메뉴 건너뛰기
Journal of Virology
Volumn 89, Issue 1, 2015, Pages 844-856
Simian hemorrhagic fever virus cell entry is dependent on CD163 and uses a clathrin-mediated endocytosis-like pathway
Author keywords

[No Author keywords available]
Indexed keywords

CD163 ANTIGEN; CELL SURFACE PROTEIN; CHYMOTRYPSIN A; CLATHRIN; PAPAIN; PHOSPHOLIPASE A2; PROTEINASE K; TRYPSIN; CELL SURFACE RECEPTOR; DIFFERENTIATION ANTIGEN; LEUKOCYTE ANTIGEN; VIRUS RECEPTOR;
EID: 84919458607     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02697-14     Document Type: Article
Times cited : (41)
References (73)
  • 1
    • 84864007198 scopus 로고    scopus 로고
    • Family Arteriviridae
    • King AMQ, Adams MJ, Carstens EB, Lefkowitz EJ (ed), Ninth report of the International Committee on Taxonomy of Viruses. Elsevier Academic Press, London, United Kingdom
    • Faaberg KS, Balasuriya UB, Brinton MA, Gorbalenya AE, Leung FC-C, Nauwynck H, Snijder EJ, Stadejek T, Yang H, Yoo D. 2011. Family Arteriviridae, p 796-805. In King AMQ, Adams MJ, Carstens EB, Lefkowitz EJ (ed), Virus taxonomy. Ninth report of the International Committee on Taxonomy of Viruses. Elsevier Academic Press, London, United Kingdom.
    • (2011) Virus taxonomy , pp. 796-805
    • Faaberg, K.S.1    Balasuriya, U.B.2    Brinton, M.A.3    Gorbalenya, A.E.4    Leung, F.C.-C.5    Nauwynck, H.6    Snijder, E.J.7    Stadejek, T.8    Yang, H.9    Yoo, D.10
  • 2
    • 79955525244 scopus 로고    scopus 로고
    • Novel, divergent simian hemorrhagic fever viruses in a wild Ugandan red colobus monkey discovered using direct pyrosequencing
    • Lauck M, Hyeroba D, Tumukunde A, Weny G, Lank SM, Chapman CA, O'Connor DH, Friedrich TC, Goldberg TL. 2011. Novel, divergent simian hemorrhagic fever viruses in a wild Ugandan red colobus monkey discovered using direct pyrosequencing. PLoS One 6:e19056. http://dx.doi.org/10.1371/journal.pone.0019056.
    • (2011) PLoS One , vol.6
    • Lauck, M.1    Hyeroba, D.2    Tumukunde, A.3    Weny, G.4    Lank, S.M.5    Chapman, C.A.6    O'Connor, D.H.7    Friedrich, T.C.8    Goldberg, T.L.9
  • 4
    • 0017714662 scopus 로고
    • Epizootiology, transmission and approach to prevention of fatal simian haemorrhagic fever in rhesus monkeys
    • London WT. 1977. Epizootiology, transmission and approach to prevention of fatal simian haemorrhagic fever in rhesus monkeys. Nature 268: 344-345. http://dx.doi.org/10.1038/268344a0.
    • (1977) Nature , vol.268 , pp. 344-345
    • London, W.T.1
  • 6
    • 17744407106 scopus 로고
    • Study of the etiology of hemorrhagic fever in monkeys
    • (In Russian)
    • Shevtsova ZV. 1967. Study of the etiology of hemorrhagic fever in monkeys. Vopr Virusol 12:47-51. (In Russian).
    • (1967) Vopr Virusol , vol.12 , pp. 47-51
    • Shevtsova, Z.V.1
  • 7
    • 0014286687 scopus 로고
    • Simian hemorrhagic fever. I. Clinical and epizootiologic aspects of an outbreak among quarantined monkeys
    • Palmer AE, Allen AM, Tauraso NM, Shelokov A. 1968. Simian hemorrhagic fever. I. Clinical and epizootiologic aspects of an outbreak among quarantined monkeys. Am J Trop Med Hyg 17:404-412.
    • (1968) Am J Trop Med Hyg , vol.17 , pp. 404-412
    • Palmer, A.E.1    Allen, A.M.2    Tauraso, N.M.3    Shelokov, A.4
  • 8
    • 0014729128 scopus 로고
    • Electron microscopic study of tissue cultures infected with simian haemorrhagic fever virus
    • Wood O, Tauraso N, Liebhaber H. 1970. Electron microscopic study of tissue cultures infected with simian haemorrhagic fever virus. J Gen Virol 7:129-136. http://dx.doi.org/10.1099/0022-1317-7-2-129.
    • (1970) J Gen Virol , vol.7 , pp. 129-136
    • Wood, O.1    Tauraso, N.2    Liebhaber, H.3
  • 9
    • 0021686725 scopus 로고
    • The genome of simian hemorrhagic fever virus
    • Sagripanti JL. 1984. The genome of simian hemorrhagic fever virus. Arch Virol 82:61-72. http://dx.doi.org/10.1007/BF01309368.
    • (1984) Arch Virol , vol.82 , pp. 61-72
    • Sagripanti, J.L.1
  • 10
    • 0021850188 scopus 로고
    • Polyadenylic acid sequences in the genomic RNA of the togavirus of simian hemorrhagic fever
    • Sagripanti JL. 1985. Polyadenylic acid sequences in the genomic RNA of the togavirus of simian hemorrhagic fever. Virology 145:350-355. http://dx.doi.org/10.1016/0042-6822(85)90171-0.
    • (1985) Virology , vol.145 , pp. 350-355
    • Sagripanti, J.L.1
  • 11
    • 0022610643 scopus 로고
    • The cap structure of simian hemorrhagic fever virion RNA
    • Sagripanti JL, Zandomeni RO, Weinmann R. 1986. The cap structure of simian hemorrhagic fever virion RNA. Virology 151:146-150. http://dx.doi.org/10.1016/0042-6822(86)90113-3.
    • (1986) Virology , vol.151 , pp. 146-150
    • Sagripanti, J.L.1    Zandomeni, R.O.2    Weinmann, R.3
  • 12
    • 0028920710 scopus 로고
    • Molecular characterization of the 3' terminus of the simian hemorrhagic fever virus genome
    • Godeny EK, Zeng L, Smith SL, Brinton MA. 1995. Molecular characterization of the 3' terminus of the simian hemorrhagic fever virus genome. J Virol 69:2679-2683.
    • (1995) J Virol , vol.69 , pp. 2679-2683
    • Godeny, E.K.1    Zeng, L.2    Smith, S.L.3    Brinton, M.A.4
  • 13
    • 84974708381 scopus 로고    scopus 로고
    • Arteriviruses
    • Knipe DM, Howley PM (ed), 6th ed, Lippincott Williams & Wilkins, Philadelphia, PA
    • Snijder EJ, Kikkert M. 2013. Arteriviruses, p 859-879. In Knipe DM, Howley PM (ed), Fields virology, 6th ed, vol 1. Lippincott Williams & Wilkins, Philadelphia, PA.
    • (2013) Fields virology , vol.1 , pp. 859-879
    • Snijder, E.J.1    Kikkert, M.2
  • 14
    • 0031964766 scopus 로고    scopus 로고
    • Identification of the leader-body junctions for the viral subgenomic mRNAs and organization of the simian hemorrhagic fever virus genome: evidence for gene duplication during arterivirus evolution
    • Godeny EK, de Vries AA, Wang XC, Smith SL, de Groot RJ. 1998. Identification of the leader-body junctions for the viral subgenomic mRNAs and organization of the simian hemorrhagic fever virus genome: evidence for gene duplication during arterivirus evolution. J Virol 72:862-867.
    • (1998) J Virol , vol.72 , pp. 862-867
    • Godeny, E.K.1    de Vries, A.A.2    Wang, X.C.3    Smith, S.L.4    de Groot, R.J.5
  • 15
    • 0029037521 scopus 로고
    • The two major envelope proteins of equine arteritis virus associate into disulfide-linked heterodimers
    • de Vries AA, Post SM, Raamsman MJ, Horzinek MC, Rottier PJ. 1995. The two major envelope proteins of equine arteritis virus associate into disulfide-linked heterodimers. J Virol 69:4668-4674.
    • (1995) J Virol , vol.69 , pp. 4668-4674
    • de Vries, A.A.1    Post, S.M.2    Raamsman, M.J.3    Horzinek, M.C.4    Rottier, P.J.5
  • 16
    • 0028969720 scopus 로고
    • Disulfide bonds between two envelope proteins of lactate dehydrogenase-elevating virus are essential for viral infectivity
    • Faaberg KS, Even C, Palmer GA, Plagemann PG. 1995. Disulfide bonds between two envelope proteins of lactate dehydrogenase-elevating virus are essential for viral infectivity. J Virol 69:613-617.
    • (1995) J Virol , vol.69 , pp. 613-617
    • Faaberg, K.S.1    Even, C.2    Palmer, G.A.3    Plagemann, P.G.4
  • 17
    • 33750051639 scopus 로고    scopus 로고
    • The small envelope protein of porcine reproductive and respiratory syndrome virus possesses ion channel protein-like properties
    • Lee C, Yoo D. 2006. The small envelope protein of porcine reproductive and respiratory syndrome virus possesses ion channel protein-like properties. Virology 355:30-43. http://dx.doi.org/10.1016/j.virol.2006.07.013.
    • (2006) Virology , vol.355 , pp. 30-43
    • Lee, C.1    Yoo, D.2
  • 18
    • 0345167080 scopus 로고    scopus 로고
    • Intra-and intermolecular disulfide bonds of the GP2b glycoprotein of equine arteritis virus: relevance for virus assembly and infectivity
    • Wieringa R, De Vries AA, Post SM, Rottier PJ. 2003. Intra-and intermolecular disulfide bonds of the GP2b glycoprotein of equine arteritis virus: relevance for virus assembly and infectivity. J Virol 77:12996-13004. http://dx.doi.org/10.1128/JVI.77.24.12996-13004.2003.
    • (2003) J Virol , vol.77 , pp. 12996-13004
    • Wieringa, R.1    De Vries, A.A.2    Post, S.M.3    Rottier, P.J.4
  • 19
    • 0037738465 scopus 로고    scopus 로고
    • Formation of disulfide-linked complexes between the three minor envelope glycoproteins (GP2b, GP3, and GP4) of equine arteritis virus
    • Wieringa R, de Vries AA, Rottier PJ. 2003. Formation of disulfide-linked complexes between the three minor envelope glycoproteins (GP2b, GP3, and GP4) of equine arteritis virus. J Virol 77:6216-6226. http://dx.doi.org/10.1128/JVI.77.11.6216-6226.2003.
    • (2003) J Virol , vol.77 , pp. 6216-6226
    • Wieringa, R.1    de Vries, A.A.2    Rottier, P.J.3
  • 21
    • 25144476250 scopus 로고    scopus 로고
    • Envelope protein requirements for the assembly of infectious virions of porcine reproductive and respiratory syndrome virus
    • Wissink EH, Kroese MV, van Wijk HA, Rijsewijk FA, Meulenberg JJ, Rottier PJ. 2005. Envelope protein requirements for the assembly of infectious virions of porcine reproductive and respiratory syndrome virus. J Virol 79:12495-12506. http://dx.doi.org/10.1128/JVI.79.19.12495-12506.2005.
    • (2005) J Virol , vol.79 , pp. 12495-12506
    • Wissink, E.H.1    Kroese, M.V.2    van Wijk, H.A.3    Rijsewijk, F.A.4    Meulenberg, J.J.5    Rottier, P.J.6
  • 22
    • 84855673964 scopus 로고    scopus 로고
    • Cell entry of enveloped viruses
    • Plemper RK. 2011. Cell entry of enveloped viruses. Curr Opin Virol 1:92-100. http://dx.doi.org/10.1016/j.coviro.2011.06.002.
    • (2011) Curr Opin Virol , vol.1 , pp. 92-100
    • Plemper, R.K.1
  • 23
    • 34447281283 scopus 로고    scopus 로고
    • CD163 expression confers susceptibility to porcine reproductive and respiratory syndrome viruses
    • Calvert JG, Slade DE, Shields SL, Jolie R, Mannan RM, Ankenbauer RG, Welch SK. 2007. CD163 expression confers susceptibility to porcine reproductive and respiratory syndrome viruses. J Virol 81:7371-7379. http://dx.doi.org/10.1128/JVI.00513-07.
    • (2007) J Virol , vol.81 , pp. 7371-7379
    • Calvert, J.G.1    Slade, D.E.2    Shields, S.L.3    Jolie, R.4    Mannan, R.M.5    Ankenbauer, R.G.6    Welch, S.K.7
  • 24
    • 58149378592 scopus 로고    scopus 로고
    • Sialoadhesin and CD163 join forces during entry of the porcine reproductive and respiratory syndrome virus
    • Van Gorp H, Van Breedam W, Delputte PL, Nauwynck HJ. 2008. Sialoadhesin and CD163 join forces during entry of the porcine reproductive and respiratory syndrome virus. J Gen Virol 89:2943-2953. http://dx.doi.org/10.1099/vir.0.2008/005009-0.
    • (2008) J Gen Virol , vol.89 , pp. 2943-2953
    • Van Gorp, H.1    Van Breedam, W.2    Delputte, P.L.3    Nauwynck, H.J.4
  • 25
    • 75449111993 scopus 로고    scopus 로고
    • The minor envelope glycoproteins GP2a and GP4 of porcine reproductive and respiratory syndrome virus interact with the receptor CD163
    • Das PB, Dinh PX, Ansari IH, de Lima M, Osorio FA, Pattnaik AK. 2010. The minor envelope glycoproteins GP2a and GP4 of porcine reproductive and respiratory syndrome virus interact with the receptor CD163. J Virol 84:1731-1740. http://dx.doi.org/10.1128/JVI.01774-09.
    • (2010) J Virol , vol.84 , pp. 1731-1740
    • Das, P.B.1    Dinh, P.X.2    Ansari, I.H.3    de Lima, M.4    Osorio, F.A.5    Pattnaik, A.K.6
  • 26
    • 76149089079 scopus 로고    scopus 로고
    • The porcine reproductive and respiratory syndrome virus requires trafficking through CD163-positive early endosomes, but not late endosomes, for productive infection
    • Van Gorp H, Van Breedam W, Delputte PL, Nauwynck HJ. 2009. The porcine reproductive and respiratory syndrome virus requires trafficking through CD163-positive early endosomes, but not late endosomes, for productive infection. Arch Virol 154:1939-1943. http://dx.doi.org/10.1007/s00705-009-0527-1.
    • (2009) Arch Virol , vol.154 , pp. 1939-1943
    • Van Gorp, H.1    Van Breedam, W.2    Delputte, P.L.3    Nauwynck, H.J.4
  • 27
    • 44949149221 scopus 로고    scopus 로고
    • Equine arteritis virus is delivered to an acidic compartment of host cells via clathrin-dependent endocytosis
    • Nitschke M, Korte T, Tielesch C, Ter-Avetisyan G, Tunnemann G, Cardoso MC, Veit M, Herrmann A. 2008. Equine arteritis virus is delivered to an acidic compartment of host cells via clathrin-dependent endocytosis. Virology 377:248-254. http://dx.doi.org/10.1016/j.virol.2008.04.041.
    • (2008) Virology , vol.377 , pp. 248-254
    • Nitschke, M.1    Korte, T.2    Tielesch, C.3    Ter-Avetisyan, G.4    Tunnemann, G.5    Cardoso, M.C.6    Veit, M.7    Herrmann, A.8
  • 28
    • 0032969255 scopus 로고    scopus 로고
    • Entry of porcine reproductive and respiratory syndrome virus into porcine alveolar macrophages via receptor-mediated endocytosis
    • Nauwynck HJ, Duan X, Favoreel HW, Van Oostveldt P, Pensaert MB. 1999. Entry of porcine reproductive and respiratory syndrome virus into porcine alveolar macrophages via receptor-mediated endocytosis. J Gen Virol 80:297-305.
    • (1999) J Gen Virol , vol.80 , pp. 297-305
    • Nauwynck, H.J.1    Duan, X.2    Favoreel, H.W.3    Van Oostveldt, P.4    Pensaert, M.B.5
  • 29
    • 0030005491 scopus 로고    scopus 로고
    • Porcine reproductive and respiratory syndrome virus enters cells through a low pH-dependent endocytic pathway
    • Kreutz LC, Ackermann MR. 1996. Porcine reproductive and respiratory syndrome virus enters cells through a low pH-dependent endocytic pathway. Virus Res 42:137-147. http://dx.doi.org/10.1016/0168-1702(96)01313-5.
    • (1996) Virus Res , vol.42 , pp. 137-147
    • Kreutz, L.C.1    Ackermann, M.R.2
  • 33
    • 0028068526 scopus 로고
    • Involvement of the vacuolar H(+)-ATPase in animal virus entry
    • Perez L, Carrasco L. 1994. Involvement of the vacuolar H(+)-ATPase in animal virus entry. J Gen Virol 75:2595-2606. http://dx.doi.org/10.1099/0022-1317-75-10-2595.
    • (1994) J Gen Virol , vol.75 , pp. 2595-2606
    • Perez, L.1    Carrasco, L.2
  • 34
    • 0040117958 scopus 로고    scopus 로고
    • Bafilomycins and concanamycins as inhibitors of V-ATPases and P-ATPases
    • Drose S, Altendorf K. 1997. Bafilomycins and concanamycins as inhibitors of V-ATPases and P-ATPases. J Exp Biol 200:1-8.
    • (1997) J Exp Biol , vol.200 , pp. 1-8
    • Drose, S.1    Altendorf, K.2
  • 35
    • 32944473016 scopus 로고    scopus 로고
    • Virus entry: open sesame
    • Marsh M, Helenius A. 2006. Virus entry: open sesame. Cell 124:729-740. http://dx.doi.org/10.1016/j.cell.2006.02.007.
    • (2006) Cell , vol.124 , pp. 729-740
    • Marsh, M.1    Helenius, A.2
  • 36
    • 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. http://dx.doi.org/10.1083/jcb.123.5.1107.
    • (1993) J Cell Biol , vol.123 , pp. 1107-1117
    • Wang, L.H.1    Rothberg, K.G.2    Anderson, R.G.3
  • 37
    • 0024456667 scopus 로고
    • Phenylarsine oxide inhibition of endocytosis: effects on asialofetuin internalization
    • Gibson AE, Noel RJ, Herlihy JT, Ward WF. 1989. Phenylarsine oxide inhibition of endocytosis: effects on asialofetuin internalization. Am J Physiol 257:C182-C184.
    • (1989) Am J Physiol , vol.257 , pp. C182-C184
    • Gibson, A.E.1    Noel, R.J.2    Herlihy, J.T.3    Ward, W.F.4
  • 38
    • 70350139505 scopus 로고    scopus 로고
    • Dissecting dynamin's role in clathrin-mediated endocytosis
    • Mettlen M, Pucadyil T, Ramachandran R, Schmid SL. 2009. Dissecting dynamin's role in clathrin-mediated endocytosis. Biochem Soc Trans 37: 1022-1026. http://dx.doi.org/10.1042/BST0371022.
    • (2009) Biochem Soc Trans , vol.37 , pp. 1022-1026
    • Mettlen, M.1    Pucadyil, T.2    Ramachandran, R.3    Schmid, S.L.4
  • 39
    • 84872835489 scopus 로고    scopus 로고
    • Targeting membrane trafficking in infection prophylaxis: dynamin inhibitors
    • Harper CB, Popoff MR, McCluskey A, Robinson PJ, Meunier FA. 2013. Targeting membrane trafficking in infection prophylaxis: dynamin inhibitors. Trends Cell Biol 23:90-101. http://dx.doi.org/10.1016/j.tcb.2012.10.007.
    • (2013) Trends Cell Biol , vol.23 , pp. 90-101
    • Harper, C.B.1    Popoff, M.R.2    McCluskey, A.3    Robinson, P.J.4    Meunier, F.A.5
  • 40
    • 84865070369 scopus 로고    scopus 로고
    • A programmable dual-RNA-guided DNA endonuclease in adaptive bacterial immunity
    • Jinek M, Chylinski K, Fonfara I, Hauer M, Doudna JA, Charpentier E. 2012. A programmable dual-RNA-guided DNA endonuclease in adaptive bacterial immunity. Science 337:816-821. http://dx.doi.org/10.1126/science.1225829.
    • (2012) Science , vol.337 , pp. 816-821
    • Jinek, M.1    Chylinski, K.2    Fonfara, I.3    Hauer, M.4    Doudna, J.A.5    Charpentier, E.6
  • 42
    • 84922015344 scopus 로고    scopus 로고
    • CRISPR-Cas-mediated targeted genome editing in human cells
    • Yang L, Mali P, Kim-Kiselak C, Church G. 2014. CRISPR-Cas-mediated targeted genome editing in human cells. Methods Mol Biol 1114:245-267. http://dx.doi.org/10.1007/978-1-62703-761-7_16.
    • (2014) Methods Mol Biol , vol.1114 , pp. 245-267
    • Yang, L.1    Mali, P.2    Kim-Kiselak, C.3    Church, G.4
  • 43
    • 0037436506 scopus 로고    scopus 로고
    • Dissecting temporal and spatial control of cytokinesis with a myosin II Inhibitor
    • Straight AF, Cheung A, Limouze J, Chen I, Westwood NJ, Sellers JR, Mitchison TJ. 2003. Dissecting temporal and spatial control of cytokinesis with a myosin II Inhibitor. Science 299:1743-1747. http://dx.doi.org/10.1126/science.1081412.
    • (2003) Science , vol.299 , pp. 1743-1747
    • Straight, A.F.1    Cheung, A.2    Limouze, J.3    Chen, I.4    Westwood, N.J.5    Sellers, J.R.6    Mitchison, T.J.7
  • 44
    • 84869238905 scopus 로고    scopus 로고
    • Rift Valley fever virus strain MP-12 enters mammalian host cells via caveola-mediated endocytosis
    • Harmon B, Schudel BR, Maar D, Kozina C, Ikegami T, Tseng CT, Negrete OA. 2012. Rift Valley fever virus strain MP-12 enters mammalian host cells via caveola-mediated endocytosis. J Virol 86:12954-12970. http://dx.doi.org/10.1128/JVI.02242-12.
    • (2012) J Virol , vol.86 , pp. 12954-12970
    • Harmon, B.1    Schudel, B.R.2    Maar, D.3    Kozina, C.4    Ikegami, T.5    Tseng, C.T.6    Negrete, O.A.7
  • 45
    • 83455224789 scopus 로고    scopus 로고
    • Cellular membrane cholesterol is required for porcine reproductive and respiratory syndrome virus entry and release in MARC-145 cells
    • Sun Y, Xiao S, Wang D, Luo R, Li B, Chen H, Fang L. 2011. Cellular membrane cholesterol is required for porcine reproductive and respiratory syndrome virus entry and release in MARC-145 cells. Sci China Life Sci 54:1011-1018. http://dx.doi.org/10.1007/s11427-011-4236-0.
    • (2011) Sci China Life Sci , vol.54 , pp. 1011-1018
    • Sun, Y.1    Xiao, S.2    Wang, D.3    Luo, R.4    Li, B.5    Chen, H.6    Fang, L.7
  • 47
    • 19144365133 scopus 로고    scopus 로고
    • Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection
    • Chandran K, Sullivan NJ, Felbor U, Whelan SP, Cunningham JM. 2005. Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection. Science 308:1643-1645. http://dx.doi.org/10.1126/science.1110656.
    • (2005) Science , vol.308 , pp. 1643-1645
    • Chandran, K.1    Sullivan, N.J.2    Felbor, U.3    Whelan, S.P.4    Cunningham, J.M.5
  • 48
    • 33645788357 scopus 로고    scopus 로고
    • Role of endosomal cathepsins in entry mediated by the Ebola virus glycoprotein
    • Schornberg K, Matsuyama S, Kabsch K, Delos S, Bouton A, White J. 2006. Role of endosomal cathepsins in entry mediated by the Ebola virus glycoprotein. J Virol 80:4174-4178. http://dx.doi.org/10.1128/JVI.80.8.4174-4178.2006.
    • (2006) J Virol , vol.80 , pp. 4174-4178
    • Schornberg, K.1    Matsuyama, S.2    Kabsch, K.3    Delos, S.4    Bouton, A.5    White, J.6
  • 49
    • 84887169848 scopus 로고    scopus 로고
    • Middle East respiratory syndrome coronavirus infection mediated by the transmembrane serine protease TMPRSS2
    • Shirato K, Kawase M, Matsuyama S. 2013. Middle East respiratory syndrome coronavirus infection mediated by the transmembrane serine protease TMPRSS2. J Virol 87:12552-12561. http://dx.doi.org/10.1128/JVI.01890-13.
    • (2013) J Virol , vol.87 , pp. 12552-12561
    • Shirato, K.1    Kawase, M.2    Matsuyama, S.3
  • 50
    • 23844448345 scopus 로고    scopus 로고
    • Inhibitors of cathepsin L prevent severe acute respiratory syndrome coronavirus entry
    • Simmons G, Gosalia DN, Rennekamp AJ, Reeves JD, Diamond SL, Bates P. 2005. Inhibitors of cathepsin L prevent severe acute respiratory syndrome coronavirus entry. Proc Natl Acad Sci USA 102:11876-11881. http://dx.doi.org/10.1073/pnas.0505577102.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 11876-11881
    • Simmons, G.1    Gosalia, D.N.2    Rennekamp, A.J.3    Reeves, J.D.4    Diamond, S.L.5    Bates, P.6
  • 51
    • 84884826544 scopus 로고    scopus 로고
    • Role of the spike glycoprotein of human Middle East respiratory syndrome coronavirus (MERS-CoV) in virus entry and syncytia formation
    • Qian Z, Dominguez SR, Holmes KV. 2013. Role of the spike glycoprotein of human Middle East respiratory syndrome coronavirus (MERS-CoV) in virus entry and syncytia formation. PLoS One 8:e76469. http://dx.doi.org/10.1371/journal.pone.0076469.
    • (2013) PLoS One , vol.8
    • Qian, Z.1    Dominguez, S.R.2    Holmes, K.V.3
  • 52
    • 65449120034 scopus 로고    scopus 로고
    • Virus entry by macropinocytosis
    • Mercer J, Helenius A. 2009. Virus entry by macropinocytosis. Nat Cell Biol 11:510-520. http://dx.doi.org/10.1038/ncb0509-510.
    • (2009) Nat Cell Biol , vol.11 , pp. 510-520
    • Mercer, J.1    Helenius, A.2
  • 53
    • 77952692673 scopus 로고    scopus 로고
    • Virus entry by endocytosis
    • Mercer J, Schelhaas M, Helenius A. 2010. Virus entry by endocytosis. Annu Rev Biochem 79:803-833. http://dx.doi.org/10.1146/annurev-biochem-060208-104626.
    • (2010) Annu Rev Biochem , vol.79 , pp. 803-833
    • Mercer, J.1    Schelhaas, M.2    Helenius, A.3
  • 55
    • 0028014372 scopus 로고
    • Vacuolar ATPase activity is required for endosomal carrier vesicle formation
    • Clague MJ, Urbe S, Aniento F, Gruenberg J. 1994. Vacuolar ATPase activity is required for endosomal carrier vesicle formation. J Biol Chem 269:21-24.
    • (1994) J Biol Chem , vol.269 , pp. 21-24
    • Clague, M.J.1    Urbe, S.2    Aniento, F.3    Gruenberg, J.4
  • 56
    • 33749033380 scopus 로고    scopus 로고
    • A novel role for phagocytosis-like uptake in herpes simplex virus entry
    • Clement C, Tiwari V, Scanlan PM, Valyi-Nagy T, Yue BY, Shukla D. 2006. A novel role for phagocytosis-like uptake in herpes simplex virus entry. J Cell Biol 174:1009-1021. http://dx.doi.org/10.1083/jcb.200509155.
    • (2006) J Cell Biol , vol.174 , pp. 1009-1021
    • Clement, C.1    Tiwari, V.2    Scanlan, P.M.3    Valyi-Nagy, T.4    Yue, B.Y.5    Shukla, D.6
  • 59
    • 84875923278 scopus 로고    scopus 로고
    • From endocytosis to membrane fusion: emerging roles of dynamin in virus entry
    • Sun Y, Tien P. 2013. From endocytosis to membrane fusion: emerging roles of dynamin in virus entry. Crit Rev Microbiol 39:166-179. http://dx.doi.org/10.3109/1040841X.2012.694412.
    • (2013) Crit Rev Microbiol , vol.39 , pp. 166-179
    • Sun, Y.1    Tien, P.2
  • 60
    • 70349664832 scopus 로고    scopus 로고
    • Cell entry of Borna disease virus follows a clathrin-mediated endocytosis pathway that requires Rab5 and microtubules
    • Clemente R, de la Torre JC. 2009. Cell entry of Borna disease virus follows a clathrin-mediated endocytosis pathway that requires Rab5 and microtubules. J Virol 83:10406-10416. http://dx.doi.org/10.1128/JVI.00990-09.
    • (2009) J Virol , vol.83 , pp. 10406-10416
    • Clemente, R.1    de la Torre, J.C.2
  • 62
    • 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 SciU S A 105:11790-11795. http://dx.doi.org/10.1073/pnas.0803711105.
    • (2008) Proc Natl Acad SciU S A , vol.105 , pp. 11790-11795
    • Chen, C.1    Zhuang, X.2
  • 63
    • 0019976569 scopus 로고
    • Pathway of vesicular stomatitis virus entry leading to infection
    • Matlin KS, Reggio H, Helenius A, Simons K. 1982. Pathway of vesicular stomatitis virus entry leading to infection. J Mol Biol 156:609-631. http://dx.doi.org/10.1016/0022-2836(82)90269-8.
    • (1982) J Mol Biol , vol.156 , pp. 609-631
    • Matlin, K.S.1    Reggio, H.2    Helenius, A.3    Simons, K.4
  • 64
    • 78249252059 scopus 로고    scopus 로고
    • Come in and take your coat off-how host cells provide endocytosis for virus entry
    • Schelhaas M. 2010. Come in and take your coat off-how host cells provide endocytosis for virus entry. Cell Microbiol 12:1378-1388. http://dx.doi.org/10.1111/j.1462-5822.2010.01510.x.
    • (2010) Cell Microbiol , vol.12 , pp. 1378-1388
    • Schelhaas, M.1
  • 65
    • 0018827560 scopus 로고
    • Three-dimensional visualization of coated vesicle formation in fibroblasts
    • Heuser J. 1980. Three-dimensional visualization of coated vesicle formation in fibroblasts. J Cell Biol 84:560-583. http://dx.doi.org/10.1083/jcb.84.3.560.
    • (1980) J Cell Biol , vol.84 , pp. 560-583
    • Heuser, J.1
  • 66
    • 0033153279 scopus 로고    scopus 로고
    • Functional organization of clathrin in coats: combining electron cryomicroscopy and X-ray crystallography
    • Musacchio A, Smith CJ, Roseman AM, Harrison SC, Kirchhausen T, Pearse BM. 1999. Functional organization of clathrin in coats: combining electron cryomicroscopy and X-ray crystallography. Mol Cell 3:761-770. http://dx.doi.org/10.1016/S1097-2765(01)80008-3.
    • (1999) Mol Cell , vol.3 , pp. 761-770
    • Musacchio, A.1    Smith, C.J.2    Roseman, A.M.3    Harrison, S.C.4    Kirchhausen, T.5    Pearse, B.M.6
  • 67
    • 84870212873 scopus 로고    scopus 로고
    • Diversity of clathrin function: new tricks for an old protein
    • Brodsky FM. 2012. Diversity of clathrin function: new tricks for an old protein. Annu Rev Cell Dev Biol 28:309-336. http://dx.doi.org/10.1146/annurev-cellbio-101011-155716.
    • (2012) Annu Rev Cell Dev Biol , vol.28 , pp. 309-336
    • Brodsky, F.M.1
  • 68
    • 0037422066 scopus 로고    scopus 로고
    • Regulated portals of entry into the cell
    • Conner SD, Schmid SL. 2003. Regulated portals of entry into the cell. Nature 422:37-44. http://dx.doi.org/10.1038/nature01451.
    • (2003) Nature , vol.422 , pp. 37-44
    • Conner, S.D.1    Schmid, S.L.2
  • 69
    • 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. http://dx.doi.org/10.1126/science.1155164.
    • (2008) Science , vol.320 , pp. 531-535
    • Mercer, J.1    Helenius, A.2
  • 70
    • 84861868826 scopus 로고    scopus 로고
    • Roles for actin assembly in endocytosis
    • Mooren OL, Galletta BJ, Cooper JA. 2012. Roles for actin assembly in endocytosis. Annu Rev Biochem 81:661-686. http://dx.doi.org/10.1146/annurev-biochem-060910-094416.
    • (2012) Annu Rev Biochem , vol.81 , pp. 661-686
    • Mooren, O.L.1    Galletta, B.J.2    Cooper, J.A.3
  • 71
    • 34147138587 scopus 로고    scopus 로고
    • Role of lipids and actin in the formation of clathrin-coated pits
    • Boucrot E, Saffarian S, Massol R, Kirchhausen T, Ehrlich M. 2006. Role of lipids and actin in the formation of clathrin-coated pits. Exp Cell Res 312:4036-4048. http://dx.doi.org/10.1016/j.yexcr.2006.09.025.
    • (2006) Exp Cell Res , vol.312 , pp. 4036-4048
    • Boucrot, E.1    Saffarian, S.2    Massol, R.3    Kirchhausen, T.4    Ehrlich, M.5
  • 72
    • 26844517614 scopus 로고    scopus 로고
    • A modular design for the clathrin-and actin-mediated endocytosis machinery
    • Kaksonen M, Toret CP, Drubin DG. 2005. A modular design for the clathrin-and actin-mediated endocytosis machinery. Cell 123:305-320. http://dx.doi.org/10.1016/j.cell.2005.09.024.
    • (2005) Cell , vol.123 , pp. 305-320
    • Kaksonen, M.1    Toret, C.P.2    Drubin, D.G.3
  • 73
    • 0037684840 scopus 로고    scopus 로고
    • Caveolae/raft-dependent endocytosis
    • Nabi IR, Le PU. 2003. Caveolae/raft-dependent endocytosis. J Cell Biol 161:673-677. http://dx.doi.org/10.1083/jcb.200302028.
    • (2003) J Cell Biol , vol.161 , pp. 673-677
    • Nabi, I.R.1    Le, P.U.2

* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.