메뉴 건너뛰기




Volumn 1, Issue , 2013, Pages

Togaviridae

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84928945488     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (31)

References (323)
  • 1
    • 0027172559 scopus 로고
    • Sindbis virus membrane fusion is mediated by reduction of glycoprotein disulfide bridges at the cell surface
    • Abell BA, Brown DT. Sindbis virus membrane fusion is mediated by reduction of glycoprotein disulfide bridges at the cell surface. J Virol 1993;67:5496-5501.
    • (1993) J Virol , vol.67 , pp. 5496-5501
    • Abell, B.A.1    Brown, D.T.2
  • 2
    • 0021963108 scopus 로고
    • Sindbis virus proteins nsP1 and nsP2 contain homology to nonstructural proteins from several RNA plant viruses
    • Ahlquist P, Strauss EG, Rice CM, et al. Sindbis virus proteins nsP1 and nsP2 contain homology to nonstructural proteins from several RNA plant viruses. J Virol 1985;53:536-542.
    • (1985) J Virol , vol.53 , pp. 536-542
    • Ahlquist, P.1    Strauss, E.G.2    Rice, C.M.3
  • 3
    • 0036118329 scopus 로고    scopus 로고
    • The fusion peptide of Semliki Forest virus associates with sterol-rich membrane domains
    • Ahn A, Gibbons DL, Kielian M. The fusion peptide of Semliki Forest virus associates with sterol-rich membrane domains. J Virol 2002;76:3267-3275.
    • (2002) J Virol , vol.76 , pp. 3267-3275
    • Ahn, A.1    Gibbons, D.L.2    Kielian, M.3
  • 4
    • 0032758908 scopus 로고    scopus 로고
    • An epitope of the Semliki Forest virus fusion protein exposed during virus-membrane fusion
    • Ahn A, Klimjack MR, Chatterjee PK, et al. An epitope of the Semliki Forest virus fusion protein exposed during virus-membrane fusion. J Virol 1999;73:10029-10039.
    • (1999) J Virol , vol.73 , pp. 10029-10039
    • Ahn, A.1    Klimjack, M.R.2    Chatterjee, P.K.3
  • 5
    • 0033619166 scopus 로고    scopus 로고
    • Growth and stability of a cholesterol-independent Semliki Forest virus mutant in mosquitoes
    • Ahn A, Schoepp RJ, Sternberg D, et al. Growth and stability of a cholesterol-independent Semliki Forest virus mutant in mosquitoes. Virology 1999;262:452-456.
    • (1999) Virology , vol.262 , pp. 452-456
    • Ahn, A.1    Schoepp, R.J.2    Sternberg, D.3
  • 6
    • 0028833053 scopus 로고
    • Reaction in alphavirus mRNA capping: formation of a covalent complex of nonstructural protein nsP1 with 7-methyl-GMP
    • Ahola T, Kaariainen L. Reaction in alphavirus mRNA capping: formation of a covalent complex of nonstructural protein nsP1 with 7-methyl-GMP. Proc Natl Acad Sci U S A 1995;92:507-511.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 507-511
    • Ahola, T.1    Kaariainen, L.2
  • 7
    • 0033928199 scopus 로고    scopus 로고
    • Effects of palmitoylation of replicase protein nsP1 on alphavirus infection
    • Ahola T, Kujala P, Tuittila M, et al. Effects of palmitoylation of replicase protein nsP1 on alphavirus infection. J Virol 2000;74:6725-6733.
    • (2000) J Virol , vol.74 , pp. 6725-6733
    • Ahola, T.1    Kujala, P.2    Tuittila, M.3
  • 8
    • 0031060112 scopus 로고    scopus 로고
    • Critical residues of Semliki Forest virus RNA capping enzyme involved in methyltransferase and guanylyltransferase-like activities
    • Ahola T, Laakkonen P, Vihinen H, et al. Critical residues of Semliki Forest virus RNA capping enzyme involved in methyltransferase and guanylyltransferase-like activities. J Virol 1997;71:392-397.
    • (1997) J Virol , vol.71 , pp. 392-397
    • Ahola, T.1    Laakkonen, P.2    Vihinen, H.3
  • 9
    • 0033152498 scopus 로고    scopus 로고
    • Semliki Forest virus mRNA capping enzyme requires association with anionic membrane phospholipids for activity
    • Ahola T, Lampio A, Auvinen P, et al. Semliki Forest virus mRNA capping enzyme requires association with anionic membrane phospholipids for activity. EMBO J 1999;18:3164-3172.
    • (1999) EMBO J , vol.18 , pp. 3164-3172
    • Ahola, T.1    Lampio, A.2    Auvinen, P.3
  • 10
    • 0018126813 scopus 로고
    • Evidence for an autoprotease activity of Sindbis virus capsid protein
    • Aliperti G, Schlesinger MJ. Evidence for an autoprotease activity of Sindbis virus capsid protein. Virology 1978;90:366-369.
    • (1978) Virology , vol.90 , pp. 366-369
    • Aliperti, G.1    Schlesinger, M.J.2
  • 11
    • 0026802051 scopus 로고
    • Disulfide bonds are essential for the stability of the Sindbis virus envelope
    • Anthony RP, Pardes AM, Brown DT. Disulfide bonds are essential for the stability of the Sindbis virus envelope. Virology 1993;190:330-336.
    • (1993) Virology , vol.190 , pp. 330-336
    • Anthony, R.P.1    Pardes, A.M.2    Brown, D.T.3
  • 12
    • 34248359925 scopus 로고    scopus 로고
    • Development of Sindbis viruses encoding nsP2/GFP chimeric proteins and their application for studying nsP2 functioning
    • Atasheva S, Gorchakov R, English R, et al. Development of Sindbis viruses encoding nsP2/GFP chimeric proteins and their application for studying nsP2 functioning. J Virol 2007;81:5046-5057.
    • (2007) J Virol , vol.81 , pp. 5046-5057
    • Atasheva, S.1    Gorchakov, R.2    English, R.3
  • 13
    • 0031954515 scopus 로고    scopus 로고
    • The rubella virus putative replicase interacts with the retinoblastoma tumor suppressor protein
    • Atreya CD, Lee NS, Forng RY, et al. The rubella virus putative replicase interacts with the retinoblastoma tumor suppressor protein. Virus Genes 1998;16:177-183.
    • (1998) Virus Genes , vol.16 , pp. 177-183
    • Atreya, C.D.1    Lee, N.S.2    Forng, R.Y.3
  • 14
    • 0026476307 scopus 로고
    • Alphavirus assembly and entry: role of the cytoplasmic tail of the E1 spike subunit
    • Barth BU, Suomalainen M, Liljeström P, et al. Alphavirus assembly and entry: role of the cytoplasmic tail of the E1 spike subunit. J Virol 1992;66:7560-7564.
    • (1992) J Virol , vol.66 , pp. 7560-7564
    • Barth, B.U.1    Suomalainen, M.2    Liljeström, P.3
  • 15
    • 0023780765 scopus 로고
    • Demonstration in vitro of temperature-sensitive elongation of RNA in Sindbis virus mutant t6
    • Barton DJ, Sawicki SG, Sawicki DL. Demonstration in vitro of temperature-sensitive elongation of RNA in Sindbis virus mutant t6. J Virol 1988;62:3597-3602.
    • (1988) J Virol , vol.62 , pp. 3597-3602
    • Barton, D.J.1    Sawicki, S.G.2    Sawicki, D.L.3
  • 16
    • 0142060863 scopus 로고    scopus 로고
    • Expression of the zinc-finger antiviral protein inhibits alphavirus replication
    • Bick MJ, Carroll JW, Gao G, et al. Expression of the zinc-finger antiviral protein inhibits alphavirus replication. J Virol 2003;77:11555-11562.
    • (2003) J Virol , vol.77 , pp. 11555-11562
    • Bick, M.J.1    Carroll, J.W.2    Gao, G.3
  • 17
    • 0024322074 scopus 로고
    • Palmitylation of viral membrane glycoproteins takes place after exit from the endoplasmic reticulum
    • Bonatti S, Migliaccio G, Simons K. Palmitylation of viral membrane glycoproteins takes place after exit from the endoplasmic reticulum. J Biol Chem 1989;264:12590-12595.
    • (1989) J Biol Chem , vol.264 , pp. 12590-12595
    • Bonatti, S.1    Migliaccio, G.2    Simons, K.3
  • 18
    • 0036146229 scopus 로고    scopus 로고
    • Positively charged amino acid substitutions in the E2 envelope glycoprotein are associated with the emergence of Venezuelan equine encephalitis virus
    • Brault AC, Powers AM, Holmes EC, et al. Positively charged amino acid substitutions in the E2 envelope glycoprotein are associated with the emergence of Venezuelan equine encephalitis virus. J Virol 2002;76:1718-1730.
    • (2002) J Virol , vol.76 , pp. 1718-1730
    • Brault, A.C.1    Powers, A.M.2    Holmes, E.C.3
  • 19
    • 0027421842 scopus 로고
    • Sindbis virus expression vectors: packaging of RNA replicons by using defective helper RNAs
    • Bredenbeek PJ, Frolov I, Rice CM, et al. Sindbis virus expression vectors: packaging of RNA replicons by using defective helper RNAs. J Virol 1993;67:6439-6446.
    • (1993) J Virol , vol.67 , pp. 6439-6446
    • Bredenbeek, P.J.1    Frolov, I.2    Rice, C.M.3
  • 20
    • 0031849754 scopus 로고    scopus 로고
    • Binding of Sindbis virus to cell surface heparan sulfate
    • Byrnes AP, Griffin DE. Binding of Sindbis virus to cell surface heparan sulfate. J Virol 1998;72:7349-7356.
    • (1998) J Virol , vol.72 , pp. 7349-7356
    • Byrnes, A.P.1    Griffin, D.E.2
  • 21
    • 0033989275 scopus 로고    scopus 로고
    • Large-plaque mutants of Sindbis virus show reduced binding to heparan sulfate, heightened viremia, and slower clearance from the circulation
    • Byrnes AP, Griffin DE. Large-plaque mutants of Sindbis virus show reduced binding to heparan sulfate, heightened viremia, and slower clearance from the circulation. J Virol 2000;74:644-651.
    • (2000) J Virol , vol.74 , pp. 644-651
    • Byrnes, A.P.1    Griffin, D.E.2
  • 22
    • 0030013728 scopus 로고    scopus 로고
    • Disulfide bridge-mediated folding of Sindbis virus glycoproteins
    • Carleton M, Brown DT. Disulfide bridge-mediated folding of Sindbis virus glycoproteins. J Virol 1996;70:5541-5547.
    • (1996) J Virol , vol.70 , pp. 5541-5547
    • Carleton, M.1    Brown, D.T.2
  • 23
    • 10044283361 scopus 로고    scopus 로고
    • A conserved histidine in the ij loop of the Semliki Forest virus E1 protein plays an important role in membrane fusion
    • Chanel-Vos C, Kielian M. A conserved histidine in the ij loop of the Semliki Forest virus E1 protein plays an important role in membrane fusion. J Virol 2004;78:13543-13552.
    • (2004) J Virol , vol.78 , pp. 13543-13552
    • Chanel-Vos, C.1    Kielian, M.2
  • 24
    • 0033918941 scopus 로고    scopus 로고
    • Biochemical consequences of a mutation that controls the cholesterol dependence of Semliki Forest virus fusion
    • Chatterjee PK, Vashishtha M, Kielian M. Biochemical consequences of a mutation that controls the cholesterol dependence of Semliki Forest virus fusion. J Virol 2000;74:1623-1631.
    • (2000) J Virol , vol.74 , pp. 1623-1631
    • Chatterjee, P.K.1    Vashishtha, M.2    Kielian, M.3
  • 25
    • 1842431531 scopus 로고    scopus 로고
    • Rubella virus capsid protein modulates viral genome replication and virus infectivity
    • Chen MH, Icenogle JP. Rubella virus capsid protein modulates viral genome replication and virus infectivity. J Virol 2004;78:4314-4322.
    • (2004) J Virol , vol.78 , pp. 4314-4322
    • Chen, M.H.1    Icenogle, J.P.2
  • 26
    • 79954632655 scopus 로고    scopus 로고
    • Generating enveloped virus-like particles with in vitro assembled cores
    • Cheng F, Mukhopadhyay S. Generating enveloped virus-like particles with in vitro assembled cores. Virology 2011;413:153-160.
    • (2011) Virology , vol.413 , pp. 153-160
    • Cheng, F.1    Mukhopadhyay, S.2
  • 27
    • 0028919758 scopus 로고
    • Nucleocapsid and glycoprotein organization in an enveloped virus
    • Cheng RH, Kuhn RJ, Olson NH, et al. Nucleocapsid and glycoprotein organization in an enveloped virus. Cell 1995;80:621-630.
    • (1995) Cell , vol.80 , pp. 621-630
    • Cheng, R.H.1    Kuhn, R.J.2    Olson, N.H.3
  • 28
    • 0030890291 scopus 로고    scopus 로고
    • The structure of Semliki Forest virus core protein
    • Choi H-K, Lu G, Lee S, et al. The structure of Semliki Forest virus core protein. Proteins 1997;27:345-359.
    • (1997) Proteins , vol.27 , pp. 345-359
    • Choi, H.-K.1    Lu, G.2    Lee, S.3
  • 29
    • 0026419333 scopus 로고
    • Structure of Sindbis virus core protein reveals a chymotrypsin-like serine proteinase and the organization of the virion
    • Choi HK, Tong L, Minor W, et al. Structure of Sindbis virus core protein reveals a chymotrypsin-like serine proteinase and the organization of the virion. Nature (London) 1991;354:37-43.
    • (1991) Nature (London) , vol.354 , pp. 37-43
    • Choi, H.K.1    Tong, L.2    Minor, W.3
  • 30
    • 0026536605 scopus 로고
    • Inhibition of enveloped RNA virus formation by peptides corresponding to glycoprotein sequences
    • Collier NC, Adams SP, Weingarten H, et al. Inhibition of enveloped RNA virus formation by peptides corresponding to glycoprotein sequences. Antivir Chem Chemother 1992;3:31-36.
    • (1992) Antivir Chem Chemother , vol.3 , pp. 31-36
    • Collier, N.C.1    Adams, S.P.2    Weingarten, H.3
  • 31
    • 0028953947 scopus 로고
    • Sphingolipid-dependent fusion of Semliki Forest virus with cholesterol-containing liposomes requires both the 3-hydroxyl group and the double bond of the sphingolipid backbone
    • Corver J, Moesby L, Erukulla RK, et al. Sphingolipid-dependent fusion of Semliki Forest virus with cholesterol-containing liposomes requires both the 3-hydroxyl group and the double bond of the sphingolipid backbone. J Virol 1995;69:3220-3223.
    • (1995) J Virol , vol.69 , pp. 3220-3223
    • Corver, J.1    Moesby, L.2    Erukulla, R.K.3
  • 32
    • 33749553499 scopus 로고    scopus 로고
    • Tracking and elucidating alphavirus-host protein interactions
    • Cristea IM, Carroll JW, Rout MP, et al. Tracking and elucidating alphavirus-host protein interactions. J Biol Chem 2006;281:30269-30278.
    • (2006) J Biol Chem , vol.281 , pp. 30269-30278
    • Cristea, I.M.1    Carroll, J.W.2    Rout, M.P.3
  • 33
    • 77953320616 scopus 로고    scopus 로고
    • Host factors associated with the Sindbis virus RNA-dependent RNA polymerase: role for G3BP1 and G3BP2 in virus replication
    • Cristea IM, Rozjabek H, Molloy KR, et al. Host factors associated with the Sindbis virus RNA-dependent RNA polymerase: role for G3BP1 and G3BP2 in virus replication. J Virol 2010;84:6720-6732.
    • (2010) J Virol , vol.84 , pp. 6720-6732
    • Cristea, I.M.1    Rozjabek, H.2    Molloy, K.R.3
  • 34
    • 0023775458 scopus 로고
    • Dissection of Semliki Forest virus glycoprotein delivery from the trans-Golgi network to the cell surface in permeabilized BHK cells
    • de Curtis I, Simons K. Dissection of Semliki Forest virus glycoprotein delivery from the trans-Golgi network to the cell surface in permeabilized BHK cells. Proc Natl Acad Sci U S A 1988;85:8052-8056.
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 8052-8056
    • de Curtis, I.1    Simons, K.2
  • 35
    • 0025352629 scopus 로고
    • Cleavage-site preferences of Sindbis virus polyproteins containing the nonstructural proteinase: Evidence for temporal regulation of polyprotein processing in vivo
    • de Groot RJ, Hardy RH, Shirako Y, et al. Cleavage-site preferences of Sindbis virus polyproteins containing the nonstructural proteinase: Evidence for temporal regulation of polyprotein processing in vivo. EMBO J 1990;9:2631-2638.
    • (1990) EMBO J , vol.9 , pp. 2631-2638
    • de Groot, R.J.1    Hardy, R.H.2    Shirako, Y.3
  • 36
    • 0026093971 scopus 로고
    • Sindbis virus RNA polymerase is degraded by the N-end rule pathway
    • de Groot RJ, Rümenapf T, Kuhn RJ, et al. Sindbis virus RNA polymerase is degraded by the N-end rule pathway. Proc Natl Acad Sci U S A 1991;88:8967-8971.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 8967-8971
    • de Groot, R.J.1    Rümenapf, T.2    Kuhn, R.J.3
  • 37
    • 0029881285 scopus 로고    scopus 로고
    • Sindbis virus RNA-negative mutants that fail to convert from minus-strand to plus-strand synthesis: role of the nsP2 protein
    • De I, Sawicki SG, Sawicki DL. Sindbis virus RNA-negative mutants that fail to convert from minus-strand to plus-strand synthesis: role of the nsP2 protein. J Virol 1996;70:2706-2719.
    • (1996) J Virol , vol.70 , pp. 2706-2719
    • De, I.1    Sawicki, S.G.2    Sawicki, D.L.3
  • 38
    • 0032541402 scopus 로고    scopus 로고
    • The clathrin endocytic pathway in viral infection
    • DeTulleo L, Kirchhausen T. The clathrin endocytic pathway in viral infection. EMBO J 1998;17:4585-4593.
    • (1998) EMBO J , vol.17 , pp. 4585-4593
    • DeTulleo, L.1    Kirchhausen, T.2
  • 39
    • 0024315805 scopus 로고
    • Evidence that Sindbis virus nsP2 is an autoprotease which processes the virus nonstructural polyprotein
    • Ding M, Schlesinger MJ. Evidence that Sindbis virus nsP2 is an autoprotease which processes the virus nonstructural polyprotein. Virology 1989;171:280-284.
    • (1989) Virology , vol.171 , pp. 280-284
    • Ding, M.1    Schlesinger, M.J.2
  • 40
    • 0025287319 scopus 로고
    • Sequence of the genome RNA of rubella virus: Evidence for genetic rearrangement during togavirus evolution
    • Dominguez G, Wang C-Y, Frey TK. Sequence of the genome RNA of rubella virus: Evidence for genetic rearrangement during togavirus evolution. Virology 1990;177:225-238.
    • (1990) Virology , vol.177 , pp. 225-238
    • Dominguez, G.1    Wang, C.-Y.2    Frey, T.K.3
  • 41
    • 79959812241 scopus 로고    scopus 로고
    • A dynamic landscape for antibody binding modulates antibody-mediated neutralization of West Nile virus
    • Dowd KA, Jost CA, Durbin AP, et al. A dynamic landscape for antibody binding modulates antibody-mediated neutralization of West Nile virus. PLoS Pathog 2011;7:e1002111.
    • (2011) PLoS Pathog , vol.7 , pp. e1002111
    • Dowd, K.A.1    Jost, C.A.2    Durbin, A.P.3
  • 42
    • 0031550546 scopus 로고    scopus 로고
    • Identification of mutations in a Sindbis virus variant able to establish persistent infection in BHK cells: the importance of a mutation in the nsP2 gene
    • Dryga SA, Dryga OA, Schlesinger S. Identification of mutations in a Sindbis virus variant able to establish persistent infection in BHK cells: the importance of a mutation in the nsP2 gene. Virology 1997;228:74-83.
    • (1997) Virology , vol.228 , pp. 74-83
    • Dryga, S.A.1    Dryga, O.A.2    Schlesinger, S.3
  • 43
    • 0025909409 scopus 로고
    • Sindbis virus infection of a Chinese hamster ovary cell mutant defective in the acidification of endosomes
    • Edwards J, Brown DT. Sindbis virus infection of a Chinese hamster ovary cell mutant defective in the acidification of endosomes. Virology 1991;182:28-33.
    • (1991) Virology , vol.182 , pp. 28-33
    • Edwards, J.1    Brown, D.T.2
  • 44
    • 0036333797 scopus 로고    scopus 로고
    • Modification of Asn374 of nsP1 suppresses a Sindbis virus nsP4 minus-strand polymerase mutant
    • Fata CL, Sawicki G, Sawicki DL. Modification of Asn374 of nsP1 suppresses a Sindbis virus nsP4 minus-strand polymerase mutant. J Virol 2002;76:8641-8649.
    • (2002) J Virol , vol.76 , pp. 8641-8649
    • Fata, C.L.1    Sawicki, G.2    Sawicki, D.L.3
  • 45
    • 2342623475 scopus 로고    scopus 로고
    • Changes of the secondary structure of the 5' end of the Sindbis virus genome inhibit virus growth in mosquito cells and lead to accumulation of adaptive mutations
    • Fayzulin R, Frolov I. Changes of the secondary structure of the 5' end of the Sindbis virus genome inhibit virus growth in mosquito cells and lead to accumulation of adaptive mutations. J Virol 2004;78:4953-4964.
    • (2004) J Virol , vol.78 , pp. 4953-4964
    • Fayzulin, R.1    Frolov, I.2
  • 46
    • 10644264272 scopus 로고    scopus 로고
    • Sindbis virus with a tricomponent genome
    • Fayzulin R, Gorchakov R, Petrakova O, et al. Sindbis virus with a tricomponent genome. J Virol 2005;79:637-643.
    • (2005) J Virol , vol.79 , pp. 637-643
    • Fayzulin, R.1    Gorchakov, R.2    Petrakova, O.3
  • 47
    • 0032538274 scopus 로고    scopus 로고
    • The first step: activation of the Semliki Forest virus spike protein precursor causes a localized conformational change in the trimeric spike
    • Ferlenghi I, Gowen B, de Haas F, et al. The first step: activation of the Semliki Forest virus spike protein precursor causes a localized conformational change in the trimeric spike. J Mol Biol 1998;283:71-81.
    • (1998) J Mol Biol , vol.283 , pp. 71-81
    • Ferlenghi, I.1    Gowen, B.2    de Haas, F.3
  • 48
    • 54049148146 scopus 로고    scopus 로고
    • Discovery of frameshifting in Alphavirus 6K resolves a 20-year enigma
    • Firth AE, Chung BY, Fleeton MN, et al. Discovery of frameshifting in Alphavirus 6K resolves a 20-year enigma. Virol J 2008;5:108.
    • (2008) Virol J , vol.5 , pp. 108
    • Firth, A.E.1    Chung, B.Y.2    Fleeton, M.N.3
  • 49
    • 0025281122 scopus 로고
    • A conformational change in Sindbis glycoprotein E1 and E2 is detected at the plasma membrane as a consequence of early virus-cell interaction
    • Flynn DC, Meyer WJ, MacKenzie JM, et al. A conformational change in Sindbis glycoprotein E1 and E2 is detected at the plasma membrane as a consequence of early virus-cell interaction. J Virol 1990;64:3643-3653.
    • (1990) J Virol , vol.64 , pp. 3643-3653
    • Flynn, D.C.1    Meyer, W.J.2    MacKenzie, J.M.3
  • 50
    • 0032970117 scopus 로고    scopus 로고
    • Mutations in the retinoblastoma protein-binding LXCXE motif of rubella virus putative replicase affect virus replication
    • Forng RY, Atreya CD. Mutations in the retinoblastoma protein-binding LXCXE motif of rubella virus putative replicase affect virus replication. J Gen Virol 1999;80(Pt 2):327-332.
    • (1999) J Gen Virol , vol.80 , Issue.PT 2 , pp. 327-332
    • Forng, R.Y.1    Atreya, C.D.2
  • 51
    • 0028890264 scopus 로고
    • Identification of the rubella virus nonstructural proteins
    • Forng RY, Frey TK. Identification of the rubella virus nonstructural proteins. Virology 1995;206:843-853.
    • (1995) Virology , vol.206 , pp. 843-853
    • Forng, R.Y.1    Frey, T.K.2
  • 52
    • 84857853808 scopus 로고    scopus 로고
    • Genome-scale phylogeny of the alphavirus genus suggests a marine origin
    • Forrester NL, Palacios G, Tesh RB, et al. Genome-scale phylogeny of the alphavirus genus suggests a marine origin. J Virol 2012;86:2729-2738.
    • (2012) J Virol , vol.86 , pp. 2729-2738
    • Forrester, N.L.1    Palacios, G.2    Tesh, R.B.3
  • 53
    • 0029823070 scopus 로고    scopus 로고
    • Preformed cytoplasmic nucleocapsids are not necessary for alphavirus budding
    • Forsell K, Griffiths G, Garoff H. Preformed cytoplasmic nucleocapsids are not necessary for alphavirus budding. EMBO J 1996;15:6495-6505.
    • (1996) EMBO J , vol.15 , pp. 6495-6505
    • Forsell, K.1    Griffiths, G.2    Garoff, H.3
  • 54
    • 0034596852 scopus 로고    scopus 로고
    • Membrane proteins organize a symmetrical virus
    • Forsell K, Xing L, Kozlovska T, et al. Membrane proteins organize a symmetrical virus. EMBO J 2000;19:5081-5091.
    • (2000) EMBO J , vol.19 , pp. 5081-5091
    • Forsell, K.1    Xing, L.2    Kozlovska, T.3
  • 55
    • 0028028506 scopus 로고
    • Molecular biology of rubella virus
    • Frey TK. Molecular biology of rubella virus. Adv Virus Res 1994;44:69-160.
    • (1994) Adv Virus Res , vol.44 , pp. 69-160
    • Frey, T.K.1
  • 56
    • 0032924734 scopus 로고    scopus 로고
    • Selection of RNA replicons capable of persistent noncytopathic replication in mammalian cells
    • Frolov I, Agapov E, Hoffman TA Jr, et al. Selection of RNA replicons capable of persistent noncytopathic replication in mammalian cells. J Virol 1999;73:3854-3865.
    • (1999) J Virol , vol.73 , pp. 3854-3865
    • Frolov, I.1    Agapov, E.2    Hoffman, T.A.3
  • 57
    • 0035175362 scopus 로고    scopus 로고
    • Cis-acting RNA elements at the 5' end of Sindbis virus genome RNA regulate minus- and plus-strand RNA synthesis
    • Frolov I, Hardy R, Rice CM. Cis-acting RNA elements at the 5' end of Sindbis virus genome RNA regulate minus- and plus-strand RNA synthesis. RNA 2001;7:1638-1651.
    • (2001) RNA , vol.7 , pp. 1638-1651
    • Frolov, I.1    Hardy, R.2    Rice, C.M.3
  • 58
    • 0029961358 scopus 로고    scopus 로고
    • Alphavirus-based expression vectors: strategies and applications
    • Frolov I, Hoffman TA, Pragai BM, et al. Alphavirus-based expression vectors: strategies and applications. Proc Natl Acad Sci U S A 1996;93:11371-11377.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 11371-11377
    • Frolov, I.1    Hoffman, T.A.2    Pragai, B.M.3
  • 59
    • 0028057720 scopus 로고
    • Comparison of the effects of Sindbis virus and Sindbis virus replicons on host cell protein synthesis and cytopathogenicity in BHK cells
    • Frolov I, Schlesinger S. Comparison of the effects of Sindbis virus and Sindbis virus replicons on host cell protein synthesis and cytopathogenicity in BHK cells. J Virol 1994;68:1721-1727.
    • (1994) J Virol , vol.68 , pp. 1721-1727
    • Frolov, I.1    Schlesinger, S.2
  • 60
    • 0030068269 scopus 로고    scopus 로고
    • Translation of Sindbis virus mRNA: analysis of sequences downstream of the initiating AUG codon that enhance translation
    • Frolov I, Schlesinger S. Translation of Sindbis virus mRNA: analysis of sequences downstream of the initiating AUG codon that enhance translation. J Virol 1996;70:1182-1190.
    • (1996) J Virol , vol.70 , pp. 1182-1190
    • Frolov, I.1    Schlesinger, S.2
  • 61
    • 78049491884 scopus 로고    scopus 로고
    • Functional Sindbis virus replicative complexes are formed at the plasma membrane
    • Frolova EI, Gorchakov R, Pereboeva L, et al. Functional Sindbis virus replicative complexes are formed at the plasma membrane. J Virol 2010;84:11679-11695.
    • (2010) J Virol , vol.84 , pp. 11679-11695
    • Frolova, E.I.1    Gorchakov, R.2    Pereboeva, L.3
  • 62
    • 0024237292 scopus 로고
    • Alphavirus RNA replicase is located on the cytoplasmic surface of endosomes and lysosomes
    • Froshauer S, Kartenbeck J, Helenius A. Alphavirus RNA replicase is located on the cytoplasmic surface of endosomes and lysosomes. J Cell Biol 1988;107:2075-2086.
    • (1988) J Cell Biol , vol.107 , pp. 2075-2086
    • Froshauer, S.1    Kartenbeck, J.2    Helenius, A.3
  • 63
    • 0029052283 scopus 로고
    • Low pH induces swiveling of the glycoprotein heterodimers in the Semliki Forest virus spike complex
    • Fuller SD, Berriman JA, Butcher SJ, et al. Low pH induces swiveling of the glycoprotein heterodimers in the Semliki Forest virus spike complex. Cell 1995;81:715-725.
    • (1995) Cell , vol.81 , pp. 715-725
    • Fuller, S.D.1    Berriman, J.A.2    Butcher, S.J.3
  • 64
    • 0025373966 scopus 로고
    • Site-directed mutations in the Sindbis virus 6K protein reveal sites for fatty acylation and the underacylated protein affects virus release and virion structure
    • Gaedigk-Nitschko K, Ding M, Schlesinger MJ. Site-directed mutations in the Sindbis virus 6K protein reveal sites for fatty acylation and the underacylated protein affects virus release and virion structure. Virology 1990;175:282-291.
    • (1990) Virology , vol.175 , pp. 282-291
    • Gaedigk-Nitschko, K.1    Ding, M.2    Schlesinger, M.J.3
  • 65
    • 0025364097 scopus 로고
    • The Sindbis virus 6K protein can be detected in virions and is acylated with fatty acids
    • Gaedigk-Nitschko K, Schlesinger MJ. The Sindbis virus 6K protein can be detected in virions and is acylated with fatty acids. Virology 1990;175:274-281.
    • (1990) Virology , vol.175 , pp. 274-281
    • Gaedigk-Nitschko, K.1    Schlesinger, M.J.2
  • 66
    • 80053154735 scopus 로고    scopus 로고
    • Heparan sulfate binding by natural eastern equine encephalitis viruses promotes neurovirulence
    • Gardner CL, Ebel GD, Ryman KD, et al. Heparan sulfate binding by natural eastern equine encephalitis viruses promotes neurovirulence. Proc Natl Acad Sci U S A 2011;108:16026-16031.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 16026-16031
    • Gardner, C.L.1    Ebel, G.D.2    Ryman, K.D.3
  • 67
    • 33744937066 scopus 로고    scopus 로고
    • Sindbis virus nonstructural protein nsP2 is cytotoxic and inhibits cellular transcription
    • Garmashova N, Gorchakov R, Frolova E, et al. Sindbis virus nonstructural protein nsP2 is cytotoxic and inhibits cellular transcription. J Virol 2006;80:5686-5696.
    • (2006) J Virol , vol.80 , pp. 5686-5696
    • Garmashova, N.1    Gorchakov, R.2    Frolova, E.3
  • 68
    • 33847199327 scopus 로고    scopus 로고
    • The Old World and New World alphaviruses use different virus-specific proteins for induction of transcriptional shutoff
    • Garmashova N, Gorchakov R, Volkova E, et al. The Old World and New World alphaviruses use different virus-specific proteins for induction of transcriptional shutoff. J Virol 2007;81:2472-2484.
    • (2007) J Virol , vol.81 , pp. 2472-2484
    • Garmashova, N.1    Gorchakov, R.2    Volkova, E.3
  • 70
    • 0025144560 scopus 로고
    • The signal sequence of the p62 protein of Semliki Forest virus is involved in initiation but not in completing chain translocation
    • Garoff H, Huylebroeck D, Robinson A, et al. The signal sequence of the p62 protein of Semliki Forest virus is involved in initiation but not in completing chain translocation. J Cell Biol 1990;111:867-876.
    • (1990) J Cell Biol , vol.111 , pp. 867-876
    • Garoff, H.1    Huylebroeck, D.2    Robinson, A.3
  • 71
    • 0020504587 scopus 로고
    • Expression of Semliki Forest virus proteins from cloned complementary DNA. II. The membrane-spanning glycoprotein E2 is transported to the cell surface without its normal cytoplasmic domain
    • Garoff H, Kondor-Koch C, Petterson R, et al. Expression of Semliki Forest virus proteins from cloned complementary DNA. II. The membrane-spanning glycoprotein E2 is transported to the cell surface without its normal cytoplasmic domain. J Cell Biol 1983;97:652.
    • (1983) J Cell Biol , vol.97 , pp. 652
    • Garoff, H.1    Kondor-Koch, C.2    Petterson, R.3
  • 72
    • 0027510702 scopus 로고
    • Deletion analysis of the capsid protein of Sindbis virus: Identification of the RNA binding region
    • Geigenmüller-Gnirke U, Nitschko H, Schlesinger S. Deletion analysis of the capsid protein of Sindbis virus: Identification of the RNA binding region. J Virol 1993;67:1620-1626.
    • (1993) J Virol , vol.67 , pp. 1620-1626
    • Geigenmüller-Gnirke, U.1    Nitschko, H.2    Schlesinger, S.3
  • 73
    • 0033809466 scopus 로고    scopus 로고
    • Alphavirus RNA genome repair and evolution: molecular characterization of infectious Sindbis virus isolates lacking a known conserved motif at the 3' end of the genome
    • George J, Raju R. Alphavirus RNA genome repair and evolution: molecular characterization of infectious Sindbis virus isolates lacking a known conserved motif at the 3' end of the genome. J Virol 2000;74:9776-9785.
    • (2000) J Virol , vol.74 , pp. 9776-9785
    • George, J.1    Raju, R.2
  • 74
    • 0033881011 scopus 로고    scopus 로고
    • Formation and characterization of the trimeric form of the fusion protein of Semliki Forest Virus
    • Gibbons DL, Ahn A, Chatterjee PK, et al. Formation and characterization of the trimeric form of the fusion protein of Semliki Forest Virus. J Virol 2000;74:7772-7780.
    • (2000) J Virol , vol.74 , pp. 7772-7780
    • Gibbons, D.L.1    Ahn, A.2    Chatterjee, P.K.3
  • 75
    • 0141429172 scopus 로고    scopus 로고
    • Visualization of the target-membrane-inserted fusion protein of Semliki Forest virus by combined electron microscopy and crystallography
    • Gibbons DL, Erk I, Reilly B, et al. Visualization of the target-membrane-inserted fusion protein of Semliki Forest virus by combined electron microscopy and crystallography. Cell 2003;114:573-583.
    • (2003) Cell , vol.114 , pp. 573-583
    • Gibbons, D.L.1    Erk, I.2    Reilly, B.3
  • 76
    • 1842562375 scopus 로고    scopus 로고
    • Purification and crystallization reveal two types of interactions of the fusion protein homotrimer of Semliki Forest virus
    • Gibbons DL, Reilly B, Ahn A, et al. Purification and crystallization reveal two types of interactions of the fusion protein homotrimer of Semliki Forest virus. J Virol 2004;78:3514-3523.
    • (2004) J Virol , vol.78 , pp. 3514-3523
    • Gibbons, D.L.1    Reilly, B.2    Ahn, A.3
  • 77
    • 1642540249 scopus 로고    scopus 로고
    • Conformational change and protein-protein interactions of the fusion protein of Semliki Forest virus
    • Gibbons DL, Vaney M-C, Roussel A, et al. Conformational change and protein-protein interactions of the fusion protein of Semliki Forest virus. Nature 2004;427:322-325.
    • (2004) Nature , vol.427 , pp. 322-325
    • Gibbons, D.L.1    Vaney, M.-C.2    Roussel, A.3
  • 78
    • 0032169169 scopus 로고    scopus 로고
    • The role of low pH and disulfide shuffling in the entry and fusion of Semliki Forest virus and Sindbis virus
    • Glomb-Reinmund S, Kielian M. The role of low pH and disulfide shuffling in the entry and fusion of Semliki Forest virus and Sindbis virus. Virology 1998;248:372-381.
    • (1998) Virology , vol.248 , pp. 372-381
    • Glomb-Reinmund, S.1    Kielian, M.2
  • 79
    • 0033033813 scopus 로고    scopus 로고
    • RNA helicase activity of Semliki Forest virus replicase protein NSP2
    • Gomez de Cedron M, Ehsani N, Mikkola ML, et al. RNA helicase activity of Semliki Forest virus replicase protein NSP2. FEBS Lett 1999;448:19-22.
    • (1999) FEBS Lett , vol.448 , pp. 19-22
    • Gomez de Cedron, M.1    Ehsani, N.2    Mikkola, M.L.3
  • 80
    • 0023705613 scopus 로고
    • A novel superfamily of nucleoside triphosphate-binding motif containing proteins which are probably involved in duplex unwinding in DNA and RNA replication and recombination
    • Gorbalenya AE, Koonin EV, Donchenko AP, et al. A novel superfamily of nucleoside triphosphate-binding motif containing proteins which are probably involved in duplex unwinding in DNA and RNA replication and recombination. FEBS Lett 1988;235:16-24.
    • (1988) FEBS Lett , vol.235 , pp. 16-24
    • Gorbalenya, A.E.1    Koonin, E.V.2    Donchenko, A.P.3
  • 81
    • 0025739985 scopus 로고
    • Putative papain-related thiol proteases of positive-strand RNA viruses
    • Gorbalenya AE, Koonin EV, Lai MMC. Putative papain-related thiol proteases of positive-strand RNA viruses. FEBS Lett 1991;288:201-205.
    • (1991) FEBS Lett , vol.288 , pp. 201-205
    • Gorbalenya, A.E.1    Koonin, E.V.2    Lai, M.M.C.3
  • 82
    • 22544443363 scopus 로고    scopus 로고
    • Inhibition of transcription and translation in Sindbis virus-infected cells
    • Gorchakov R, Frolova E, Frolov I. Inhibition of transcription and translation in Sindbis virus-infected cells. J Virol 2005;79:9397-9409.
    • (2005) J Virol , vol.79 , pp. 9397-9409
    • Gorchakov, R.1    Frolova, E.2    Frolov, I.3
  • 83
    • 45749090147 scopus 로고    scopus 로고
    • A new role for ns polyprotein cleavage in Sindbis virus replication
    • Gorchakov R, Frolova E, Sawicki S, et al. A new role for ns polyprotein cleavage in Sindbis virus replication. J Virol 2008;82:6218-6231.
    • (2008) J Virol , vol.82 , pp. 6218-6231
    • Gorchakov, R.1    Frolova, E.2    Sawicki, S.3
  • 84
    • 8644267555 scopus 로고    scopus 로고
    • The zinc finger antiviral protein directly binds to specific viral mRNAs through the CCCH zinc finger motifs
    • Guo X, Carroll JW, Macdonald MR, et al. The zinc finger antiviral protein directly binds to specific viral mRNAs through the CCCH zinc finger motifs. J Virol 2004;78:12781-12787.
    • (2004) J Virol , vol.78 , pp. 12781-12787
    • Guo, X.1    Carroll, J.W.2    Macdonald, M.R.3
  • 85
    • 0037009367 scopus 로고    scopus 로고
    • Acid-induced movements in the glycoprotein shell of an alphavirus turn the spikes into membrane fusion mode
    • Haag L, Garoff H, Xing L, et al. Acid-induced movements in the glycoprotein shell of an alphavirus turn the spikes into membrane fusion mode. EMBO J 2002;21:4402-4410.
    • (2002) EMBO J , vol.21 , pp. 4402-4410
    • Haag, L.1    Garoff, H.2    Xing, L.3
  • 86
    • 0012471185 scopus 로고
    • Sequence analysis of three Sindbis virus mutants temperature-sensitive in the capsid protein autoprotease
    • Hahn CS, Strauss EG, Strauss JH. Sequence analysis of three Sindbis virus mutants temperature-sensitive in the capsid protein autoprotease. Proc Natl Acad Sci U S A 1985;82:4648-4652.
    • (1985) Proc Natl Acad Sci U S A , vol.82 , pp. 4648-4652
    • Hahn, C.S.1    Strauss, E.G.2    Strauss, J.H.3
  • 87
    • 0025352036 scopus 로고
    • Site-directed mutagenesis of the proposed catalytic amino acids of the Sindbis virus capsid protein autoprotease
    • Hahn CS, Strauss JH. Site-directed mutagenesis of the proposed catalytic amino acids of the Sindbis virus capsid protein autoprotease. J Virol 1990;64:3069-3073.
    • (1990) J Virol , vol.64 , pp. 3069-3073
    • Hahn, C.S.1    Strauss, J.H.2
  • 88
    • 0024582528 scopus 로고
    • Mapping of RNA- temperature-sensitive mutants of Sindbis virus: Complementation group F mutants have lesions in nsP4
    • Hahn YS, Grakoui A, Rice CM, et al. Mapping of RNA- temperature-sensitive mutants of Sindbis virus: Complementation group F mutants have lesions in nsP4. J Virol 1989;63:1194-1202.
    • (1989) J Virol , vol.63 , pp. 1194-1202
    • Hahn, Y.S.1    Grakoui, A.2    Rice, C.M.3
  • 89
    • 0037470148 scopus 로고    scopus 로고
    • Prefusion rearrangements resulting in fusion Peptide exposure in Semliki forest virus
    • Hammar L, Markarian S, Haag L, et al. Prefusion rearrangements resulting in fusion Peptide exposure in Semliki forest virus. J Biol Chem 2003;278:7189-7198.
    • (2003) J Biol Chem , vol.278 , pp. 7189-7198
    • Hammar, L.1    Markarian, S.2    Haag, L.3
  • 90
    • 31944440868 scopus 로고    scopus 로고
    • The role of the 3' terminus of the Sindbis virus genome in minus-strand initiation site selection
    • Hardy RW. The role of the 3' terminus of the Sindbis virus genome in minus-strand initiation site selection. Virology 2006;345:520-531.
    • (2006) Virology , vol.345 , pp. 520-531
    • Hardy, R.W.1
  • 91
    • 16244413640 scopus 로고    scopus 로고
    • Requirements at the 3' end of the Sindbis virus genome for efficient synthesis of minus-strand RNA
    • Hardy RW, Rice CM. Requirements at the 3' end of the Sindbis virus genome for efficient synthesis of minus-strand RNA. J Virol 2005;79:4630-4639.
    • (2005) J Virol , vol.79 , pp. 4630-4639
    • Hardy, R.W.1    Rice, C.M.2
  • 92
    • 0023972122 scopus 로고
    • Processing of the nonstructural polyproteins of Sindbis virus: Study of the kinetics in vivo using monospecific antibodies
    • Hardy WR, Strauss JH. Processing of the nonstructural polyproteins of Sindbis virus: Study of the kinetics in vivo using monospecific antibodies. J Virol 1988;62:998-1007.
    • (1988) J Virol , vol.62 , pp. 998-1007
    • Hardy, W.R.1    Strauss, J.H.2
  • 93
    • 0024421374 scopus 로고
    • Processing the nonstructural proteins of Sindbis virus: Nonstructural proteinase is in the C-terminal half of nsP2 and functions both in cis and trans
    • Hardy WR, Strauss JH. Processing the nonstructural proteins of Sindbis virus: Nonstructural proteinase is in the C-terminal half of nsP2 and functions both in cis and trans. J Virol 1989;63:4653-4664.
    • (1989) J Virol , vol.63 , pp. 4653-4664
    • Hardy, W.R.1    Strauss, J.H.2
  • 94
    • 49649147698 scopus 로고
    • Lipid and protein organization in Sindbis virus
    • Harrison SC, David A, Jumblatt J, et al. Lipid and protein organization in Sindbis virus. J Mol Biol 1971;60:532.
    • (1971) J Mol Biol , vol.60 , pp. 532
    • Harrison, S.C.1    David, A.2    Jumblatt, J.3
  • 95
    • 0026767049 scopus 로고
    • Crystallization of Sindbis virus and its nucleocapsid
    • Harrison SC, Strong RK, Schlesinger S, et al. Crystallization of Sindbis virus and its nucleocapsid. J Mol Biol 1992;226:277-280.
    • (1992) J Mol Biol , vol.226 , pp. 277-280
    • Harrison, S.C.1    Strong, R.K.2    Schlesinger, S.3
  • 96
    • 0030051091 scopus 로고    scopus 로고
    • Differential processing of sindbis virus glycoprotein PE2 in cultured vertebrate and arthropod cells
    • Heidner HW, Knott TA, Johnston RE. Differential processing of sindbis virus glycoprotein PE2 in cultured vertebrate and arthropod cells. J Virol 1996;70:2069-2073.
    • (1996) J Virol , vol.70 , pp. 2069-2073
    • Heidner, H.W.1    Knott, T.A.2    Johnston, R.E.3
  • 97
    • 0028196638 scopus 로고
    • Lethality of PE2 incorporation into Sindbis virus can be suppressed by second-site mutations in E3 and E2
    • Heidner HW, McKnight KL, Davis NL, et al. Lethality of PE2 incorporation into Sindbis virus can be suppressed by second-site mutations in E3 and E2. J Virol 1994;68:2683-2692.
    • (1994) J Virol , vol.68 , pp. 2683-2692
    • Heidner, H.W.1    McKnight, K.L.2    Davis, N.L.3
  • 98
    • 0034984146 scopus 로고    scopus 로고
    • An amino acid substitution in the coding region of the E2 glycoprotein adapts Ross River Virus to utilize heparan sulfate as an attachment moiety
    • Heil ML, Albee A, Strauss JH, et al. An amino acid substitution in the coding region of the E2 glycoprotein adapts Ross River Virus to utilize heparan sulfate as an attachment moiety. J Virol 2001;7:6303-6309.
    • (2001) J Virol , vol.7 , pp. 6303-6309
    • Heil, M.L.1    Albee, A.2    Strauss, J.H.3
  • 99
    • 0018853517 scopus 로고
    • On the entry of Semliki Forest virus into BHK-21 cells
    • Helenius A, Kartenbeck J, Simons K, et al. On the entry of Semliki Forest virus into BHK-21 cells. J Cell Biol 1980;84:404-420.
    • (1980) J Cell Biol , vol.84 , pp. 404-420
    • Helenius, A.1    Kartenbeck, J.2    Simons, K.3
  • 100
    • 0020042010 scopus 로고
    • Inhibition of Semliki Forest virus penetration by lysosomotropic weak bases
    • Helenius A, Marsh M, White J. Inhibition of Semliki Forest virus penetration by lysosomotropic weak bases. J Gen Virol 1982;58:47-61.
    • (1982) J Gen Virol , vol.58 , pp. 47-61
    • Helenius, A.1    Marsh, M.2    White, J.3
  • 101
    • 0035132288 scopus 로고    scopus 로고
    • Exposure to low pH is not required for penetration of mosquito cells by Sindbis virus
    • Hernandez R, Luo TC, Brown DT. Exposure to low pH is not required for penetration of mosquito cells by Sindbis virus. J Virol 2001;75:2010-2013.
    • (2001) J Virol , vol.75 , pp. 2010-2013
    • Hernandez, R.1    Luo, T.C.2    Brown, D.T.3
  • 102
    • 0028971187 scopus 로고
    • Evolution of the Sindbis virus subgenomic mRNA promoter in cultured cells
    • Hertz JM, Huang HV. Evolution of the Sindbis virus subgenomic mRNA promoter in cultured cells. J Virol 1995;69:7768-7774.
    • (1995) J Virol , vol.69 , pp. 7768-7774
    • Hertz, J.M.1    Huang, H.V.2
  • 103
    • 0028971188 scopus 로고
    • Host-dependent evolution of the Sindbis virus promoter for subgenomic mRNA synthesis
    • Hertz JM, Huang HV. Host-dependent evolution of the Sindbis virus promoter for subgenomic mRNA synthesis. J Virol 1995;69:7775-7781.
    • (1995) J Virol , vol.69 , pp. 7775-7781
    • Hertz, J.M.1    Huang, H.V.2
  • 104
    • 0028065160 scopus 로고
    • Assembly of rubella virus structural proteins into virus-like particles in transfected cells
    • Hobman TC, Lundstrom ML, Mauracher CA, et al. Assembly of rubella virus structural proteins into virus-like particles in transfected cells. Virology 1994;202:574-585.
    • (1994) Virology , vol.202 , pp. 574-585
    • Hobman, T.C.1    Lundstrom, M.L.2    Mauracher, C.A.3
  • 105
    • 0029064295 scopus 로고
    • Targeting of a heterodimeric membrane protein complex to the Golgi: rubella virus E2 glycoprotein contains a transmembrane Golgi retention signal
    • Hobman TC, Woodward L, Farquhar MG. Targeting of a heterodimeric membrane protein complex to the Golgi: rubella virus E2 glycoprotein contains a transmembrane Golgi retention signal. Mol Biol Cell 1995;6:7-20.
    • (1995) Mol Biol Cell , vol.6 , pp. 7-20
    • Hobman, T.C.1    Woodward, L.2    Farquhar, M.G.3
  • 106
    • 0021419204 scopus 로고
    • Envelope proteins of Semliki Forest virus synthesized in Xenopus oocytes are transported to the cell surface
    • Huth A, Rapoport TA, Kaariainen L. Envelope proteins of Semliki Forest virus synthesized in Xenopus oocytes are transported to the cell surface. EMBO J 1984;3:767-771.
    • (1984) EMBO J , vol.3 , pp. 767-771
    • Huth, A.1    Rapoport, T.A.2    Kaariainen, L.3
  • 107
    • 79952221290 scopus 로고    scopus 로고
    • The Rubella virus capsid is an anti-apoptotic protein that attenuates the pore-forming ability of Bax
    • Ilkow CS, Goping IS, Hobman TC. The Rubella virus capsid is an anti-apoptotic protein that attenuates the pore-forming ability of Bax. PLoS Pathog 2011;7:e1001291.
    • (2011) PLoS Pathog , vol.7 , pp. e1001291
    • Ilkow, C.S.1    Goping, I.S.2    Hobman, T.C.3
  • 108
    • 0028985015 scopus 로고
    • A pseudo-revertant of a Sindbis virus 6K protein mutant, which corrects for aberrant particle formation, contains two new mutations that map to the ectodomain of the E2 glycoprotein
    • Ivanova L, Lustig S, Schlesinger MJ. A pseudo-revertant of a Sindbis virus 6K protein mutant, which corrects for aberrant particle formation, contains two new mutations that map to the ectodomain of the E2 glycoprotein. Virology 1995;206:1027-1034.
    • (1995) Virology , vol.206 , pp. 1027-1034
    • Ivanova, L.1    Lustig, S.2    Schlesinger, M.J.3
  • 109
    • 0033033071 scopus 로고    scopus 로고
    • Characterization of a Chinese hamster ovary cell line developed by retroviral insertional mutagenesis that is resistant to Sindbis virus infection
    • Jan JT, Byrnes AP, Griffin DE. Characterization of a Chinese hamster ovary cell line developed by retroviral insertional mutagenesis that is resistant to Sindbis virus infection. J Virol 1999;73:4919-4924.
    • (1999) J Virol , vol.73 , pp. 4919-4924
    • Jan, J.T.1    Byrnes, A.P.2    Griffin, D.E.3
  • 110
    • 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, et al. Interactions of the cytoplasmic domain of Sindbis virus E2 with nucleocapsid cores promote alphavirus budding. J Virol 2012;86:2585-2599.
    • (2012) J Virol , vol.86 , pp. 2585-2599
    • Jose, J.1    Przybyla, L.2    Edwards, T.J.3
  • 111
    • 70349199877 scopus 로고    scopus 로고
    • A structural and functional perspective of alphavirus replication and assembly
    • Jose J, Snyder JE, Kuhn RJ. A structural and functional perspective of alphavirus replication and assembly. Future Microbiol 2009;4:837-856.
    • (2009) Future Microbiol , vol.4 , pp. 837-856
    • Jose, J.1    Snyder, J.E.2    Kuhn, R.J.3
  • 112
    • 0021770887 scopus 로고
    • Primary structural comparison of RNA-dependent polymerases from plant, animal and bacterial viruses
    • Kamer G, Argos P. Primary structural comparison of RNA-dependent polymerases from plant, animal and bacterial viruses. Nucleic Acids Res 1984;12:7269-7282.
    • (1984) Nucleic Acids Res , vol.12 , pp. 7269-7282
    • Kamer, G.1    Argos, P.2
  • 113
    • 0030741052 scopus 로고    scopus 로고
    • Characterization of the infection of Aedes albopictus cell clones by Sindbis virus
    • Karpf AR, Blake JM, Brown DT. Characterization of the infection of Aedes albopictus cell clones by Sindbis virus. Virus Res 1997;50:1-13.
    • (1997) Virus Res , vol.50 , pp. 1-13
    • Karpf, A.R.1    Blake, J.M.2    Brown, D.T.3
  • 114
    • 0023768226 scopus 로고
    • Low pH-induced conformational change of rubella virus envelope proteins
    • Katow S, Sugiura A. Low pH-induced conformational change of rubella virus envelope proteins. J Gen Virol 1988;69(Pt 11):2797-2807.
    • (1988) J Gen Virol , vol.69 , Issue.PT 11 , pp. 2797-2807
    • Katow, S.1    Sugiura, A.2
  • 115
    • 0033649526 scopus 로고    scopus 로고
    • Specific roles for lipids in virus fusion and exit. Examples from the alphaviruses
    • Kielian M, Chatterjee PK, Gibbons DL, et al. Specific roles for lipids in virus fusion and exit. Examples from the alphaviruses. Subcell Biochem 2000;34:409-455.
    • (2000) Subcell Biochem , vol.34 , pp. 409-455
    • Kielian, M.1    Chatterjee, P.K.2    Gibbons, D.L.3
  • 116
    • 31344432402 scopus 로고    scopus 로고
    • Virus membrane-fusion proteins: more than one way to make a hairpin
    • Kielian M, Rey FA. Virus membrane-fusion proteins: more than one way to make a hairpin. Nat Rev Microbiol 2006;4:67-76.
    • (2006) Nat Rev Microbiol , vol.4 , pp. 67-76
    • Kielian, M.1    Rey, F.A.2
  • 117
    • 0021177971 scopus 로고
    • Role of cholesterol in fusion of Semliki Forest virus with membranes
    • Kielian MC, Helenius A. Role of cholesterol in fusion of Semliki Forest virus with membranes. J Virol 1984;52:281-283.
    • (1984) J Virol , vol.52 , pp. 281-283
    • Kielian, M.C.1    Helenius, A.2
  • 118
    • 79961205984 scopus 로고    scopus 로고
    • Conservation of a packaging signal and the viral genome RNA packaging mechanism in alphavirus evolution
    • Kim DY, Firth AE, Atasheva S, et al. Conservation of a packaging signal and the viral genome RNA packaging mechanism in alphavirus evolution. J Virol 2011;85:8022-8036.
    • (2011) J Virol , vol.85 , pp. 8022-8036
    • Kim, D.Y.1    Firth, A.E.2    Atasheva, S.3
  • 119
    • 0242363253 scopus 로고    scopus 로고
    • DC-SIGN and L-SIGN can act as attachment receptors for alphaviruses and distinguish between mosquito cell- and mammalian cell-derived viruses
    • Klimstra WB, Nangle EM, Smith MS, et al. DC-SIGN and L-SIGN can act as attachment receptors for alphaviruses and distinguish between mosquito cell- and mammalian cell-derived viruses. J Virol 2003;77:12022-12032.
    • (2003) J Virol , vol.77 , pp. 12022-12032
    • Klimstra, W.B.1    Nangle, E.M.2    Smith, M.S.3
  • 120
    • 0031869503 scopus 로고    scopus 로고
    • Adaptation of Sindbis virus to BHK cells selects for use of heparan sulfate as an attachment receptor
    • Klimstra WB, Ryman KD, Johnston RE. Adaptation of Sindbis virus to BHK cells selects for use of heparan sulfate as an attachment receptor. J Virol 1998;72:7357-7366.
    • (1998) J Virol , vol.72 , pp. 7357-7366
    • Klimstra, W.B.1    Ryman, K.D.2    Johnston, R.E.3
  • 121
    • 0024523663 scopus 로고
    • Intracellular transport and processing of Sindbis virus glycoproteins
    • Knipfer KW, Brown DT. Intracellular transport and processing of Sindbis virus glycoproteins. Virology 1989;170:117-122.
    • (1989) Virology , vol.170 , pp. 117-122
    • Knipfer, K.W.1    Brown, D.T.2
  • 122
    • 0027504136 scopus 로고
    • Evolution and taxonomy of positive-strand RNA viruses: implications of comparative analysis of amino acid sequences
    • Koonin EV, Dolja VV. Evolution and taxonomy of positive-strand RNA viruses: implications of comparative analysis of amino acid sequences. Crit Rev Biochem Mol Biol 1993;28:375-430.
    • (1993) Crit Rev Biochem Mol Biol , vol.28 , pp. 375-430
    • Koonin, E.V.1    Dolja, V.V.2
  • 123
    • 80052503042 scopus 로고    scopus 로고
    • The structure of barmah forest virus as revealed by cryo-electron microscopy at a 6-angstrom resolution has detailed transmembrane protein architecture and interactions
    • Kostyuchenko VA, Jakana J, Liu X, et al. The structure of barmah forest virus as revealed by cryo-electron microscopy at a 6-angstrom resolution has detailed transmembrane protein architecture and interactions. J Virol 2011;85:9327-9333.
    • (2011) J Virol , vol.85 , pp. 9327-9333
    • Kostyuchenko, V.A.1    Jakana, J.2    Liu, X.3
  • 124
    • 0025255251 scopus 로고
    • Mutagenesis of the 3' nontranslated region of Sindbis virus RNA
    • Kuhn RJ, Hong Z, Strauss JH. Mutagenesis of the 3' nontranslated region of Sindbis virus RNA. J Virol 1990;64:1465-1476.
    • (1990) J Virol , vol.64 , pp. 1465-1476
    • Kuhn, R.J.1    Hong, Z.2    Strauss, J.H.3
  • 125
    • 18344387519 scopus 로고    scopus 로고
    • Structure of dengue virus: implications for flavivirus organization, maturation, and fusion
    • Kuhn RJ, Zhang W, Rossmann MG, et al. Structure of dengue virus: implications for flavivirus organization, maturation, and fusion. Cell 2002;108:717-725.
    • (2002) Cell , vol.108 , pp. 717-725
    • Kuhn, R.J.1    Zhang, W.2    Rossmann, M.G.3
  • 126
    • 0032866181 scopus 로고    scopus 로고
    • Intracellular distribution of rubella virus nonstructural protein P150
    • Kujala P, Ahola T, Ehsani N, et al. Intracellular distribution of rubella virus nonstructural protein P150. J Virol 1999;73:7805-7811.
    • (1999) J Virol , vol.73 , pp. 7805-7811
    • Kujala, P.1    Ahola, T.2    Ehsani, N.3
  • 127
    • 0035082679 scopus 로고    scopus 로고
    • Biogenesis of the Semliki Forest virus RNA replication complex
    • Kujala P, Ikaheimonen A, Ehsani N, et al. Biogenesis of the Semliki Forest virus RNA replication complex. J Virol 2001;75:3873-3884.
    • (2001) J Virol , vol.75 , pp. 3873-3884
    • Kujala, P.1    Ikaheimonen, A.2    Ehsani, N.3
  • 128
    • 0029956554 scopus 로고    scopus 로고
    • The effects of palmitoylation on membrane association of Semliki forest virus RNA capping enzyme
    • Laakkonen P, Ahola T, Kaariainen L. The effects of palmitoylation on membrane association of Semliki forest virus RNA capping enzyme. J Biol Chem 1996;271:28567-28571.
    • (1996) J Biol Chem , vol.271 , pp. 28567-28571
    • Laakkonen, P.1    Ahola, T.2    Kaariainen, L.3
  • 129
    • 0028173041 scopus 로고
    • Expression of Semliki Forest virus nsP1-specific methyltransferase in insect cells and in Escherichia coli
    • Laakkonen P, Hyvonen M, Peranen J, et al. Expression of Semliki Forest virus nsP1-specific methyltransferase in insect cells and in Escherichia coli. J Virol 1994;68:7418-7425.
    • (1994) J Virol , vol.68 , pp. 7418-7425
    • Laakkonen, P.1    Hyvonen, M.2    Peranen, J.3
  • 130
    • 0034536098 scopus 로고    scopus 로고
    • Membrane binding mechanism of an RNA virus-capping enzyme
    • Lampio A, Kilpelainen I, Pesonen S, et al. Membrane binding mechanism of an RNA virus-capping enzyme. J Biol Chem 2000;275:37853-37859.
    • (2000) J Biol Chem , vol.275 , pp. 37853-37859
    • Lampio, A.1    Kilpelainen, I.2    Pesonen, S.3
  • 131
    • 0028142238 scopus 로고
    • Deletion and duplication mutations in the C-terminal nonconserved region of Sindbis virus nsP3: effects on phosphorylation and on virus replication in vertebrate and invertebrate cells
    • Lastarza MW, Grakoui A, Rice CM. Deletion and duplication mutations in the C-terminal nonconserved region of Sindbis virus nsP3: effects on phosphorylation and on virus replication in vertebrate and invertebrate cells. Virology 1994;202:224-232.
    • (1994) Virology , vol.202 , pp. 224-232
    • Lastarza, M.W.1    Grakoui, A.2    Rice, C.M.3
  • 132
    • 0027935902 scopus 로고
    • Genetic analysis of the nsP3 region of Sindbis virus: evidence for roles in minus-strand and subgenomic RNA synthesis
    • LaStarza MW, Lemm JA, Rice CM. Genetic analysis of the nsP3 region of Sindbis virus: evidence for roles in minus-strand and subgenomic RNA synthesis. J Virol 1994;68:5781-5791.
    • (1994) J Virol , vol.68 , pp. 5781-5791
    • LaStarza, M.W.1    Lemm, J.A.2    Rice, C.M.3
  • 133
    • 0037302253 scopus 로고    scopus 로고
    • Phosphorylation of rubella virus capsid regulates its RNA binding activity and virus replication
    • Law LM, Everitt JC, Beatch MD, et al. Phosphorylation of rubella virus capsid regulates its RNA binding activity and virus replication. J Virol 2003;77:1764-1771.
    • (2003) J Virol , vol.77 , pp. 1764-1771
    • Law, L.M.1    Everitt, J.C.2    Beatch, M.D.3
  • 134
    • 0030585119 scopus 로고    scopus 로고
    • Identification of a protein binding site on the surface of the alphavirus nucleocapsid and its implication in virus assembly
    • Lee S, Owen KE, Choi HK, et al. Identification of a protein binding site on the surface of the alphavirus nucleocapsid and its implication in virus assembly. Structure 1996;4:531-541.
    • (1996) Structure , vol.4 , pp. 531-541
    • Lee, S.1    Owen, K.E.2    Choi, H.K.3
  • 135
    • 0031878237 scopus 로고    scopus 로고
    • Template-dependent initiation of Sindbis virus RNA replication in vitro
    • Lemm JA, Bergqvist A, Read CM, et al. Template-dependent initiation of Sindbis virus RNA replication in vitro. J Virol 1998;72:6546-6553.
    • (1998) J Virol , vol.72 , pp. 6546-6553
    • Lemm, J.A.1    Bergqvist, A.2    Read, C.M.3
  • 136
    • 0027463085 scopus 로고
    • Assembly of functional Sindbis virus RNA replication complexes: requirement for coexpression of P123 and P34
    • Lemm JA, Rice CM. Assembly of functional Sindbis virus RNA replication complexes: requirement for coexpression of P123 and P34. J Virol 1993;67:1905-1915.
    • (1993) J Virol , vol.67 , pp. 1905-1915
    • Lemm, J.A.1    Rice, C.M.2
  • 137
    • 0027475009 scopus 로고
    • Roles of nonstructural polyproteins and cleavage products in regulating Sindbis virus RNA replication and transcription
    • Lemm JA, Rice CM. Roles of nonstructural polyproteins and cleavage products in regulating Sindbis virus RNA replication and transcription. J Virol 1993;67:1916-1926.
    • (1993) J Virol , vol.67 , pp. 1916-1926
    • Lemm, J.A.1    Rice, C.M.2
  • 138
    • 0028221438 scopus 로고
    • Polypeptide requirements for assembly of functional Sindbis virus replication complexes: a model for the temporal regulation of minus- and plus-strand RNA synthesis
    • Lemm JA, Rumenapf T, Strauss EG, et al. Polypeptide requirements for assembly of functional Sindbis virus replication complexes: a model for the temporal regulation of minus- and plus-strand RNA synthesis. EMBO J 1994;13:2925-2934.
    • (1994) EMBO J , vol.13 , pp. 2925-2934
    • Lemm, J.A.1    Rumenapf, T.2    Strauss, E.G.3
  • 139
    • 0035815282 scopus 로고    scopus 로고
    • The fusion glycoprotein shell of Semliki Forest virus: an icosahedral assembly primed for fusogenic activation at endosomal pH
    • Lescar J, Roussel A, Wein MW, et al. The fusion glycoprotein shell of Semliki Forest virus: an icosahedral assembly primed for fusogenic activation at endosomal pH. Cell 2001;105:137-148.
    • (2001) Cell , vol.105 , pp. 137-148
    • Lescar, J.1    Roussel, A.2    Wein, M.W.3
  • 140
    • 0027532285 scopus 로고
    • Conversion of lytic to persistent alphavirus infection by the bcl-2 cellular oncogene
    • Levine B, Huang Q, Isaacs JT, et al. Conversion of lytic to persistent alphavirus infection by the bcl-2 cellular oncogene. Nature 1993;361:739-742.
    • (1993) Nature , vol.361 , pp. 739-742
    • Levine, B.1    Huang, Q.2    Isaacs, J.T.3
  • 141
    • 0023369822 scopus 로고
    • Engineered defective interfering RNAs of Sindbis virus express bacterial chloramphenicol acetyltransferase in avian cells
    • Levis R, Huang H, Schlesinger S. Engineered defective interfering RNAs of Sindbis virus express bacterial chloramphenicol acetyltransferase in avian cells. Proc Natl Acad Sci U S A 1987;84:4811-4815.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 4811-4815
    • Levis, R.1    Huang, H.2    Schlesinger, S.3
  • 142
    • 0022498060 scopus 로고
    • Deletion mapping of Sindbis virus DI RNAs derived from cDNAs defines the sequences essential for replication and packaging
    • Levis R, Weiss BG, Tsiang M, et al. Deletion mapping of Sindbis virus DI RNAs derived from cDNAs defines the sequences essential for replication and packaging. Cell 1986;44:137-145.
    • (1986) Cell , vol.44 , pp. 137-145
    • Levis, R.1    Weiss, B.G.2    Tsiang, M.3
  • 143
    • 0030050637 scopus 로고    scopus 로고
    • Alphavirus-induced apoptosis in mouse brains correlates with neurovirulence
    • Lewis J, Wesselingh SL, Griffin DE, et al. Alphavirus-induced apoptosis in mouse brains correlates with neurovirulence. J Virol 1996;70:1828-1835.
    • (1996) J Virol , vol.70 , pp. 1828-1835
    • Lewis, J.1    Wesselingh, S.L.2    Griffin, D.E.3
  • 144
    • 0025045885 scopus 로고
    • Phosphorylation of Sindbis virus nsP3 in vivo and in vitro
    • Li G, LaStarza MW, Hardy WR, et al. Phosphorylation of Sindbis virus nsP3 in vivo and in vitro. Virology 1990;179:416-427.
    • (1990) Virology , vol.179 , pp. 416-427
    • Li, G.1    LaStarza, M.W.2    Hardy, W.R.3
  • 145
    • 0024556696 scopus 로고
    • Mutagenesis of the in-frame opal termination codon preceding nsP4 of Sindbis virus: Studies of translational readthrough and its effect on virus replication
    • Li G, Rice CM. Mutagenesis of the in-frame opal termination codon preceding nsP4 of Sindbis virus: Studies of translational readthrough and its effect on virus replication. J Virol 1989;63:1326-1337.
    • (1989) J Virol , vol.63 , pp. 1326-1337
    • Li, G.1    Rice, C.M.2
  • 146
    • 78649891889 scopus 로고    scopus 로고
    • Structural changes of envelope proteins during alphavirus fusion
    • Li L, Jose J, Xiang Y, et al. Structural changes of envelope proteins during alphavirus fusion. Nature 2010;468:705-708.
    • (2010) Nature , vol.468 , pp. 705-708
    • Li, L.1    Jose, J.2    Xiang, Y.3
  • 147
    • 26444506252 scopus 로고    scopus 로고
    • Domain III from class II fusion proteins functions as a dominant-negative inhibitor of virus membrane fusion
    • Liao M, Kielian M. Domain III from class II fusion proteins functions as a dominant-negative inhibitor of virus membrane fusion. J Cell Biol 2005;171:111-120.
    • (2005) J Cell Biol , vol.171 , pp. 111-120
    • Liao, M.1    Kielian, M.2
  • 148
    • 14744304517 scopus 로고
    • A new generation of animal cell expression vectors based on the Semliki Forest virus replicon
    • Liljeström P, Garoff H. A new generation of animal cell expression vectors based on the Semliki Forest virus replicon. Biotechnology 1991;9:1356-1361.
    • (1991) Biotechnology , vol.9 , pp. 1356-1361
    • Liljeström, P.1    Garoff, H.2
  • 149
    • 0025957563 scopus 로고
    • Internally located cleavable signal sequences direct the formation of Semliki Forest virus membrane proteins from a polyprotein precursor
    • Liljeström P, Garoff H. Internally located cleavable signal sequences direct the formation of Semliki Forest virus membrane proteins from a polyprotein precursor. J Virol 1991;65:147-154.
    • (1991) J Virol , vol.65 , pp. 147-154
    • Liljeström, P.1    Garoff, H.2
  • 150
    • 0025912001 scopus 로고
    • In vitro mutagenesis of a full-length cDNA clone of Semliki Forest virus: the small 6000-molecular-weight membrane protein modulates virus release
    • Liljeström P, Lusa S, Huylebroeck D, et al. In vitro mutagenesis of a full-length cDNA clone of Semliki Forest virus: the small 6000-molecular-weight membrane protein modulates virus release. J Virol 1991;65:4107-4113.
    • (1991) J Virol , vol.65 , pp. 4107-4113
    • Liljeström, P.1    Lusa, S.2    Huylebroeck, D.3
  • 151
    • 0345731281 scopus 로고    scopus 로고
    • Sindbis virus nucleocapsid assembly: RNA folding promotes capsid protein dimerization
    • Linger BR, Kunovska L, Kuhn RJ, et al. Sindbis virus nucleocapsid assembly: RNA folding promotes capsid protein dimerization. RNA 2004;10:128-138.
    • (2004) RNA , vol.10 , pp. 128-138
    • Linger, B.R.1    Kunovska, L.2    Kuhn, R.J.3
  • 152
    • 0035043272 scopus 로고    scopus 로고
    • Arbovirus of marine mammals: a new alphavirus isolated from the elephant seal louse, Lepidophthirus macrorhini
    • Linn ML, Gardner J, Warrilow D, et al. Arbovirus of marine mammals: a new alphavirus isolated from the elephant seal louse, Lepidophthirus macrorhini. J Virol 2001;75:4103-4109.
    • (2001) J Virol , vol.75 , pp. 4103-4109
    • Linn, M.L.1    Gardner, J.2    Warrilow, D.3
  • 153
    • 70350327357 scopus 로고    scopus 로고
    • E1 mutants identify a critical region in the trimer interface of the Semliki forest virus fusion protein
    • Liu CY, Kielian M. E1 mutants identify a critical region in the trimer interface of the Semliki forest virus fusion protein. J Virol 2009;83:11298-11306.
    • (2009) J Virol , vol.83 , pp. 11298-11306
    • Liu, C.Y.1    Kielian, M.2
  • 154
    • 0027452740 scopus 로고
    • Transient translocation of the cytoplasmic (Endo) domain of a type I membrane glycoprotein into cellular membranes
    • Liu N, Brown DT. Transient translocation of the cytoplasmic (Endo) domain of a type I membrane glycoprotein into cellular membranes. J Cell Biol 1993;120:877-883.
    • (1993) J Cell Biol , vol.120 , pp. 877-883
    • Liu, N.1    Brown, D.T.2
  • 155
    • 0029887660 scopus 로고    scopus 로고
    • Identification of domains in rubella virus genomic RNA and capsid protein necessary for specific interaction
    • Liu Z, Yang D, Qiu Z, et al. Identification of domains in rubella virus genomic RNA and capsid protein necessary for specific interaction. J Virol 1996;70:2184-2190.
    • (1996) J Virol , vol.70 , pp. 2184-2190
    • Liu, Z.1    Yang, D.2    Qiu, Z.3
  • 156
    • 0025219313 scopus 로고
    • Fusion function of the Semliki Forest virus spike is activated by proteolytic cleavage of the envelope glycoprotein precursor p62
    • Lobigs M, Garoff H. Fusion function of the Semliki Forest virus spike is activated by proteolytic cleavage of the envelope glycoprotein precursor p62. J Virol 1990;64:1233-1240.
    • (1990) J Virol , vol.64 , pp. 1233-1240
    • Lobigs, M.1    Garoff, H.2
  • 157
    • 0025012156 scopus 로고
    • Spike protein oligomerization control of Semliki Forest virus fusion
    • Lobigs M, Wahlberg JM, Garoff H. Spike protein oligomerization control of Semliki Forest virus fusion. J Virol 1990;64:5214-5218.
    • (1990) J Virol , vol.64 , pp. 5214-5218
    • Lobigs, M.1    Wahlberg, J.M.2    Garoff, H.3
  • 158
    • 0025003156 scopus 로고
    • Function of Semliki Forest virus E3 peptide in virus assembly: replacement of E3 with an artificial signal peptide abolishes spike heterodimerization and surface expression of E1
    • Lobigs M, Zhao HX, Garoff H. Function of Semliki Forest virus E3 peptide in virus assembly: replacement of E3 with an artificial signal peptide abolishes spike heterodimerization and surface expression of E1. J Virol 1990;64:4346-4355.
    • (1990) J Virol , vol.64 , pp. 4346-4355
    • Lobigs, M.1    Zhao, H.X.2    Garoff, H.3
  • 159
    • 0028936836 scopus 로고
    • The 6-kilodalton membrane protein of Semliki Forest virus is involved in the budding process
    • Loewy A, Smyth J, von Bonsdorff CH, et al. The 6-kilodalton membrane protein of Semliki Forest virus is involved in the budding process. J Virol 1995;69:469-475.
    • (1995) J Virol , vol.69 , pp. 469-475
    • Loewy, A.1    Smyth, J.2    von Bonsdorff, C.H.3
  • 160
    • 0032930413 scopus 로고    scopus 로고
    • The cholesterol requirement for sindbis virus entry and exit and characterization of a spike protein region involved in cholesterol dependence
    • Lu YE, Cassese T, Kielian M. The cholesterol requirement for sindbis virus entry and exit and characterization of a spike protein region involved in cholesterol dependence. J Virol 1999;73:4272-4278.
    • (1999) J Virol , vol.73 , pp. 4272-4278
    • Lu, Y.E.1    Cassese, T.2    Kielian, M.3
  • 161
    • 0028222202 scopus 로고
    • A 55-kDa protein induced in Aedes albopictus (mosquito) cells by antiviral protein
    • Luo T, Brown DT. A 55-kDa protein induced in Aedes albopictus (mosquito) cells by antiviral protein. Virology 1994;200:200-206.
    • (1994) Virology , vol.200 , pp. 200-206
    • Luo, T.1    Brown, D.T.2
  • 162
    • 0027185474 scopus 로고
    • Purification and characterization of a Sindbis virus-induced peptide which stimulates its own production and blocks virus RNA synthesis
    • Luo T, Brown DT. Purification and characterization of a Sindbis virus-induced peptide which stimulates its own production and blocks virus RNA synthesis. Virology 1993;194:44-49.
    • (1993) Virology , vol.194 , pp. 44-49
    • Luo, T.1    Brown, D.T.2
  • 163
    • 0026323917 scopus 로고
    • Fate of the 6K membrane protein of Semliki Forest virus during virus assembly
    • Lusa S, Garoff H, Liljestrom P. Fate of the 6K membrane protein of Semliki Forest virus during virus assembly. Virology 1991;185:843-846.
    • (1991) Virology , vol.185 , pp. 843-846
    • Lusa, S.1    Garoff, H.2    Liljestrom, P.3
  • 164
    • 67449102614 scopus 로고    scopus 로고
    • The crystal structures of Chikungunya and Venezuelan equine encephalitis virus nsP3 macro domains define a conserved adenosine binding pocket
    • Malet H, Coutard B, Jamal S, et al. The crystal structures of Chikungunya and Venezuelan equine encephalitis virus nsP3 macro domains define a conserved adenosine binding pocket. J Virol 2009;83:6534-6545.
    • (2009) J Virol , vol.83 , pp. 6534-6545
    • Malet, H.1    Coutard, B.2    Jamal, S.3
  • 165
    • 0027420702 scopus 로고
    • Cholesterol is required in the exit pathway of Semliki Forest virus
    • Marquardt MT, Phalen T, Kielian M. Cholesterol is required in the exit pathway of Semliki Forest virus. J Cell Biol 1993;123:57-65.
    • (1993) J Cell Biol , vol.123 , pp. 57-65
    • Marquardt, M.T.1    Phalen, T.2    Kielian, M.3
  • 166
    • 0025958399 scopus 로고
    • Efficient in vitro translation and processing of the rubella virus structural proteins in the presence of microsomes
    • Marr LD, Sanchez A, Frey TK. Efficient in vitro translation and processing of the rubella virus structural proteins in the presence of microsomes. Virology 1991;180:400-405.
    • (1991) Virology , vol.180 , pp. 400-405
    • Marr, L.D.1    Sanchez, A.2    Frey, T.K.3
  • 167
    • 0020724144 scopus 로고
    • Penetration of Semliki Forest virus from acidic prelysosomal vacuoles
    • Marsh M, Bolzau E, Helenius A. Penetration of Semliki Forest virus from acidic prelysosomal vacuoles. Cell 1983;32:931-940.
    • (1983) Cell , vol.32 , pp. 931-940
    • Marsh, M.1    Bolzau, E.2    Helenius, A.3
  • 168
    • 0020015596 scopus 로고
    • Classification and nomenclature of viruses
    • Matthews REF. Classification and nomenclature of viruses. Intervirology 1982;17:1-199.
    • (1982) Intervirology , vol.17 , pp. 1-199
    • Matthews, R.E.F.1
  • 169
    • 0023275581 scopus 로고
    • Processing of the Semliki Forest virus structural polyprotein: role of the capsid protease
    • Melancon P, Garoff H. Processing of the Semliki Forest virus structural polyprotein: role of the capsid protease. J Virol 1987;61:1301-1309.
    • (1987) J Virol , vol.61 , pp. 1301-1309
    • Melancon, P.1    Garoff, H.2
  • 170
    • 0347928844 scopus 로고    scopus 로고
    • Alphavirus 6K proteins form ion channels
    • Melton JV, Ewart GD, Weir RC, et al. Alphavirus 6K proteins form ion channels. J Biol Chem 2002;277:46923-46931.
    • (2002) J Biol Chem , vol.277 , pp. 46923-46931
    • Melton, J.V.1    Ewart, G.D.2    Weir, R.C.3
  • 171
    • 0025129428 scopus 로고
    • Oligomers of the cytoplasmic domain of the p62/E2 membrane protein of Semliki Forest virus bind to the nucleocapsid in vitro
    • Metsikkö K, Garoff H. Oligomers of the cytoplasmic domain of the p62/E2 membrane protein of Semliki Forest virus bind to the nucleocapsid in vitro. J Virol 1990;64:4678-4683.
    • (1990) J Virol , vol.64 , pp. 4678-4683
    • Metsikkö, K.1    Garoff, H.2
  • 172
    • 0026655252 scopus 로고
    • Conformational alteration of Sindbis virion glycoproteins induced by heat, reducing agents, or low pH
    • Meyer WJ, Gidwitz S, Ayers VK, et al. Conformational alteration of Sindbis virion glycoproteins induced by heat, reducing agents, or low pH. J Virol 1992;66:3504-3513.
    • (1992) J Virol , vol.66 , pp. 3504-3513
    • Meyer, W.J.1    Gidwitz, S.2    Ayers, V.K.3
  • 173
    • 0027219587 scopus 로고
    • Structural rearrangement of infecting Sindbis virions at the cell surface: mapping of newly accessible epitopes
    • Meyer WJ, Johnston RE. Structural rearrangement of infecting Sindbis virions at the cell surface: mapping of newly accessible epitopes. J Virol 1993;67:5117-5125.
    • (1993) J Virol , vol.67 , pp. 5117-5125
    • Meyer, W.J.1    Johnston, R.E.2
  • 174
    • 0024328925 scopus 로고
    • Association of the Sindbis virus RNA methytransferase activity with the nonstructural protein nsP1
    • Mi S, Durbin R, Huang HV, et al. Association of the Sindbis virus RNA methytransferase activity with the nonstructural protein nsP1. Virology 1989;170:385-391.
    • (1989) Virology , vol.170 , pp. 385-391
    • Mi, S.1    Durbin, R.2    Huang, H.V.3
  • 175
    • 0025851067 scopus 로고
    • Expression of Sindbis virus nsP1 and methyltransferase activity in Escherichia coli
    • Mi S, Stollar V. Expression of Sindbis virus nsP1 and methyltransferase activity in Escherichia coli. Virology 1991;184:423-427.
    • (1991) Virology , vol.184 , pp. 423-427
    • Mi, S.1    Stollar, V.2
  • 176
    • 0026664169 scopus 로고
    • Morphogenesis of Sindbis virus in three subclones of Aedes albopictus (mosquito) cells
    • Miller ML, Brown DT. Morphogenesis of Sindbis virus in three subclones of Aedes albopictus (mosquito) cells. J Virol 1992;66:4180-4190.
    • (1992) J Virol , vol.66 , pp. 4180-4190
    • Miller, M.L.1    Brown, D.T.2
  • 177
    • 0029112141 scopus 로고
    • Sphingolipids activate membrane fusion of Semliki Forest virus in a stereospecific manner
    • Moesby L, Corver J, Erukulla RK, et al. Sphingolipids activate membrane fusion of Semliki Forest virus in a stereospecific manner. Biochemistry 1995;34:10319-10324.
    • (1995) Biochemistry , vol.34 , pp. 10319-10324
    • Moesby, L.1    Corver, J.2    Erukulla, R.K.3
  • 178
    • 34648836389 scopus 로고    scopus 로고
    • Nuclear import and export of Venezuelan equine encephalitis virus nonstructural protein 2
    • Montgomery SA, Johnston RE. Nuclear import and export of Venezuelan equine encephalitis virus nonstructural protein 2. J Virol 2007;81:10268-10279.
    • (2007) J Virol , vol.81 , pp. 10268-10279
    • Montgomery, S.A.1    Johnston, R.E.2
  • 179
    • 0036838225 scopus 로고    scopus 로고
    • In vitro-assembled alphavirus core-like particles maintain a structure similar to that of nucleocapsid cores in mature virus
    • Mukhopadhyay S, Chipman PR, Hong EM, et al. In vitro-assembled alphavirus core-like particles maintain a structure similar to that of nucleocapsid cores in mature virus. J Virol 2002;76:11128-11132.
    • (2002) J Virol , vol.76 , pp. 11128-11132
    • Mukhopadhyay, S.1    Chipman, P.R.2    Hong, E.M.3
  • 180
    • 33644815756 scopus 로고    scopus 로고
    • Mapping the structure and function of the E1 and E2 glycoproteins in alphaviruses
    • Mukhopadhyay S, Zhang W, Gabler S, et al. Mapping the structure and function of the E1 and E2 glycoproteins in alphaviruses. Structure 2006;14:63-73.
    • (2006) Structure , vol.14 , pp. 63-73
    • Mukhopadhyay, S.1    Zhang, W.2    Gabler, S.3
  • 181
    • 0029953199 scopus 로고    scopus 로고
    • Assembly of the Sindbis virus spike protein complex
    • Mulvey M, Brown DT. Assembly of the Sindbis virus spike protein complex. Virology 1996;219:125-132.
    • (1996) Virology , vol.219 , pp. 125-132
    • Mulvey, M.1    Brown, D.T.2
  • 182
    • 0028120912 scopus 로고
    • Formation and rearrangement of disulfide bonds during maturation of the Sindbis virus E1 glycoprotein
    • Mulvey M, Brown DT. Formation and rearrangement of disulfide bonds during maturation of the Sindbis virus E1 glycoprotein. J Virol 1994;68:805-812.
    • (1994) J Virol , vol.68 , pp. 805-812
    • Mulvey, M.1    Brown, D.T.2
  • 183
    • 0003000404 scopus 로고
    • Togavirus morphology and morphogenesis
    • Schlesinger RW, ed, New York: Academic Press
    • Murphy FA. Togavirus morphology and morphogenesis. In: Schlesinger RW, ed. The Togaviruses. New York: Academic Press; 1980:241-316.
    • (1980) The Togaviruses. , pp. 241-316
    • Murphy, F.A.1
  • 184
    • 0025930801 scopus 로고
    • Specific binding of host cell proteins to the 3'-terminal stem-loop structure of rubella virus negative-strand RNA
    • Nakhasi HL, Cao X-Q, Rouault TA, et al. Specific binding of host cell proteins to the 3'-terminal stem-loop structure of rubella virus negative-strand RNA. J Virol 1991;65:5961-5967.
    • (1991) J Virol , vol.65 , pp. 5961-5967
    • Nakhasi, H.L.1    Cao, X.-Q.2    Rouault, T.A.3
  • 185
    • 0025352499 scopus 로고
    • Specific high-affinity binding of host cell proteins to the 3' region of rubella virus RNA
    • Nakhasi HL, Rouault TA, Haile DJ, et al. Specific high-affinity binding of host cell proteins to the 3' region of rubella virus RNA. New Biol 1990;2:255-264.
    • (1990) New Biol , vol.2 , pp. 255-264
    • Nakhasi, H.L.1    Rouault, T.A.2    Haile, D.J.3
  • 186
    • 81755182978 scopus 로고    scopus 로고
    • SH3 domain-mediated recruitment of host cell amphiphysins by alphavirus nsP3 promotes viral RNA replication
    • Neuvonen M, Kazlauskas A, Martikainen M, et al. SH3 domain-mediated recruitment of host cell amphiphysins by alphavirus nsP3 promotes viral RNA replication. PLoS Pathog 2011;7:e1002383.
    • (2011) PLoS Pathog , vol.7 , pp. e1002383
    • Neuvonen, M.1    Kazlauskas, A.2    Martikainen, M.3
  • 187
    • 55849116755 scopus 로고    scopus 로고
    • Effect of host cell lipid metabolism on alphavirus replication, virion morphogenesis, and infectivity
    • Ng CG, Coppens I, Govindarajan D, et al. Effect of host cell lipid metabolism on alphavirus replication, virion morphogenesis, and infectivity. Proc Natl Acad Sci U S A 2008;105:16326-16331.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 16326-16331
    • Ng, C.G.1    Coppens, I.2    Govindarajan, D.3
  • 188
    • 0025047017 scopus 로고
    • Defined mutations in the 5' nontranslated sequence of Sindbis virus RNA
    • Niesters HGM, Strauss JH. Defined mutations in the 5' nontranslated sequence of Sindbis virus RNA. J Virol 1990;64:4162-4168.
    • (1990) J Virol , vol.64 , pp. 4162-4168
    • Niesters, H.G.M.1    Strauss, J.H.2
  • 189
    • 0025212683 scopus 로고
    • Mutagenesis of the conserved 51-nucleotide region of Sindbis virus
    • Niesters HGM, Strauss JH. Mutagenesis of the conserved 51-nucleotide region of Sindbis virus. J Virol 1990;64:1639-1647.
    • (1990) J Virol , vol.64 , pp. 1639-1647
    • Niesters, H.G.M.1    Strauss, J.H.2
  • 190
    • 0028199032 scopus 로고
    • Membrane fusion of Semliki Forest virus requires sphingolipids in the target membrane
    • Nieva JL, Bron R, Corver J, et al. Membrane fusion of Semliki Forest virus requires sphingolipids in the target membrane. EMBO J 1994;13:2797-2804.
    • (1994) EMBO J , vol.13 , pp. 2797-2804
    • Nieva, J.L.1    Bron, R.2    Corver, J.3
  • 191
    • 0021268016 scopus 로고
    • The gene order for Rubella virus structural proteins is NH2-C-E2-E1-COOH
    • Oker-Blom C. The gene order for Rubella virus structural proteins is NH2-C-E2-E1-COOH. J Virol 1984;51:354-358.
    • (1984) J Virol , vol.51 , pp. 354-358
    • Oker-Blom, C.1
  • 192
    • 0021360118 scopus 로고
    • Rubella virus 40S genome RNA specifies a 24S subgenomic mRNA that codes for a precursor to structural proteins
    • Oker-Blom C, Ulmanen I, Kääriäinen L, et al. Rubella virus 40S genome RNA specifies a 24S subgenomic mRNA that codes for a precursor to structural proteins. J Virol 1984;49:403-408.
    • (1984) J Virol , vol.49 , pp. 403-408
    • Oker-Blom, C.1    Ulmanen, I.2    Kääriäinen, L.3
  • 193
    • 0029876709 scopus 로고    scopus 로고
    • Identification of a region in the Sindbis virus nucleocapsid protein that is involved in specificity of RNA encapsidation
    • Owen KE, Kuhn RJ. Identification of a region in the Sindbis virus nucleocapsid protein that is involved in specificity of RNA encapsidation. J Virol 1996;70:2757-2763.
    • (1996) J Virol , vol.70 , pp. 2757-2763
    • Owen, K.E.1    Kuhn, R.J.2
  • 194
    • 0027255003 scopus 로고
    • Multiple binding sites for cellular proteins in the 3' end of Sindbis alphavirus minue-sense RNA
    • Pardigon N, Lenches E, Strauss JH. Multiple binding sites for cellular proteins in the 3' end of Sindbis alphavirus minue-sense RNA. J Virol 1993;67:5003-5011.
    • (1993) J Virol , vol.67 , pp. 5003-5011
    • Pardigon, N.1    Lenches, E.2    Strauss, J.H.3
  • 195
    • 0026584175 scopus 로고
    • Cellular proteins bind to the 3' end of Sindbis virus minus strand RNA
    • Pardigon N, Strauss JH. Cellular proteins bind to the 3' end of Sindbis virus minus strand RNA. J Virol 1992;66:1007-1015.
    • (1992) J Virol , vol.66 , pp. 1007-1015
    • Pardigon, N.1    Strauss, J.H.2
  • 196
    • 0030060397 scopus 로고    scopus 로고
    • Mosquito homolog of the La autoantigen binds to Sindbis virus RNA
    • Pardigon N, Strauss JH. Mosquito homolog of the La autoantigen binds to Sindbis virus RNA. J Virol 1996;70:1173-1181.
    • (1996) J Virol , vol.70 , pp. 1173-1181
    • Pardigon, N.1    Strauss, J.H.2
  • 197
    • 0037213901 scopus 로고    scopus 로고
    • Structure of isolated nucleocapsids from venezuelan equine encephalitis virus and implications for assembly and disassembly of enveloped virus
    • Paredes A, Alwell-Warda K, Weaver SC, et al. Structure of isolated nucleocapsids from venezuelan equine encephalitis virus and implications for assembly and disassembly of enveloped virus. J Virol 2003;77:659-664.
    • (2003) J Virol , vol.77 , pp. 659-664
    • Paredes, A.1    Alwell-Warda, K.2    Weaver, S.C.3
  • 198
    • 0034855251 scopus 로고    scopus 로고
    • Venezuelan equine encephalomyelitis virus structure and its divergence from Old World alphaviruses
    • Paredes A, Alwell-Warda K, Weaver SC, et al. Venezuelan equine encephalomyelitis virus structure and its divergence from Old World alphaviruses. J Virol 2001;75:9532-9537.
    • (2001) J Virol , vol.75 , pp. 9532-9537
    • Paredes, A.1    Alwell-Warda, K.2    Weaver, S.C.3
  • 199
    • 0027359884 scopus 로고
    • Three-dimensional structure of a membrane-containing virus
    • Paredes AM, Brown DT, Rothnagel R, et al. Three-dimensional structure of a membrane-containing virus. Proc Natl Acad Sci U S A 1993;90:9095-9099.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 9095-9099
    • Paredes, A.M.1    Brown, D.T.2    Rothnagel, R.3
  • 200
    • 2942733550 scopus 로고    scopus 로고
    • Conformational changes in Sindbis virions resulting from exposure to low pH and interactions with cells suggest that cell penetration may occur at the cell surface in the absence of membrane fusion
    • Paredes AM, Ferreira D, Horton M, et al. Conformational changes in Sindbis virions resulting from exposure to low pH and interactions with cells suggest that cell penetration may occur at the cell surface in the absence of membrane fusion. Virology 2004;324:373-386.
    • (2004) Virology , vol.324 , pp. 373-386
    • Paredes, A.M.1    Ferreira, D.2    Horton, M.3
  • 201
    • 0031930769 scopus 로고    scopus 로고
    • Structural localization of the E3 glycoprotein in attenuated Sindbis virus mutants
    • Paredes AM, Heidner H, Thuman-Commike P, et al. Structural localization of the E3 glycoprotein in attenuated Sindbis virus mutants. J Virol 1998;72:1534-1541.
    • (1998) J Virol , vol.72 , pp. 1534-1541
    • Paredes, A.M.1    Heidner, H.2    Thuman-Commike, P.3
  • 202
    • 0026538052 scopus 로고
    • The mass of the Sindbis virus nucleocapsid suggests it has T = 4 icosahedral symmetry
    • Paredes AM, Simon ML, Brown DT. The mass of the Sindbis virus nucleocapsid suggests it has T = 4 icosahedral symmetry. Virology 1993;187:329-332.
    • (1993) Virology , vol.187 , pp. 329-332
    • Paredes, A.M.1    Simon, M.L.2    Brown, D.T.3
  • 203
    • 0026102072 scopus 로고
    • Biogenesis of type I cytopathic vacuoles in Semliki Forest virus-infected BHK cells
    • Peranen J, Kaariainen L. Biogenesis of type I cytopathic vacuoles in Semliki Forest virus-infected BHK cells. J Virol 1991;65:1623-1627.
    • (1991) J Virol , vol.65 , pp. 1623-1627
    • Peranen, J.1    Kaariainen, L.2
  • 204
    • 0029060940 scopus 로고
    • The alphavirus replicase protein nsP1 is membrane-associated and has affinity to endocytic organelles
    • Peranen J, Laakkonen P, Hyvonen M, et al. The alphavirus replicase protein nsP1 is membrane-associated and has affinity to endocytic organelles. Virology 1995;208:610-620.
    • (1995) Virology , vol.208 , pp. 610-620
    • Peranen, J.1    Laakkonen, P.2    Hyvonen, M.3
  • 205
    • 0023731901 scopus 로고
    • Semliki Forest virus-specific non-structural protein nsP3 is a phosphoprotein
    • Peränen J, Takkinen K, Kalkkinen N, et al. Semliki Forest virus-specific non-structural protein nsP3 is a phosphoprotein. J Gen Virol 1988;69:2165-2178.
    • (1988) J Gen Virol , vol.69 , pp. 2165-2178
    • Peränen, J.1    Takkinen, K.2    Kalkkinen, N.3
  • 206
    • 19944373420 scopus 로고    scopus 로고
    • Noncytopathic replication of Venezuelan equine encephalitis virus and eastern equine encephalitis virus replicons in Mammalian cells
    • Petrakova O, Volkova E, Gorchakov R, et al. Noncytopathic replication of Venezuelan equine encephalitis virus and eastern equine encephalitis virus replicons in Mammalian cells. J Virol 2005;79:7597-7608.
    • (2005) J Virol , vol.79 , pp. 7597-7608
    • Petrakova, O.1    Volkova, E.2    Gorchakov, R.3
  • 207
    • 0026022952 scopus 로고
    • Cholesterol is required for infection by Semliki Forest virus
    • Phalen T, Kielian M. Cholesterol is required for infection by Semliki Forest virus. J Cell Biol 1991;112:615-623.
    • (1991) J Cell Biol , vol.112 , pp. 615-623
    • Phalen, T.1    Kielian, M.2
  • 208
    • 0035815301 scopus 로고    scopus 로고
    • Locations of carbohydrate sites on alphavirus glycoproteins show that E1 forms an icosahedral scaffold
    • Pletnev SV, Zhang W, Mukhopadhyay S, et al. Locations of carbohydrate sites on alphavirus glycoproteins show that E1 forms an icosahedral scaffold. Cell 2001;105:127-136.
    • (2001) Cell , vol.105 , pp. 127-136
    • Pletnev, S.V.1    Zhang, W.2    Mukhopadhyay, S.3
  • 209
    • 0039098910 scopus 로고
    • Comparative and historical aspects of the Togaviridae and Flaviviridae
    • Schlesinger S, Schlesinger MJ, eds, New York: Plenum Press
    • Porterfield JS. Comparative and historical aspects of the Togaviridae and Flaviviridae. In: Schlesinger S, Schlesinger MJ, eds. The Togaviridae and Flaviviridae. New York: Plenum Press; 1986:1-19.
    • (1986) The Togaviridae and Flaviviridae. , pp. 1-19
    • Porterfield, J.S.1
  • 210
    • 0034795886 scopus 로고    scopus 로고
    • Evolutionary relationships and systematics of the alphaviruses
    • Powers AM, Brault AC, Shirako Y, et al. Evolutionary relationships and systematics of the alphaviruses. J Virol 2001;75:10118-10131.
    • (2001) J Virol , vol.75 , pp. 10118-10131
    • Powers, A.M.1    Brault, A.C.2    Shirako, Y.3
  • 211
    • 0024600786 scopus 로고
    • The proteolytic cleavage of PE2 to envelope glycoprotein E2 is not strictly required for the maturation of Sindbis virus
    • Presley JF, Brown DT. The proteolytic cleavage of PE2 to envelope glycoprotein E2 is not strictly required for the maturation of Sindbis virus. J Virol 1989;63:1975-1980.
    • (1989) J Virol , vol.63 , pp. 1975-1980
    • Presley, J.F.1    Brown, D.T.2
  • 212
    • 0025968097 scopus 로고
    • Proteolytic processing of the Sindbis virus membrane protein precursor PE2 is nonessential for growth in vertebrate cells but is required for efficient growth in invertebrate cells
    • Presley JF, Polo JM, Johnston RE, et al. Proteolytic processing of the Sindbis virus membrane protein precursor PE2 is nonessential for growth in vertebrate cells but is required for efficient growth in invertebrate cells. J Virol 1991;65:1905-1909.
    • (1991) J Virol , vol.65 , pp. 1905-1909
    • Presley, J.F.1    Polo, J.M.2    Johnston, R.E.3
  • 213
    • 0030918382 scopus 로고    scopus 로고
    • Genomic sequence of the RA27/3 vaccine strain of rubella virus
    • Pugachev KV, Abernathy ES, Frey TK. Genomic sequence of the RA27/3 vaccine strain of rubella virus. Arch Virol 1997;142:1165-1180.
    • (1997) Arch Virol , vol.142 , pp. 1165-1180
    • Pugachev, K.V.1    Abernathy, E.S.2    Frey, T.K.3
  • 214
    • 0031060534 scopus 로고    scopus 로고
    • Improvement of the specific infectivity of the rubella virus (RUB) infectious clone: determinants of cytopathogenicity induced by RUB map to the nonstructural proteins
    • Pugachev KV, Abernathy ES, Frey TK. Improvement of the specific infectivity of the rubella virus (RUB) infectious clone: determinants of cytopathogenicity induced by RUB map to the nonstructural proteins. J Virol 1997;71:562-568.
    • (1997) J Virol , vol.71 , pp. 562-568
    • Pugachev, K.V.1    Abernathy, E.S.2    Frey, T.K.3
  • 215
    • 0031583842 scopus 로고    scopus 로고
    • Replicon-helper systems from attenuated Venezuelan equine encephalitis virus: expression of heterologous genes in vitro and immunization against heterologous pathogens in vivo
    • Pushko P, Parker M, Ludwig GV, et al. Replicon-helper systems from attenuated Venezuelan equine encephalitis virus: expression of heterologous genes in vitro and immunization against heterologous pathogens in vivo. Virology 1997;239:389-401.
    • (1997) Virology , vol.239 , pp. 389-401
    • Pushko, P.1    Parker, M.2    Ludwig, G.V.3
  • 216
    • 66149140928 scopus 로고    scopus 로고
    • Role of conserved histidine residues in the low-pH dependence of the Semliki Forest virus fusion protein
    • Qin ZL, Zheng Y, Kielian M. Role of conserved histidine residues in the low-pH dependence of the Semliki Forest virus fusion protein. J Virol 2009;83:4670-4677.
    • (2009) J Virol , vol.83 , pp. 4670-4677
    • Qin, Z.L.1    Zheng, Y.2    Kielian, M.3
  • 217
    • 0025784087 scopus 로고
    • Analysis of Sindbis virus promoter recognition in vivo, using novel vectors with two subgenomic mRNA promoters
    • Raju R, Huang HV. Analysis of Sindbis virus promoter recognition in vivo, using novel vectors with two subgenomic mRNA promoters. J Virol 1991;65:2501-2510.
    • (1991) J Virol , vol.65 , pp. 2501-2510
    • Raju, R.1    Huang, H.V.2
  • 218
    • 0029014434 scopus 로고
    • The envelope glycoprotein from tick-borne encephalitis virus at 2 Å resolution
    • Rey FA, Heinz FX, Mandl C, et al. The envelope glycoprotein from tick-borne encephalitis virus at 2 Å resolution. Nature (London) 1995;375:291-298.
    • (1995) Nature (London) , vol.375 , pp. 291-298
    • Rey, F.A.1    Heinz, F.X.2    Mandl, C.3
  • 219
    • 0020085011 scopus 로고
    • Association of Sindbis virion glycoproteins and their precursors
    • Rice CM, Strauss JH. Association of Sindbis virion glycoproteins and their precursors. J Mol Biol 1982;154:325-348.
    • (1982) J Mol Biol , vol.154 , pp. 325-348
    • Rice, C.M.1    Strauss, J.H.2
  • 220
    • 0038212351 scopus 로고
    • Nucleotide sequence of the 26S mRNA of Sindbis virus and deduced sequence of the encoded virus structural proteins
    • Rice CM, Strauss JH. Nucleotide sequence of the 26S mRNA of Sindbis virus and deduced sequence of the encoded virus structural proteins. Proc Natl Acad Sci U S A 1981;78:2062-2066.
    • (1981) Proc Natl Acad Sci U S A , vol.78 , pp. 2062-2066
    • Rice, C.M.1    Strauss, J.H.2
  • 221
    • 0030011522 scopus 로고    scopus 로고
    • Functional significance of the nuclear-targeting and NTP-binding motifs of Semliki Forest virus nonstructural protein nsP2
    • Rikkonen M. Functional significance of the nuclear-targeting and NTP-binding motifs of Semliki Forest virus nonstructural protein nsP2. Virology 1996;218:352-361.
    • (1996) Virology , vol.218 , pp. 352-361
    • Rikkonen, M.1
  • 222
    • 0028018141 scopus 로고
    • ATPase and GTPase activities associated with Semliki Forest virus nonstructural protein nsP2
    • Rikkonen M, Peranen J, Kaariainen L. ATPase and GTPase activities associated with Semliki Forest virus nonstructural protein nsP2. J Virol 1994;68:5804-5810.
    • (1994) J Virol , vol.68 , pp. 5804-5810
    • Rikkonen, M.1    Peranen, J.2    Kaariainen, L.3
  • 223
    • 0026650834 scopus 로고
    • Nuclear and nucleolar targeting signals of Semliki Forest virus nonstructural protein nsP2
    • Rikkonen M, Peranen J, Kaariainen L. Nuclear and nucleolar targeting signals of Semliki Forest virus nonstructural protein nsP2. Virology 1992;189:462-473.
    • (1992) Virology , vol.189 , pp. 462-473
    • Rikkonen, M.1    Peranen, J.2    Kaariainen, L.3
  • 224
    • 0028251545 scopus 로고
    • Nuclear targeting of Semliki Forest virus nsP2
    • Rikkonen M, Peranen J, Kaariainen L. Nuclear targeting of Semliki Forest virus nsP2. Arch Virol 1994;9:369-377.
    • (1994) Arch Virol , vol.9 , pp. 369-377
    • Rikkonen, M.1    Peranen, J.2    Kaariainen, L.3
  • 225
    • 0042062406 scopus 로고    scopus 로고
    • Structural maturation of rubella virus in the Golgi complex
    • Risco C, Carrascosa JL, Frey TK. Structural maturation of rubella virus in the Golgi complex. Virology 2003;312:261-269.
    • (2003) Virology , vol.312 , pp. 261-269
    • Risco, C.1    Carrascosa, J.L.2    Frey, T.K.3
  • 226
    • 0022896244 scopus 로고
    • Alteration of the cytoplasmic domain of the membrane-spanning glycoprotein p62 of Semliki Forest virus does not affect its polar distribution in established lines of Madin-Darby canine kidney cells
    • Roman LM, Garoff H. Alteration of the cytoplasmic domain of the membrane-spanning glycoprotein p62 of Semliki Forest virus does not affect its polar distribution in established lines of Madin-Darby canine kidney cells. J Cell Biol 1986;103:2607-2618.
    • (1986) J Cell Biol , vol.103 , pp. 2607-2618
    • Roman, L.M.1    Garoff, H.2
  • 227
    • 80051881398 scopus 로고    scopus 로고
    • Natural resistance-associated macrophage protein is a cellular receptor for sindbis virus in both insect and mammalian hosts
    • Rose PP, Hanna SL, Spiridigliozzi A, et al. Natural resistance-associated macrophage protein is a cellular receptor for sindbis virus in both insect and mammalian hosts. Cell Host Microbe 2011;10:97-104.
    • (2011) Cell Host Microbe , vol.10 , pp. 97-104
    • Rose, P.P.1    Hanna, S.L.2    Spiridigliozzi, A.3
  • 228
    • 0028246506 scopus 로고
    • Mutations in the nsP1 coding sequence of Sindbis virus which restrict viral replication in secondary cultures of chick embryo fibroblasts prepared from aged primary cultures
    • Rosenblum CI, Scheidel LM, Stollar V. Mutations in the nsP1 coding sequence of Sindbis virus which restrict viral replication in secondary cultures of chick embryo fibroblasts prepared from aged primary cultures. Virology 1994;198:100-108.
    • (1994) Virology , vol.198 , pp. 100-108
    • Rosenblum, C.I.1    Scheidel, L.M.2    Stollar, V.3
  • 229
    • 33644799064 scopus 로고    scopus 로고
    • Structure and interactions at the viral surface of the envelope protein E1 of Semliki Forest virus
    • Roussel A, Lescar J, Vaney M-C, et al. Structure and interactions at the viral surface of the envelope protein E1 of Semliki Forest virus. Structure 2006;14:75-86.
    • (2006) Structure , vol.14 , pp. 75-86
    • Roussel, A.1    Lescar, J.2    Vaney, M.-C.3
  • 230
    • 58549095054 scopus 로고    scopus 로고
    • Characterization of purified Sindbis virus nsP4 RNA-dependent RNA polymerase activity in vitro
    • Rubach JK, Wasik BR, Rupp JC, et al. Characterization of purified Sindbis virus nsP4 RNA-dependent RNA polymerase activity in vitro. Virology 2009;384:201-208.
    • (2009) Virology , vol.384 , pp. 201-208
    • Rubach, J.K.1    Wasik, B.R.2    Rupp, J.C.3
  • 231
    • 0028877868 scopus 로고
    • Aura alphavirus subgenomic RNA is packaged into virions of two sizes
    • Rümenapf T, Brown DT, Strauss EG, et al. Aura alphavirus subgenomic RNA is packaged into virions of two sizes. J Virol 1995;69:1741-1746.
    • (1995) J Virol , vol.69 , pp. 1741-1746
    • Rümenapf, T.1    Brown, D.T.2    Strauss, E.G.3
  • 232
    • 0028181666 scopus 로고
    • Subgenomic mRNA of Aura alphavirus is packaged into virions
    • Rümenapf T, Strauss EG, Strauss JH. Subgenomic mRNA of Aura alphavirus is packaged into virions. J Virol 1994;68:56-62.
    • (1994) J Virol , vol.68 , pp. 56-62
    • Rümenapf, T.1    Strauss, E.G.2    Strauss, J.H.3
  • 233
    • 0024565079 scopus 로고
    • Sindbis virus mutations which coordinately affect glycoprotein processing, penetration and virulence in mice
    • Russell DL, Dalrymple JM, Johnston RE. Sindbis virus mutations which coordinately affect glycoprotein processing, penetration and virulence in mice. J Virol 1989;63:1619-1629.
    • (1989) J Virol , vol.63 , pp. 1619-1629
    • Russell, D.L.1    Dalrymple, J.M.2    Johnston, R.E.3
  • 234
    • 77955773469 scopus 로고    scopus 로고
    • Structural basis for substrate specificity of alphavirus nsP2 proteases
    • Russo AT, Malmstrom RD, White MA, et al. Structural basis for substrate specificity of alphavirus nsP2 proteases. J Mol Graph Model 2010;29:46-53.
    • (2010) J Mol Graph Model , vol.29 , pp. 46-53
    • Russo, A.T.1    Malmstrom, R.D.2    White, M.A.3
  • 235
    • 33748304343 scopus 로고    scopus 로고
    • The crystal structure of the Venezuelan equine encephalitis alphavirus nsP2 protease
    • Russo AT, White MA, Watowich SJ. The crystal structure of the Venezuelan equine encephalitis alphavirus nsP2 protease. Structure 2006;14:1449-1458.
    • (2006) Structure , vol.14 , pp. 1449-1458
    • Russo, A.T.1    White, M.A.2    Watowich, S.J.3
  • 236
    • 13744249590 scopus 로고    scopus 로고
    • Sindbis virus translation is inhibited by a PKR/RNase L-independent effector induced by alpha/beta interferon priming of dendritic cells
    • Ryman KD, Meier KC, Nangle EM, et al. Sindbis virus translation is inhibited by a PKR/RNase L-independent effector induced by alpha/beta interferon priming of dendritic cells. J Virol 2005;79:1487-1499.
    • (2005) J Virol , vol.79 , pp. 1487-1499
    • Ryman, K.D.1    Meier, K.C.2    Nangle, E.M.3
  • 237
    • 0026567676 scopus 로고
    • Membrane fusion process of Semliki Forest virus II: Cleavage-dependent reorganization of the spike protein complex controls virus entry
    • Salminen A, Wahlberg JM, Lobigs M, et al. Membrane fusion process of Semliki Forest virus II: Cleavage-dependent reorganization of the spike protein complex controls virus entry. J Cell Biol 1992;116:349-357.
    • (1992) J Cell Biol , vol.116 , pp. 349-357
    • Salminen, A.1    Wahlberg, J.M.2    Lobigs, M.3
  • 238
    • 0033658703 scopus 로고    scopus 로고
    • Sulfhydryl involvement in fusion mechanisms
    • Hilderson H, Fuller S, eds, New York: Kluwer Academic/Plenum Publishers
    • Sanders DA. Sulfhydryl involvement in fusion mechanisms. In: Hilderson H, Fuller S, eds. Fusion of Biological Membranes and Related Problems. New York: Kluwer Academic/Plenum Publishers; 2000:483-514.
    • (2000) Fusion of Biological Membranes and Related Problems. , pp. 483-514
    • Sanders, D.A.1
  • 239
    • 0034904097 scopus 로고    scopus 로고
    • Sindbis virus variant with a deletion in the 6K gene shows defects in glycoprotein processing and trafficking: lack of complementation by a wild-type 6K gene in trans
    • Sanz MA, Carrasco L. Sindbis virus variant with a deletion in the 6K gene shows defects in glycoprotein processing and trafficking: lack of complementation by a wild-type 6K gene in trans. J Virol 2001;75:7778-7784.
    • (2001) J Virol , vol.75 , pp. 7778-7784
    • Sanz, M.A.1    Carrasco, L.2
  • 240
    • 0025141312 scopus 로고
    • Temperature sensitive shut-off of alphavirus minus strand RNA synthesis maps to a nonstructural protein, nsP4
    • Sawicki D, Barkhimer DB, Sawicki SG, et al. Temperature sensitive shut-off of alphavirus minus strand RNA synthesis maps to a nonstructural protein, nsP4. Virology 1990;174:43-52.
    • (1990) Virology , vol.174 , pp. 43-52
    • Sawicki, D.1    Barkhimer, D.B.2    Sawicki, S.G.3
  • 241
    • 33645972603 scopus 로고    scopus 로고
    • Role for nsP2 proteins in the cessation of alphavirus minus-strand synthesis by host cells
    • Sawicki DL, Perri S, Polo JM, et al. Role for nsP2 proteins in the cessation of alphavirus minus-strand synthesis by host cells. J Virol 2006;80:360-371.
    • (2006) J Virol , vol.80 , pp. 360-371
    • Sawicki, D.L.1    Perri, S.2    Polo, J.M.3
  • 242
    • 0027166774 scopus 로고
    • A second nonstructural protein functions in the regulation of alphavirus negative-strand RNA synthesis
    • Sawicki DL, Sawicki SG. A second nonstructural protein functions in the regulation of alphavirus negative-strand RNA synthesis. J Virol 1993;67:3605-3610.
    • (1993) J Virol , vol.67 , pp. 3605-3610
    • Sawicki, D.L.1    Sawicki, S.G.2
  • 243
    • 0019637489 scopus 로고
    • A Sindbis virus mutant temperature-sensitive in the regulation of minus-strand RNA synthesis
    • Sawicki SG, Sawicki DL, Kääriäinen L, et al. A Sindbis virus mutant temperature-sensitive in the regulation of minus-strand RNA synthesis. Virology 1981;115:161-172.
    • (1981) Virology , vol.115 , pp. 161-172
    • Sawicki, S.G.1    Sawicki, D.L.2    Kääriäinen, L.3
  • 244
    • 0001420627 scopus 로고
    • Formation and assembly of alphavirus glycoproteins
    • Schlesinger S, Schlesinger MJ, eds, New York: Plenum Publishing Corp.
    • Schlesinger MJ, Schlesinger S. Formation and assembly of alphavirus glycoproteins. In: Schlesinger S, Schlesinger MJ, eds. The Togaviridae and Flaviviridae. New York: Plenum Publishing Corp.; 1986:121-148.
    • (1986) The Togaviridae and Flaviviridae. , pp. 121-148
    • Schlesinger, M.J.1    Schlesinger, S.2
  • 245
    • 0034567812 scopus 로고    scopus 로고
    • Alphavirus expression vectors
    • Schlesinger S. Alphavirus expression vectors. Adv Virus Res 2000;55:565-577.
    • (2000) Adv Virus Res , vol.55 , pp. 565-577
    • Schlesinger, S.1
  • 246
    • 0017371658 scopus 로고
    • Immediate glycosylation of Sindbis virus membrane proteins
    • Sefton BM. Immediate glycosylation of Sindbis virus membrane proteins. Cell 1977;10:659-668.
    • (1977) Cell , vol.10 , pp. 659-668
    • Sefton, B.M.1
  • 247
    • 0035123812 scopus 로고    scopus 로고
    • Ross River virus glycoprotein-pseudotyped retroviruses and stable cell lines for their production
    • Sharkey CM, North CL, Kuhn RJ, et al. Ross River virus glycoprotein-pseudotyped retroviruses and stable cell lines for their production. J Virol 2001;75:2653-2659.
    • (2001) J Virol , vol.75 , pp. 2653-2659
    • Sharkey, C.M.1    North, C.L.2    Kuhn, R.J.3
  • 248
    • 77956829733 scopus 로고    scopus 로고
    • Structure of the recombinant alphavirus Western equine encephalitis virus revealed by cryoelectron microscopy
    • Sherman MB, Weaver SC. Structure of the recombinant alphavirus Western equine encephalitis virus revealed by cryoelectron microscopy. J Virol 2010;84:9775-9782.
    • (2010) J Virol , vol.84 , pp. 9775-9782
    • Sherman, M.B.1    Weaver, S.C.2
  • 249
    • 0037289824 scopus 로고    scopus 로고
    • Modification of the 5' terminus of Sindbis virus genomic RNA allows nsP4 RNA polymerases with nonaromatic amino acids at the N terminus to function in RNA replication
    • Shirako Y, Strauss EG, Strauss JH. Modification of the 5' terminus of Sindbis virus genomic RNA allows nsP4 RNA polymerases with nonaromatic amino acids at the N terminus to function in RNA replication. J Virol 2003;77:2301-2309.
    • (2003) J Virol , vol.77 , pp. 2301-2309
    • Shirako, Y.1    Strauss, E.G.2    Strauss, J.H.3
  • 250
    • 0034633849 scopus 로고    scopus 로고
    • Suppressor mutations that allow Sindbis virus RNA polymerase to function with nonaromatic amino acids at the N-terminus: evidence for interaction between nsP1 and nsP4 in minus-strand RNA synthesis
    • Shirako Y, Strauss EG, Strauss JH. Suppressor mutations that allow Sindbis virus RNA polymerase to function with nonaromatic amino acids at the N-terminus: evidence for interaction between nsP1 and nsP4 in minus-strand RNA synthesis. Virology 2000;276:148-160.
    • (2000) Virology , vol.276 , pp. 148-160
    • Shirako, Y.1    Strauss, E.G.2    Strauss, J.H.3
  • 251
    • 0027979138 scopus 로고
    • Regulation of Sindbis virus RNA replication: uncleaved P123 and nsP4 function in minus-strand RNA synthesis, whereas cleaved products from P123 are required for efficient plus-strand RNA synthesis
    • Shirako Y, Strauss JH. Regulation of Sindbis virus RNA replication: uncleaved P123 and nsP4 function in minus-strand RNA synthesis, whereas cleaved products from P123 are required for efficient plus-strand RNA synthesis. J Virol 1994;68:1874-1885.
    • (1994) J Virol , vol.68 , pp. 1874-1885
    • Shirako, Y.1    Strauss, J.H.2
  • 252
    • 0015527746 scopus 로고
    • Replication of Sindbis virus. I. Relative size and genetic content of 26S and 49S RNA
    • Simmons DT, Strauss JH. Replication of Sindbis virus. I. Relative size and genetic content of 26S and 49S RNA. J Mol Biol 1972;71:599-613.
    • (1972) J Mol Biol , vol.71 , pp. 599-613
    • Simmons, D.T.1    Strauss, J.H.2
  • 253
    • 0031937629 scopus 로고    scopus 로고
    • Requirement for an aromatic amino acid or histidine at the N terminus of Sindbis virus RNA polymerase
    • Shirako Y, Strauss JH. Requirement for an aromatic amino acid or histidine at the N terminus of Sindbis virus RNA polymerase. J Virol 1998;72:2310-2315.
    • (1998) J Virol , vol.72 , pp. 2310-2315
    • Shirako, Y.1    Strauss, J.H.2
  • 254
    • 0026490846 scopus 로고
    • Role of ribosomes in Semliki Forest virus nucleocapsid uncoating
    • Singh I, Helenius A. Role of ribosomes in Semliki Forest virus nucleocapsid uncoating. J Virol 1992;66:7049-7058.
    • (1992) J Virol , vol.66 , pp. 7049-7058
    • Singh, I.1    Helenius, A.2
  • 255
    • 0030977374 scopus 로고    scopus 로고
    • Multiple mechanisms for the inhibition of entry and uncoating of superinfecting Semliki Forest virus
    • Singh IR, Suomalainen M, Varadarajan S, et al. Multiple mechanisms for the inhibition of entry and uncoating of superinfecting Semliki Forest virus. Virology 1997;231:59-71.
    • (1997) Virology , vol.231 , pp. 59-71
    • Singh, I.R.1    Suomalainen, M.2    Varadarajan, S.3
  • 256
    • 0028606112 scopus 로고
    • Identification of calreticulin as a rubella virus RNA binding protein
    • Singh NK, Atreya CD, Nakhasi HL. Identification of calreticulin as a rubella virus RNA binding protein. Proc Natl Acad Sci U S A 1994;91:12770-12774.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 12770-12774
    • Singh, N.K.1    Atreya, C.D.2    Nakhasi, H.L.3
  • 257
    • 0030585135 scopus 로고    scopus 로고
    • Aromatic interactions define the binding of the alphavirus spike to its nucleocapsid
    • Skoging U, Vihinen M, Nilsson L, et al. Aromatic interactions define the binding of the alphavirus spike to its nucleocapsid. Structure 1996;4:519-529.
    • (1996) Structure , vol.4 , pp. 519-529
    • Skoging, U.1    Vihinen, M.2    Nilsson, L.3
  • 258
    • 0036784563 scopus 로고    scopus 로고
    • Adaptation of alphaviruses to heparan sulfate: Interaction of Sindbis and Semliki Forest virus with liposomes containing lipid-conjugated heparin
    • Smit JM, Waarts B-L, Kimata K, et al. Adaptation of alphaviruses to heparan sulfate: Interaction of Sindbis and Semliki Forest virus with liposomes containing lipid-conjugated heparin. J Virol 2002;76:10128-10137.
    • (2002) J Virol , vol.76 , pp. 10128-10137
    • Smit, J.M.1    Waarts, B.-L.2    Kimata, K.3
  • 259
    • 79958150853 scopus 로고    scopus 로고
    • Rescue of infectious particles from preassembled alphavirus nucleocapsid cores
    • Snyder JE, Azizgolshani O, Wu B, et al. Rescue of infectious particles from preassembled alphavirus nucleocapsid cores. J Virol 2011;85:5773-5781.
    • (2011) J Virol , vol.85 , pp. 5773-5781
    • Snyder, J.E.1    Azizgolshani, O.2    Wu, B.3
  • 260
    • 0017661273 scopus 로고
    • Transient association of Semliki Forest virus capsid protein with ribosomes
    • Söderlund H, Ulmanen I. Transient association of Semliki Forest virus capsid protein with ribosomes. J Virol 1977;24:907-909.
    • (1977) J Virol , vol.24 , pp. 907-909
    • Söderlund, H.1    Ulmanen, I.2
  • 261
    • 77956312311 scopus 로고    scopus 로고
    • Sindbis virus usurps the cellular HuR protein to stabilize its transcripts and promote productive infections in mammalian and mosquito cells
    • Sokoloski KJ, Dickson AM, Chaskey EL, et al. Sindbis virus usurps the cellular HuR protein to stabilize its transcripts and promote productive infections in mammalian and mosquito cells. Cell Host Microbe 2010;8:196-207.
    • (2010) Cell Host Microbe , vol.8 , pp. 196-207
    • Sokoloski, K.J.1    Dickson, A.M.2    Chaskey, E.L.3
  • 262
    • 77957957373 scopus 로고    scopus 로고
    • Structural evidence of glycoprotein assembly in cellular membrane compartments prior to Alphavirus budding
    • Soonsawad P, Xing L, Milla E, et al. Structural evidence of glycoprotein assembly in cellular membrane compartments prior to Alphavirus budding. J Virol 2010;84:11145-11151.
    • (2010) J Virol , vol.84 , pp. 11145-11151
    • Soonsawad, P.1    Xing, L.2    Milla, E.3
  • 263
    • 77954505687 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase-, actin-, and microtubule-dependent transport of Semliki Forest Virus replication complexes from the plasma membrane to modified lysosomes
    • Spuul P, Balistreri G, Kaariainen L, et al. Phosphatidylinositol 3-kinase-, actin-, and microtubule-dependent transport of Semliki Forest Virus replication complexes from the plasma membrane to modified lysosomes. J Virol 2010;84:7543-7557.
    • (2010) J Virol , vol.84 , pp. 7543-7557
    • Spuul, P.1    Balistreri, G.2    Kaariainen, L.3
  • 264
    • 0027067063 scopus 로고
    • Identification of the active site residues in the nsP2 proteinase of Sindbis virus
    • Strauss EG, De Groot RJ, Levinson R, et al. Identification of the active site residues in the nsP2 proteinase of Sindbis virus. Virology 1992;191:932-940.
    • (1992) Virology , vol.191 , pp. 932-940
    • Strauss, E.G.1    De Groot, R.J.2    Levinson, R.3
  • 265
    • 0017091647 scopus 로고
    • Mutants of Sindbis virus. I. Isolation and partial characterization of 89 new temperature-sensitive mutants
    • Strauss EG, Lenches EM, Strauss JH. Mutants of Sindbis virus. I. Isolation and partial characterization of 89 new temperature-sensitive mutants. Virology 1976;74:154-168.
    • (1976) Virology , vol.74 , pp. 154-168
    • Strauss, E.G.1    Lenches, E.M.2    Strauss, J.H.3
  • 266
    • 0021319456 scopus 로고
    • Complete nucleotide sequence of the genomic RNA of Sindbis virus
    • Strauss EG, Rice CM, Strauss JH. Complete nucleotide sequence of the genomic RNA of Sindbis virus. Virology 1984;133:92-110.
    • (1984) Virology , vol.133 , pp. 92-110
    • Strauss, E.G.1    Rice, C.M.2    Strauss, J.H.3
  • 267
    • 0001906409 scopus 로고
    • Cellular receptors for alphaviruses
    • Wimmer E, ed, Cold Spring Harbor: Cold Spring Harbor Press
    • Strauss JH, Rümenapf T, Weir RC, et al. Cellular receptors for alphaviruses. In: Wimmer E, ed. Cellular Receptors for Animal Viruses. Cold Spring Harbor: Cold Spring Harbor Press; 1994:141-163.
    • (1994) Cellular Receptors for Animal Viruses. , pp. 141-163
    • Strauss, J.H.1    Rümenapf, T.2    Weir, R.C.3
  • 269
    • 0028088152 scopus 로고
    • The alphaviruses: gene expression, replication, and evolution
    • Strauss JH, Strauss EG. The alphaviruses: gene expression, replication, and evolution. Microbiol Rev 1994;58:491-562.
    • (1994) Microbiol Rev , vol.58 , pp. 491-562
    • Strauss, J.H.1    Strauss, E.G.2
  • 270
    • 0035815307 scopus 로고    scopus 로고
    • Virus evolution: how does an enveloped virus make a regular structure?
    • Strauss JH, Strauss EG. Virus evolution: how does an enveloped virus make a regular structure? Cell 2001;105:5-8.
    • (2001) Cell , vol.105 , pp. 5-8
    • Strauss, J.H.1    Strauss, E.G.2
  • 271
    • 0026691322 scopus 로고
    • Spike protein-nucleocapsid interactions drive the budding of alphaviruses
    • Suomalainen M, Liljestrom P, Garoff H. Spike protein-nucleocapsid interactions drive the budding of alphaviruses. J Virol 1992;66:4737-4747.
    • (1992) J Virol , vol.66 , pp. 4737-4747
    • Suomalainen, M.1    Liljestrom, P.2    Garoff, H.3
  • 272
    • 82555176572 scopus 로고    scopus 로고
    • Molecular links between the E2 envelope glycoprotein and nucleocapsid core in Sindbis virus
    • Tang J, Jose J, Chipman P, et al. Molecular links between the E2 envelope glycoprotein and nucleocapsid core in Sindbis virus. J Mol Biol 2011;414:442-459.
    • (2011) J Mol Biol , vol.414 , pp. 442-459
    • Tang, J.1    Jose, J.2    Chipman, P.3
  • 273
    • 0033028591 scopus 로고    scopus 로고
    • In vitro assembly of alphavirus cores by using nucleocapsid protein expressed in Escherichia coli
    • Tellinghuisen TL, Hamburger AE, Fisher BR, et al. In vitro assembly of alphavirus cores by using nucleocapsid protein expressed in Escherichia coli. J Virol 1999;73:5309-5319.
    • (1999) J Virol , vol.73 , pp. 5309-5319
    • Tellinghuisen, T.L.1    Hamburger, A.E.2    Fisher, B.R.3
  • 274
    • 0033995285 scopus 로고    scopus 로고
    • Nucleic acid-dependent cross-linking of the nucleocapsid protein of Sindbis virus
    • Tellinghuisen TL, Kuhn RJ. Nucleic acid-dependent cross-linking of the nucleocapsid protein of Sindbis virus. J Virol 2000;74:4302-4309.
    • (2000) J Virol , vol.74 , pp. 4302-4309
    • Tellinghuisen, T.L.1    Kuhn, R.J.2
  • 275
    • 0035128334 scopus 로고    scopus 로고
    • In vitro assembly of Sindbis virus core-like particles from cross-linked dimers of truncated and mutant capsid proteins
    • Tellinghuisen TL, Perera R, Kuhn RJ. In vitro assembly of Sindbis virus core-like particles from cross-linked dimers of truncated and mutant capsid proteins. J Virol 2001;75:2810-2817.
    • (2001) J Virol , vol.75 , pp. 2810-2817
    • Tellinghuisen, T.L.1    Perera, R.2    Kuhn, R.J.3
  • 276
    • 33749473615 scopus 로고    scopus 로고
    • Catalytic core of alphavirus nonstructural protein nsP4 possesses terminal adenylyltransferase activity
    • Tomar S, Hardy RW, Smith JL, et al. Catalytic core of alphavirus nonstructural protein nsP4 possesses terminal adenylyltransferase activity. J Virol 2006;80:9962-9969.
    • (2006) J Virol , vol.80 , pp. 9962-9969
    • Tomar, S.1    Hardy, R.W.2    Smith, J.L.3
  • 277
    • 0037639148 scopus 로고    scopus 로고
    • Amino acid mutations in the replicase protein nsP3 of Semliki Forest virus cumulatively affect neurovirulence
    • Tuittila M, Hinkkanen AE. Amino acid mutations in the replicase protein nsP3 of Semliki Forest virus cumulatively affect neurovirulence. J Gen Virol 2003;84:1525-1533.
    • (2003) J Gen Virol , vol.84 , pp. 1525-1533
    • Tuittila, M.1    Hinkkanen, A.E.2
  • 278
    • 0041888255 scopus 로고    scopus 로고
    • Complementation of a deletion in the rubella virus p150 nonstructural protein by the viral capsid protein
    • Tzeng WP, Frey TK. Complementation of a deletion in the rubella virus p150 nonstructural protein by the viral capsid protein. J Virol 2003;77:9502-9510.
    • (2003) J Virol , vol.77 , pp. 9502-9510
    • Tzeng, W.P.1    Frey, T.K.2
  • 279
    • 0025841911 scopus 로고
    • Identification of a putative alphavirus receptor on mouse neural cells
    • Ubol S, Griffin DE. Identification of a putative alphavirus receptor on mouse neural cells. J Virol 1991;65:6913-6921.
    • (1991) J Virol , vol.65 , pp. 6913-6921
    • Ubol, S.1    Griffin, D.E.2
  • 280
    • 0017110423 scopus 로고
    • Semliki Forest virus capsid protein associates with the 60S ribosomal subunit in infected cells
    • Ulmanen I, Soderlund H, Kaariainen L. Semliki Forest virus capsid protein associates with the 60S ribosomal subunit in infected cells. J Virol 1976;20:203-210.
    • (1976) J Virol , vol.20 , pp. 203-210
    • Ulmanen, I.1    Soderlund, H.2    Kaariainen, L.3
  • 281
    • 0031919431 scopus 로고    scopus 로고
    • A single point mutation controls the cholesterol dependence of Semliki Forest virus entry and exit
    • Vashishtha M, Phalen T, Marquardt MT, et al. A single point mutation controls the cholesterol dependence of Semliki Forest virus entry and exit. J Cell Biol 1998;140:91-99.
    • (1998) J Cell Biol , vol.140 , pp. 91-99
    • Vashishtha, M.1    Phalen, T.2    Marquardt, M.T.3
  • 282
    • 0034625437 scopus 로고    scopus 로고
    • Identification of a novel function of the alphavirus capping apparatus. RNA 5'-triphosphatase activity of Nsp2
    • Vasiljeva L, Merits A, Auvinen P, et al. Identification of a novel function of the alphavirus capping apparatus. RNA 5'-triphosphatase activity of Nsp2. J Biol Chem 2000;275:17281-17287.
    • (2000) J Biol Chem , vol.275 , pp. 17281-17287
    • Vasiljeva, L.1    Merits, A.2    Auvinen, P.3
  • 283
    • 0035903188 scopus 로고    scopus 로고
    • Site-specific protease activity of the carboxyl-terminal domain of Semliki Forest virus replicase protein nsP2
    • Vasiljeva L, Valmu L, Kaariainen L, et al. Site-specific protease activity of the carboxyl-terminal domain of Semliki Forest virus replicase protein nsP2. J Biol Chem 2001;276:30786-30793.
    • (2001) J Biol Chem , vol.276 , pp. 30786-30793
    • Vasiljeva, L.1    Valmu, L.2    Kaariainen, L.3
  • 284
    • 0028316182 scopus 로고
    • The organization of the spike complex of Semliki Forest virus
    • Venien-Bryan C, Fuller SD. The organization of the spike complex of Semliki Forest virus. J Mol Biol 1994;236:572-583.
    • (1994) J Mol Biol , vol.236 , pp. 572-583
    • Venien-Bryan, C.1    Fuller, S.D.2
  • 285
    • 0035937166 scopus 로고    scopus 로고
    • Elimination of phosphorylation sites of Semliki Forest virus replicase protein nsP3
    • Vihinen H, Ahola T, Tuittila M, et al. Elimination of phosphorylation sites of Semliki Forest virus replicase protein nsP3. J Biol Chem 2001;276:5745-5752.
    • (2001) J Biol Chem , vol.276 , pp. 5745-5752
    • Vihinen, H.1    Ahola, T.2    Tuittila, M.3
  • 286
    • 0034623235 scopus 로고    scopus 로고
    • Phosphorylation site analysis of Semliki Forest virus nonstructural protein 3
    • Vihinen H, Saarinen J. Phosphorylation site analysis of Semliki Forest virus nonstructural protein 3. J Biol Chem 2000;275:27775-27783.
    • (2000) J Biol Chem , vol.275 , pp. 27775-27783
    • Vihinen, H.1    Saarinen, J.2
  • 287
    • 30044437341 scopus 로고    scopus 로고
    • The efficient packaging of Venezuelan equine encephalitis virus-specific RNAs into viral particles is determined by nsP1-3 synthesis
    • Volkova E, Gorchakov R, Frolov I. The efficient packaging of Venezuelan equine encephalitis virus-specific RNAs into viral particles is determined by nsP1-3 synthesis. Virology 2006;344:315-327.
    • (2006) Virology , vol.344 , pp. 315-327
    • Volkova, E.1    Gorchakov, R.2    Frolov, I.3
  • 288
    • 0018141590 scopus 로고
    • Hexagonal glycoprotein arrays from Sindbis virus membranes
    • von Bonsdorff CH, Harrison SC. Hexagonal glycoprotein arrays from Sindbis virus membranes. J Virol 1978;28:578-583.
    • (1978) J Virol , vol.28 , pp. 578-583
    • von Bonsdorff, C.H.1    Harrison, S.C.2
  • 289
    • 0016821407 scopus 로고
    • Sindbis virus glycoproteins form a regular icosahedral surface lattice
    • von Bonsdorff CH, Harrison SC. Sindbis virus glycoproteins form a regular icosahedral surface lattice. J Virol 1975;16:141-145.
    • (1975) J Virol , vol.16 , pp. 141-145
    • von Bonsdorff, C.H.1    Harrison, S.C.2
  • 290
    • 78649817910 scopus 로고    scopus 로고
    • Glycoprotein organization of Chikungunya virus particles revealed by X-ray crystallography
    • Voss JE, Vaney MC, Duquerroy S, et al. Glycoprotein organization of Chikungunya virus particles revealed by X-ray crystallography. Nature 2010;468:709-712.
    • (2010) Nature , vol.468 , pp. 709-712
    • Voss, J.E.1    Vaney, M.C.2    Duquerroy, S.3
  • 291
    • 0037063998 scopus 로고    scopus 로고
    • Sphingolipid and cholesterol dependence of alphavirus membrane fusion
    • Waarts B-L, Bittman R, Wilschut J. Sphingolipid and cholesterol dependence of alphavirus membrane fusion. J Biol Chem 2002;277:38141-38147.
    • (2002) J Biol Chem , vol.277 , pp. 38141-38147
    • Waarts, B.-L.1    Bittman, R.2    Wilschut, J.3
  • 292
    • 0024455501 scopus 로고
    • The heterodimeric association between the membrane proteins of Semliki Forest virus changes its sensitivity to low pH during virus maturation
    • Wahlberg JM, Boere WA, Garoff H. The heterodimeric association between the membrane proteins of Semliki Forest virus changes its sensitivity to low pH during virus maturation. J Virol 1989;63:4991-4997.
    • (1989) J Virol , vol.63 , pp. 4991-4997
    • Wahlberg, J.M.1    Boere, W.A.2    Garoff, H.3
  • 293
    • 0026495818 scopus 로고
    • Membrane fusion of Semliki Forest virus involves homotrimers of the fusion protein
    • Wahlberg JM, Bron R, Wilschut J, et al. Membrane fusion of Semliki Forest virus involves homotrimers of the fusion protein. J Virol 1992;66:7309-7318.
    • (1992) J Virol , vol.66 , pp. 7309-7318
    • Wahlberg, J.M.1    Bron, R.2    Wilschut, J.3
  • 294
    • 0026584727 scopus 로고
    • Membrane fusion process of Semliki Forest virus I: Low pH-induced rearrangement in spike glycoprotein quaternary structure precedes virus penetration into cells
    • Wahlberg JM, Garoff H. Membrane fusion process of Semliki Forest virus I: Low pH-induced rearrangement in spike glycoprotein quaternary structure precedes virus penetration into cells. J Cell Biol 1992;116:339-348.
    • (1992) J Cell Biol , vol.116 , pp. 339-348
    • Wahlberg, J.M.1    Garoff, H.2
  • 295
    • 0028362119 scopus 로고
    • Construction of rubella virus genome-length cDNA clones and synthesis of infectious RNA transcripts
    • Wang CY, Dominguez G, Frey TK. Construction of rubella virus genome-length cDNA clones and synthesis of infectious RNA transcripts. J Virol 1994;68:3550-3557.
    • (1994) J Virol , vol.68 , pp. 3550-3557
    • Wang, C.Y.1    Dominguez, G.2    Frey, T.K.3
  • 296
    • 0026628752 scopus 로고
    • High-affinity laminin receptor is a receptor for Sindbis virus in mammalian cells
    • Wang KS, Kuhn RJ, Strauss EG, et al. High-affinity laminin receptor is a receptor for Sindbis virus in mammalian cells. J Virol 1992;66:4992-5001.
    • (1992) J Virol , vol.66 , pp. 4992-5001
    • Wang, K.S.1    Kuhn, R.J.2    Strauss, E.G.3
  • 297
    • 0025791013 scopus 로고
    • Antiidiotypic antibodies as probes for the Sindbis virus receptor
    • Wang K-S, Schmaljohn AL, Kuhn RJ, et al. Antiidiotypic antibodies as probes for the Sindbis virus receptor. Virology 1991;181:694-702.
    • (1991) Virology , vol.181 , pp. 694-702
    • Wang, K.-S.1    Schmaljohn, A.L.2    Kuhn, R.J.3
  • 298
    • 0028040383 scopus 로고
    • Alphavirus nsP3 functions to form replication complexes transcribing negative-strand RNA
    • Wang Y-F, Sawicki SG, Sawicki D. Alphavirus nsP3 functions to form replication complexes transcribing negative-strand RNA. J Virol 1994;68:6466-6475.
    • (1994) J Virol , vol.68 , pp. 6466-6475
    • Wang, Y.-F.1    Sawicki, S.G.2    Sawicki, D.3
  • 299
    • 0026086221 scopus 로고
    • Sindbis virus nsP1 functions in negative-strand RNA synthesis
    • Wang YF, Sawicki SG, Sawicki DL. Sindbis virus nsP1 functions in negative-strand RNA synthesis. J Virol 1991;65:985-988.
    • (1991) J Virol , vol.65 , pp. 985-988
    • Wang, Y.F.1    Sawicki, S.G.2    Sawicki, D.L.3
  • 300
    • 77949264955 scopus 로고    scopus 로고
    • et al. A virus-like particle vaccine for epidemic Chikungunya virus protects nonhuman primates against infection
    • Wataru A, Yang ZY, Andersen H. et al. A virus-like particle vaccine for epidemic Chikungunya virus protects nonhuman primates against infection. Natl Med 2010;16:334-338.
    • (2010) Natl Med , vol.16 , pp. 334-338
    • Wataru, A.1    Yang, Z.Y.2    Andersen, H.3
  • 301
    • 0028359402 scopus 로고
    • Interactions between Sindbis virus RNAs and a 68 amino acid derivative of the viral capsid protein further defines the capsid binding site
    • Weiss B, Geigenmüller-Gnirke U, Schlesinger S. Interactions between Sindbis virus RNAs and a 68 amino acid derivative of the viral capsid protein further defines the capsid binding site. Nucleic Acids Res 1994;22:780-786.
    • (1994) Nucleic Acids Res , vol.22 , pp. 780-786
    • Weiss, B.1    Geigenmüller-Gnirke, U.2    Schlesinger, S.3
  • 302
    • 0024428285 scopus 로고
    • Evidence for specificity in the encapsidation of Sindbis virus RNAs
    • Weiss B, Nitschko H, Ghattas I, et al. Evidence for specificity in the encapsidation of Sindbis virus RNAs. J Virol 1989;63:5310-5318.
    • (1989) J Virol , vol.63 , pp. 5310-5318
    • Weiss, B.1    Nitschko, H.2    Ghattas, I.3
  • 303
    • 0023118357 scopus 로고
    • The mode of assembly of alphavirus cores implies a mechanism for the disassembly of the cores in the early stages of infection
    • Wengler G. The mode of assembly of alphavirus cores implies a mechanism for the disassembly of the cores in the early stages of infection. Arch Virol 1987;94:1-14.
    • (1987) Arch Virol , vol.94 , pp. 1-14
    • Wengler, G.1
  • 304
    • 0020053676 scopus 로고
    • The core protein of the alphavirus Sindbis virus assembles into core-like nucleoproteins with the viral genome RNA and with other single-stranded nucleic acids in vitro
    • Wengler G, Boege U, Wengler G, et al. The core protein of the alphavirus Sindbis virus assembles into core-like nucleoproteins with the viral genome RNA and with other single-stranded nucleic acids in vitro. Virology 1982;118:401-410.
    • (1982) Virology , vol.118 , pp. 401-410
    • Wengler, G.1    Boege, U.2    Wengler, G.3
  • 305
    • 0030219428 scopus 로고    scopus 로고
    • Analyses of the role of structural changes in the regulation of uncoating and assembly of alphavirus cores
    • Wengler G, Gros C, Wengler G. Analyses of the role of structural changes in the regulation of uncoating and assembly of alphavirus cores. Virology 1996;222:123-132.
    • (1996) Virology , vol.222 , pp. 123-132
    • Wengler, G.1    Gros, C.2    Wengler, G.3
  • 306
    • 0037234234 scopus 로고    scopus 로고
    • Entry of alphaviruses at the plasma membrane converts the viral surface proteins into an ion-permeable pore that can be detected by electrophysiological analyses of whole-cell membrane currents
    • Wengler G, Koschinski A, Wengler G, et al. Entry of alphaviruses at the plasma membrane converts the viral surface proteins into an ion-permeable pore that can be detected by electrophysiological analyses of whole-cell membrane currents. J Gen Virol 2003;84:173-181.
    • (2003) J Gen Virol , vol.84 , pp. 173-181
    • Wengler, G.1    Koschinski, A.2    Wengler, G.3
  • 307
    • 0021262413 scopus 로고
    • Identification of a transfer of viral core protein to cellular ribosomes during the early stages of alphavirus infection
    • Wengler G, Wengler G. Identification of a transfer of viral core protein to cellular ribosomes during the early stages of alphavirus infection. Virology 1984;134:435.
    • (1984) Virology , vol.134 , pp. 435
    • Wengler, G.1    Wengler, G.2
  • 308
    • 0036787227 scopus 로고    scopus 로고
    • In vitro analysis of factors involved in the disassembly of Sindbis virus cores by 60S ribosomal subunits identifies a possible role of low pH
    • Wengler G, Wengler G. In vitro analysis of factors involved in the disassembly of Sindbis virus cores by 60S ribosomal subunits identifies a possible role of low pH. J Gen Virol 2002;83:2417-2426.
    • (2002) J Gen Virol , vol.83 , pp. 2417-2426
    • Wengler, G.1    Wengler, G.2
  • 309
    • 0033541949 scopus 로고    scopus 로고
    • The isolation of the ectodomain of the alphavirus E1 protein as a soluble hemagglutinin and its crystalization
    • Wengler G, Wengler G, Rey FA. The isolation of the ectodomain of the alphavirus E1 protein as a soluble hemagglutinin and its crystalization. Virology 1999;257:472-482.
    • (1999) Virology , vol.257 , pp. 472-482
    • Wengler, G.1    Wengler, G.2    Rey, F.A.3
  • 310
    • 0027054277 scopus 로고
    • Identification of a sequence element in the alphavirus core protein which mediates interaction of cores with ribosomes and the disassembly of cores
    • Wengler G, Würkner D, Wengler G. Identification of a sequence element in the alphavirus core protein which mediates interaction of cores with ribosomes and the disassembly of cores. Virology 1992;191:880-888.
    • (1992) Virology , vol.191 , pp. 880-888
    • Wengler, G.1    Würkner, D.2    Wengler, G.3
  • 311
    • 0033541385 scopus 로고    scopus 로고
    • Salmon pancreas disease virus, an alphavirus infecting farmed Atlantic salmon, Salmo salar L
    • Weston JH, Welsh MD, McLoughlin MF, et al. Salmon pancreas disease virus, an alphavirus infecting farmed Atlantic salmon, Salmo salar L. Virology 1999;256:188-195.
    • (1999) Virology , vol.256 , pp. 188-195
    • Weston, J.H.1    Welsh, M.D.2    McLoughlin, M.F.3
  • 312
    • 0019069749 scopus 로고
    • Fusion of Semliki Forest virus with the plasma membrane can be induced by low pH
    • White J, Kartenbeck J, Helenius A. Fusion of Semliki Forest virus with the plasma membrane can be induced by low pH. J Cell Biol 1980;87:264-272.
    • (1980) J Cell Biol , vol.87 , pp. 264-272
    • White, J.1    Kartenbeck, J.2    Helenius, A.3
  • 313
    • 0035078780 scopus 로고    scopus 로고
    • Sequence requirements for Sindbis virus subgenomic mRNA promoter function in cultured cells
    • Wielgosz MM, Raju R, Huang HV. Sequence requirements for Sindbis virus subgenomic mRNA promoter function in cultured cells. J Virol 2001;75:3509-3519.
    • (2001) J Virol , vol.75 , pp. 3509-3519
    • Wielgosz, M.M.1    Raju, R.2    Huang, H.V.3
  • 314
    • 0029201982 scopus 로고
    • Fusion of Semliki Forest virus with cholesterol-containing liposomes at low pH: a specific requirement for sphingolipids
    • Wilschut J, Corver J, Nieva JL, et al. Fusion of Semliki Forest virus with cholesterol-containing liposomes at low pH: a specific requirement for sphingolipids. Mol Membr Biol 1995;12:143-149.
    • (1995) Mol Membr Biol , vol.12 , pp. 143-149
    • Wilschut, J.1    Corver, J.2    Nieva, J.L.3
  • 315
    • 0024514346 scopus 로고
    • Sindbis virus: an efficient, broad host range vector for gene expression in animal cells
    • Xiong C, Levis R, Shen P, et al. Sindbis virus: an efficient, broad host range vector for gene expression in animal cells. Science 1989;243:1188-1191.
    • (1989) Science , vol.243 , pp. 1188-1191
    • Xiong, C.1    Levis, R.2    Shen, P.3
  • 316
    • 0013007874 scopus 로고    scopus 로고
    • Interactions between PE2, E1, and 6K required for assembly of alphaviruses studied with chimeric viruses
    • Yao JS, Strauss EG, Strauss JH. Interactions between PE2, E1, and 6K required for assembly of alphaviruses studied with chimeric viruses. J Virol 1996;70:7910-7920.
    • (1996) J Virol , vol.70 , pp. 7910-7920
    • Yao, J.S.1    Strauss, E.G.2    Strauss, J.H.3
  • 317
    • 80052731717 scopus 로고    scopus 로고
    • 4.4 Å cryo-EM structure of an enveloped alphavirus Venezuelan equine encephalitis virus
    • Zhang R, Hryc CF, Cong Y, et al. 4.4 Å cryo-EM structure of an enveloped alphavirus Venezuelan equine encephalitis virus. EMBO J 2011;30:3854-3863.
    • (2011) EMBO J , vol.30 , pp. 3854-3863
    • Zhang, R.1    Hryc, C.F.2    Cong, Y.3
  • 318
    • 0036633673 scopus 로고    scopus 로고
    • Aura virus structure suggests that the T_4 organization is a fundamental property of viral structural proteins
    • Zhang W, Fisher BR, Olson NH, et al. Aura virus structure suggests that the T_4 organization is a fundamental property of viral structural proteins. J Virol 2002;76:7239-7246.
    • (2002) J Virol , vol.76 , pp. 7239-7246
    • Zhang, W.1    Fisher, B.R.2    Olson, N.H.3
  • 319
    • 13144266721 scopus 로고    scopus 로고
    • Heparin binding sites on Ross River virus revealed by electron cryo-microscopy
    • Zhang W, Heil M, Kuhn RJ, et al. Heparin binding sites on Ross River virus revealed by electron cryo-microscopy. Virology 2005;332:511-518.
    • (2005) Virology , vol.332 , pp. 511-518
    • Zhang, W.1    Heil, M.2    Kuhn, R.J.3
  • 320
    • 0036827856 scopus 로고    scopus 로고
    • Placement of the structural proteins in Sindbis virus
    • Zhang W, Mukhopadhyay S, Pletnev SV, et al. Placement of the structural proteins in Sindbis virus. J Virol 2002;76:11645-11658.
    • (2002) J Virol , vol.76 , pp. 11645-11658
    • Zhang, W.1    Mukhopadhyay, S.2    Pletnev, S.V.3
  • 321
    • 0027965259 scopus 로고
    • A tyrosine-based motif in the cytoplasmic domain of the alphavirus envelope protein is essential for budding
    • Zhao H, Lindqvist B, Garoff H, et al. A tyrosine-based motif in the cytoplasmic domain of the alphavirus envelope protein is essential for budding. EMBO J 1994;13:4204-4211.
    • (1994) EMBO J , vol.13 , pp. 4204-4211
    • Zhao, H.1    Lindqvist, B.2    Garoff, H.3
  • 322
    • 80052056371 scopus 로고    scopus 로고
    • The domain I-domain III linker plays an important role in the fusogenic conformational change of the alphavirus membrane fusion protein
    • Zheng Y, Sanchez-San Martin C, Qin ZL, et al. The domain I-domain III linker plays an important role in the fusogenic conformational change of the alphavirus membrane fusion protein. J Virol 2011;85:6334-6342.
    • (2011) J Virol , vol.85 , pp. 6334-6342
    • Zheng, Y.1    Sanchez-San Martin, C.2    Qin, Z.L.3
  • 323
    • 0017803335 scopus 로고
    • Subunit composition of the membrane glycoprotein complex of Semliki Forest virus
    • Ziemiecki A, Garoff H. Subunit composition of the membrane glycoprotein complex of Semliki Forest virus. J Mol Biol 1978;122:259-269.
    • (1978) J Mol Biol , vol.122 , pp. 259-269
    • Ziemiecki, A.1    Garoff, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.