메뉴 건너뛰기




Volumn 10, Issue 4, 2014, Pages

IFITM3 Restricts Influenza A Virus Entry by Blocking the Formation of Fusion Pores following Virus-Endosome Hemifusion

Author keywords

[No Author keywords available]

Indexed keywords

CHOLESTEROL; INTERFERON INDUCED TRANSMEMBRANE PROTEIN; MEMBRANE PROTEIN; UNCLASSIFIED DRUG; IFITM3 PROTEIN, HUMAN; RNA BINDING PROTEIN;

EID: 84901337841     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1004048     Document Type: Article
Times cited : (250)

References (58)
  • 1
    • 84871484827 scopus 로고    scopus 로고
    • The broad-spectrum antiviral functions of IFIT and IFITM proteins
    • Diamond MS, Farzan M, (2013) The broad-spectrum antiviral functions of IFIT and IFITM proteins. Nat Rev Immunol 13: 46-57.
    • (2013) Nat Rev Immunol , vol.13 , pp. 46-57
    • Diamond, M.S.1    Farzan, M.2
  • 2
    • 72549116887 scopus 로고    scopus 로고
    • The IFITM proteins mediate cellular resistance to influenza A H1N1 virus, West Nile virus, and dengue virus
    • Brass AL, Huang IC, Benita Y, John SP, Krishnan MN, et al. (2009) The IFITM proteins mediate cellular resistance to influenza A H1N1 virus, West Nile virus, and dengue virus. Cell 139: 1243-1254.
    • (2009) Cell , vol.139 , pp. 1243-1254
    • Brass, A.L.1    Huang, I.C.2    Benita, Y.3    John, S.P.4    Krishnan, M.N.5
  • 3
    • 84888015374 scopus 로고    scopus 로고
    • IFITMs Restrict the Replication of Multiple Pathogenic Viruses
    • doi:10.1016/j.jmb.2013.09.024
    • Perreira JM, Chin CR, Feeley EM, Brass AL, (2013) IFITMs Restrict the Replication of Multiple Pathogenic Viruses. J Mol Biol 425: 4937-55 doi:10.1016/j.jmb.2013.09.024.
    • (2013) J Mol Biol , vol.425 , pp. 4937-4955
    • Perreira, J.M.1    Chin, C.R.2    Feeley, E.M.3    Brass, A.L.4
  • 4
    • 84880599167 scopus 로고    scopus 로고
    • IFITM-2 and IFITM-3 but not IFITM-1 restrict Rift Valley fever virus
    • Mudhasani R, Tran JP, Retterer C, Radoshitzky SR, Kota KP, et al. (2013) IFITM-2 and IFITM-3 but not IFITM-1 restrict Rift Valley fever virus. J Virol 87: 8451-8464.
    • (2013) J Virol , vol.87 , pp. 8451-8464
    • Mudhasani, R.1    Tran, J.P.2    Retterer, C.3    Radoshitzky, S.R.4    Kota, K.P.5
  • 6
    • 79551532447 scopus 로고    scopus 로고
    • Distinct patterns of IFITM-mediated restriction of filoviruses, SARS coronavirus, and influenza A virus
    • Huang IC, Bailey CC, Weyer JL, Radoshitzky SR, Becker MM, et al. (2011) Distinct patterns of IFITM-mediated restriction of filoviruses, SARS coronavirus, and influenza A virus. PLoS Pathog 7: e1001258.
    • (2011) PLoS Pathog , vol.7
    • Huang, I.C.1    Bailey, C.C.2    Weyer, J.L.3    Radoshitzky, S.R.4    Becker, M.M.5
  • 7
    • 77954983994 scopus 로고    scopus 로고
    • Identification of five interferon-induced cellular proteins that inhibit west nile virus and dengue virus infections
    • Jiang D, Weidner JM, Qing M, Pan XB, Guo H, et al. (2010) Identification of five interferon-induced cellular proteins that inhibit west nile virus and dengue virus infections. J Virol 84: 8332-8341.
    • (2010) J Virol , vol.84 , pp. 8332-8341
    • Jiang, D.1    Weidner, J.M.2    Qing, M.3    Pan, X.B.4    Guo, H.5
  • 8
    • 84866930893 scopus 로고    scopus 로고
    • Ifitm3 limits the severity of acute influenza in mice
    • Bailey CC, Huang IC, Kam C, Farzan M, (2012) Ifitm3 limits the severity of acute influenza in mice. PLoS Pathog 8: e1002909.
    • (2012) PLoS Pathog , vol.8
    • Bailey, C.C.1    Huang, I.C.2    Kam, C.3    Farzan, M.4
  • 9
    • 84862777209 scopus 로고    scopus 로고
    • IFITM3 restricts the morbidity and mortality associated with influenza
    • Everitt AR, Clare S, Pertel T, John SP, Wash RS, et al. (2012) IFITM3 restricts the morbidity and mortality associated with influenza. Nature 484: 519-523.
    • (2012) Nature , vol.484 , pp. 519-523
    • Everitt, A.R.1    Clare, S.2    Pertel, T.3    John, S.P.4    Wash, R.S.5
  • 10
    • 84894247386 scopus 로고    scopus 로고
    • Defining the range of pathogens susceptible to Ifitm3 restriction using a knockout mouse model
    • Everitt AR, Clare S, McDonald JU, Kane L, Harcourt K, et al. (2013) Defining the range of pathogens susceptible to Ifitm3 restriction using a knockout mouse model. PLoS ONE 8: e80723.
    • (2013) PLoS ONE , vol.8
    • Everitt, A.R.1    Clare, S.2    McDonald, J.U.3    Kane, L.4    Harcourt, K.5
  • 12
    • 79551715390 scopus 로고    scopus 로고
    • The IFITM proteins inhibit HIV-1 infection
    • Lu J, Pan Q, Rong L, He W, Liu SL, et al. (2011) The IFITM proteins inhibit HIV-1 infection. J Virol 85: 2126-2137.
    • (2011) J Virol , vol.85 , pp. 2126-2137
    • Lu, J.1    Pan, Q.2    Rong, L.3    He, W.4    Liu, S.L.5
  • 13
    • 80055078235 scopus 로고    scopus 로고
    • IFITM3 inhibits influenza A virus infection by preventing cytosolic entry
    • Feeley EM, Sims JS, John SP, Chin CR, Pertel T, et al. (2011) IFITM3 inhibits influenza A virus infection by preventing cytosolic entry. PLoS Pathog 7: e1002337.
    • (2011) PLoS Pathog , vol.7
    • Feeley, E.M.1    Sims, J.S.2    John, S.P.3    Chin, C.R.4    Pertel, T.5
  • 14
    • 84876349734 scopus 로고    scopus 로고
    • The antiviral effector IFITM3 disrupts intracellular cholesterol homeostasis to block viral entry
    • Amini-Bavil-Olyaee S, Choi YJ, Lee JH, Shi M, Huang IC, et al. (2013) The antiviral effector IFITM3 disrupts intracellular cholesterol homeostasis to block viral entry. Cell Host Microbe 13: 452-464.
    • (2013) Cell Host Microbe , vol.13 , pp. 452-464
    • Amini-Bavil-Olyaee, S.1    Choi, Y.J.2    Lee, J.H.3    Shi, M.4    Huang, I.C.5
  • 15
    • 84880297659 scopus 로고    scopus 로고
    • The CD225 domain of IFITM3 is required for both IFITM protein association and inhibition of influenza A virus and dengue virus replication
    • John SP, Chin CR, Perreira JM, Feeley EM, Aker AM, et al. (2013) The CD225 domain of IFITM3 is required for both IFITM protein association and inhibition of influenza A virus and dengue virus replication. J Virol 87: 7837-7852.
    • (2013) J Virol , vol.87 , pp. 7837-7852
    • John, S.P.1    Chin, C.R.2    Perreira, J.M.3    Feeley, E.M.4    Aker, A.M.5
  • 16
    • 77955892540 scopus 로고    scopus 로고
    • Palmitoylome profiling reveals S-palmitoylation-dependent antiviral activity of IFITM3
    • Yount JS, Moltedo B, Yang YY, Charron G, Moran TM, et al. (2010) Palmitoylome profiling reveals S-palmitoylation-dependent antiviral activity of IFITM3. Nat Chem Biol 6: 610-614.
    • (2010) Nat Chem Biol , vol.6 , pp. 610-614
    • Yount, J.S.1    Moltedo, B.2    Yang, Y.Y.3    Charron, G.4    Moran, T.M.5
  • 17
    • 84887417852 scopus 로고    scopus 로고
    • Interferon-Induced Transmembrane Protein 3 is a Type II Transmembrane Protein
    • doi:10.1074/jbc.M113.514356
    • Bailey CC, Kondur HR, Huang IC, Farzan M, (2013) Interferon-Induced Transmembrane Protein 3 is a Type II Transmembrane Protein. J Biol Chem 288doi:10.1074/jbc.M113.514356.
    • (2013) J Biol Chem , vol.288
    • Bailey, C.C.1    Kondur, H.R.2    Huang, I.C.3    Farzan, M.4
  • 18
    • 0037690744 scopus 로고    scopus 로고
    • Differential requirements of Rab5 and Rab7 for endocytosis of influenza and other enveloped viruses
    • Sieczkarski SB, Whittaker GR, (2003) Differential requirements of Rab5 and Rab7 for endocytosis of influenza and other enveloped viruses. Traffic 4: 333-343.
    • (2003) Traffic , vol.4 , pp. 333-343
    • Sieczkarski, S.B.1    Whittaker, G.R.2
  • 19
    • 0022462117 scopus 로고
    • Interaction of polyene antibiotics with membrane lipids: physicochemical studies of the molecular basis of selectivity
    • Bolard J, (1986) Interaction of polyene antibiotics with membrane lipids: physicochemical studies of the molecular basis of selectivity. Drugs Exp Clin Res 12: 613-618.
    • (1986) Drugs Exp Clin Res , vol.12 , pp. 613-618
    • Bolard, J.1
  • 20
    • 84888439736 scopus 로고    scopus 로고
    • Amphotericin B increases influenza A virus infection by preventing IFITM3-mediated restriction
    • Lin TY, Chin CR, Everitt AR, Clare S, Perreira JM, et al. (2013) Amphotericin B increases influenza A virus infection by preventing IFITM3-mediated restriction. Cell Rep 5: 895-908.
    • (2013) Cell Rep , vol.5 , pp. 895-908
    • Lin, T.Y.1    Chin, C.R.2    Everitt, A.R.3    Clare, S.4    Perreira, J.M.5
  • 21
    • 47749148446 scopus 로고    scopus 로고
    • Different mechanisms of cell entry by human-pathogenic Old World and New World arenaviruses
    • Rojek JM, Sanchez AB, Nguyen NT, de la Torre JC, Kunz S, (2008) Different mechanisms of cell entry by human-pathogenic Old World and New World arenaviruses. J Virol 82: 7677-7687.
    • (2008) J Virol , vol.82 , pp. 7677-7687
    • Rojek, J.M.1    Sanchez, A.B.2    Nguyen, N.T.3    de la Torre, J.C.4    Kunz, S.5
  • 22
    • 23244461734 scopus 로고    scopus 로고
    • Caveola-dependent endocytic entry of amphotropic murine leukemia virus
    • Beer C, Andersen DS, Rojek A, Pedersen L, (2005) Caveola-dependent endocytic entry of amphotropic murine leukemia virus. J Virol 79: 10776-10787.
    • (2005) J Virol , vol.79 , pp. 10776-10787
    • Beer, C.1    Andersen, D.S.2    Rojek, A.3    Pedersen, L.4
  • 23
    • 0036844376 scopus 로고    scopus 로고
    • A sensitive and specific enzyme-based assay detecting HIV-1 virion fusion in primary T lymphocytes
    • Cavrois M, De Noronha C, Greene WC, (2002) A sensitive and specific enzyme-based assay detecting HIV-1 virion fusion in primary T lymphocytes. Nat Biotechnol 20: 1151-1154.
    • (2002) Nat Biotechnol , vol.20 , pp. 1151-1154
    • Cavrois, M.1    De Noronha, C.2    Greene, W.C.3
  • 24
    • 65249139458 scopus 로고    scopus 로고
    • HIV enters cells via endocytosis and dynamin-dependent fusion with endosomes
    • Miyauchi K, Kim Y, Latinovic O, Morozov V, Melikyan GB, (2009) HIV enters cells via endocytosis and dynamin-dependent fusion with endosomes. Cell 137: 433-444.
    • (2009) Cell , vol.137 , pp. 433-444
    • Miyauchi, K.1    Kim, Y.2    Latinovic, O.3    Morozov, V.4    Melikyan, G.B.5
  • 25
    • 73049089683 scopus 로고    scopus 로고
    • An enzymatic virus-like particle assay for sensitive detection of virus entry
    • Tscherne DM, Manicassamy B, Garcia-Sastre A, (2010) An enzymatic virus-like particle assay for sensitive detection of virus entry. J Virol Methods 163: 336-343.
    • (2010) J Virol Methods , vol.163 , pp. 336-343
    • Tscherne, D.M.1    Manicassamy, B.2    Garcia-Sastre, A.3
  • 26
    • 27544473312 scopus 로고    scopus 로고
    • Membrane hemifusion: crossing a chasm in two leaps
    • Chernomordik LV, Kozlov MM, (2005) Membrane hemifusion: crossing a chasm in two leaps. Cell 123: 375-382.
    • (2005) Cell , vol.123 , pp. 375-382
    • Chernomordik, L.V.1    Kozlov, M.M.2
  • 27
    • 2942635759 scopus 로고    scopus 로고
    • The energetics of membrane fusion from binding, through hemifusion, pore formation, and pore enlargement
    • Cohen FS, Melikyan GB, (2004) The energetics of membrane fusion from binding, through hemifusion, pore formation, and pore enlargement. J Membr Biol 199: 1-14.
    • (2004) J Membr Biol , vol.199 , pp. 1-14
    • Cohen, F.S.1    Melikyan, G.B.2
  • 29
    • 35448960873 scopus 로고    scopus 로고
    • Characterization of the early events in dengue virus cell entry by biochemical assays and single-virus tracking
    • van der Schaar HM, Rust MJ, Waarts BL, van der Ende-Metselaar H, Kuhn RJ, et al. (2007) Characterization of the early events in dengue virus cell entry by biochemical assays and single-virus tracking. J Virol 81: 12019-12028.
    • (2007) J Virol , vol.81 , pp. 12019-12028
    • van der Schaar, H.M.1    Rust, M.J.2    Waarts, B.L.3    van der Ende-Metselaar, H.4    Kuhn, R.J.5
  • 30
    • 0028865392 scopus 로고
    • GPI-anchored influenza hemagglutinin induces hemifusion to both red blood cell and planar bilayer membranes
    • Melikyan GB, White JM, Cohen FS, (1995) GPI-anchored influenza hemagglutinin induces hemifusion to both red blood cell and planar bilayer membranes. J Cell Biol 131: 679-691.
    • (1995) J Cell Biol , vol.131 , pp. 679-691
    • Melikyan, G.B.1    White, J.M.2    Cohen, F.S.3
  • 31
    • 84884680449 scopus 로고    scopus 로고
    • Viral Membrane Fusion and Nucleocapsid Delivery into the Cytoplasm are Distinct Events in Some Flaviviruses
    • Nour AM, Li Y, Wolenski J, Modis Y, (2013) Viral Membrane Fusion and Nucleocapsid Delivery into the Cytoplasm are Distinct Events in Some Flaviviruses. PLoS Pathog 9: e1003585.
    • (2013) PLoS Pathog , vol.9
    • Nour, A.M.1    Li, Y.2    Wolenski, J.3    Modis, Y.4
  • 32
    • 0025192947 scopus 로고
    • Observation of single influenza virus-cell fusion and measurement by fluorescence video microscopy
    • Lowy RJ, Sarkar DP, Chen Y, Blumenthal R, (1990) Observation of single influenza virus-cell fusion and measurement by fluorescence video microscopy. Proc Natl Acad Sci U S A 87: 1850-1854.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 1850-1854
    • Lowy, R.J.1    Sarkar, D.P.2    Chen, Y.3    Blumenthal, R.4
  • 33
    • 0025087319 scopus 로고
    • Diffusion and redistribution of lipid-like molecules between membranes in virus-cell and cell-cell fusion systems
    • Rubin RJ, Chen YD, (1990) Diffusion and redistribution of lipid-like molecules between membranes in virus-cell and cell-cell fusion systems. Biophys J 58: 1157-1167.
    • (1990) Biophys J , vol.58 , pp. 1157-1167
    • Rubin, R.J.1    Chen, Y.D.2
  • 34
    • 0027180538 scopus 로고
    • Membrane flux through the pore formed by a fusogenic viral envelope protein during cell fusion
    • Tse FW, Iwata A, Almers W, (1993) Membrane flux through the pore formed by a fusogenic viral envelope protein during cell fusion. J Cell Biol 121: 543-552.
    • (1993) J Cell Biol , vol.121 , pp. 543-552
    • Tse, F.W.1    Iwata, A.2    Almers, W.3
  • 35
    • 0032559801 scopus 로고    scopus 로고
    • The pathway of membrane fusion catalyzed by influenza hemagglutinin: restriction of lipids, hemifusion, and lipidic fusion pore formation
    • Chernomordik LV, Frolov VA, Leikina E, Bronk P, Zimmerberg J, (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.V.1    Frolov, V.A.2    Leikina, E.3    Bronk, P.4    Zimmerberg, J.5
  • 37
    • 84881229466 scopus 로고    scopus 로고
    • Fusion of Mature HIV-1 Particles Leads to Complete Release of a Gag-GFP-Based Content Marker and Raises the Intraviral pH
    • Padilla-Parra S, Marin M, Gahlaut N, Suter R, Kondo N, et al. (2013) Fusion of Mature HIV-1 Particles Leads to Complete Release of a Gag-GFP-Based Content Marker and Raises the Intraviral pH. PLoS ONE 8: e71002.
    • (2013) PLoS ONE , vol.8
    • Padilla-Parra, S.1    Marin, M.2    Gahlaut, N.3    Suter, R.4    Kondo, N.5
  • 38
    • 33749247584 scopus 로고    scopus 로고
    • Cellular mechanism of U18666A-mediated apoptosis in cultured murine cortical neurons: bridging Niemann-Pick disease type C and Alzheimer's disease
    • Koh CH, Cheung NS, (2006) Cellular mechanism of U18666A-mediated apoptosis in cultured murine cortical neurons: bridging Niemann-Pick disease type C and Alzheimer's disease. Cell Signal 18: 1844-1853.
    • (2006) Cell Signal , vol.18 , pp. 1844-1853
    • Koh, C.H.1    Cheung, N.S.2
  • 39
    • 4744376060 scopus 로고    scopus 로고
    • Lipid and cholesterol trafficking in NPC
    • Mukherjee S, Maxfield FR, (2004) Lipid and cholesterol trafficking in NPC. Biochim Biophys Acta 1685: 28-37.
    • (2004) Biochim Biophys Acta , vol.1685 , pp. 28-37
    • Mukherjee, S.1    Maxfield, F.R.2
  • 40
    • 80052851832 scopus 로고    scopus 로고
    • Ebola virus entry requires the cholesterol transporter Niemann-Pick C1
    • Carette JE, Raaben M, Wong AC, Herbert AS, Obernosterer G, et al. (2011) Ebola virus entry requires the cholesterol transporter Niemann-Pick C1. Nature 477: 340-343.
    • (2011) Nature , vol.477 , pp. 340-343
    • Carette, J.E.1    Raaben, M.2    Wong, A.C.3    Herbert, A.S.4    Obernosterer, G.5
  • 41
    • 80052868218 scopus 로고    scopus 로고
    • Small molecule inhibitors reveal Niemann-Pick C1 is essential for Ebola virus infection
    • Cote M, Misasi J, Ren T, Bruchez A, Lee K, et al. (2011) Small molecule inhibitors reveal Niemann-Pick C1 is essential for Ebola virus infection. Nature 477: 344-348.
    • (2011) Nature , vol.477 , pp. 344-348
    • Cote, M.1    Misasi, J.2    Ren, T.3    Bruchez, A.4    Lee, K.5
  • 42
    • 50549104079 scopus 로고    scopus 로고
    • Regulation of the V-ATPase along the endocytic pathway occurs through reversible subunit association and membrane localization
    • Lafourcade C, Sobo K, Kieffer-Jaquinod S, Garin J, van der Goot FG, (2008) Regulation of the V-ATPase along the endocytic pathway occurs through reversible subunit association and membrane localization. PLoS ONE 3: e2758.
    • (2008) PLoS ONE , vol.3
    • Lafourcade, C.1    Sobo, K.2    Kieffer-Jaquinod, S.3    Garin, J.4    van der Goot, F.G.5
  • 43
    • 0019474782 scopus 로고
    • pH-dependent hemolysis by influenza, Semliki, Forest virus, and Sendai virus
    • Lenard J, Miller DK, (1981) pH-dependent hemolysis by influenza, Semliki, Forest virus, and Sendai virus. Virology 110: 479-482.
    • (1981) Virology , vol.110 , pp. 479-482
    • Lenard, J.1    Miller, D.K.2
  • 44
    • 0038158091 scopus 로고    scopus 로고
    • The transport of low density lipoprotein-derived cholesterol to the plasma membrane is defective in NPC1 cells
    • Wojtanik KM, Liscum L, (2003) The transport of low density lipoprotein-derived cholesterol to the plasma membrane is defective in NPC1 cells. J Biol Chem 278: 14850-14856.
    • (2003) J Biol Chem , vol.278 , pp. 14850-14856
    • Wojtanik, K.M.1    Liscum, L.2
  • 45
    • 84874138355 scopus 로고    scopus 로고
    • Multiple cationic amphiphiles induce a Niemann-Pick C phenotype and inhibit Ebola virus entry and infection
    • Shoemaker CJ, Schornberg KL, Delos SE, Scully C, Pajouhesh H, et al. (2013) Multiple cationic amphiphiles induce a Niemann-Pick C phenotype and inhibit Ebola virus entry and infection. PLoS ONE 8: e56265.
    • (2013) PLoS ONE , vol.8
    • Shoemaker, C.J.1    Schornberg, K.L.2    Delos, S.E.3    Scully, C.4    Pajouhesh, H.5
  • 46
    • 42949150297 scopus 로고    scopus 로고
    • Cholesterol promotes hemifusion and pore widening in membrane fusion induced by influenza hemagglutinin
    • Biswas S, Yin SR, Blank PS, Zimmerberg J, (2008) Cholesterol promotes hemifusion and pore widening in membrane fusion induced by influenza hemagglutinin. J Gen Physiol 131: 503-513.
    • (2008) J Gen Physiol , vol.131 , pp. 503-513
    • Biswas, S.1    Yin, S.R.2    Blank, P.S.3    Zimmerberg, J.4
  • 47
    • 0034619518 scopus 로고    scopus 로고
    • Sterols and sphingolipids strongly affect the growth of fusion pores induced by the hemagglutinin of influenza virus
    • Razinkov VI, Cohen FS, (2000) Sterols and sphingolipids strongly affect the growth of fusion pores induced by the hemagglutinin of influenza virus. Biochemistry 39: 13462-13468.
    • (2000) Biochemistry , vol.39 , pp. 13462-13468
    • Razinkov, V.I.1    Cohen, F.S.2
  • 48
    • 84884342800 scopus 로고    scopus 로고
    • Multiphasic effects of cholesterol on influenza fusion kinetics reflect multiple mechanistic roles
    • Domanska MK, Wrona D, Kasson PM, (2013) Multiphasic effects of cholesterol on influenza fusion kinetics reflect multiple mechanistic roles. Biophys J 105: 1383-1387.
    • (2013) Biophys J , vol.105 , pp. 1383-1387
    • Domanska, M.K.1    Wrona, D.2    Kasson, P.M.3
  • 49
    • 77957134067 scopus 로고    scopus 로고
    • Non-vesicular lipid transport by lipid-transfer proteins and beyond
    • Lev S, (2010) Non-vesicular lipid transport by lipid-transfer proteins and beyond. Nat Rev Mol Cell Biol 11: 739-750.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 739-750
    • Lev, S.1
  • 51
    • 80053437934 scopus 로고    scopus 로고
    • Old world arenaviruses enter the host cell via the multivesicular body and depend on the endosomal sorting complex required for transport
    • Pasqual G, Rojek JM, Masin M, Chatton JY, Kunz S, (2011) Old world arenaviruses enter the host cell via the multivesicular body and depend on the endosomal sorting complex required for transport. PLoS Pathog 7: e1002232.
    • (2011) PLoS Pathog , vol.7
    • Pasqual, G.1    Rojek, J.M.2    Masin, M.3    Chatton, J.Y.4    Kunz, S.5
  • 52
    • 79551572796 scopus 로고    scopus 로고
    • Imaging single retrovirus entry through alternative receptor isoforms and intermediates of virus-endosome fusion
    • Jha NK, Latinovic O, Martin E, Novitskiy G, Marin M, et al. (2011) Imaging single retrovirus entry through alternative receptor isoforms and intermediates of virus-endosome fusion. PLoS Pathog 7: e1001260.
    • (2011) PLoS Pathog , vol.7
    • Jha, N.K.1    Latinovic, O.2    Martin, E.3    Novitskiy, G.4    Marin, M.5
  • 53
    • 0034037991 scopus 로고    scopus 로고
    • The lipid-anchored ectodomain of influenza virus hemagglutinin (GPI-HA) is capable of inducing nonenlarging fusion pores
    • Markosyan RM, Cohen FS, Melikyan GB, (2000) The lipid-anchored ectodomain of influenza virus hemagglutinin (GPI-HA) 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
  • 54
    • 0028587209 scopus 로고
    • Restricted movement of lipid and aqueous dyes through pores formed by influenza hemagglutinin during cell fusion
    • Zimmerberg J, Blumenthal R, Sarkar DP, Curran M, Morris SJ, (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    Sarkar, D.P.3    Curran, M.4    Morris, S.J.5
  • 55
    • 82655186589 scopus 로고    scopus 로고
    • Inhibition of HIV-1 endocytosis allows lipid mixing at the plasma membrane, but not complete fusion
    • de la Vega M, Marin M, Kondo N, Miyauchi K, Kim Y, et al. (2011) Inhibition of HIV-1 endocytosis allows lipid mixing at the plasma membrane, but not complete fusion. Retrovirology 8: 99.
    • (2011) Retrovirology , vol.8 , pp. 99
    • de la Vega, M.1    Marin, M.2    Kondo, N.3    Miyauchi, K.4    Kim, Y.5
  • 56
    • 63149160467 scopus 로고    scopus 로고
    • Characterization of Lassa virus cell entry and neutralization with Lassa virus pseudoparticles
    • Cosset FL, Marianneau P, Verney G, Gallais F, Tordo N, et al. (2009) Characterization of Lassa virus cell entry and neutralization with Lassa virus pseudoparticles. J Virol 83: 3228-3237.
    • (2009) J Virol , vol.83 , pp. 3228-3237
    • Cosset, F.L.1    Marianneau, P.2    Verney, G.3    Gallais, F.4    Tordo, N.5
  • 57
    • 16244391124 scopus 로고    scopus 로고
    • Comprehensive analysis of ebola virus GP1 in viral entry
    • Manicassamy B, Wang J, Jiang H, Rong L, (2005) Comprehensive analysis of ebola virus GP1 in viral entry. J Virol 79: 4793-4805.
    • (2005) J Virol , vol.79 , pp. 4793-4805
    • Manicassamy, B.1    Wang, J.2    Jiang, H.3    Rong, L.4
  • 58
    • 84865271846 scopus 로고    scopus 로고
    • Multifaceted mechanisms of HIV-1 entry inhibition by human alpha-defensin
    • Demirkhanyan LH, Marin M, Padilla-Parra S, Zhan C, Miyauchi K, et al. (2012) Multifaceted mechanisms of HIV-1 entry inhibition by human alpha-defensin. J Biol Chem 287: 28821-28838.
    • (2012) J Biol Chem , vol.287 , pp. 28821-28838
    • Demirkhanyan, L.H.1    Marin, M.2    Padilla-Parra, S.3    Zhan, C.4    Miyauchi, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.