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Volumn 1, Issue , 2013, Pages

Virus entry and uncoating

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EID: 84974698845     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (17)

References (220)
  • 1
    • 0024370460 scopus 로고
    • A putative murine ecotropic retrovirus receptor gene codes a multiple membrane spanning protein and confers susceptibility to virus infection
    • Albritton LM, Tseng L, Scadden D, et al. A putative murine ecotropic retrovirus receptor gene codes a multiple membrane spanning protein and confers susceptibility to virus infection. Cell 1989;57:659-666.
    • (1989) Cell , vol.57 , pp. 659-666
    • Albritton, L.M.1    Tseng, L.2    Scadden, D.3
  • 2
    • 0030018156 scopus 로고    scopus 로고
    • CC CKR5: a RANTES, MIP-1alpha, MIP-1beta receptor as a fusion cofactor for macrophage-tropic HIV-1
    • Alkhatib G, Combadiere C, Broder CC, et al. CC CKR5: a RANTES, MIP-1alpha, MIP-1beta receptor as a fusion cofactor for macrophage-tropic HIV-1. Science 1996;272:1955-1958.
    • (1996) Science , vol.272 , pp. 1955-1958
    • Alkhatib, G.1    Combadiere, C.2    Broder, C.C.3
  • 3
    • 1842293926 scopus 로고    scopus 로고
    • A new SIV co-receptor, STRL33
    • Alkhatib G, Liao F, Berger EA, et al. A new SIV co-receptor, STRL33. Nature 1997;388:238.
    • (1997) Nature , vol.388 , pp. 238
    • Alkhatib, G.1    Liao, F.2    Berger, E.A.3
  • 4
    • 41949139871 scopus 로고    scopus 로고
    • Subversion of CtBP1-controlled macropinocytosis by human adenovirus serotype 3
    • Amstutz B, Gastaldelli M, Kalin S, et al. Subversion of CtBP1-controlled macropinocytosis by human adenovirus serotype 3. EMBO J 2008;27:956-969.
    • (2008) EMBO J , vol.27 , pp. 956-969
    • Amstutz, B.1    Gastaldelli, M.2    Kalin, S.3
  • 5
    • 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 HA, Chen Y, Norkin LC. Bound simian virus 40 translocates to caveolin-enriched membrane domains, and its entry is inhibited by drugs that selectively disrupt caveolae. Mol Biol Cell 1996;7:1825-1834.
    • (1996) Mol Biol Cell , vol.7 , pp. 1825-1834
    • Anderson, H.A.1    Chen, Y.2    Norkin, L.C.3
  • 6
    • 77953076127 scopus 로고    scopus 로고
    • Proteoglycans in host-pathogen interactions: molecular mechanisms and therapeutic implications
    • Bartlett AH, Park PW. Proteoglycans in host-pathogen interactions: molecular mechanisms and therapeutic implications. Expert Rev Mol Med 2010;12:e5.
    • (2010) Expert Rev Mol Med , vol.12 , pp. e5
    • Bartlett, A.H.1    Park, P.W.2
  • 7
    • 0027421873 scopus 로고
    • A receptor for subgroup A Rous sarcoma virus is related to the low density lipoprotein receptor
    • Bates P, Young JA, Varmus HE. A receptor for subgroup A Rous sarcoma virus is related to the low density lipoprotein receptor. Cell 1993;74:1043-1051.
    • (1993) Cell , vol.74 , pp. 1043-1051
    • Bates, P.1    Young, J.A.2    Varmus, H.E.3
  • 8
    • 0033573904 scopus 로고    scopus 로고
    • A human cell-surface receptor for xenotropic and polytropic murine leukemia viruses: possible role in G protein-coupled signal transduction
    • Battini JL, Rasko JE, Miller AD. A human cell-surface receptor for xenotropic and polytropic murine leukemia viruses: possible role in G protein-coupled signal transduction. Proc Natl Acad Sci U S A 1999;96:1385-1390.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 1385-1390
    • Battini, J.L.1    Rasko, J.E.2    Miller, A.D.3
  • 9
    • 0041694394 scopus 로고    scopus 로고
    • Virus interactions with mucosal surfaces: alternative receptors, alternative pathways
    • Bergelson JM. Virus interactions with mucosal surfaces: alternative receptors, alternative pathways. Curr Opin Microbiol 2003;6:386-391.
    • (2003) Curr Opin Microbiol , vol.6 , pp. 386-391
    • Bergelson, J.M.1
  • 10
    • 0031052263 scopus 로고    scopus 로고
    • Isolation of a common receptor for coxsackie B viruses and adenoviruses 2 and 5
    • Bergelson JM, Cunningham JA, Droguett G, et al. Isolation of a common receptor for coxsackie B viruses and adenoviruses 2 and 5. Science 1997;275:1320-1323.
    • (1997) Science , vol.275 , pp. 1320-1323
    • Bergelson, J.M.1    Cunningham, J.A.2    Droguett, G.3
  • 11
    • 0028795653 scopus 로고
    • Coxsackievirus B3 adapted to growth in RD cells binds to decay-accelerating factor (CD55)
    • Bergelson JM, Mohanty JG, Crowell RL, et al. Coxsackievirus B3 adapted to growth in RD cells binds to decay-accelerating factor (CD55). J Virol 1995;69:1903-1906.
    • (1995) J Virol , vol.69 , pp. 1903-1906
    • Bergelson, J.M.1    Mohanty, J.G.2    Crowell, R.L.3
  • 12
    • 0026580865 scopus 로고
    • Identification of the integrin VLA-2 as a receptor for echovirus 1
    • Bergelson JM, Shepley MP, Chan BM, et al. Identification of the integrin VLA-2 as a receptor for echovirus 1. Science 1992;255:1718-1720.
    • (1992) Science , vol.255 , pp. 1718-1720
    • Bergelson, J.M.1    Shepley, M.P.2    Chan, B.M.3
  • 13
    • 0033012398 scopus 로고    scopus 로고
    • Chemokine receptors as HIV-1 coreceptors: roles in viral entry, tropism, and disease
    • Berger EA, Murphy PM, Farber JM. Chemokine receptors as HIV-1 coreceptors: roles in viral entry, tropism, and disease. Annu Rev Immunol 1999;17:657-700.
    • (1999) Annu Rev Immunol , vol.17 , pp. 657-700
    • Berger, E.A.1    Murphy, P.M.2    Farber, J.M.3
  • 14
    • 0028904534 scopus 로고
    • Antibodies to the vitronectin receptor (integrin alpha V beta 3) inhibit binding and infection of foot-and-mouth disease virus to cultured cells
    • Berinstein A, Roivainen M, Hovi T, et al. Antibodies to the vitronectin receptor (integrin alpha V beta 3) inhibit binding and infection of foot-and-mouth disease virus to cultured cells. J Virol 1995;69:2664-2666.
    • (1995) J Virol , vol.69 , pp. 2664-2666
    • Berinstein, A.1    Roivainen, M.2    Hovi, T.3
  • 15
    • 0033584785 scopus 로고    scopus 로고
    • Structural analysis of the mechanism of adenovirus binding to its human cellular receptor, CAR
    • Bewley MC, Springer K, Zhang YB, et al. Structural analysis of the mechanism of adenovirus binding to its human cellular receptor, CAR. Science 1999;286:1579-1583.
    • (1999) Science , vol.286 , pp. 1579-1583
    • Bewley, M.C.1    Springer, K.2    Zhang, Y.B.3
  • 17
    • 0030606315 scopus 로고    scopus 로고
    • CAR1, a TNFR-related protein, is a cellular receptor for cytopathic avian leukosis-sarcoma viruses and mediates apoptosis
    • Brojatsch J, Naughton J, Rolls MM, et al. CAR1, a TNFR-related protein, is a cellular receptor for cytopathic avian leukosis-sarcoma viruses and mediates apoptosis. Cell 1996;87:845-855.
    • (1996) Cell , vol.87 , pp. 845-855
    • Brojatsch, J.1    Naughton, J.2    Rolls, M.M.3
  • 18
    • 17044373783 scopus 로고    scopus 로고
    • The structure of the poliovirus 135S cell entry intermediate at 10-angstrom resolution reveals the location of an externalized polypeptide that binds to membranes
    • Bubeck D, Filman DJ, Cheng N, et al. The structure of the poliovirus 135S cell entry intermediate at 10-angstrom resolution reveals the location of an externalized polypeptide that binds to membranes. J Virol 2005;79:7745-7755.
    • (2005) J Virol , vol.79 , pp. 7745-7755
    • Bubeck, D.1    Filman, D.J.2    Cheng, N.3
  • 19
    • 22144468063 scopus 로고    scopus 로고
    • Cryo-electron microscopy reconstruction of a poliovirus-receptor-membrane complex
    • Bubeck D, Filman DJ, Hogle JM. Cryo-electron microscopy reconstruction of a poliovirus-receptor-membrane complex. Nat Struct Mol Biol 2005;12:615-618.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 615-618
    • Bubeck, D.1    Filman, D.J.2    Hogle, J.M.3
  • 20
    • 0029861558 scopus 로고    scopus 로고
    • The effect of M1 protein and low pH on nuclear import of influenza virus vRNPs
    • Bui M, Whittaker G, Helenius A. The effect of M1 protein and low pH on nuclear import of influenza virus vRNPs. J Virol 1996;70:8391-8401.
    • (1996) J Virol , vol.70 , pp. 8391-8401
    • Bui, M.1    Whittaker, G.2    Helenius, A.3
  • 21
    • 0020315175 scopus 로고
    • Influenza virus uncoating in infected cells and effect of rimatidine
    • Bukrinskaya AG, Vorkunova NK, Kornilayeva GV, et al. Influenza virus uncoating in infected cells and effect of rimatidine. J Gen Virol 1982;60:49-59.
    • (1982) J Gen Virol , vol.60 , pp. 49-59
    • Bukrinskaya, A.G.1    Vorkunova, N.K.2    Kornilayeva, G.V.3
  • 22
    • 0033989275 scopus 로고    scopus 로고
    • Large-plaque mutants of Sindbis virus show reduced binding to heparan sulfate, heightened viremia, and slower clearance from the circulation
    • Byrnes AP, Griffin DE. Large-plaque mutants of Sindbis virus show reduced binding to heparan sulfate, heightened viremia, and slower clearance from the circulation. J Virol 2000;74:644-651.
    • (2000) J Virol , vol.74 , pp. 644-651
    • Byrnes, A.P.1    Griffin, D.E.2
  • 23
    • 36348932884 scopus 로고    scopus 로고
    • N-glycolyl GM1 ganglioside as a receptor for simian virus 40
    • Campanero-Rhodes MA, Smith A, Chai W, et al. N-glycolyl GM1 ganglioside as a receptor for simian virus 40. J Virol 2007;81:12846-12858.
    • (2007) J Virol , vol.81 , pp. 12846-12858
    • Campanero-Rhodes, M.A.1    Smith, A.2    Chai, W.3
  • 24
    • 0032509177 scopus 로고    scopus 로고
    • Identification of alpha-dystroglycan as a receptor for lymphocytic choriomeningitis virus and Lassa fever virus [see comments]
    • Cao W, Henry MD, Borrow P, et al. Identification of alpha-dystroglycan as a receptor for lymphocytic choriomeningitis virus and Lassa fever virus [see comments]. Science 1998;282:2079-2081.
    • (1998) Science , vol.282 , pp. 2079-2081
    • Cao, W.1    Henry, M.D.2    Borrow, P.3
  • 25
    • 0025832880 scopus 로고
    • The CD4-gp120 interaction and AIDS pathogenesis
    • Capon DJ, Ward RH. The CD4-gp120 interaction and AIDS pathogenesis. Annu Rev Immunol 1991;9:649-678.
    • (1991) Annu Rev Immunol , vol.9 , pp. 649-678
    • Capon, D.J.1    Ward, R.H.2
  • 26
    • 0034892857 scopus 로고    scopus 로고
    • Herpes simplex virus glycoprotein D bound to the human receptor HveA
    • Carfi A, Willis SH, Whitbeck JC, et al. Herpes simplex virus glycoprotein D bound to the human receptor HveA. Mol Cell 2001;8:169-179.
    • (2001) Mol Cell , vol.8 , pp. 169-179
    • Carfi, A.1    Willis, S.H.2    Whitbeck, J.C.3
  • 27
    • 0027253445 scopus 로고
    • A spring-loaded mechanism for the conformational change of influenza hemagglutinin
    • Carr CM, Kim PS. A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell 1993;73:823-832.
    • (1993) Cell , vol.73 , pp. 823-832
    • Carr, C.M.1    Kim, P.S.2
  • 28
    • 77649197259 scopus 로고    scopus 로고
    • Early events in Kaposi's sarcoma-associated herpesvirus infection of target cells
    • Chandran B. Early events in Kaposi's sarcoma-associated herpesvirus infection of target cells. J Virol 2010;84:2188-2199.
    • (2010) J Virol , vol.84 , pp. 2188-2199
    • Chandran, B.1
  • 29
    • 0036776328 scopus 로고    scopus 로고
    • Strategy for nonenveloped virus entry: a hydrophobic conformer of the reovirus membrane penetration protein micro 1 mediates membrane disruption
    • Chandran K, Farsetta DL, Nibert ML. Strategy for nonenveloped virus entry: a hydrophobic conformer of the reovirus membrane penetration protein micro 1 mediates membrane disruption. J Virol 2002;76:9920-9933.
    • (2002) J Virol , vol.76 , pp. 9920-9933
    • Chandran, K.1    Farsetta, D.L.2    Nibert, M.L.3
  • 30
    • 19144365133 scopus 로고    scopus 로고
    • Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection
    • Chandran K, Sullivan NJ, Felbor U, et al. Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection. Science 2005;308:1643-1645.
    • (2005) Science , vol.308 , pp. 1643-1645
    • Chandran, K.1    Sullivan, N.J.2    Felbor, U.3
  • 31
    • 45849151106 scopus 로고    scopus 로고
    • Genomic RNAi screening in Drosophila S2 cells: what have we learned about host-pathogen interactions?
    • Cherry S. Genomic RNAi screening in Drosophila S2 cells: what have we learned about host-pathogen interactions? Curr Opin Microbiol 2008;11:262-270.
    • (2008) Curr Opin Microbiol , vol.11 , pp. 262-270
    • Cherry, S.1
  • 32
    • 0005014748 scopus 로고    scopus 로고
    • The beta-chemokine receptors CCR3 and CCR5 facilitate infection by primary HIV-1 isolates
    • Choe H, Farzan M, Sun Y, et al. The beta-chemokine receptors CCR3 and CCR5 facilitate infection by primary HIV-1 isolates. Cell 1996;85:1135-1148.
    • (1996) Cell , vol.85 , pp. 1135-1148
    • Choe, H.1    Farzan, M.2    Sun, Y.3
  • 33
    • 0001818698 scopus 로고
    • Replication of paramyxoviruses
    • Fraenkel-Conrat H, Wagner RR, eds., New York: Plenum
    • Choppin PW, Compans RW. Replication of paramyxoviruses. In: Fraenkel-Conrat H, Wagner RR, eds. Comprehensive Virology, Vol. 4. New York: Plenum; 1975:94-178.
    • (1975) Comprehensive Virology , vol.4 , pp. 94-178
    • Choppin, P.W.1    Compans, R.W.2
  • 34
  • 35
    • 77949424084 scopus 로고    scopus 로고
    • Systems survey of endocytosis by multiparametric image analysis
    • Collinet C, Stoter M, Bradshaw CR, et al. Systems survey of endocytosis by multiparametric image analysis. Nature 2010;464:243-249.
    • (2010) Nature , vol.464 , pp. 243-249
    • Collinet, C.1    Stoter, M.2    Bradshaw, C.R.3
  • 36
    • 0015414910 scopus 로고
    • Structure of the ribonucleoprotein of influenza virus
    • Compans RW, Content J, Duesberg PH. Structure of the ribonucleoprotein of influenza virus. J Virol 1972;10:795-800.
    • (1972) J Virol , vol.10 , pp. 795-800
    • Compans, R.W.1    Content, J.2    Duesberg, P.H.3
  • 37
    • 0037422066 scopus 로고    scopus 로고
    • Regulated portals of entry into the cell
    • Conner SD, Schmid SL. Regulated portals of entry into the cell. Nature 2003;422:37-44.
    • (2003) Nature , vol.422 , pp. 37-44
    • Conner, S.D.1    Schmid, S.L.2
  • 38
    • 34548250956 scopus 로고    scopus 로고
    • Parvoviral host range and cell entry mechanisms
    • Cotmore SF, Tattersall P. Parvoviral host range and cell entry mechanisms. Adv Virus Res 2007;70:183-232.
    • (2007) Adv Virus Res , vol.70 , pp. 183-232
    • Cotmore, S.F.1    Tattersall, P.2
  • 39
    • 30344475861 scopus 로고    scopus 로고
    • Virus-induced Abl and Fyn kinase signals permit coxsackievirus entry through epithelial tight junctions
    • Coyne CB, Bergelson JM. Virus-induced Abl and Fyn kinase signals permit coxsackievirus entry through epithelial tight junctions. Cell 2006;124:119-131.
    • (2006) Cell , vol.124 , pp. 119-131
    • Coyne, C.B.1    Bergelson, J.M.2
  • 40
    • 0035875067 scopus 로고    scopus 로고
    • Journey to the center of the cell
    • Cullen B. Journey to the center of the cell. Cell 2001;105:697-700.
    • (2001) Cell , vol.105 , pp. 697-700
    • Cullen, B.1
  • 41
    • 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, et al. Vesicular stomatitis virus enters cells through vesicles incompletely coated with clathrin that depend upon actin for internalization. PLoS Pathog 2009;5:e1000394.
    • (2009) PLoS Pathog , vol.5 , pp. e1000394
    • Cureton, D.K.1    Massol, R.H.2    Saffarian, S.3
  • 42
    • 13744252968 scopus 로고    scopus 로고
    • Involvement of clathrin-mediated endocytosis in human immunodeficiency virus type 1 entry
    • Daecke J, Fackler OT, Dittmar MT, et al. Involvement of clathrin-mediated endocytosis in human immunodeficiency virus type 1 entry. J Virol 2005;79:1581-1594.
    • (2005) J Virol , vol.79 , pp. 1581-1594
    • Daecke, J.1    Fackler, O.T.2    Dittmar, M.T.3
  • 43
    • 0015829192 scopus 로고
    • Early events in cell-animal virus interactions
    • Dales S. Early events in cell-animal virus interactions. Bacteriol Rev 1973;37:103-135.
    • (1973) Bacteriol Rev , vol.37 , pp. 103-135
    • Dales, S.1
  • 44
    • 13444273098 scopus 로고    scopus 로고
    • Clathrin- and caveolin-1-independent endocytosis: entry of simian virus 40 into cells devoid of caveolae
    • Damm EM, Pelkmans L, Kartenbeck J, et al. Clathrin- and caveolin-1-independent endocytosis: entry of simian virus 40 into cells devoid of caveolae. J Cell Biol 2005;168:477-488.
    • (2005) J Cell Biol , vol.168 , pp. 477-488
    • Damm, E.M.1    Pelkmans, L.2    Kartenbeck, J.3
  • 45
    • 21244468590 scopus 로고    scopus 로고
    • Viral stop-and-go along microtubules: taking a ride with dynein and kinesins
    • Dohner K, Nagel CH, Sodeik B. Viral stop-and-go along microtubules: taking a ride with dynein and kinesins. Trends Microbiol 2005;13:320-327.
    • (2005) Trends Microbiol , vol.13 , pp. 320-327
    • Dohner, K.1    Nagel, C.H.2    Sodeik, B.3
  • 46
    • 56949091061 scopus 로고    scopus 로고
    • Clathrin-independent endocytosis: a unique platform for cell signaling and PM remodeling
    • Donaldson JG, Porat-Shliom N, Cohen LA. Clathrin-independent endocytosis: a unique platform for cell signaling and PM remodeling. Cell Signal 2009;21:1-6.
    • (2009) Cell Signal , vol.21 , pp. 1-6
    • Donaldson, J.G.1    Porat-Shliom, N.2    Cohen, L.A.3
  • 47
    • 0030604727 scopus 로고    scopus 로고
    • A dual-tropic primary HIV-1 isolate that uses fusin and the beta-chemokine receptors CKR-5, CKR-3, and CKR-2b as fusion cofactors
    • Doranz BJ, Rucker J, Yi Y, et al. A dual-tropic primary HIV-1 isolate that uses fusin and the beta-chemokine receptors CKR-5, CKR-3, and CKR-2b as fusion cofactors. Cell 1996;85:1149-1158.
    • (1996) Cell , vol.85 , pp. 1149-1158
    • Doranz, B.J.1    Rucker, J.2    Yi, Y.3
  • 48
    • 0027426010 scopus 로고
    • The human CD46 molecule is a receptor for measles virus (Edmonston strain)
    • Dorig RE, Marcil A, Chopra A, et al. The human CD46 molecule is a receptor for measles virus (Edmonston strain). Cell 1993;75:295-305.
    • (1993) Cell , vol.75 , pp. 295-305
    • Dorig, R.E.1    Marcil, A.2    Chopra, A.3
  • 49
    • 0025723997 scopus 로고
    • Cloning of the mouse hepatitis virus (MHV) receptor: expression in human and hamster cell lines confers susceptibility to MHV
    • Dveksler GS, Pensiero MN, Cardellichio CB, et al. Cloning of the mouse hepatitis virus (MHV) receptor: expression in human and hamster cell lines confers susceptibility to MHV. J Virol 1991;65:6881-6891.
    • (1991) J Virol , vol.65 , pp. 6881-6891
    • Dveksler, G.S.1    Pensiero, M.N.2    Cardellichio, C.B.3
  • 50
    • 4444224966 scopus 로고    scopus 로고
    • Endocytosis by random initiation and stabilization of clathrin-coated pits
    • Ehrlich M, Boll W, Van Oijen A, et al. Endocytosis by random initiation and stabilization of clathrin-coated pits. Cell 2004;118:591-605.
    • (2004) Cell , vol.118 , pp. 591-605
    • Ehrlich, M.1    Boll, W.2    Van Oijen, A.3
  • 51
    • 79955436301 scopus 로고    scopus 로고
    • The role of endosomes in SV40 entry and infection
    • Engel S, Heger T, Mancini R, et al. The role of endosomes in SV40 entry and infection. J Virol 2011;85:4198-4211.
    • (2011) J Virol , vol.85 , pp. 4198-4211
    • Engel, S.1    Heger, T.2    Mancini, R.3
  • 52
    • 21244485921 scopus 로고    scopus 로고
    • The effect of cellular receptor diffusion on receptor-mediated viral binding using Brownian adhesive dynamics (BRAD) simulations
    • English TJ, Hammer DA. The effect of cellular receptor diffusion on receptor-mediated viral binding using Brownian adhesive dynamics (BRAD) simulations. Biophys J 2005;88:1666-1675.
    • (2005) Biophys J , vol.88 , pp. 1666-1675
    • English, T.J.1    Hammer, D.A.2
  • 53
    • 84862989117 scopus 로고    scopus 로고
    • GM1 structure determines SV40-induced membrane invagination and infection
    • Ewers H, Römer W, Smith AE, et al. GM1 structure determines SV40-induced membrane invagination and infection. Nat Cell Biol 2010;12:11-18.
    • (2010) Nat Cell Biol , vol.12 , pp. 11-18
    • Ewers, H.1    Römer, W.2    Smith, A.E.3
  • 54
    • 27244450483 scopus 로고    scopus 로고
    • Single-particle tracking of murine polyoma virus-like particles on live cells and artificial membranes
    • Ewers H, Smith AE, Sbalzarini IF, et al. Single-particle tracking of murine polyoma virus-like particles on live cells and artificial membranes. Proc Natl Acad Sci U S A 2005;102:15110-15115.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 15110-15115
    • Ewers, H.1    Smith, A.E.2    Sbalzarini, I.F.3
  • 55
    • 0031849291 scopus 로고    scopus 로고
    • The role of phosphatidylserine in recognition of apoptotic cells by phagocytes
    • Fadok VA, Bratton DL, Frasch SC, et al. The role of phosphatidylserine in recognition of apoptotic cells by phagocytes. Cell Death Differ 1998;5:551-562.
    • (1998) Cell Death Differ , vol.5 , pp. 551-562
    • Fadok, V.A.1    Bratton, D.L.2    Frasch, S.C.3
  • 56
    • 0030749247 scopus 로고    scopus 로고
    • Two orphan seven-transmembrane segment receptors which are expressed in CD4-positive cells support simian immunodeficiency virus infection
    • Farzan M, Choe H, Martin K, et al. Two orphan seven-transmembrane segment receptors which are expressed in CD4-positive cells support simian immunodeficiency virus infection. J Exp Med 1997;186:405-411.
    • (1997) J Exp Med , vol.186 , pp. 405-411
    • Farzan, M.1    Choe, H.2    Martin, K.3
  • 57
    • 0035824446 scopus 로고    scopus 로고
    • Structural basis for selective recognition of oligosaccharides by DC-SIGN and DC-SIGNR
    • Feinberg H, Mitchell DA, Drickamer K, et al. Structural basis for selective recognition of oligosaccharides by DC-SIGN and DC-SIGNR. Science 2001;294:2163-2166.
    • (2001) Science , vol.294 , pp. 2163-2166
    • Feinberg, H.1    Mitchell, D.A.2    Drickamer, K.3
  • 58
    • 7444256550 scopus 로고    scopus 로고
    • Cellular integrins function as entry receptors for human cytomegalovirus via a highly conserved disintegrin-like domain
    • Feire AL, Koss H, Compton T. Cellular integrins function as entry receptors for human cytomegalovirus via a highly conserved disintegrin-like domain. Proc Natl Acad Sci U S A 2004;101:15470-15475.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 15470-15475
    • Feire, A.L.1    Koss, H.2    Compton, T.3
  • 59
    • 0342437200 scopus 로고
    • Epstein-Barr virus receptor of human B lymphocytes is the C3d receptor CR2
    • Fingeroth JD, Weis JJ, Tedder TF, et al. Epstein-Barr virus receptor of human B lymphocytes is the C3d receptor CR2. Proc Natl Acad Sci U S A 1984;81:4510-4514.
    • (1984) Proc Natl Acad Sci U S A , vol.81 , pp. 4510-4514
    • Fingeroth, J.D.1    Weis, J.J.2    Tedder, T.F.3
  • 60
    • 0021928143 scopus 로고
    • gp140, the C3d receptor of human B lymphocytes, is also the Epstein-Barr virus receptor
    • Frade R, Barel M, Ehlin-Henriksson B, et al. gp140, the C3d receptor of human B lymphocytes, is also the Epstein-Barr virus receptor. Proc Natl Acad Sci U S A 1985;82:1490-1493.
    • (1985) Proc Natl Acad Sci U S A , vol.82 , pp. 1490-1493
    • Frade, R.1    Barel, M.2    Ehlin-Henriksson, B.3
  • 61
    • 0025273268 scopus 로고
    • Cell-induced conformational change in poliovirus: externalization of the amino terminus of VP1 is responsible for liposome binding
    • Fricks CE, Hogle JM. Cell-induced conformational change in poliovirus: externalization of the amino terminus of VP1 is responsible for liposome binding. J Virol 1990;64:1934-1945.
    • (1990) J Virol , vol.64 , pp. 1934-1945
    • Fricks, C.E.1    Hogle, J.M.2
  • 62
    • 0035182168 scopus 로고    scopus 로고
    • Surfing pathogens and the lessons learned for actin polymerization
    • Frischknecht F, Way M. Surfing pathogens and the lessons learned for actin polymerization. Trends Cell Biol 2001;11:30-38.
    • (2001) Trends Cell Biol , vol.11 , pp. 30-38
    • Frischknecht, F.1    Way, M.2
  • 63
    • 64049113389 scopus 로고    scopus 로고
    • Site of human rhinovirus RNA uncoating revealed by fluorescent in situ hybridization
    • Brabec-Zaruba M, Pfanzagl B, et al. Site of human rhinovirus RNA uncoating revealed by fluorescent in situ hybridization. J Virol. 2009:83:3770-3777.
    • (2009) J Virol. , vol.83 , pp. 3770-3777
    • Brabec-Zaruba, M.1    Pfanzagl, B.2
  • 64
    • 77956625541 scopus 로고    scopus 로고
    • Uncoating of human rhinoviruses
    • Fuchs R, Blaas D. Uncoating of human rhinoviruses. Rev Med Virol 2010;20:281-297.
    • (2010) Rev Med Virol , vol.20 , pp. 281-297
    • Fuchs, R.1    Blaas, D.2
  • 65
    • 0032499532 scopus 로고    scopus 로고
    • beta3 Integrins mediate the cellular entry of hantaviruses that cause respiratory failure
    • Gavrilovskaya IN, Shepley M, Shaw R, et al. beta3 Integrins mediate the cellular entry of hantaviruses that cause respiratory failure. Proc Natl Acad Sci U S A 1998;95:7074-7079.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 7074-7079
    • Gavrilovskaya, I.N.1    Shepley, M.2    Shaw, R.3
  • 66
    • 0034598905 scopus 로고    scopus 로고
    • DC-SIGN, a dendritic cell-specific HIV-1-binding protein that enhances trans-infection of T cells
    • Geijtenbeek TB, Kwon DS, Torensma R, et al. DC-SIGN, a dendritic cell-specific HIV-1-binding protein that enhances trans-infection of T cells. Cell 2000;100:587-597.
    • (2000) Cell , vol.100 , pp. 587-597
    • Geijtenbeek, T.B.1    Kwon, D.S.2    Torensma, R.3
  • 67
    • 0032486317 scopus 로고    scopus 로고
    • Entry of alphaherpesviruses mediated by poliovirus receptor-related protein 1 and poliovirus receptor
    • Geraghty RJ, Krummenacher C, Cohen GH, et al. Entry of alphaherpesviruses mediated by poliovirus receptor-related protein 1 and poliovirus receptor. Science 1998;280:1618-1620.
    • (1998) Science , vol.280 , pp. 1618-1620
    • Geraghty, R.J.1    Krummenacher, C.2    Cohen, G.H.3
  • 68
    • 0036233715 scopus 로고    scopus 로고
    • Signalling in viral entry
    • Greber U. Signalling in viral entry. Cell Mol Life Sci 2002;59:608-626.
    • (2002) Cell Mol Life Sci , vol.59 , pp. 608-626
    • Greber, U.1
  • 69
    • 0038187637 scopus 로고    scopus 로고
    • Nuclear import of viral DNA genomes
    • Greber UF, Fassati A. Nuclear import of viral DNA genomes. Traffic 2003;4:136-143.
    • (2003) Traffic , vol.4 , pp. 136-143
    • Greber, U.F.1    Fassati, A.2
  • 70
    • 32944475622 scopus 로고    scopus 로고
    • A superhighway to virus infection
    • Greber UF, Way M. A superhighway to virus infection. Cell 2006;124:741-754.
    • (2006) Cell , vol.124 , pp. 741-754
    • Greber, U.F.1    Way, M.2
  • 71
    • 0024542689 scopus 로고
    • The major human rhinovirus receptor is ICAM-1
    • Greve JM, Davis G, Meyer AM, et al. The major human rhinovirus receptor is ICAM-1. Cell 1989;56:839-847.
    • (1989) Cell , vol.56 , pp. 839-847
    • Greve, J.M.1    Davis, G.2    Meyer, A.M.3
  • 72
    • 67949124782 scopus 로고    scopus 로고
    • Viruses and endosome membrane dynamics
    • Gruenberg J. Viruses and endosome membrane dynamics. Curr Opin Cell Biol 2009;21:582-588.
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 582-588
    • Gruenberg, J.1
  • 73
    • 1842784049 scopus 로고    scopus 로고
    • The biogenesis of multivesicular endosomes
    • Gruenberg J, Stenmark H. The biogenesis of multivesicular endosomes. Nat Rev Mol Cell Biol 2004;5:317-323.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 317-323
    • Gruenberg, J.1    Stenmark, H.2
  • 74
    • 43049089793 scopus 로고    scopus 로고
    • The parvovirus capsid odyssey: from the cell surface to the nucleus
    • Harbison CE, Chiorini JA, Parrish CR. The parvovirus capsid odyssey: from the cell surface to the nucleus. Trends Microbiol 2008;16:208-214.
    • (2008) Trends Microbiol , vol.16 , pp. 208-214
    • Harbison, C.E.1    Chiorini, J.A.2    Parrish, C.R.3
  • 75
    • 0034905041 scopus 로고    scopus 로고
    • The machinery for flavivirus fusion with host cell membranes
    • Heinz FX, Allison SL. The machinery for flavivirus fusion with host cell membranes. Curr Opin Microbiol 2001;4:450-455.
    • (2001) Curr Opin Microbiol , vol.4 , pp. 450-455
    • Heinz, F.X.1    Allison, S.L.2
  • 76
    • 0018853517 scopus 로고
    • On the entry of Semliki forest virus into BHK-21 cells
    • Helenius A, Kartenbeck J, Simons K, et al. On the entry of Semliki forest virus into BHK-21 cells. J Cell Biol 1980;84:404-420.
    • (1980) J Cell Biol , vol.84 , pp. 404-420
    • Helenius, A.1    Kartenbeck, J.2    Simons, K.3
  • 77
    • 65849206909 scopus 로고    scopus 로고
    • Shape reconstruction of subcellular structures from live cell fluorescence microscopy images
    • Helmuth JA, Burckhardt CJ, Greber UF, et al. Shape reconstruction of subcellular structures from live cell fluorescence microscopy images. J Struct Biol 2009;167:1-10.
    • (2009) J Struct Biol , vol.167 , pp. 1-10
    • Helmuth, J.A.1    Burckhardt, C.J.2    Greber, U.F.3
  • 78
    • 0033622332 scopus 로고    scopus 로고
    • Integrins alpha2beta1 and alpha4beta1 can mediate SA11 rotavirus attachment and entry into cells
    • Hewish MJ, Takada Y, Coulson BS. Integrins alpha2beta1 and alpha4beta1 can mediate SA11 rotavirus attachment and entry into cells. J Virol 2000;74:228-236.
    • (2000) J Virol , vol.74 , pp. 228-236
    • Hewish, M.J.1    Takada, Y.2    Coulson, B.S.3
  • 79
    • 77951138358 scopus 로고    scopus 로고
    • The use of RNAi-based screens to identify host proteins involved in viral replication
    • Hirsch AJ. The use of RNAi-based screens to identify host proteins involved in viral replication. Future Microbiol 2010;5:303-311.
    • (2010) Future Microbiol , vol.5 , pp. 303-311
    • Hirsch, A.J.1
  • 80
    • 0028262187 scopus 로고
    • Members of the low density lipoprotein receptor family mediate cell entry of a minor-group common cold virus
    • Hofer F, Gruenberger M, Kowalski H, et al. Members of the low density lipoprotein receptor family mediate cell entry of a minor-group common cold virus. Proc Natl Acad Sci U S A 1994;91:1839-1842.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 1839-1842
    • Hofer, F.1    Gruenberger, M.2    Kowalski, H.3
  • 81
    • 0036403802 scopus 로고    scopus 로고
    • Poliovirus cell entry: common structural themes in viral cell entry pathways
    • Hogle JM. Poliovirus cell entry: common structural themes in viral cell entry pathways. Annu Rev Microbiol 2002;56:677-702.
    • (2002) Annu Rev Microbiol , vol.56 , pp. 677-702
    • Hogle, J.M.1
  • 82
    • 80052233389 scopus 로고    scopus 로고
    • Endosome maturation
    • Huotari J, Helenius A. Endosome maturation. EMBO J 2011;30:3481-3500.
    • (2011) EMBO J , vol.30 , pp. 3481-3500
    • Huotari, J.1    Helenius, A.2
  • 83
    • 0242515763 scopus 로고    scopus 로고
    • Spread of HTLV-I between lymphocytes by virus-induced polarization of the cytoskeleton
    • Igakura T, Stinchcombe JC, Goon PK, et al. Spread of HTLV-I between lymphocytes by virus-induced polarization of the cytoskeleton. Science 2003;299:1713-1716.
    • (2003) Science , vol.299 , pp. 1713-1716
    • Igakura, T.1    Stinchcombe, J.C.2    Goon, P.K.3
  • 84
    • 0034010674 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus is a ligand for the high-affinity binding conformation of integrin alpha5beta1: influence of the leucine residue within the RGDL motif on selectivity of integrin binding
    • Jackson T, Blakemore W, Newman JW, et al. Foot-and-mouth disease virus is a ligand for the high-affinity binding conformation of integrin alpha5beta1: influence of the leucine residue within the RGDL motif on selectivity of integrin binding. J Gen Virol 2000;81:1383-1391.
    • (2000) J Gen Virol , vol.81 , pp. 1383-1391
    • Jackson, T.1    Blakemore, W.2    Newman, J.W.3
  • 85
    • 58149390171 scopus 로고    scopus 로고
    • Host cell factors and functions involved in vesicular stomatitis virus entry
    • Johannsdottir HK, Mancini R, Kartenbeck J, et al. Host cell factors and functions involved in vesicular stomatitis virus entry. J Virol 2009;83:440-453.
    • (2009) J Virol , vol.83 , pp. 440-453
    • Johannsdottir, H.K.1    Mancini, R.2    Kartenbeck, J.3
  • 86
    • 0033526096 scopus 로고    scopus 로고
    • Phosphorylation-dependent binding of Hepatitis B virus core particles to the nuclear pore complex
    • Kann M, Sodeik B, Vlachou A, et al. Phosphorylation-dependent binding of Hepatitis B virus core particles to the nuclear pore complex. J Cell Biol 1999;145:45-55.
    • (1999) J Cell Biol , vol.145 , pp. 45-55
    • Kann, M.1    Sodeik, B.2    Vlachou, A.3
  • 87
    • 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, et al. A Raft-derived, Pak1-regulated entry participates in alpha2beta1 integrin-dependent sorting to caveosomes. Mol Biol Cell 2008;19:2857-2869.
    • (2008) Mol Biol Cell , vol.19 , pp. 2857-2869
    • Karjalainen, M.1    Kakkonen, E.2    Upla, P.3
  • 88
    • 0014966066 scopus 로고
    • Ribonucleic acid synthesis in vaccnina virus. I. The mechanism of synthesis and release of RNA in vaccinia cores
    • Kates J, Beeson J. Ribonucleic acid synthesis in vaccnina virus. I. The mechanism of synthesis and release of RNA in vaccinia cores. J Mol Biol 1970;50:1-18.
    • (1970) J Mol Biol , vol.50 , pp. 1-18
    • Kates, J.1    Beeson, J.2
  • 89
    • 1842457821 scopus 로고    scopus 로고
    • Monitoring RNA release from human rhinovirus by dynamic force microscopy
    • Kienberger F, Zhu R, Moser R, et al. Monitoring RNA release from human rhinovirus by dynamic force microscopy. J Virol 2004;78:3203-3209.
    • (2004) J Virol , vol.78 , pp. 3203-3209
    • Kienberger, F.1    Zhu, R.2    Moser, R.3
  • 90
    • 0016679968 scopus 로고
    • Activation of influenza A viruses by trypsin treatment
    • Klenk HD, Rott R, Orlich M, et al. Activation of influenza A viruses by trypsin treatment. Virology 1975;68:426-439.
    • (1975) Virology , vol.68 , pp. 426-439
    • Klenk, H.D.1    Rott, R.2    Orlich, M.3
  • 91
    • 0242363253 scopus 로고    scopus 로고
    • DC-SIGN and L-SIGN can act as attachment receptors for alphaviruses and distinguish between mosquito cell- and mammalian cell-derived viruses
    • Klimstra WB, Nangle EM, Smith MS, et al. DC-SIGN and L-SIGN can act as attachment receptors for alphaviruses and distinguish between mosquito cell- and mammalian cell-derived viruses. J Virol 2003;77:12022-12032.
    • (2003) J Virol , vol.77 , pp. 12022-12032
    • Klimstra, W.B.1    Nangle, E.M.2    Smith, M.S.3
  • 92
    • 34447273317 scopus 로고    scopus 로고
    • Small interfering RNA profiling reveals key role of clathrin-mediated endocytosis and early endosome formation for infection by respiratory syncytial virus
    • Kolokoltsov AA, Deniger D, Fleming EH, et al. Small interfering RNA profiling reveals key role of clathrin-mediated endocytosis and early endosome formation for infection by respiratory syncytial virus. J Virol 2007;81:7786-7800.
    • (2007) J Virol , vol.81 , pp. 7786-7800
    • Kolokoltsov, A.A.1    Deniger, D.2    Fleming, E.H.3
  • 93
    • 0036172314 scopus 로고    scopus 로고
    • DC-SIGN-mediated internalization of HIV is required for trans-enhancement of T cell infection
    • Kwon DS, Gregorio G, Bitton N, et al. DC-SIGN-mediated internalization of HIV is required for trans-enhancement of T cell infection. Immunity 2002;16:135-144.
    • (2002) Immunity , vol.16 , pp. 135-144
    • Kwon, D.S.1    Gregorio, G.2    Bitton, N.3
  • 94
    • 34548150618 scopus 로고    scopus 로고
    • Regulation of raft-dependent endocytosis
    • Lajoie P, Nabi IR. Regulation of raft-dependent endocytosis. J Cell Mol Med 2007;11:644-653.
    • (2007) J Cell Mol Med , vol.11 , pp. 644-653
    • Lajoie, P.1    Nabi, I.R.2
  • 96
    • 22944446447 scopus 로고    scopus 로고
    • Actin- and myosin-driven movement of viruses along filopodia precedes their entry into cells
    • Lehmann MJ, Sherer NM, Marks CB, et al. Actin- and myosin-driven movement of viruses along filopodia precedes their entry into cells. J Cell Biol 2005;170:317-325.
    • (2005) J Cell Biol , vol.170 , pp. 317-325
    • Lehmann, M.J.1    Sherer, N.M.2    Marks, C.B.3
  • 97
    • 0028055281 scopus 로고
    • Passage through mitosis is required for oncoretroviruses but not for the human immunodeficiency virus
    • Lewis PF, Emerman M. Passage through mitosis is required for oncoretroviruses but not for the human immunodeficiency virus. J Virol 1994;68:510-516.
    • (1994) J Virol , vol.68 , pp. 510-516
    • Lewis, P.F.1    Emerman, M.2
  • 98
    • 55849137214 scopus 로고    scopus 로고
    • Protein kinases: starting a molecular systems view of endocytosis
    • Liberali P, Ramo P, Pelkmans L. Protein kinases: starting a molecular systems view of endocytosis. Annu Rev Cell Dev Biol 2008;24:501-523.
    • (2008) Annu Rev Cell Dev Biol , vol.24 , pp. 501-523
    • Liberali, P.1    Ramo, P.2    Pelkmans, L.3
  • 99
    • 12644278319 scopus 로고    scopus 로고
    • TYMSTR, a putative chemokine receptor selectively expressed in activated T cells, exhibits HIV-1 coreceptor function
    • Loetscher M, Amara A, Oberlin E, et al. TYMSTR, a putative chemokine receptor selectively expressed in activated T cells, exhibits HIV-1 coreceptor function. Curr Biol 1997;7:652-660.
    • (1997) Curr Biol , vol.7 , pp. 652-660
    • Loetscher, M.1    Amara, A.2    Oberlin, E.3
  • 100
    • 0016363888 scopus 로고
    • Early interaction between animal viruses and cells
    • Lonberg-Holm K, Philipson L. Early interaction between animal viruses and cells. Monogr Virol 1974;9:1-149.
    • (1974) Monogr Virol , vol.9 , pp. 1-149
    • Lonberg-Holm, K.1    Philipson, L.2
  • 103
    • 0038165533 scopus 로고    scopus 로고
    • DC-SIGN and L-SIGN are high affinity binding receptors for hepatitis C virus glycoprotein E2
    • Lozach PY, Lortat-Jacob H, de Lacroix de Lavalette A, et al. DC-SIGN and L-SIGN are high affinity binding receptors for hepatitis C virus glycoprotein E2. J Biol Chem 2003;278:20358-20366.
    • (2003) J Biol Chem , vol.278 , pp. 20358-20366
    • Lozach, P.Y.1    Lortat-Jacob, H.2    de Lacroix de Lavalette, A.3
  • 104
    • 0028271684 scopus 로고
    • CD4 is a critical component of the receptor for human herpesvirus 7: interference with human immunodeficiency virus
    • Lusso P, Secchiero P, Crowley RW, et al. CD4 is a critical component of the receptor for human herpesvirus 7: interference with human immunodeficiency virus. Proc Natl Acad Sci U S A 1994;91:3872-3876.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 3872-3876
    • Lusso, P.1    Secchiero, P.2    Crowley, R.W.3
  • 105
    • 60049098650 scopus 로고    scopus 로고
    • Herpesvirus interactions with the host cytoskeleton
    • Lyman MG, Enquist LW. Herpesvirus interactions with the host cytoskeleton. J Virol 2009;83:2058-2066.
    • (2009) J Virol , vol.83 , pp. 2058-2066
    • Lyman, M.G.1    Enquist, L.W.2
  • 106
    • 0023028190 scopus 로고
    • The T4 gene encodes the AIDS virus receptor and is expressed in the immune system and the brain
    • Maddon P, Dalgleish A, McDougal J, et al. The T4 gene encodes the AIDS virus receptor and is expressed in the immune system and the brain. Cell 1986;47:333-348.
    • (1986) Cell , vol.47 , pp. 333-348
    • Maddon, P.1    Dalgleish, A.2    McDougal, J.3
  • 107
    • 0034755158 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 entry into macrophages mediated by macropinocytosis
    • Marechal V, Prevost MC, Petit C, et al. Human immunodeficiency virus type 1 entry into macrophages mediated by macropinocytosis. J Virol 2001;75:11166-11177.
    • (2001) J Virol , vol.75 , pp. 11166-11177
    • Marechal, V.1    Prevost, M.C.2    Petit, C.3
  • 108
    • 0031026138 scopus 로고    scopus 로고
    • SFV infection in CHO cells: cell-type specific restrictions to productive virus entry at the cell surface
    • Marsh M, Bron R. SFV infection in CHO cells: cell-type specific restrictions to productive virus entry at the cell surface. J Cell Sci 1997;110(Pt 1):95-103.
    • (1997) J Cell Sci , vol.110 , Issue.PT 1 , pp. 95-103
    • Marsh, M.1    Bron, R.2
  • 109
    • 0024534779 scopus 로고
    • Virus entry into animal cells
    • Marsh M, Helenius A. Virus entry into animal cells. Adv Virus Res 1989;36:107-151.
    • (1989) Adv Virus Res , vol.36 , pp. 107-151
    • Marsh, M.1    Helenius, A.2
  • 110
    • 32944473016 scopus 로고    scopus 로고
    • Virus entry: open sesame
    • Marsh M, Helenius A. Virus entry: open sesame. Cell 2006;124:729-740.
    • (2006) Cell , vol.124 , pp. 729-740
    • Marsh, M.1    Helenius, A.2
  • 111
    • 0026006258 scopus 로고
    • Nuclear transport of influenza virus ribonucleoproteins: the viral matrix protein (M1) promotes export and inhibits import
    • Martin K, Helenius A. Nuclear transport of influenza virus ribonucleoproteins: the viral matrix protein (M1) promotes export and inhibits import. Cell 1991;67:117-130.
    • (1991) Cell , vol.67 , pp. 117-130
    • Martin, K.1    Helenius, A.2
  • 112
    • 0019814443 scopus 로고
    • Infectious entry pathway of influenza virus in a canine kidney cell line
    • Matlin KS, Reggio H, Helenius A, et al. Infectious entry pathway of influenza virus in a canine kidney cell line. J Cell Biol 1982;91:601-613.
    • (1982) J Cell Biol , vol.91 , pp. 601-613
    • Matlin, K.S.1    Reggio, H.2    Helenius, A.3
  • 113
    • 0019976569 scopus 로고
    • The pathway of vesicular stomatitis virus entry leading to infection
    • Matlin KS, Reggio H, Helenius A, et al. The pathway of vesicular stomatitis virus entry leading to infection. J Mol Biol 1982;156:609-631.
    • (1982) J Mol Biol , vol.156 , pp. 609-631
    • Matlin, K.S.1    Reggio, H.2    Helenius, A.3
  • 114
    • 0018070374 scopus 로고
    • Membrane fusion as a mechanism of Simian Virus 40 entry into different cellular compartments
    • Maul GG, Rovera G, Vorbrodt A, et al. Membrane fusion as a mechanism of Simian Virus 40 entry into different cellular compartments. J Virol 1978;28:936-944.
    • (1978) J Virol , vol.28 , pp. 936-944
    • Maul, G.G.1    Rovera, G.2    Vorbrodt, A.3
  • 115
    • 0031907988 scopus 로고    scopus 로고
    • LIGHT, a new member of the TNF superfamily, and lymphotoxin alpha are ligands for herpesvirus entry mediator
    • Mauri DN, Ebner R, Montgomery RI, et al. LIGHT, a new member of the TNF superfamily, and lymphotoxin alpha are ligands for herpesvirus entry mediator. Immunity 1998;8:21-30.
    • (1998) Immunity , vol.8 , pp. 21-30
    • Mauri, D.N.1    Ebner, R.2    Montgomery, R.I.3
  • 116
    • 34547114456 scopus 로고    scopus 로고
    • Pathways of clathrin-independent endocytosis
    • Mayor S, Pagano RE. Pathways of clathrin-independent endocytosis. Nat Rev Mol Cell Biol 2007;8:603-612.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 603-612
    • Mayor, S.1    Pagano, R.E.2
  • 117
    • 0345283128 scopus 로고    scopus 로고
    • Endocytosis of adenovirus and adenovirus capsid proteins
    • Medina-Kauwe LK. Endocytosis of adenovirus and adenovirus capsid proteins. Adv Drug Deliv Rev 2003;55:1485-1496.
    • (2003) Adv Drug Deliv Rev , vol.55 , pp. 1485-1496
    • Medina-Kauwe, L.K.1
  • 118
    • 0037119944 scopus 로고    scopus 로고
    • Adenovirus triggers macropinocytosis and endosomal leakage together with its clathrin-mediated uptake
    • Meier O, Boucke K, Hammer SV, et al. Adenovirus triggers macropinocytosis and endosomal leakage together with its clathrin-mediated uptake. J Cell Biol 2002;158:1119-1131.
    • (2002) J Cell Biol , vol.158 , pp. 1119-1131
    • Meier, O.1    Boucke, K.2    Hammer, S.V.3
  • 119
    • 0042668823 scopus 로고    scopus 로고
    • Adenovirus endocytosis
    • Meier O, Greber UF. Adenovirus endocytosis. J Gene Med 2003;5:451-462.
    • (2003) J Gene Med , vol.5 , pp. 451-462
    • Meier, O.1    Greber, U.F.2
  • 120
    • 0029752791 scopus 로고    scopus 로고
    • Endocytosis and molecular sorting
    • Mellman I. Endocytosis and molecular sorting. Annu Rev Cell Dev Biol 1996;12:575-625.
    • (1996) Annu Rev Cell Dev Biol , vol.12 , pp. 575-625
    • Mellman, I.1
  • 121
    • 0024519677 scopus 로고
    • Cellular receptor for poliovirus: molecular cloning, nucleotide sequence, and expression of a new member of the immunoglobulin superfamily
    • Mendelsohn CL, Wimmer E, Racaniello VR. Cellular receptor for poliovirus: molecular cloning, nucleotide sequence, and expression of a new member of the immunoglobulin superfamily. Cell 1989;56:855-865.
    • (1989) Cell , vol.56 , pp. 855-865
    • Mendelsohn, C.L.1    Wimmer, E.2    Racaniello, V.R.3
  • 122
    • 42549153337 scopus 로고    scopus 로고
    • Vaccinia virus uses macropinocytosis and apoptotic mimicry to enter host cells
    • Mercer J, Helenius A. Vaccinia virus uses macropinocytosis and apoptotic mimicry to enter host cells. Science 2008;320:531-535.
    • (2008) Science , vol.320 , pp. 531-535
    • Mercer, J.1    Helenius, A.2
  • 123
    • 65449120034 scopus 로고    scopus 로고
    • Virus entry by macropinocytosis
    • Mercer J, Helenius A. Virus entry by macropinocytosis. Nat Cell Biol 2009;11:510-520.
    • (2009) Nat Cell Biol , vol.11 , pp. 510-520
    • Mercer, J.1    Helenius, A.2
  • 125
    • 0028072043 scopus 로고
    • A family of retroviruses that utilize related phosphate transporters for cell entry
    • Miller D, Miller A. A family of retroviruses that utilize related phosphate transporters for cell entry. J Virol 1994;68:8270-8276.
    • (1994) J Virol , vol.68 , pp. 8270-8276
    • Miller, D.1    Miller, A.2
  • 126
    • 0030972160 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 preintegration complexes: studies of organization and composition
    • Miller M, Farnet C, Bushman F. Human immunodeficiency virus type 1 preintegration complexes: studies of organization and composition. J Virol 1997;71:5382-5390.
    • (1997) J Virol , vol.71 , pp. 5382-5390
    • Miller, M.1    Farnet, C.2    Bushman, F.3
  • 127
    • 0031976829 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 attachment to HeLa CD4 cells is CD4 independent and gp120 dependent and requires cell surface heparans
    • Mondor I, Ugolini S, Sattentau QJ. Human immunodeficiency virus type 1 attachment to HeLa CD4 cells is CD4 independent and gp120 dependent and requires cell surface heparans. J Virol 1998;72:3623-3634.
    • (1998) J Virol , vol.72 , pp. 3623-3634
    • Mondor, I.1    Ugolini, S.2    Sattentau, Q.J.3
  • 128
    • 0033697734 scopus 로고    scopus 로고
    • Retroviral entry mediated by receptor priming and low pH triggering of an envelope glycoprotein
    • Mothes W, Boerger AL, Narayan S, et al. Retroviral entry mediated by receptor priming and low pH triggering of an envelope glycoprotein. Cell 2000;103:679-689.
    • (2000) Cell , vol.103 , pp. 679-689
    • Mothes, W.1    Boerger, A.L.2    Narayan, S.3
  • 129
    • 77956643036 scopus 로고    scopus 로고
    • Virus cell-to-cell transmission
    • Mothes W, Sherer NM, Jin J, et al. Virus cell-to-cell transmission. J Virol 2010;84:8360-8368.
    • (2010) J Virol , vol.84 , pp. 8360-8368
    • Mothes, W.1    Sherer, N.M.2    Jin, J.3
  • 130
    • 79952419255 scopus 로고    scopus 로고
    • Functional genetic and biophysical analyses of membrane disruption by human adenovirus
    • Moyer CL, Wiethoff CM, Maier O, et al. Functional genetic and biophysical analyses of membrane disruption by human adenovirus. J Virol 2011;85:2631-2641.
    • (2011) J Virol , vol.85 , pp. 2631-2641
    • Moyer, C.L.1    Wiethoff, C.M.2    Maier, O.3
  • 131
    • 0034663422 scopus 로고    scopus 로고
    • Cell receptors involved in adenovirus entry
    • Nemerow GR. Cell receptors involved in adenovirus entry. Virology 2000;274:1-4.
    • (2000) Virology , vol.274 , pp. 1-4
    • Nemerow, G.R.1
  • 132
    • 59349116159 scopus 로고    scopus 로고
    • The Polyomaviridae: contributions of virus structure to our understanding of virus receptors and infectious entry
    • Neu U, Stehle T, Atwood WJ. The Polyomaviridae: contributions of virus structure to our understanding of virus receptors and infectious entry. Virology 2009;384:389-399.
    • (2009) Virology , vol.384 , pp. 389-399
    • Neu, U.1    Stehle, T.2    Atwood, W.J.3
  • 133
    • 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, et al. Herpes simplex virus type 1 enters human epidermal keratinocytes, but not neurons, via a pH-dependent endocytic pathway. J Virol 2005;79:7609-7616.
    • (2005) J Virol , vol.79 , pp. 7609-7616
    • Nicola, A.V.1    Hou, J.2    Major, E.O.3
  • 134
    • 4344652071 scopus 로고    scopus 로고
    • Early steps of retrovirus replicative cycle
    • Nisole S, Saib A. Early steps of retrovirus replicative cycle. Retrovirology 2004;1:9.
    • (2004) Retrovirology , vol.1 , pp. 9
    • Nisole, S.1    Saib, A.2
  • 135
    • 0035963944 scopus 로고    scopus 로고
    • Caveolae in the uptake and targeting of infectious agents and secreted toxins
    • Norkin LC. Caveolae in the uptake and targeting of infectious agents and secreted toxins. Adv Drug Deliv Rev 2001;49:301-315.
    • (2001) Adv Drug Deliv Rev , vol.49 , pp. 301-315
    • Norkin, L.C.1
  • 136
    • 14544300928 scopus 로고    scopus 로고
    • Virus factories: associations of cell organelles for viral replication and morphogenesis
    • Novoa RR, Calderita G, Arranz R, et al. Virus factories: associations of cell organelles for viral replication and morphogenesis. Biol Cell 2005;97:147-172.
    • (2005) Biol Cell , vol.97 , pp. 147-172
    • Novoa, R.R.1    Calderita, G.2    Arranz, R.3
  • 137
    • 0025400304 scopus 로고
    • Characterization of a human gene conferring sensitivity to infection by gibbon ape leukemia virus
    • O'Hara B, Johann S, Klinger H, et al. Characterization of a human gene conferring sensitivity to infection by gibbon ape leukemia virus. Cell Growth Differ 1990;1:119-127.
    • (1990) Cell Growth Differ , vol.1 , pp. 119-127
    • O'Hara, B.1    Johann, S.2    Klinger, H.3
  • 138
    • 0029130751 scopus 로고
    • Nuclear import of influenza virus RNA can be mediated by viral nucleoprotein and transport factors required for protein import
    • O'Neill RE, Jaskunas R, Blobel G, et al. Nuclear import of influenza virus RNA can be mediated by viral nucleoprotein and transport factors required for protein import. J Biol Chem 1995;270:22701-22704.
    • (1995) J Biol Chem , vol.270 , pp. 22701-22704
    • O'Neill, R.E.1    Jaskunas, R.2    Blobel, G.3
  • 139
    • 0034091334 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 entry into host cells: reconstitution of capsid binding and uncoating at the nuclear pore complex in vitro
    • Ojala PM, Sodeik B, Ebersold MW, et al. Herpes simplex virus type 1 entry into host cells: reconstitution of capsid binding and uncoating at the nuclear pore complex in vitro. Mol Cell Biol 2000;20:4922-4931.
    • (2000) Mol Cell Biol , vol.20 , pp. 4922-4931
    • Ojala, P.M.1    Sodeik, B.2    Ebersold, M.W.3
  • 140
    • 0036175701 scopus 로고    scopus 로고
    • Nuclear pore complex is able to transport macromolecules with diameters of about 39 nm
    • Pante N, Kann M. Nuclear pore complex is able to transport macromolecules with diameters of about 39 nm. Mol Biol Cell 2002;13:425-434.
    • (2002) Mol Biol Cell , vol.13 , pp. 425-434
    • Pante, N.1    Kann, M.2
  • 142
    • 67449089967 scopus 로고    scopus 로고
    • Herpesvirus capsid association with the nuclear pore complex and viral DNA release involve the nucleoporin CAN/Nup214 and the capsid protein pUL25
    • Pasdeloup D, Blondel D, Isidro AL, et al. Herpesvirus capsid association with the nuclear pore complex and viral DNA release involve the nucleoporin CAN/Nup214 and the capsid protein pUL25. J Virol 2009;83:6610-6623.
    • (2009) J Virol , vol.83 , pp. 6610-6623
    • Pasdeloup, D.1    Blondel, D.2    Isidro, A.L.3
  • 143
    • 0018636837 scopus 로고
    • Antibody mediated enhancement of flavivirus replication in macrophage-like cell lines
    • Peiris JSM, Porterfileld JS. Antibody mediated enhancement of flavivirus replication in macrophage-like cell lines. Nature 1979;282:509-511.
    • (1979) Nature , vol.282 , pp. 509-511
    • Peiris, J.S.M.1    Porterfileld, J.S.2
  • 144
    • 21844440569 scopus 로고    scopus 로고
    • Genome-wide analysis of human kinases in clathrin- and caveolae/raft-mediated endocytosis
    • Pelkmans L, Fava E, Grabner H, et al. Genome-wide analysis of human kinases in clathrin- and caveolae/raft-mediated endocytosis. Nature 2005;436:78-86.
    • (2005) Nature , vol.436 , pp. 78-86
    • Pelkmans, L.1    Fava, E.2    Grabner, H.3
  • 145
    • 0037134014 scopus 로고    scopus 로고
    • Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae
    • Pelkmans L, Puntener D, Helenius A. Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae. Science 2002;296:535-539.
    • (2002) Science , vol.296 , pp. 535-539
    • Pelkmans, L.1    Puntener, D.2    Helenius, A.3
  • 146
    • 21844454457 scopus 로고    scopus 로고
    • Kinase-regulated quantal assemblies and kiss-and-run recycling of caveolae
    • Pelkmans L, Zerial M. Kinase-regulated quantal assemblies and kiss-and-run recycling of caveolae. Nature 2005;436:128-133.
    • (2005) Nature , vol.436 , pp. 128-133
    • Pelkmans, L.1    Zerial, M.2
  • 147
    • 0032582538 scopus 로고    scopus 로고
    • Binding of hepatitis C virus to CD81
    • Pileri P, Uematsu Y, Campagnoli S, et al. Binding of hepatitis C virus to CD81. Science 1998;282:938-941.
    • (1998) Science , vol.282 , pp. 938-941
    • Pileri, P.1    Uematsu, Y.2    Campagnoli, S.3
  • 148
    • 0026612385 scopus 로고
    • Influenza virus M2 protein has ion channel activity
    • Pinto LH, Holsinger LJ, Lamb RA. Influenza virus M2 protein has ion channel activity. Cell 1992;69:1-20.
    • (1992) Cell , vol.69 , pp. 1-20
    • Pinto, L.H.1    Holsinger, L.J.2    Lamb, R.A.3
  • 149
    • 0035655108 scopus 로고    scopus 로고
    • DC-SIGN and DC-SIGNR: helping hands for HIV
    • Pohlmann S, Baribaud F, Doms RW. DC-SIGN and DC-SIGNR: helping hands for HIV. Trends Immunol 2001;22:643-646.
    • (2001) Trends Immunol , vol.22 , pp. 643-646
    • Pohlmann, S.1    Baribaud, F.2    Doms, R.W.3
  • 151
    • 61449235414 scopus 로고    scopus 로고
    • Establishment of human papillomavirus infection requires cell cycle progression
    • Pyeon D, Pearce SM, Lank SM, et al. Establishment of human papillomavirus infection requires cell cycle progression. PLoS Pathog 2009;5:e1000318.
    • (2009) PLoS Pathog , vol.5 , pp. e1000318
    • Pyeon, D.1    Pearce, S.M.2    Lank, S.M.3
  • 152
    • 67650912077 scopus 로고    scopus 로고
    • A lipid receptor sorts polyomavirus from the endolysosome to the endoplasmic reticulum to cause infection
    • Qian M, Cai D, Verhey KJ, et al. A lipid receptor sorts polyomavirus from the endolysosome to the endoplasmic reticulum to cause infection. PLoS Pathog 2009;5:e1000465.
    • (2009) PLoS Pathog , vol.5 , pp. e1000465
    • Qian, M.1    Cai, D.2    Verhey, K.J.3
  • 153
    • 0042692926 scopus 로고    scopus 로고
    • Nuclear import of hepatitis B virus capsids and release of the viral genome
    • Rabe B, Vlachou A, Pante N, et al. Nuclear import of hepatitis B virus capsids and release of the viral genome. Proc Natl Acad Sci U S A 2003;100:9849-9854.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 9849-9854
    • Rabe, B.1    Vlachou, A.2    Pante, N.3
  • 154
    • 77957652501 scopus 로고    scopus 로고
    • Plus- and minus-end directed microtubule motors bind simultaneously to herpes simplex virus capsids using different inner tegument structures
    • Radtke K, Kieneke D, Wolfstein A, et al. Plus- and minus-end directed microtubule motors bind simultaneously to herpes simplex virus capsids using different inner tegument structures. PLoS Pathog 2010;6:e1000991.
    • (2010) PLoS Pathog , vol.6 , pp. e1000991
    • Radtke, K.1    Kieneke, D.2    Wolfstein, A.3
  • 155
    • 0019363272 scopus 로고
    • Interacting phospholipid bilayers: measured forces and induced structural changes
    • Rand RP. Interacting phospholipid bilayers: measured forces and induced structural changes. Annu Rev Biophys Bioeng 1981;10:277-314.
    • (1981) Annu Rev Biophys Bioeng , vol.10 , pp. 277-314
    • Rand, R.P.1
  • 156
    • 0036733284 scopus 로고    scopus 로고
    • Caveolae: from cell biology to animal physiology
    • Razani B, Woodman SE, Lisanti MP. Caveolae: from cell biology to animal physiology. Pharmacol Rev 2002;54:431-467.
    • (2002) Pharmacol Rev , vol.54 , pp. 431-467
    • Razani, B.1    Woodman, S.E.2    Lisanti, M.P.3
  • 157
    • 0019777842 scopus 로고
    • Electrophoretic separation of influenza virus ribonucleoproteins
    • Rees PJ, Dimmock NJ. Electrophoretic separation of influenza virus ribonucleoproteins. J Gen Virol 1981;53:125-132.
    • (1981) J Gen Virol , vol.53 , pp. 125-132
    • Rees, P.J.1    Dimmock, N.J.2
  • 158
    • 0034755553 scopus 로고    scopus 로고
    • Caveolae are involved in the trafficking of mouse polyomavirus virions and artificial VP1 pseudocapsids toward cell nuclei
    • Richterova Z, Liebl D, Horak M, et al. Caveolae are involved in the trafficking of mouse polyomavirus virions and artificial VP1 pseudocapsids toward cell nuclei. J Virol 2001;75:10880-10891.
    • (2001) J Virol , vol.75 , pp. 10880-10891
    • Richterova, Z.1    Liebl, D.2    Horak, M.3
  • 159
    • 0028167928 scopus 로고
    • Entry of coxsackievirus A9 into host cells: specific interactions with alpha v beta 3 integrin, the vitronectin receptor
    • Roivainen M, Piirainen L, Hovi T, et al. Entry of coxsackievirus A9 into host cells: specific interactions with alpha v beta 3 integrin, the vitronectin receptor. Virology 1994;203:357-365.
    • (1994) Virology , vol.203 , pp. 357-365
    • Roivainen, M.1    Piirainen, L.2    Hovi, T.3
  • 160
    • 36749032244 scopus 로고    scopus 로고
    • Shiga toxin induces tubular membrane invaginations for its uptake into cells
    • Römer W, Berland L, Chambon V, et al. Shiga toxin induces tubular membrane invaginations for its uptake into cells. Nature 2007;450:670-675.
    • (2007) Nature , vol.450 , pp. 670-675
    • Römer, W.1    Berland, L.2    Chambon, V.3
  • 162
    • 79952575472 scopus 로고    scopus 로고
    • Promotion of vesicular stomatitis virus fusion by the endosome-specific phospholipid bis(monoacylglycero)phosphate (BMP)
    • Roth SL, Whittaker GR. Promotion of vesicular stomatitis virus fusion by the endosome-specific phospholipid bis(monoacylglycero)phosphate (BMP). FEBS Lett 2011;585:865-869.
    • (2011) FEBS Lett , vol.585 , pp. 865-869
    • Roth, S.L.1    Whittaker, G.R.2
  • 163
    • 0030831545 scopus 로고    scopus 로고
    • Utilization of chemokine receptors, orphan receptors, and herpesvirus-encoded receptors by diverse human and simian immunodeficiency viruses
    • Rucker J, Edinger AL, Sharron M, et al. Utilization of chemokine receptors, orphan receptors, and herpesvirus-encoded receptors by diverse human and simian immunodeficiency viruses. J Virol 1997;71:8999-9007.
    • (1997) J Virol , vol.71 , pp. 8999-9007
    • Rucker, J.1    Edinger, A.L.2    Sharron, M.3
  • 164
    • 2542452779 scopus 로고    scopus 로고
    • Assembly of endocytic machinery around individual influenza viruses during viral entry
    • Rust MJ, Lakadamyali M, Zhang F, et al. Assembly of endocytic machinery around individual influenza viruses during viral entry. Nat Struct Mol Biol 2004;11:567-573.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 567-573
    • Rust, M.J.1    Lakadamyali, M.2    Zhang, F.3
  • 165
    • 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, et al. Cellular entry of Ebola virus involves uptake by a macropinocytosis-like mechanism and subsequent trafficking through early and late endosomes. PLoS Pathog 2010;6:e1001110.
    • (2010) PLoS Pathog , vol.6 , pp. e1001110
    • Saeed, M.F.1    Kolokoltsov, A.A.2    Albrecht, T.3
  • 166
    • 69249227502 scopus 로고    scopus 로고
    • Lysosome biogenesis and lysosomal membrane proteins: trafficking meets function
    • Saftig P, Klumperman J. Lysosome biogenesis and lysosomal membrane proteins: trafficking meets function. Nat Rev Mol Cell Biol 2009;10:623-635.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 623-635
    • Saftig, P.1    Klumperman, J.2
  • 167
    • 54149119141 scopus 로고    scopus 로고
    • Avoiding the void: cell-to-cell spread of human viruses
    • Sattentau Q. Avoiding the void: cell-to-cell spread of human viruses. Nat Rev Microbiol 2008;6:815-826.
    • (2008) Nat Rev Microbiol , vol.6 , pp. 815-826
    • Sattentau, Q.1
  • 168
    • 53049094647 scopus 로고    scopus 로고
    • Human papillomavirus type 16 entry: retrograde cell surface transport along actin-rich protrusions
    • Schelhaas M, Ewers H, Rajamaki ML, et al. Human papillomavirus type 16 entry: retrograde cell surface transport along actin-rich protrusions. PLoS Pathog 2008;4:e1000148.
    • (2008) PLoS Pathog , vol.4 , pp. e1000148
    • Schelhaas, M.1    Ewers, H.2    Rajamaki, M.L.3
  • 169
    • 35548992416 scopus 로고    scopus 로고
    • Simian virus 40 depends on ER protein folding and quality control factors for entry into host cells
    • Schelhaas M, Malmstrom J, Pelkmans L, et al. Simian virus 40 depends on ER protein folding and quality control factors for entry into host cells. Cell 2007;131:516-529.
    • (2007) Cell , vol.131 , pp. 516-529
    • Schelhaas, M.1    Malmstrom, J.2    Pelkmans, L.3
  • 170
    • 78651415502 scopus 로고    scopus 로고
    • Ion flux and the function of endosomes and lysosomes: pH is just the start: the flux of ions across endosomal membranes influences endosome function not only through regulation of the luminal pH
    • Scott CC, Gruenberg J. Ion flux and the function of endosomes and lysosomes: pH is just the start: the flux of ions across endosomal membranes influences endosome function not only through regulation of the luminal pH. Bioessays 2011;33:103-110.
    • (2011) Bioessays , vol.33 , pp. 103-110
    • Scott, C.C.1    Gruenberg, J.2
  • 171
    • 0035976603 scopus 로고    scopus 로고
    • Real-time single-molecule imaging of the infection pathway of an adeno-associated virus
    • Seisenberger G, Ried MU, Endress T, et al. Real-time single-molecule imaging of the infection pathway of an adeno-associated virus. Science 2001;294:1929-1932.
    • (2001) Science , vol.294 , pp. 1929-1932
    • Seisenberger, G.1    Ried, M.U.2    Endress, T.3
  • 172
    • 0021170531 scopus 로고
    • Role of a low-pH environment in adenovirus enhancement of the toxicity of a Pseudomonas exotoxin-epidermal growth factor conjugate
    • Seth P, FitzGerald DJP, Willigham MC, et al. Role of a low-pH environment in adenovirus enhancement of the toxicity of a Pseudomonas exotoxin-epidermal growth factor conjugate. J Virol 1984;51:650-655.
    • (1984) J Virol , vol.51 , pp. 650-655
    • Seth, P.1    FitzGerald, D.J.P.2    Willigham, M.C.3
  • 173
    • 0029043121 scopus 로고
    • Coxsackieviruses B1, B3, and B5 use decay accelerating factor as a receptor for cell attachment
    • Shafren DR, Bates RC, Agrez MV, et al. Coxsackieviruses B1, B3, and B5 use decay accelerating factor as a receptor for cell attachment. J Virol 1995;69:3873-3877.
    • (1995) J Virol , vol.69 , pp. 3873-3877
    • Shafren, D.R.1    Bates, R.C.2    Agrez, M.V.3
  • 174
    • 0037213578 scopus 로고    scopus 로고
    • Role of protein kinase C beta II in influenza virus entry via late endosomes
    • Sieczkarski SB, Brown HA, Whittaker GR. Role of protein kinase C beta II in influenza virus entry via late endosomes. J Virol 2003;77:460-469.
    • (2003) J Virol , vol.77 , pp. 460-469
    • Sieczkarski, S.B.1    Brown, H.A.2    Whittaker, G.R.3
  • 175
    • 0036784565 scopus 로고    scopus 로고
    • Influenza virus can enter and infect cells in the absence of clathrin-mediated endocytosis
    • Sieczkarski SB, Whittaker GR. Influenza virus can enter and infect cells in the absence of clathrin-mediated endocytosis. J Virol 2002;76:10455-10464.
    • (2002) J Virol , vol.76 , pp. 10455-10464
    • Sieczkarski, S.B.1    Whittaker, G.R.2
  • 176
    • 0037690744 scopus 로고    scopus 로고
    • Differential requirements of Rab5 and Rab7 for endocytosis of influenza and other enveloped viruses
    • Sieczkarski SB, Whittaker GR. Differential requirements of Rab5 and Rab7 for endocytosis of influenza and other enveloped viruses. Traffic 2003;4:333-343.
    • (2003) Traffic , vol.4 , pp. 333-343
    • Sieczkarski, S.B.1    Whittaker, G.R.2
  • 177
    • 0015304204 scopus 로고
    • The mechanisms of reovirus uncoating and gene activation in vivo
    • Silverstein SC, Astell C, Levin DH, et al. The mechanisms of reovirus uncoating and gene activation in vivo. Virology 1972;47:797-806.
    • (1972) Virology , vol.47 , pp. 797-806
    • Silverstein, S.C.1    Astell, C.2    Levin, D.H.3
  • 178
    • 0037227457 scopus 로고    scopus 로고
    • DC-SIGN and DC-SIGNR bind ebola glycoproteins and enhance infection of macrophages and endothelial cells
    • Simmons G, Reeves JD, Grogan CC, et al. DC-SIGN and DC-SIGNR bind ebola glycoproteins and enhance infection of macrophages and endothelial cells. Virology 2003;305:115-123.
    • (2003) Virology , vol.305 , pp. 115-123
    • Simmons, G.1    Reeves, J.D.2    Grogan, C.C.3
  • 179
    • 0026490846 scopus 로고
    • Role of ribosomes in Semliki Forest virus nucleocapsid uncoating
    • Singh I, Helenius A. Role of ribosomes in Semliki Forest virus nucleocapsid uncoating. J Virol 1992;66:7049-7058.
    • (1992) J Virol , vol.66 , pp. 7049-7058
    • Singh, I.1    Helenius, A.2
  • 180
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin
    • Skehel JJ, Wiley DC. Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu Rev Biochem 2000;69:531-569.
    • (2000) Annu Rev Biochem , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 181
    • 0036784563 scopus 로고    scopus 로고
    • Adaptation of alphaviruses to heparan sulfate: interaction of Sindbis and Semliki Forest viruses with liposomes containing lipid-conjugated heparin
    • Smit JM, Waarts BL, Kimata K, et al. Adaptation of alphaviruses to heparan sulfate: interaction of Sindbis and Semliki Forest viruses with liposomes containing lipid-conjugated heparin. J Virol 2002;76:10128-10137.
    • (2002) J Virol , vol.76 , pp. 10128-10137
    • Smit, J.M.1    Waarts, B.L.2    Kimata, K.3
  • 182
    • 0036437319 scopus 로고    scopus 로고
    • Break ins and break outs: viral interactions with the cytoskeleton of mammalian cells
    • Smith GA, Enquist LW. Break ins and break outs: viral interactions with the cytoskeleton of mammalian cells. Annu Rev Cell Dev Biol 2002;18:135-161.
    • (2002) Annu Rev Cell Dev Biol , vol.18 , pp. 135-161
    • Smith, G.A.1    Enquist, L.W.2
  • 184
    • 0034307164 scopus 로고    scopus 로고
    • Mechanisms of viral transport in the cytoplasm
    • Sodeik B. Mechanisms of viral transport in the cytoplasm. Trends Microbiol 2000;8:465-472.
    • (2000) Trends Microbiol , vol.8 , pp. 465-472
    • Sodeik, B.1
  • 185
    • 0034665214 scopus 로고    scopus 로고
    • Three classes of cell surface receptors for alphaherpesvirus entry
    • Spear PG, Eisenberg RJ, Cohen GH. Three classes of cell surface receptors for alphaherpesvirus entry. Virology 2000;275:1-8.
    • (2000) Virology , vol.275 , pp. 1-8
    • Spear, P.G.1    Eisenberg, R.J.2    Cohen, G.H.3
  • 186
    • 0030764780 scopus 로고    scopus 로고
    • Proteolytic activation of tick-borne encephalitis virus by furin
    • Stadler K, Allison SL, Schalich J, et al. Proteolytic activation of tick-borne encephalitis virus by furin. J Virol 1997;71:8475-8481.
    • (1997) J Virol , vol.71 , pp. 8475-8481
    • Stadler, K.1    Allison, S.L.2    Schalich, J.3
  • 187
    • 0030745673 scopus 로고    scopus 로고
    • Major histocompatibility complex class I molecules mediate association of SV40 with caveolae
    • Stang E, Kartenbeck J, Parton RG. Major histocompatibility complex class I molecules mediate association of SV40 with caveolae. Mol Biol Cell 1997;8:47-57.
    • (1997) Mol Biol Cell , vol.8 , pp. 47-57
    • Stang, E.1    Kartenbeck, J.2    Parton, R.G.3
  • 188
    • 0024521781 scopus 로고
    • A cell adhesion molecule, ICAM-1, is the major surface receptor for rhinoviruses
    • Staunton DE, Merluzzi VJ, Rothlein R, et al. A cell adhesion molecule, ICAM-1, is the major surface receptor for rhinoviruses. Cell 1989;56:849-853.
    • (1989) Cell , vol.56 , pp. 849-853
    • Staunton, D.E.1    Merluzzi, V.J.2    Rothlein, R.3
  • 190
    • 36049006185 scopus 로고    scopus 로고
    • Cell integrins: commonly used receptors for diverse viral pathogens
    • Stewart PL, Nemerow GR. Cell integrins: commonly used receptors for diverse viral pathogens. Trends Microbiol 2007;15:500-507.
    • (2007) Trends Microbiol , vol.15 , pp. 500-507
    • Stewart, P.L.1    Nemerow, G.R.2
  • 191
    • 0026008031 scopus 로고
    • Structural characteristics of the M2 protein of influenza A viruses: evidence that it forms a tetrameric channel
    • Sugrue RJ, Hay AJ. Structural characteristics of the M2 protein of influenza A viruses: evidence that it forms a tetrameric channel. Virology 1991;180:617-624.
    • (1991) Virology , vol.180 , pp. 617-624
    • Sugrue, R.J.1    Hay, A.J.2
  • 192
    • 0036223563 scopus 로고    scopus 로고
    • Role of recycling endosomes and lysosomes in dynein-dependent entry of canine parvovirus
    • Suikkanen S, Saajarvi K, Hirsimaki J, et al. Role of recycling endosomes and lysosomes in dynein-dependent entry of canine parvovirus. J Virol 2002;76:4401-4411.
    • (2002) J Virol , vol.76 , pp. 4401-4411
    • Suikkanen, S.1    Saajarvi, K.2    Hirsimaki, J.3
  • 193
    • 0033593811 scopus 로고    scopus 로고
    • Microtubule-dependent plus- and minus end-directed motilities are competing processes for nuclear targeting of adenovirus
    • Suomalainen M, Nakano MY, Keller S, et al. Microtubule-dependent plus- and minus end-directed motilities are competing processes for nuclear targeting of adenovirus. J Cell Biol 1999;144:657-672.
    • (1999) J Cell Biol , vol.144 , pp. 657-672
    • Suomalainen, M.1    Nakano, M.Y.2    Keller, S.3
  • 195
    • 0033514357 scopus 로고    scopus 로고
    • Cloning and characterization of a cell surface receptor for xenotropic and polytropic murine leukemia viruses
    • Tailor CS, Nouri A, Lee CG, et al. Cloning and characterization of a cell surface receptor for xenotropic and polytropic murine leukemia viruses. Proc Natl Acad Sci U S A 1999;96:927-932.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 927-932
    • Tailor, C.S.1    Nouri, A.2    Lee, C.G.3
  • 196
    • 0026512199 scopus 로고
    • Feline leukemia virus subgroup B uses the same cell surface receptor as gibbon ape leukemia virus
    • Takeuchi Y, Vile RG, Simpson G, et al. Feline leukemia virus subgroup B uses the same cell surface receptor as gibbon ape leukemia virus. J Virol 1992;66:1219-1222.
    • (1992) J Virol , vol.66 , pp. 1219-1222
    • Takeuchi, Y.1    Vile, R.G.2    Simpson, G.3
  • 197
    • 0344642934 scopus 로고    scopus 로고
    • DC-SIGN (CD209) mediates dengue virus infection of human dendritic cells
    • Tassaneetrithep B, Burgess TH, Granelli-Piperno A, et al. DC-SIGN (CD209) mediates dengue virus infection of human dendritic cells. J Exp Med 2003;197:823-829.
    • (2003) J Exp Med , vol.197 , pp. 823-829
    • Tassaneetrithep, B.1    Burgess, T.H.2    Granelli-Piperno, A.3
  • 198
    • 0030915715 scopus 로고    scopus 로고
    • HCAR and MCAR: the human and mouse cellular receptors for subgroup C adenoviruses and group B coxsackieviruses
    • Tomko RP, Xu R, Philipson L. HCAR and MCAR: the human and mouse cellular receptors for subgroup C adenoviruses and group B coxsackieviruses. Proc Natl Acad Sci U S A 1997;94:3352-3356.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 3352-3356
    • Tomko, R.P.1    Xu, R.2    Philipson, L.3
  • 199
    • 0031060329 scopus 로고    scopus 로고
    • Characterization of the ion channels formed by poliovirus in planar lipid membranes
    • Tosteson MT, Chow M. Characterization of the ion channels formed by poliovirus in planar lipid membranes. J Virol 1997;71:507-511.
    • (1997) J Virol , vol.71 , pp. 507-511
    • Tosteson, M.T.1    Chow, M.2
  • 200
    • 0035195085 scopus 로고    scopus 로고
    • Import of adenovirus DNA involves the nuclear pore complex receptor CAN/Nup214 and histone H1
    • Trotman L, Mosberger N, Fornerod M, et al. Import of adenovirus DNA involves the nuclear pore complex receptor CAN/Nup214 and histone H1. Nat Cell Biol 2001;3:1092-1100.
    • (2001) Nat Cell Biol , vol.3 , pp. 1092-1100
    • Trotman, L.1    Mosberger, N.2    Fornerod, M.3
  • 201
    • 77958089167 scopus 로고    scopus 로고
    • A virus takes an "L" turn to find its receptor
    • Tsai B, Inoue T. A virus takes an "L" turn to find its receptor. Cell Host Microbe 2010;8:301-302.
    • (2010) Cell Host Microbe , vol.8 , pp. 301-302
    • Tsai, B.1    Inoue, T.2
  • 202
    • 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, et al. Interaction of c-Cbl with myosin IIA regulates bleb associated macropinocytosis of Kaposi's sarcoma-associated herpesvirus. PLoS Pathog 2010;6:e1001238.
    • (2010) PLoS Pathog , vol.6 , pp. e1001238
    • Valiya Veettil, M.1    Sadagopan, S.2    Kerur, N.3
  • 204
    • 0037306525 scopus 로고    scopus 로고
    • Caveolae: anchored, multifunctional platforms in the lipid ocean
    • van Deurs B, Roepstorff K, Hommelgaard AM, et al. Caveolae: anchored, multifunctional platforms in the lipid ocean. Trends Cell Biol 2003;13:92-100.
    • (2003) Trends Cell Biol , vol.13 , pp. 92-100
    • van Deurs, B.1    Roepstorff, K.2    Hommelgaard, A.M.3
  • 205
    • 0028158411 scopus 로고
    • A human amphotropic retrovirus receptor is a second member of the gibbon ape leukemia virus receptor family
    • van Zeijl M, Johann S, Closs E, et al. A human amphotropic retrovirus receptor is a second member of the gibbon ape leukemia virus receptor family. Proc Natl Acad Sci U S A 1994;91:1168-1172.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 1168-1172
    • van Zeijl, M.1    Johann, S.2    Closs, E.3
  • 206
    • 2942650156 scopus 로고    scopus 로고
    • Pathways of cell infection by parvoviruses and adeno-associated viruses
    • Vihinen-Ranta M, Suikkanen S, Parrish CR. Pathways of cell infection by parvoviruses and adeno-associated viruses. J Virol 2004;78:6709-6714.
    • (2004) J Virol , vol.78 , pp. 6709-6714
    • Vihinen-Ranta, M.1    Suikkanen, S.2    Parrish, C.R.3
  • 207
    • 22744447453 scopus 로고    scopus 로고
    • Rab7 associates with early endosomes to mediate sorting and transport of Semliki Forest virus to late endosomes
    • Vonderheit A, Helenius A. Rab7 associates with early endosomes to mediate sorting and transport of Semliki Forest virus to late endosomes. PLoS Biol 2005;3:e233.
    • (2005) PLoS Biol , vol.3 , pp. e233
    • Vonderheit, A.1    Helenius, A.2
  • 208
    • 0024327726 scopus 로고
    • Cell-associated West Nile flavivirus is covered with E+pre-M protein heterodimers which are destroyed and reorganized by proteolytic cleavage during virus release
    • Wengler G. Cell-associated West Nile flavivirus is covered with E+pre-M protein heterodimers which are destroyed and reorganized by proteolytic cleavage during virus release. J Virol 1989;63:2521-2526.
    • (1989) J Virol , vol.63 , pp. 2521-2526
    • Wengler, G.1
  • 209
    • 62149100727 scopus 로고    scopus 로고
    • The regulation of disassembly of alphavirus cores
    • Wengler G. The regulation of disassembly of alphavirus cores. Arch Virol 2009;154:381-390.
    • (2009) Arch Virol , vol.154 , pp. 381-390
    • Wengler, G.1
  • 210
    • 0020752797 scopus 로고
    • Membrane fusion proteins of enveloped animal viruses
    • White J, Kielian M, Helenius A. Membrane fusion proteins of enveloped animal viruses. Q Rev Biophys 1983;16:151-195.
    • (1983) Q Rev Biophys , vol.16 , pp. 151-195
    • White, J.1    Kielian, M.2    Helenius, A.3
  • 211
  • 213
    • 0028169584 scopus 로고
    • Integrin alpha v beta 5 selectively promotes adenovirus mediated cell membrane permeabilization
    • Wickham TJ, Filardo EJ, Cheresh DA, et al. Integrin alpha v beta 5 selectively promotes adenovirus mediated cell membrane permeabilization. J Cell Biol 1994;127:257-264.
    • (1994) J Cell Biol , vol.127 , pp. 257-264
    • Wickham, T.J.1    Filardo, E.J.2    Cheresh, D.A.3
  • 214
    • 0027166647 scopus 로고
    • Integrins alpha v beta 3 and alpha v beta 5 promote adenovirus internalization but not virus attachment
    • Wickham TJ, Mathias P, Cheresh DA, et al. Integrins alpha v beta 3 and alpha v beta 5 promote adenovirus internalization but not virus attachment. Cell 1993;73:309-319.
    • (1993) Cell , vol.73 , pp. 309-319
    • Wickham, T.J.1    Mathias, P.2    Cheresh, D.A.3
  • 215
    • 35848956344 scopus 로고    scopus 로고
    • Aggresomes and pericentriolar sites of virus assembly: cellular defense or viral design?
    • Wileman T. Aggresomes and pericentriolar sites of virus assembly: cellular defense or viral design? Annu Rev Microbiol 2007;61:149-167.
    • (2007) Annu Rev Microbiol , vol.61 , pp. 149-167
    • Wileman, T.1
  • 216
    • 0032565358 scopus 로고    scopus 로고
    • Role for the vaccinia virus A36R outer envelope protein in the formation of virus-tipped actin-containing microvilli and cell-to-cell virus spread
    • Wolffe EJ, Weisberg AS, Moss B. Role for the vaccinia virus A36R outer envelope protein in the formation of virus-tipped actin-containing microvilli and cell-to-cell virus spread. Virology 1998;244:20-26.
    • (1998) Virology , vol.244 , pp. 20-26
    • Wolffe, E.J.1    Weisberg, A.S.2    Moss, B.3
  • 217
    • 0026693135 scopus 로고
    • Human aminopeptidase N is a receptor for human coronavirus 229E
    • Yeager CL, Ashmun RA, Williams RK, et al. Human aminopeptidase N is a receptor for human coronavirus 229E. Nature 1992;357:420-422.
    • (1992) Nature , vol.357 , pp. 420-422
    • Yeager, C.L.1    Ashmun, R.A.2    Williams, R.K.3
  • 218
    • 18944375873 scopus 로고    scopus 로고
    • Structural studies of the parainfluenza virus 5 hemagglutinin-neuraminidase tetramer in complex with its receptor, sialyllactose
    • Yuan P, Thompson TB, Wurzburg BA, et al. Structural studies of the parainfluenza virus 5 hemagglutinin-neuraminidase tetramer in complex with its receptor, sialyllactose. Structure (Camb) 2005;13:803-815.
    • (2005) Structure (Camb) , vol.13 , pp. 803-815
    • Yuan, P.1    Thompson, T.B.2    Wurzburg, B.A.3
  • 219
    • 25144499159 scopus 로고    scopus 로고
    • Adenovirus receptors
    • Zhang Y, Bergelson JM. Adenovirus receptors. J Virol 2005;79:12125-12131.
    • (2005) J Virol , vol.79 , pp. 12125-12131
    • Zhang, Y.1    Bergelson, J.M.2
  • 220
    • 0018877089 scopus 로고
    • Influence of membrane (M) protein on influenza A virus virion transcriptase activity in vitro and its susceptibility to rimantadine
    • Zvonarjev AY, Ghendon YZ. Influence of membrane (M) protein on influenza A virus virion transcriptase activity in vitro and its susceptibility to rimantadine. J Virol 1980;33:583-586.
    • (1980) J Virol , vol.33 , pp. 583-586
    • Zvonarjev, A.Y.1    Ghendon, Y.Z.2


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