메뉴 건너뛰기




Volumn 44, Issue C, 1997, Pages 403-445

Chapter 11 Morphology of Membrane Fusion

Author keywords

[No Author keywords available]

Indexed keywords


EID: 77956686958     PISSN: 00702161     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0070-2161(08)60215-4     Document Type: Article
Times cited : (10)

References (136)
  • 1
    • 0028355514 scopus 로고
    • Fusion of influenza virus with sialic acid-bearing target membranes
    • Alford D., Ellens H., and Bentz J. Fusion of influenza virus with sialic acid-bearing target membranes. Biochemistry 33 (1994) 1977-1987
    • (1994) Biochemistry , vol.33 , pp. 1977-1987
    • Alford, D.1    Ellens, H.2    Bentz, J.3
  • 5
    • 0018972314 scopus 로고
    • Control of membrane fusion in exocytosis: Physiological studies on a Puramecium mutant blocked in the final step of the trichocyst extrusion process
    • Beisson J., Cohen J., Lefort-Tran M., Pouphile M., and Rossignol M. Control of membrane fusion in exocytosis: Physiological studies on a Puramecium mutant blocked in the final step of the trichocyst extrusion process. J. Cell Biol. 85 (1980) 213-227
    • (1980) J. Cell Biol. , vol.85 , pp. 213-227
    • Beisson, J.1    Cohen, J.2    Lefort-Tran, M.3    Pouphile, M.4    Rossignol, M.5
  • 6
    • 0027714924 scopus 로고
    • Interactions of synapsin I with phospholipids: Possible role in synaptic vesicle clustering and in the maintenance of bilayer structures
    • Benfenati F., Valtorta F., Rossi M.C., Onofri F., Sihra T., and Greengard P. Interactions of synapsin I with phospholipids: Possible role in synaptic vesicle clustering and in the maintenance of bilayer structures. J. Cell Biol. 123 (1993) 1845-1855
    • (1993) J. Cell Biol. , vol.123 , pp. 1845-1855
    • Benfenati, F.1    Valtorta, F.2    Rossi, M.C.3    Onofri, F.4    Sihra, T.5    Greengard, P.6
  • 7
    • 0004060046 scopus 로고
    • Bentz J. (Ed), CRC Press, Boca Raton, FL.
    • In: Bentz J. (Ed). Viral Fusion Mechanisms. (1993), CRC Press, Boca Raton, FL.
    • (1993) Viral Fusion Mechanisms.
  • 8
    • 0023308543 scopus 로고
    • Membrane fusion: Kinetics and mechanisms
    • Bentz J., and Ellens H. Membrane fusion: Kinetics and mechanisms. Colloid Surfaces 30 (1988) 65-112
    • (1988) Colloid Surfaces , vol.30 , pp. 65-112
    • Bentz, J.1    Ellens, H.2
  • 9
    • 0025639178 scopus 로고
    • An architecture for the fusion site of influenza hemagglutinin
    • Bentz J., Ellens H., and Alford D. An architecture for the fusion site of influenza hemagglutinin. FEBS Lett. 276 (1990) 1-5
    • (1990) FEBS Lett. , vol.276 , pp. 1-5
    • Bentz, J.1    Ellens, H.2    Alford, D.3
  • 10
    • 0026510747 scopus 로고
    • A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion
    • Blobel C.P., Wolfsberg T.G., Turck C.W., Myles D.G., Primakoff P., and White J.M. A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion. Nature (London) 356 (1992) 248-252
    • (1992) Nature (London) , vol.356 , pp. 248-252
    • Blobel, C.P.1    Wolfsberg, T.G.2    Turck, C.W.3    Myles, D.G.4    Primakoff, P.5    White, J.M.6
  • 11
    • 0015908195 scopus 로고
    • Studies in fixation for electron microscopy using cultured cells
    • Buckley I.K. Studies in fixation for electron microscopy using cultured cells. Lab. Invest. 29 (1973) 398-410
    • (1973) Lab. Invest. , vol.29 , pp. 398-410
    • Buckley, I.K.1
  • 13
    • 0024294320 scopus 로고
    • Influenza virus-model membrane interaction: A morphological approach using modern cryotechniques
    • Burger K.N.J., Knoll G., and Verkleij A.J. Influenza virus-model membrane interaction: A morphological approach using modern cryotechniques. Biochim. Biophys. Acad 939 (1988) 89-101
    • (1988) Biochim. Biophys. Acad , vol.939 , pp. 89-101
    • Burger, K.N.J.1    Knoll, G.2    Verkleij, A.J.3
  • 14
    • 77956696927 scopus 로고
    • Influenza virus mediated membrane fusion: The identification of fusion intermediates using modern cryotechniques
    • Op den Kamp J.A.F. (Ed), Springer-Verlag, Berlin NATO-ASI Series Vol. H40
    • Burger K.N.J., Knoll G., Frederik P.M., and Verkleij A.J. Influenza virus mediated membrane fusion: The identification of fusion intermediates using modern cryotechniques. In: Op den Kamp J.A.F. (Ed). Dynamics and Biogenesis of Membranes (1990), Springer-Verlag, Berlin 185-196 NATO-ASI Series Vol. H40
    • (1990) Dynamics and Biogenesis of Membranes , pp. 185-196
    • Burger, K.N.J.1    Knoll, G.2    Frederik, P.M.3    Verkleij, A.J.4
  • 15
    • 0025858611 scopus 로고
    • Phospholipase C activily-induced fusion of pure lipid model membranes: A freeze fracture study
    • Burger K.N.J., Nieva J.L., Alonso A., and Verkleij A.J. Phospholipase C activily-induced fusion of pure lipid model membranes: A freeze fracture study. Biochim. Biophys. Acta 1068 (1991) 249-253
    • (1991) Biochim. Biophys. Acta , vol.1068 , pp. 249-253
    • Burger, K.N.J.1    Nieva, J.L.2    Alonso, A.3    Verkleij, A.J.4
  • 16
    • 0026315845 scopus 로고
    • Interaction of influenza virus hemagglutinin with a lipid monolayer: A comparison of the surface activities of intact virions, isolated hemagglutinins. and a synthetic fusion peptide
    • Burger K.N.J., Wharton S.A., Demel R.A., and Verkleij A.J. Interaction of influenza virus hemagglutinin with a lipid monolayer: A comparison of the surface activities of intact virions, isolated hemagglutinins. and a synthetic fusion peptide. Biochemistry 30 (1991) 11173-11180
    • (1991) Biochemistry , vol.30 , pp. 11173-11180
    • Burger, K.N.J.1    Wharton, S.A.2    Demel, R.A.3    Verkleij, A.J.4
  • 18
    • 0027258953 scopus 로고
    • Regulated exocytosis
    • Burgoyne R.D., and Morgan A. Regulated exocytosis. Biochem. J. 293 (1993) 305-316
    • (1993) Biochem. J. , vol.293 , pp. 305-316
    • Burgoyne, R.D.1    Morgan, A.2
  • 19
    • 0021647507 scopus 로고
    • Comparison of quick-frozen and chemically fixed sea-urchin eggs: Structural evidence that cortical granule exocytosis is preceded by a local increase in membrane mobility
    • Chandler D.E. Comparison of quick-frozen and chemically fixed sea-urchin eggs: Structural evidence that cortical granule exocytosis is preceded by a local increase in membrane mobility. J. Cell Sci. 72 (1984) 23-36
    • (1984) J. Cell Sci. , vol.72 , pp. 23-36
    • Chandler, D.E.1
  • 20
    • 0342702976 scopus 로고
    • Exocytosis and endocytosis: Membrane fusion events captured in rapidly frozen cells
    • Chandler D.E. Exocytosis and endocytosis: Membrane fusion events captured in rapidly frozen cells. Curr. Top. Membr. Transp. 32 (1988) 169-202
    • (1988) Curr. Top. Membr. Transp. , vol.32 , pp. 169-202
    • Chandler, D.E.1
  • 21
    • 0018644692 scopus 로고
    • Membrane fusion during secretion: Cortical granule exocytosis in sea urchin eggs as studied by quick-freezing and freeze-fracture
    • Chandler D.E., and Heuser J.E. Membrane fusion during secretion: Cortical granule exocytosis in sea urchin eggs as studied by quick-freezing and freeze-fracture. J. Cell Biol. 83 (1979) 91-108
    • (1979) J. Cell Biol. , vol.83 , pp. 91-108
    • Chandler, D.E.1    Heuser, J.E.2
  • 22
    • 0019305230 scopus 로고
    • Arrest of membrane fusion events in mast cells by quick-freezing
    • Chandler D.E., and Heuser J.E. Arrest of membrane fusion events in mast cells by quick-freezing. J. Cell Biol. 86 (1980) 666-674
    • (1980) J. Cell Biol. , vol.86 , pp. 666-674
    • Chandler, D.E.1    Heuser, J.E.2
  • 23
    • 0024722946 scopus 로고
    • High molecular weight polymers block cortical granule exocytosis in sea urchin eggs at the level of granule matrix disassembly
    • Chandler D.E., Whitaker M., and Zimmerberg J. High molecular weight polymers block cortical granule exocytosis in sea urchin eggs at the level of granule matrix disassembly. J. Cell Biol. 109 (1989) 1269-1278
    • (1989) J. Cell Biol. , vol.109 , pp. 1269-1278
    • Chandler, D.E.1    Whitaker, M.2    Zimmerberg, J.3
  • 25
    • 0023636677 scopus 로고
    • Biomembrane fusion: A new concept derived from model studies using two interacting planar lipid bilayers
    • Chernomordik L.V., Melikyan G.B., and Chizmadzhev Y.A. Biomembrane fusion: A new concept derived from model studies using two interacting planar lipid bilayers. Biochim. Biophys. Acta 906 (1987) 309-352
    • (1987) Biochim. Biophys. Acta , vol.906 , pp. 309-352
    • Chernomordik, L.V.1    Melikyan, G.B.2    Chizmadzhev, Y.A.3
  • 26
    • 0027510261 scopus 로고
    • Lysolipids reversibly inhibit Ca-2+ -dependent, GTP-dependent and pH-dependent fusion of biological membranes
    • Chernomordik L.V., Vogel S.S., Sokoloff A., Onaran H.O., Leikina E.A., and Zimmerberg J. Lysolipids reversibly inhibit Ca-2+ -dependent, GTP-dependent and pH-dependent fusion of biological membranes. FEBS Lett 318 (1993) 71-76
    • (1993) FEBS Lett , vol.318 , pp. 71-76
    • Chernomordik, L.V.1    Vogel, S.S.2    Sokoloff, A.3    Onaran, H.O.4    Leikina, E.A.5    Zimmerberg, J.6
  • 27
    • 0026527830 scopus 로고
    • A temperature-jump device for time-resolved cryo-transmission electron microscopy
    • Chestnut M.H., Siegel D.P., Burns J.L., and Talmon Y. A temperature-jump device for time-resolved cryo-transmission electron microscopy. Micros. Res. Tech. 20 (1992) 95-101
    • (1992) Micros. Res. Tech. , vol.20 , pp. 95-101
    • Chestnut, M.H.1    Siegel, D.P.2    Burns, J.L.3    Talmon, Y.4
  • 31
    • 0025876649 scopus 로고
    • Static and dynamic lipid asymmetry in cell membranes
    • Devaux P.F. Static and dynamic lipid asymmetry in cell membranes. Biochemistry 30 (1991) 1163-1173
    • (1991) Biochemistry , vol.30 , pp. 1163-1173
    • Devaux, P.F.1
  • 36
    • 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. Fusion of influenza hemagglutinin-expressing fibroblasts with glycophorin-bearing liposomes: Role of hemagglutinin surface density. Biochemistry 29 (1990) 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
  • 38
    • 84986676687 scopus 로고
    • Phospholipid, nature's own slide and cover slip for cryo-electron microscopy
    • Frederik P.M., Stuart M.G., Bomans P.H., and Busing W.M. Phospholipid, nature's own slide and cover slip for cryo-electron microscopy. J. Micros. 153 (1989) 81-92
    • (1989) J. Micros. , vol.153 , pp. 81-92
    • Frederik, P.M.1    Stuart, M.G.2    Bomans, P.H.3    Busing, W.M.4
  • 40
    • 0019422177 scopus 로고
    • Orderly particle arrays on the mitochondrial outer membrane in rapidly frozen sperm
    • Friend D.S., and Heuser J.E. Orderly particle arrays on the mitochondrial outer membrane in rapidly frozen sperm. Anat. Rec. 199 (1981) 159-175
    • (1981) Anat. Rec. , vol.199 , pp. 159-175
    • Friend, D.S.1    Heuser, J.E.2
  • 41
    • 0021921188 scopus 로고
    • Arachidonic acid release and catecholamine secretion from digitonin-treated chromaffin cells: Effects of micromolar calcium, phorbol ester, and protein alkylating agents
    • Frye R.A., and Holz R.W. Arachidonic acid release and catecholamine secretion from digitonin-treated chromaffin cells: Effects of micromolar calcium, phorbol ester, and protein alkylating agents. J. Neurochem. 44 (1985) 265-273
    • (1985) J. Neurochem. , vol.44 , pp. 265-273
    • Frye, R.A.1    Holz, R.W.2
  • 42
    • 0025601479 scopus 로고
    • Membrane fusion events during endocytosis in mouse kidney tubule cells detected by rapid freezing followed by freezesubstitution
    • Fujioka A., Ohtsuki M., Nagano M., and Mori S. Membrane fusion events during endocytosis in mouse kidney tubule cells detected by rapid freezing followed by freezesubstitution. J. Electron Micros. Tokyo. 39 (1990) 356-362
    • (1990) J. Electron Micros. Tokyo. , vol.39 , pp. 356-362
    • Fujioka, A.1    Ohtsuki, M.2    Nagano, M.3    Mori, S.4
  • 43
    • 0022619527 scopus 로고
    • Studies on the mechanism of membrane fusion: Site-specific mutagenesis of the hemagglutinin of influenza virus
    • Gething M.J., Doms R.W., York D., and White J. Studies on the mechanism of membrane fusion: Site-specific mutagenesis of the hemagglutinin of influenza virus. J. Cell Biol. 102 (1986) 11-23
    • (1986) J. Cell Biol. , vol.102 , pp. 11-23
    • Gething, M.J.1    Doms, R.W.2    York, D.3    White, J.4
  • 44
    • 0022653966 scopus 로고
    • Advances in ultrarapid freezing for the preservation of cellular ultrastructure
    • Gilkey J.C., and Staehelin L.A. Advances in ultrarapid freezing for the preservation of cellular ultrastructure. J. Electron Micros. Tech. 3 (1986) 177-210
    • (1986) J. Electron Micros. Tech. , vol.3 , pp. 177-210
    • Gilkey, J.C.1    Staehelin, L.A.2
  • 45
    • 0028301321 scopus 로고
    • II phase with its ability to promote membrane fusion
    • II phase with its ability to promote membrane fusion. Biochemistry 33 (1994) 5805-5812
    • (1994) Biochemistry , vol.33 , pp. 5805-5812
    • Glaser, P.E.1    Gross, R.W.2
  • 46
    • 0024564217 scopus 로고
    • Hydrophobic binding of the ectodomain of influenza hemagglutinin to membranes occurs through the "fusion peptide"
    • Harter C., James P., Bschi T., Semenza G., and Brunner J. Hydrophobic binding of the ectodomain of influenza hemagglutinin to membranes occurs through the "fusion peptide". J. Biol. Chem. 264 (1989) 6459-6464
    • (1989) J. Biol. Chem. , vol.264 , pp. 6459-6464
    • Harter, C.1    James, P.2    Bschi, T.3    Semenza, G.4    Brunner, J.5
  • 47
    • 0026602695 scopus 로고
    • Role of hydrophobic forces in bilayer adhesion and fusion
    • Helm C.A., Israelachvili J.N., and McGuiggan P.M. Role of hydrophobic forces in bilayer adhesion and fusion. Biochemistry 31 (1992) 1794-1805
    • (1992) Biochemistry , vol.31 , pp. 1794-1805
    • Helm, C.A.1    Israelachvili, J.N.2    McGuiggan, P.M.3
  • 48
    • 0016366689 scopus 로고
    • Functional changes in frog neuromuscular junctions studied with freeze-fracture
    • Heuser J.E., Reese T.S., and Landis D.M.D. Functional changes in frog neuromuscular junctions studied with freeze-fracture. J. Neurocytol. 3 (1974) 109-131
    • (1974) J. Neurocytol. , vol.3 , pp. 109-131
    • Heuser, J.E.1    Reese, T.S.2    Landis, D.M.D.3
  • 49
    • 0018746093 scopus 로고
    • Synaptic vesicle exocytosis captured by quick freezing and correlated with quantal transmitter release
    • Heuser J.E., Reese T.S., Dennis M.J., Jan Y., Jan L., and Evans L. Synaptic vesicle exocytosis captured by quick freezing and correlated with quantal transmitter release. J. Cell Biol. 81 (1979) 275-300
    • (1979) J. Cell Biol. , vol.81 , pp. 275-300
    • Heuser, J.E.1    Reese, T.S.2    Dennis, M.J.3    Jan, Y.4    Jan, L.5    Evans, L.6
  • 50
    • 0026646436 scopus 로고
    • A cortical phosphoprotein ('PP63') sensitive to exocytosis triggering in Paramecium cells: Immunolocalization and quenched-flow correlation of time course of dephosphorylation with membrane fusion
    • Hohne-Zell B., Knoll G., Riedel-Gras U., Hofer W., and Plattner H. A cortical phosphoprotein ('PP63') sensitive to exocytosis triggering in Paramecium cells: Immunolocalization and quenched-flow correlation of time course of dephosphorylation with membrane fusion. Biochem. J. 286 (1992) 843-849
    • (1992) Biochem. J. , vol.286 , pp. 843-849
    • Hohne-Zell, B.1    Knoll, G.2    Riedel-Gras, U.3    Hofer, W.4    Plattner, H.5
  • 51
    • 33845457521 scopus 로고
    • The role of non-bilayer structures in the fusion of human erythrocytes induced by lipid fusogens
    • Hope M.J., and Cullis P.R. The role of non-bilayer structures in the fusion of human erythrocytes induced by lipid fusogens. Biochim. Biophys. Acta 640 (1981) 82-90
    • (1981) Biochim. Biophys. Acta , vol.640 , pp. 82-90
    • Hope, M.J.1    Cullis, P.R.2
  • 52
    • 0027484593 scopus 로고
    • Orientation of fusion-active synthetic peptides in phospholipid bilayers-determination by Fourier transform infrared spectroscopy
    • Ishiguro R., Kimura N., and Takahashi S. Orientation of fusion-active synthetic peptides in phospholipid bilayers-determination by Fourier transform infrared spectroscopy. Biochemistry 32 (1993) 9792-9797
    • (1993) Biochemistry , vol.32 , pp. 9792-9797
    • Ishiguro, R.1    Kimura, N.2    Takahashi, S.3
  • 53
    • 0015925372 scopus 로고
    • Fluidity of phospholipid bilayers and membranes after exposure to osmium tetroxide and glutaraldehyde
    • Jost P., Brooks U.J., and Griffith O.H. Fluidity of phospholipid bilayers and membranes after exposure to osmium tetroxide and glutaraldehyde. J. Mol. Biol. 76 (1973) 313-318
    • (1973) J. Mol. Biol. , vol.76 , pp. 313-318
    • Jost, P.1    Brooks, U.J.2    Griffith, O.H.3
  • 54
    • 38249004014 scopus 로고
    • Much ado about docking
    • Kelly R.B. Much ado about docking. Curr. Biol. 7 (1993) 474-476
    • (1993) Curr. Biol. , vol.7 , pp. 474-476
    • Kelly, R.B.1
  • 55
    • 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
  • 56
    • 0005648680 scopus 로고
    • Cryofixation of dynamic processes in cells and organelles
    • Steinbrecht R.A., and Zierold K. (Eds), Springer-Verlag, Berlin
    • Knoll G., Verkleij A.J., and Plattner H. Cryofixation of dynamic processes in cells and organelles. In: Steinbrecht R.A., and Zierold K. (Eds). Cryotechniques in Biological Electron Microscopy (1987), Springer-Verlag, Berlin 258-271
    • (1987) Cryotechniques in Biological Electron Microscopy , pp. 258-271
    • Knoll, G.1    Verkleij, A.J.2    Plattner, H.3
  • 57
    • 0024242687 scopus 로고
    • Fusion of liposomes with the plasma membrane of epithelial cells: Fate of incorporated lipids as followed by freeze fracture and autoradiography of plastic sections
    • Knoll G., Burger K.N.J., Bron R., van Meer G., and Verkleij A.J. Fusion of liposomes with the plasma membrane of epithelial cells: Fate of incorporated lipids as followed by freeze fracture and autoradiography of plastic sections. J. Cell Biol 107 (1988) 2511-2521
    • (1988) J. Cell Biol , vol.107 , pp. 2511-2521
    • Knoll, G.1    Burger, K.N.J.2    Bron, R.3    van Meer, G.4    Verkleij, A.J.5
  • 58
    • 0025827296 scopus 로고
    • Quenched flow analysis of exocytosis in Paramecium cells: Time course, changes in membrane structure, and calcium requirements revealed after rapid mixing and rapid freezing of intact cells
    • Knoll G., Braun C., and Plattner H. Quenched flow analysis of exocytosis in Paramecium cells: Time course, changes in membrane structure, and calcium requirements revealed after rapid mixing and rapid freezing of intact cells. J. Cell Biol. 113 (1991) 1295-1304
    • (1991) J. Cell Biol. , vol.113 , pp. 1295-1304
    • Knoll, G.1    Braun, C.2    Plattner, H.3
  • 59
    • 0027050390 scopus 로고
    • pH-dependent hydrophobicity profile of hemagglutinin of influenza virus and its possible relevance in virus fusion
    • Korte T., Ludwig K., and Herrmann A. pH-dependent hydrophobicity profile of hemagglutinin of influenza virus and its possible relevance in virus fusion. Biosci. Rep. 12 (1992) 397-406
    • (1992) Biosci. Rep. , vol.12 , pp. 397-406
    • Korte, T.1    Ludwig, K.2    Herrmann, A.3
  • 62
    • 0022511350 scopus 로고
    • Electron microscopy of frozen hydrated specimens: Preparation and characteristics
    • Lepault J., and Dubochet J. Electron microscopy of frozen hydrated specimens: Preparation and characteristics. Methods Enzymol. 127 (1986) 719-730
    • (1986) Methods Enzymol. , vol.127 , pp. 719-730
    • Lepault, J.1    Dubochet, J.2
  • 63
    • 0024603546 scopus 로고
    • Cubic phases and isotropic structures formed by membrane lipids-possible biological relevance
    • Lindblom G., and Rilfors L. Cubic phases and isotropic structures formed by membrane lipids-possible biological relevance. Biochim. Biophys. Acta 988 (1989) 221-256
    • (1989) Biochim. Biophys. Acta , vol.988 , pp. 221-256
    • Lindblom, G.1    Rilfors, L.2
  • 64
    • 0014958799 scopus 로고
    • The fusion of biological membranes
    • Lucy J.A. The fusion of biological membranes. Nature (London) 227 (1970) 814-817
    • (1970) Nature (London) , vol.227 , pp. 814-817
    • Lucy, J.A.1
  • 65
    • 0038675896 scopus 로고
    • Mechanisms of chemically induced cell fusion
    • Lucy J.A. Mechanisms of chemically induced cell fusion. Cell Surface Rev. 5 (1978) 267-304
    • (1978) Cell Surface Rev. , vol.5 , pp. 267-304
    • Lucy, J.A.1
  • 66
    • 0023043923 scopus 로고
    • An osmotic model for the fusion of biological membranes
    • Lucy J.A., and Ahkong Q.F. An osmotic model for the fusion of biological membranes. FEBS Lett. 199 (1986) 1-11
    • (1986) FEBS Lett. , vol.199 , pp. 1-11
    • Lucy, J.A.1    Ahkong, Q.F.2
  • 67
    • 0020474447 scopus 로고
    • Stabilization of bilayer structure for unsaturated phosphatidylethanolamines by detergents
    • Madden T.D., and Cullis P.R. Stabilization of bilayer structure for unsaturated phosphatidylethanolamines by detergents. Biochim. Biophys. Acta 684 (1982) 149-153
    • (1982) Biochim. Biophys. Acta , vol.684 , pp. 149-153
    • Madden, T.D.1    Cullis, P.R.2
  • 68
    • 0027690647 scopus 로고
    • To fuse or not to fuse?
    • Markin V.S., and Hudspeth A.J. To fuse or not to fuse?. Biophys. J. 65 (1993) 1752-1754
    • (1993) Biophys. J. , vol.65 , pp. 1752-1754
    • Markin, V.S.1    Hudspeth, A.J.2
  • 70
    • 84986506419 scopus 로고
    • A survey of ultra-rapid cryofixation methods with particular emphasis on applications to freeze-fracturing
    • Menco B.P.M. A survey of ultra-rapid cryofixation methods with particular emphasis on applications to freeze-fracturing. J. Electron Micros. Tech. 4 (1986) 177-240
    • (1986) J. Electron Micros. Tech. , vol.4 , pp. 177-240
    • Menco, B.P.M.1
  • 71
    • 0018073825 scopus 로고
    • Monitoring of the course of fixation of plant cells
    • Mersey B., and McCully M.E. Monitoring of the course of fixation of plant cells. J. Micros. 114 (1978) 49-76
    • (1978) J. Micros. , vol.114 , pp. 49-76
    • Mersey, B.1    McCully, M.E.2
  • 72
    • 0027096398 scopus 로고
    • The exocytotic fusion pore
    • Monck J.R., and Fernandez J.M. The exocytotic fusion pore. J. Cell Biol. 119 (1992) 1395-1404
    • (1992) J. Cell Biol. , vol.119 , pp. 1395-1404
    • Monck, J.R.1    Fernandez, J.M.2
  • 73
    • 0028353472 scopus 로고
    • The exocytotic fusion pore and neurotransmitter release
    • Monck J.R., and Fernandez J.M. The exocytotic fusion pore and neurotransmitter release. Neuron 12 (1994) 707-716
    • (1994) Neuron , vol.12 , pp. 707-716
    • Monck, J.R.1    Fernandez, J.M.2
  • 74
    • 0002133971 scopus 로고
    • Theory and practice of high pressure freezing
    • Steinbrecht R.A., and Zierold K. (Eds), Springer-Verlag, Berlin
    • Moor H. Theory and practice of high pressure freezing. In: Steinbrecht R.A., and Zierold K. (Eds). Cryotechniques in Biological Electron Microscopy (1987), Springer-Verlag, Berlin 175-191
    • (1987) Cryotechniques in Biological Electron Microscopy , pp. 175-191
    • Moor, H.1
  • 76
    • 0024457473 scopus 로고
    • Liposome fusion catalytically induced by phospholipase C
    • Nieva J.L., Goni F.M., and Alonso A. Liposome fusion catalytically induced by phospholipase C. Biochemistry 28 (1989) 7364-7367
    • (1989) Biochemistry , vol.28 , pp. 7364-7367
    • Nieva, J.L.1    Goni, F.M.2    Alonso, A.3
  • 77
    • 77956664173 scopus 로고
    • Ultrastructural aspects of exocytotic membrane fusion
    • Orci L., and Perrelet A. Ultrastructural aspects of exocytotic membrane fusion. Cell Surface Rev. 5 (1978) 629-656
    • (1978) Cell Surface Rev. , vol.5 , pp. 629-656
    • Orci, L.1    Perrelet, A.2
  • 79
    • 0014301569 scopus 로고
    • Structural modulations of plasmalemmal vesicles
    • Palade G.E., and Bruns R.R. Structural modulations of plasmalemmal vesicles. J. Cell Biol. 37 (1968) 633-649
    • (1968) J. Cell Biol. , vol.37 , pp. 633-649
    • Palade, G.E.1    Bruns, R.R.2
  • 80
  • 82
    • 0019307757 scopus 로고
    • Quick freezing versus chemical fixation: Capture and identification of membrane fusion intermediates
    • Pinto da Silva P., and Kachar B. Quick freezing versus chemical fixation: Capture and identification of membrane fusion intermediates. Cell Biol. Int. Rep. 4 (1980) 625-640
    • (1980) Cell Biol. Int. Rep. , vol.4 , pp. 625-640
    • Pinto da Silva, P.1    Kachar, B.2
  • 83
    • 0017579114 scopus 로고
    • Membrane fusion during secretion: A hypothesis based on electron microscope observation of Phytophthora palmivora zoospores during encystment
    • Pinto da Silva P., and Nogueira M.L. Membrane fusion during secretion: A hypothesis based on electron microscope observation of Phytophthora palmivora zoospores during encystment. J. Cell Biol. 73 (1977) 161-181
    • (1977) J. Cell Biol. , vol.73 , pp. 161-181
    • Pinto da Silva, P.1    Nogueira, M.L.2
  • 84
    • 0019828157 scopus 로고
    • Membrane behaviour during exocytosis
    • Plattner H. Membrane behaviour during exocytosis. Cell Biol. Int. Rep. 5 (1981) 435-459
    • (1981) Cell Biol. Int. Rep. , vol.5 , pp. 435-459
    • Plattner, H.1
  • 85
    • 0020333280 scopus 로고
    • Cryofixation: A tool in biological ultrastructural research
    • Plattner H., and Bachmann L. Cryofixation: A tool in biological ultrastructural research. Int. Rev. Cytol. 79 (1982) 237-304
    • (1982) Int. Rev. Cytol. , vol.79 , pp. 237-304
    • Plattner, H.1    Bachmann, L.2
  • 86
    • 0020651559 scopus 로고
    • Electron microscopic methods in cellular and molecular biology
    • Plattner H., and Zingsheim H.P. Electron microscopic methods in cellular and molecular biology. Subcell. Biochem. 9 (1983) 1-236
    • (1983) Subcell. Biochem. , vol.9 , pp. 1-236
    • Plattner, H.1    Zingsheim, H.P.2
  • 87
    • 0027057592 scopus 로고
    • The mechanics of biological membrane fusion-merger of aspects from electron microscopy and patch-clamp analysis
    • Plattner H., Knoll G., and Erxleben C. The mechanics of biological membrane fusion-merger of aspects from electron microscopy and patch-clamp analysis. J. Cell Sci. 103 (1992) 613-618
    • (1992) J. Cell Sci. , vol.103 , pp. 613-618
    • Plattner, H.1    Knoll, G.2    Erxleben, C.3
  • 88
    • 0027197065 scopus 로고
    • Synaptotagmin: A calcium-sensitive inhibitor of exocytosis?
    • Popov S.V., and Poo M.M. Synaptotagmin: A calcium-sensitive inhibitor of exocytosis?. Cell 73 (1993) 1247-1249
    • (1993) Cell , vol.73 , pp. 1247-1249
    • Popov, S.V.1    Poo, M.M.2
  • 89
    • 0022559222 scopus 로고
    • Mimicry and mechanism in phospholipid models of membrane fusion
    • Rand R.P., and Parsegian V.A. Mimicry and mechanism in phospholipid models of membrane fusion. Annu. Rev. Physiol. 48 (1986) 201-212
    • (1986) Annu. Rev. Physiol. , vol.48 , pp. 201-212
    • Rand, R.P.1    Parsegian, V.A.2
  • 90
    • 0023052450 scopus 로고
    • Relationship between three-dimensional arrays of "lipidic particles" and bicontinuous cubic lipid phases
    • Rilfors L., Eriksson P.O., Arvidson G., and Lindblom G. Relationship between three-dimensional arrays of "lipidic particles" and bicontinuous cubic lipid phases. Biochemistry 25 (1986) 7702-7711
    • (1986) Biochemistry , vol.25 , pp. 7702-7711
    • Rilfors, L.1    Eriksson, P.O.2    Arvidson, G.3    Lindblom, G.4
  • 91
    • 0016308773 scopus 로고
    • Ultrastructural aspects of membrane fusion
    • Satir B. Ultrastructural aspects of membrane fusion. J. Suprurnol. Sfrucl. 2 (1974) 529-537
    • (1974) J. Suprurnol. Sfrucl. , vol.2 , pp. 529-537
    • Satir, B.1
  • 92
    • 0020857080 scopus 로고
    • Membrane events in adrenal chromaffin cells during exocytosis: A freeze-etching analysis after rapid cryofixation
    • Schmidt W., Patzak A., Lingg G., Winkler H., and Plattner H. Membrane events in adrenal chromaffin cells during exocytosis: A freeze-etching analysis after rapid cryofixation. Eur. J. Cell Biol. 32 (1983) 31-37
    • (1983) Eur. J. Cell Biol. , vol.32 , pp. 31-37
    • Schmidt, W.1    Patzak, A.2    Lingg, G.3    Winkler, H.4    Plattner, H.5
  • 93
    • 0021378778 scopus 로고
    • Inverted micellar structures in bilayer membranes: Formation rates and half-lives
    • Siegel D.P. Inverted micellar structures in bilayer membranes: Formation rates and half-lives. Biophys. J. 45 (1984) 399-420
    • (1984) Biophys. J. , vol.45 , pp. 399-420
    • Siegel, D.P.1
  • 94
    • 0022728192 scopus 로고
    • II phase transitions
    • II phase transitions. Biophys. J. 49 (1986) 1155-1170
    • (1986) Biophys. J. , vol.49 , pp. 1155-1170
    • Siegel, D.P.1
  • 95
    • 0022725330 scopus 로고
    • Inverted micellar intermediates and the transitions between lamellar, cubic, and inverted hexagonal lipid phases. II. Implications for membrane-membrane interactions and membrane fusion
    • Siegel D.P. Inverted micellar intermediates and the transitions between lamellar, cubic, and inverted hexagonal lipid phases. II. Implications for membrane-membrane interactions and membrane fusion. Biophys. J. 49 (1986) 1171-1183
    • (1986) Biophys. J. , vol.49 , pp. 1171-1183
    • Siegel, D.P.1
  • 96
    • 0002780891 scopus 로고
    • Membrane-membrane interactions via intermediates in lamellar-to-inverted hexagonal phase transitions
    • Sowers A.E. (Ed), Plenum Press, New York
    • Siegel D.P. Membrane-membrane interactions via intermediates in lamellar-to-inverted hexagonal phase transitions. In: Sowers A.E. (Ed). Cell Fusion (1987), Plenum Press, New York 181-208
    • (1987) Cell Fusion , pp. 181-208
    • Siegel, D.P.1
  • 97
    • 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
  • 98
    • 0001835372 scopus 로고
    • Modeling protein-induced fusion mechanisms: Insights form the relative stability of lipidic structures
    • Bentz J. (Ed), CRC Press, Boca Raton, FL.
    • Siegel D.P. Modeling protein-induced fusion mechanisms: Insights form the relative stability of lipidic structures. In: Bentz J. (Ed). Viral Fusion Mechanisms (1993), CRC Press, Boca Raton, FL. 475-512
    • (1993) Viral Fusion Mechanisms , pp. 475-512
    • Siegel, D.P.1
  • 99
    • 0024582146 scopus 로고
    • Physiological levels of diacylglycerols in phospholipid membranes induce membrane fusion and stabilize inverted phases
    • Siegel D.P., Banschbach J., Alford D., Ellens H., Lis L.J., Quinn P.J., Yeagle P.L., and Bentz J. Physiological levels of diacylglycerols in phospholipid membranes induce membrane fusion and stabilize inverted phases. Biochemistry 28 (1989) 3703-3709
    • (1989) Biochemistry , vol.28 , pp. 3703-3709
    • Siegel, D.P.1    Banschbach, J.2    Alford, D.3    Ellens, H.4    Lis, L.J.5    Quinn, P.J.6    Yeagle, P.L.7    Bentz, J.8
  • 100
    • 0024706764 scopus 로고
    • Intermediates in membrane fusion and bilayer/nonbilayer phase transitions imaged by time-resolved cryo-transmission electron microscopy
    • Siegel D.P., Burns J.L., Chestnut M.H., and Talmon Y. Intermediates in membrane fusion and bilayer/nonbilayer phase transitions imaged by time-resolved cryo-transmission electron microscopy. Biophys. J. 56 (1989) 161-169
    • (1989) Biophys. J. , vol.56 , pp. 161-169
    • Siegel, D.P.1    Burns, J.L.2    Chestnut, M.H.3    Talmon, Y.4
  • 101
    • 0028158758 scopus 로고
    • The mechanism of lamellar-to-inverted hexagonal phase transitions-a study using temperature-jump cryo-electron microscopy
    • Siegel D.P., Green W.J., and Talmon Y. The mechanism of lamellar-to-inverted hexagonal phase transitions-a study using temperature-jump cryo-electron microscopy. Biophys. J. 66 (1994) 402-414
    • (1994) Biophys. J. , vol.66 , pp. 402-414
    • Siegel, D.P.1    Green, W.J.2    Talmon, Y.3
  • 102
    • 0002933416 scopus 로고
    • Cryofixation without pretreatment at ambient pressure
    • Steinbrecht R.A., and Zierold K. (Eds), Springer-Verlag, Berlin
    • Sitte H., Edelmann L., and Neumann K. Cryofixation without pretreatment at ambient pressure. In: Steinbrecht R.A., and Zierold K. (Eds). Cryotechniques in Biological Electron Microscopy (1987), Springer-Verlag, Berlin 87-113
    • (1987) Cryotechniques in Biological Electron Microscopy , pp. 87-113
    • Sitte, H.1    Edelmann, L.2    Neumann, K.3
  • 103
    • 0027517462 scopus 로고
    • A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion
    • Söllner T., Bennett M.K., Whiteheart S.W., Scheller R.H., and 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 (1993) 409-418
    • (1993) Cell , vol.75 , pp. 409-418
    • Söllner, T.1    Bennett, M.K.2    Whiteheart, S.W.3    Scheller, R.H.4    Rothman, J.E.5
  • 104
    • 0019309991 scopus 로고
    • Mechanism of rapid mucus secretion in goblet cells stimulated by acetylcholine
    • Specian R.D., and Neutra M.R. Mechanism of rapid mucus secretion in goblet cells stimulated by acetylcholine. J. Cell Biol. 85 (1980) 626-640
    • (1980) J. Cell Biol. , vol.85 , pp. 626-640
    • Specian, R.D.1    Neutra, M.R.2
  • 105
    • 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. The first milliseconds of the pore formed by a fusogenic viral envelope protein during membrane fusion. Proc. Natl. Acad. Sci. U. S. A. 88 (1991) 3623-3627
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 3623-3627
    • Spruce, A.E.1    Iwata, A.2    Almers, W.3
  • 106
    • 0027488372 scopus 로고
    • Influenza hemagglutinin-mediated membrane fusion does not involve inverted phase lipid intermediates
    • Stegmann T. Influenza hemagglutinin-mediated membrane fusion does not involve inverted phase lipid intermediates. J. Biol. Chem. 268 (1993) 1716-1722
    • (1993) J. Biol. Chem. , vol.268 , pp. 1716-1722
    • Stegmann, T.1
  • 107
    • 0028448430 scopus 로고
    • Membrane fusion: Anchors aweigh
    • Stegmann T. Membrane fusion: Anchors aweigh. Curr. Biol. 4 (1994) 551-554
    • (1994) Curr. Biol. , vol.4 , pp. 551-554
    • Stegmann, T.1
  • 108
    • 0021832341 scopus 로고
    • Kinetics of pH-dependent fusion between influenza virus and liposomes
    • Stegmann T., Hoekstra D., Scherphof G., and Wilschut J. Kinetics of pH-dependent fusion between influenza virus and liposomes. Biochemistry 24 (1985) 3107-3113
    • (1985) Biochemistry , vol.24 , pp. 3107-3113
    • Stegmann, T.1    Hoekstra, D.2    Scherphof, G.3    Wilschut, J.4
  • 110
    • 0025647464 scopus 로고
    • Intermediates in influenza induced membrane fusion
    • Stegmann T., White J.M., and Helenius A. Intermediates in influenza induced membrane fusion. EMBO J. 9 (1990) 4231-4241
    • (1990) EMBO J. , vol.9 , pp. 4231-4241
    • Stegmann, T.1    White, J.M.2    Helenius, A.3
  • 111
    • 0026062948 scopus 로고
    • The HA2 subunit of influenza hemagglutinin inserts into the target membrane prior to fusion
    • Stegmann T., Delfino J.M., Richards F.M., and Helenius A. The HA2 subunit of influenza hemagglutinin inserts into the target membrane prior to fusion. J. Biol. Chem. 266 (1991) 18404-18410
    • (1991) J. Biol. Chem. , vol.266 , pp. 18404-18410
    • Stegmann, T.1    Delfino, J.M.2    Richards, F.M.3    Helenius, A.4
  • 112
    • 0002743936 scopus 로고
    • Freeze-substitution and freeze-drying
    • Steinbrecht R.A., and Zierold K. (Eds), Springer-Verlag, Berlin
    • Steinbrecht R.A., and Müller M. Freeze-substitution and freeze-drying. In: Steinbrecht R.A., and Zierold K. (Eds). Cryotechniques in Biological Electron Microscopy (1987), Springer-Verlag, Berlin 149-172
    • (1987) Cryotechniques in Biological Electron Microscopy , pp. 149-172
    • Steinbrecht, R.A.1    Müller, M.2
  • 113
    • 0025072806 scopus 로고
    • Gramicidin A induced fusion of large unilamellar dioleoylphosphatidylcholine vesicles and its relation to the induction of type II nonbilayer structures
    • Tournois H., Fabrie C.H., Burger K.N.J., Mandersloot J., Hilgers P., van Dalen H., de Gier J., and de Kruijff B. Gramicidin A induced fusion of large unilamellar dioleoylphosphatidylcholine vesicles and its relation to the induction of type II nonbilayer structures. Biochemistry 29 (1990) 8297-8307
    • (1990) Biochemistry , vol.29 , pp. 8297-8307
    • Tournois, H.1    Fabrie, C.H.2    Burger, K.N.J.3    Mandersloot, J.4    Hilgers, P.5    van Dalen, H.6    de Gier, J.7    de Kruijff, B.8
  • 114
    • 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. Membrane flux through the pore formed by a fusogenic viral envelope protein during cell fusion. J. Cell Biol. 121 (1993) 543-552
    • (1993) J. Cell Biol. , vol.121 , pp. 543-552
    • Tse, F.W.1    Iwata, A.2    Almers, W.3
  • 115
    • 0026705651 scopus 로고
    • Lipid interactions of the hemagglutinin HA2 NH2-terminal segment during influenza virusinduced membrane fusion
    • Tsurudome M., Gluck R., Graf R., Falchetto R., Schaller U., and Brunner J. Lipid interactions of the hemagglutinin HA2 NH2-terminal segment during influenza virusinduced membrane fusion. J. Biol. Chem. 267 (1992) 20225-20232
    • (1992) J. Biol. Chem. , vol.267 , pp. 20225-20232
    • Tsurudome, M.1    Gluck, R.2    Graf, R.3    Falchetto, R.4    Schaller, U.5    Brunner, J.6
  • 116
    • 0026337550 scopus 로고
    • Subcellular localization of Forssman glycolipid in epithelial MDCK cells by immunoelectronmicroscopy after freeze-substitution
    • van Genderen I.L., van Meer G., Slot J.W., Geuze H.J., and Voorhout W.F. Subcellular localization of Forssman glycolipid in epithelial MDCK cells by immunoelectronmicroscopy after freeze-substitution. J. Cell Biol. 115 (1991) 1009-1019
    • (1991) J. Cell Biol. , vol.115 , pp. 1009-1019
    • van Genderen, I.L.1    van Meer, G.2    Slot, J.W.3    Geuze, H.J.4    Voorhout, W.F.5
  • 117
    • 78651164594 scopus 로고
    • Electron microscopy after rapid freezing on a metal surface and substitution fixation
    • Van Harreveld A., and Crowell J. Electron microscopy after rapid freezing on a metal surface and substitution fixation. Anat. Rec. 149 (1964) 381-386
    • (1964) Anat. Rec. , vol.149 , pp. 381-386
    • Van Harreveld, A.1    Crowell, J.2
  • 118
    • 0020339953 scopus 로고
    • Viruses budding from either the apical or the basolateral plasma membrane domain of MDCK cells have unique phospholipid compositions
    • van Meer G., and Simons K. Viruses budding from either the apical or the basolateral plasma membrane domain of MDCK cells have unique phospholipid compositions. EMBO J. 7 (1982) 847-852
    • (1982) EMBO J. , vol.7 , pp. 847-852
    • van Meer, G.1    Simons, K.2
  • 119
    • 0022258785 scopus 로고
    • Parameters affecting low-pH-mediated fusion of liposomes with the plasma membrane of cells infected with influenza virus
    • van Meer G., Davoust J., and Simons K. Parameters affecting low-pH-mediated fusion of liposomes with the plasma membrane of cells infected with influenza virus. Biochemistry 24 (1985) 3593-3602
    • (1985) Biochemistry , vol.24 , pp. 3593-3602
    • van Meer, G.1    Davoust, J.2    Simons, K.3
  • 120
    • 0019885231 scopus 로고
    • Analysis of the hexagonal HII phase and its relation to lipidic particles and the lamellar phase. A freeze-fracture study
    • van Venetië R., and Verkleij A.J. Analysis of the hexagonal HII phase and its relation to lipidic particles and the lamellar phase. A freeze-fracture study. Biochim. Biophys. Acta 645 (1981) 262-269
    • (1981) Biochim. Biophys. Acta , vol.645 , pp. 262-269
    • van Venetië, R.1    Verkleij, A.J.2
  • 121
    • 0019619298 scopus 로고
    • Propane jet-freezing: A valid ultra-rapid freezing method for preservation of temperature-dependent lipid phases
    • van Venetië R., Hage W.J., Bluemink J.G., and Verkleij A.J. Propane jet-freezing: A valid ultra-rapid freezing method for preservation of temperature-dependent lipid phases. J. Micros. 123 (1981) 287-292
    • (1981) J. Micros. , vol.123 , pp. 287-292
    • van Venetië, R.1    Hage, W.J.2    Bluemink, J.G.3    Verkleij, A.J.4
  • 122
    • 0021771603 scopus 로고
    • Lipidic intramembranous particles
    • Verkleij A.J. Lipidic intramembranous particles. Biochim. Biophys. Acta 779 (1984) 43-63
    • (1984) Biochim. Biophys. Acta , vol.779 , pp. 43-63
    • Verkleij, A.J.1
  • 125
    • 4243496283 scopus 로고
    • "Lipidic particle" systems as visualized by thin-section electron microscopy
    • Verkleij A.J., Humbel B., Studer D., and Müller M. "Lipidic particle" systems as visualized by thin-section electron microscopy. Biochim. Biophys. Acta 812 (1985) 591-594
    • (1985) Biochim. Biophys. Acta , vol.812 , pp. 591-594
    • Verkleij, A.J.1    Humbel, B.2    Studer, D.3    Müller, M.4
  • 126
    • 0027441876 scopus 로고
    • Lysophosphatidylcholine reversibly arrests exocytosis and viral fusion at a stage between triggering and membrane merger
    • Vogel S.S., Leikina E.A., and Chernomordik L.V. Lysophosphatidylcholine reversibly arrests exocytosis and viral fusion at a stage between triggering and membrane merger. J. Biol. Chem. 268 (1993) 25764-25768
    • (1993) J. Biol. Chem. , vol.268 , pp. 25764-25768
    • Vogel, S.S.1    Leikina, E.A.2    Chernomordik, L.V.3
  • 127
    • 0020661615 scopus 로고
    • Extraction of membrane lipids during fixation, dehydration and embedding of Acholeplasmu laidluwii cells for electron microscopy
    • Weibull C., Christiansson A., and Carlemalm E. Extraction of membrane lipids during fixation, dehydration and embedding of Acholeplasmu laidluwii cells for electron microscopy. J. Micros. 129 (1983) 201-207
    • (1983) J. Micros. , vol.129 , pp. 201-207
    • Weibull, C.1    Christiansson, A.2    Carlemalm, E.3
  • 128
    • 84985204958 scopus 로고
    • Extraction of lipids during freezesubstitution of Acholeplasma laidlawii cells for electron microscopy
    • Weibull C., Villiger W., and Carlemalm E. Extraction of lipids during freezesubstitution of Acholeplasma laidlawii cells for electron microscopy. J. Micros. Oxford. 134 (1984) 213-216
    • (1984) J. Micros. Oxford. , vol.134 , pp. 213-216
    • Weibull, C.1    Villiger, W.2    Carlemalm, E.3
  • 129
    • 0026492542 scopus 로고
    • Membrane fusion
    • White J.M. Membrane fusion. Science 258 (1992) 917-924
    • (1992) Science , vol.258 , pp. 917-924
    • White, J.M.1
  • 130
    • 0023574003 scopus 로고
    • Anti-peptide antibodies detect steps in a protein conformational change: Low-pH activation of the influenza virus hemagglutinin
    • White J.M., and Wilson I.A. Anti-peptide antibodies detect steps in a protein conformational change: Low-pH activation of the influenza virus hemagglutinin. J. Cell Biol. 105 (1987) 2887-2896
    • (1987) J. Cell Biol. , vol.105 , pp. 2887-2896
    • White, J.M.1    Wilson, I.A.2
  • 131
    • 0020338520 scopus 로고
    • Membrane fusion activity of influenza virus
    • White J., Kartenbeck J., and Helenius A. Membrane fusion activity of influenza virus. EMBO J. 1 (1982) 217-222
    • (1982) EMBO J. , vol.1 , pp. 217-222
    • White, J.1    Kartenbeck, J.2    Helenius, A.3
  • 132
    • 0000385225 scopus 로고
    • Membrane fusion: From liposomes to biological membranes
    • Wilschut J., and Hoekstra D. Membrane fusion: From liposomes to biological membranes. Trends Biochem. Sci. 11 (1984) 479-483
    • (1984) Trends Biochem. Sci. , vol.11 , pp. 479-483
    • Wilschut, J.1    Hoekstra, D.2
  • 133
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution
    • Wilson I.A., Skehel J.J., and Wiley D.S. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution. Nature (London) 289 (1981) 366-373
    • (1981) Nature (London) , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.S.3
  • 134
    • 0028271679 scopus 로고
    • Inhibition of membrane fusion by lysophosphatidylcholine
    • Yeagle P.L., Smith F.T., Young J.E., and Flanagan T.D. Inhibition of membrane fusion by lysophosphatidylcholine. Biochemistry 33 (1994) 1820-1827
    • (1994) Biochemistry , vol.33 , pp. 1820-1827
    • Yeagle, P.L.1    Smith, F.T.2    Young, J.E.3    Flanagan, T.D.4
  • 135
    • 0005521375 scopus 로고
    • Simultaneous electrical and optical measurements show that membrane fusion precedes secretory granule swelling during exocytosis of beige mouse mast cells
    • Zimmerberg J., Curran M., Cohen F.S., and Brodwick M. Simultaneous electrical and optical measurements show that membrane fusion precedes secretory granule swelling during exocytosis of beige mouse mast cells. Proc. Natl. Acad. Sci. U. S. A. 84 (1987) 1585-1589
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 1585-1589
    • Zimmerberg, J.1    Curran, M.2    Cohen, F.S.3    Brodwick, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.