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Volumn 79, Issue 4, 2015, Pages 403-418

Cell Walls and the Convergent Evolution of the Viral Envelope

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Indexed keywords

RIBONUCLEOPROTEIN;

EID: 84948414254     PISSN: 10922172     EISSN: 10985557     Source Type: Journal    
DOI: 10.1128/MMBR.00017-15     Document Type: Review
Times cited : (27)

References (245)
  • 1
    • 77953210064 scopus 로고    scopus 로고
    • Beyond the green: Understanding the evolutionary puzzle of plant and algal cell walls
    • Popper ZA, Tuohy MG. 2010. Beyond the green: understanding the evolutionary puzzle of plant and algal cell walls. Plant Physiol 153:373-383. http://dx.doi.org/10.1104/pp.110.158055.
    • (2010) Plant Physiol , vol.153 , pp. 373-383
    • Popper, Z.A.1    Tuohy, M.G.2
  • 2
    • 22444447926 scopus 로고    scopus 로고
    • The cell walls that bind the tree of life
    • Niklas KJ. 2004. The cell walls that bind the tree of life. BioScience 54: 831-841. http://dx.doi.org/10.1641/0006-3568(2004)054[0831:TCWTBT ]2.0.CO;2.
    • (2004) BioScience , vol.54 , pp. 831-841
    • Niklas, K.J.1
  • 4
    • 0036096326 scopus 로고    scopus 로고
    • Cellular impermeability and uptake of biocides and antibiotics in Gram-positive bacteria and mycobacteria
    • Lambert PA. 2002. Cellular impermeability and uptake of biocides and antibiotics in Gram-positive bacteria and mycobacteria. J Appl Microbiol 92(Suppl):46S-54S. http://dx.doi.org/10.1046/j.1365-2672.92.5s1.7.x.
    • (2002) J Appl Microbiol , vol.92 , pp. 46S-54S
    • Lambert, P.A.1
  • 5
    • 0001578915 scopus 로고
    • The permeability of plant cell walls as measured by gel filtration chromatography
    • Tepfer M, Taylor IE. 1981. The permeability of plant cell walls as measured by gel filtration chromatography. Science 213:761-763. http://dx .doi.org/10.1126/science.213.4509.761.
    • (1981) Science , vol.213 , pp. 761-763
    • Tepfer, M.1    Taylor, I.E.2
  • 7
    • 24944498782 scopus 로고
    • Cell coverings of microalgae
    • Berner T (ed), CRC Press, Boca Raton, FL
    • Leadbeater BSC, Green JC. 1993. Cell coverings of microalgae, p 71-98. In Berner T (ed), Ultrastructure of microalgae. CRC Press, Boca Raton, FL.
    • (1993) Ultrastructure of Microalgae , pp. 71-98
    • Leadbeater, B.S.C.1    Green, J.C.2
  • 9
    • 0028212959 scopus 로고
    • Cell wall biochemistry and three-domain concept of life
    • Kandler O. 1994. Cell wall biochemistry and three-domain concept of life. Syst Appl Microbiol 16:501-509.
    • (1994) Syst Appl Microbiol , vol.16 , pp. 501-509
    • Kandler, O.1
  • 10
    • 0031945225 scopus 로고    scopus 로고
    • Cell wall polymers in Archaea (Archaebacteria)
    • Kandler O, König H. 1998. Cell wall polymers in Archaea (Archaebacteria). Cell Mol Life Sci 54:305-308. http://dx.doi.org/10.1007/s00018 0050156.
    • (1998) Cell Mol Life Sci , vol.54 , pp. 305-308
    • Kandler, O.1    König, H.2
  • 12
    • 79956100429 scopus 로고    scopus 로고
    • The archaeal cell envelope
    • Albers S-V, Meyer BH. 2011. The archaeal cell envelope. Nat Rev Microbiol 9:414-426. http://dx.doi.org/10.1038/nrmicro2576.
    • (2011) Nat Rev Microbiol , vol.9 , pp. 414-426
    • Albers, S.-V.1    Meyer, B.H.2
  • 13
    • 84948400240 scopus 로고    scopus 로고
    • Biochemistry and molecular biology education, p 126-128
    • Lodish H, Berk A, Zipursky SL, Matsudaira P, Baltimore D, Darnell J, 4th ed.WHFreeman&Co., New York, NY
    • Uzman A. 1999. Biochemistry and molecular biology education, p 126-128. In Lodish H, Berk A, Zipursky SL, Matsudaira P, Baltimore D, Darnell J, Molecular cell biology, 4th ed.WHFreeman&Co., New York, NY.
    • (1999) Molecular Cell Biology
    • Uzman, A.1
  • 14
    • 3242665450 scopus 로고    scopus 로고
    • The origin of phospholipids of the enveloped bacteriophage 6
    • Laurinavicius S, Käkelä R, Bamford DH, Somerharju P. 2004. The origin of phospholipids of the enveloped bacteriophage 6. Virology 326:182-190. http://dx.doi.org/10.1016/j.virol.2004.05.021.
    • (2004) Virology , vol.326 , pp. 182-190
    • Laurinavicius, S.1    Käkelä, R.2    Bamford, D.H.3    Somerharju, P.4
  • 15
    • 34248229690 scopus 로고    scopus 로고
    • More than one door-budding of enveloped viruses through cellular membranes
    • Welsch S, Müller B, Kräusslich H-G. 2007. More than one door-budding of enveloped viruses through cellular membranes. FEBS Lett 581:2089-2097. http://dx.doi.org/10.1016/j.febslet.2007.03.060.
    • (2007) FEBS Lett , vol.581 , pp. 2089-2097
    • Welsch, S.1    Müller, B.2    Kräusslich, H.-G.3
  • 16
    • 33947585383 scopus 로고    scopus 로고
    • Virus transmission- getting out and in, p 1-28
    • Waigmann E, HeinleinM(ed), Springer, Berlin, Germany
    • Blanc S. 2007. Virus transmission- getting out and in, p 1-28. In Waigmann E, HeinleinM(ed), Viral transport in plants, vol 7. Springer, Berlin, Germany.
    • (2007) Viral Transport in Plants , vol.7
    • Blanc, S.1
  • 17
    • 84877898099 scopus 로고    scopus 로고
    • Virus entry at a glance
    • Yamauchi Y, Helenius A. 2013. Virus entry at a glance. J Cell Sci 126: 1289-1295. http://dx.doi.org/10.1242/jcs.119685.
    • (2013) J Cell Sci , vol.126 , pp. 1289-1295
    • Yamauchi, Y.1    Helenius, A.2
  • 18
    • 84905435323 scopus 로고    scopus 로고
    • Localizing viruses in their insect vectors
    • Blanc S, Drucker M, Uzest M. 2014. Localizing viruses in their insect vectors. Annu Rev Phytopathol 52:403-425. http://dx.doi.org/10.1146/annurev-phyto-102313-045920.
    • (2014) Annu Rev Phytopathol , vol.52 , pp. 403-425
    • Blanc, S.1    Drucker, M.2    Uzest, M.3
  • 19
    • 69449086077 scopus 로고    scopus 로고
    • No strings attached: The ESCRT machinery in viral budding and cytokinesis
    • McDonald B, Martin-Serrano J. 2009. No strings attached: The ESCRT machinery in viral budding and cytokinesis. J Cell Sci 122:2167-2177. http://dx.doi.org/10.1242/jcs.028308.
    • (2009) J Cell Sci , vol.122 , pp. 2167-2177
    • McDonald, B.1    Martin-Serrano, J.2
  • 20
    • 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
  • 21
    • 77954325765 scopus 로고    scopus 로고
    • Lifestyles of plant viruses
    • Roossinck MJ. 2010. Lifestyles of plant viruses. Philos Trans R Soc Lond B Biol Sci 365:1899-1905. http://dx.doi.org/10.1098/rstb.2010.0057.
    • (2010) Philos Trans R Soc Lond B Biol Sci , vol.365 , pp. 1899-1905
    • Roossinck, M.J.1
  • 23
    • 85007895151 scopus 로고
    • A chilo iridescent virus (CIV) from the rice stem borer, Chilo suppressalis Walker (Lepidoptera: Pyralidae)
    • Fukaya M, Nasu S. 1966. A chilo iridescent virus (CIV) from the rice stem borer, Chilo suppressalis Walker (Lepidoptera: Pyralidae). Appl Entomol Zool 1:69-72.
    • (1966) Appl Entomol Zool , vol.1 , pp. 69-72
    • Fukaya, M.1    Nasu, S.2
  • 24
    • 0031881860 scopus 로고    scopus 로고
    • Is the major capsid protein of iridoviruses a suitable target for the study of viral evolution?
    • Tidona CA, Schnitzler P, Kehm R, Darai G. 1998. Is the major capsid protein of iridoviruses a suitable target for the study of viral evolution? Virus Genes 16:59-66. http://dx.doi.org/10.1023/A:1007949710031.
    • (1998) Virus Genes , vol.16 , pp. 59-66
    • Tidona, C.A.1    Schnitzler, P.2    Kehm, R.3    Darai, G.4
  • 25
    • 84255195107 scopus 로고    scopus 로고
    • Shaping development with ESCRTs
    • Rusten TE, Vaccari T, Stenmark H. 2012. Shaping development with ESCRTs. Nat Cell Biol 14:38-45. http://dx.doi.org/10.1038/nrm3495.
    • (2012) Nat Cell Biol , vol.14 , pp. 38-45
    • Rusten, T.E.1    Vaccari, T.2    Stenmark, H.3
  • 26
    • 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
  • 27
    • 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
  • 28
    • 0018853517 scopus 로고
    • On the entry of Semliki forest virus into BHK-21 cells
    • Helenius A, Kartenbeck J, Simons K, Fries E. 1980. On the entry of Semliki forest virus into BHK-21 cells. J Cell Biol 84:404-420. http://dx .doi.org/10.1083/jcb.84.2.404.
    • (1980) J Cell Biol , vol.84 , pp. 404-420
    • Helenius, A.1    Kartenbeck, J.2    Simons, K.3    Fries, E.4
  • 29
    • 0029154615 scopus 로고
    • Virus-mediated release of endosomal content in vitro: Different behavior of adenovirus and rhinovirus serotype 2
    • Prchla E, Plank C, Wagner E, Blaas D, Fuchs R. 1995. Virus-mediated release of endosomal content in vitro: different behavior of adenovirus and rhinovirus serotype 2. J Cell Biol 131:111-123. http://dx.doi.org/10 .1083/jcb.131.1.111.
    • (1995) J Cell Biol , vol.131 , pp. 111-123
    • Prchla, E.1    Plank, C.2    Wagner, E.3    Blaas, D.4    Fuchs, R.5
  • 30
    • 0031883836 scopus 로고    scopus 로고
    • Major and minor receptor group human rhinoviruses penetrate from endosomes by different mechanisms
    • Schober D, Kronenberger P, Prchla E, Blaas D, Fuchs R. 1998. Major and minor receptor group human rhinoviruses penetrate from endosomes by different mechanisms. J Virol 72:1354-1364.
    • (1998) J Virol , vol.72 , pp. 1354-1364
    • Schober, D.1    Kronenberger, P.2    Prchla, E.3    Blaas, D.4    Fuchs, R.5
  • 32
    • 79955051520 scopus 로고    scopus 로고
    • The soluble serum protein Gas6 bridges virion envelope phosphatidylserine to the TAM receptor tyrosine kinase Axl to mediate viral entry
    • Morizono K, Xie Y, Olafsen T, Lee B, Dasgupta A, Wu AM, Chen ISY. 2011. The soluble serum protein Gas6 bridges virion envelope phosphatidylserine to the TAM receptor tyrosine kinase Axl to mediate viral entry. Cell Host Microbe 9:286-298. http://dx.doi.org/10.1016/j.chom .2011.03.012.
    • (2011) Cell Host Microbe , vol.9 , pp. 286-298
    • Morizono, K.1    Xie, Y.2    Olafsen, T.3    Lee, B.4    Dasgupta, A.5    Wu, A.M.6    Chen, I.S.Y.7
  • 35
    • 79959829850 scopus 로고    scopus 로고
    • Clathrin mediates endocytosis and polar distribution of PIN auxin transporters in Arabidopsis
    • Kitakura S, Vanneste S, Robert S, Löfke C, Teichmann T, Tanaka H, Friml J. 2011. Clathrin mediates endocytosis and polar distribution of PIN auxin transporters in Arabidopsis. Plant Cell 23:1920-1931. http://dx.doi.org/10.1105/tpc.111.083030.
    • (2011) Plant Cell , vol.23 , pp. 1920-1931
    • Kitakura, S.1    Vanneste, S.2    Robert, S.3    Löfke, C.4    Teichmann, T.5    Tanaka, H.6    Friml, J.7
  • 37
    • 0021169826 scopus 로고
    • Gemmata obscuriglobus, a new genus and species of the budding bacteria
    • Franzmann PD, Skerman VB. 1984. Gemmata obscuriglobus, a new genus and species of the budding bacteria. Antonie Van Leeuwenhoek 50:261-268. http://dx.doi.org/10.1007/BF02342136.
    • (1984) Antonie van Leeuwenhoek , vol.50 , pp. 261-268
    • Franzmann, P.D.1    Skerman, V.B.2
  • 38
    • 0029847806 scopus 로고    scopus 로고
    • Crystal structure of the Aequorea Victoria green fluorescent protein
    • Ormö M, Cubitt AB, Kallio K, Gross LA, Tsien RY, Remington SJ. 1996. Crystal structure of the Aequorea victoria green fluorescent protein. Science 273:1392-1395. http://dx.doi.org/10.1126/science.273.5280.1392.
    • (1996) Science , vol.273 , pp. 1392-1395
    • Ormö, M.1    Cubitt, A.B.2    Kallio, K.3    Gross, L.A.4    Tsien, R.Y.5    Remington, S.J.6
  • 39
    • 0029780351 scopus 로고    scopus 로고
    • The molecular structure of green fluorescent protein
    • Yang F, Moss LG, Phillips JGN. 1996. The molecular structure of green fluorescent protein. Nat Biotechnol 14:1246-1251. http://dx.doi.org/10 .1038/nbt1096-1246.
    • (1996) Nat Biotechnol , vol.14 , pp. 1246-1251
    • Yang, F.1    Moss, L.G.2    Phillips, J.G.N.3
  • 40
    • 84887929250 scopus 로고    scopus 로고
    • Filamentous plant pathogen effectors in action
    • Giraldo MC, Valent B. 2013. Filamentous plant pathogen effectors in action. Nat Rev Microbiol 11:800-814. http://dx.doi.org/10.1038/nrmicro3119.
    • (2013) Nat Rev Microbiol , vol.11 , pp. 800-814
    • Giraldo, M.C.1    Valent, B.2
  • 41
    • 0036197728 scopus 로고    scopus 로고
    • Transmission by Olpidium brassicae of Mirafiori lettuce virus and Lettuce bigvein virus, and their roles in lettuce big-vein etiology
    • Lot H, Campbell RN, Souche S, Milne RG, Roggero P. 2002. Transmission by Olpidium brassicae of Mirafiori lettuce virus and Lettuce bigvein virus, and their roles in lettuce big-vein etiology. Phytopathology 92:288-293. http://dx.doi.org/10.1094/PHYTO.2002.92.3.288.
    • (2002) Phytopathology , vol.92 , pp. 288-293
    • Lot, H.1    Campbell, R.N.2    Souche, S.3    Milne, R.G.4    Roggero, P.5
  • 42
    • 0004250845 scopus 로고    scopus 로고
    • 6th ed. Wolters Kluwer Health/Lippincott Williams & Wilkins, Philadelphia, PA
    • Fields BN, Knipe DM, Howley PM (ed). 2013. Fields virology, 6th ed. Wolters Kluwer Health/Lippincott Williams & Wilkins, Philadelphia, PA.
    • (2013) Fields Virology
    • Fields, B.N.1    Knipe, D.M.2    Howley, P.M.3
  • 43
    • 50549173053 scopus 로고
    • Transmission of soil-borne viruses through seed
    • Lister RM. 1960. Transmission of soil-borne viruses through seed. Virology 10:547-549. http://dx.doi.org/10.1016/0042-6822(60)90138-0.
    • (1960) Virology , vol.10 , pp. 547-549
    • Lister, R.M.1
  • 44
    • 0346599192 scopus 로고    scopus 로고
    • Unusual life style of giant chlorella viruses
    • Van Etten JL. 2003. Unusual life style of giant chlorella viruses. Annu Rev Genet 37:153-195. http://dx.doi.org/10.1146/annurev.genet.37 .110801.143915.
    • (2003) Annu Rev Genet , vol.37 , pp. 153-195
    • Van Etten, J.L.1
  • 48
    • 0023337259 scopus 로고
    • Membrane fusion in prokaryotes: Bacteriophage 6 membrane fuses with the Pseudomonas syringae outer membrane
    • Bamford DH, Romantschuk M, Somerharju PJ. 1987. Membrane fusion in prokaryotes: bacteriophage 6 membrane fuses with the Pseudomonas syringae outer membrane. EMBO J 6:1467-1473.
    • (1987) EMBO J , vol.6 , pp. 1467-1473
    • Bamford, D.H.1    Romantschuk, M.2    Somerharju, P.J.3
  • 49
    • 16244394849 scopus 로고    scopus 로고
    • Penetration of enveloped double-stranded RNA bacteriophages 13 and 6 into Pseudomonas syringae cells
    • Daugelavicius R, Cvirkaite V, Gaidelyte A, Bakiene E, Gabrenaite-Verkhovskaya R, Bamford DH. 2005. Penetration of enveloped double-stranded RNA bacteriophages 13 and 6 into Pseudomonas syringae cells. J Virol 79:5017-5026. http://dx.doi.org/10.1128/JVI.79.8 .5017-5026.2005.
    • (2005) J Virol , vol.79 , pp. 5017-5026
    • Daugelavicius, R.1    Cvirkaite, V.2    Gaidelyte, A.3    Bakiene, E.4    Gabrenaite-Verkhovskaya, R.5    Bamford, D.H.6
  • 51
    • 27944481316 scopus 로고    scopus 로고
    • Membrane proteins modulate the bilayer curvature in the bacterial virus Bam35
    • Laurinmäki PA, Huiskonen JT, Bamford DH, Butcher SJ. 2005. Membrane proteins modulate the bilayer curvature in the bacterial virus Bam35. Structure 13:1819-1828. http://dx.doi.org/10.1016/j.str.2005.08 .020.
    • (2005) Structure , vol.13 , pp. 1819-1828
    • Laurinmäki, P.A.1    Huiskonen, J.T.2    Bamford, D.H.3    Butcher, S.J.4
  • 52
    • 0036887159 scopus 로고    scopus 로고
    • Sequential model of phage PRD1 DNA delivery: Active involvement of the viral membrane
    • Grahn AM, Daugelavicius R, Bamford DH. 2002. Sequential model of phage PRD1 DNA delivery: active involvement of the viral membrane. Mol Microbiol 46:1199-1209. http://dx.doi.org/10.1046/j.1365-2958 .2002.03250.x.
    • (2002) Mol Microbiol , vol.46 , pp. 1199-1209
    • Grahn, A.M.1    Daugelavicius, R.2    Bamford, D.H.3
  • 53
    • 84921755292 scopus 로고    scopus 로고
    • Probing protein interactions in the membrane-containing virus PRD1
    • Mattila S, Oksanen HM, Bamford JKH. 2015. Probing protein interactions in the membrane-containing virus PRD1. J Gen Virol 96:453-462. http://dx.doi.org/10.1099/vir.0.069187-0.
    • (2015) J Gen Virol , vol.96 , pp. 453-462
    • Mattila, S.1    Oksanen, H.M.2    Bamford, J.K.H.3
  • 54
    • 0345687907 scopus 로고    scopus 로고
    • The Bacillus thuringiensis linear double-stranded DNA phage Bam35, which is highly similar to the Bacillus cereus linear plasmid pBClin15, has a prophage state
    • Strömsten NJ, Benson SD, Burnett RM, Bamford DH, Bamford JKH. 2003. The Bacillus thuringiensis linear double-stranded DNA phage Bam35, which is highly similar to the Bacillus cereus linear plasmid pBClin15, has a prophage state. J Bacteriol 185:6985-6989. http://dx.doi .org/10.1128/JB.185.23.6985-6989.2003.
    • (2003) J Bacteriol , vol.185 , pp. 6985-6989
    • Strömsten, N.J.1    Benson, S.D.2    Burnett, R.M.3    Bamford, D.H.4    Bamford, J.K.H.5
  • 55
    • 18244365103 scopus 로고    scopus 로고
    • The linear double-stranded DNA of phage Bam35 enters lysogenic host cells, but the late phage functions are suppressed
    • Gaidelyte A, Jaatinen ST, Daugelavicius R, Bamford JKH, Bamford DH. 2005. The linear double-stranded DNA of phage Bam35 enters lysogenic host cells, but the late phage functions are suppressed. J Bacteriol 187:3521-3527. http://dx.doi.org/10.1128/JB.187.10.3521-3527.2005.
    • (2005) J Bacteriol , vol.187 , pp. 3521-3527
    • Gaidelyte, A.1    Jaatinen, S.T.2    Daugelavicius, R.3    Bamford, J.K.H.4    Bamford, D.H.5
  • 56
    • 33748663313 scopus 로고    scopus 로고
    • The entry mechanism of membrane-containing phage Bam35 infecting Bacillus thuringiensis
    • Gaidelyte A, Cvirkaite-Krupovic V, Daugelavicius R, Bamford JKH, Bamford DH. 2006. The entry mechanism of membrane-containing phage Bam35 infecting Bacillus thuringiensis. J Bacteriol 188:5925-5934. http://dx.doi.org/10.1128/JB.00107-06.
    • (2006) J Bacteriol , vol.188 , pp. 5925-5934
    • Gaidelyte, A.1    Cvirkaite-Krupovic, V.2    Daugelavicius, R.3    Bamford, J.K.H.4    Bamford, D.H.5
  • 57
    • 0030755555 scopus 로고    scopus 로고
    • Changes in host cell energetics in response to bacteriophage PRD1 DNA entry
    • Daugelavicius R, Bamford JK, Bamford DH. 1997. Changes in host cell energetics in response to bacteriophage PRD1 DNA entry. J Bacteriol 179:5203-5210.
    • (1997) J Bacteriol , vol.179 , pp. 5203-5210
    • Daugelavicius, R.1    Bamford, J.K.2    Bamford, D.H.3
  • 58
    • 84948394353 scopus 로고    scopus 로고
    • Plasmavirus, p 1341-1345
    • Tidona C, Darai G (ed), Springer, New York, NY
    • Maniloff J. 2011. Plasmavirus, p 1341-1345. In Tidona C, Darai G (ed), The Springer index of viruses. Springer, New York, NY.
    • (2011) The Springer Index of Viruses
    • Maniloff, J.1
  • 59
    • 31944445169 scopus 로고    scopus 로고
    • Identification and specificity of pilus adsorption proteins of filamentous bacteriophages infecting Pseudomonas aeruginosa
    • Holland SJ, Sanz C, Perham RN. 2006. Identification and specificity of pilus adsorption proteins of filamentous bacteriophages infecting Pseudomonas aeruginosa. Virology 345:540-548. http://dx.doi.org/10.1016/j .virol.2005.10.020.
    • (2006) Virology , vol.345 , pp. 540-548
    • Holland, S.J.1    Sanz, C.2    Perham, R.N.3
  • 61
    • 0030464941 scopus 로고    scopus 로고
    • Cell-tocell and long-distance transport of viruses in plants
    • Carrington JC, Kasschau KD, Mahajan SK, Schaad MC. 1996. Cell-tocell and long-distance transport of viruses in plants. Plant Cell 8:1669-1681. http://dx.doi.org/10.1105/tpc.8.10.1669.
    • (1996) Plant Cell , vol.8 , pp. 1669-1681
    • Carrington, J.C.1    Kasschau, K.D.2    Mahajan, S.K.3    Schaad, M.C.4
  • 62
    • 34250302446 scopus 로고
    • Hyphal anastomosis in Pyricularia oryzae cav
    • Chen JT, Wu HK. 1977. Hyphal anastomosis in Pyricularia oryzae cav. Protoplasma 92:281-287. http://dx.doi.org/10.1007/BF01279465.
    • (1977) Protoplasma , vol.92 , pp. 281-287
    • Chen, J.T.1    Wu, H.K.2
  • 63
    • 33751203519 scopus 로고    scopus 로고
    • Non-self recognition and programmed cell death in filamentous fungi
    • Glass NL, Dementhon K. 2006. Non-self recognition and programmed cell death in filamentous fungi. Curr Opin Microbiol 9:553-558. http://dx.doi.org/10.1016/j.mib.2006.09.001.
    • (2006) Curr Opin Microbiol , vol.9 , pp. 553-558
    • Glass, N.L.1    Dementhon, K.2
  • 64
    • 0012173279 scopus 로고
    • A comparative study of the transmission of Hyoscyamus virus 3, potato virus y and cucumber virus 1 by the vectors Myzus persicae (Sulz), M. Circumflexus (Buckton), and Macrosiphum gei (Koch)
    • Watson MA, Roberts FM. 1939. A comparative study of the transmission of Hyoscyamus virus 3, potato virus Y and cucumber virus 1 by the vectors Myzus persicae (Sulz), M. circumflexus (Buckton), and Macrosiphum gei (Koch). Proc R Soc Lond B Biol Sci 127:543-576. http://dx .doi.org/10.1098/rspb.1939.0039.
    • (1939) Proc R Soc Lond B Biol Sci , vol.127 , pp. 543-576
    • Watson, M.A.1    Roberts, F.M.2
  • 66
    • 84892557229 scopus 로고    scopus 로고
    • Viral and cellular factors involved in phloem transport of plant viruses
    • Hipper C, Brault V, Ziegler-Graff V, Revers F. 2013. Viral and cellular factors involved in phloem transport of plant viruses. Front Plant Sci 4:154. http://dx.doi.org/10.3389/fpls.2013.00154.
    • (2013) Front Plant Sci , vol.4 , pp. 154
    • Hipper, C.1    Brault, V.2    Ziegler-Graff, V.3    Revers, F.4
  • 68
    • 0028874314 scopus 로고
    • Tomato leaf curl geminivirus from India has a bipartite genome and coat protein is not essential for infectivity
    • Padidam M, Beachy RN, Fauquet CM. 1995. Tomato leaf curl geminivirus from India has a bipartite genome and coat protein is not essential for infectivity. J Gen Virol 76:25-35. http://dx.doi.org/10.1099/0022-1317-76-1-25.
    • (1995) J Gen Virol , vol.76 , pp. 25-35
    • Padidam, M.1    Beachy, R.N.2    Fauquet, C.M.3
  • 69
    • 0030588207 scopus 로고    scopus 로고
    • The role of AV2 ("precoat") and coat protein in viral replication and movement in tomato leaf curl geminivirus
    • Padidam M, Beachy RN, Fauquet CM. 1996. The role of AV2 ("precoat") and coat protein in viral replication and movement in tomato leaf curl geminivirus. Virology 224:390-404. http://dx.doi.org/10.1006/viro .1996.0546.
    • (1996) Virology , vol.224 , pp. 390-404
    • Padidam, M.1    Beachy, R.N.2    Fauquet, C.M.3
  • 70
    • 0000935989 scopus 로고
    • The capsid protein gene of tomato bushy stunt virus is dispensable for systemic movement and can be replaced for localized expression of foreign genes
    • Scholthof HB, Morirs TJ, Jackson AO. 1993. The capsid protein gene of tomato bushy stunt virus is dispensable for systemic movement and can be replaced for localized expression of foreign genes. Mol Plant Microbe Interact 6:309-322. http://dx.doi.org/10.1094/MPMI-6-309.
    • (1993) Mol Plant Microbe Interact , vol.6 , pp. 309-322
    • Scholthof, H.B.1    Morirs, T.J.2    Jackson, A.O.3
  • 71
    • 0036944628 scopus 로고    scopus 로고
    • Host-dependent recombination of a Tomato bushy stunt virus coat protein mutant yields truncated capsid subunits that form virus-like complexes which benefit systemic spread
    • Desvoyes B, Scholthof HB. 2002. Host-dependent recombination of a Tomato bushy stunt virus coat protein mutant yields truncated capsid subunits that form virus-like complexes which benefit systemic spread. Virology 304:434-442. http://dx.doi.org/10.1006/viro.2002.1714.
    • (2002) Virology , vol.304 , pp. 434-442
    • Desvoyes, B.1    Scholthof, H.B.2
  • 72
    • 0035987132 scopus 로고    scopus 로고
    • Efficient infection of Nicotiana benthamiana by Tomato bushy stunt virus is facilitated by the coat protein and maintained by p19 through suppression of gene silencing
    • Qu F, Morris TJ. 2002. Efficient infection of Nicotiana benthamiana by Tomato bushy stunt virus is facilitated by the coat protein and maintained by p19 through suppression of gene silencing. Mol Plant Microbe Interact 15:193-202. http://dx.doi.org/10.1094/MPMI.2002.15.3.193.
    • (2002) Mol Plant Microbe Interact , vol.15 , pp. 193-202
    • Qu, F.1    Morris, T.J.2
  • 73
    • 60549106098 scopus 로고    scopus 로고
    • Cellular and molecular aspects of rhabdovirus interactions with insect and plant hosts
    • Ammar E-D, Tsai C-W, Whitfield AE, Redinbaugh MG, Hogenhout SA. 2009. Cellular and molecular aspects of rhabdovirus interactions with insect and plant hosts. Annu Rev Entomol 54:447-468. http://dx .doi.org/10.1146/annurev.ento.54.110807.090454.
    • (2009) Annu Rev Entomol , vol.54 , pp. 447-468
    • Ammar, E.-D.1    Tsai, C.-W.2    Whitfield, A.E.3    Redinbaugh, M.G.4    Hogenhout, S.A.5
  • 75
    • 84867009705 scopus 로고    scopus 로고
    • Emaravirus: A novel genus of multipartite, negative strand RNA plant viruses
    • Mielke-Ehret N, Mühlbach H-P. 2012. Emaravirus: A novel genus of multipartite, negative strand RNA plant viruses. Viruses 4:1515-1536. http://dx.doi.org/10.3390/v4091515.
    • (2012) Viruses , vol.4 , pp. 1515-1536
    • Mielke-Ehret, N.1    Mühlbach, H.-P.2
  • 77
    • 0034060138 scopus 로고    scopus 로고
    • Impeded thrips transmission of defective Tomato spotted wilt virus isolates
    • Nagata T, Inoue-Nagata AK, Prins M, Goldbach R, Peters D. 2000. Impeded thrips transmission of defective Tomato spotted wilt virus isolates. Phytopathology 90:454-459. http://dx.doi.org/10.1094/PHYTO .2000.90.5.454.
    • (2000) Phytopathology , vol.90 , pp. 454-459
    • Nagata, T.1    Inoue-Nagata, A.K.2    Prins, M.3    Goldbach, R.4    Peters, D.5
  • 78
    • 8644273255 scopus 로고    scopus 로고
    • Expression and characterization of a soluble form of tomato spotted wilt virus glycoprotein GN
    • Whitfield AE, Ullman DE, German TL. 2004. Expression and characterization of a soluble form of tomato spotted wilt virus glycoprotein GN. J Virol 78:13197-13206. http://dx.doi.org/10.1128/JVI.78.23.13197-13206 .2004.
    • (2004) J Virol , vol.78 , pp. 13197-13206
    • Whitfield, A.E.1    Ullman, D.E.2    German, T.L.3
  • 79
    • 51849116462 scopus 로고    scopus 로고
    • Insect vector interactions with persistently transmitted viruses
    • Hogenhout SA, Ammar E-D, Whitfield AE, Redinbaugh MG. 2008. Insect vector interactions with persistently transmitted viruses. Annu Rev Phytopathol 46:327-359. http://dx.doi.org/10.1146/annurev.phyto .022508.092135.
    • (2008) Annu Rev Phytopathol , vol.46 , pp. 327-359
    • Hogenhout, S.A.1    Ammar, E.-D.2    Whitfield, A.E.3    Redinbaugh, M.G.4
  • 80
    • 39549095341 scopus 로고    scopus 로고
    • Mechanisms for enveloped virus budding: Can some viruses do without an ESCRT?
    • Chen BJ, Lamb RA. 2008. Mechanisms for enveloped virus budding: can some viruses do without an ESCRT? Virology 372:221-232. http://dx.doi .org/10.1016/j.virol.2007.11.008.
    • (2008) Virology , vol.372 , pp. 221-232
    • Chen, B.J.1    Lamb, R.A.2
  • 81
    • 84868557725 scopus 로고    scopus 로고
    • The spanin complex is essential for lambda lysis
    • Berry J, Rajaure M, Pang T, Young R. 2012. The spanin complex is essential for lambda lysis. J Bacteriol 194:5667-5674. http://dx.doi.org/10.1128/JB.01245-12.
    • (2012) J Bacteriol , vol.194 , pp. 5667-5674
    • Berry, J.1    Rajaure, M.2    Pang, T.3    Young, R.4
  • 82
    • 0037310365 scopus 로고    scopus 로고
    • Sizing the holin lesion with an endolysin-beta-galactosidase fusion
    • Wang I-N, Deaton J, Young R. 2003. Sizing the holin lesion with an endolysin-beta-galactosidase fusion. J Bacteriol 185:779-787. http://dx .doi.org/10.1128/JB.185.3.779-787.2003.
    • (2003) J Bacteriol , vol.185 , pp. 779-787
    • Wang, I.-N.1    Deaton, J.2    Young, R.3
  • 85
    • 37449031844 scopus 로고    scopus 로고
    • The pinholin of lambdoid phage 21: Control of lysis by membrane depolarization
    • Park T, Struck DK, Dankenbring CA, Young R. 2007. The pinholin of lambdoid phage 21: control of lysis by membrane depolarization. J Bacteriol 189:9135-9139. http://dx.doi.org/10.1128/JB.00847-07.
    • (2007) J Bacteriol , vol.189 , pp. 9135-9139
    • Park, T.1    Struck, D.K.2    Dankenbring, C.A.3    Young, R.4
  • 86
    • 84878448732 scopus 로고    scopus 로고
    • Visualization of pinholin lesions in vivo
    • Pang T, Fleming TC, Pogliano K, Young R. 2013. Visualization of pinholin lesions in vivo. Proc Natl Acad Sci U S A 110:E2054-E2063. http://dx.doi.org/10.1073/pnas.1222283110.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. E2054-E2063
    • Pang, T.1    Fleming, T.C.2    Pogliano, K.3    Young, R.4
  • 87
    • 84895198685 scopus 로고    scopus 로고
    • Phage lysis: Three steps, three choices, one outcome
    • Young R. 2014. Phage lysis: three steps, three choices, one outcome. J Microbiol 52:243-258. http://dx.doi.org/10.1007/s12275-014-4087-z.
    • (2014) J Microbiol , vol.52 , pp. 243-258
    • Young, R.1
  • 88
    • 84964694285 scopus 로고    scopus 로고
    • Unprecedented genomic diversity of RNA viruses in arthropods reveals the ancestry of negative-sense RNA viruses
    • Li C-X, Shi M, Tian J-H, Lin X-D, Kang Y-J, Chen L-J, Qin X-C, Xu J, Holmes EC, Zhang Y-Z. 2015. Unprecedented genomic diversity of RNA viruses in arthropods reveals the ancestry of negative-sense RNA viruses. eLife 4:e05378. http://dx.doi.org/10.7554/eLife.05378.
    • (2015) ELife , vol.4 , pp. e05378
    • Li, C.-X.1    Shi, M.2    Tian, J.-H.3    Lin, X.-D.4    Kang, Y.-J.5    Chen, L.-J.6    Qin, X.-C.7    Xu, J.8    Holmes, E.C.9    Zhang, Y.-Z.10
  • 90
    • 17844369974 scopus 로고    scopus 로고
    • Invasion of the continents: Cyanobacterial crusts to tree-inhabiting arthropods
    • Labandeira CC. 2005. Invasion of the continents: cyanobacterial crusts to tree-inhabiting arthropods. Trends Ecol Evol 20:253-262. http://dx .doi.org/10.1016/j.tree.2005.03.002.
    • (2005) Trends Ecol Evol , vol.20 , pp. 253-262
    • Labandeira, C.C.1
  • 91
    • 0002026854 scopus 로고
    • RNA viral supergroups and the evolution ofRNAviruses, p 105-119
    • Morse SS (ed), Raven Press, New York, NY
    • Goldbach R, de Haan P. 1994. RNA viral supergroups and the evolution ofRNAviruses, p 105-119. In Morse SS (ed), The evolutionary biology of viruses. Raven Press, New York, NY.
    • (1994) The Evolutionary Biology of Viruses
    • Goldbach, R.1    De Haan, P.2
  • 93
    • 0034715515 scopus 로고    scopus 로고
    • The GroEL protein of the whitefly Bemisia tabaci interacts with the coat protein of transmissible and nontransmissible begomoviruses in the yeast two-hybrid system
    • Morin S, Ghanim M, Sobol I, Czosnek H. 2000. The GroEL protein of the whitefly Bemisia tabaci interacts with the coat protein of transmissible and nontransmissible begomoviruses in the yeast two-hybrid system. Virology 276:404-416. http://dx.doi.org/10.1006/viro.2000.0549.
    • (2000) Virology , vol.276 , pp. 404-416
    • Morin, S.1    Ghanim, M.2    Sobol, I.3    Czosnek, H.4
  • 94
    • 79956295862 scopus 로고    scopus 로고
    • Interactions between a luteovirus and the GroEL chaperonin protein of the symbiotic bacterium Buchnera aphidicola of aphids
    • Bouvaine S, Boonham N, Douglas AE. 2011. Interactions between a luteovirus and the GroEL chaperonin protein of the symbiotic bacterium Buchnera aphidicola of aphids. J Gen Virol 92:1467-1474. http://dx.doi .org/10.1099/vir.0.029355-0.
    • (2011) J Gen Virol , vol.92 , pp. 1467-1474
    • Bouvaine, S.1    Boonham, N.2    Douglas, A.E.3
  • 95
    • 0033616529 scopus 로고    scopus 로고
    • A GroEL homologue from endosymbiotic bacteria of the whitefly Bemisia tabaci is implicated in the circulative transmission of tomato yellow leaf curl virus
    • Morin S, Ghanim M, Zeidan M, Czosnek H, Verbeek M, van den Heuvel JF. 1999. A GroEL homologue from endosymbiotic bacteria of the whitefly Bemisia tabaci is implicated in the circulative transmission of tomato yellow leaf curl virus. Virology 256:75-84. http://dx.doi.org/10 .1006/viro.1999.9631.
    • (1999) Virology , vol.256 , pp. 75-84
    • Morin, S.1    Ghanim, M.2    Zeidan, M.3    Czosnek, H.4    Verbeek, M.5    Van Den Heuvel, J.F.6
  • 96
    • 1842372081 scopus 로고    scopus 로고
    • The N-terminal region of the luteovirus readthrough domain determines virus binding to Buchnera GroEL and is essential for virus persistence in the aphid
    • van den Heuvel JF, Bruyère A, Hogenhout SA, Ziegler-Graff V, Brault V, Verbeek M, van der Wilk F, Richards K. 1997. The N-terminal region of the luteovirus readthrough domain determines virus binding to Buchnera GroEL and is essential for virus persistence in the aphid. J Virol 71:7258-7265.
    • (1997) J Virol , vol.71 , pp. 7258-7265
    • Van Den Heuvel, J.F.1    Bruyère, A.2    Hogenhout, S.A.3    Ziegler-Graff, V.4    Brault, V.5    Verbeek, M.6    Van Der Wilk, F.7    Richards, K.8
  • 97
    • 0033625053 scopus 로고    scopus 로고
    • The epithelial integrin v-6 is a receptor for foot-and-mouth disease virus
    • Jackson T, Sheppard D, Denyer M, Blakemore W, King AM. 2000. The epithelial integrin v-6 is a receptor for foot-and-mouth disease virus. J Virol 74:4949-4956. http://dx.doi.org/10.1128/JVI.74.11.4949-4956.2000.
    • (2000) J Virol , vol.74 , pp. 4949-4956
    • Jackson, T.1    Sheppard, D.2    Denyer, M.3    Blakemore, W.4    King, A.M.5
  • 98
    • 50949121523 scopus 로고    scopus 로고
    • Heparan sulfate-binding footand-mouth disease virus enters cells via caveola-mediated endocytosis
    • O'Donnell V, Larocco M, Baxt B. 2008. Heparan sulfate-binding footand-mouth disease virus enters cells via caveola-mediated endocytosis. J Virol 82:9075-9085. http://dx.doi.org/10.1128/JVI.00732-08.
    • (2008) J Virol , vol.82 , pp. 9075-9085
    • O'Donnell, V.1    Larocco, M.2    Baxt, B.3
  • 99
    • 0033924317 scopus 로고    scopus 로고
    • Accurate calculation of the density of proteins
    • Quillin ML, Matthews BW. 2000. Accurate calculation of the density of proteins. Acta Crystallogr D Biol Crystallogr 56:791-794. http://dx.doi .org/10.1107/S090744490000679X.
    • (2000) Acta Crystallogr D Biol Crystallogr , vol.56 , pp. 791-794
    • Quillin, M.L.1    Matthews, B.W.2
  • 100
    • 4644311920 scopus 로고    scopus 로고
    • Average protein density is a molecular-weight-dependent function
    • Fischer H, Polikarpov I, Craievich AF. 2004. Average protein density is a molecular-weight-dependent function. Protein Sci 13:2825-2828.
    • (2004) Protein Sci , vol.13 , pp. 2825-2828
    • Fischer, H.1    Polikarpov, I.2    Craievich, A.F.3
  • 101
    • 77952693635 scopus 로고    scopus 로고
    • Endocytosis of murine norovirus 1 into murine macrophages is dependent on dynamin II and cholesterol
    • Perry JW, Wobus CE. 2010. Endocytosis of murine norovirus 1 into murine macrophages is dependent on dynamin II and cholesterol. J Virol 84:6163-6176. http://dx.doi.org/10.1128/JVI.00331-10.
    • (2010) J Virol , vol.84 , pp. 6163-6176
    • Perry, J.W.1    Wobus, C.E.2
  • 103
    • 34548236927 scopus 로고    scopus 로고
    • Intracellular trafficking of adenovirus: Many means to many ends
    • Leopold PL, Crystal RG. 2007. Intracellular trafficking of adenovirus: many means to many ends. Adv Drug Deliv Rev 59:810-821. http://dx .doi.org/10.1016/j.addr.2007.06.007.
    • (2007) Adv Drug Deliv Rev , vol.59 , pp. 810-821
    • Leopold, P.L.1    Crystal, R.G.2
  • 105
    • 0033998692 scopus 로고    scopus 로고
    • Infectious entry pathway of adeno-associated virus and adeno-associated virus vectors
    • Bartlett JS, Wilcher R, Samulski RJ. 2000. Infectious entry pathway of adeno-associated virus and adeno-associated virus vectors. J Virol 74: 2777-2785. http://dx.doi.org/10.1128/JVI.74.6.2777-2785.2000.
    • (2000) J Virol , vol.74 , pp. 2777-2785
    • Bartlett, J.S.1    Wilcher, R.2    Samulski, R.J.3
  • 106
    • 71949096137 scopus 로고    scopus 로고
    • Viral entry mechanisms: Human papillomavirus and a long journey from extracellular matrix to the nucleus
    • Sapp M, Bienkowska-Haba M. 2009. Viral entry mechanisms: human papillomavirus and a long journey from extracellular matrix to the nucleus. FEBS J 276:7206-7216. http://dx.doi.org/10.1111/j.1742-4658 .2009.07400.x.
    • (2009) FEBS J , vol.276 , pp. 7206-7216
    • Sapp, M.1    Bienkowska-Haba, M.2
  • 107
    • 84858864021 scopus 로고    scopus 로고
    • Cell culture-adapted IBDV uses endocytosis for entry in DF-1 chicken embryonic fibroblasts
    • Yip CW, Hon CC, Zeng F, Leung FCC. 2012. Cell culture-adapted IBDV uses endocytosis for entry in DF-1 chicken embryonic fibroblasts. Virus Res 165:9-16. http://dx.doi.org/10.1016/j.virusres.2011.12.016.
    • (2012) Virus Res , vol.165 , pp. 9-16
    • Yip, C.W.1    Hon, C.C.2    Zeng, F.3    Leung, F.C.C.4
  • 108
    • 3843084996 scopus 로고    scopus 로고
    • Penetration of membrane-containing double-stranded-DNA bacteriophage PM2 into Pseudoalteromonas hosts
    • Kivelä HM, Daugelavicius R, Hankkio RH, Bamford JKH, Bamford DH. 2004. Penetration of membrane-containing double-stranded-DNA bacteriophage PM2 into Pseudoalteromonas hosts. J Bacteriol 186:5342-5354. http://dx.doi.org/10.1128/JB.186.16.5342-5354.2004.
    • (2004) J Bacteriol , vol.186 , pp. 5342-5354
    • Kivelä, H.M.1    Daugelavicius, R.2    Hankkio, R.H.3    Bamford, J.K.H.4    Bamford, D.H.5
  • 109
    • 67349273766 scopus 로고    scopus 로고
    • The picobirnavirus crystal structure provides functional insights into virion assembly and cell entry
    • Duquerroy S, Da Costa B, Henry C, Vigouroux A, Libersou S, Lepault J, Navaza J, Delmas B, Rey FA. 2009. The picobirnavirus crystal structure provides functional insights into virion assembly and cell entry. EMBO J 28:1655-1665. http://dx.doi.org/10.1038/emboj.2009.109.
    • (2009) EMBO J , vol.28 , pp. 1655-1665
    • Duquerroy, S.1    Da Costa, B.2    Henry, C.3    Vigouroux, A.4    Libersou, S.5    Lepault, J.6    Navaza, J.7    Delmas, B.8    Rey, F.A.9
  • 110
    • 72849138163 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans are required for cellular binding of the hepatitis e virus ORF2 capsid protein and for viral infection
    • Kalia M, Chandra V, Rahman SA, Sehgal D, Jameel S. 2009. Heparan sulfate proteoglycans are required for cellular binding of the hepatitis E virus ORF2 capsid protein and for viral infection. J Virol 83:12714-12724. http://dx.doi.org/10.1128/JVI.00717-09.
    • (2009) J Virol , vol.83 , pp. 12714-12724
    • Kalia, M.1    Chandra, V.2    Rahman, S.A.3    Sehgal, D.4    Jameel, S.5
  • 112
    • 39049088957 scopus 로고    scopus 로고
    • New (fluorescent) light on poliovirus entry
    • Bergelson JM. 2008. New (fluorescent) light on poliovirus entry. Trends Microbiol 16:44-47. http://dx.doi.org/10.1016/j.tim.2007.12.004.
    • (2008) Trends Microbiol , vol.16 , pp. 44-47
    • Bergelson, J.M.1
  • 113
    • 77952676295 scopus 로고    scopus 로고
    • Murine norovirus-1 cell entry is mediated through a non-clathrin-, non-caveolae-, dynamin-and cholesterol-dependent pathway
    • Gerondopoulos A, Jackson T, Monaghan P, Doyle N, Roberts LO. 2010. Murine norovirus-1 cell entry is mediated through a non-clathrin-, non-caveolae-, dynamin-and cholesterol-dependent pathway. J Gen Virol 91:1428-1438. http://dx.doi.org/10.1099/vir.0.016717-0.
    • (2010) J Gen Virol , vol.91 , pp. 1428-1438
    • Gerondopoulos, A.1    Jackson, T.2    Monaghan, P.3    Doyle, N.4    Roberts, L.O.5
  • 114
    • 84858189224 scopus 로고    scopus 로고
    • Contractile tail machines of bacteriophages
    • Leiman PG, Shneider MM. 2012. Contractile tail machines of bacteriophages. Adv Exp Med Biol 726:93-114. http://dx.doi.org/10.1007/978-1-4614-0980-9-5.
    • (2012) Adv Exp Med Biol , vol.726 , pp. 93-114
    • Leiman, P.G.1    Shneider, M.M.2
  • 116
    • 84861207605 scopus 로고    scopus 로고
    • Entry of human papillomavirus type 16 by actin-dependent, clathrin-and lipid raft-independent endocytosis
    • Schelhaas M, Shah B, Holzer M, Blattmann P, Kühling L, Day PM, Schiller JT, Helenius A. 2012. Entry of human papillomavirus type 16 by actin-dependent, clathrin-and lipid raft-independent endocytosis. PLoS Pathog 8:e1002657. http://dx.doi.org/10.1371/journal.ppat.1002657.
    • (2012) PLoS Pathog , vol.8 , pp. e1002657
    • Schelhaas, M.1    Shah, B.2    Holzer, M.3    Blattmann, P.4    Kühling, L.5    Day, P.M.6    Schiller, J.T.7    Helenius, A.8
  • 117
    • 21544444146 scopus 로고    scopus 로고
    • Binding and entry characteristics of porcine circovirus 2 in cells of the porcine monocytic line 3D4/31
    • Misinzo G, Meerts P, Bublot M, Mast J, Weingartl HM, Nauwynck HJ. 2005. Binding and entry characteristics of porcine circovirus 2 in cells of the porcine monocytic line 3D4/31. J Gen Virol 86:2057-2068. http://dx .doi.org/10.1099/vir.0.80652-0.
    • (2005) J Gen Virol , vol.86 , pp. 2057-2068
    • Misinzo, G.1    Meerts, P.2    Bublot, M.3    Mast, J.4    Weingartl, H.M.5    Nauwynck, H.J.6
  • 118
    • 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. 2009. The Polyomaviridae: contributions of virus structure to our understanding of virus receptors and infectious entry. Virology 384:389-399. http://dx.doi.org/10.1016/j.virol.2008.12 .021.
    • (2009) Virology , vol.384 , pp. 389-399
    • Neu, U.1    Stehle, T.2    Atwood, W.J.3
  • 119
    • 6344219974 scopus 로고    scopus 로고
    • Infection of Vero cells by BK virus is dependent on caveolae
    • Eash S, Querbes W, Atwood WJ. 2004. Infection of Vero cells by BK virus is dependent on caveolae. J Virol 78:11583-11590. http://dx.doi.org/10.1128/JVI.78.21.11583-11590.2004.
    • (2004) J Virol , vol.78 , pp. 11583-11590
    • Eash, S.1    Querbes, W.2    Atwood, W.J.3
  • 120
    • 0030754578 scopus 로고    scopus 로고
    • Entry of mouse hepatitis virus into cells by endosomal and nonendosomal pathways
    • Nash TC, Buchmeier MJ. 1997. Entry of mouse hepatitis virus into cells by endosomal and nonendosomal pathways. Virology 233:1-8. http://dx .doi.org/10.1006/viro.1997.8609.
    • (1997) Virology , vol.233 , pp. 1-8
    • Nash, T.C.1    Buchmeier, M.J.2
  • 123
    • 0036246727 scopus 로고    scopus 로고
    • The VP1 capsid protein of adenoassociated virus type 2 is carrying a phospholipase A2 domain required for virus infectivity
    • Girod A, Wobus CE, Zádori Z, Ried M, Leike K, Tijssen P, Kleinschmidt JA, Hallek M. 2002. The VP1 capsid protein of adenoassociated virus type 2 is carrying a phospholipase A2 domain required for virus infectivity. J Gen Virol 83:973-978.
    • (2002) J Gen Virol , vol.83 , pp. 973-978
    • Girod, A.1    Wobus, C.E.2    Zádori, Z.3    Ried, M.4    Leike, K.5    Tijssen, P.6    Kleinschmidt, J.A.7    Hallek, M.8
  • 124
    • 46449108849 scopus 로고    scopus 로고
    • Ameobal pathogen mimivirus infects macrophages through phagocytosis
    • Ghigo E, Kartenbeck J, Lien P, Pelkmans L, Capo C, Mege J-L, Raoult D. 2008. Ameobal pathogen mimivirus infects macrophages through phagocytosis. PLoS Pathog 4:e1000087. http://dx.doi.org/10 .1371/journal.ppat.1000087.
    • (2008) PLoS Pathog , vol.4 , pp. e1000087
    • Ghigo, E.1    Kartenbeck, J.2    Lien, P.3    Pelkmans, L.4    Capo, C.5    Mege, J.-L.6    Raoult, D.7
  • 125
    • 0347382528 scopus 로고    scopus 로고
    • Posterior midgut and hindgut are both sites of acquisition of Cucurbit aphid-borne yellows virus in Myzus persicae and Aphis gossypii
    • Reinbold C, Herrbach E, Brault V. 2003. Posterior midgut and hindgut are both sites of acquisition of Cucurbit aphid-borne yellows virus in Myzus persicae and Aphis gossypii. J Gen Virol 84:3473-3484. http://dx.doi .org/10.1099/vir.0.19415-0.
    • (2003) J Gen Virol , vol.84 , pp. 3473-3484
    • Reinbold, C.1    Herrbach, E.2    Brault, V.3
  • 126
    • 72849144468 scopus 로고    scopus 로고
    • Hepatitis B virus requires intact caveolin-1 function for productive infection in HepaRG cells
    • Macovei A, Radulescu C, Lazar C, Petrescu S, Durantel D, Dwek RA, Zitzmann N, Nichita NB. 2010. Hepatitis B virus requires intact caveolin-1 function for productive infection in HepaRG cells. J Virol 84:243-253. http://dx.doi.org/10.1128/JVI.01207-09.
    • (2010) J Virol , vol.84 , pp. 243-253
    • Macovei, A.1    Radulescu, C.2    Lazar, C.3    Petrescu, S.4    Durantel, D.5    Dwek, R.A.6    Zitzmann, N.7    Nichita, N.B.8
  • 127
    • 0347482478 scopus 로고    scopus 로고
    • Influenza virus hemagglutinin concentrates in lipid raft microdomains for efficient viral fusion
    • Takeda M, Leser GP, Russell CJ, Lamb RA. 2003. Influenza virus hemagglutinin concentrates in lipid raft microdomains for efficient viral fusion. Proc Natl Acad Sci U S A 100:14610-14617. http://dx.doi.org/10 .1073/pnas.2235620100.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 14610-14617
    • Takeda, M.1    Leser, G.P.2    Russell, C.J.3    Lamb, R.A.4
  • 128
    • 0017077863 scopus 로고
    • Events in lambda injection between phage adsorption and DNA entry
    • Mackay DJ, Bode VC. 1976. Events in lambda injection between phage adsorption and DNA entry. Virology 72:154-166. http://dx.doi.org/10 .1016/0042-6822(76)90320-2.
    • (1976) Virology , vol.72 , pp. 154-166
    • Mackay, D.J.1    Bode, V.C.2
  • 129
    • 84876408129 scopus 로고    scopus 로고
    • Receptor-mediated endocytosis and trafficking between endosomal-lysosomal vacuoles in Giardia lamblia
    • Rivero MR, Jausoro I, Bisbal M, Feliziani C, Lanfredi-Rangel A, Touz MC. 2013. Receptor-mediated endocytosis and trafficking between endosomal-lysosomal vacuoles in Giardia lamblia. Parasitol Res 112:1813-1818. http://dx.doi.org/10.1007/s00436-012-3253-7.
    • (2013) Parasitol Res , vol.112 , pp. 1813-1818
    • Rivero, M.R.1    Jausoro, I.2    Bisbal, M.3    Feliziani, C.4    Lanfredi-Rangel, A.5    Touz, M.C.6
  • 131
    • 59349098016 scopus 로고    scopus 로고
    • Structure, attachment and entry of polyomaand papillomaviruses
    • Sapp M, Day PM. 2009. Structure, attachment and entry of polyomaand papillomaviruses. Virology 384:400-409. http://dx.doi.org/10.1016/j.virol.2008.12.022.
    • (2009) Virology , vol.384 , pp. 400-409
    • Sapp, M.1    Day, P.M.2
  • 132
    • 23244461734 scopus 로고    scopus 로고
    • Caveola-dependent endocytic entry of amphotropic murine leukemia virus
    • Beer C, Andersen DS, Rojek A, Pedersen L. 2005. Caveola-dependent endocytic entry of amphotropic murine leukemia virus. J Virol 79: 10776-10787. http://dx.doi.org/10.1128/JVI.79.16.10776-10787.2005.
    • (2005) J Virol , vol.79 , pp. 10776-10787
    • Beer, C.1    Andersen, D.S.2    Rojek, A.3    Pedersen, L.4
  • 133
    • 0019477841 scopus 로고
    • Penetration and uncoating of frog virus 3 (FV3) in cultured rat Kupffer cells
    • Gendrault JL, Steffan AM, Bingen A, Kirn A. 1981. Penetration and uncoating of frog virus 3 (FV3) in cultured rat Kupffer cells. Virology 112:375-384. http://dx.doi.org/10.1016/0042-6822(81)90284-1.
    • (1981) Virology , vol.112 , pp. 375-384
    • Gendrault, J.L.1    Steffan, A.M.2    Bingen, A.3    Kirn, A.4
  • 135
    • 78149355646 scopus 로고    scopus 로고
    • Ebolavirus is internalized into host cells via macropinocytosis in a viral glycoprotein-dependent manner
    • Nanbo A, Imai M, Watanabe S, Noda T, Takahashi K, Neumann G, Halfmann P, Kawaoka Y. 2010. Ebolavirus is internalized into host cells via macropinocytosis in a viral glycoprotein-dependent manner. PLoS Pathog 6:e1001121. http://dx.doi.org/10.1371/journal.ppat.1001121.
    • (2010) PLoS Pathog , vol.6 , pp. e1001121
    • Nanbo, A.1    Imai, M.2    Watanabe, S.3    Noda, T.4    Takahashi, K.5    Neumann, G.6    Halfmann, P.7    Kawaoka, Y.8
  • 136
    • 78149301316 scopus 로고    scopus 로고
    • Cellular entry of Ebola virus involves uptake by a macropinocytosis-like mechanism and subsequent trafficking through early and late endosomes
    • Saeed MF, Kolokoltsov AA, Albrecht T, Davey RA. 2010. Cellular entry of Ebola virus involves uptake by a macropinocytosis-like mechanism and subsequent trafficking through early and late endosomes. PLoS Pathog 6:e1001110. http://dx.doi.org/10.1371/journal.ppat.1001110.
    • (2010) PLoS Pathog , vol.6 , pp. e1001110
    • Saeed, M.F.1    Kolokoltsov, A.A.2    Albrecht, T.3    Davey, R.A.4
  • 137
    • 78650045778 scopus 로고    scopus 로고
    • The Tyro3 receptor kinase Axl enhances macropinocytosis of Zaire ebolavirus
    • Hunt CL, Kolokoltsov AA, Davey RA, Maury W. 2011. The Tyro3 receptor kinase Axl enhances macropinocytosis of Zaire ebolavirus. J Virol 85:334-347. http://dx.doi.org/10.1128/JVI.01278-09.
    • (2011) J Virol , vol.85 , pp. 334-347
    • Hunt, C.L.1    Kolokoltsov, A.A.2    Davey, R.A.3    Maury, W.4
  • 138
    • 77952093909 scopus 로고    scopus 로고
    • Entry of bovine viral diarrhea virus into ovine cells occurs through clathrin-dependent endocytosis and low pH-dependent fusion
    • Mathapati BS, Mishra N, Rajukumar K, Nema RK, Behera SP, Dubey SC. 2010. Entry of bovine viral diarrhea virus into ovine cells occurs through clathrin-dependent endocytosis and low pH-dependent fusion. In Vitro Cell Dev Biol Anim 46:403-407. http://dx.doi.org/10.1007/s11626-009-9263-9.
    • (2010) Vitro Cell Dev Biol Anim , vol.46 , pp. 403-407
    • Mathapati, B.S.1    Mishra, N.2    Rajukumar, K.3    Nema, R.K.4    Behera, S.P.5    Dubey, S.C.6
  • 139
    • 0029812792 scopus 로고    scopus 로고
    • Low-pH-induced fusion of Vero cells infected with Junin virus
    • Castilla V, Mersich SE. 1996. Low-pH-induced fusion of Vero cells infected with Junin virus. Arch Virol 141:1307-1317. http://dx.doi.org/10.1007/BF01718832.
    • (1996) Arch Virol , vol.141 , pp. 1307-1317
    • Castilla, V.1    Mersich, S.E.2
  • 140
    • 65349165676 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus utilizes an actin polymerization-dependent macropinocytic pathway to enter human dermal microvascular endothelial and human umbilical vein endothelial cells
    • Raghu H, Sharma-Walia N, Veettil MV, Sadagopan S, Chandran B. 2009. Kaposi's sarcoma-associated herpesvirus utilizes an actin polymerization-dependent macropinocytic pathway to enter human dermal microvascular endothelial and human umbilical vein endothelial cells. J Virol 83:4895-4911. http://dx.doi.org/10.1128/JVI.02498-08.
    • (2009) J Virol , vol.83 , pp. 4895-4911
    • Raghu, H.1    Sharma-Walia, N.2    Veettil, M.V.3    Sadagopan, S.4    Chandran, B.5
  • 141
    • 84861092514 scopus 로고    scopus 로고
    • Hepatitis e virus enters liver cells through receptor-dependent clathrin-mediated endocytosis
    • Kapur N, Thakral D, Durgapal H, Panda SK. 2012. Hepatitis E virus enters liver cells through receptor-dependent clathrin-mediated endocytosis. J Viral Hepat 19:436-448. http://dx.doi.org/10.1111/j.1365-2893 .2011.01559.x.
    • (2012) J Viral Hepat , vol.19 , pp. 436-448
    • Kapur, N.1    Thakral, D.2    Durgapal, H.3    Panda, S.K.4
  • 142
    • 77956625541 scopus 로고    scopus 로고
    • Uncoating of human rhinoviruses
    • Fuchs R, Blaas D. 2010. Uncoating of human rhinoviruses. Rev Med Virol 20:281-297. http://dx.doi.org/10.1002/rmv.654.
    • (2010) Rev Med Virol , vol.20 , pp. 281-297
    • Fuchs, R.1    Blaas, D.2
  • 143
    • 0019382221 scopus 로고
    • In vivo pathway of Autographa californica baculovirus invasion and infection
    • Granados RR, Lawler KA. 1981. In vivo pathway of Autographa californica baculovirus invasion and infection. Virology 108:297-308. http://dx .doi.org/10.1016/0042-6822(81)90438-4.
    • (1981) Virology , vol.108 , pp. 297-308
    • Granados, R.R.1    Lawler, K.A.2
  • 144
    • 69249212526 scopus 로고    scopus 로고
    • Low endocytic pH and capsid protein autocleavage are critical components of Flock House virus cell entry
    • Odegard AL, Kwan MH, Walukiewicz HE, Banerjee M, Schneemann A, Johnson JE. 2009. Low endocytic pH and capsid protein autocleavage are critical components of Flock House virus cell entry. J Virol 83:8628-8637. http://dx.doi.org/10.1128/JVI.00873-09.
    • (2009) J Virol , vol.83 , pp. 8628-8637
    • Odegard, A.L.1    Kwan, M.H.2    Walukiewicz, H.E.3    Banerjee, M.4    Schneemann, A.5    Johnson, J.E.6
  • 145
    • 0033968050 scopus 로고    scopus 로고
    • JC virus enters human glial cells by clathrin-dependent receptor-mediated endocytosis
    • Pho MT, Ashok A, Atwood WJ. 2000. JC virus enters human glial cells by clathrin-dependent receptor-mediated endocytosis. J Virol 74:2288-2292. http://dx.doi.org/10.1128/JVI.74.5.2288-2292.2000.
    • (2000) J Virol , vol.74 , pp. 2288-2292
    • Pho, M.T.1    Ashok, A.2    Atwood, W.J.3
  • 146
    • 84871868782 scopus 로고    scopus 로고
    • Mechanisms of coronavirus cell entry mediated by the viral spike protein
    • Belouzard S, Millet JK, Licitra BN, Whittaker GR. 2012. Mechanisms of coronavirus cell entry mediated by the viral spike protein. Viruses 4:1011-1033. http://dx.doi.org/10.3390/v4061011.
    • (2012) Viruses , vol.4 , pp. 1011-1033
    • Belouzard, S.1    Millet, J.K.2    Licitra, B.N.3    Whittaker, G.R.4
  • 147
    • 70450223511 scopus 로고    scopus 로고
    • Nipah virus entry can occur by macropinocytosis
    • Pernet O, Pohl C, Ainouze M, Kweder H, Buckland R. 2009. Nipah virus entry can occur by macropinocytosis. Virology 395:298-311. http://dx.doi.org/10.1016/j.virol.2009.09.016.
    • (2009) Virology , vol.395 , pp. 298-311
    • Pernet, O.1    Pohl, C.2    Ainouze, M.3    Kweder, H.4    Buckland, R.5
  • 148
    • 84876871358 scopus 로고    scopus 로고
    • Host cell entry of respiratory syncytial virus involves macropinocytosis followed by proteolytic activation of the F protein
    • Krzyzaniak MA, Zumstein MT, Gerez JA, Picotti P, Helenius A. 2013. Host cell entry of respiratory syncytial virus involves macropinocytosis followed by proteolytic activation of the F protein. PLoS Pathog 9:e1003309. http://dx.doi.org/10.1371/journal.ppat.1003309.
    • (2013) PLoS Pathog , vol.9 , pp. e1003309
    • Krzyzaniak, M.A.1    Zumstein, M.T.2    Gerez, J.A.3    Picotti, P.4    Helenius, A.5
  • 150
    • 34247609683 scopus 로고    scopus 로고
    • Bluetongue virus entry into cells
    • Forzan M, Marsh M, Roy P. 2007. Bluetongue virus entry into cells. J Virol 81:4819-4827. http://dx.doi.org/10.1128/JVI.02284-06.
    • (2007) J Virol , vol.81 , pp. 4819-4827
    • Forzan, M.1    Marsh, M.2    Roy, P.3
  • 151
    • 0021962370 scopus 로고
    • Ultrastructural and biochemical study of frog virus 3 uptake by BHK-21 cells
    • Braunwald J, Nonnenmacher H, Tripier-Darcy F. 1985. Ultrastructural and biochemical study of frog virus 3 uptake by BHK-21 cells. J Gen Virol 66:283-293. http://dx.doi.org/10.1099/0022-1317-66-2-283.
    • (1985) J Gen Virol , vol.66 , pp. 283-293
    • Braunwald, J.1    Nonnenmacher, H.2    Tripier-Darcy, F.3
  • 154
    • 84883295201 scopus 로고    scopus 로고
    • Physiological change under OsHV-1 contamination in pacific oyster Crassostrea gigas through massive mortality events on fields
    • Jouaux A, Lafont M, Blin J-L, Houssin M, Mathieu M, Lelong C. 2013. Physiological change under OsHV-1 contamination in pacific oyster Crassostrea gigas through massive mortality events on fields. BMC Genomics 14:590. http://dx.doi.org/10.1186/1471-2164-14-590.
    • (2013) BMC Genomics , vol.14 , pp. 590
    • Jouaux, A.1    Lafont, M.2    Blin, J.-L.3    Houssin, M.4    Mathieu, M.5    Lelong, C.6
  • 155
    • 68049085465 scopus 로고    scopus 로고
    • Involvement of cellular proteins in Junin arenavirus entry
    • Martinez MG, Forlenza MB, Candurra NA. 2009. Involvement of cellular proteins in Junin arenavirus entry. Biotechnol J 4:866-870. http://dx.doi.org/10.1002/biot.200800357.
    • (2009) Biotechnol J , vol.4 , pp. 866-870
    • Martinez, M.G.1    Forlenza, M.B.2    Candurra, N.A.3
  • 156
    • 71949123985 scopus 로고    scopus 로고
    • Viral entry mechanisms: The increasing diversity of paramyxovirus entry
    • Smith EC, Popa A, Chang A, Masante C, Dutch RE. 2009. Viral entry mechanisms: The increasing diversity of paramyxovirus entry. FEBS J 276:7217-7227. http://dx.doi.org/10.1111/j.1742-4658.2009.07401.x.
    • (2009) FEBS J , vol.276 , pp. 7217-7227
    • Smith, E.C.1    Popa, A.2    Chang, A.3    Masante, C.4    Dutch, R.E.5
  • 157
    • 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, Tünnemann 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    Tünnemann, G.5    Cardoso, M.C.6    Veit, M.7    Herrmann, A.8
  • 158
    • 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
  • 160
    • 0024248199 scopus 로고
    • Mycoplasma viruses
    • Maniloff J. 1988. Mycoplasma viruses. Crit Rev Microbiol 15:339-389. http://dx.doi.org/10.3109/10408418809104462.
    • (1988) Crit Rev Microbiol , vol.15 , pp. 339-389
    • Maniloff, J.1
  • 161
    • 75449110786 scopus 로고    scopus 로고
    • Dynamin-and clathrin-dependent endocytosis in African swine fever virus entry
    • Hernaez B, Alonso C. 2010. Dynamin-and clathrin-dependent endocytosis in African swine fever virus entry. J Virol 84:2100-2109. http://dx .doi.org/10.1128/JVI.01557-09.
    • (2010) J Virol , vol.84 , pp. 2100-2109
    • Hernaez, B.1    Alonso, C.2
  • 162
    • 0018378509 scopus 로고
    • Penetration into caterpillar cells of viruslike particles injected during oviposition by parasitoid ichneumonid wasps
    • Stoltz DB, Vinson SB. 1979. Penetration into caterpillar cells of viruslike particles injected during oviposition by parasitoid ichneumonid wasps. Can J Microbiol 25:207-216. http://dx.doi.org/10.1139/m79-032.
    • (1979) Can J Microbiol , vol.25 , pp. 207-216
    • Stoltz, D.B.1    Vinson, S.B.2
  • 163
    • 0017186242 scopus 로고
    • Baculovirus-like particles in the reproductive tracts of female parasitoid wasps
    • Stoltz DB, Vinson SB, MacKinnon EA. 1976. Baculovirus-like particles in the reproductive tracts of female parasitoid wasps. Can J Microbiol 22:1013-1023. http://dx.doi.org/10.1139/m76-148.
    • (1976) Can J Microbiol , vol.22 , pp. 1013-1023
    • Stoltz, D.B.1    Vinson, S.B.2    MacKinnon, E.A.3
  • 164
    • 36248981477 scopus 로고    scopus 로고
    • Exposure of ichnovirus particles to digitonin leads to enhanced infectivity and induces fusion from without in an in vitro model system
    • Stoltz D, Lapointe R, Makkay A, Cusson M. 2007. Exposure of ichnovirus particles to digitonin leads to enhanced infectivity and induces fusion from without in an in vitro model system. J Gen Virol 88:2977-2984. http://dx.doi.org/10.1099/vir.0.83118-0.
    • (2007) J Gen Virol , vol.88 , pp. 2977-2984
    • Stoltz, D.1    Lapointe, R.2    Makkay, A.3    Cusson, M.4
  • 165
    • 33748674858 scopus 로고    scopus 로고
    • Functional entry of baculovirus into insect and mammalian cells is dependent on clathrinmediated endocytosis
    • Long G, Pan X, Kormelink R, Vlak JM. 2006. Functional entry of baculovirus into insect and mammalian cells is dependent on clathrinmediated endocytosis. J Virol 80:8830-8833. http://dx.doi.org/10.1128/JVI.00880-06.
    • (2006) J Virol , vol.80 , pp. 8830-8833
    • Long, G.1    Pan, X.2    Kormelink, R.3    Vlak, J.M.4
  • 166
    • 0021985857 scopus 로고
    • Mechanism of neutralization of budded Autographa californica nuclear polyhedrosis virus by a monoclonal antibody: Inhibition of entry by adsorptive endocytosis
    • Volkman LE, Goldsmith PA. 1985. Mechanism of neutralization of budded Autographa californica nuclear polyhedrosis virus by a monoclonal antibody: inhibition of entry by adsorptive endocytosis. Virology 143:185-195. http://dx.doi.org/10.1016/0042-6822(85)90107-2.
    • (1985) Virology , vol.143 , pp. 185-195
    • Volkman, L.E.1    Goldsmith, P.A.2
  • 167
    • 0032546844 scopus 로고    scopus 로고
    • The HIV-1 envelope glycoproteins: Fusogens, antigens, and immunogens
    • Wyatt R, Sodroski J. 1998. The HIV-1 envelope glycoproteins: fusogens, antigens, and immunogens. Science 280:1884-1888. http://dx.doi.org/10.1126/science.280.5371.1884.
    • (1998) Science , vol.280 , pp. 1884-1888
    • Wyatt, R.1    Sodroski, J.2
  • 168
    • 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
  • 169
    • 59849116492 scopus 로고    scopus 로고
    • Crimean-Congo hemorrhagic fever virus entry and replication is clathrin-, pH-and cholesterol-dependent
    • Simon M, Johansson C, Mirazimi A. 2009. Crimean-Congo hemorrhagic fever virus entry and replication is clathrin-, pH-and cholesterol-dependent. J Gen Virol 90:210-215. http://dx.doi.org/10.1099/vir.0.006387-0.
    • (2009) J Gen Virol , vol.90 , pp. 210-215
    • Simon, M.1    Johansson, C.2    Mirazimi, A.3
  • 170
    • 77950934528 scopus 로고    scopus 로고
    • Ebola virus uses clathrin-mediated endocytosis as an entry pathway
    • Bhattacharyya S, Warfield KL, Ruthel G, Bavari S, Aman MJ, Hope TJ. 2010. Ebola virus uses clathrin-mediated endocytosis as an entry pathway. Virology 401:18-28. http://dx.doi.org/10.1016/j.virol.2010.02.015.
    • (2010) Virology , vol.401 , pp. 18-28
    • Bhattacharyya, S.1    Warfield, K.L.2    Ruthel, G.3    Bavari, S.4    Aman, M.J.5    Hope, T.J.6
  • 171
    • 63449089372 scopus 로고    scopus 로고
    • Characterization of dengue virus entry into HepG2 cells
    • Suksanpaisan L, Susantad T, Smith DR. 2009. Characterization of dengue virus entry into HepG2 cells. J Biomed Sci 16:17. http://dx.doi .org/10.1186/1423-0127-16-17.
    • (2009) J Biomed Sci , vol.16 , pp. 17
    • Suksanpaisan, L.1    Susantad, T.2    Smith, D.R.3
  • 172
    • 4544266363 scopus 로고    scopus 로고
    • Infectious entry of West Nile virus occurs through a clathrin-mediated endocytic pathway
    • Chu JJH, Ng ML. 2004. Infectious entry of West Nile virus occurs through a clathrin-mediated endocytic pathway. J Virol 78:10543-10555. http://dx.doi.org/10.1128/JVI.78.19.10543-10555.2004.
    • (2004) J Virol , vol.78 , pp. 10543-10555
    • Chu, J.J.H.1    Ng, M.L.2
  • 173
    • 50149096579 scopus 로고    scopus 로고
    • Epsin 1 is a cargo-specific adaptor for the clathrin-mediated endocytosis of the influenza virus
    • Chen C, Zhuang X. 2008. Epsin 1 is a cargo-specific adaptor for the clathrin-mediated endocytosis of the influenza virus. Proc Natl Acad Sci U S A 105:11790-11795. http://dx.doi.org/10.1073/pnas.0803711105.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 11790-11795
    • Chen, C.1    Zhuang, X.2
  • 174
    • 23844555503 scopus 로고    scopus 로고
    • The Nipah virus fusion protein is cleaved within the endosomal compartment
    • Diederich S, Moll M, Klenk H-D, Maisner A. 2005. The Nipah virus fusion protein is cleaved within the endosomal compartment. J Biol Chem 280:29899-29903. http://dx.doi.org/10.1074/jbc.M504598200.
    • (2005) J Biol Chem , vol.280 , pp. 29899-29903
    • Diederich, S.1    Moll, M.2    Klenk, H.-D.3    Maisner, A.4
  • 175
    • 19444368439 scopus 로고    scopus 로고
    • Cellular uptake of avian leukosis virus subgroup B is mediated by clathrin
    • Diaz-Griffero F, Jackson AP, Brojatsch J. 2005. Cellular uptake of avian leukosis virus subgroup B is mediated by clathrin. Virology 337:45-54. http://dx.doi.org/10.1016/j.virol.2005.02.027.
    • (2005) Virology , vol.337 , pp. 45-54
    • Diaz-Griffero, F.1    Jackson, A.P.2    Brojatsch, J.3
  • 176
    • 65249139458 scopus 로고    scopus 로고
    • HIV enters cells via endocytosis and dynamin-dependent fusion with endosomes
    • Miyauchi K, Kim Y, Latinovic O, Morozov V, Melikyan GB. 2009. HIV enters cells via endocytosis and dynamin-dependent fusion with endosomes. Cell 137:433-444. http://dx.doi.org/10.1016/j.cell.2009.02.046.
    • (2009) Cell , vol.137 , pp. 433-444
    • Miyauchi, K.1    Kim, Y.2    Latinovic, O.3    Morozov, V.4    Melikyan, G.B.5
  • 177
    • 78149305588 scopus 로고    scopus 로고
    • The length of vesicular stomatitis virus particles dictates a need for actin assembly during clathrin-dependent endocytosis
    • Cureton DK, Massol RH, Whelan SPJ, Kirchhausen T. 2010. The length of vesicular stomatitis virus particles dictates a need for actin assembly during clathrin-dependent endocytosis. PLoS Pathog 6:e1001127. http://dx.doi.org/10.1371/journal.ppat.1001127.
    • (2010) PLoS Pathog , vol.6 , pp. e1001127
    • Cureton, D.K.1    Massol, R.H.2    Whelan, S.P.J.3    Kirchhausen, T.4
  • 178
    • 0032541402 scopus 로고    scopus 로고
    • The clathrin endocytic pathway in viral infection
    • DeTulleo L, Kirchhausen T. 1998. The clathrin endocytic pathway in viral infection. EMBO J 17:4585-4593. http://dx.doi.org/10.1093/emboj/17.16.4585.
    • (1998) EMBO J , vol.17 , pp. 4585-4593
    • DeTulleo, L.1    Kirchhausen, T.2
  • 179
    • 10044236498 scopus 로고    scopus 로고
    • Effects of endocytosis inhibitory drugs on rubella virus entry into VeroE6 cells
    • Kee S-H, Cho E-J, Song J-W, Park KS, Baek LJ, Song K-J. 2004. Effects of endocytosis inhibitory drugs on rubella virus entry into VeroE6 cells. Microbiol Immunol 48:823-829. http://dx.doi.org/10.1111/j.1348-0421 .2004.tb03614.x.
    • (2004) Microbiol Immunol , vol.48 , pp. 823-829
    • Kee, S.-H.1    Cho, E.-J.2    Song, J.-W.3    Park, K.S.4    Baek, L.J.5    Song, K.-J.6
  • 180
    • 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. 2005. Rab7 associates with early endosomes to mediate sorting and transport of Semliki forest virus to late endosomes. PLoS Biol 3:e233. http://dx.doi.org/10.1371/journal.pbio.0030233.
    • (2005) PLoS Biol , vol.3 , pp. e233
    • Vonderheit, A.1    Helenius, A.2
  • 181
    • 0033919799 scopus 로고    scopus 로고
    • Infection of polarized cultures of human intestinal epithelial cells with hepatitis A virus: Vectorial release of progeny virions through apical cellular membranes
    • Blank CA, Anderson DA, Beard M, Lemon SM. 2000. Infection of polarized cultures of human intestinal epithelial cells with hepatitis A virus: vectorial release of progeny virions through apical cellular membranes. J Virol 74:6476-6484. http://dx.doi.org/10.1128/JVI.74.14.6476-6484.2000.
    • (2000) J Virol , vol.74 , pp. 6476-6484
    • Blank, C.A.1    Anderson, D.A.2    Beard, M.3    Lemon, S.M.4
  • 182
    • 77956033632 scopus 로고    scopus 로고
    • Release of genotype 1 hepatitis e virus from cultured hepatoma and polarized intestinal cells depends on open reading frame 3 protein and requires an intact PXXP motif
    • Emerson SU, Nguyen HT, Torian U, Burke D, Engle R, Purcell RH. 2010. Release of genotype 1 hepatitis E virus from cultured hepatoma and polarized intestinal cells depends on open reading frame 3 protein and requires an intact PXXP motif. J Virol 84:9059-9069. http://dx.doi.org/10.1128/JVI.00593-10.
    • (2010) J Virol , vol.84 , pp. 9059-9069
    • Emerson, S.U.1    Nguyen, H.T.2    Torian, U.3    Burke, D.4    Engle, R.5    Purcell, R.H.6
  • 183
    • 23044490802 scopus 로고    scopus 로고
    • Replication of TT virus in hepatocyte and leucocyte cell lines
    • Desai M, Pal R, Deshmukh R, Banker D. 2005. Replication of TT virus in hepatocyte and leucocyte cell lines. J Med Virol 77:136-143. http://dx .doi.org/10.1002/jmv.20426.
    • (2005) J Med Virol , vol.77 , pp. 136-143
    • Desai, M.1    Pal, R.2    Deshmukh, R.3    Banker, D.4
  • 184
    • 77958531364 scopus 로고    scopus 로고
    • Human anelloviruses and the central nervous system
    • Maggi F, Bendinelli M. 2010. Human anelloviruses and the central nervous system. Rev Med Virol 20:392-407. http://dx.doi.org/10.1002/rmv.668.
    • (2010) Rev Med Virol , vol.20 , pp. 392-407
    • Maggi, F.1    Bendinelli, M.2
  • 185
    • 0242331609 scopus 로고    scopus 로고
    • The small RING finger protein Z drives arenavirus budding: Implications for antiviral strategies
    • Perez M, Craven RC, de la Torre JC. 2003. The small RING finger protein Z drives arenavirus budding: implications for antiviral strategies. Proc Natl Acad Sci U S A 100:12978-12983. http://dx.doi.org/10.1073/pnas.2133782100.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 12978-12983
    • Perez, M.1    Craven, R.C.2    De La Torre, J.C.3
  • 186
    • 33645991207 scopus 로고    scopus 로고
    • Nonstructural protein 3 of bluetongue virus assists virus release by recruiting ESCRT-I protein Tsg101
    • Wirblich C, Bhattacharya B, Roy P. 2006. Nonstructural protein 3 of bluetongue virus assists virus release by recruiting ESCRT-I protein Tsg101. J Virol 80:460-473. http://dx.doi.org/10.1128/JVI.80.1.460-473 .2006.
    • (2006) J Virol , vol.80 , pp. 460-473
    • Wirblich, C.1    Bhattacharya, B.2    Roy, P.3
  • 187
    • 3543145929 scopus 로고    scopus 로고
    • Caspases mediate processing of the capsid precursor and cell release of human astroviruses
    • Méndez E, Salas-Ocampo E, Arias CF. 2004. Caspases mediate processing of the capsid precursor and cell release of human astroviruses. J Virol 78:8601-8608. http://dx.doi.org/10.1128/JVI.78.16.8601-8608.2004.
    • (2004) J Virol , vol.78 , pp. 8601-8608
    • Méndez, E.1    Salas-Ocampo, E.2    Arias, C.F.3
  • 188
    • 0027352762 scopus 로고
    • The intestine is a site of passage for potato leafroll virus from the gut lumen into the haemocoel in the aphid vector, Myzus persicae Sulz
    • Garret A, Kerlan C, Thomas D. 1993. The intestine is a site of passage for potato leafroll virus from the gut lumen into the haemocoel in the aphid vector, Myzus persicae Sulz. Arch Virol 131:377-392. http://dx.doi.org/10.1007/BF01378639.
    • (1993) Arch Virol , vol.131 , pp. 377-392
    • Garret, A.1    Kerlan, C.2    Thomas, D.3
  • 189
    • 77954471091 scopus 로고    scopus 로고
    • Tsg101 is recruited by a late domain of the nucleocapsid protein to support budding of Marburg virus-like particles
    • Dolnik O, Kolesnikova L, Stevermann L, Becker S. 2010. Tsg101 is recruited by a late domain of the nucleocapsid protein to support budding of Marburg virus-like particles. J Virol 84:7847-7856. http://dx.doi .org/10.1128/JVI.00476-10.
    • (2010) J Virol , vol.84 , pp. 7847-7856
    • Dolnik, O.1    Kolesnikova, L.2    Stevermann, L.3    Becker, S.4
  • 191
    • 76149130046 scopus 로고    scopus 로고
    • The VP5 protein of infectious bursal disease virus promotes virion release from infected cells and is not involved in cell death
    • Wu Y, Hong L, Ye J, Huang Z, Zhou J. 2009. The VP5 protein of infectious bursal disease virus promotes virion release from infected cells and is not involved in cell death. Arch Virol 154:1873-1882. http://dx.doi .org/10.1007/s00705-009-0524-4.
    • (2009) Arch Virol , vol.154 , pp. 1873-1882
    • Wu, Y.1    Hong, L.2    Ye, J.3    Huang, Z.4    Zhou, J.5
  • 192
    • 34547108622 scopus 로고    scopus 로고
    • Infectious bursal disease virus, a nonenveloped virus, possesses a capsid-associated peptide that deforms and perforates biological membranes
    • Galloux M, Libersou S, Morellet N, Bouaziz S, Da Costa B, Ouldali M, Lepault J, Delmas B. 2007. Infectious bursal disease virus, a nonenveloped virus, possesses a capsid-associated peptide that deforms and perforates biological membranes. J Biol Chem 282:20774-20784. http://dx.doi.org/10.1074/jbc.M701048200.
    • (2007) J Biol Chem , vol.282 , pp. 20774-20784
    • Galloux, M.1    Libersou, S.2    Morellet, N.3    Bouaziz, S.4    Da Costa, B.5    Ouldali, M.6    Lepault, J.7    Delmas, B.8
  • 194
    • 79251580950 scopus 로고    scopus 로고
    • The ESCRT system is required for hepatitis C virus production
    • Ariumi Y, Kuroki M, Maki M, Ikeda M, Dansako H, Wakita T, Kato N. 2011. The ESCRT system is required for hepatitis C virus production. PLoS One 6:e14517. http://dx.doi.org/10.1371/journal.pone.0014517.
    • (2011) PLoS One , vol.6 , pp. e14517
    • Ariumi, Y.1    Kuroki, M.2    Maki, M.3    Ikeda, M.4    Dansako, H.5    Wakita, T.6    Kato, N.7
  • 195
    • 29144474440 scopus 로고    scopus 로고
    • Conserved molecular systems of the Baculoviridae
    • Okano K, Vanarsdall AL, Mikhailov VS, Rohrmann GF. 2006. Conserved molecular systems of the Baculoviridae. Virology 344:77-87. http://dx.doi.org/10.1016/j.virol.2005.09.019.
    • (2006) Virology , vol.344 , pp. 77-87
    • Okano, K.1    Vanarsdall, A.L.2    Mikhailov, V.S.3    Rohrmann, G.F.4
  • 198
    • 52649094943 scopus 로고    scopus 로고
    • PPEY motif within the rabies virus (RV) matrix protein is essential for efficient virion release and RV pathogenicity
    • Wirblich C, Tan GS, Papaneri A, Godlewski PJ, Orenstein JM, Harty RN, Schnell MJ. 2008. PPEY motif within the rabies virus (RV) matrix protein is essential for efficient virion release and RV pathogenicity. J Virol 82:9730-9738. http://dx.doi.org/10.1128/JVI.00889-08.
    • (2008) J Virol , vol.82 , pp. 9730-9738
    • Wirblich, C.1    Tan, G.S.2    Papaneri, A.3    Godlewski, P.J.4    Orenstein, J.M.5    Harty, R.N.6    Schnell, M.J.7
  • 199
    • 0028133370 scopus 로고
    • Coronavirus M proteins accumulate in the Golgi complex beyond the site of virion budding
    • Klumperman J, Locker JK, Meijer A, Horzinek MC, Geuze HJ, Rottier PJ. 1994. Coronavirus M proteins accumulate in the Golgi complex beyond the site of virion budding. J Virol 68:6523-6534.
    • (1994) J Virol , vol.68 , pp. 6523-6534
    • Klumperman, J.1    Locker, J.K.2    Meijer, A.3    Horzinek, M.C.4    Geuze, H.J.5    Rottier, P.J.6
  • 200
    • 34249993104 scopus 로고    scopus 로고
    • A novel lysis system in PM2, a lipid-containing marine double-strandedDNAbacteriophage
    • Krupovic M, Daugelavicius R, Bamford DH. 2007. A novel lysis system in PM2, a lipid-containing marine double-strandedDNAbacteriophage. Mol Microbiol 64:1635-1648. http://dx.doi.org/10.1111/j.1365-2958 .2007.05769.x.
    • (2007) Mol Microbiol , vol.64 , pp. 1635-1648
    • Krupovic, M.1    Daugelavicius, R.2    Bamford, D.H.3
  • 201
    • 84864123408 scopus 로고    scopus 로고
    • Biology of human papillomavirus infections in head and neck carcinogenesis
    • Rautava J, Syrjänen S. 2012. Biology of human papillomavirus infections in head and neck carcinogenesis. Head Neck Pathol 6(Suppl 1):S3-S15. http://dx.doi.org/10.1007/s12105-012-0367-2.
    • (2012) Head Neck Pathol , vol.6 , pp. S3-S15
    • Rautava, J.1    Syrjänen, S.2
  • 202
    • 34548157926 scopus 로고    scopus 로고
    • Hepatitis B virus maturation is sensitive to functional inhibition of ESCRT-III, Vps4, and gamma 2-adaptin
    • Lambert C, Döring T, Prange R. 2007. Hepatitis B virus maturation is sensitive to functional inhibition of ESCRT-III, Vps4, and gamma 2-adaptin. J Virol 81:9050-9060. http://dx.doi.org/10.1128/JVI.00479-07.
    • (2007) J Virol , vol.81 , pp. 9050-9060
    • Lambert, C.1    Döring, T.2    Prange, R.3
  • 203
    • 80055001131 scopus 로고    scopus 로고
    • The molecular biology of frog virus 3 and other iridoviruses infecting cold-blooded vertebrates
    • Chinchar VG, Yu KH, Jancovich JK. 2011. The molecular biology of frog virus 3 and other iridoviruses infecting cold-blooded vertebrates. Viruses 3:1959-1985. http://dx.doi.org/10.3390/v3101959.
    • (2011) Viruses , vol.3 , pp. 1959-1985
    • Chinchar, V.G.1    Yu, K.H.2    Jancovich, J.K.3
  • 204
    • 0021092804 scopus 로고
    • The lysis function of RNA bacteriophage Qbeta is mediated by the maturation (A2) protein
    • Karnik S, Billeter M. 1983. The lysis function of RNA bacteriophage Qbeta is mediated by the maturation (A2) protein.EMBOJ 2:1521-1526.
    • (1983) EMBOJ , vol.2 , pp. 1521-1526
    • Karnik, S.1    Billeter, M.2
  • 205
    • 8144224232 scopus 로고    scopus 로고
    • Molecular detection and genotyping of male-specific coliphages by reverse transcription-PCR and reverse line blot hybridization
    • Vinjé J, Oudejans SJG, Stewart JR, Sobsey MD, Long SC. 2004. Molecular detection and genotyping of male-specific coliphages by reverse transcription-PCR and reverse line blot hybridization. Appl Environ Microbiol 70:5996-6004. http://dx.doi.org/10.1128/AEM .70.10.5996-6004.2004.
    • (2004) Appl Environ Microbiol , vol.70 , pp. 5996-6004
    • Vinjé, J.1    Oudejans, S.J.G.2    Stewart, J.R.3    Sobsey, M.D.4    Long, S.C.5
  • 206
    • 18044373611 scopus 로고    scopus 로고
    • A novel rudivirus, ARV1, of the hyperthermophilic archaeal genus Acidianus
    • Vestergaard G, Häring M, Peng X, Rachel R, Garrett RA, Prangishvili D. 2005. A novel rudivirus, ARV1, of the hyperthermophilic archaeal genus Acidianus. Virology 336:83-92. http://dx.doi.org/10.1016/j.virol .2005.02.025.
    • (2005) Virology , vol.336 , pp. 83-92
    • Vestergaard, G.1    Häring, M.2    Peng, X.3    Rachel, R.4    Garrett, R.A.5    Prangishvili, D.6
  • 207
  • 209
    • 0242500253 scopus 로고    scopus 로고
    • Characterization of HaRNAV, a single-stranded RNA virus causing lysis of Heterosigma akashiwo (Raphidophyceae)
    • Tai V, Lawrence JE, Lang AS, Chan AM, Culley AI, Suttle CA. 2003. Characterization of HaRNAV, a single-stranded RNA virus causing lysis of Heterosigma akashiwo (Raphidophyceae). J Phycol 39:343-352. http://dx.doi.org/10.1046/j.1529-8817.2003.01162.x.
    • (2003) J Phycol , vol.39 , pp. 343-352
    • Tai, V.1    Lawrence, J.E.2    Lang, A.S.3    Chan, A.M.4    Culley, A.I.5    Suttle, C.A.6
  • 210
    • 33845521662 scopus 로고    scopus 로고
    • Virus-specific responses of Heterosigma akashiwo to infection
    • Lawrence JE, Brussaard CPD, Suttle CA. 2006. Virus-specific responses of Heterosigma akashiwo to infection. Appl Environ Microbiol 72:7829-7834. http://dx.doi.org/10.1128/AEM.01207-06.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 7829-7834
    • Lawrence, J.E.1    Brussaard, C.P.D.2    Suttle, C.A.3
  • 211
    • 0023029855 scopus 로고
    • Discovery of a specific double-stranded RNA virus in Giardia lamblia
    • Wang AL, Wang CC. 1986. Discovery of a specific double-stranded RNA virus in Giardia lamblia. Mol Biochem Parasitol 21:269-276. http://dx .doi.org/10.1016/0166-6851(86)90132-5.
    • (1986) Mol Biochem Parasitol , vol.21 , pp. 269-276
    • Wang, A.L.1    Wang, C.C.2
  • 212
    • 33845432820 scopus 로고    scopus 로고
    • Mutation of YMYL in the Nipah virus matrix protein abrogates budding and alters subcellular localization
    • Ciancanelli MJ, Basler CF. 2006. Mutation of YMYL in the Nipah virus matrix protein abrogates budding and alters subcellular localization. J Virol 80:12070-12078. http://dx.doi.org/10.1128/JVI.01743-06.
    • (2006) J Virol , vol.80 , pp. 12070-12078
    • Ciancanelli, M.J.1    Basler, C.F.2
  • 213
    • 27644440465 scopus 로고    scopus 로고
    • Influenza virus assembly and budding in raft-derived microdomains: A quantitative analysis of the surface distribution of HA, NA and M2 proteins
    • Leser GP, Lamb RA. 2005. Influenza virus assembly and budding in raft-derived microdomains: A quantitative analysis of the surface distribution of HA, NA and M2 proteins. Virology 342:215-227. http://dx.doi .org/10.1016/j.virol.2005.09.049.
    • (2005) Virology , vol.342 , pp. 215-227
    • Leser, G.P.1    Lamb, R.A.2
  • 216
    • 34250842469 scopus 로고    scopus 로고
    • The vaccinia virus F13L YPPL motif is required for efficient release of extracellular enveloped virus
    • Honeychurch KM, Yang G, Jordan R, Hruby DE. 2007. The vaccinia virus F13L YPPL motif is required for efficient release of extracellular enveloped virus. J Virol 81:7310-7315. http://dx.doi.org/10.1128/JVI .00034-07.
    • (2007) J Virol , vol.81 , pp. 7310-7315
    • Honeychurch, K.M.1    Yang, G.2    Jordan, R.3    Hruby, D.E.4
  • 217
    • 0021866381 scopus 로고
    • Heterogeneous progeny viruses are produced by a budding enveloped phage
    • Poddar SK, Cadden SP, Das J, Maniloff J. 1985. Heterogeneous progeny viruses are produced by a budding enveloped phage. Intervirology 23:208-221. http://dx.doi.org/10.1159/000149607.
    • (1985) Intervirology , vol.23 , pp. 208-221
    • Poddar, S.K.1    Cadden, S.P.2    Das, J.3    Maniloff, J.4
  • 218
    • 0018967464 scopus 로고
    • Effect of cell membrane composition on the growth and composition of a nonlytic enveloped mycoplasmavirus
    • Putzrath RM, Cadden SP, Maniloff J. 1980. Effect of cell membrane composition on the growth and composition of a nonlytic enveloped mycoplasmavirus. Virology 106:162-167. http://dx.doi.org/10.1016/0042-6822(80)90235-4.
    • (1980) Virology , vol.106 , pp. 162-167
    • Putzrath, R.M.1    Cadden, S.P.2    Maniloff, J.3
  • 219
    • 66649137113 scopus 로고    scopus 로고
    • Purification and functional characterization of X174 lysis protein e
    • Zheng Y, Struck DK, Young R. 2009. Purification and functional characterization of X174 lysis protein E. Biochemistry 48:4999-5006. http://dx.doi.org/10.1021/bi900469g.
    • (2009) Biochemistry , vol.48 , pp. 4999-5006
    • Zheng, Y.1    Struck, D.K.2    Young, R.3
  • 220
    • 0025266306 scopus 로고
    • Molecular biology of the Bunyaviridae
    • Elliott RM. 1990. Molecular biology of the Bunyaviridae. J Gen Virol 71:501-522. http://dx.doi.org/10.1099/0022-1317-71-3-501.
    • (1990) J Gen Virol , vol.71 , pp. 501-522
    • Elliott, R.M.1
  • 221
    • 80051767703 scopus 로고    scopus 로고
    • The role of cellular factors in promoting HIV budding
    • Weiss ER, Göttlinger H. 2011. The role of cellular factors in promoting HIV budding. J Mol Biol 410:525-533. http://dx.doi.org/10.1016/j.jmb .2011.04.055.
    • (2011) J Mol Biol , vol.410 , pp. 525-533
    • Weiss, E.R.1    Göttlinger, H.2
  • 222
    • 84857809812 scopus 로고    scopus 로고
    • Interactions of the cytoplasmic domain of Sindbis virus E2 with nucleocapsid cores promote alphavirus budding
    • Jose J, Przybyla L, Edwards TJ, Perera R, Burgner JW, II, Kuhn RJ. 2012. Interactions of the cytoplasmic domain of Sindbis virus E2 with nucleocapsid cores promote alphavirus budding. J Virol 86:2585-2599. http://dx.doi.org/10.1128/JVI.05860-11.
    • (2012) J Virol , vol.86 , pp. 2585-2599
    • Jose, J.1    Przybyla, L.2    Edwards, T.J.3    Perera, R.4    Burgner, I.I.J.W.5    Kuhn, R.J.6
  • 223
    • 41249097397 scopus 로고    scopus 로고
    • Ultrastructural characterization of the giant volcano-like virus factory of Acanthamoeba polyphaga Mimivirus
    • Suzan-Monti M, La Scola B, Barrassi L, Espinosa L, Raoult D. 2007. Ultrastructural characterization of the giant volcano-like virus factory of Acanthamoeba polyphaga Mimivirus. PLoS One 2:e328. http://dx.doi.org/10.1371/journal.pone.0000328.
    • (2007) PLoS One , vol.2 , pp. e328
    • Suzan-Monti, M.1    La Scola, B.2    Barrassi, L.3    Espinosa, L.4    Raoult, D.5
  • 224
    • 21644445703 scopus 로고    scopus 로고
    • Sulfolobus tengchongensis spindle-shaped virus STSV1: Virus-host interactions and genomic features
    • Xiang X, Chen L, Huang X, Luo Y, She Q, Huang L. 2005. Sulfolobus tengchongensis spindle-shaped virus STSV1: virus-host interactions and genomic features. J Virol 79:8677-8686. http://dx.doi.org/10.1128/JVI .79.14.8677-8686.2005.
    • (2005) J Virol , vol.79 , pp. 8677-8686
    • Xiang, X.1    Chen, L.2    Huang, X.3    Luo, Y.4    She, Q.5    Huang, L.6
  • 225
    • 0014752947 scopus 로고
    • The lysis mechanism of phage T4: Mutants affecting lysis
    • Josslin R. 1970. The lysis mechanism of phage T4: mutants affecting lysis. Virology 40:719-726. http://dx.doi.org/10.1016/0042-6822(70)90216-3.
    • (1970) Virology , vol.40 , pp. 719-726
    • Josslin, R.1
  • 226
    • 78650062665 scopus 로고    scopus 로고
    • Parvovirus infection-induced cell death and cell cycle arrest
    • Chen AY, Qiu J. 2010. Parvovirus infection-induced cell death and cell cycle arrest. Future Virol 5:731-743. http://dx.doi.org/10.2217/fvl.10.56.
    • (2010) Future Virol , vol.5 , pp. 731-743
    • Chen, A.Y.1    Qiu, J.2
  • 228
    • 53249103315 scopus 로고    scopus 로고
    • Functional and structural characterization of 2B viroporin membranolytic domains
    • Sánchez-Martínez S, Huarte N, Maeso R, Madan V, Carrasco L, Nieva JL. 2008. Functional and structural characterization of 2B viroporin membranolytic domains. Biochemistry 47:10731-10739. http://dx.doi .org/10.1021/bi800997a.
    • (2008) Biochemistry , vol.47 , pp. 10731-10739
    • Sánchez-Martínez, S.1    Huarte, N.2    Maeso, R.3    Madan, V.4    Carrasco, L.5    Nieva, J.L.6
  • 229
    • 0021891846 scopus 로고
    • Phage P22 lysis genes: Nucleotide sequences and functional relationships with T4 and lambda genes
    • Rennell D, Poteete AR. 1985. Phage P22 lysis genes: nucleotide sequences and functional relationships with T4 and lambda genes. Virology 143:280-289. http://dx.doi.org/10.1016/0042-6822(85)90115-1.
    • (1985) Virology , vol.143 , pp. 280-289
    • Rennell, D.1    Poteete, A.R.2
  • 230
    • 84883128337 scopus 로고    scopus 로고
    • Genomic characterization of JG068, a novel virulent podovirus active against Burkholderia cenocepacia
    • Lynch KH, Abdu AH, Schobert M, Dennis JJ. 2013. Genomic characterization of JG068, a novel virulent podovirus active against Burkholderia cenocepacia.BMCGenomics 14:574. http://dx.doi.org/10.1186/1471-2164-14-574.
    • (2013) BMCGenomics , vol.14 , pp. 574
    • Lynch, K.H.1    Abdu, A.H.2    Schobert, M.3    Dennis, J.J.4
  • 231
    • 79959832190 scopus 로고    scopus 로고
    • The SV40 late protein VP4 is a viroporin that forms pores to disrupt membranes for viral release
    • Raghava S, Giorda KM, Romano FB, Heuck AP, Hebert DN. 2011. The SV40 late protein VP4 is a viroporin that forms pores to disrupt membranes for viral release. PLoS Pathog 7:e1002116. http://dx.doi.org/10 .1371/journal.ppat.1002116.
    • (2011) PLoS Pathog , vol.7 , pp. e1002116
    • Raghava, S.1    Giorda, K.M.2    Romano, F.B.3    Heuck, A.P.4    Hebert, D.N.5
  • 232
    • 5644221347 scopus 로고    scopus 로고
    • The NS3 protein of bluetongue virus exhibits viroporin-like properties
    • Han Z, Harty RN. 2004. The NS3 protein of bluetongue virus exhibits viroporin-like properties. J Biol Chem 279:43092-43097. http://dx.doi .org/10.1074/jbc.M403663200.
    • (2004) J Biol Chem , vol.279 , pp. 43092-43097
    • Han, Z.1    Harty, R.N.2
  • 234
    • 0029020763 scopus 로고
    • S gene expression and the timing of lysis by bacteriophage lambda
    • Chang CY, Nam K, Young R. 1995. S gene expression and the timing of lysis by bacteriophage lambda. J Bacteriol 177:3283-3294.
    • (1995) J Bacteriol , vol.177 , pp. 3283-3294
    • Chang, C.Y.1    Nam, K.2    Young, R.3
  • 235
    • 56349116764 scopus 로고    scopus 로고
    • Virus evolution: How far does the double beta-barrel viral lineage extend?
    • Krupovic M, Bamford DH. 2008. Virus evolution: how far does the double beta-barrel viral lineage extend? Nat Rev Microbiol 6:941-948. http://dx.doi.org/10.1038/nrmicro2033.
    • (2008) Nat Rev Microbiol , vol.6 , pp. 941-948
    • Krupovic, M.1    Bamford, D.H.2
  • 236
    • 80051781242 scopus 로고    scopus 로고
    • Sulfolobus turreted icosahedral virus c92 protein responsible for the formation of pyramid-like cellular lysis structures
    • Snyder JC, Brumfield SK, Peng N, She Q, Young MJ. 2011. Sulfolobus turreted icosahedral virus c92 protein responsible for the formation of pyramid-like cellular lysis structures. J Virol 85:6287-6292. http://dx.doi .org/10.1128/JVI.00379-11.
    • (2011) J Virol , vol.85 , pp. 6287-6292
    • Snyder, J.C.1    Brumfield, S.K.2    Peng, N.3    She, Q.4    Young, M.J.5
  • 237
    • 0029872241 scopus 로고    scopus 로고
    • The adenovirus death protein (E3-11.6K) is required at very late stages of infection for efficient cell lysis and release of adenovirus from infected cells
    • Tollefson AE, Scaria A, Hermiston TW, Ryerse JS, Wold LJ, Wold WS. 1996. The adenovirus death protein (E3-11.6K) is required at very late stages of infection for efficient cell lysis and release of adenovirus from infected cells. J Virol 70:2296-2306.
    • (1996) J Virol , vol.70 , pp. 2296-2306
    • Tollefson, A.E.1    Scaria, A.2    Hermiston, T.W.3    Ryerse, J.S.4    Wold, L.J.5    Wold, W.S.6
  • 238
    • 0021015110 scopus 로고
    • Enveloped double-stranded DNA insect virus with novel structure and cytopathology
    • Federici BA. 1983. Enveloped double-stranded DNA insect virus with novel structure and cytopathology. Proc Natl Acad Sci U S A 80:7664-7668. http://dx.doi.org/10.1073/pnas.80.24.7664.
    • (1983) Proc Natl Acad Sci U S A , vol.80 , pp. 7664-7668
    • Federici, B.A.1
  • 239
    • 84866866594 scopus 로고    scopus 로고
    • PCV2 induces apoptosis and modulates calcium homeostasis in piglet lymphocytes in vitro
    • Lv Y, Dai L, Han H, Zhang S. 2012. PCV2 induces apoptosis and modulates calcium homeostasis in piglet lymphocytes in vitro. Res Vet Sci 93:1525-1530. http://dx.doi.org/10.1016/j.rvsc.2012.04.003.
    • (2012) Res Vet Sci , vol.93 , pp. 1525-1530
    • Lv, Y.1    Dai, L.2    Han, H.3    Zhang, S.4
  • 240
    • 78650722964 scopus 로고    scopus 로고
    • ORF3 of porcine circovirus 2 enhances the in vitro and in vivo spread of the virus
    • Karuppannan AK, Kwang J. 2011. ORF3 of porcine circovirus 2 enhances the in vitro and in vivo spread of the virus. Virology 410:248-256. http://dx.doi.org/10.1016/j.virol.2010.11.009.
    • (2011) Virology , vol.410 , pp. 248-256
    • Karuppannan, A.K.1    Kwang, J.2
  • 241
    • 0018386121 scopus 로고
    • Cell wall lysin as a component of the bacteriophage 6 virion
    • Mindich L, Lehman J. 1979. Cell wall lysin as a component of the bacteriophage 6 virion. J Virol 30:489-496.
    • (1979) J Virol , vol.30 , pp. 489-496
    • Mindich, L.1    Lehman, J.2
  • 242
    • 0038752050 scopus 로고    scopus 로고
    • Ovary development and polydnavirus morphogenesis in the parasitic wasp Chelonus inanitus. II. Ultrastructural analysis of calyx cell development, virion formation and release
    • Wyler T, Lanzrein B. 2003. Ovary development and polydnavirus morphogenesis in the parasitic wasp Chelonus inanitus. II. Ultrastructural analysis of calyx cell development, virion formation and release. J Gen Virol 84:1151-1163.
    • (2003) J Gen Virol , vol.84 , pp. 1151-1163
    • Wyler, T.1    Lanzrein, B.2
  • 243
    • 0023688813 scopus 로고
    • Characterization of ion channels involved in the penetration of phage T4 DNA into Escherichia coli cells
    • Boulanger P, Letellier L. 1988. Characterization of ion channels involved in the penetration of phage T4 DNA into Escherichia coli cells. J Biol Chem 263:9767-9775.
    • (1988) J Biol Chem , vol.263 , pp. 9767-9775
    • Boulanger, P.1    Letellier, L.2
  • 244
    • 4344559453 scopus 로고    scopus 로고
    • The PM2 virion has a novel organization with an internal membrane and pentameric receptor binding spikes
    • Huiskonen JT, Kivelä HM, Bamford DH, Butcher SJ. 2004. The PM2 virion has a novel organization with an internal membrane and pentameric receptor binding spikes. Nat Struct Mol Biol 11:850-856. http://dx .doi.org/10.1038/nsmb807.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 850-856
    • Huiskonen, J.T.1    Kivelä, H.M.2    Bamford, D.H.3    Butcher, S.J.4
  • 245
    • 0017371171 scopus 로고
    • Structure and synthesis of a lipid-containing bacteriophage. An endolysin activity associated with bacteriophage PM2
    • Tsukagoshi N, Schäfer R, Franklin RM. 1977. Structure and synthesis of a lipid-containing bacteriophage. An endolysin activity associated with bacteriophage PM2. Eur J Biochem 77:585-588.
    • (1977) Eur J Biochem , vol.77 , pp. 585-588
    • Tsukagoshi, N.1    Schäfer, R.2    Franklin, R.M.3


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