implication of α-helix formation for membrane fusion
    • Takahashi S. (1990) Conformation of membrane fusion-active 20 residues peptides with or without lipid bilayers. Implication of α-helix formation for membrane fusion. Biochemistry, 29, 6257-6264.
    • (1990) Biochemistry , vol.29 , pp. 6257-6264
    • Takahashi, S.1
  • 124
    • 0027092981 scopus 로고
    • The Glycophorin a transmembrane domain dimer: Sequence-specific propensity for a right-handed supercoil of helices
    • Treutlein, H. R., Lemmon, M. A., Engelman, D. M. and Brünger, A. T. (1992) The Glycophorin A transmembrane domain dimer: sequence-specific propensity for a right-handed supercoil of helices. Biochemistry, 31, 12726-12733.
    • (1992) Biochemistry , vol.31 , pp. 12726-12733
    • Treutlein, H.R.1    Lemmon, M.A.2    Engelman, D.M.3    Brünger, A.T.4
  • 125
    • 0027180538 scopus 로고
    • Membrane flux through the pore formed by a fusogenic viral envelope protein during cell fusion
    • Tse, F. W., Iwata, A. and Almers, W. (1993) Membrane flux through the pore formed by a fusogenic viral envelope protein during cell fusion. Journal of Cell Biology, 121, 543-552.
    • (1993) Journal of Cell Biology , vol.121 , pp. 543-552
    • Tse, F.W.1    Iwata, A.2    Almers, W.3
  • 126
    • 0026795207 scopus 로고
    • Secondary structure and orientation of the surfactant protein SP-B in a lipid environment. A Fourier transform infrared spectroscopy study
    • Vandenbussche, G., Clercx, A., Clercx, M., Curstedt, T., Johansson, J., Jornvall, H. and Ruysschaert, J.-M. (1992) Secondary structure and orientation of the surfactant protein SP-B in a lipid environment. A Fourier transform infrared spectroscopy study. Biochemistry, 31, 9169-9176.
    • (1992) Biochemistry , vol.31 , pp. 9169-9176
    • Vandenbussche, G.1    Clercx, A.2    Clercx, M.3    Curstedt, T.4    Johansson, J.5    Jornvall, H.6    Ruysschaert, J.-M.7
  • 128
    • 0027458763 scopus 로고
    • Importance of conserved amino acids at the cleavage site of the haemagglutinin of a virulent avian influenza A virus
    • Walker, J. A. and Kawaoka, Y. (1993) Importance of conserved amino acids at the cleavage site of the haemagglutinin of a virulent avian influenza A virus. Journal of General Virology, 74, 311-314.
    • (1993) Journal of General Virology , vol.74 , pp. 311-314
    • Walker, J.A.1    Kawaoka, Y.2
  • 129
    • 0028298880 scopus 로고
    • Evidence for H+-induced insertion of the influenza hemagglutinin HA2 N-terminal segment into the viral membrane
    • Weber, T., Paesold, G., Mischler, R., Semenza, G. and Brunner, J. (1994) Evidence for H+-induced insertion of the influenza hemagglutinin HA2 N-terminal segment into the viral membrane. Journal of Biological Chemistry, 269, 18353-18358.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 18353-18358
    • Weber, T.1    Paesold, G.2    Mischler, R.3    Semenza, G.4    Brunner, J.5
  • 130
  • 132
    • 0028855669 scopus 로고
    • Electron microscopy of antibody complexes of influenza virus haemagglutinin in the fusion pH conformation
    • Wharton, S. A., Calder, L. J., Ruigrok, R. W. H., Skehel, J. J., Steinhauer, D. A. and Wiley, D. C. (1995) Electron microscopy of antibody complexes of influenza virus haemagglutinin in the fusion pH conformation. EMBO Journal, 14, 240-246.
    • (1995) EMBO Journal , vol.14 , pp. 240-246
    • Wharton, S.A.1    Calder, L.J.2    Ruigrok, R.W.H.3    Skehel, J.J.4    Steinhauer, D.A.5    Wiley, D.C.6
  • 134
    • 0002865114 scopus 로고
    • Structure, Function, and Antigenicity of the Hemagglutinin of Influenza Virus
    • R. M. Krug (Plenum Press)
    • Wharton, S. A., Weis, W., Skehel, J. J. and Wiley, D. C. (1989) Structure, Function, and Antigenicity of the Hemagglutinin of Influenza Virus. In The Influenza Viruses, R. M. Krug (Plenum Press), pp. 153-173.
    • (1989) The Influenza Viruses , pp. 153-173
    • Wharton, S.A.1    Weis, W.2    Skehel, J.J.3    Wiley, D.C.4
  • 135
    • 0025276435 scopus 로고
    • Iral and cellular membrane fusion proteins
    • White, J. M. (1990) iral and cellular membrane fusion proteins. Annual Review of Physiology, 52, 675-697.
    • (1990) Annual Review of Physiology , vol.52 , pp. 675-697
    • White, J.M.1
  • 136
    • 0026492542 scopus 로고
    • Membrane Fusion
    • White, J. M. (1992) Membrane Fusion. Science, 258, 917-924.
    • (1992) Science , vol.258 , pp. 917-924
    • White, J.M.1
  • 137
    • 0002641729 scopus 로고
    • Fusion of influenza virus in endosomes: Role of the hemagglutinin
    • E. Wimmer, ed (Cold Spring Harbor Press, New York)
    • White, J. M. (1994) Fusion of influenza virus in endosomes: role of the hemagglutinin. In Cellular Receptors for Animal Viruses, E. Wimmer, ed (Cold Spring Harbor Press, New York), pp. 281-301.
    • (1994) Cellular Receptors for Animal Viruses , pp. 281-301
    • White, J.M.1
  • 139
    • 0023574003 scopus 로고
    • Antipeptide antibodies detect steps in a protein conformational change: Low-pH activation of the influenza virus hemagglutinin
    • White, J. M. and Wilson, I. A. (1987) Antipeptide antibodies detect steps in a protein conformational change: low-pH activation of the influenza virus hemagglutinin. Journal of Cell Biology, 105, 2887-2896.
    • (1987) Journal of Cell Biology , vol.105 , pp. 2887-2896
    • White, J.M.1    Wilson, I.A.2
  • 140
    • 0025165610 scopus 로고
    • A fusion-defective mutant of the vesicular stomatitis virus glycoprotein
    • Whitt, M. A., Zagouras, P., Crise, B. and Rose, J. K. (1990) A fusion-defective mutant of the vesicular stomatitis virus glycoprotein. Journal of Virology, 64, 4907-4913.
    • (1990) Journal of Virology , vol.64 , pp. 4907-4913
    • Whitt, M.A.1    Zagouras, P.2    Crise, B.3    Rose, J.K.4
  • 141
    • 0028575843 scopus 로고
    • Propensity for a leucine zipper-like domain of human immunodeficiency virus type 1 gp41 to form oligomers correlates with a role in virus-induced fusion rather than assembly of the glycoprotein complex
    • Wild, C., Dubay, J. W., Greenwell, T., Baird, Jr., T., Oas, T. G., McDanal, C., Hunter, E. and Matthews, T. (1994) Propensity for a leucine zipper-like domain of human immunodeficiency virus type 1 gp41 to form oligomers correlates with a role in virus-induced fusion rather than assembly of the glycoprotein complex. Proceedings of the National Academy of Sciences, 91, 12676-12680.
    • (1994) Proceedings of the National Academy of Sciences , vol.91 , pp. 12676-12680
    • Wild, C.1    Dubay, J.W.2    Greenwell, T.3    Baird Jr., T.4    Oas, T.G.5    McDanal, C.6    Hunter, E.7    Matthews, T.8
  • 142
    • 0023082135 scopus 로고
    • The structure and function of the hemagglutinin membrane glycoprotein of influenza virus
    • Wiley, D. C. and Skehel, J. J. (1987) The structure and function of the hemagglutinin membrane glycoprotein of influenza virus. Annual Review of Biochemistry, 56, 365-394.
    • (1987) Annual Review of Biochemistry , vol.56 , pp. 365-394
    • Wiley, D.C.1    Skehel, J.J.2
  • 143
    • 0002466516 scopus 로고
    • The influenza virus hemagglutinin: Membrane fusion activity in intact virions and reconstructed virosomes
    • J. Bentz, ed (CRC Press, Boca Raton, Ann Arbor, London & Tokyo)
    • Wilschut, J. and Bron, R. (1993) The influenza virus hemagglutinin: membrane fusion activity in intact virions and reconstructed virosomes. In Viral Fusion Mechanisms, J. Bentz, ed (CRC Press, Boca Raton, Ann Arbor, London & Tokyo), pp. 133-161.
    • (1993) Viral Fusion Mechanisms , pp. 133-161
    • Wilschut, J.1    Bron, R.2
  • 144
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 angstroms resolution
    • Wilson, I. A., Skehel, J. J. and Wiley, D. C. (1981) Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 angstroms resolution. Nature, 289, 366-373.
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 145
    • 0027967960 scopus 로고
    • Insertion of a coiled-coil peptide from influenza virus hemagglutinin into membranes
    • Yu, Y. G., King, D. S. and Shin, Y.-K. (1994) Insertion of a coiled-coil peptide from influenza virus hemagglutinin into membranes. Science, 266, 274-276
    • (1994) Science , vol.266 , pp. 274-276
    • Yu, Y.G.1    King, D.S.2    Shin, Y.-K.3
  • 146
    • 0028288527 scopus 로고
    • Characterization of the putative fusogenic domain in vesicular stomatitis virus glycoprotein G
    • Zhang, L. and Ghosh, H. P. (1994) Characterization of the putative fusogenic domain in vesicular stomatitis virus glycoprotein G. Journal of Virology, 68, 2186-2193.
    • (1994) Journal of Virology , vol.68 , pp. 2186-2193
    • Zhang, L.1    Ghosh, H.P.2
  • 147
    • 0028587209 scopus 로고
    • Restricted movement of lipid and aqueous dyes through pores formed by influenza hemagglutinin during cell fusion
    • Zimmerberg, J., Blumenthal, R., Sarkar, D. P., Curran, M. and Morris, S. J. (1994) Restricted movement of lipid and aqueous dyes through pores formed by influenza hemagglutinin during cell fusion. Journal of Cell Biology, 127, 1885-1894.
    • (1994) Journal of Cell Biology , vol.127 , pp. 1885-1894
    • Zimmerberg, J.1    Blumenthal, R.2    Sarkar, D.P.3    Curran, M.4    Morris, S.J.5


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