메뉴 건너뛰기




Volumn 131, Issue 5, 2008, Pages 503-513

Cholesterol promotes hemifusion and pore widening in membrane fusion induced by influenza hemagglutinin

Author keywords

[No Author keywords available]

Indexed keywords

CHOLESTEROL; HEMAGGLUTININ; MEMBRANE LIPID; OLEIC ACID;

EID: 42949150297     PISSN: 00221295     EISSN: 00221295     Source Type: Journal    
DOI: 10.1085/jgp.200709932     Document Type: Article
Times cited : (64)

References (73)
  • 1
    • 0034676041 scopus 로고    scopus 로고
    • The transmembrane domain of influenza hemagglutinin exhibits a stringent length requirement to support the hemifusion to fusion transition
    • Armstrong, R.T., A.S. Kushnir, and J.M. White. 2000. The transmembrane domain of influenza hemagglutinin exhibits a stringent length requirement to support the hemifusion to fusion transition. J. Cell Biol. 151:425-437.
    • (2000) J. Cell Biol , vol.151 , pp. 425-437
    • Armstrong, R.T.1    Kushnir, A.S.2    White, J.M.3
  • 2
    • 0037320081 scopus 로고    scopus 로고
    • The coxsackie B virus and adenovirus receptor resides in a distinct membrane microdomain
    • Ashbourne Excoffon, K.J., T. Moninger, and J. Zabner. 2003. The coxsackie B virus and adenovirus receptor resides in a distinct membrane microdomain. J. Virol. 77:2559-2567.
    • (2003) J. Virol , vol.77 , pp. 2559-2567
    • Ashbourne Excoffon, K.J.1    Moninger, T.2    Zabner, J.3
  • 4
    • 0019075644 scopus 로고
    • Intermolecular hydrogen bonding between lipids: Influence on organization and function of lipids in membranes
    • Boggs, J.M. 1980. Intermolecular hydrogen bonding between lipids: influence on organization and function of lipids in membranes. Can. J. Biochem. 58:755-770.
    • (1980) Can. J. Biochem , vol.58 , pp. 755-770
    • Boggs, J.M.1
  • 5
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown, D.A., and E. London. 1998. Functions of lipid rafts in biological membranes. Annu. Rev. Cell Dev. Biol. 14:111-136.
    • (1998) Annu. Rev. Cell Dev. Biol , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 6
    • 0038314400 scopus 로고    scopus 로고
    • Virus entry, assembly, budding, and membrane rafts
    • 226-237
    • Chazal, N., and D. Gerlier. 2003. Virus entry, assembly, budding, and membrane rafts. Microbiol. Mol. Biol. Rev. 67(2):226-237.
    • (2003) Microbiol. Mol. Biol. Rev , vol.67 , Issue.2
    • Chazal, N.1    Gerlier, D.2
  • 7
    • 0030586161 scopus 로고    scopus 로고
    • Non-bilayer lipids and biological fusion intermediates
    • Chernomordik, L. 1996. Non-bilayer lipids and biological fusion intermediates. Chem. Phys. Lipids. 81:203-213.
    • (1996) Chem. Phys. Lipids , vol.81 , pp. 203-213
    • Chernomordik, L.1
  • 8
    • 0031012628 scopus 로고    scopus 로고
    • An early stage of membrane fusion mediated by the low pH conformation of influenza hemagglutinin depends upon membrane lipids
    • Chernomordik, L., E. Leikina, V. Frolov, P. Bronk, and J. Zimmerberg. 1997. An early stage of membrane fusion mediated by the low pH conformation of influenza hemagglutinin depends upon membrane lipids. J. Cell Biol. 136:81-93.
    • (1997) J. Cell Biol , vol.136 , pp. 81-93
    • Chernomordik, L.1    Leikina, E.2    Frolov, V.3    Bronk, P.4    Zimmerberg, J.5
  • 9
    • 0032559801 scopus 로고    scopus 로고
    • The pathway of membrane fusion catalyzed by influenza hemagglutinin: Restriction of lipids, hemifusion, and lipidic fusion pore formation
    • Chernomordik L, V.A. Frolov, E. Leikina, P. Bronk, and J. Zimmerberg. 1998. The pathway of membrane fusion catalyzed by influenza hemagglutinin: restriction of lipids, hemifusion, and lipidic fusion pore formation. J. Cell Biol. 140:1369-1382.
    • (1998) J. Cell Biol , vol.140 , pp. 1369-1382
    • Chernomordik, L.1    Frolov, V.A.2    Leikina, E.3    Bronk, P.4    Zimmerberg, J.5
  • 10
    • 0028845658 scopus 로고
    • Membrane mechanics can account for fusion pore dilation in stages
    • Chizmadzhev, Y.A., F.S. Cohen, A. Shcherbakov, and J. Zimmerberg. 1995. Membrane mechanics can account for fusion pore dilation in stages. Biophys. J. 69(6):2489-2500.
    • (1995) Biophys. J , vol.69 , Issue.6 , pp. 2489-2500
    • Chizmadzhev, Y.A.1    Cohen, F.S.2    Shcherbakov, A.3    Zimmerberg, J.4
  • 11
    • 0030695849 scopus 로고    scopus 로고
    • Use of cyclodextrin for manipulating cellular cholesterol content
    • Christian, A.E., M.P. Haynes, M.C. Phillips, and G.H. Rothblat. 1997. Use of cyclodextrin for manipulating cellular cholesterol content. J. Lipid Res. 38:2264-2272.
    • (1997) J. Lipid Res , vol.38 , pp. 2264-2272
    • Christian, A.E.1    Haynes, M.P.2    Phillips, M.C.3    Rothblat, G.H.4
  • 14
    • 0018797519 scopus 로고
    • Lipid polymorphism and the functional roles of lipids in biological membranes
    • Cullis, P.R., and B. de Kruijff. 1979. Lipid polymorphism and the functional roles of lipids in biological membranes. Biochim. Biophys. Acta. 559:399-420.
    • (1979) Biochim. Biophys. Acta , vol.559 , pp. 399-420
    • Cullis, P.R.1    de Kruijff, B.2
  • 15
    • 0029898564 scopus 로고    scopus 로고
    • Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers
    • Danieli, T., S.L. Pelletier, Y.I. Henis, and J.M. White. 1996. Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers. J. Cell Biol. 133:559-569.
    • (1996) J. Cell Biol , vol.133 , pp. 559-569
    • Danieli, T.1    Pelletier, S.L.2    Henis, Y.I.3    White, J.M.4
  • 17
    • 0037959071 scopus 로고    scopus 로고
    • The state of lipid rafts: From model membranes to cells
    • Edidin, M. 2003. The state of lipid rafts: from model membranes to cells. Annu. Rev. Biophys. Biomol. Struct. 32:257-283.
    • (2003) Annu. Rev. Biophys. Biomol. Struct , vol.32 , pp. 257-283
    • Edidin, M.1
  • 18
    • 0024387465 scopus 로고
    • Delivery of macromolecules into cells expressing a viral membrane fusion protein
    • Ellens, H., S. Doxsey, J.S. Glenn, and J.M. White. 1989. Delivery of macromolecules into cells expressing a viral membrane fusion protein. Methods Cell Biol. 31:155-178.
    • (1989) Methods Cell Biol , vol.31 , pp. 155-178
    • Ellens, H.1    Doxsey, S.2    Glenn, J.S.3    White, J.M.4
  • 19
    • 0035016931 scopus 로고    scopus 로고
    • Ternary phase diagram of dipalmitoyl-PC/dilauroyl-PC/cholesterol: Nanoscopic domain formation driven by cholesterol
    • Feigenson, G.W., and J.T. Buboltz. 2001. Ternary phase diagram of dipalmitoyl-PC/dilauroyl-PC/cholesterol: nanoscopic domain formation driven by cholesterol. Biophys. J. 80:2775-2788.
    • (2001) Biophys. J , vol.80 , pp. 2775-2788
    • Feigenson, G.W.1    Buboltz, J.T.2
  • 20
    • 0033594934 scopus 로고    scopus 로고
    • Quantitative analysis of phospholipids in functionally important membrane domains from RBL-2H3 mast cells using tandem high-resolution mass spectrometry
    • Fridriksson, E.K., P.A. Shipkova, E.D. Sheets, D. Holowka, B. Baird, and F.W. McLafferty. 1999. Quantitative analysis of phospholipids in functionally important membrane domains from RBL-2H3 mast cells using tandem high-resolution mass spectrometry. Biochemistry. 38:8056-8063.
    • (1999) Biochemistry , vol.38 , pp. 8056-8063
    • Fridriksson, E.K.1    Shipkova, P.A.2    Sheets, E.D.3    Holowka, D.4    Baird, B.5    McLafferty, F.W.6
  • 21
    • 0034252335 scopus 로고    scopus 로고
    • Multiple local contact sites are induced by GPI-linked influenza hemagglutinin during hemifusion and flickering pore formation
    • Frolov, V.A., M.S. Cho, P. Bronk, T.S. Reese, and J. Zimmerberg. 2000. Multiple local contact sites are induced by GPI-linked influenza hemagglutinin during hemifusion and flickering pore formation. Traffic. 1:622-630.
    • (2000) Traffic , vol.1 , pp. 622-630
    • Frolov, V.A.1    Cho, M.S.2    Bronk, P.3    Reese, T.S.4    Zimmerberg, J.5
  • 22
    • 0042631498 scopus 로고    scopus 로고
    • Membrane permeability changes at early stages of influenza hemagglutinin-mediated fusion
    • Frolov, V.A., A.Y. Dunina-Barkovskaya, A.V. Samsonov, and J. Zimmerberg. 2003. Membrane permeability changes at early stages of influenza hemagglutinin-mediated fusion. Biophys. J. 85(3):1725-1733.
    • (2003) Biophys. J , vol.85 , Issue.3 , pp. 1725-1733
    • Frolov, V.A.1    Dunina-Barkovskaya, A.Y.2    Samsonov, A.V.3    Zimmerberg, J.4
  • 23
    • 0028879530 scopus 로고
    • Expression of the human oxytocin receptor in baculovirus-infected insect cells: High-affinity binding is induced by a cholesterolcyclodextrin complex
    • Gimpl, G., U. Klein, H. Reiländer, and F. Fahrenholz. 1995. Expression of the human oxytocin receptor in baculovirus-infected insect cells: high-affinity binding is induced by a cholesterolcyclodextrin complex. Biochemistry. 34:13794-13801.
    • (1995) Biochemistry , vol.34 , pp. 13794-13801
    • Gimpl, G.1    Klein, U.2    Reiländer, H.3    Fahrenholz, F.4
  • 24
    • 0036786465 scopus 로고    scopus 로고
    • Role for human immunodeficiency virus type 1 membrane cholesterol in viral internalization
    • Guyader, M., E. Kiyokawa, L. Abrami, P. Turelli, and D. Trono. 2002. Role for human immunodeficiency virus type 1 membrane cholesterol in viral internalization. J. Virol. 76:10356-10364.
    • (2002) J. Virol , vol.76 , pp. 10356-10364
    • Guyader, M.1    Kiyokawa, E.2    Abrami, L.3    Turelli, P.4    Trono, D.5
  • 25
    • 0035836511 scopus 로고    scopus 로고
    • Influence of lipid composition on physical properties and peg-mediated fusion of curved and uncurved model membrane vesicles: "nature's own" fusogenic lipid bilayer
    • Haque, M.E., T.J. McIntosh, and B.R. Lentz. 2001. Influence of lipid composition on physical properties and peg-mediated fusion of curved and uncurved model membrane vesicles: "nature's own" fusogenic lipid bilayer. Biochemistry. 40:4340-4348.
    • (2001) Biochemistry , vol.40 , pp. 4340-4348
    • Haque, M.E.1    McIntosh, T.J.2    Lentz, B.R.3
  • 26
    • 0031750335 scopus 로고    scopus 로고
    • Lipid domain structure of the plasma membrane revealed by patching of membrane components
    • Harder, T., P. Scheiffele, P. Verkade, and K. Simons. 1998. Lipid domain structure of the plasma membrane revealed by patching of membrane components. J. Cell Biol. 141:929-942.
    • (1998) J. Cell Biol , vol.141 , pp. 929-942
    • Harder, T.1    Scheiffele, P.2    Verkade, P.3    Simons, K.4
  • 27
    • 22344442585 scopus 로고    scopus 로고
    • Quantitative electron microscopy and fluorescence spectroscopy of the membrane distribution of influenza hemagglutinin
    • Hess, S.T., M. Kumar, A. Verma, J. Farrington, A. Kenworthy, and J. Zimmerberg. 2005. Quantitative electron microscopy and fluorescence spectroscopy of the membrane distribution of influenza hemagglutinin. J. Cell Biol. 169:965-976.
    • (2005) J. Cell Biol , vol.169 , pp. 965-976
    • Hess, S.T.1    Kumar, M.2    Verma, A.3    Farrington, J.4    Kenworthy, A.5    Zimmerberg, J.6
  • 28
    • 36849053761 scopus 로고    scopus 로고
    • Dynamic clustered distribution of hemagglutinin resolved at 40 nm in living cell membranes discriminates between raft theories
    • Hess, S.T., T.J. Gould, M.V. Gudheti, S.A. Maas, K.D. Mills, and J. Zimmerberg. 2007. Dynamic clustered distribution of hemagglutinin resolved at 40 nm in living cell membranes discriminates between raft theories. Proc. Natl. Acad. Sci. USA. 104:17370-17375.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 17370-17375
    • Hess, S.T.1    Gould, T.J.2    Gudheti, M.V.3    Maas, S.A.4    Mills, K.D.5    Zimmerberg, J.6
  • 29
    • 0033065591 scopus 로고    scopus 로고
    • A microscopic interaction model of maximum solubility of cholesterol in lipid bilayers
    • Huang, J., and G.W. Feigenson. 1999. A microscopic interaction model of maximum solubility of cholesterol in lipid bilayers. Biophys. J. 76:2142-2157.
    • (1999) Biophys. J , vol.76 , pp. 2142-2157
    • Huang, J.1    Feigenson, G.W.2
  • 30
    • 0032559854 scopus 로고    scopus 로고
    • Cholesterol is required for surface transport of influenza virus hemagglutinin
    • Keller, P., and K. Simons. 1998. Cholesterol is required for surface transport of influenza virus hemagglutinin. J. Cell Biol. 140:1357-1367.
    • (1998) J. Cell Biol , vol.140 , pp. 1357-1367
    • Keller, P.1    Simons, K.2
  • 31
    • 0028179011 scopus 로고
    • Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion
    • Kemble, G.W., T. Danieli, and J.M. White. 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
  • 32
    • 0034075971 scopus 로고    scopus 로고
    • High-resolution FRET microscopy of cholera toxin B-subunit and GPI-anchored proteins in cell plasma membranes
    • Kenworthy, A.K., N. Petranova, and M. Edidin. 2000. High-resolution FRET microscopy of cholera toxin B-subunit and GPI-anchored proteins in cell plasma membranes. Mol. Biol. Cell. 11:1645-1655.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1645-1655
    • Kenworthy, A.K.1    Petranova, N.2    Edidin, M.3
  • 33
    • 0021177971 scopus 로고
    • Role of cholesterol in fusion of Semliki forest virus with membranes
    • Kielian, M.C., and A. Helenius. 1984. Role of cholesterol in fusion of Semliki forest virus with membranes. J. Virol. 52:281-283.
    • (1984) J. Virol , vol.52 , pp. 281-283
    • Kielian, M.C.1    Helenius, A.2
  • 34
    • 0036148171 scopus 로고    scopus 로고
    • Segregation of CD4 and CXCR4 into distinct lipid microdomains in T lymphocytes suggests a mechanism for membrane destabilization by human immunodeficiency virus
    • Kozak, S.L., J.M. Heard, and D. Kabat. 2002. Segregation of CD4 and CXCR4 into distinct lipid microdomains in T lymphocytes suggests a mechanism for membrane destabilization by human immunodeficiency virus. J. Virol. 76:1802-1815.
    • (2002) J. Virol , vol.76 , pp. 1802-1815
    • Kozak, S.L.1    Heard, J.M.2    Kabat, D.3
  • 36
    • 0037974484 scopus 로고    scopus 로고
    • Membrane fission: Model for intermediate structures
    • Kozlovsky, Y., and M.M. Kozlov. 2003. Membrane fission: model for intermediate structures. Biophys. J. 85:85-96.
    • (2003) Biophys. J , vol.85 , pp. 85-96
    • Kozlovsky, Y.1    Kozlov, M.M.2
  • 37
    • 0029186072 scopus 로고
    • Baculovirus expression protocols
    • C.D. Richardson, editor. Humana Press, New Jersey
    • Kretzschmar, E., K. Kuroda, and H.D. Klenk. 1995. Baculovirus expression protocols. In Methods in Molecular Biology. Vol. 39. C.D. Richardson, editor. Humana Press, New Jersey. 317-336.
    • (1995) Methods in Molecular Biology , vol.39 , pp. 317-336
    • Kretzschmar, E.1    Kuroda, K.2    Klenk, H.D.3
  • 39
    • 0034972583 scopus 로고    scopus 로고
    • Formation of wild-type and chimeric influenza virus-like particles following simultaneous expression of only four structural proteins
    • Latham, T., and J.M. Galarza. 2001. Formation of wild-type and chimeric influenza virus-like particles following simultaneous expression of only four structural proteins. J. Virol. 75:6154-6165.
    • (2001) J. Virol , vol.75 , pp. 6154-6165
    • Latham, T.1    Galarza, J.M.2
  • 40
    • 0032514155 scopus 로고    scopus 로고
    • Mutations in the middle of the transmembrane domain reverse the polarity of transport of the influenza virus hemagglutinin in MDCK epithelial cells
    • Lin, S., H. Y. Naim, C. Rodriguez, and M. Roth. 1998. Mutations in the middle of the transmembrane domain reverse the polarity of transport of the influenza virus hemagglutinin in MDCK epithelial cells. J. Cell Biol. 142:51-57.
    • (1998) J. Cell Biol , vol.142 , pp. 51-57
    • Lin, S.1    Naim, H.Y.2    Rodriguez, C.3    Roth, M.4
  • 41
    • 0344820768 scopus 로고    scopus 로고
    • Lipid composition of Spodoptera frugiperda (Sf9) and Trichopulsia ni (Tn) insect cells used for baculovirus infection
    • Marheineke, K., S. Grünewald, W. Christie, and H. Reiländer. 1998. Lipid composition of Spodoptera frugiperda (Sf9) and Trichopulsia ni (Tn) insect cells used for baculovirus infection. FEBS Lett. 441:49-52.
    • (1998) FEBS Lett , vol.441 , pp. 49-52
    • Marheineke, K.1    Grünewald, S.2    Christie, W.3    Reiländer, H.4
  • 43
    • 0034037991 scopus 로고    scopus 로고
    • The lipid-anchored ectodomain of influenza virus hemagglutinin (GPIHA) is capable of inducing nonenlarging fusion pores
    • Markosyan, R.M., F.S. Cohen, and G.B. Melikyan. 2000. The lipid-anchored ectodomain of influenza virus hemagglutinin (GPIHA) is capable of inducing nonenlarging fusion pores. Mol. Biol. Cell. 11:1143-1152.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1143-1152
    • Markosyan, R.M.1    Cohen, F.S.2    Melikyan, G.B.3
  • 44
    • 0029837381 scopus 로고    scopus 로고
    • Degradation of 3-hydroxy-3-methylglutaryl-CoA reductase in endoplasmic reticulum membranes is accelerated as a result of increased susceptibility to proteolysis
    • McGee, T.P., H.H. Cheng, H. Kumagai, S. Omura, and R.D. Simoni. 1996. Degradation of 3-hydroxy-3-methylglutaryl-CoA reductase in endoplasmic reticulum membranes is accelerated as a result of increased susceptibility to proteolysis. J. Biol. Chem. 271:25630-25638.
    • (1996) J. Biol. Chem , vol.271 , pp. 25630-25638
    • McGee, T.P.1    Cheng, H.H.2    Kumagai, H.3    Omura, S.4    Simoni, R.D.5
  • 45
    • 0028838681 scopus 로고
    • Comparison of transient and successful fusion pores connecting influenza hemagglutinin expressing cells to planar membranes
    • Melikyan, G.B., W.D. Niles, V.A. Ratinov, M. Karhanek, J. Zimmerberg, and F.S. Cohen. 1995. Comparison of transient and successful fusion pores connecting influenza hemagglutinin expressing cells to planar membranes. J. Gen. Physiol. 106:803-819.
    • (1995) J. Gen. Physiol , vol.106 , pp. 803-819
    • Melikyan, G.B.1    Niles, W.D.2    Ratinov, V.A.3    Karhanek, M.4    Zimmerberg, J.5    Cohen, F.S.6
  • 46
    • 0028865392 scopus 로고    scopus 로고
    • GPI-anchored influenza hemagglutinin induces hemifusion to both red blood cell and planar bilayer membranes
    • Melikyan, G.B., J.M. White, and F.S. Cohen. 2000. GPI-anchored influenza hemagglutinin induces hemifusion to both red blood cell and planar bilayer membranes. J. Cell Biol. 131:679-691.
    • (2000) J. Cell Biol , vol.131 , pp. 679-691
    • Melikyan, G.B.1    White, J.M.2    Cohen, F.S.3
  • 47
    • 0028199032 scopus 로고
    • Membrane fusion of Semliki Forest virus requires sphingolipids in the target membrane
    • Nieva, J.L., R. Bron, J. Corver, and J. Wilschut. 1994. Membrane fusion of Semliki Forest virus requires sphingolipids in the target membrane. EMBO J. 13:2797-2804.
    • (1994) EMBO J , vol.13 , pp. 2797-2804
    • Nieva, J.L.1    Bron, R.2    Corver, J.3    Wilschut, J.4
  • 48
    • 0035923525 scopus 로고    scopus 로고
    • Plasma membrane rafts play a critical role in HIV-1 assembly and release
    • Ono, A., and E.O. Freed. 2001. Plasma membrane rafts play a critical role in HIV-1 assembly and release. Proc. Natl. Acad. Sci. USA. 98:13925-13930.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 13925-13930
    • Ono, A.1    Freed, E.O.2
  • 49
    • 0026022952 scopus 로고
    • Cholesterol is required for infection by Semliki Forest virus
    • Phalen, T., and M. Kielian. 1991. Cholesterol is required for infection by Semliki Forest virus. J. Cell Biol. 112:615-623.
    • (1991) J. Cell Biol , vol.112 , pp. 615-623
    • Phalen, T.1    Kielian, M.2
  • 50
    • 0030472394 scopus 로고    scopus 로고
    • The initial fusion pore induced by baculovirus GP64 is large and forms quickly
    • Plonsky, I., and J. Zimmerberg. 1996. The initial fusion pore induced by baculovirus GP64 is large and forms quickly. J. Cell Biol. 135:1831-1839.
    • (1996) J. Cell Biol , vol.135 , pp. 1831-1839
    • Plonsky, I.1    Zimmerberg, J.2
  • 51
    • 42949085300 scopus 로고    scopus 로고
    • Initial size and dynamics of viral fusion pores are a function of the fusion protein mediating membrane fusion
    • Jan. 22 Epub ahead of print, doi:10.1042/BC20070040
    • Plonsky, I., D.H. Kingsley, A. Rashtian, P.S. Blank, and J. Zimmerberg. 2008. Initial size and dynamics of viral fusion pores are a function of the fusion protein mediating membrane fusion. Biol. Cell. Jan. 22 (Epub ahead of print). doi:10.1042/BC20070040.
    • (2008) Biol. Cell
    • Plonsky, I.1    Kingsley, D.H.2    Rashtian, A.3    Blank, P.S.4    Zimmerberg, J.5
  • 52
    • 40949088194 scopus 로고    scopus 로고
    • Progressive ordering with decreasing temperature of the phospholipids of influenza virus
    • Polozov, I. V., L. Bezrukov, K. Gawrisch, and J. Zimmerberg. 2008. Progressive ordering with decreasing temperature of the phospholipids of influenza virus. Nat. Chem. Biol. 4:248-255.
    • (2008) Nat. Chem. Biol , vol.4 , pp. 248-255
    • Polozov, I.V.1    Bezrukov, L.2    Gawrisch, K.3    Zimmerberg, J.4
  • 54
    • 0031954979 scopus 로고    scopus 로고
    • Fusion pore conductance: Experimental approaches and theoretical algorithms
    • Ratinov, V., I. Plonsky, and J. Zimmerberg. 1998. Fusion pore conductance: experimental approaches and theoretical algorithms. Biophys. J. 74:2374-2387.
    • (1998) Biophys. J , vol.74 , pp. 2374-2387
    • Ratinov, V.1    Plonsky, I.2    Zimmerberg, J.3
  • 55
    • 0034619518 scopus 로고    scopus 로고
    • Sterol and sphingolipids strongly affects the growth of fusion pores induced by the hemagglutinin of influenza virus
    • Raznikov, V.I., and F.S. Cohen. 2000. Sterol and sphingolipids strongly affects the growth of fusion pores induced by the hemagglutinin of influenza virus. Biochemistry. 39:13462-13468.
    • (2000) Biochemistry , vol.39 , pp. 13462-13468
    • Raznikov, V.I.1    Cohen, F.S.2
  • 56
    • 0032480012 scopus 로고    scopus 로고
    • 2+ and protein kinase C via distinct mechanisms
    • 2+ and protein kinase C via distinct mechanisms. EMBO J. 17:4340-4345.
    • (1998) EMBO J , vol.17 , pp. 4340-4345
    • Scepek, S.1    Coorssen, J.R.2    Lindau, M.3
  • 57
    • 0030804183 scopus 로고    scopus 로고
    • Interaction of influenza virus haemagglutinin with sphingolipid-cholesterol membrane domains via its transmembrane domain
    • Scheiffele, P., M.G. Roth, and K. Simons. 1997. Interaction of influenza virus haemagglutinin with sphingolipid-cholesterol membrane domains via its transmembrane domain. EMBO J. 16:5501-5508.
    • (1997) EMBO J , vol.16 , pp. 5501-5508
    • Scheiffele, P.1    Roth, M.G.2    Simons, K.3
  • 58
    • 0033593321 scopus 로고    scopus 로고
    • Influenza viruses select ordered lipid domains during budding from the plasma membrane
    • Scheiffele, P., A. Rietveld, T. Wilk, and K. Simons. 1999. Influenza viruses select ordered lipid domains during budding from the plasma membrane. J. Biol. Chem. 274:2038-2044.
    • (1999) J. Biol. Chem , vol.274 , pp. 2038-2044
    • Scheiffele, P.1    Rietveld, A.2    Wilk, T.3    Simons, K.4
  • 59
    • 2442690486 scopus 로고    scopus 로고
    • Escaping from the cell: Assembly and budding of negative-strand RNA viruses
    • Schmitt, A.P., and R.A. Lamb. 2004. Escaping from the cell: assembly and budding of negative-strand RNA viruses. Curr. Top. Microbiol. Immunol. 283:145-196.
    • (2004) Curr. Top. Microbiol. Immunol , vol.283 , pp. 145-196
    • Schmitt, A.P.1    Lamb, R.A.2
  • 60
    • 0017378125 scopus 로고
    • A nuclear magnetic resonance study of sphingomyelin in bilayer systems
    • Schmidt, C.F., Y. Barenholz, and T.E. Thompson. 1977. A nuclear magnetic resonance study of sphingomyelin in bilayer systems. Biochemistry. 16:2649-2656.
    • (1977) Biochemistry , vol.16 , pp. 2649-2656
    • Schmidt, C.F.1    Barenholz, Y.2    Thompson, T.E.3
  • 61
    • 0032926928 scopus 로고    scopus 로고
    • The modified stalk mechanism of lamellar/inverted phase transitions and its implications for membrane fusion
    • Siegel, D.P. 1999. The modified stalk mechanism of lamellar/inverted phase transitions and its implications for membrane fusion. Biophys. J. 76:291-313.
    • (1999) Biophys. J , vol.76 , pp. 291-313
    • Siegel, D.P.1
  • 62
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons, K., and E. Ikonen. 1997. Functional rafts in cell membranes. Nature. 387:569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 63
    • 0024331657 scopus 로고
    • Patch clamp studies of single cell-fusion events mediated by a viral protein
    • Spruce, A.E., A. Iwata, J.M. White, and W. Almers. 1989. Patch clamp studies of single cell-fusion events mediated by a viral 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
  • 64
    • 0036721021 scopus 로고    scopus 로고
    • A novel cell entry pathway for a DAF-using human enterovirus is dependent on lipid rafts
    • Stuart, A.D., H.E. Eustace, T.A. McKee, and T.D. Brown. 2002. A novel cell entry pathway for a DAF-using human enterovirus is dependent on lipid rafts. J. Virol. 76:9307-9322.
    • (2002) J. Virol , vol.76 , pp. 9307-9322
    • Stuart, A.D.1    Eustace, H.E.2    McKee, T.A.3    Brown, T.D.4
  • 65
    • 0242409482 scopus 로고    scopus 로고
    • Role for influenza virus envelope cholesterol in virus entry and infection
    • Sun, X., and G.R. Whittaker. 2003. Role for influenza virus envelope cholesterol in virus entry and infection. J. Virol. 77:12543-12551.
    • (2003) J. Virol , vol.77 , pp. 12543-12551
    • Sun, X.1    Whittaker, G.R.2
  • 66
    • 0036789014 scopus 로고    scopus 로고
    • Lipid rafts and assembly of enveloped viruses
    • Suomalainen, M. 2002. Lipid rafts and assembly of enveloped viruses. Traffic. 3:705-709.
    • (2002) Traffic , vol.3 , pp. 705-709
    • Suomalainen, M.1
  • 67
    • 0347482478 scopus 로고    scopus 로고
    • Influenza virus hemagglutinin concentrates in lipid raft microdomains for efficient viral fusion
    • Takeda. M., G.P. Leser, C.J. Russell, and R.A. Lamb. 2003. Influenza virus hemagglutinin concentrates in lipid raft microdomains for efficient viral fusion. Proc. Natl. Acad. Sci. USA. 100:14610-14617.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 14610-14617
    • Takeda, M.1    Leser, G.P.2    Russell, C.J.3    Lamb, R.A.4
  • 69
    • 0035980238 scopus 로고    scopus 로고
    • Partitioning of lipidated peptide sequences into liquid-ordered lipid domains in model and biological membranes
    • Wang, T.Y., R. Leventis, and J.R. Silvius. 2001. Partitioning of lipidated peptide sequences into liquid-ordered lipid domains in model and biological membranes. Biochemistry. 40:13031-13040.
    • (2001) Biochemistry , vol.40 , pp. 13031-13040
    • Wang, T.Y.1    Leventis, R.2    Silvius, J.R.3
  • 70
    • 0001696895 scopus 로고
    • pH-dependent fusion between the Semliki Forest virus membrane and liposomes
    • White, J., and A. Helenius. 1980. pH-dependent fusion between the Semliki Forest virus membrane and liposomes. Proc. Natl. Acad. Sci. USA. 77:3273-3277.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 3273-3277
    • White, J.1    Helenius, A.2
  • 71
    • 0033995067 scopus 로고    scopus 로고
    • Influenza virus assembly and lipid raft microdomains: A role for the cytoplasmic tails of the spike glycoproteins
    • Zhang, J., A. Pekosz, and R.A. Lamb. 2000. Influenza virus assembly and lipid raft microdomains: a role for the cytoplasmic tails of the spike glycoproteins. J. Virol. 74:4634-4644.
    • (2000) J. Virol , vol.74 , pp. 4634-4644
    • Zhang, J.1    Pekosz, A.2    Lamb, R.A.3
  • 72
    • 33644846421 scopus 로고    scopus 로고
    • How proteins produce cellular membrane curvature
    • Zimmerberg, J., and M.M. Kozlov. 2006. How proteins produce cellular membrane curvature. Nat. Rev. Mol. Cell Biol. 7:9-19.
    • (2006) Nat. Rev. Mol. Cell Biol , vol.7 , pp. 9-19
    • Zimmerberg, J.1    Kozlov, M.M.2
  • 73
    • 0028587209 scopus 로고
    • Restricted movement of lipid and aqueous dyes through pores formed by influenza hemagglutinin during cell fusion
    • Zimmerberg, J., R. Blumenthal, M. Curran, D. Sarkar, and S. Morris. 1994. Restricted movement of lipid and aqueous dyes through pores formed by influenza hemagglutinin during cell fusion. J. Cell Biol. 127:1885-1894.
    • (1994) J. Cell Biol , vol.127 , pp. 1885-1894
    • Zimmerberg, J.1    Blumenthal, R.2    Curran, M.3    Sarkar, D.4    Morris, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.