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Volumn 3, Issue , 2016, Pages 263-281

Properties and Functions of the Dengue Virus Capsid Protein

Author keywords

Arbovirus; Capsid protein; Dengue virus; Flavivirus; Lipid droplets; RNA virus; Viral assembly; Viral encapsidation

Indexed keywords

CAPSID PROTEIN; FAT DROPLET; PROTEIN BINDING; VIRUS RECEPTOR; VIRUS RNA;

EID: 84992079423     PISSN: 2327056X     EISSN: 23270578     Source Type: Journal    
DOI: 10.1146/annurev-virology-110615-042334     Document Type: Review
Times cited : (110)

References (131)
  • 2
    • 84973436381 scopus 로고    scopus 로고
    • Flaviviridae
    • ed. DM Knipe, P Howley Philadelphia: LippincottWilliams &Wilkins
    • Lindenbach BD, Murray CL, Thiel HJ, Rice CM. 2013. Flaviviridae. In Fields Virology, ed. DM Knipe, P Howley, pp. 712-46. Philadelphia: LippincottWilliams &Wilkins
    • (2013) Fields Virology , pp. 712-746
    • Lindenbach, B.D.1    Murray, C.L.2    Thiel, H.J.3    Rice, C.M.4
  • 3
    • 84937550619 scopus 로고    scopus 로고
    • Zika virus: Following the path of dengue and chikungunya
    • Musso D, Cao-Lormeau VM, Gubler DJ. 2015. Zika virus: following the path of dengue and chikungunya? Lancet 386:243-44
    • (2015) Lancet , vol.386 , pp. 243-244
    • Musso, D.1    Cao-Lormeau, V.M.2    Gubler, D.J.3
  • 4
    • 84928951064 scopus 로고    scopus 로고
    • Insect-specific flaviviruses: A systematic review of their discovery, host range, mode of transmission, superinfection exclusion potential and genomic organization
    • Blitvich BJ, Firth AE. 2015. Insect-specific flaviviruses: a systematic review of their discovery, host range, mode of transmission, superinfection exclusion potential and genomic organization. Viruses 7:1927-59
    • (2015) Viruses , vol.7 , pp. 1927-1959
    • Blitvich, B.J.1    Firth, A.E.2
  • 5
    • 35748929379 scopus 로고    scopus 로고
    • Dengue
    • Halstead SB. 2007. Dengue. Lancet 370:1644-52
    • (2007) Lancet , vol.370 , pp. 1644-1652
    • Halstead, S.B.1
  • 6
    • 18344387519 scopus 로고    scopus 로고
    • Structure of dengue virus: Implications for flavivirus organization, maturation, and fusion
    • Kuhn RJ, Zhang W, Rossmann MG, Pletnev SV, Corver J, et al. 2002. Structure of dengue virus: implications for flavivirus organization, maturation, and fusion. Cell 108:717-25
    • (2002) Cell , vol.108 , pp. 717-725
    • Kuhn, R.J.1    Zhang, W.2    Rossmann, M.G.3    Pletnev, S.V.4    Corver, J.5
  • 7
    • 0242574743 scopus 로고    scopus 로고
    • Visualization ofmembrane protein domains by cryo-electron microscopy of dengue virus
    • ZhangW, Chipman PR, Corver J, Johnson PR, Zhang Y, et al. 2003. Visualization ofmembrane protein domains by cryo-electron microscopy of dengue virus. Nat. Struct. Biol. 10:907-12
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 907-912
    • Zhang, W.1    Chipman, P.R.2    Corver, J.3    Johnson, P.R.4    Zhang, Y.5
  • 8
    • 84872048730 scopus 로고    scopus 로고
    • Cryo-EM structure of the mature dengue virus at 3 5-A resolution
    • Zhang X, Ge P, Yu X, Brannan JM, Bi G, et al. 2013. Cryo-EM structure of the mature dengue virus at 3.5-A resolution. Nat. Struct. Mol. Biol. 20:105-10
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 105-110
    • Zhang, X.1    Ge, P.2    Yu, X.3    Brannan, J.M.4    Bi, G.5
  • 10
    • 41649101680 scopus 로고    scopus 로고
    • Functional entry of dengue virus into Aedes albopictus mosquito cells is dependent on clathrin-mediated endocytosis
    • Acosta EG, Castilla V, DamonteEB. 2008. Functional entry of dengue virus into Aedes albopictus mosquito cells is dependent on clathrin-mediated endocytosis. J. Gen. Virol. 89:474-84
    • (2008) J. Gen. Virol. , vol.89 , pp. 474-484
    • Acosta, E.G.1    Castilla, V.2    Damonte, E.B.3
  • 11
    • 70350719853 scopus 로고    scopus 로고
    • Alternative infectious entry pathways for dengue virus serotypes into mammalian cells
    • Acosta EG, Castilla V, Damonte EB. 2009. Alternative infectious entry pathways for dengue virus serotypes into mammalian cells. Cell Microbiol. 11:1533-49
    • (2009) Cell Microbiol. , vol.11 , pp. 1533-1549
    • Acosta, E.G.1    Castilla, V.2    Damonte, E.B.3
  • 12
    • 84866102237 scopus 로고    scopus 로고
    • Differential requirements in endocytic trafficking for penetration of dengue virus
    • Acosta EG, Castilla V, Damonte EB. 2012. Differential requirements in endocytic trafficking for penetration of dengue virus. PLOS ONE 7:e44835
    • (2012) PLOS ONE , vol.7 , pp. e44835
    • Acosta, E.G.1    Castilla, V.2    Damonte, E.B.3
  • 13
    • 34247637615 scopus 로고    scopus 로고
    • Rab 5 is required for the cellular entry of dengue and West Nile viruses
    • KrishnanMN, Sukumaran B, Pal U, Agaisse H, Murray JL, et al. 2007. Rab 5 is required for the cellular entry of dengue and West Nile viruses. J. Virol. 81:4881-85
    • (2007) J. Virol. , vol.81 , pp. 4881-4885
    • Krishnan, M.N.1    Sukumaran, B.2    Pal, U.3    Agaisse, H.4    Murray, J.L.5
  • 14
    • 47749122553 scopus 로고    scopus 로고
    • Endocytic pathway followed by dengue virus to infect the mosquito cell line C6/36 HT
    • Mosso C, Galvan-Mendoza IJ, Ludert JE, del Angel RM. 2008. Endocytic pathway followed by dengue virus to infect the mosquito cell line C6/36 HT. Virology 378:193-99
    • (2008) Virology , vol.378 , pp. 193-199
    • Mosso, C.1    Galvan-Mendoza, I.J.2    Ludert, J.E.3    Del Angel, R.M.4
  • 16
    • 1642499388 scopus 로고    scopus 로고
    • Structure of the dengue virus envelope protein after membrane fusion
    • Modis Y, Ogata S, Clements D, Harrison SC. 2004. Structure of the dengue virus envelope protein after membrane fusion. Nature 427:313-19
    • (2004) Nature , vol.427 , pp. 313-319
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 17
    • 66149103151 scopus 로고    scopus 로고
    • Crystal structure of dengue virus type 1 envelope protein in the postfusion conformation and its implications for membrane fusion
    • Nayak V, Dessau M, Kucera K, Anthony K, Ledizet M, Modis Y. 2009. Crystal structure of dengue virus type 1 envelope protein in the postfusion conformation and its implications for membrane fusion. J. Virol. 83:4338-44
    • (2009) J. Virol. , vol.83 , pp. 4338-4344
    • Nayak, V.1    Dessau, M.2    Kucera, K.3    Anthony, K.4    Ledizet, M.5    Modis, Y.6
  • 20
    • 34247848008 scopus 로고    scopus 로고
    • The non-structural protein 4A of dengue virus is an integral membrane protein inducing membrane alterations in a 2K-regulated manner
    • Miller S, Kastner S, Krijnse-Locker J, Buhler S, Bartenschlager R. 2007. The non-structural protein 4A of dengue virus is an integral membrane protein inducing membrane alterations in a 2K-regulated manner. J. Biol. Chem. 282:8873-82
    • (2007) J. Biol. Chem. , vol.282 , pp. 8873-8882
    • Miller, S.1    Kastner, S.2    Krijnse-Locker, J.3    Buhler, S.4    Bartenschlager, R.5
  • 21
    • 33646851580 scopus 로고    scopus 로고
    • Subcellular localization and membrane topology of the Dengue virus type 2 non-structural protein 4B
    • Miller S, Sparacio S, Bartenschlager R. 2006. Subcellular localization and membrane topology of the Dengue virus type 2 non-structural protein 4B. J. Biol. Chem. 281:8854-63
    • (2006) J. Biol. Chem. , vol.281 , pp. 8854-8863
    • Miller, S.1    Sparacio, S.2    Bartenschlager, R.3
  • 22
    • 84875777404 scopus 로고    scopus 로고
    • Membrane topology and function of dengue virusNS2A protein
    • Xie X, Gayen S, Kang C, Yuan Z, Shi PY. 2013. Membrane topology and function of dengue virusNS2A protein. J. Virol. 87:4609-22
    • (2013) J. Virol. , vol.87 , pp. 4609-4622
    • Xie, X.1    Gayen, S.2    Kang, C.3    Yuan, Z.4    Shi, P.Y.5
  • 23
    • 77957201605 scopus 로고    scopus 로고
    • The endoplasmic reticulum provides the membrane platform for biogenesis of the flavivirus replication complex
    • Gillespie LK, Hoenen A, Morgan G, Mackenzie JM. 2010. The endoplasmic reticulum provides the membrane platform for biogenesis of the flavivirus replication complex. J. Virol. 84:10438-47
    • (2010) J. Virol. , vol.84 , pp. 10438-10447
    • Gillespie, L.K.1    Hoenen, A.2    Morgan, G.3    Mackenzie, J.M.4
  • 24
    • 64649097038 scopus 로고    scopus 로고
    • Composition and three-dimensional architecture of the dengue virus replication and assembly sites
    • Welsch S, Miller S, Romero-Brey I, Merz A, Bleck CK, et al. 2009. Composition and three-dimensional architecture of the dengue virus replication and assembly sites. Cell Host Microbe 5:365-75
    • (2009) Cell Host Microbe , vol.5 , pp. 365-375
    • Welsch, S.1    Miller, S.2    Romero-Brey, I.3    Merz, A.4    Bleck, C.K.5
  • 25
    • 0029941322 scopus 로고    scopus 로고
    • Immunolocalization of the dengue virus nonstructural glycoprotein NS1 suggests a role in viral RNA replication
    • Mackenzie JM, Jones MK, Young PR. 1996. Immunolocalization of the dengue virus nonstructural glycoprotein NS1 suggests a role in viral RNA replication. Virology 220:232-40
    • (1996) Virology , vol.220 , pp. 232-240
    • Mackenzie, J.M.1    Jones, M.K.2    Young, P.R.3
  • 26
    • 84897546853 scopus 로고    scopus 로고
    • Ultrastructural characterization and three-dimensional architecture of replication sites in dengue virus-infected mosquito cells
    • Junjhon J, Pennington JG, Edwards TJ, Perera R, Lanman J, Kuhn RJ. 2014. Ultrastructural characterization and three-dimensional architecture of replication sites in dengue virus-infected mosquito cells. J. Virol. 88:4687-97
    • (2014) J. Virol. , vol.88 , pp. 4687-4697
    • Junjhon, J.1    Pennington, J.G.2    Edwards, T.J.3    Perera, R.4    Lanman, J.5    Kuhn, R.J.6
  • 27
    • 84878209731 scopus 로고    scopus 로고
    • Three-dimensional architecture of tick-borne encephalitis virus replication sites and trafficking of the replicated RNA
    • Miorin L, Romero-Brey I, Maiuri P, Hoppe S, Krijnse-Locker J, et al. 2013. Three-dimensional architecture of tick-borne encephalitis virus replication sites and trafficking of the replicated RNA. J. Virol. 87:6469-81
    • (2013) J. Virol. , vol.87 , pp. 6469-6481
    • Miorin, L.1    Romero-Brey, I.2    Maiuri, P.3    Hoppe, S.4    Krijnse-Locker, J.5
  • 30
    • 41349112304 scopus 로고    scopus 로고
    • Structure of the immature dengue virus at low pH primes proteolytic maturation
    • Yu IM, Zhang W, Holdaway HA, Li L, Kostyuchenko VA, et al. 2008. Structure of the immature dengue virus at low pH primes proteolytic maturation. Science 319:1834-37
    • (2008) Science , vol.319 , pp. 1834-1837
    • Yu, I.M.1    Zhang, W.2    Holdaway, H.A.3    Li, L.4    Kostyuchenko, V.A.5
  • 31
    • 4043104128 scopus 로고    scopus 로고
    • Identification of the homotypic interaction domain of the core protein of dengue virus type 2
    • Wang SH, Syu WJ, Hu ST. 2004. Identification of the homotypic interaction domain of the core protein of dengue virus type 2. J. Gen. Virol. 85:2307-14
    • (2004) J. Gen. Virol. , vol.85 , pp. 2307-2314
    • Wang, S.H.1    Syu, W.J.2    Hu, S.T.3
  • 33
    • 1542723492 scopus 로고    scopus 로고
    • Solution structure of dengue virus capsid protein reveals another fold
    • Ma L, Jones CT, Groesch TD, Kuhn RJ, Post CB. 2004. Solution structure of dengue virus capsid protein reveals another fold. PNAS 101:3414-19
    • (2004) PNAS , vol.101 , pp. 3414-3419
    • Ma, L.1    Jones, C.T.2    Groesch, T.D.3    Kuhn, R.J.4    Post, C.B.5
  • 35
    • 84904694717 scopus 로고    scopus 로고
    • Maintenance of dimer conformation by the dengue virus core protein α4-α4- helix pair is critical for nucleocapsid formation and virus production
    • Teoh PG, Huang ZS, Pong WL, Chen PC, Wu HN. 2014. Maintenance of dimer conformation by the dengue virus core protein α4-α4- helix pair is critical for nucleocapsid formation and virus production. J. Virol. 88:7998-8015
    • (2014) J. Virol. , vol.88 , pp. 7998-8015
    • Teoh, P.G.1    Huang, Z.S.2    Pong, W.L.3    Chen, P.C.4    Wu, H.N.5
  • 36
    • 84879947276 scopus 로고    scopus 로고
    • Hydrophobic segment of dengue virus C protein Interaction with model membranes
    • Nemesio H, Palomares-Jerez MF, Villalain J. 2013. Hydrophobic segment of dengue virus C protein. Interaction with model membranes. Mol. Membr. Biol. 30:273-87
    • (2013) Mol. Membr. Biol. , vol.30 , pp. 273-287
    • Nemesio, H.1    Palomares-Jerez, M.F.2    Villalain, J.3
  • 37
    • 0030838369 scopus 로고    scopus 로고
    • A conserved internal hydrophobic domain mediates the stable membrane integration of the dengue virus capsid protein
    • Markoff L, Falgout B, Chang A. 1997. A conserved internal hydrophobic domain mediates the stable membrane integration of the dengue virus capsid protein. Virology 233:105-17
    • (1997) Virology , vol.233 , pp. 105-117
    • Markoff, L.1    Falgout, B.2    Chang, A.3
  • 38
    • 84856860540 scopus 로고    scopus 로고
    • Uncoupling cis-acting RNA elements from coding sequences revealed a requirement of the N-terminal region of dengue virus capsid protein in virus particle formation
    • Samsa MM, Mondotte JA, Caramelo JJ, Gamarnik AV. 2012. Uncoupling cis-acting RNA elements from coding sequences revealed a requirement of the N-terminal region of dengue virus capsid protein in virus particle formation. J. Virol. 86:1046-58
    • (2012) J. Virol. , vol.86 , pp. 1046-1058
    • Samsa, M.M.1    Mondotte, J.A.2    Caramelo, J.J.3    Gamarnik, A.V.4
  • 39
    • 0029684652 scopus 로고    scopus 로고
    • RNA binding properties of core protein of the flavivirus Kunjin
    • Khromykh AA, Westaway EG. 1996. RNA binding properties of core protein of the flavivirus Kunjin. Arch. Virol. 141:685-99
    • (1996) Arch. Virol. , vol.141 , pp. 685-699
    • Khromykh, A.A.1    Westaway, E.G.2
  • 40
    • 78650613867 scopus 로고    scopus 로고
    • Dephosphorylation of WestNile virus capsid protein enhances the processes of nucleocapsid assembly
    • Cheong YK, NgML. 2011. Dephosphorylation of WestNile virus capsid protein enhances the processes of nucleocapsid assembly. Microbes Infect. 13:76-84
    • (2011) Microbes Infect. , vol.13 , pp. 76-84
    • Cheong, Y.K.1    Ng, M.L.2
  • 42
    • 80051788479 scopus 로고    scopus 로고
    • RNAbinding property and RNA chaperone activity of dengue virus core protein and other viral RNA-interacting proteins
    • Pong WL, Huang ZS, Teoh PG, Wang CC, WuHN. 2011.RNAbinding property and RNA chaperone activity of dengue virus core protein and other viral RNA-interacting proteins. FEBS Lett. 585:2575-81
    • (2011) FEBS Lett. , vol.585 , pp. 2575-2581
    • Pong, W.L.1    Huang, Z.S.2    Teoh, P.G.3    Wang, C.C.4    Wu, H.N.5
  • 45
    • 0029163563 scopus 로고
    • RNA chaperones and the RNA folding problem
    • Herschlag D. 1995. RNA chaperones and the RNA folding problem. J. Biol. Chem. 270:20871-74
    • (1995) J. Biol. Chem. , vol.270 , pp. 20871-20874
    • Herschlag, D.1
  • 46
    • 84863877179 scopus 로고    scopus 로고
    • Core protein-mediated 5-3- annealing of the West Nile virus genomic RNA in vitro
    • Ivanyi-Nagy R, Darlix JL. 2012. Core protein-mediated 5-3- annealing of the West Nile virus genomic RNA in vitro. Virus Res. 167:226-35
    • (2012) Virus Res. , vol.167 , pp. 226-235
    • Ivanyi-Nagy, R.1    Darlix, J.L.2
  • 47
    • 0028146784 scopus 로고
    • Processing of the intracellular form of theWestNile virus capsid protein by the viral NS2B-NS3 protease: An in vitro study
    • Yamshchikov VF, Compans RW. 1994. Processing of the intracellular form of theWestNile virus capsid protein by the viral NS2B-NS3 protease: an in vitro study. J. Virol. 68:5765-71
    • (1994) J. Virol. , vol.68 , pp. 5765-5771
    • Yamshchikov, V.F.1    Compans, R.W.2
  • 48
    • 0028304762 scopus 로고
    • NS2B-3 proteinase-mediated processing in the yellow fever virus structural region: In vitro and in vivo studies
    • Amberg SM, Nestorowicz A, McCourt DW, Rice CM. 1994. NS2B-3 proteinase-mediated processing in the yellow fever virus structural region: in vitro and in vivo studies. J. Virol. 68:3794-802
    • (1994) J. Virol. , vol.68 , pp. 3794-3802
    • Amberg, S.M.1    Nestorowicz, A.2    McCourt, D.W.3    Rice, C.M.4
  • 49
    • 77950928603 scopus 로고    scopus 로고
    • A flavivirus signal peptide balances the catalytic activity of two proteases and thereby facilitates virus morphogenesis
    • Lobigs M, Lee E, Ng ML, Pavy M, Lobigs P. 2010. A flavivirus signal peptide balances the catalytic activity of two proteases and thereby facilitates virus morphogenesis. Virology 401:80-89
    • (2010) Virology , vol.401 , pp. 80-89
    • Lobigs, M.1    Lee, E.2    Ng, M.L.3    Pavy, M.4    Lobigs, P.5
  • 50
    • 0031935890 scopus 로고    scopus 로고
    • Signal peptidase cleavage at the flavivirus C-prM junction: Dependence on the viral NS2B-3 protease for efficient processing requires determinants in C, the signal peptide, and prM
    • Stocks CE, Lobigs M. 1998. Signal peptidase cleavage at the flavivirus C-prM junction: dependence on the viral NS2B-3 protease for efficient processing requires determinants in C, the signal peptide, and prM. J. Virol. 72:2141-49
    • (1998) J. Virol. , vol.72 , pp. 2141-2149
    • Stocks, C.E.1    Lobigs, M.2
  • 51
    • 0033986872 scopus 로고    scopus 로고
    • Mutagenesis of the signal sequence of yellow fever virus prM protein: Enhancement of signalase cleavage in vitro is lethal for virus production
    • Lee E, Stocks CE, Amberg SM, Rice CM, Lobigs M. 2000. Mutagenesis of the signal sequence of yellow fever virus prM protein: Enhancement of signalase cleavage in vitro is lethal for virus production. J. Virol. 74:24-32
    • (2000) J. Virol. , vol.74 , pp. 24-32
    • Lee, E.1    Stocks, C.E.2    Amberg, S.M.3    Rice, C.M.4    Lobigs, M.5
  • 52
    • 0345734203 scopus 로고    scopus 로고
    • Inefficient signalase cleavage promotes efficient nucleocapsid incorporation into budding flavivirus membranes
    • Lobigs M, Lee E. 2004. Inefficient signalase cleavage promotes efficient nucleocapsid incorporation into budding flavivirus membranes. J. Virol. 78:178-86
    • (2004) J. Virol. , vol.78 , pp. 178-186
    • Lobigs, M.1    Lee, E.2
  • 53
    • 33846232731 scopus 로고    scopus 로고
    • Structural analysis of viral nucleocapsids by subtraction of partial projections
    • Zhang Y, Kostyuchenko VA, Rossmann MG. 2007. Structural analysis of viral nucleocapsids by subtraction of partial projections. J. Struct. Biol. 157:356-64
    • (2007) J. Struct. Biol. , vol.157 , pp. 356-364
    • Zhang, Y.1    Kostyuchenko, V.A.2    Rossmann, M.G.3
  • 54
    • 0029888374 scopus 로고    scopus 로고
    • Recombinant subviral particles from tick-borne encephalitis virus are fusogenic and provide a model system for studying flavivirus envelope glycoprotein functions
    • Schalich J, Allison SL, Stiasny K, Mandl CW, Kunz C, Heinz FX. 1996. Recombinant subviral particles from tick-borne encephalitis virus are fusogenic and provide a model system for studying flavivirus envelope glycoprotein functions. J. Virol. 70:4549-57
    • (1996) J. Virol. , vol.70 , pp. 4549-4557
    • Schalich, J.1    Allison, S.L.2    Stiasny, K.3    Mandl, C.W.4    Kunz, C.5    Heinz, F.X.6
  • 55
    • 0035032324 scopus 로고    scopus 로고
    • Coupling between replication and packaging of flavivirus RNA: Evidence derived from the use of DNA-based full-length cDNA clones of Kunjin virus
    • Khromykh AA, Varnavski AN, Sedlak PL, Westaway EG. 2001. Coupling between replication and packaging of flavivirus RNA: evidence derived from the use of DNA-based full-length cDNA clones of Kunjin virus. J. Virol. 75:4633-40
    • (2001) J. Virol. , vol.75 , pp. 4633-4640
    • Khromykh, A.A.1    Varnavski, A.N.2    Sedlak, P.L.3    Westaway, E.G.4
  • 56
    • 33750690231 scopus 로고    scopus 로고
    • Translation of the flavivirus Kunjin NS3 gene in cis but not its RNA sequence or secondary structure is essential for efficient RNA packaging
    • Pijlman GP, Kondratieva N, Khromykh AA. 2006. Translation of the flavivirus Kunjin NS3 gene in cis but not its RNA sequence or secondary structure is essential for efficient RNA packaging. J. Virol. 80:11255-64
    • (2006) J. Virol. , vol.80 , pp. 11255-11264
    • Pijlman, G.P.1    Kondratieva, N.2    Khromykh, A.A.3
  • 57
    • 41149101538 scopus 로고    scopus 로고
    • Yellow fever virus NS3 plays an essential role in virus assembly independent of its known enzymatic functions
    • Patkar CG, Kuhn RJ. 2008. Yellow fever virus NS3 plays an essential role in virus assembly independent of its known enzymatic functions. J. Virol. 82:3342-52
    • (2008) J. Virol. , vol.82 , pp. 3342-3352
    • Patkar, C.G.1    Kuhn, R.J.2
  • 58
    • 84971482981 scopus 로고    scopus 로고
    • A prolinerich N-terminal region of the dengue virus NS3 is crucial for infectious particle production
    • Gebhard LG, Iglesias NG, Byk LA, Filomatori CV, De Maio FA, Gamarnik AV. 2016. A prolinerich N-terminal region of the dengue virus NS3 is crucial for infectious particle production. J. Virol. 90:5451-61
    • (2016) J. Virol. , vol.90 , pp. 5451-5461
    • Gebhard, L.G.1    Iglesias, N.G.2    Byk, L.A.3    Filomatori, C.V.4    De Maio, F.A.5    Gamarnik, A.V.6
  • 59
    • 0036232747 scopus 로고    scopus 로고
    • Mutations in the yellow fever virus nonstructural protein NS2A selectively block production of infectious particles
    • Kummerer BM, Rice CM. 2002. Mutations in the yellow fever virus nonstructural protein NS2A selectively block production of infectious particles. J. Virol. 76:4773-84
    • (2002) J. Virol. , vol.76 , pp. 4773-4784
    • Kummerer, B.M.1    Rice, C.M.2
  • 60
    • 84948988051 scopus 로고    scopus 로고
    • Dengue virus nonstructural protein 1 modulates infectious particle production via interaction with the structural proteins
    • Scaturro P, Cortese M, Chatel-Chaix L, Fischl W, Bartenschlager R. 2015. Dengue virus nonstructural protein 1 modulates infectious particle production via interaction with the structural proteins. PLOS Pathog. 11:e1005277
    • (2015) PLOS Pathog. , vol.11 , pp. e1005277
    • Scaturro, P.1    Cortese, M.2    Chatel-Chaix, L.3    Fischl, W.4    Bartenschlager, R.5
  • 61
    • 84923166254 scopus 로고    scopus 로고
    • Overlapping local and long-range RNA-RNA interactions modulate dengue virus genome cyclization and replication
    • de Borba L, Villordo SM, Iglesias NG, Filomatori CV, Gebhard LG, Gamarnik AV. 2015. Overlapping local and long-range RNA-RNA interactions modulate dengue virus genome cyclization and replication. J. Virol. 89:3430-37
    • (2015) J. Virol. , vol.89 , pp. 3430-3437
    • De Borba, L.1    Villordo, S.M.2    Iglesias, N.G.3    Filomatori, C.V.4    Gebhard, L.G.5    Gamarnik, A.V.6
  • 62
    • 59749084360 scopus 로고    scopus 로고
    • Genome cyclization as strategy for flavivirus RNA replication
    • Villordo SM, Gamarnik AV. 2009. Genome cyclization as strategy for flavivirus RNA replication. Virus Res. 139:230-39
    • (2009) Virus Res. , vol.139 , pp. 230-239
    • Villordo, S.M.1    Gamarnik, A.V.2
  • 63
    • 50349101877 scopus 로고    scopus 로고
    • The capsid-coding region hairpin element (cHP) is a critical determinant of dengue virus and West Nile virus RNA synthesis
    • Clyde K, Barrera J, Harris E. 2008. The capsid-coding region hairpin element (cHP) is a critical determinant of dengue virus and West Nile virus RNA synthesis. Virology 379:314-23
    • (2008) Virology , vol.379 , pp. 314-323
    • Clyde, K.1    Barrera, J.2    Harris, E.3
  • 64
    • 84878526763 scopus 로고    scopus 로고
    • Novel cis-acting element within the capsid-coding region enhances flavivirus viral-RNA replication by regulating genome cyclization
    • Liu ZY, Li XF, JiangT, Deng YQ, Zhao H, et al. 2013. Novel cis-acting element within the capsid-coding region enhances flavivirus viral-RNA replication by regulating genome cyclization. J. Virol. 87:6804-18
    • (2013) J. Virol. , vol.87 , pp. 6804-6818
    • Liu, Z.Y.1    Li, X.F.2    Jiang, T.3    Deng, Y.Q.4    Zhao, H.5
  • 65
    • 34249929993 scopus 로고    scopus 로고
    • Functional requirements of the yellow fever virus capsid protein
    • Patkar CG, Jones CT, Chang YH, Warrier R, Kuhn RJ. 2007. Functional requirements of the yellow fever virus capsid protein. J. Virol. 81:6471-81
    • (2007) J. Virol. , vol.81 , pp. 6471-6481
    • Patkar, C.G.1    Jones, C.T.2    Chang, Y.H.3    Warrier, R.4    Kuhn, R.J.5
  • 66
    • 0036118270 scopus 로고    scopus 로고
    • Capsid protein C of tick-borne encephalitis virus tolerates large internal deletions and is a favorable target for attenuation of virulence
    • Kofler RM, Heinz FX, Mandl CW. 2002. Capsid protein C of tick-borne encephalitis virus tolerates large internal deletions and is a favorable target for attenuation of virulence. J. Virol. 76:3534-43
    • (2002) J. Virol. , vol.76 , pp. 3534-3543
    • Kofler, R.M.1    Heinz, F.X.2    Mandl, C.W.3
  • 67
    • 34248202492 scopus 로고    scopus 로고
    • Attenuated dengue 2 viruses with deletions in capsid protein derived from an infectious full-length cDNA clone
    • ZhuW, Qin C, Chen S, Jiang T, YuM, et al. 2007. Attenuated dengue 2 viruses with deletions in capsid protein derived from an infectious full-length cDNA clone. Virus Res. 126:226-32
    • (2007) Virus Res. , vol.126 , pp. 226-232
    • Zhu, W.1    Qin, C.2    Chen, S.3    Jiang, T.4    Yu, M.5
  • 68
    • 66149154330 scopus 로고    scopus 로고
    • Helices α2 and α3 ofWest Nile virus capsid protein are dispensable for assembly of infectious virions
    • Schlick P, Taucher C, Schittl B, Tran JL, Kofler RM, et al. 2009. Helices α2 and α3 ofWest Nile virus capsid protein are dispensable for assembly of infectious virions. J. Virol. 83:5581-91
    • (2009) J. Virol. , vol.83 , pp. 5581-5591
    • Schlick, P.1    Taucher, C.2    Schittl, B.3    Tran, J.L.4    Kofler, R.M.5
  • 69
    • 0037213602 scopus 로고    scopus 로고
    • Spontaneous mutations restore the viability of tick-borne encephalitis virus mutants with large deletions in protein C
    • Kofler RM, Leitner A, O'Riordain G, Heinz FX, Mandl CW. 2003. Spontaneous mutations restore the viability of tick-borne encephalitis virus mutants with large deletions in protein C. J. Virol. 77:443-51
    • (2003) J. Virol. , vol.77 , pp. 443-451
    • Kofler, R.M.1    Leitner, A.2    O'Riordain, G.3    Heinz, F.X.4    Mandl, C.W.5
  • 70
    • 0026438869 scopus 로고
    • Nuclear localization of dengue 2 virus core protein detected with monoclonal antibodies
    • Bulich R, Aaskov JG. 1992. Nuclear localization of dengue 2 virus core protein detected with monoclonal antibodies. J. Gen. Virol. 73(Pt. 11):2999-3003
    • (1992) J. Gen. Virol. , vol.73 , pp. 2999-3003
    • Bulich, R.1    Aaskov, J.G.2
  • 71
    • 0024318343 scopus 로고
    • Detection of dengue 4 virus core protein in the nucleus I. A monoclonal antibody to dengue 4 virus reacts with the antigen in the nucleus and cytoplasm
    • Tadano M, Makino Y, Fukunaga T, Okuno Y, Fukai K. 1989. Detection of dengue 4 virus core protein in the nucleus. I. A monoclonal antibody to dengue 4 virus reacts with the antigen in the nucleus and cytoplasm. J. Gen. Virol. 70(Pt. 6):1409-15
    • (1989) J. Gen. Virol , vol.70 , pp. 1409-1415
    • Tadano, M.1    Makino, Y.2    Fukunaga, T.3    Okuno, Y.4    Fukai, K.5
  • 72
    • 0036932907 scopus 로고    scopus 로고
    • Intracellular localization and determination of a nuclear localization signal of the core protein of dengue virus
    • Wang SH, Syu WJ, Huang KJ, Lei HY, Yao CW, et al. 2002. Intracellular localization and determination of a nuclear localization signal of the core protein of dengue virus. J. Gen. Virol. 83:3093-102
    • (2002) J. Gen. Virol. , vol.83 , pp. 3093-3102
    • Wang, S.H.1    Syu, W.J.2    Huang, K.J.3    Lei, H.Y.4    Yao, C.W.5
  • 73
    • 72949113840 scopus 로고    scopus 로고
    • Nuclear localization of dengue virus capsid protein is required for DAXX interaction and apoptosis
    • Netsawang J, Noisakran S, Puttikhunt C, Kasinrerk W, WongwiwatW, et al. 2010. Nuclear localization of dengue virus capsid protein is required for DAXX interaction and apoptosis. Virus Res. 147:275-83
    • (2010) Virus Res. , vol.147 , pp. 275-283
    • Netsawang, J.1    Noisakran, S.2    Puttikhunt, C.3    Kasinrerk, W.4    Wongwiwat, W.5
  • 74
    • 84939777157 scopus 로고    scopus 로고
    • Dengue virus uses a non-canonical function of the host GBF1-Arf-COPI system for capsid protein accumulation on lipid droplets
    • Iglesias N, Mondotte JA, Byk LA, DeMaio FA, SamsaMM, et al. 2015. Dengue virus uses a non-canonical function of the host GBF1-Arf-COPI system for capsid protein accumulation on lipid droplets. Traffic 16:962-77
    • (2015) Traffic , vol.16 , pp. 962-977
    • Iglesias, N.1    Mondotte, J.A.2    Byk, L.A.3    DeMaio, F.A.4    Samsa, M.M.5
  • 75
    • 44649173963 scopus 로고    scopus 로고
    • Multiple regions in dengue virus capsid protein contribute to nuclear localization during virus infection
    • Sangiambut S, Keelapang P, Aaskov J, PuttikhuntC, Kasinrerk W, et al. 2008. Multiple regions in dengue virus capsid protein contribute to nuclear localization during virus infection. J. Gen. Virol. 89:1254-64
    • (2008) J. Gen. Virol. , vol.89 , pp. 1254-1264
    • Sangiambut, S.1    Keelapang, P.2    Aaskov, J.3    Puttikhunt, C.4    Kasinrerk, W.5
  • 76
    • 0034767341 scopus 로고    scopus 로고
    • Assembly and maturation of the flavivirus Kunjin virus appear to occur in the rough endoplasmic reticulum and along the secretory pathway, respectively
    • Mackenzie JM, Westaway EG. 2001. Assembly and maturation of the flavivirus Kunjin virus appear to occur in the rough endoplasmic reticulum and along the secretory pathway, respectively. J. Virol. 75:10787-99
    • (2001) J. Virol. , vol.75 , pp. 10787-10799
    • Mackenzie, J.M.1    Westaway, E.G.2
  • 78
    • 20044394203 scopus 로고    scopus 로고
    • Nuclear localization of Japanese encephalitis virus core protein enhances viral replication
    • Mori Y, Okabayashi T, Yamashita T, Zhao Z, Wakita T, et al. 2005. Nuclear localization of Japanese encephalitis virus core protein enhances viral replication. J. Virol. 79:3448-58
    • (2005) J. Virol. , vol.79 , pp. 3448-3458
    • Mori, Y.1    Okabayashi, T.2    Yamashita, T.3    Zhao, Z.4    Wakita, T.5
  • 79
    • 0031582633 scopus 로고    scopus 로고
    • Proteins C and NS4B of the flavivirus Kunjin translocate independently into the nucleus
    • Westaway EG, Khromykh AA, Kenney MT, Mackenzie JM, Jones MK. 1997. Proteins C and NS4B of the flavivirus Kunjin translocate independently into the nucleus. Virology 234:31-41
    • (1997) Virology , vol.234 , pp. 31-41
    • Westaway, E.G.1    Khromykh, A.A.2    Kenney, M.T.3    Mackenzie, J.M.4    Jones, M.K.5
  • 80
    • 70349124965 scopus 로고    scopus 로고
    • Specific interaction of capsid protein and importin-α/β influencesWest Nile virus production
    • Bhuvanakantham R, ChongMK, Ng ML. 2009. Specific interaction of capsid protein and importin-α/β influencesWest Nile virus production. Biochem. Biophys. Res. Commun. 389:63-69
    • (2009) Biochem. Biophys. Res. Commun. , vol.389 , pp. 63-69
    • Bhuvanakantham, R.1    Chong, M.K.2    Ng, M.L.3
  • 81
    • 77954955663 scopus 로고    scopus 로고
    • West Nile virus capsid protein interactionwith importin and HDM2 protein is regulated by protein kinase C-mediated phosphorylation
    • Bhuvanakantham R, Cheong YK, NgML. 2010. West Nile virus capsid protein interactionwith importin and HDM2 protein is regulated by protein kinase C-mediated phosphorylation. Microbes Infect. 12:615-25
    • (2010) Microbes Infect. , vol.12 , pp. 615-625
    • Bhuvanakantham, R.1    Cheong, Y.K.2    Ng, M.L.3
  • 82
    • 84862165670 scopus 로고    scopus 로고
    • The disordered N-terminal region of dengue virus capsid protein contains a lipid-droplet-binding motif
    • Martins IC, Gomes-Neto F, Faustino AF, Carvalho FA, Carneiro FA, et al. 2012. The disordered N-terminal region of dengue virus capsid protein contains a lipid-droplet-binding motif. Biochem. J. 444:405-15
    • (2012) Biochem. J. , vol.444 , pp. 405-415
    • Martins, I.C.1    Gomes-Neto, F.2    Faustino, A.F.3    Carvalho, F.A.4    Carneiro, F.A.5
  • 83
    • 84923345392 scopus 로고    scopus 로고
    • Understanding dengue virus capsid protein disordered N-terminus and pep14-23-based inhibition
    • Faustino AF, Guerra GM, Huber RG, Hollmann A, Domingues MM, et al. 2015. Understanding dengue virus capsid protein disordered N-terminus and pep14-23-based inhibition. ACS Chem. Biol. 10:517-26
    • (2015) ACS Chem. Biol. , vol.10 , pp. 517-526
    • Faustino, A.F.1    Guerra, G.M.2    Huber, R.G.3    Hollmann, A.4    Domingues, M.M.5
  • 84
    • 84857094659 scopus 로고    scopus 로고
    • Dengue virus capsid protein binding to hepatic lipid droplets (LD) is potassium ion dependent and is mediated by LD surface proteins
    • Carvalho FA, Carneiro FA, Martins IC, Assuncao-Miranda I, Faustino AF, et al. 2012. Dengue virus capsid protein binding to hepatic lipid droplets (LD) is potassium ion dependent and is mediated by LD surface proteins. J. Virol. 86:2096-108
    • (2012) J. Virol. , vol.86 , pp. 2096-2108
    • Carvalho, F.A.1    Carneiro, F.A.2    Martins, I.C.3    Assuncao-Miranda, I.4    Faustino, A.F.5
  • 85
    • 33748598240 scopus 로고    scopus 로고
    • The lipid-droplet proteome reveals that droplets are a protein-storage depot
    • Cermelli S, Guo Y, Gross SP, Welte MA. 2006. The lipid-droplet proteome reveals that droplets are a protein-storage depot. Curr. Biol. 16:1783-95
    • (2006) Curr. Biol. , vol.16 , pp. 1783-1795
    • Cermelli, S.1    Guo, Y.2    Gross, S.P.3    Welte, M.A.4
  • 86
    • 33646168160 scopus 로고    scopus 로고
    • Lipid droplets: A unified view of a dynamic organelle
    • Martin S, Parton RG. 2006. Lipid droplets: a unified view of a dynamic organelle. Nat. Rev. Mol. Cell Biol. 7:373-78
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 373-378
    • Martin, S.1    Parton, R.G.2
  • 87
    • 84861913952 scopus 로고    scopus 로고
    • Lipid droplets and cellular lipid metabolism
    • Walther TC, Farese RV Jr. 2012. Lipid droplets and cellular lipid metabolism. Annu. Rev. Biochem. 81:687-714
    • (2012) Annu. Rev. Biochem. , vol.81 , pp. 687-714
    • Walther, T.C.1    Farese, R.V.2
  • 88
    • 77949524635 scopus 로고    scopus 로고
    • Proteomic insights into an expanded cellular role for cytoplasmic lipid droplets
    • Hodges BD, Wu CC. 2010. Proteomic insights into an expanded cellular role for cytoplasmic lipid droplets. J. Lipid Res. 51:262-73
    • (2010) J. Lipid Res. , vol.51 , pp. 262-273
    • Hodges, B.D.1    Wu, C.C.2
  • 89
    • 84867654401 scopus 로고    scopus 로고
    • Emerging roles for lipid droplets in immunity and host-pathogen interactions
    • Saka HA, Valdivia R. 2012. Emerging roles for lipid droplets in immunity and host-pathogen interactions. Annu. Rev. Cell Dev. Biol. 28:411-37
    • (2012) Annu. Rev. Cell Dev. Biol. , vol.28 , pp. 411-437
    • Saka, H.A.1    Valdivia, R.2
  • 90
    • 75149134774 scopus 로고    scopus 로고
    • Contribution of macrophagemigration inhibitory factor to the pathogenesis of dengue virus infection
    • Assuncao-Miranda I, Amaral FA, Bozza FA, Fagundes CT, Sousa LP, et al. 2010. Contribution of macrophagemigration inhibitory factor to the pathogenesis of dengue virus infection. FASEB J. 24:218-28
    • (2010) FASEB J. , vol.24 , pp. 218-228
    • Assuncao-Miranda, I.1    Amaral, F.A.2    Bozza, F.A.3    Fagundes, C.T.4    Sousa, L.P.5
  • 91
    • 84906971635 scopus 로고    scopus 로고
    • Characterization of the mode of action of a potent dengue virus capsid inhibitor
    • Scaturro P, Trist IM, Paul D, Kumar A, Acosta EG, et al. 2014. Characterization of the mode of action of a potent dengue virus capsid inhibitor. J. Virol. 88:11540-55
    • (2014) J. Virol. , vol.88 , pp. 11540-11555
    • Scaturro, P.1    Trist, I.M.2    Paul, D.3    Kumar, A.4    Acosta, E.G.5
  • 92
    • 84901296162 scopus 로고    scopus 로고
    • Rab18 facilitates dengue virus infection by targeting fatty acid synthase to sites of viral replication
    • Tang WC, Lin RJ, Liao CL, Lin YL. 2014. Rab18 facilitates dengue virus infection by targeting fatty acid synthase to sites of viral replication. J. Virol. 88:6793-804
    • (2014) J. Virol. , vol.88 , pp. 6793-6804
    • Tang, W.C.1    Lin, R.J.2    Liao, C.L.3    Lin, Y.L.4
  • 93
    • 77958100661 scopus 로고    scopus 로고
    • Dengue virus nonstructural protein 3 redistributes fatty acid synthase to sites of viral replication and increases cellular fatty acid synthesis
    • Heaton NS, Perera R, BergerKL, Khadka S, Lacount DJ, et al. 2010. Dengue virus nonstructural protein 3 redistributes fatty acid synthase to sites of viral replication and increases cellular fatty acid synthesis. PNAS 107:17345-50
    • (2010) PNAS , vol.107 , pp. 17345-17350
    • Heaton, N.S.1    Perera, R.2    Berger, K.L.3    Khadka, S.4    Lacount, D.J.5
  • 94
    • 78349237370 scopus 로고    scopus 로고
    • Dengue virus-induced autophagy regulates lipid metabolism
    • Heaton NS, Randall G. 2010. Dengue virus-induced autophagy regulates lipid metabolism. Cell Host Microbe 8:422-32
    • (2010) Cell Host Microbe , vol.8 , pp. 422-432
    • Heaton, N.S.1    Randall, G.2
  • 95
    • 84873031729 scopus 로고    scopus 로고
    • Inhibition of cellular autophagy deranges dengue virion maturation
    • Mateo R, Nagamine CM, Spagnolo J, Mendez E, Rahe M, et al. 2013. Inhibition of cellular autophagy deranges dengue virion maturation. J. Virol. 87:1312-21
    • (2013) J. Virol. , vol.87 , pp. 1312-1321
    • Mateo, R.1    Nagamine, C.M.2    Spagnolo, J.3    Mendez, E.4    Rahe, M.5
  • 96
    • 84856075144 scopus 로고    scopus 로고
    • Emerging role of lipid droplets in host/pathogen interactions
    • Herker E, Ott M. 2012. Emerging role of lipid droplets in host/pathogen interactions. J. Biol. Chem. 287:2280-87
    • (2012) J. Biol. Chem. , vol.287 , pp. 2280-2287
    • Herker, E.1    Ott, M.2
  • 98
    • 0030218609 scopus 로고    scopus 로고
    • Characterization of cell lines allowing tightly regulated expression of hepatitis C virus core protein
    • Moradpour D, Englert C, Wakita T, Wands JR. 1996. Characterization of cell lines allowing tightly regulated expression of hepatitis C virus core protein. Virology 222:51-63
    • (1996) Virology , vol.222 , pp. 51-63
    • Moradpour, D.1    Englert, C.2    Wakita, T.3    Wands, J.R.4
  • 99
    • 11144357274 scopus 로고    scopus 로고
    • Hepatitis C virus core protein shows a cytoplasmic localization and associates to cellular lipid storage droplets
    • Barba G, Harper F, Harada T, Kohara M, Goulinet S, et al. 1997. Hepatitis C virus core protein shows a cytoplasmic localization and associates to cellular lipid storage droplets. PNAS 94:1200-5
    • (1997) PNAS , vol.94 , pp. 1200-1205
    • Barba, G.1    Harper, F.2    Harada, T.3    Kohara, M.4    Goulinet, S.5
  • 100
    • 0033880575 scopus 로고    scopus 로고
    • Sequence motifs required for lipid droplet association and protein stability are unique to the hepatitis C virus core protein
    • Hope RG, McLauchlan J. 2000. Sequence motifs required for lipid droplet association and protein stability are unique to the hepatitis C virus core protein. J. Gen. Virol. 81:1913-25
    • (2000) J. Gen. Virol. , vol.81 , pp. 1913-1925
    • Hope, R.G.1    McLauchlan, J.2
  • 101
    • 0036683052 scopus 로고    scopus 로고
    • Intramembrane proteolysis promotes trafficking of hepatitis C virus core protein to lipid droplets
    • McLauchlan J, Lemberg MK, Hope G, Martoglio B. 2002. Intramembrane proteolysis promotes trafficking of hepatitis C virus core protein to lipid droplets. EMBO J. 21:3980-88
    • (2002) EMBO J. , vol.21 , pp. 3980-3988
    • McLauchlan, J.1    Lemberg, M.K.2    Hope, G.3    Martoglio, B.4
  • 102
    • 37549005607 scopus 로고    scopus 로고
    • The lipid droplet binding domain of hepatitis C virus core protein is a major determinant for efficient virus assembly
    • Shavinskaya A, Boulant S, Penin F, McLauchlan J, Bartenschlager R. 2007. The lipid droplet binding domain of hepatitis C virus core protein is a major determinant for efficient virus assembly. J. Biol. Chem. 282:37158-69
    • (2007) J. Biol. Chem. , vol.282 , pp. 37158-37169
    • Shavinskaya, A.1    Boulant, S.2    Penin, F.3    McLauchlan, J.4    Bartenschlager, R.5
  • 103
    • 34547592075 scopus 로고    scopus 로고
    • Disrupting the association of hepatitis C virus core proteinwith lipid droplets correlates with a loss in production of infectious virus
    • Boulant S, Targett-Adams P, McLauchlan J. 2007. Disrupting the association of hepatitis C virus core proteinwith lipid droplets correlates with a loss in production of infectious virus. J. Gen. Virol. 88:2204-13
    • (2007) J. Gen. Virol. , vol.88 , pp. 2204-2213
    • Boulant, S.1    Targett-Adams, P.2    McLauchlan, J.3
  • 104
    • 47649114826 scopus 로고    scopus 로고
    • Hepatitis C virus core protein induces lipid droplet redistribution in a microtubule-and dynein-dependent manner
    • Boulant S, Douglas MW, Moody L, Budkowska A, Targett-Adams P, McLauchlan J. 2008. Hepatitis C virus core protein induces lipid droplet redistribution in a microtubule-and dynein-dependent manner. Traffic 9:1268-82
    • (2008) Traffic , vol.9 , pp. 1268-1282
    • Boulant, S.1    Douglas, M.W.2    Moody, L.3    Budkowska, A.4    Targett-Adams, P.5    McLauchlan, J.6
  • 105
    • 34548316984 scopus 로고    scopus 로고
    • The lipid droplet is an important organelle for hepatitis C virus production
    • Miyanari Y, Atsuzawa K, Usuda N, Watashi K, Hishiki T, et al. 2007. The lipid droplet is an important organelle for hepatitis C virus production. Nat. Cell Biol. 9:1089-97
    • (2007) Nat. Cell Biol. , vol.9 , pp. 1089-1097
    • Miyanari, Y.1    Atsuzawa, K.2    Usuda, N.3    Watashi, K.4    Hishiki, T.5
  • 106
    • 33746830410 scopus 로고    scopus 로고
    • Structural determinants that target the hepatitis C virus core protein to lipid droplets
    • Boulant S, Montserret R, Hope RG, Ratinier M, Targett-Adams P, et al. 2006. Structural determinants that target the hepatitis C virus core protein to lipid droplets. J. Biol. Chem. 281:22236-47
    • (2006) J. Biol. Chem. , vol.281 , pp. 22236-22247
    • Boulant, S.1    Montserret, R.2    Hope, R.G.3    Ratinier, M.4    Targett-Adams, P.5
  • 107
    • 80055073369 scopus 로고    scopus 로고
    • Trafficking of hepatitisCvirus core protein during virus particle assembly
    • Counihan NA, Rawlinson SM, Lindenbach BD. 2011. Trafficking of hepatitisCvirus core protein during virus particle assembly. PLOS Pathog. 7:e1002302
    • (2011) PLOS Pathog. , vol.7 , pp. e1002302
    • Counihan, N.A.1    Rawlinson, S.M.2    Lindenbach, B.D.3
  • 108
    • 84919793281 scopus 로고    scopus 로고
    • The hepatitis C virus core protein inhibits adipose triglyceride lipase (ATGL)-mediated lipid mobilization and enhances the ATGL interaction with comparative gene identification 58 (CGI-58) and lipid droplets
    • Camus G, Schweiger M, Herker E, Harris C, Kondratowicz AS, et al. 2014. The hepatitis C virus core protein inhibits adipose triglyceride lipase (ATGL)-mediated lipid mobilization and enhances the ATGL interaction with comparative gene identification 58 (CGI-58) and lipid droplets. J. Biol. Chem. 289:35770-80
    • (2014) J. Biol. Chem. , vol.289 , pp. 35770-35780
    • Camus, G.1    Schweiger, M.2    Herker, E.3    Harris, C.4    Kondratowicz, A.S.5
  • 110
    • 44449095056 scopus 로고    scopus 로고
    • Functional genomic screen reveals genes involved in lipid-droplet formation and utilization
    • Guo Y, Walther TC, Rao M, Stuurman N, Goshima G, et al. 2008. Functional genomic screen reveals genes involved in lipid-droplet formation and utilization. Nature 453:657-61
    • (2008) Nature , vol.453 , pp. 657-661
    • Guo, Y.1    Walther, T.C.2    Rao, M.3    Stuurman, N.4    Goshima, G.5
  • 113
    • 80052361705 scopus 로고    scopus 로고
    • Dengue virus capsid protein binds core histones and inhibits nucleosome formation in human liver cells
    • Colpitts TM, Barthel S, Wang P, Fikrig E. 2011. Dengue virus capsid protein binds core histones and inhibits nucleosome formation in human liver cells. PLOS ONE 6:e24365
    • (2011) PLOS ONE , vol.6 , pp. e24365
    • Colpitts, T.M.1    Barthel, S.2    Wang, P.3    Fikrig, E.4
  • 114
    • 0034761111 scopus 로고    scopus 로고
    • The heterogeneous nuclear ribonucleoprotein K (hnRNP K) interacts with dengue virus core protein
    • Chang CJ, Luh HW, Wang SH, Lin HJ, Lee SC, Hu ST. 2001. The heterogeneous nuclear ribonucleoprotein K (hnRNP K) interacts with dengue virus core protein. DNA Cell Biol. 20:569-77
    • (2001) DNA Cell Biol. , vol.20 , pp. 569-577
    • Chang, C.J.1    Luh, H.W.2    Wang, S.H.3    Lin, H.J.4    Lee, S.C.5    Hu, S.T.6
  • 115
    • 84888026992 scopus 로고    scopus 로고
    • Nucleolin interacts with the dengue virus capsid protein and plays a role in formation of infectious virus particles
    • Balinsky CA, Schmeisser H, Ganesan S, Singh K, Pierson TC, Zoon KC. 2013. Nucleolin interacts with the dengue virus capsid protein and plays a role in formation of infectious virus particles. J. Virol. 87:13094-106
    • (2013) J. Virol. , vol.87 , pp. 13094-13106
    • Balinsky, C.A.1    Schmeisser, H.2    Ganesan, S.3    Singh, K.4    Pierson, T.C.5    Zoon, K.C.6
  • 116
    • 84862814793 scopus 로고    scopus 로고
    • Dengue virus utilizes calcium modulating cyclophilinbinding ligand to subvert apoptosis
    • Li J, Huang R, Liao W, Chen Z, Zhang S. 2012. Dengue virus utilizes calcium modulating cyclophilinbinding ligand to subvert apoptosis. Biochem. Biophys. Res. Commun. 418:622-27
    • (2012) Biochem. Biophys. Res. Commun. , vol.418 , pp. 622-627
    • Li, J.1    Huang, R.2    Liao, W.3    Chen, Z.4    Zhang, S.5
  • 117
    • 0036917561 scopus 로고    scopus 로고
    • Induction of inflammation by West Nile virus capsid through the caspase-9 apoptotic pathway
    • Yang JS, Ramanathan MP, Muthumani K, Choo AY, Jin SH, et al. 2002. Induction of inflammation by West Nile virus capsid through the caspase-9 apoptotic pathway. Emerg. Infect. Dis. 8:1379-84
    • (2002) Emerg. Infect. Dis. , vol.8 , pp. 1379-1384
    • Yang, J.S.1    Ramanathan, M.P.2    Muthumani, K.3    Choo, A.Y.4    Jin, S.H.5
  • 118
    • 36949005877 scopus 로고    scopus 로고
    • West Nile virus capsid protein induces p53-mediated apoptosis via the sequestration of HDM2 to the nucleolus
    • Yang MR, Lee SR, Oh W, Lee EW, Yeh JY, et al. 2008. West Nile virus capsid protein induces p53-mediated apoptosis via the sequestration of HDM2 to the nucleolus. Cell Microbiol. 10:165-76
    • (2008) Cell Microbiol. , vol.10 , pp. 165-176
    • Yang, M.R.1    Lee, S.R.2    Oh, W.3    Lee, E.W.4    Yeh, J.Y.5
  • 119
    • 34848850994 scopus 로고    scopus 로고
    • West Nile virus-induced neuroinflammation: Glial infection and capsid protein-mediated neurovirulence
    • van Marle G, Antony J, Ostermann H, Dunham C, Hunt T, et al. 2007. West Nile virus-induced neuroinflammation: glial infection and capsid protein-mediated neurovirulence. J. Virol. 81:10933-49
    • (2007) J. Virol. , vol.81 , pp. 10933-10949
    • Van Marle, G.1    Antony, J.2    Ostermann, H.3    Dunham, C.4    Hunt, T.5
  • 120
    • 77954263501 scopus 로고    scopus 로고
    • Human Sec 3 protein is a novel transcriptional and translational repressor of flavivirus
    • Bhuvanakantham R, Li J, Tan TT, Ng ML. 2010. Human Sec 3 protein is a novel transcriptional and translational repressor of flavivirus. Cell Microbiol. 12:453-72
    • (2010) Cell Microbiol. , vol.12 , pp. 453-472
    • Bhuvanakantham, R.1    Li, J.2    Tan, T.T.3    Ng, M.L.4
  • 121
    • 84884699555 scopus 로고    scopus 로고
    • West Nile virus and dengue virus capsid protein negates the antiviral activity of human Sec 3 protein through the proteasome pathway
    • Bhuvanakantham R, Ng ML. 2013. West Nile virus and dengue virus capsid protein negates the antiviral activity of human Sec 3 protein through the proteasome pathway. Cell Microbiol. 15:1688-706
    • (2013) Cell Microbiol. , vol.15 , pp. 1688-1706
    • Bhuvanakantham, R.1    Ng, M.L.2
  • 122
    • 33749559162 scopus 로고    scopus 로고
    • Jab1 mediates cytoplasmic localization and degradation ofWest Nile virus capsid protein
    • Oh W, Yang MR, Lee EW, Park KM, Pyo S, et al. 2006. Jab1 mediates cytoplasmic localization and degradation ofWest Nile virus capsid protein. J. Biol. Chem. 281:30166-74
    • (2006) J. Biol. Chem. , vol.281 , pp. 30166-30174
    • Oh, W.1    Yang, M.R.2    Lee, E.W.3    Park, K.M.4    Pyo, S.5
  • 123
    • 34848917602 scopus 로고    scopus 로고
    • Interactions between theWest Nile virus capsid protein and the host cell-encoded phosphatase inhibitor, I2PP2A
    • Hunt TA, Urbanowski MD, Kakani K, Law LM, Brinton MA, Hobman TC. 2007. Interactions between theWest Nile virus capsid protein and the host cell-encoded phosphatase inhibitor, I2PP2A. Cell Microbiol. 9:2756-66
    • (2007) Cell Microbiol. , vol.9 , pp. 2756-2766
    • Hunt, T.A.1    Urbanowski, M.D.2    Kakani, K.3    Law, L.M.4    Brinton, M.A.5    Hobman, T.C.6
  • 124
    • 79956115023 scopus 로고    scopus 로고
    • The capsid-binding nucleolar helicase DDX56 is important for infectivity ofWest Nile virus
    • Xu Z, Anderson R, Hobman TC. 2011. The capsid-binding nucleolar helicase DDX56 is important for infectivity ofWest Nile virus. J. Virol. 85:5571-80
    • (2011) J. Virol. , vol.85 , pp. 5571-5580
    • Xu, Z.1    Anderson, R.2    Hobman, T.C.3
  • 125
    • 84866181965 scopus 로고    scopus 로고
    • The helicase activity of DDX56 is required for its role in assembly of infectious West Nile virus particles
    • Xu Z, Hobman TC. 2012. The helicase activity of DDX56 is required for its role in assembly of infectious West Nile virus particles. Virology 433:226-35
    • (2012) Virology , vol.433 , pp. 226-235
    • Xu, Z.1    Hobman, T.C.2
  • 127
    • 84871954468 scopus 로고    scopus 로고
    • Japanese encephalitis virus core protein inhibits stress granule formation through an interaction with Caprin-1 and facilitates viral propagation
    • Katoh H, Okamoto T, Fukuhara T, Kambara H, Morita E, et al. 2013. Japanese encephalitis virus core protein inhibits stress granule formation through an interaction with Caprin-1 and facilitates viral propagation. J. Virol. 87:489-502
    • (2013) J. Virol. , vol.87 , pp. 489-502
    • Katoh, H.1    Okamoto, T.2    Fukuhara, T.3    Kambara, H.4    Morita, E.5
  • 128
    • 84949844295 scopus 로고    scopus 로고
    • Flavivirus infection impairs peroxisome biogenesis and early antiviral signaling
    • You J, Hou S, Malik-Soni N, Xu Z, Kumar A, et al. 2015. Flavivirus infection impairs peroxisome biogenesis and early antiviral signaling. J. Virol. 89:12349-61
    • (2015) J. Virol. , vol.89 , pp. 12349-12361
    • You, J.1    Hou, S.2    Malik-Soni, N.3    Xu, Z.4    Kumar, A.5
  • 129
    • 84896742498 scopus 로고    scopus 로고
    • Capsid proteins of enveloped viruses as antiviral drug targets
    • Klumpp K, Crepin T. 2014. Capsid proteins of enveloped viruses as antiviral drug targets. Curr. Opin. Virol. 5:63-71
    • (2014) Curr. Opin. Virol. , vol.5 , pp. 63-71
    • Klumpp, K.1    Crepin, T.2
  • 131
    • 84952845489 scopus 로고    scopus 로고
    • Suppression of drug resistance in dengue virus
    • Mateo R, Nagamine CM, Kirkegaard K. 2015. Suppression of drug resistance in dengue virus. mBio 6:e01960-15
    • (2015) MBio , vol.6 , pp. e01960-e02015
    • Mateo, R.1    Nagamine, C.M.2    Kirkegaard, K.3


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