메뉴 건너뛰기




Volumn 88, Issue 2, 2007, Pages 559-569

Newcastle disease virus may enter cells by caveolae-mediated endocytosis

Author keywords

[No Author keywords available]

Indexed keywords

CHLORPROMAZINE; CHOLESTEROL; METHYL BETA CYCLODEXTRIN; MONOCLONAL ANTIBODY; NYSTATIN; PHORBOL 13 ACETATE 12 MYRISTATE;

EID: 33846844906     PISSN: 00221317     EISSN: None     Source Type: Journal    
DOI: 10.1099/vir.0.82150-0     Document Type: Article
Times cited : (80)

References (70)
  • 1
    • 0027443234 scopus 로고
    • Caveolae: Where incoming and outgoing messengers meet
    • Anderson, R. G. (1993). Caveolae: where incoming and outgoing messengers meet. Proc Natl Acad Sci U S A 90, 10909-10913.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 10909-10913
    • Anderson, R.G.1
  • 2
    • 0029987340 scopus 로고    scopus 로고
    • Bound simian virus 40 translocates to caveolin-enriched membrane domains, and its entry is inhibited by drugs that selectively disrupt caveolae
    • Anderson, H. A., Chen, Y. & Norkin, L. C. (1996). Bound simian virus 40 translocates to caveolin-enriched membrane domains, and its entry is inhibited by drugs that selectively disrupt caveolae. Mol Biol Cell 7, 1825-1834.
    • (1996) Mol Biol Cell , vol.7 , pp. 1825-1834
    • Anderson, H.A.1    Chen, Y.2    Norkin, L.C.3
  • 3
    • 4544371670 scopus 로고    scopus 로고
    • Low pH is required for avian sarcoma and leukosis virus Env-dependent viral penetration into the cytosol and not for viral uncoating
    • Barnard, R. J., Narayan, S., Domadula, G., Miller, M. D. & Young, J. A. (2004). Low pH is required for avian sarcoma and leukosis virus Env-dependent viral penetration into the cytosol and not for viral uncoating. J Virol 78, 10433-10441.
    • (2004) J Virol , vol.78 , pp. 10433-10441
    • Barnard, R.J.1    Narayan, S.2    Domadula, G.3    Miller, M.D.4    Young, J.A.5
  • 4
    • 0033998692 scopus 로고    scopus 로고
    • Infectious entry pathway of adeno-associated virus and adeno-associated virus vectors
    • Bartlett, J. S., Wilcher, R. & Samulski, R. J. (2000). Infectious entry pathway of adeno-associated virus and adeno-associated virus vectors. J Virol 74, 2777-2785.
    • (2000) J Virol , vol.74 , pp. 2777-2785
    • Bartlett, J.S.1    Wilcher, R.2    Samulski, R.J.3
  • 5
    • 8644247468 scopus 로고    scopus 로고
    • Biological significance of the second receptor binding site of Newcastle disease virus hemagglutinin-neuraminidase protein
    • Bousse, T. L., Taylor, G., Krishnamurthy, S., Portner, A., Samal, S. K & Takimoto, T. (2004). Biological significance of the second receptor binding site of Newcastle disease virus hemagglutinin-neuraminidase protein. J Virol 78, 13351-13355.
    • (2004) J Virol , vol.78 , pp. 13351-13355
    • Bousse, T.L.1    Taylor, G.2    Krishnamurthy, S.3    Portner, A.4    Samal, S.K.5    Takimoto, T.6
  • 6
    • 19144365133 scopus 로고    scopus 로고
    • Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection
    • Chandran, K, Sullivan, N. J., Felbor, U., Whelan, S. P. & Cunningham, J. M. (2005). Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection. Science 308, 1643-1645.
    • (2005) Science , vol.308 , pp. 1643-1645
    • Chandran, K.1    Sullivan, N.J.2    Felbor, U.3    Whelan, S.P.4    Cunningham, J.M.5
  • 7
    • 0036168574 scopus 로고    scopus 로고
    • Fusogenic activity of reconstituted Newcastle disease virus envelopes: A role for the hemagglutinin-neuraminidase protein in the fusion process
    • Cobaleda, C., Muñoz-Barroso, I., Sagrera, A. & Villar, E. (2002). Fusogenic activity of reconstituted Newcastle disease virus envelopes: a role for the hemagglutinin-neuraminidase protein in the fusion process. Int J Biochem Cell Biol 34, 403-413.
    • (2002) Int J Biochem Cell Biol , vol.34 , pp. 403-413
    • Cobaleda, C.1    Muñoz-Barroso, I.2    Sagrera, A.3    Villar, E.4
  • 8
    • 0037422066 scopus 로고    scopus 로고
    • Regulated portals of entry into the cell
    • Conner, S. D. & Schmid, S. L. (2003). Regulated portals of entry into the cell. Nature 422, 37-44.
    • (2003) Nature , vol.422 , pp. 37-44
    • Conner, S.D.1    Schmid, S.L.2
  • 9
    • 13744252968 scopus 로고    scopus 로고
    • Involvement of clathrin-mediated endocytosis in human immuno-deficiency virus type I entry
    • Daecke, J., Fackler, O. T., Dittmar, M. T. & Krausslich, H. G. (2005). Involvement of clathrin-mediated endocytosis in human immuno-deficiency virus type I entry. J Virol 79, 1581-1594.
    • (2005) J Virol , vol.79 , pp. 1581-1594
    • Daecke, J.1    Fackler, O.T.2    Dittmar, M.T.3    Krausslich, H.G.4
  • 10
    • 13444273098 scopus 로고    scopus 로고
    • Clathrin- and caveolin-l-independent endocytosis: Entry of simian virus 40 into cells devoid of caveolae
    • Damm, E. M., Pelkmans, L., Kartenbeck, J., Mezzacasa, A., Kurzchalia, T. & Helenius, A. (2005). Clathrin- and caveolin-l-independent endocytosis: entry of simian virus 40 into cells devoid of caveolae. J Cell Biol 168, 477-488.
    • (2005) J Cell Biol , vol.168 , pp. 477-488
    • Damm, E.M.1    Pelkmans, L.2    Kartenbeck, J.3    Mezzacasa, A.4    Kurzchalia, T.5    Helenius, A.6
  • 11
    • 0345734205 scopus 로고    scopus 로고
    • Cholesterol removal by methyl-beta-cyclodextrin inhibits poliovirus entry
    • Danthi, P. & Chow, M. (2004). Cholesterol removal by methyl-beta-cyclodextrin inhibits poliovirus entry. J Virol 78, 33-41.
    • (2004) J Virol , vol.78 , pp. 33-41
    • Danthi, P.1    Chow, M.2
  • 12
    • 0032541402 scopus 로고    scopus 로고
    • The clathrin endocytic pathway in viral infection
    • DeTulleo, L. & Kirchhausen, T. (1998). The clathrin endocytic pathway in viral infection. EMBO J 17, 4585-4593.
    • (1998) EMBO J , vol.17 , pp. 4585-4593
    • DeTulleo, L.1    Kirchhausen, T.2
  • 13
    • 23844555503 scopus 로고    scopus 로고
    • The Nipah virus fusion protein is cleaved within the endosomal compartment
    • Diederich, S., Moll, M., Klenk, H.-D. & Maisner, A. (2005). The Nipah virus fusion protein is cleaved within the endosomal compartment. J Biol Chem 280, 29899-29903.
    • (2005) J Biol Chem , vol.280 , pp. 29899-29903
    • Diederich, S.1    Moll, M.2    Klenk, H.-D.3    Maisner, A.4
  • 14
    • 0037370724 scopus 로고    scopus 로고
    • The avian retrovirus avian sarcoma/leukosis virus subtype A reaches the lipid mixing stage of fusion at neutral pH
    • Earp, L. J., Delos, S. E., Netter, R. C., Bates, P. & White, J. M. (2003). The avian retrovirus avian sarcoma/leukosis virus subtype A reaches the lipid mixing stage of fusion at neutral pH. J Virol 77, 3058-3066.
    • (2003) J Virol , vol.77 , pp. 3058-3066
    • Earp, L.J.1    Delos, S.E.2    Netter, R.C.3    Bates, P.4    White, J.M.5
  • 15
    • 6344219974 scopus 로고    scopus 로고
    • Infection of vero cells by BK virus is dependent on caveolae
    • Eash, S., Querbes, W. & Atwood, W. J. (2004). Infection of vero cells by BK virus is dependent on caveolae. J Virol 78, 11583-11590.
    • (2004) J Virol , vol.78 , pp. 11583-11590
    • Eash, S.1    Querbes, W.2    Atwood, W.J.3
  • 16
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • Eckert, D. M. & Kim, P. S. (2001). Mechanisms of viral membrane fusion and its inhibition. Annu Rev Biochem 70, 777-810.
    • (2001) Annu Rev Biochem , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 17
    • 0036239229 scopus 로고    scopus 로고
    • Association of the caveola vesicular system with cellular entry by filoviruses
    • Empig, C. J. & Goldsmith, M. A. (2002). Association of the caveola vesicular system with cellular entry by filoviruses. J Virol 76, 5266-5270.
    • (2002) J Virol , vol.76 , pp. 5266-5270
    • Empig, C.J.1    Goldsmith, M.A.2
  • 18
    • 4143064852 scopus 로고    scopus 로고
    • Gangliosides and N-glycoproteins function as Newcastle disease virus receptors
    • Ferreira, L., Villar, E. & Muñoz-Barroso, I. (2004). Gangliosides and N-glycoproteins function as Newcastle disease virus receptors. Int J Biochem Cell Biol 36, 2344-2356.
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 2344-2356
    • Ferreira, L.1    Villar, E.2    Muñoz-Barroso, I.3
  • 19
    • 0024396034 scopus 로고
    • Proteins of Newcastle disease virus envelope: Interaction between the outer hemagglutinin-neuraminidase glycoprotein and the inner non-glycosylated matrix protein
    • Garcia-Sastre, A., Cabezas, J. A. & Villar, E. (1989). Proteins of Newcastle disease virus envelope: interaction between the outer hemagglutinin-neuraminidase glycoprotein and the inner non-glycosylated matrix protein. Biochim Biophys Acta 999, 171-175.
    • (1989) Biochim Biophys Acta , vol.999 , pp. 171-175
    • Garcia-Sastre, A.1    Cabezas, J.A.2    Villar, E.3
  • 20
    • 0033851301 scopus 로고    scopus 로고
    • Early steps of polyomavirus entry into cells
    • Gilbert, J. M. & Benjamin, T. L. (2000). Early steps of polyomavirus entry into cells. J Viral 74, 8582-8588.
    • (2000) J Viral , vol.74 , pp. 8582-8588
    • Gilbert, J.M.1    Benjamin, T.L.2
  • 21
    • 0021673527 scopus 로고
    • Fluorescence method for measuring the kinetics of fusion between biological membranes
    • Hoekstra, D., de Boer, T., Klappe, K. & Wilschut, J. (1984). Fluorescence method for measuring the kinetics of fusion between biological membranes. Biochemistry 23, 5675-5681.
    • (1984) Biochemistry , vol.23 , pp. 5675-5681
    • Hoekstra, D.1    de Boer, T.2    Klappe, K.3    Wilschut, J.4
  • 22
    • 0022997339 scopus 로고
    • Internalization and recycling of transferrin and its receptor. Effect of trifluoperazine on recycling in human erythroleukemic cells
    • Hunt, R. C. & Marshall-Carlson, L. (1986). Internalization and recycling of transferrin and its receptor. Effect of trifluoperazine on recycling in human erythroleukemic cells. J Biol Chem 261, 3681-3686.
    • (1986) J Biol Chem , vol.261 , pp. 3681-3686
    • Hunt, R.C.1    Marshall-Carlson, L.2
  • 23
    • 1642540252 scopus 로고    scopus 로고
    • Virology: A class act
    • Jardetzky, T. S. & Lamb, R. A. (2004). Virology: a class act. Nature 427, 307-308.
    • (2004) Nature , vol.427 , pp. 307-308
    • Jardetzky, T.S.1    Lamb, R.A.2
  • 26
    • 31344432402 scopus 로고    scopus 로고
    • Virus membrane-fusion proteins: More than one way to make a hairpin
    • Kiellan, M. & Rey, F. A. (2006). Virus membrane-fusion proteins: more than one way to make a hairpin. Nat Rev Microbiol 4, 67-76.
    • (2006) Nat Rev Microbiol , vol.4 , pp. 67-76
    • Kiellan, M.1    Rey, F.A.2
  • 27
    • 0027430672 scopus 로고
    • Paramyxovirus fusion: A hypothesis for changes
    • Lamb, R. A. (1993). Paramyxovirus fusion: a hypothesis for changes. Virology 197, 1-11.
    • (1993) Virology , vol.197 , pp. 1-11
    • Lamb, R.A.1
  • 28
    • 0027363575 scopus 로고
    • Caveolin forms a hetero-oligomeric protein complex that interacts with an apical GPI-linked protein: Implications for the biogenesis of caveolae
    • Lisanti, M. P., Tang, Z. L. & Sargiacomo, M. (1993). Caveolin forms a hetero-oligomeric protein complex that interacts with an apical GPI-linked protein: implications for the biogenesis of caveolae. J Cell Biol 123, 595-604.
    • (1993) J Cell Biol , vol.123 , pp. 595-604
    • Lisanti, M.P.1    Tang, Z.L.2    Sargiacomo, M.3
  • 30
    • 0019256559 scopus 로고
    • Adsorptive endocytosis of Semliki Forest virus
    • Marsh, M. & Helenius, A. (1980). Adsorptive endocytosis of Semliki Forest virus. J Mol Biol 142, 439-454.
    • (1980) J Mol Biol , vol.142 , pp. 439-454
    • Marsh, M.1    Helenius, A.2
  • 31
    • 0024534779 scopus 로고
    • Virus entry into animal cells
    • Marsh, M. & Helenius, A. (1989). Virus entry into animal cells. Adv Virus Res 36, 107-151.
    • (1989) Adv Virus Res , vol.36 , pp. 107-151
    • Marsh, M.1    Helenius, A.2
  • 32
    • 32944473016 scopus 로고    scopus 로고
    • Virus entry: Open sesame
    • Marsh, M. & Helenius, A. (2006). Virus entry: open sesame. Cell 124, 729-740.
    • (2006) Cell , vol.124 , pp. 729-740
    • Marsh, M.1    Helenius, A.2
  • 33
    • 0019814443 scopus 로고
    • Infectious entry pathway of influenza virus in a canine kidney cell line
    • Matlin, K. S., Reggio, H., Helenius, A. & Simons, K. (1981). Infectious entry pathway of influenza virus in a canine kidney cell line. J Cell Biol 91, 601-613.
    • (1981) J Cell Biol , vol.91 , pp. 601-613
    • Matlin, K.S.1    Reggio, H.2    Helenius, A.3    Simons, K.4
  • 34
    • 0019976569 scopus 로고
    • Pathway of vesicular stomatitis virus entry leading to infection
    • Matlin, K. S., Reggio, H., Helenius, A. & Simons, K. (1982). Pathway of vesicular stomatitis virus entry leading to infection. J Mol Biol 156, 609-631.
    • (1982) J Mol Biol , vol.156 , pp. 609-631
    • Matlin, K.S.1    Reggio, H.2    Helenius, A.3    Simons, K.4
  • 35
    • 3242713988 scopus 로고    scopus 로고
    • Sequential roles of receptor binding and low PH in forming prehairpin and hairpin conformations of a retroviral envelope glycoprotein
    • Matsuyama, S., Delos, S. E. & White, J. M. (2004). Sequential roles of receptor binding and low PH in forming prehairpin and hairpin conformations of a retroviral envelope glycoprotein. J Virol 78, 8201-8209.
    • (2004) J Virol , vol.78 , pp. 8201-8209
    • Matsuyama, S.1    Delos, S.E.2    White, J.M.3
  • 36
    • 1842509971 scopus 로고    scopus 로고
    • Low PH is required for avian sarcoma and leukosis virus Env-induced hemifusion and fusion pore formation but not for pore growth
    • Melikyan, G. B., Barnard, R. J., Markosyan, R. M., Young, J. A. & Cohen, F. S. (2004). Low PH is required for avian sarcoma and leukosis virus Env-induced hemifusion and fusion pore formation but not for pore growth. J Virol 78, 3753-3762.
    • (2004) J Virol , vol.78 , pp. 3753-3762
    • Melikyan, G.B.1    Barnard, R.J.2    Markosyan, R.M.3    Young, J.A.4    Cohen, F.S.5
  • 37
    • 26444565765 scopus 로고    scopus 로고
    • Endocytosis plays a critical role in proteolytic processing of the Hendra virus fusion protein
    • Meulendyke, K. A., Wurth, M. A., McCann, R. O. & Dutch, R. E. (2005). Endocytosis plays a critical role in proteolytic processing of the Hendra virus fusion protein. J Virol 79, 12643-12649.
    • (2005) J Virol , vol.79 , pp. 12643-12649
    • Meulendyke, K.A.1    Wurth, M.A.2    McCann, R.O.3    Dutch, R.E.4
  • 38
    • 0026696312 scopus 로고
    • Epstein-Barr virus enters B cells and epithelial cells by different routes
    • Miller, N. & Hutt-Fletcher, L. M. (1992). Epstein-Barr virus enters B cells and epithelial cells by different routes. J Virol 66, 3409-3414.
    • (1992) J Virol , vol.66 , pp. 3409-3414
    • Miller, N.1    Hutt-Fletcher, L.M.2
  • 39
    • 18744382150 scopus 로고    scopus 로고
    • Glycoprotein D receptor-dependent, low-pH-independent endocytic entry of herpes simplex virus type 1
    • Milne, R. S., Nicola, A. V., Whitbeck, J. C., Eisenberg, R. J. & Cohen, G. H. (2005). Glycoprotein D receptor-dependent, low-pH-independent endocytic entry of herpes simplex virus type 1. J Virol 79, 6655-6663.
    • (2005) J Virol , vol.79 , pp. 6655-6663
    • Milne, R.S.1    Nicola, A.V.2    Whitbeck, J.C.3    Eisenberg, R.J.4    Cohen, G.H.5
  • 40
    • 0033697734 scopus 로고    scopus 로고
    • Retroviral entry mediated by receptor priming and low pH triggering of an envelope glycoprotein
    • Mothes, W., Boerger, A. L., Narayan, S., Cunningham, J. M. & Young, J. A. (2000). Retroviral entry mediated by receptor priming and low pH triggering of an envelope glycoprotein. Cell 103, 679-689.
    • (2000) Cell , vol.103 , pp. 679-689
    • Mothes, W.1    Boerger, A.L.2    Narayan, S.3    Cunningham, J.M.4    Young, J.A.5
  • 41
    • 0037404499 scopus 로고    scopus 로고
    • Roles for endocytosis and low PH in herpes simplex virus entry into HeLa and Chinese hamster ovary cells
    • Nicola, A. V., McEvoy, A. M. & Straus, S. E. (2003). Roles for endocytosis and low PH in herpes simplex virus entry into HeLa and Chinese hamster ovary cells. J Virol 77, 5324-5332.
    • (2003) J Virol , vol.77 , pp. 5324-5332
    • Nicola, A.V.1    McEvoy, A.M.2    Straus, S.E.3
  • 42
    • 2342439156 scopus 로고    scopus 로고
    • Caveolae as an additional route for influenza virus endocytosis in MDCK cells
    • Nunes-Correia, I., Eulallo, A., Nir, S. & Pedroso de Lima, M. C. (2004). Caveolae as an additional route for influenza virus endocytosis in MDCK cells. Cell Mol Biol Lett 9, 47-60.
    • (2004) Cell Mol Biol Lett , vol.9 , pp. 47-60
    • Nunes-Correia, I.1    Eulallo, A.2    Nir, S.3    Pedroso de Lima, M.C.4
  • 43
    • 0033937284 scopus 로고    scopus 로고
    • Cellular uptake and infection by canine parvovirus involves rapid dynamin-regulated clathrin-mediated endocytosis, followed by slower intracellular trafficking
    • Parker, J. S. & Parrish, C. R. (2000). Cellular uptake and infection by canine parvovirus involves rapid dynamin-regulated clathrin-mediated endocytosis, followed by slower intracellular trafficking. J Virol 74, 1919-1930.
    • (2000) J Virol , vol.74 , pp. 1919-1930
    • Parker, J.S.1    Parrish, C.R.2
  • 44
    • 0041765800 scopus 로고    scopus 로고
    • Insider information: What viruses tell us about endocytosis
    • Pelkmans, L. & Helenius, A. (2003). Insider information: what viruses tell us about endocytosis. Curr Opin Cell Biol 15, 414-422.
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 414-422
    • Pelkmans, L.1    Helenius, A.2
  • 45
    • 0035017308 scopus 로고    scopus 로고
    • Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER
    • Pelkmans, L., Kartenbeck, J. & Helenius, A. (2001). Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER. Nat Cell Biol 3, 473-483.
    • (2001) Nat Cell Biol , vol.3 , pp. 473-483
    • Pelkmans, L.1    Kartenbeck, J.2    Helenius, A.3
  • 46
    • 0033968050 scopus 로고    scopus 로고
    • JC virus enters human glial cells by clathrin-dependent receptor-mediated endocytosis
    • Pho, M. T., Ashok, A. & Atwood, W. J. (2000). JC virus enters human glial cells by clathrin-dependent receptor-mediated endocytosis. J Virol 74, 2288-2292.
    • (2000) J Virol , vol.74 , pp. 2288-2292
    • Pho, M.T.1    Ashok, A.2    Atwood, W.J.3
  • 47
    • 0037333844 scopus 로고    scopus 로고
    • Triggering of human parainfluenza virus 3 fusion protein (F) by the hemagglutinin-neuraminidase (HN) protein: An HN mutation diminishes the rate of F activation and fusion
    • Porotto, M., Murrell, M., Greengard, O. & Moscona, A. (2003). Triggering of human parainfluenza virus 3 fusion protein (F) by the hemagglutinin-neuraminidase (HN) protein: an HN mutation diminishes the rate of F activation and fusion. J Virol 77, 3647-3654.
    • (2003) J Virol , vol.77 , pp. 3647-3654
    • Porotto, M.1    Murrell, M.2    Greengard, O.3    Moscona, A.4
  • 48
    • 31144439130 scopus 로고    scopus 로고
    • Paramyxovirus receptor-binding molecules: Engagement of one site on the hemagglutinin-neuraminidase protein modulates activity at the second site
    • Porotto, M., Fornabaio, M., Greengard, O., Murrell, M. T., Kellogg, G. E. & Moscona, A. (2006). Paramyxovirus receptor-binding molecules: engagement of one site on the hemagglutinin-neuraminidase protein modulates activity at the second site. J Virol 80, 1204-1213.
    • (2006) J Virol , vol.80 , pp. 1204-1213
    • Porotto, M.1    Fornabaio, M.2    Greengard, O.3    Murrell, M.T.4    Kellogg, G.E.5    Moscona, A.6
  • 49
    • 0032931988 scopus 로고    scopus 로고
    • Extraction of cholesterol with methyl-beta-cyclodextrin perturbs formation of clathrin-coated endocytic vesicles
    • Rodal, S. K., Skretting, G., Garred, O., Vilhardt, F., van Deurs, B. & Sandvig, K. (1999). Extraction of cholesterol with methyl-beta-cyclodextrin perturbs formation of clathrin-coated endocytic vesicles. Mol Biol Cell 10, 961-974.
    • (1999) Mol Biol Cell , vol.10 , pp. 961-974
    • Rodal, S.K.1    Skretting, G.2    Garred, O.3    Vilhardt, F.4    van Deurs, B.5    Sandvig, K.6
  • 50
    • 0025695634 scopus 로고
    • Cholesterol controls the clustering of the glycophospholipid-anchored membrane receptor for 5-methyltetrahydrofolate
    • Rothberg, K. G., Ying, Y. S., Kamen, B. A. & Anderson, R. G. (1990). Cholesterol controls the clustering of the glycophospholipid-anchored membrane receptor for 5-methyltetrahydrofolate. J Cell Biol 111, 2931-2938.
    • (1990) J Cell Biol , vol.111 , pp. 2931-2938
    • Rothberg, K.G.1    Ying, Y.S.2    Kamen, B.A.3    Anderson, R.G.4
  • 51
    • 0034142287 scopus 로고    scopus 로고
    • Early stages of influenza virus entry into Mv-1 lung cells: Involvement of dynamin
    • Roy, A. M., Parker, J. S., Parrish, C. R. & Whittaker, G. R. (2000). Early stages of influenza virus entry into Mv-1 lung cells: involvement of dynamin. Virology 267, 17-28.
    • (2000) Virology , vol.267 , pp. 17-28
    • Roy, A.M.1    Parker, J.S.2    Parrish, C.R.3    Whittaker, G.R.4
  • 52
    • 0035421959 scopus 로고    scopus 로고
    • Membrane fusion machines of paramyxoviruses: Capture of intermediates of fusion
    • Russell, C. J., Jardetzky, T. S. & Lamb, R. A. (2001). Membrane fusion machines of paramyxoviruses: capture of intermediates of fusion. EMBO J 20, 4024-4034.
    • (2001) EMBO J , vol.20 , pp. 4024-4034
    • Russell, C.J.1    Jardetzky, T.S.2    Lamb, R.A.3
  • 53
    • 33645453800 scopus 로고    scopus 로고
    • Structural analysis of a designed inhibitor complexed with the hemagglutinin-neuraminidase of Newcastle disease virus
    • Ryan, C., Zaitsev, V., Tindal, D. J., Dyason, J. C., Thomson, R. J., Alymova, I., Portner, A., Itzstein, M. & Taylor, G. (2006). Structural analysis of a designed inhibitor complexed with the hemagglutinin-neuraminidase of Newcastle disease virus. Glycoconj J 23, 135-141.
    • (2006) Glycoconj J , vol.23 , pp. 135-141
    • Ryan, C.1    Zaitsev, V.2    Tindal, D.J.3    Dyason, J.C.4    Thomson, R.J.5    Alymova, I.6    Portner, A.7    Itzstein, M.8    Taylor, G.9
  • 55
    • 0033179017 scopus 로고    scopus 로고
    • Acidic pH enhancement of the fusion of Newcastle disease virus with cultured cells
    • San Roman, K., Villar, E. & Muñoz-Barroso, I. (1999). Acidic pH enhancement of the fusion of Newcastle disease virus with cultured cells. Virology 260, 329-341.
    • (1999) Virology , vol.260 , pp. 329-341
    • San Roman, K.1    Villar, E.2    Muñoz-Barroso, I.3
  • 56
    • 0035986610 scopus 로고    scopus 로고
    • Mode of action of two inhibitory peptides from heptad repeat domains of the fusion protein of Newcastle disease virus
    • San Roman, K., Villar, E. & Muñoz-Barroso, I. (2002). Mode of action of two inhibitory peptides from heptad repeat domains of the fusion protein of Newcastle disease virus. Int J Biochem Cell Biol 34, 1207-1220.
    • (2002) Int J Biochem Cell Biol , vol.34 , pp. 1207-1220
    • San Roman, K.1    Villar, E.2    Muñoz-Barroso, I.3
  • 57
    • 11144340301 scopus 로고    scopus 로고
    • Class I and class II viral fusion protein structures reveal similar principles in membrane fusion
    • Schibli, D. J. & Weissenhorn, W. (2004). Class I and class II viral fusion protein structures reveal similar principles in membrane fusion. Mol Membr Biol 21, 361-371.
    • (2004) Mol Membr Biol , vol.21 , pp. 361-371
    • Schibli, D.J.1    Weissenhorn, W.2
  • 58
    • 0034024481 scopus 로고    scopus 로고
    • A single amino acid change in the Newcastle disease virus fusion protein alters the requirement for HN protein in fusion
    • Sergel, T. A., McGinnes, L. W. & Morrison, T. G. (2000). A single amino acid change in the Newcastle disease virus fusion protein alters the requirement for HN protein in fusion. J Virol 74, 5101-5107.
    • (2000) J Virol , vol.74 , pp. 5101-5107
    • Sergel, T.A.1    McGinnes, L.W.2    Morrison, T.G.3
  • 59
    • 0038364256 scopus 로고    scopus 로고
    • Activation of fusion by the SER virus F protein: A low-pH-dependent paramyxovirus entry process
    • Seth, S., Vincent, A. & Compans, R. W. (2003). Activation of fusion by the SER virus F protein: a low-pH-dependent paramyxovirus entry process. J Virol 77, 6520-6527.
    • (2003) J Virol , vol.77 , pp. 6520-6527
    • Seth, S.1    Vincent, A.2    Compans, R.W.3
  • 60
    • 0036298810 scopus 로고    scopus 로고
    • Dissecting virus entry via endocytosis
    • Sieczkarski, S. B. & Whittaker, G. R. (2002a). Dissecting virus entry via endocytosis. J Gen Virol 83, 1535-1545.
    • (2002) J Gen Virol , vol.83 , pp. 1535-1545
    • Sieczkarski, S.B.1    Whittaker, G.R.2
  • 61
    • 0036784565 scopus 로고    scopus 로고
    • Influenza virus can enter and infect cells in the absence of clathrin -mediated endocytosis
    • Sieczkarski, S. B. & Whittaker, G. R. (2002b). Influenza virus can enter and infect cells in the absence of clathrin -mediated endocytosis. J Virol 76, 10455-10464.
    • (2002) J Virol , vol.76 , pp. 10455-10464
    • Sieczkarski, S.B.1    Whittaker, G.R.2
  • 63
    • 0036721021 scopus 로고    scopus 로고
    • A novel cell entry pathway for a DAF-using human enterovirus is dependent on lipid rafts
    • Stuart, A. D., Eustace, H. E, McKee, T. A. & Brown, T. D. (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
    • 20644463701 scopus 로고    scopus 로고
    • Role of the clathrin-mediated endocytosis during vesicular stomatitis virus entry into host cells
    • Sun, X., Yau, V. K., Briggs, B. J. & Whittaker, G. R. (2005). Role of the clathrin-mediated endocytosis during vesicular stomatitis virus entry into host cells. Virology 338, 53-60.
    • (2005) Virology , vol.338 , pp. 53-60
    • Sun, X.1    Yau, V.K.2    Briggs, B.J.3    Whittaker, G.R.4
  • 66
    • 33748483495 scopus 로고    scopus 로고
    • Vaccinia virus entry into cells via a low-pH-dependent endosomal pathway
    • Townsley, A. C., Weisberg, A. S., Wagenaar, T. R. & Moss, B. (2006). Vaccinia virus entry into cells via a low-pH-dependent endosomal pathway. J Virol 80, 8899-8908.
    • (2006) J Virol , vol.80 , pp. 8899-8908
    • Townsley, A.C.1    Weisberg, A.S.2    Wagenaar, T.R.3    Moss, B.4
  • 67
    • 0027520440 scopus 로고
    • Mis-assembly of clathrin lattices on endosomes reveals a regulatory switch for coated pit formation
    • Wang, L. H., Rothberg, K. G. & Anderson, R. G. (1993). Mis-assembly of clathrin lattices on endosomes reveals a regulatory switch for coated pit formation. J Cell Biol 123, 1107-1117.
    • (1993) J Cell Biol , vol.123 , pp. 1107-1117
    • Wang, L.H.1    Rothberg, K.G.2    Anderson, R.G.3
  • 68
    • 0020752797 scopus 로고
    • Membrane fusion proteins of enveloped animal viruses
    • White, J., Kielian, M. & Helenius, A. (1983). Membrane fusion proteins of enveloped animal viruses. Q Rev Biophys 16, 151-195.
    • (1983) Q Rev Biophys , vol.16 , pp. 151-195
    • White, J.1    Kielian, M.2    Helenius, A.3
  • 69
    • 0031585556 scopus 로고    scopus 로고
    • Analysis of a peptide inhibitor of paramyxovirus (NDV) fusion using biological assays, NMR, and molecular modeling
    • Young, J. K., Hicks, R. P., Wright, G. E. & Morrison, T. G. (1997). Analysis of a peptide inhibitor of paramyxovirus (NDV) fusion using biological assays, NMR, and molecular modeling. Virology 238, 291-304.
    • (1997) Virology , vol.238 , pp. 291-304
    • Young, J.K.1    Hicks, R.P.2    Wright, G.E.3    Morrison, T.G.4
  • 70
    • 1842614339 scopus 로고    scopus 로고
    • Second sialic acid binding site in Newcastle disease virus hemagglutinin-neuraminidase: Implications for fusion
    • Zaitsev, V., von Itzstein, M., Groves, D., Kiefel, M., Takimoto, T., Portner, A. & Taylor, G. (2004). Second sialic acid binding site in Newcastle disease virus hemagglutinin-neuraminidase: implications for fusion. J Virol 78, 3733-3741.
    • (2004) J Virol , vol.78 , pp. 3733-3741
    • Zaitsev, V.1    von Itzstein, M.2    Groves, D.3    Kiefel, M.4    Takimoto, T.5    Portner, A.6    Taylor, G.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.