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Volumn 8, Issue 6, 2012, Pages

African swine fever virus uses macropinocytosis to enter host cells

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; DEXTRAN; EPIDERMAL GROWTH FACTOR RECEPTOR; P21 ACTIVATED KINASE 1; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE B; RAC1 PROTEIN; SODIUM PROTON EXCHANGE PROTEIN;

EID: 84875079560     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1002754     Document Type: Article
Times cited : (157)

References (116)
  • 2
    • 84858008817 scopus 로고    scopus 로고
    • Quantitative Risk Assessment for the Introduction of African Swine Fever Virus into the European Union by Legal Import of Live Pigs
    • Mur L, Martinez-Lopez B, Martinez-Aviles M, Costard S, Wieland B, et al. (2012) Quantitative Risk Assessment for the Introduction of African Swine Fever Virus into the European Union by Legal Import of Live Pigs. Transbound Emerg Dis 59: 134-144.
    • (2012) Transbound Emerg Dis , vol.59 , pp. 134-144
    • Mur, L.1    Martinez-Lopez, B.2    Martinez-Aviles, M.3    Costard, S.4    Wieland, B.5
  • 3
    • 0021908410 scopus 로고
    • African swine fever virus
    • Vinuela E, (1985) African swine fever virus. Curr Top Microbiol Immunol 116: 151-170.
    • (1985) Curr Top Microbiol Immunol , vol.116 , pp. 151-170
    • Vinuela, E.1
  • 5
    • 29644432635 scopus 로고    scopus 로고
    • The viral protein A238L inhibits TNF-alpha expression through a CBP/p300 transcriptional coactivators pathway
    • Granja AG, Nogal ML, Hurtado C, Del Aguila C, Carrascosa AL, et al. (2006) The viral protein A238L inhibits TNF-alpha expression through a CBP/p300 transcriptional coactivators pathway. J Immunol 176: 451-462.
    • (2006) J Immunol , vol.176 , pp. 451-462
    • Granja, A.G.1    Nogal, M.L.2    Hurtado, C.3    Del Aguila, C.4    Carrascosa, A.L.5
  • 6
    • 2942641706 scopus 로고    scopus 로고
    • Modulation of p53 cellular function and cell death by African swine fever virus
    • Granja AG, Nogal ML, Hurtado C, Salas J, Salas ML, et al. (2004) Modulation of p53 cellular function and cell death by African swine fever virus. J Virol 78: 7165-7174.
    • (2004) J Virol , vol.78 , pp. 7165-7174
    • Granja, A.G.1    Nogal, M.L.2    Hurtado, C.3    Salas, J.4    Salas, M.L.5
  • 7
    • 11144229616 scopus 로고    scopus 로고
    • The viral protein A238L inhibits cyclooxygenase-2 expression through a nuclear factor of activated T cell-dependent transactivation pathway
    • Granja AG, Nogal ML, Hurtado C, Vila V, Carrascosa AL, et al. (2004) The viral protein A238L inhibits cyclooxygenase-2 expression through a nuclear factor of activated T cell-dependent transactivation pathway. J Biol Chem 279: 53736-53746.
    • (2004) J Biol Chem , vol.279 , pp. 53736-53746
    • Granja, A.G.1    Nogal, M.L.2    Hurtado, C.3    Vila, V.4    Carrascosa, A.L.5
  • 8
    • 42149193168 scopus 로고    scopus 로고
    • A238L inhibits NF-ATc2, NF-kappa B, and c-Jun activation through a novel mechanism involving protein kinase C-theta-mediated up-regulation of the amino-terminal transactivation domain of p300
    • Granja AG, Perkins ND, Revilla Y, (2008) A238L inhibits NF-ATc2, NF-kappa B, and c-Jun activation through a novel mechanism involving protein kinase C-theta-mediated up-regulation of the amino-terminal transactivation domain of p300. J Immunol 180: 2429-2442.
    • (2008) J Immunol , vol.180 , pp. 2429-2442
    • Granja, A.G.1    Perkins, N.D.2    Revilla, Y.3
  • 9
    • 33750309635 scopus 로고    scopus 로고
    • Regulation of inducible nitric oxide synthase expression by viral A238L-mediated inhibition of p65/RelA acetylation and p300 transactivation
    • Granja AG, Sabina P, Salas ML, Fresno M, Revilla Y, (2006) Regulation of inducible nitric oxide synthase expression by viral A238L-mediated inhibition of p65/RelA acetylation and p300 transactivation. J Virol 80: 10487-10496.
    • (2006) J Virol , vol.80 , pp. 10487-10496
    • Granja, A.G.1    Sabina, P.2    Salas, M.L.3    Fresno, M.4    Revilla, Y.5
  • 10
    • 58149502582 scopus 로고    scopus 로고
    • African swine fever virus blocks the host cell antiviral inflammatory response through a direct inhibition of PKC-theta-mediated p300 transactivation
    • Granja AG, Sanchez EG, Sabina P, Fresno M, Revilla Y, (2009) African swine fever virus blocks the host cell antiviral inflammatory response through a direct inhibition of PKC-theta-mediated p300 transactivation. J Virol 83: 969-980.
    • (2009) J Virol , vol.83 , pp. 969-980
    • Granja, A.G.1    Sanchez, E.G.2    Sabina, P.3    Fresno, M.4    Revilla, Y.5
  • 11
    • 3242727007 scopus 로고    scopus 로고
    • The C-type lectin homologue gene (EP153R) of African swine fever virus inhibits apoptosis both in virus infection and in heterologous expression
    • Hurtado C, Granja AG, Bustos MJ, Nogal ML, Gonzalez de Buitrago G, et al. (2004) The C-type lectin homologue gene (EP153R) of African swine fever virus inhibits apoptosis both in virus infection and in heterologous expression. Virology 326: 160-170.
    • (2004) Virology , vol.326 , pp. 160-170
    • Hurtado, C.1    Granja, A.G.2    Bustos, M.J.3    Nogal, M.L.4    Gonzalez de Buitrago, G.5
  • 12
    • 0028962282 scopus 로고
    • Analysis of the complete nucleotide sequence of African swine fever virus
    • Yanez RJ, Rodriguez JM, Nogal ML, Yuste L, Enriquez C, et al. (1995) Analysis of the complete nucleotide sequence of African swine fever virus. Virology 208: 249-278.
    • (1995) Virology , vol.208 , pp. 249-278
    • Yanez, R.J.1    Rodriguez, J.M.2    Nogal, M.L.3    Yuste, L.4    Enriquez, C.5
  • 13
    • 79961195840 scopus 로고    scopus 로고
    • Disruption of nuclear organization during the initial phase of African swine fever virus infection
    • Ballester M, Rodriguez-Carino C, Perez M, Gallardo C, Rodriguez JM, et al. (2011) Disruption of nuclear organization during the initial phase of African swine fever virus infection. J Virol 85: 8263-8269.
    • (2011) J Virol , vol.85 , pp. 8263-8269
    • Ballester, M.1    Rodriguez-Carino, C.2    Perez, M.3    Gallardo, C.4    Rodriguez, J.M.5
  • 14
    • 0026708727 scopus 로고
    • Role of the host cell nucleus in the replication of African swine fever virus DNA
    • Garcia-Beato R, Salas ML, Vinuela E, Salas J, (1992) Role of the host cell nucleus in the replication of African swine fever virus DNA. Virology 188: 637-649.
    • (1992) Virology , vol.188 , pp. 637-649
    • Garcia-Beato, R.1    Salas, M.L.2    Vinuela, E.3    Salas, J.4
  • 15
    • 70049089250 scopus 로고    scopus 로고
    • Regulation of host translational machinery by African swine fever virus
    • Castello A, Quintas A, Sanchez EG, Sabina P, Nogal M, et al. (2009) Regulation of host translational machinery by African swine fever virus. PLoS Pathog 5: e1000562.
    • (2009) PLoS Pathog , vol.5
    • Castello, A.1    Quintas, A.2    Sanchez, E.G.3    Sabina, P.4    Nogal, M.5
  • 16
    • 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
  • 17
    • 50149096579 scopus 로고    scopus 로고
    • Epsin 1 is a cargo-specific adaptor for the clathrin-mediated endocytosis of the influenza virus
    • Chen C, Zhuang X, (2008) Epsin 1 is a cargo-specific adaptor for the clathrin-mediated endocytosis of the influenza virus. Proc Natl Acad Sci U S A 105: 11790-11795.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 11790-11795
    • Chen, C.1    Zhuang, X.2
  • 18
    • 66349113767 scopus 로고    scopus 로고
    • Vesicular stomatitis virus enters cells through vesicles incompletely coated with clathrin that depend upon actin for internalization
    • Cureton DK, Massol RH, Saffarian S, Kirchhausen TL, Whelan SP, (2009) Vesicular stomatitis virus enters cells through vesicles incompletely coated with clathrin that depend upon actin for internalization. PLoS Pathog 5: e1000394.
    • (2009) PLoS Pathog , vol.5
    • Cureton, D.K.1    Massol, R.H.2    Saffarian, S.3    Kirchhausen, T.L.4    Whelan, S.P.5
  • 19
    • 0018853517 scopus 로고
    • On the entry of Semliki forest virus into BHK-21 cells
    • Helenius A, Kartenbeck J, Simons K, Fries E, (1980) On the entry of Semliki forest virus into BHK-21 cells. J Cell Biol 84: 404-420.
    • (1980) J Cell Biol , vol.84 , pp. 404-420
    • Helenius, A.1    Kartenbeck, J.2    Simons, K.3    Fries, E.4
  • 20
    • 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
  • 21
    • 65449120034 scopus 로고    scopus 로고
    • Virus entry by macropinocytosis
    • Mercer J, Helenius A, (2009) Virus entry by macropinocytosis. Nat Cell Biol 11: 510-520.
    • (2009) Nat Cell Biol , vol.11 , pp. 510-520
    • Mercer, J.1    Helenius, A.2
  • 23
    • 42549153337 scopus 로고    scopus 로고
    • Vaccinia virus uses macropinocytosis and apoptotic mimicry to enter host cells
    • Mercer J, Helenius A, (2008) Vaccinia virus uses macropinocytosis and apoptotic mimicry to enter host cells. Science 320: 531-535.
    • (2008) Science , vol.320 , pp. 531-535
    • Mercer, J.1    Helenius, A.2
  • 24
    • 33748483495 scopus 로고    scopus 로고
    • Vaccinia virus entry into cells via a low-pH-dependent endosomal pathway
    • Townsley AC, Weisberg AS, Wagenaar TR, 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
  • 25
    • 34548433948 scopus 로고    scopus 로고
    • Coxsackievirus entry across epithelial tight junctions requires occludin and the small GTPases Rab34 and Rab5
    • Coyne CB, Shen L, Turner JR, Bergelson JM, (2007) Coxsackievirus entry across epithelial tight junctions requires occludin and the small GTPases Rab34 and Rab5. Cell Host Microbe 2: 181-192.
    • (2007) Cell Host Microbe , vol.2 , pp. 181-192
    • Coyne, C.B.1    Shen, L.2    Turner, J.R.3    Bergelson, J.M.4
  • 26
    • 41949139871 scopus 로고    scopus 로고
    • Subversion of CtBP1-controlled macropinocytosis by human adenovirus serotype 3
    • Amstutz B, Gastaldelli M, Kalin S, Imelli N, Boucke K, et al. (2008) Subversion of CtBP1-controlled macropinocytosis by human adenovirus serotype 3. EMBO J 27: 956-969.
    • (2008) EMBO J , vol.27 , pp. 956-969
    • Amstutz, B.1    Gastaldelli, M.2    Kalin, S.3    Imelli, N.4    Boucke, K.5
  • 27
    • 19944423114 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 enters human epidermal keratinocytes, but not neurons, via a pH-dependent endocytic pathway
    • Nicola AV, Hou J, Major EO, Straus SE, (2005) Herpes simplex virus type 1 enters human epidermal keratinocytes, but not neurons, via a pH-dependent endocytic pathway. J Virol 79: 7609-7616.
    • (2005) J Virol , vol.79 , pp. 7609-7616
    • Nicola, A.V.1    Hou, J.2    Major, E.O.3    Straus, S.E.4
  • 28
    • 0037404499 scopus 로고    scopus 로고
    • Roles for endocytosis and low pH in herpes simplex virus entry into HeLa and Chinese hamster ovary cells
    • Nicola AV, McEvoy AM, Straus SE, (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
  • 29
    • 78651237433 scopus 로고    scopus 로고
    • Interaction of c-Cbl with myosin IIA regulates Bleb associated macropinocytosis of Kaposi's sarcoma-associated herpesvirus
    • Valiya Veettil M, Sadagopan S, Kerur N, Chakraborty S, Chandran B, (2010) Interaction of c-Cbl with myosin IIA regulates Bleb associated macropinocytosis of Kaposi's sarcoma-associated herpesvirus. PLoS Pathog 6: e1001238.
    • (2010) PLoS Pathog , vol.6
    • Valiya Veettil, M.1    Sadagopan, S.2    Kerur, N.3    Chakraborty, S.4    Chandran, B.5
  • 30
    • 80054774353 scopus 로고    scopus 로고
    • Ebola virus enters host cells by macropinocytosis and clathrin-mediated endocytosis
    • Aleksandrowicz P, Marzi A, Biedenkopf N, Beimforde N, Becker S, et al. (2011) Ebola virus enters host cells by macropinocytosis and clathrin-mediated endocytosis. J Infect Dis 204 (Suppl 3): S957-967.
    • (2011) J Infect Dis , vol.204 , Issue.SUPPL. 3
    • Aleksandrowicz, P.1    Marzi, A.2    Biedenkopf, N.3    Beimforde, N.4    Becker, S.5
  • 31
    • 10044236498 scopus 로고    scopus 로고
    • Effects of endocytosis inhibitory drugs on rubella virus entry into VeroE6 cells
    • Kee SH, Cho EJ, Song JW, Park KS, Baek LJ, et al. (2004) Effects of endocytosis inhibitory drugs on rubella virus entry into VeroE6 cells. Microbiol Immunol 48: 823-829.
    • (2004) Microbiol Immunol , vol.48 , pp. 823-829
    • Kee, S.H.1    Cho, E.J.2    Song, J.W.3    Park, K.S.4    Baek, L.J.5
  • 32
    • 0037119944 scopus 로고    scopus 로고
    • Adenovirus triggers macropinocytosis and endosomal leakage together with its clathrin-mediated uptake
    • Meier O, Boucke K, Hammer SV, Keller S, Stidwill RP, et al. (2002) Adenovirus triggers macropinocytosis and endosomal leakage together with its clathrin-mediated uptake. J Cell Biol 158: 1119-1131.
    • (2002) J Cell Biol , vol.158 , pp. 1119-1131
    • Meier, O.1    Boucke, K.2    Hammer, S.V.3    Keller, S.4    Stidwill, R.P.5
  • 33
    • 0024603575 scopus 로고
    • Saturable binding sites mediate the entry of African swine fever virus into Vero cells
    • Alcami A, Carrascosa AL, Vinuela E, (1989) Saturable binding sites mediate the entry of African swine fever virus into Vero cells. Virology 168: 393-398.
    • (1989) Virology , vol.168 , pp. 393-398
    • Alcami, A.1    Carrascosa, A.L.2    Vinuela, E.3
  • 34
    • 0024309157 scopus 로고
    • The entry of African swine fever virus into Vero cells
    • Alcami A, Carrascosa AL, Vinuela E, (1989) The entry of African swine fever virus into Vero cells. Virology 171: 68-75.
    • (1989) Virology , vol.171 , pp. 68-75
    • Alcami, A.1    Carrascosa, A.L.2    Vinuela, E.3
  • 35
    • 0032780352 scopus 로고    scopus 로고
    • Virus-specific cell receptors are necessary, but not sufficient, to confer cell susceptibility to African swine fever virus
    • Carrascosa AL, Bustos MJ, Galindo I, Vinuela E, (1999) Virus-specific cell receptors are necessary, but not sufficient, to confer cell susceptibility to African swine fever virus. Arch Virol 144: 1309-1321.
    • (1999) Arch Virol , vol.144 , pp. 1309-1321
    • Carrascosa, A.L.1    Bustos, M.J.2    Galindo, I.3    Vinuela, E.4
  • 36
    • 0021854277 scopus 로고
    • Effect of chloroquine on African swine fever virus infection
    • Geraldes A, Valdeira ML, (1985) Effect of chloroquine on African swine fever virus infection. J Gen Virol 66 (Pt 5): 1145-1148.
    • (1985) J Gen Virol , vol.66 , Issue.Pt 5 , pp. 1145-1148
    • Geraldes, A.1    Valdeira, M.L.2
  • 37
    • 0032574111 scopus 로고    scopus 로고
    • Entry of African swine fever virus into Vero cells and uncoating
    • Valdeira ML, Bernardes C, Cruz B, Geraldes A, (1998) Entry of African swine fever virus into Vero cells and uncoating. Vet Microbiol 60: 131-140.
    • (1998) Vet Microbiol , vol.60 , pp. 131-140
    • Valdeira, M.L.1    Bernardes, C.2    Cruz, B.3    Geraldes, A.4
  • 38
    • 75449110786 scopus 로고    scopus 로고
    • Dynamin- and clathrin-dependent endocytosis in African swine fever virus entry
    • Hernaez B, Alonso C, (2010) Dynamin- and clathrin-dependent endocytosis in African swine fever virus entry. J Virol 84: 2100-2109.
    • (2010) J Virol , vol.84 , pp. 2100-2109
    • Hernaez, B.1    Alonso, C.2
  • 40
    • 0019767062 scopus 로고
    • Production and titration of African swine fever virus in porcine alveolar macrophages
    • Carrascosa AL, Santaren JF, Vinuela E, (1982) Production and titration of African swine fever virus in porcine alveolar macrophages. J Virol Methods 3: 303-310.
    • (1982) J Virol Methods , vol.3 , pp. 303-310
    • Carrascosa, A.L.1    Santaren, J.F.2    Vinuela, E.3
  • 42
    • 0022053407 scopus 로고
    • Monoclonal antibodies specific for African swine fever virus proteins
    • Sanz A, Garcia-Barreno B, Nogal ML, Vinuela E, Enjuanes L, (1985) Monoclonal antibodies specific for African swine fever virus proteins. J Virol 54: 199-206.
    • (1985) J Virol , vol.54 , pp. 199-206
    • Sanz, A.1    Garcia-Barreno, B.2    Nogal, M.L.3    Vinuela, E.4    Enjuanes, L.5
  • 43
    • 0021340584 scopus 로고
    • General morphology and capsid fine structure of African swine fever virus particles
    • Carrascosa JL, Carazo JM, Carrascosa AL, Garcia N, Santisteban A, et al. (1984) General morphology and capsid fine structure of African swine fever virus particles. Virology 132: 160-172.
    • (1984) Virology , vol.132 , pp. 160-172
    • Carrascosa, J.L.1    Carazo, J.M.2    Carrascosa, A.L.3    Garcia, N.4    Santisteban, A.5
  • 44
    • 0025850663 scopus 로고
    • African swine fever virus attachment protein
    • Carrascosa AL, Sastre I, Vinuela E, (1991) African swine fever virus attachment protein. J Virol 65: 2283-2289.
    • (1991) J Virol , vol.65 , pp. 2283-2289
    • Carrascosa, A.L.1    Sastre, I.2    Vinuela, E.3
  • 45
    • 77952710490 scopus 로고    scopus 로고
    • Vaccinia virus strains use distinct forms of macropinocytosis for host-cell entry
    • Mercer J, Knebel S, Schmidt FI, Crouse J, Burkard C, et al. (2010) Vaccinia virus strains use distinct forms of macropinocytosis for host-cell entry. Proc Natl Acad Sci U S A 107: 9346-9351.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 9346-9351
    • Mercer, J.1    Knebel, S.2    Schmidt, F.I.3    Crouse, J.4    Burkard, C.5
  • 46
    • 80052264028 scopus 로고    scopus 로고
    • Vaccinia extracellular virions enter cells by macropinocytosis and acid-activated membrane rupture
    • Schmidt FI, Bleck CK, Helenius A, Mercer J, (2011) Vaccinia extracellular virions enter cells by macropinocytosis and acid-activated membrane rupture. EMBO J 30: 3647-3661.
    • (2011) EMBO J , vol.30 , pp. 3647-3661
    • Schmidt, F.I.1    Bleck, C.K.2    Helenius, A.3    Mercer, J.4
  • 47
    • 78149301316 scopus 로고    scopus 로고
    • Cellular entry of ebola virus involves uptake by a macropinocytosis-like mechanism and subsequent trafficking through early and late endosomes
    • Saeed MF, Kolokoltsov AA, Albrecht T, Davey RA, (2010) Cellular entry of ebola virus involves uptake by a macropinocytosis-like mechanism and subsequent trafficking through early and late endosomes. PLoS Pathog 6: e1001110.
    • (2010) PLoS Pathog , vol.6
    • Saeed, M.F.1    Kolokoltsov, A.A.2    Albrecht, T.3    Davey, R.A.4
  • 48
    • 65349165676 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus utilizes an actin polymerization-dependent macropinocytic pathway to enter human dermal microvascular endothelial and human umbilical vein endothelial cells
    • Raghu H, Sharma-Walia N, Veettil MV, Sadagopan S, Chandran B, (2009) Kaposi's sarcoma-associated herpesvirus utilizes an actin polymerization-dependent macropinocytic pathway to enter human dermal microvascular endothelial and human umbilical vein endothelial cells. J Virol 83: 4895-4911.
    • (2009) J Virol , vol.83 , pp. 4895-4911
    • Raghu, H.1    Sharma-Walia, N.2    Veettil, M.V.3    Sadagopan, S.4    Chandran, B.5
  • 51
    • 13444281919 scopus 로고    scopus 로고
    • Blebbistatin and blebbistatin-inactivated myosin II inhibit myosin II-independent processes in Dictyostelium
    • Shu S, Liu X, Korn ED, (2005) Blebbistatin and blebbistatin-inactivated myosin II inhibit myosin II-independent processes in Dictyostelium. Proc Natl Acad Sci U S A 102: 1472-1477.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 1472-1477
    • Shu, S.1    Liu, X.2    Korn, E.D.3
  • 52
    • 55549131537 scopus 로고    scopus 로고
    • The Diaphanous-related Formin FHOD1 associates with ROCK1 and promotes Src-dependent plasma membrane blebbing
    • Hannemann S, Madrid R, Stastna J, Kitzing T, Gasteier J, et al. (2008) The Diaphanous-related Formin FHOD1 associates with ROCK1 and promotes Src-dependent plasma membrane blebbing. J Biol Chem 283: 27891-27903.
    • (2008) J Biol Chem , vol.283 , pp. 27891-27903
    • Hannemann, S.1    Madrid, R.2    Stastna, J.3    Kitzing, T.4    Gasteier, J.5
  • 53
    • 77149129342 scopus 로고    scopus 로고
    • Amiloride inhibits macropinocytosis by lowering submembranous pH and preventing Rac1 and Cdc42 signaling
    • Koivusalo M, Welch C, Hayashi H, Scott CC, Kim M, et al. (2010) Amiloride inhibits macropinocytosis by lowering submembranous pH and preventing Rac1 and Cdc42 signaling. J Cell Biol 188: 547-563.
    • (2010) J Cell Biol , vol.188 , pp. 547-563
    • Koivusalo, M.1    Welch, C.2    Hayashi, H.3    Scott, C.C.4    Kim, M.5
  • 54
    • 0038121757 scopus 로고    scopus 로고
    • An overview of inhibitors of Na(+)/H(+) exchanger
    • Masereel B, Pochet L, Laeckmann D, (2003) An overview of inhibitors of Na(+)/H(+) exchanger. Eur J Med Chem 38: 547-554.
    • (2003) Eur J Med Chem , vol.38 , pp. 547-554
    • Masereel, B.1    Pochet, L.2    Laeckmann, D.3
  • 55
    • 0024836461 scopus 로고
    • Distinct endocytotic pathways in epidermal growth factor-stimulated human carcinoma A431 cells
    • West MA, Bretscher MS, Watts C, (1989) Distinct endocytotic pathways in epidermal growth factor-stimulated human carcinoma A431 cells. J Cell Biol 109: 2731-2739.
    • (1989) J Cell Biol , vol.109 , pp. 2731-2739
    • West, M.A.1    Bretscher, M.S.2    Watts, C.3
  • 56
    • 0022459110 scopus 로고
    • Localization of structural proteins in African swine fever virus particles by immunoelectron microscopy
    • Carrascosa JL, Gonzalez P, Carrascosa AL, Garcia-Barreno B, Enjuanes L, et al. (1986) Localization of structural proteins in African swine fever virus particles by immunoelectron microscopy. J Virol 58: 377-384.
    • (1986) J Virol , vol.58 , pp. 377-384
    • Carrascosa, J.L.1    Gonzalez, P.2    Carrascosa, A.L.3    Garcia-Barreno, B.4    Enjuanes, L.5
  • 57
    • 0027463702 scopus 로고
    • High-level expression in Escherichia coli of the gene coding for the major structural protein (p72) of African swine fever virus
    • Freije JM, Munoz M, Vinuela E, Lopez-Otin C, (1993) High-level expression in Escherichia coli of the gene coding for the major structural protein (p72) of African swine fever virus. Gene 123: 259-262.
    • (1993) Gene , vol.123 , pp. 259-262
    • Freije, J.M.1    Munoz, M.2    Vinuela, E.3    Lopez-Otin, C.4
  • 58
    • 0027419556 scopus 로고
    • Sequence and characterization of the major early phosphoprotein p32 of African swine fever virus
    • Prados FJ, Vinuela E, Alcami A, (1993) Sequence and characterization of the major early phosphoprotein p32 of African swine fever virus. J Virol 67: 2475-2485.
    • (1993) J Virol , vol.67 , pp. 2475-2485
    • Prados, F.J.1    Vinuela, E.2    Alcami, A.3
  • 60
    • 0022487140 scopus 로고
    • African swine fever virus-induced polypeptides in Vero cells
    • Santaren JF, Vinuela E, (1986) African swine fever virus-induced polypeptides in Vero cells. Virus Res 5: 391-405.
    • (1986) Virus Res , vol.5 , pp. 391-405
    • Santaren, J.F.1    Vinuela, E.2
  • 61
    • 34548172649 scopus 로고    scopus 로고
    • Macropinocytosis: searching for an endocytic identity and role in the uptake of cell penetrating peptides
    • Jones AT, (2007) Macropinocytosis: searching for an endocytic identity and role in the uptake of cell penetrating peptides. J Cell Mol Med 11: 670-684.
    • (2007) J Cell Mol Med , vol.11 , pp. 670-684
    • Jones, A.T.1
  • 62
    • 63049113263 scopus 로고    scopus 로고
    • Defining macropinocytosis
    • Kerr MC, Teasdale RD, (2009) Defining macropinocytosis. Traffic 10: 364-371.
    • (2009) Traffic , vol.10 , pp. 364-371
    • Kerr, M.C.1    Teasdale, R.D.2
  • 63
    • 0016366562 scopus 로고
    • Action of cytochalasin D on cells of established lines. I. Early events
    • Miranda AF, Godman GC, Deitch AD, Tanenbaum SW, (1974) Action of cytochalasin D on cells of established lines. I. Early events. J Cell Biol 61: 481-500.
    • (1974) J Cell Biol , vol.61 , pp. 481-500
    • Miranda, A.F.1    Godman, G.C.2    Deitch, A.D.3    Tanenbaum, S.W.4
  • 64
    • 0016234522 scopus 로고
    • Action of cytochalasin D on cells of established lines. II. Cortex and microfilaments
    • Miranda AF, Godman GC, Tanenbaum SW, (1974) Action of cytochalasin D on cells of established lines. II. Cortex and microfilaments. J Cell Biol 62: 406-423.
    • (1974) J Cell Biol , vol.62 , pp. 406-423
    • Miranda, A.F.1    Godman, G.C.2    Tanenbaum, S.W.3
  • 65
    • 0023142377 scopus 로고
    • Inhibition of actin polymerization by latrunculin A
    • Coue M, Brenner SL, Spector I, Korn ED, (1987) Inhibition of actin polymerization by latrunculin A. FEBS Lett 213: 316-318.
    • (1987) FEBS Lett , vol.213 , pp. 316-318
    • Coue, M.1    Brenner, S.L.2    Spector, I.3    Korn, E.D.4
  • 66
    • 0030727217 scopus 로고    scopus 로고
    • Jasplakinolide, a novel actin targeting peptide, inhibits cell growth and induces actin filament polymerization in the green alga Micrasterias
    • Holzinger A, Meindl U, (1997) Jasplakinolide, a novel actin targeting peptide, inhibits cell growth and induces actin filament polymerization in the green alga Micrasterias. Cell Motil Cytoskeleton 38: 365-372.
    • (1997) Cell Motil Cytoskeleton , vol.38 , pp. 365-372
    • Holzinger, A.1    Meindl, U.2
  • 67
    • 0025731586 scopus 로고
    • Effects of cytochalasin, phalloidin, and pH on the elongation of actin filaments
    • Sampath P, Pollard TD, (1991) Effects of cytochalasin, phalloidin, and pH on the elongation of actin filaments. Biochemistry 30: 1973-1980.
    • (1991) Biochemistry , vol.30 , pp. 1973-1980
    • Sampath, P.1    Pollard, T.D.2
  • 70
    • 0030920202 scopus 로고    scopus 로고
    • Nanomolar concentrations of nocodazole alter microtubule dynamic instability in vivo and in vitro
    • Vasquez RJ, Howell B, Yvon AM, Wadsworth P, Cassimeris L, (1997) Nanomolar concentrations of nocodazole alter microtubule dynamic instability in vivo and in vitro. Mol Biol Cell 8: 973-985.
    • (1997) Mol Biol Cell , vol.8 , pp. 973-985
    • Vasquez, R.J.1    Howell, B.2    Yvon, A.M.3    Wadsworth, P.4    Cassimeris, L.5
  • 71
    • 3242707647 scopus 로고    scopus 로고
    • Transport of African swine fever virus from assembly sites to the plasma membrane is dependent on microtubules and conventional kinesin
    • Jouvenet N, Monaghan P, Way M, Wileman T, (2004) Transport of African swine fever virus from assembly sites to the plasma membrane is dependent on microtubules and conventional kinesin. J Virol 78: 7990-8001.
    • (2004) J Virol , vol.78 , pp. 7990-8001
    • Jouvenet, N.1    Monaghan, P.2    Way, M.3    Wileman, T.4
  • 72
    • 0035972239 scopus 로고    scopus 로고
    • Aggresomes resemble sites specialized for virus assembly
    • Heath CM, Windsor M, Wileman T, (2001) Aggresomes resemble sites specialized for virus assembly. J Cell Biol 153: 449-455.
    • (2001) J Cell Biol , vol.153 , pp. 449-455
    • Heath, C.M.1    Windsor, M.2    Wileman, T.3
  • 73
    • 0018581544 scopus 로고
    • Rapid stimulation of pinocytosis in human carcinoma cells A-431 by epidermal growth factor
    • Haigler HT, McKanna JA, Cohen S, (1979) Rapid stimulation of pinocytosis in human carcinoma cells A-431 by epidermal growth factor. J Cell Biol 83: 82-90.
    • (1979) J Cell Biol , vol.83 , pp. 82-90
    • Haigler, H.T.1    McKanna, J.A.2    Cohen, S.3
  • 74
    • 33644542081 scopus 로고    scopus 로고
    • Discovery of EGFR selective 4,6-disubstituted pyrimidines from a combinatorial kinase-directed heterocycle library
    • Zhang Q, Liu Y, Gao F, Ding Q, Cho C, et al. (2006) Discovery of EGFR selective 4,6-disubstituted pyrimidines from a combinatorial kinase-directed heterocycle library. J Am Chem Soc 128: 2182-2183.
    • (2006) J Am Chem Soc , vol.128 , pp. 2182-2183
    • Zhang, Q.1    Liu, Y.2    Gao, F.3    Ding, Q.4    Cho, C.5
  • 75
    • 0023664272 scopus 로고
    • Genistein, a specific inhibitor of tyrosine-specific protein kinases
    • Akiyama T, Ishida J, Nakagawa S, Ogawara H, Watanabe S, et al. (1987) Genistein, a specific inhibitor of tyrosine-specific protein kinases. J Biol Chem 262: 5592-5595.
    • (1987) J Biol Chem , vol.262 , pp. 5592-5595
    • Akiyama, T.1    Ishida, J.2    Nakagawa, S.3    Ogawara, H.4    Watanabe, S.5
  • 77
    • 33947718766 scopus 로고    scopus 로고
    • Phosphoinositide metabolism during membrane ruffling and macropinosome formation in EGF-stimulated A431 cells
    • Araki N, Egami Y, Watanabe Y, Hatae T, (2007) Phosphoinositide metabolism during membrane ruffling and macropinosome formation in EGF-stimulated A431 cells. Exp Cell Res 313: 1496-1507.
    • (2007) Exp Cell Res , vol.313 , pp. 1496-1507
    • Araki, N.1    Egami, Y.2    Watanabe, Y.3    Hatae, T.4
  • 78
    • 0030459125 scopus 로고    scopus 로고
    • A role for phosphoinositide 3-kinase in the completion of macropinocytosis and phagocytosis by macrophages
    • Araki N, Johnson MT, Swanson JA, (1996) A role for phosphoinositide 3-kinase in the completion of macropinocytosis and phagocytosis by macrophages. J Cell Biol 135: 1249-1260.
    • (1996) J Cell Biol , vol.135 , pp. 1249-1260
    • Araki, N.1    Johnson, M.T.2    Swanson, J.A.3
  • 79
    • 33645078650 scopus 로고    scopus 로고
    • Regulation of membrane traffic by phosphoinositide 3-kinases
    • Lindmo K, Stenmark H, (2006) Regulation of membrane traffic by phosphoinositide 3-kinases. J Cell Sci 119: 605-614.
    • (2006) J Cell Sci , vol.119 , pp. 605-614
    • Lindmo, K.1    Stenmark, H.2
  • 81
    • 0033634827 scopus 로고    scopus 로고
    • Structural determinants of phosphoinositide 3-kinase inhibition by wortmannin, LY294002, quercetin, myricetin, and staurosporine
    • Walker EH, Pacold ME, Perisic O, Stephens L, Hawkins PT, et al. (2000) Structural determinants of phosphoinositide 3-kinase inhibition by wortmannin, LY294002, quercetin, myricetin, and staurosporine. Mol Cell 6: 909-919.
    • (2000) Mol Cell , vol.6 , pp. 909-919
    • Walker, E.H.1    Pacold, M.E.2    Perisic, O.3    Stephens, L.4    Hawkins, P.T.5
  • 82
    • 2442686585 scopus 로고    scopus 로고
    • The pivotal role of phosphatidylinositol 3-kinase-Akt signal transduction in virus survival
    • Cooray S, (2004) The pivotal role of phosphatidylinositol 3-kinase-Akt signal transduction in virus survival. J Gen Virol 85: 1065-1076.
    • (2004) J Gen Virol , vol.85 , pp. 1065-1076
    • Cooray, S.1
  • 83
    • 0029804116 scopus 로고    scopus 로고
    • Mechanism of activation of protein kinase B by insulin and IGF-1
    • Alessi DR, Andjelkovic M, Caudwell B, Cron P, Morrice N, et al. (1996) Mechanism of activation of protein kinase B by insulin and IGF-1. EMBO J 15: 6541-6551.
    • (1996) EMBO J , vol.15 , pp. 6541-6551
    • Alessi, D.R.1    Andjelkovic, M.2    Caudwell, B.3    Cron, P.4    Morrice, N.5
  • 84
    • 17044393948 scopus 로고    scopus 로고
    • Regulation of Akt/PKB Ser473 phosphorylation
    • Bayascas JR, Alessi DR, (2005) Regulation of Akt/PKB Ser473 phosphorylation. Mol Cell 18: 143-145.
    • (2005) Mol Cell , vol.18 , pp. 143-145
    • Bayascas, J.R.1    Alessi, D.R.2
  • 85
    • 13844312400 scopus 로고    scopus 로고
    • Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
    • Sarbassov DD, Guertin DA, Ali SM, Sabatini DM, (2005) Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex. Science 307: 1098-1101.
    • (2005) Science , vol.307 , pp. 1098-1101
    • Sarbassov, D.D.1    Guertin, D.A.2    Ali, S.M.3    Sabatini, D.M.4
  • 86
    • 40949116686 scopus 로고    scopus 로고
    • The TORrid affairs of viruses: effects of mammalian DNA viruses on the PI3K-Akt-mTOR signalling pathway
    • Buchkovich NJ, Yu Y, Zampieri CA, Alwine JC, (2008) The TORrid affairs of viruses: effects of mammalian DNA viruses on the PI3K-Akt-mTOR signalling pathway. Nat Rev Microbiol 6: 266-275.
    • (2008) Nat Rev Microbiol , vol.6 , pp. 266-275
    • Buchkovich, N.J.1    Yu, Y.2    Zampieri, C.A.3    Alwine, J.C.4
  • 87
    • 0026654125 scopus 로고
    • The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
    • Ridley AJ, Paterson HF, Johnston CL, Diekmann D, Hall A, (1992) The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell 70: 401-410.
    • (1992) Cell , vol.70 , pp. 401-410
    • Ridley, A.J.1    Paterson, H.F.2    Johnston, C.L.3    Diekmann, D.4    Hall, A.5
  • 89
    • 0028078824 scopus 로고
    • A brain serine/threonine protein kinase activated by Cdc42 and Rac1
    • Manser E, Leung T, Salihuddin H, Zhao ZS, Lim L, (1994) A brain serine/threonine protein kinase activated by Cdc42 and Rac1. Nature 367: 40-46.
    • (1994) Nature , vol.367 , pp. 40-46
    • Manser, E.1    Leung, T.2    Salihuddin, H.3    Zhao, Z.S.4    Lim, L.5
  • 91
    • 2442664118 scopus 로고    scopus 로고
    • Rational design and characterization of a Rac GTPase-specific small molecule inhibitor
    • Gao Y, Dickerson JB, Guo F, Zheng J, Zheng Y, (2004) Rational design and characterization of a Rac GTPase-specific small molecule inhibitor. Proc Natl Acad Sci U S A 101: 7618-7623.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 7618-7623
    • Gao, Y.1    Dickerson, J.B.2    Guo, F.3    Zheng, J.4    Zheng, Y.5
  • 92
    • 41949113636 scopus 로고    scopus 로고
    • A Raft-derived, Pak1-regulated entry participates in alpha2beta1 integrin-dependent sorting to caveosomes
    • Karjalainen M, Kakkonen E, Upla P, Paloranta H, Kankaanpaa P, et al. (2008) A Raft-derived, Pak1-regulated entry participates in alpha2beta1 integrin-dependent sorting to caveosomes. Mol Biol Cell 19: 2857-2869.
    • (2008) Mol Biol Cell , vol.19 , pp. 2857-2869
    • Karjalainen, M.1    Kakkonen, E.2    Upla, P.3    Paloranta, H.4    Kankaanpaa, P.5
  • 94
    • 0032748298 scopus 로고    scopus 로고
    • Identification of a central phosphorylation site in p21-activated kinase regulating autoinhibition and kinase activity
    • Zenke FT, King CC, Bohl BP, Bokoch GM, (1999) Identification of a central phosphorylation site in p21-activated kinase regulating autoinhibition and kinase activity. J Biol Chem 274: 32565-32573.
    • (1999) J Biol Chem , vol.274 , pp. 32565-32573
    • Zenke, F.T.1    King, C.C.2    Bohl, B.P.3    Bokoch, G.M.4
  • 95
    • 41949100602 scopus 로고    scopus 로고
    • An isoform-selective, small-molecule inhibitor targets the autoregulatory mechanism of p21-activated kinase
    • Deacon SW, Beeser A, Fukui JA, Rennefahrt UE, Myers C, et al. (2008) An isoform-selective, small-molecule inhibitor targets the autoregulatory mechanism of p21-activated kinase. Chem Biol 15: 322-331.
    • (2008) Chem Biol , vol.15 , pp. 322-331
    • Deacon, S.W.1    Beeser, A.2    Fukui, J.A.3    Rennefahrt, U.E.4    Myers, C.5
  • 96
    • 0742288598 scopus 로고    scopus 로고
    • The dynamin superfamily: universal membrane tubulation and fission molecules?
    • Praefcke GJ, McMahon HT, (2004) The dynamin superfamily: universal membrane tubulation and fission molecules? Nat Rev Mol Cell Biol 5: 133-147.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 133-147
    • Praefcke, G.J.1    McMahon, H.T.2
  • 98
    • 0027520440 scopus 로고
    • Mis-assembly of clathrin lattices on endosomes reveals a regulatory switch for coated pit formation
    • Wang LH, Rothberg KG, Anderson RG, (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
  • 99
    • 33845209963 scopus 로고    scopus 로고
    • Effects of Na+/H+ exchanger inhibitors on subcellular localisation of endocytic organelles and intracellular dynamics of protein transduction domains HIV-TAT peptide and octaarginine
    • Fretz M, Jin J, Conibere R, Penning NA, Al-Taei S, et al. (2006) Effects of Na+/H+ exchanger inhibitors on subcellular localisation of endocytic organelles and intracellular dynamics of protein transduction domains HIV-TAT peptide and octaarginine. J Control Release 116: 247-254.
    • (2006) J Control Release , vol.116 , pp. 247-254
    • Fretz, M.1    Jin, J.2    Conibere, R.3    Penning, N.A.4    Al-Taei, S.5
  • 100
    • 0042668823 scopus 로고    scopus 로고
    • Adenovirus endocytosis
    • Meier O, Greber UF, (2003) Adenovirus endocytosis. J Gene Med 5: 451-462.
    • (2003) J Gene Med , vol.5 , pp. 451-462
    • Meier, O.1    Greber, U.F.2
  • 101
    • 4644298997 scopus 로고    scopus 로고
    • Adenovirus endocytosis
    • Meier O, Greber UF, (2004) Adenovirus endocytosis. J Gene Med 6 (Suppl 1): S152-163.
    • (2004) J Gene Med , vol.6 , Issue.SUPPL. 1
    • Meier, O.1    Greber, U.F.2
  • 103
    • 0031663239 scopus 로고    scopus 로고
    • Adenovirus endocytosis requires actin cytoskeleton reorganization mediated by Rho family GTPases
    • Li E, Stupack D, Bokoch GM, Nemerow GR, (1998) Adenovirus endocytosis requires actin cytoskeleton reorganization mediated by Rho family GTPases. J Virol 72: 8806-8812.
    • (1998) J Virol , vol.72 , pp. 8806-8812
    • Li, E.1    Stupack, D.2    Bokoch, G.M.3    Nemerow, G.R.4
  • 104
    • 84857097606 scopus 로고    scopus 로고
    • Small rho GTPases and cholesterol biosynthetic pathway intermediates in African swine fever virus infection
    • Quetglas JI, Hernaez B, Galindo I, Munoz-Moreno R, Cuesta-Geijo MA, et al. (2011) Small rho GTPases and cholesterol biosynthetic pathway intermediates in African swine fever virus infection. J Virol 86: 1758-1767.
    • (2011) J Virol , vol.86 , pp. 1758-1767
    • Quetglas, J.I.1    Hernaez, B.2    Galindo, I.3    Munoz-Moreno, R.4    Cuesta-Geijo, M.A.5
  • 105
    • 41949093447 scopus 로고    scopus 로고
    • The closure of Pak1-dependent macropinosomes requires the phosphorylation of CtBP1/BARS
    • Liberali P, Kakkonen E, Turacchio G, Valente C, Spaar A, et al. (2008) The closure of Pak1-dependent macropinosomes requires the phosphorylation of CtBP1/BARS. EMBO J 27: 970-981.
    • (2008) EMBO J , vol.27 , pp. 970-981
    • Liberali, P.1    Kakkonen, E.2    Turacchio, G.3    Valente, C.4    Spaar, A.5
  • 106
    • 82655173730 scopus 로고    scopus 로고
    • AMP-activated protein kinase enhances the phagocytic ability of macrophages and neutrophils
    • Bae HB, Zmijewski JW, Deshane JS, Tadie JM, Chaplin DD, et al. (2011) AMP-activated protein kinase enhances the phagocytic ability of macrophages and neutrophils. FASEB J 25: 4358-4368.
    • (2011) FASEB J , vol.25 , pp. 4358-4368
    • Bae, H.B.1    Zmijewski, J.W.2    Deshane, J.S.3    Tadie, J.M.4    Chaplin, D.D.5
  • 107
    • 12844287455 scopus 로고    scopus 로고
    • Cdc42 and RhoB activation are required for mannose receptor-mediated phagocytosis by human alveolar macrophages
    • Zhang J, Zhu J, Bu X, Cushion M, Kinane TB, et al. (2005) Cdc42 and RhoB activation are required for mannose receptor-mediated phagocytosis by human alveolar macrophages. Mol Biol Cell 16: 824-834.
    • (2005) Mol Biol Cell , vol.16 , pp. 824-834
    • Zhang, J.1    Zhu, J.2    Bu, X.3    Cushion, M.4    Kinane, T.B.5
  • 108
    • 0022530266 scopus 로고
    • Glycosylated components of African swine fever virus particles
    • del Val M, Carrascosa JL, Vinuela E, (1986) Glycosylated components of African swine fever virus particles. Virology 152: 39-49.
    • (1986) Virology , vol.152 , pp. 39-49
    • del Val, M.1    Carrascosa, J.L.2    Vinuela, E.3
  • 109
    • 77649197259 scopus 로고    scopus 로고
    • Early events in Kaposi's sarcoma-associated herpesvirus infection of target cells
    • Chandran B, (2010) Early events in Kaposi's sarcoma-associated herpesvirus infection of target cells. J Virol 84: 2188-2199.
    • (2010) J Virol , vol.84 , pp. 2188-2199
    • Chandran, B.1
  • 110
    • 84863246380 scopus 로고    scopus 로고
    • Structure of an Antibody in Complex with Its Mucin Domain Linear Epitope That Is Protective against Ebola Virus
    • Olal D, Kuehne AI, Bale S, Halfmann P, Hashiguchi T, et al. (2012) Structure of an Antibody in Complex with Its Mucin Domain Linear Epitope That Is Protective against Ebola Virus. J Virol 86: 2809-2816.
    • (2012) J Virol , vol.86 , pp. 2809-2816
    • Olal, D.1    Kuehne, A.I.2    Bale, S.3    Halfmann, P.4    Hashiguchi, T.5
  • 111
    • 78049274849 scopus 로고    scopus 로고
    • Cell adhesion-dependent membrane trafficking of a binding partner for the ebolavirus glycoprotein is a determinant of viral entry
    • Dube D, Schornberg KL, Shoemaker CJ, Delos SE, Stantchev TS, et al. (2010) Cell adhesion-dependent membrane trafficking of a binding partner for the ebolavirus glycoprotein is a determinant of viral entry. Proc Natl Acad Sci U S A 107: 16637-16642.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 16637-16642
    • Dube, D.1    Schornberg, K.L.2    Shoemaker, C.J.3    Delos, S.E.4    Stantchev, T.S.5
  • 112
    • 0033429706 scopus 로고    scopus 로고
    • Participation of dynamin in the biogenesis of cytoplasmic vesicles
    • Henley JR, Cao H, McNiven MA, (1999) Participation of dynamin in the biogenesis of cytoplasmic vesicles. FASEB J 13 (Suppl 2): S243-247.
    • (1999) FASEB J , vol.13 , Issue.SUPPL. 2
    • Henley, J.R.1    Cao, H.2    McNiven, M.A.3
  • 114
    • 33745026786 scopus 로고    scopus 로고
    • GTP-dependent twisting of dynamin implicates constriction and tension in membrane fission
    • Roux A, Uyhazi K, Frost A, De Camilli P, (2006) GTP-dependent twisting of dynamin implicates constriction and tension in membrane fission. Nature 441: 528-531.
    • (2006) Nature , vol.441 , pp. 528-531
    • Roux, A.1    Uyhazi, K.2    Frost, A.3    de Camilli, P.4
  • 115
    • 84934436076 scopus 로고    scopus 로고
    • Pharmacological inhibition of endocytic pathways: is it specific enough to be useful?
    • Ivanov AI, (2008) Pharmacological inhibition of endocytic pathways: is it specific enough to be useful? Methods Mol Biol 440: 15-33.
    • (2008) Methods Mol Biol , vol.440 , pp. 15-33
    • Ivanov, A.I.1


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