메뉴 건너뛰기




Volumn 5, Issue 5, 2010, Pages 575-592

Insights into dengue virus genome replication

Author keywords

dengue virus; endoplasmic reticulum; nonstructural proteins; replicative complex; RNA protein interactions; RNA RNA interactions; trans acting factors; viral proteins; viral replicase; viral RNA

Indexed keywords

CIS ACTING ELEMENT; ELONGATION FACTOR 1ALPHA; GENOMIC RNA; LA ANTIGEN; POLYPYRIMIDINE TRACT BINDING PROTEIN; TRANS ACTING FACTOR; Y BOX BINDING PROTEIN 1;

EID: 77957294373     PISSN: 17460794     EISSN: None     Source Type: Journal    
DOI: 10.2217/fvl.10.49     Document Type: Review
Times cited : (38)

References (172)
  • 2
    • 74449092224 scopus 로고    scopus 로고
    • Present and future arboviral threats
    • Weaver SC, Reisen WK: Present and future arboviral threats. Antiviral Res. 85, 328-345 (2010).
    • (2010) Antiviral Res. , vol.85 , pp. 328-345
    • Weaver, S.C.1    Reisen, W.K.2
  • 3
    • 0036468861 scopus 로고    scopus 로고
    • Epidemic dengue/dengue hemorrhagic fever as a public health, social and economic problem in the 21st Century
    • Gubler DJ: Epidemic dengue/dengue hemorrhagic fever as a public health, social and economic problem in the 21st Century. Trends Microbiol. 10, 100-103 (2002).
    • (2002) Trends Microbiol. , vol.10 , pp. 100-103
    • Gubler, D.J.1
  • 4
    • 0023403265 scopus 로고
    • Clinical spectrum and management of dengue haemorrhagic fever. Southeast Asian
    • Nimmannitya, S: Clinical spectrum and management of dengue haemorrhagic fever. Southeast Asian J. Trop. Med. Public Health 18, 392-397 (1987).
    • (1987) J. Trop. Med. Public Health , vol.18 , pp. 392-397
    • Nimmannitya, S.1
  • 5
    • 0026847240 scopus 로고
    • Immunity and immunopathology in dengue virus infections
    • Kurane I, Ennis FE: Immunity and immunopathology in dengue virus infections. Semin Immunol. 4, 121-127 (1992).
    • (1992) Semin. Immunol. , vol.4 , pp. 121-127
    • Kurane, I.1    Ennis, F.E.2
  • 6
    • 0033602558 scopus 로고    scopus 로고
    • Immunopathogenesis of dengue hemorrhagic fever
    • Rothman AL, Ennis FA: Immunopathogenesis of dengue hemorrhagic fever. Virology 257, 1-6 (1999).
    • (1999) Virology , vol.257 , pp. 1-6
    • Rothman, A.L.1    Ennis, F.A.2
  • 7
    • 0024565393 scopus 로고
    • Antibody-dependent enhancement of dengue virus growth in human monocytes as a risk factor for dengue hemorrhagic fever
    • □□ Describes that dengue antibodies can be neutralizing and, therefore, protect against dengue virus DENV infection; however, they can be enhancing and increase the risk of dengue hemorrhagic fever
    • Kliks SC, Nisalak A, Brandt WE, Wahl L, Burke DS: Antibody-dependent enhancement of dengue virus growth in human monocytes as a risk factor for dengue hemorrhagic fever. Am. J. Trop. Med. Hyg 40, 444-451 (1989). □□ Describes that dengue antibodies can be neutralizing and, therefore, protect against dengue virus (DENV) infection; however, they can be enhancing and increase the risk of dengue hemorrhagic fever.
    • (1989) Am. J. Trop. Med. Hyg. , vol.40 , pp. 444-451
    • Kliks, S.C.1    Nisalak, A.2    Brandt, W.E.3    Wahl, L.4    Burke, D.S.5
  • 8
    • 33749454503 scopus 로고    scopus 로고
    • Differential enhancement of dengue virus immune complex infectivity mediated by signaling-competent and signaling-incompetent human Fcy RIA (CD64) or Fcγ RIIA (CD32)
    • □ Describes that Fcγ RIA CD64 or Fcγ RIIA CD32 mediate enhanced DENV immune complex infectivity, but CD32 appeared to do so far more effectively
    • Rodrigo WW, Jin X, Blackley SD, Rose RC, Schlesinger JJ: Differential enhancement of dengue virus immune complex infectivity mediated by signaling-competent and signaling-incompetent human Fcy RIA (CD64) or Fcγ RIIA (CD32). J. Virol. 80, 10128-10138 (2006). □ Describes that Fcγ RIA (CD64) or Fcγ RIIA (CD32) mediate enhanced DENV immune complex infectivity, but CD32 appeared to do so far more effectively.
    • (2006) J. Virol. , vol.80 , pp. 10128-10138
    • Rodrigo, W.W.1    Jin, X.2    Blackley, S.D.3    Rose, R.C.4    Schlesinger, J.J.5
  • 9
    • 74049115561 scopus 로고    scopus 로고
    • Dengue virus virulence and transmission determinants
    • Rico-Hesse R: Dengue virus virulence and transmission determinants. Curr. Top. Microbiol. Immunol. 338, 45-55 (2010).
    • (2010) Curr. Top. Microbiol. Immunol. , vol.338 , pp. 45-55
    • Rico-Hesse, R.1
  • 10
    • 18344387519 scopus 로고    scopus 로고
    • Structure of dengue virus: Implications for flavivirus organization, maturation, and fusion
    • □□ Determination of the first structure of the DENV particle and the suggestion of a pH-induced class II fusion mechanism by the domain II of the envelope glycoprotein
    • Kuhn RJ, Zhang W, Rossman MG et al.: Structure of dengue virus: implications for flavivirus organization, maturation, and fusion. Cell 108, 717-725 (2002). □□ Determination of the first structure of the DENV particle and the suggestion of a pH-induced class II fusion mechanism by the domain II of the envelope glycoprotein.
    • (2002) Cell. , vol.108 , pp. 717-725
    • Kuhn, R.J.1    Zhang, W.2    Rossman, M.G.3
  • 11
    • 41349112506 scopus 로고    scopus 로고
    • The flavivirus precursor membrane-envelope protein complex: Structure and maturation
    • □ Provides a crystal structure of the recombinant protein precursor membrane linked to the envelope from DENV providing the identification of the stages of the pH-directed confomational changes during maturation of the viral particle
    • Li L, Lok SM, Yu IM, et al.: The flavivirus precursor membrane-envelope protein complex: structure and maturation. Science 319, 1830-1834 (2008). □ Provides a crystal structure of the recombinant protein precursor membrane linked to the envelope from DENV providing the identification of the stages of the pH-directed confomational changes during maturation of the viral particle.
    • (2008) Science , vol.319 , pp. 1830-1834
    • Li, L.1    Lok, S.M.2    Yu, I.M.3
  • 12
    • 0034899311 scopus 로고    scopus 로고
    • Monoclonal antibodies that bind to domain III of dengue virus e glycoprotein are the most efficient blockers of virus adsorption to Vero cells
    • Crill W, Roehring J: Monoclonal antibodies that bind to domain III of dengue virus e glycoprotein are the most efficient blockers of virus adsorption to Vero cells. J. Virol. 75, 4002-4007 (2001).
    • (2001) J. Virol. , vol.75 , pp. 4002-4007
    • Crill, W.1    Roehring, J.2
  • 13
    • 0038810275 scopus 로고    scopus 로고
    • Dengue virus envelope glycoprotein structure: New insight into its interactions during viral entry
    • Rey FA: Dengue virus envelope glycoprotein structure: new insight into its interactions during viral entry. Proc. Natl Acad. Sci. USA 100, 6899-6901 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6899-6901
    • Rey, F.A.1
  • 14
    • 11144244755 scopus 로고    scopus 로고
    • Variable surface epitopes in the crystal structure of dengue virus type 3 envelope glycoprotein
    • Modis Y, Ogata S, Clements D, Harrison SC: Variable surface epitopes in the crystal structure of dengue virus type 3 envelope glycoprotein. J. Virol. 79, 1223-1231 (2005).
    • (2005) J. Virol. , vol.79 , pp. 1223-1231
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 16
    • 70949093288 scopus 로고    scopus 로고
    • The dengue virus type 2 envelope protein fusion peptide is essential for membrane fusion
    • □ Determination of DENV envelope protein-specific aminoacids, which are essential for cell-to-cell fusion
    • Huang CY, Butrapet S, Moss KJ et al.: The dengue virus type 2 envelope protein fusion peptide is essential for membrane fusion. Virology 396, 305-315 (2010). □ Determination of DENV envelope protein-specific aminoacids, which are essential for cell-to-cell fusion.
    • (2010) Virology , vol.396 , pp. 305-315
    • Huang, C.Y.1    Butrapet, S.2    Moss, K.J.3
  • 18
    • 0000163169 scopus 로고    scopus 로고
    • Knipe DM, Howley PM Eds. Lippincott Williams & Wilkins, PA, USA
    • Lindenbach BD, Rice CM: Fields Virology. Knipe DM, Howley PM (Eds). Lippincott Williams & Wilkins, PA, USA 991-1041 (2001).
    • (2001) Fields Virology , pp. 991-1041
    • Lindenbach, B.D.1    Rice, C.M.2
  • 19
    • 41849125306 scopus 로고    scopus 로고
    • Specific requirements for elements of the 5' and 3' terminal regions in flavivirus RNA synthesis and viral replication
    • Yu L, Nomaguchi M, Padmanabhan R, Markoff L: Specific requirements for elements of the 5' and 3' terminal regions in flavivirus RNA synthesis and viral replication. Virology 374, 170-185 (2008).
    • (2008) Virology , vol.374 , pp. 170-185
    • Yu, L.1    Nomaguchi, M.2    Padmanabhan, R.3    Markoff, L.4
  • 21
    • 0025864149 scopus 로고
    • Both nonstructural proteins NS2B and NS3 are required for the proteolytic processing of dengue virus nonstructural proteins
    • Falgout B, Pethel M, Zhang YM, Lai CJ: Both nonstructural proteins NS2B and NS3 are required for the proteolytic processing of dengue virus nonstructural proteins. J. Virol. 65, 2467-2475 (1991).
    • (1991) J. Virol. , vol.65 , pp. 2467-2475
    • Falgout, B.1    Pethel, M.2    Zhang, Y.M.3    Lai, C.J.4
  • 22
    • 0026540617 scopus 로고
    • Cleavage of the dengue virus polyprotein at the NS3/NS4A and NS4B/NS5 junctions is mediated by viral protease NS2B-NS3, whereas NS4A/NS4B may be processed by a cellular protease
    • Cahour A, Falgout B, Lai CJ: Cleavage of the dengue virus polyprotein at the NS3/NS4A and NS4B/NS5 junctions is mediated by viral protease NS2B-NS3, whereas NS4A/NS4B may be processed by a cellular protease. J. Virol. 66, 1535-1542 (1992).
    • (1992) J. Virol. , vol.66 , pp. 1535-1542
    • Cahour, A.1    Falgout, B.2    Lai, C.J.3
  • 23
    • 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: NS2B-3 proteinase-mediated processing in the yellow fever virus structural region: in vitro and in vivo studies. J. Virol. 68, 3794-3802 (1994).
    • (1994) J. Virol. , vol.68 , pp. 3794-3802
    • Amberg, S.M.1    Nestorowicz, A.2    McCourt, D.W.3    Rice, C.M.4
  • 24
    • 0028849770 scopus 로고
    • Evidence that flavivirus NS1-NS2A cleavage is mediated by a membrane-bound host protease in the endoplasmic reticulum
    • Falgout B, Markoff L: Evidence that flavivirus NS1-NS2A cleavage is mediated by a membrane-bound host protease in the endoplasmic reticulum. J. Virol. 69, 7232-7243 (1995).
    • (1995) J. Virol. , vol.69 , pp. 7232-7243
    • Falgout, B.1    Markoff, L.2
  • 25
    • 0027530821 scopus 로고
    • Processing of the dengue virus type 2 proteins prM and C-prM
    • Murray JM, Aaskov JG, Wright PJ: Processing of the dengue virus type 2 proteins prM and C-prM. J. Gen. Virol. 74, 175-182 (1993).
    • (1993) J. Gen. Virol. , vol.74 , pp. 175-182
    • Murray, J.M.1    Aaskov, J.G.2    Wright, P.J.3
  • 26
    • 0030764780 scopus 로고    scopus 로고
    • Proteolytic activation of tick-borne encephalitis virus by furin
    • Stadler K, Allison SL, Schalich J, Heinz FX: Proteolytic activation of tick-borne encephalitis virus by furin. J. Virol. 71, 8475-8481 (1997).
    • (1997) J. Virol. , vol.71 , pp. 8475-8481
    • Stadler, K.1    Allison, S.L.2    Schalich, J.3    Heinz, F.X.4
  • 27
    • 0030846512 scopus 로고    scopus 로고
    • Ultrastructure of Kunjin virus-infected cells: Colocalization of NS1 and NS3 with double-stranded RNA, and of NS2B with NS3, in virus-induced membrane structures
    • □ Describes that during Kunjin infection, one set of induced membranes comprised vesicle packets of smooth membranes were dual labeled with anti-dsRNA and anti-NS1 or anti-NS3 antibodies, while the presence of NS2B and NS3 was demonstrated in paracrystalline arrays and in convoluted smooth membranes
    • Westaway EG, Mackenzie JM, Kenney MT, Jones MK, Khromykh AA: Ultrastructure of Kunjin virus-infected cells: colocalization of NS1 and NS3 with double-stranded RNA, and of NS2B with NS3, in virus-induced membrane structures. J. Virol. 71, 6650-6661 (1997). □ Describes that during Kunjin infection, one set of induced membranes comprised vesicle packets of smooth membranes were dual labeled with anti-dsRNA and anti-NS1 or anti-NS3 antibodies, while the presence of NS2B and NS3 was demonstrated in paracrystalline arrays and in convoluted smooth membranes.
    • (1997) J. Virol. , vol.71 , pp. 6650-6661
    • Westaway, E.G.1    Mackenzie, J.M.2    Kenney, M.T.3    Jones, M.K.4    Khromykh, A.A.5
  • 28
    • 0032486487 scopus 로고    scopus 로고
    • Subcellular localization and some biochemical properties of the flavivirus Kunjin nonstructural proteins NS2A and NS4A
    • Mackenzie JM, Khromykh AA, Jones MK, Westaway EG: Subcellular localization and some biochemical properties of the flavivirus Kunjin nonstructural proteins NS2A and NS4A. Virology 245, 203-215 (1998)
    • (1998) Virology , vol.245 , pp. 203-215
    • Mackenzie, J.M.1    Khromykh, A.A.2    Jones, M.K.3    Westaway, E.G.4
  • 29
    • 0036056151 scopus 로고    scopus 로고
    • Heparan sulfate-mediated binding of infectious dengue virus type 2 and yellow fever virus
    • Germi R, Crance JM, Garin D et al.: Heparan sulfate-mediated binding of infectious dengue virus type 2 and yellow fever virus. Virology 292, 162-168 (2002).
    • (2002) Virology , vol.292 , pp. 162-168
    • Germi, R.1    Crance, J.M.2    Garin, D.3
  • 30
    • 2442457815 scopus 로고    scopus 로고
    • Identification of GRP 78 (BiP) as a liver cell expressed receptor element for dengue virus serotype 2
    • Jindadamrongwech S, Thepparit C, Smith DR: Identification of GRP 78 (BiP) as a liver cell expressed receptor element for dengue virus serotype 2. Arch. Virol. 149, 915-927 (2004).
    • (2004) Arch. Virol. , vol.149 , pp. 915-927
    • Jindadamrongwech, S.1    Thepparit, C.2    Smith, D.R.3
  • 31
    • 7644219512 scopus 로고    scopus 로고
    • Serotype-specific entry of dengue virus into liver cells: Identification of the 37-kilodalton/67-kilodalton high-affinity laminin receptor as a dengue virus serotype 1 receptor
    • Thepparit C, Smith DR: Serotype-specific entry of dengue virus into liver cells: identification of the 37-kilodalton/67-kilodalton high-affinity laminin receptor as a dengue virus serotype 1 receptor. J. Virol. 78, 12647-12656 (2004).
    • (2004) J. Virol. , vol.78 , pp. 12647-12656
    • Thepparit, C.1    Smith, D.R.2
  • 32
    • 21244462832 scopus 로고    scopus 로고
    • Dendritic cell-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN)-mediated enhancement of dengue virus infection is independent of DC-SIGN internalization signals
    • Lozach PY, Burleigh L, Staropoli I et al.: Dendritic cell-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN)-mediated enhancement of dengue virus infection is independent of DC-SIGN internalization signals. J. Biol. Chem. 280, 23698-23708 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 23698-23708
    • Lozach, P.Y.1    Burleigh, L.2    Staropoli, I.3
  • 33
    • 16244364801 scopus 로고    scopus 로고
    • Heat shock protein 90 and heat shock protein 70 are components of dengue virus receptor complex in human cells
    • Reyes-del Valle J, Chávez-Salinas S, Medina F, del Angel RM: Heat shock protein 90 and heat shock protein 70 are components of dengue virus receptor complex in human cells. J. Virol. 79, 4557-4567 (2005).
    • (2005) J. Virol. , vol.79 , pp. 4557-4567
    • Reyes-del Valle, J.1    Chávez-Salinas, S.2    Medina, F.3    Del Angel, R.M.4
  • 34
    • 40349100411 scopus 로고    scopus 로고
    • The mannose receptor mediates dengue virus infection of macrophages
    • Miller JL, de Wet BJ, Martinez-Pomares L et al.: The mannose receptor mediates dengue virus infection of macrophages. PLoS Pathog 4(2), e17 (2008).
    • (2008) PLoS Pathog , vol.4 , Issue.2
    • Miller, J.L.1    De Wet, B.J.2    Martinez-Pomares, L.3
  • 35
    • 33749042583 scopus 로고    scopus 로고
    • Flavivirus membrane fusion
    • Stiasny K, Heinz FX: Flavivirus membrane fusion. J. Gen. Virol. 87, 2755-2766 (2006).
    • (2006) J. Gen. Virol. , vol.87 , pp. 2755-2766
    • Stiasny, K.1    Heinz, F.X.2
  • 36
  • 37
    • 35448960873 scopus 로고    scopus 로고
    • Characterization of the early events in dengue virus cell entry by biochemical assays and single-virus tracking
    • van der Schaar HM, Rust MJ, Waarts B-L et al.: Characterization of the early events in dengue virus cell entry by biochemical assays and single-virus tracking. J. Virol. 81, 12019-12028 (2007).
    • (2007) J. Virol. , vol.81 , pp. 12019-12028
    • Van Der Schaar, H.M.1    Rust, M.J.2    Waarts, B.-L.3
  • 38
    • 41649101680 scopus 로고    scopus 로고
    • Functional entry of dengue virus into Aedes albopictus mosquito cells is dependent on clathrinmediated endocytosis
    • Acosta E, Castilla V, Damonte E: Functional entry of dengue virus into Aedes albopictus mosquito cells is dependent on clathrinmediated endocytosis. J. Gen. Virol. 89, 474-484 (2008).
    • (2008) J. Gen. Virol. , vol.89 , pp. 474-484
    • Acosta, E.1    Castilla, V.2    Damonte, E.3
  • 40
    • 47749122553 scopus 로고    scopus 로고
    • Endocytic pathway followed by dengue virus to infect the mosquito cell line C6/36 HT
    • Mosso C, Galván-Mendoza IJ, Ludert JE, del Angel RM: Endocytic pathway followed by dengue virus to infect the mosquito cell line C6/36 HT. Virology 378, 193-199 (2008).
    • (2008) Virology , vol.378 , pp. 193-199
    • Mosso, C.1    Galván-Mendoza, I.J.2    Ludert, J.E.3    Del Angel, R.M.4
  • 41
    • 58149265437 scopus 로고    scopus 로고
    • Dissecting the cell entry pathway of dengue virus by single-particle tracking in living cells
    • □ First study describing the cell entry process of DENV and determines that this virus infects the cell host via a clathrin-mediated endocytosis
    • van der Schaar HM, Rust MJ, Chen C et al.: Dissecting the cell entry pathway of dengue virus by single-particle tracking in living cells. PLoS Pathog. 4(12), e1000244 (2008). □ First study describing the cell entry process of DENV and determines that this virus infects the cell host via a clathrin-mediated endocytosis.
    • (2008) PLoS Pathog , vol.4 , Issue.12
    • Van Der Schaar, H.M.1    Rust, M.J.2    Chen, C.3
  • 42
    • 70350719853 scopus 로고    scopus 로고
    • Alternative infectious entry pathways for dengue virus serotypes into mammalian cells
    • □ Using different approaches this article proposes for the first time that DENV has alternative pathways of entry given by serotype and cell type. These pathways can be either dependent or independent of clathrin, but are always dependent on dynamin
    • Acosta EG, Castilla V, Damonte EB: Alternative infectious entry pathways for dengue virus serotypes into mammalian cells. Cell Microbiol. 11, 1533-1549 (2009). □ Using different approaches this article proposes for the first time that DENV has alternative pathways of entry given by serotype and cell type. These pathways can be either dependent or independent of clathrin, but are always dependent on dynamin.
    • (2009) Cell. Microbiol. , vol.11 , pp. 1533-1549
    • Acosta, E.G.1    Castilla, V.2    Damonte, E.B.3
  • 43
    • 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: 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, 10787-10799 (2001).
    • (2001) J. Virol. , vol.75 , pp. 10787-10799
    • Mackenzie, J.M.1    Westaway, E.G.2
  • 44
    • 0033602697 scopus 로고    scopus 로고
    • Nascent flavivirus RNA colocalized in situ with double-stranded RNA in stable replication complexes
    • Westaway EG, Khromykh AA, Mackenzie JM: Nascent flavivirus RNA colocalized in situ with double-stranded RNA in stable replication complexes. Virology 258, 108-117 (1999).
    • (1999) Virology , vol.258 , pp. 108-117
    • Westaway, E.G.1    Khromykh, A.A.2    Mackenzie, J.M.3
  • 45
    • 0042591335 scopus 로고    scopus 로고
    • Architecture of the flaviviral replication complex - Protease, nuclease, and detergents reveal encasement within double-layered membrane compartments
    • □ The first report providing biochemical evidence of the double-layered membranous compartment of the flavivirus replicative complex
    • Uchil PD, Satchidanandam V: Architecture of the flaviviral replication complex - protease, nuclease, and detergents reveal encasement within double-layered membrane compartments. J. Biol. Chem. 278, 24388-24398 (2003). □ The first report providing biochemical evidence of the double-layered membranous compartment of the flavivirus replicative complex.
    • (2003) J. Biol. Chem. , vol.278 , pp. 24388-24398
    • Uchil, P.D.1    Satchidanandam, V.2
  • 46
    • 41349112304 scopus 로고    scopus 로고
    • Structure of immature dengue virus at low pH primes proteolytic maturation
    • Yu M, Zhang W, Holdaway HA et al.: Structure of immature dengue virus at low pH primes proteolytic maturation. Science 319, 1834-1837 (2008).
    • (2008) Science , vol.319 , pp. 1834-1837
    • Yu, M.1    Zhang, W.2    Holdaway, H.A.3
  • 47
    • 0022530829 scopus 로고
    • Analysis of structural properties which possibly are characteristic for the 3'-terminal sequence of the genome RNA of flaviviruses
    • Wengler G, Castle E: Analysis of structural properties which possibly are characteristic for the 3'-terminal sequence of the genome RNA of flaviviruses. J. Gen. Virol. 67, 1183-1188 (1986).
    • (1986) J. Gen. Virol. , vol.67 , pp. 1183-1188
    • Wengler, G.1    Castle, E.2
  • 48
    • 0029893436 scopus 로고    scopus 로고
    • Dengue type 4 virus mutants containing deletions in the 3' noncoding region of the RNA genome: Analysis of growth restriction in cell culture and altered viremia pattern and immunogenicity in rhesus monkeys
    • Men RH, Bray M, Clark D et al.: Dengue type 4 virus mutants containing deletions in the 3' noncoding region of the RNA genome: analysis of growth restriction in cell culture and altered viremia pattern and immunogenicity in rhesus monkeys. J. Virol. 70, 3930-3937 (1996).
    • (1996) J. Virol. , vol.70 , pp. 3930-3937
    • Men, R.H.1    Bray, M.2    Clark, D.3
  • 49
  • 50
    • 13444288088 scopus 로고    scopus 로고
    • The topology of bulges in the long stem of the flavivirus 3' stem-loop is a major determinant of RNA replication competence
    • Yu L, Markoff L: The topology of bulges in the long stem of the flavivirus 3' stem-loop is a major determinant of RNA replication competence. J. Virol. 79, 2309-2324 (2005).
    • (2005) J. Virol. , vol.79 , pp. 2309-2324
    • Yu, L.1    Markoff, L.2
  • 51
    • 33750231544 scopus 로고    scopus 로고
    • Direct repeats in the 3' untranslated regions of mosquito-borne flaviviruses: Possible implications for virus transmission
    • Gritsun TS, Gould A: Direct repeats in the 3' untranslated regions of mosquito-borne flaviviruses: possible implications for virus transmission. J. Gen. Virol. 87, 3297-3305 (2006).
    • (2006) J. Gen. Virol. , vol.87 , pp. 3297-3305
    • Gritsun, T.S.1    Gould, A.2
  • 52
    • 33144458778 scopus 로고    scopus 로고
    • RNA secondary structure in the coding region of dengue virus type 2 directs translation start codon selection and is required for viral replication
    • Clyde K, Harris E: RNA secondary structure in the coding region of dengue virus type 2 directs translation start codon selection and is required for viral replication. J. Virol. 80, 2170-2182 (2006).
    • (2006) J. Virol. , vol.80 , pp. 2170-2182
    • Clyde, K.1    Harris, E.2
  • 53
    • 33747344212 scopus 로고    scopus 로고
    • A 5' RNA element promotes dengue virus RNA synthesis on a circular genome
    • □□ Describes how the 5-stem-loop A SLA element acts as the promoter for DENV RNA synthesis and proposes a novel mechanism for minus-strand RNA synthesis
    • Filomatori CV, Lodeiro MF, Alvarez DE et al.: A 5' RNA element promotes dengue virus RNA synthesis on a circular genome. Genes Dev. 20, 2238-2249 (2006). □□ Describes how the 5-stem-loop A (SLA) element acts as the promoter for DENV RNA synthesis and proposes a novel mechanism for minus-strand RNA synthesis.
    • (2006) Genes Dev. , vol.20 , pp. 2238-2249
    • Filomatori, C.V.1    Lodeiro, M.F.2    Alvarez, D.E.3
  • 54
    • 54049142396 scopus 로고    scopus 로고
    • Terminal structures of West Nile virus genomic RNA and their interactions with viral NS5 protein
    • Dong H, Zhang B, Shi PY: Terminal structures of West Nile virus genomic RNA and their interactions with viral NS5 protein. Virology 381, 123-135 (2008).
    • (2008) Virology , vol.381 , pp. 123-135
    • Dong, H.1    Zhang, B.2    Shi, P.Y.3
  • 55
    • 59749084360 scopus 로고    scopus 로고
    • Genome cyclization as strategy for flavivirus RNA replication
    • □□ Provides an insightful review of the elements involved in flavivirus genome cyclization
    • Villordo SM, Gamarnik AV: Genome cyclization as strategy for flavivirus RNA replication. Virus Res. 139, 230-239 (2009). □□ Provides an insightful review of the elements involved in flavivirus genome cyclization.
    • (2009) Virus Res. , vol.139 , pp. 230-239
    • Villordo, S.M.1    Gamarnik, A.V.2
  • 56
    • 58149487592 scopus 로고    scopus 로고
    • Structural and functional studies of the promoter element for dengue virus RNA replication
    • □ It presents a detailed study of the structural elements of the 5-SLA required for DENV RNA replication
    • Lodeiro MF, Filomatori C, Gamarnik AV: Structural and functional studies of the promoter element for dengue virus RNA replication. J. Virol. 83, 93-1008 (2009). □ It presents a detailed study of the structural elements of the 5-SLA required for DENV RNA replication.
    • (2009) J. Virol. , vol.83 , pp. 93-1008
    • Lodeiro, M.F.1    Filomatori, C.2    Gamarnik, A.V.3
  • 57
    • 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: 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, 4633-4640 (2001).
    • (2001) J. Virol. , vol.75 , pp. 4633-4640
    • Khromykh, A.A.1    Varnavski, A.N.2    Sedlak, P.L.3    Westaway, E.G.4
  • 58
    • 0037303672 scopus 로고    scopus 로고
    • Fine mapping of a cis-acting sequence element in yellow fever virus RNA that is required for RNA replication and cyclization
    • Corver J, Lenches E, Smith K et al.: Fine mapping of a cis-acting sequence element in yellow fever virus RNA that is required for RNA replication and cyclization. J. Virol. 77, 2265-2270 (2003).
    • (2003) J. Virol. , vol.77 , pp. 2265-2270
    • Corver, J.1    Lenches, E.2    Smith, K.3
  • 59
    • 18744362727 scopus 로고    scopus 로고
    • Long-range RNA-RNA interactions circularize the dengue virus genome
    • □□ Reports the interaction between the 5-and 3-ends of the DENV genome by atomic force microscopy and the identification of a new set of 16 nucleotides important for RNA-RNA association, termed upstream AUG region
    • Alvarez DE, Lodeiro MF, Luduena SJ et al.: Long-range RNA-RNA interactions circularize the dengue virus genome. J. Virol. 79, 6631-6643 (2005). □□ Reports the interaction between the 5-and 3-ends of the DENV genome by atomic force microscopy and the identification of a new set of 16 nucleotides important for RNA-RNA association, termed upstream AUG region.
    • (2005) J. Virol. , vol.79 , pp. 6631-6643
    • Alvarez, D.E.1    Lodeiro, M.F.2    Luduena, S.J.3
  • 60
    • 23844507858 scopus 로고    scopus 로고
    • Role of RNA structures present at the 3'UTR of dengue virus on translation, RNA synthesis and viral replication
    • Alvarez DE, De Lella Ezcurra AL, Fucito S, Gamarnik AV: Role of RNA structures present at the 3'UTR of dengue virus on translation, RNA synthesis and viral replication. Virology 339, 200-212 (2005).
    • (2005) Virology , vol.339 , pp. 200-212
    • Alvarez, D.E.1    De Lella Ezcurra, A.L.2    Fucito, S.3    Gamarnik, A.V.4
  • 61
    • 33645783003 scopus 로고    scopus 로고
    • Functional analysis of the tick-borne encephalitis virus cyclization elements indicates major differences between mosquito-borne and tick-borne flaviviruses
    • Kofler RM, Hoenninger VM, Thurner C et al.: Functional analysis of the tick-borne encephalitis virus cyclization elements indicates major differences between mosquito-borne and tick-borne flaviviruses. J. Virol. 80, 4099-4113 (2006).
    • (2006) J. Virol. , vol.80 , pp. 4099-4113
    • Kofler, R.M.1    Hoenninger, V.M.2    Thurner, C.3
  • 62
    • 42749084987 scopus 로고    scopus 로고
    • Functional analysis of dengue virus cyclization sequences located at the 5' and 3'UTRs
    • Alvarez DE, Filomatori CV, Gamarnik AV: Functional analysis of dengue virus cyclization sequences located at the 5' and 3'UTRs. Virology 375, 223-235 (2008).
    • (2008) Virology , vol.375 , pp. 223-235
    • Alvarez, D.E.1    Filomatori, C.V.2    Gamarnik, A.V.3
  • 63
    • 47049089643 scopus 로고    scopus 로고
    • Genetic interactions among the West Nile Virus Methyltransferase, the RNA-dependent RNA polymerase, and the 5' stem-loop of genomic RNA
    • Zhang B, Zhou Y, Shi PY: Genetic interactions among the West Nile Virus Methyltransferase, the RNA-dependent RNA polymerase, and the 5' stem-loop of genomic RNA. J. Virol. 82, 7047-7058 (2008).
    • (2008) J. Virol. , vol.82 , pp. 7047-7058
    • Zhang, B.1    Zhou, Y.2    Shi, P.Y.3
  • 64
    • 77952736780 scopus 로고    scopus 로고
    • The interplay of RNA elements in the dengue virus 5' and 3' ends required for viral RNA replication
    • Friebe P, Harris E: The interplay of RNA elements in the dengue virus 5' and 3' ends required for viral RNA replication. J. Virol. 84(12), 6103-6118 (2010).
    • (2010) J. Virol. , vol.84 , Issue.12 , pp. 6103-6118
    • Friebe, P.1    Harris, E.2
  • 65
    • 50349101877 scopus 로고    scopus 로고
    • The capsidcoding region hairpin element (cHP) is a critical determinant of dengue virus and West Nile virus RNA synthesis
    • Clyde K, Barrera J, Harris E: The capsidcoding region hairpin element (cHP) is a critical determinant of dengue virus and West Nile virus RNA synthesis. Virology 379, 314-323 (2008).
    • (2008) Virology , vol.379 , pp. 314-323
    • Clyde, K.1    Barrera, J.2    Harris, E.3
  • 66
    • 0033585015 scopus 로고    scopus 로고
    • A novel in vitro replication system for dengue virus. Initiation of RNA synthesis at the 3 "-end of exogenous viral RNA templates requires 5"-and 3"-terminal complementary sequence motifs of the viral RNA
    • □□ This study reports the first in vitro replication assay of DENV using cell-free extracts. It also determines that the interaction between the 5-and 3-ends of the viral genome is modulated by complementary sequences, which are required for the viral RNA synthesis
    • You S, Padmanabhan R: A novel in vitro replication system for dengue virus. Initiation of RNA synthesis at the 3 "-end of exogenous viral RNA templates requires 5"-and 3"-terminal complementary sequence motifs of the viral RNA. J. Biol. Chem. 274, 33714-33722 (1999). □□ This study reports the first in vitro replication assay of DENV using cell-free extracts. It also determines that the interaction between the 5-and 3-ends of the viral genome is modulated by complementary sequences, which are required for the viral RNA synthesis.
    • (1999) J. Biol. Chem. , vol.274 , pp. 33714-33722
    • You, S.1    Padmanabhan, R.2
  • 67
    • 0035844132 scopus 로고    scopus 로고
    • In vitro RNA synthesis from exogenous dengue viral RNA templates requires long range interactions between 5"-and 3"-terminal regions that influence RNA structure
    • You S, Falgout B, Markoff L et al.: In vitro RNA synthesis from exogenous dengue viral RNA templates requires long range interactions between 5"-and 3"-terminal regions that influence RNA structure. J. Biol. Chem. 276, 15581-15591 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 15581-15591
    • You, S.1    Falgout, B.2    Markoff, L.3
  • 68
    • 34547570863 scopus 로고    scopus 로고
    • Characterization of the variable region in the 3' non-translated region of dengue type 1 virus
    • Tajima S, Nukui Y, Takasaki T et al.: Characterization of the variable region in the 3' non-translated region of dengue type 1 virus. J. Gen. Virol. 88, 2214-2222 (2007).
    • (2007) J. Gen. Virol. , vol.88 , pp. 2214-2222
    • Tajima, S.1    Nukui, Y.2    Takasaki, T.3
  • 69
    • 70349448653 scopus 로고    scopus 로고
    • Molecular genetic relationship of the 3' untranslated region among Thai dengue-3 virus, Bangkok isolates, during 1973-2000
    • Pankhong P, Ramanathan MP, Weiner DB et al.: Molecular genetic relationship of the 3' untranslated region among Thai dengue-3 virus, Bangkok isolates, during 1973-2000. DNA Cell Biol. 28, 481-491 (2009).
    • (2009) DNA Cell. Biol. , vol.28 , pp. 481-491
    • Pankhong, P.1    Ramanathan, M.P.2    Weiner, D.B.3
  • 70
    • 0037223896 scopus 로고    scopus 로고
    • A live, attenuated dengue virus type 1 vaccine candidate with a 30-nucleotide deletion in the 3' untranslated region is highly attenuated and immunogenic in monkeys
    • Whitehead SS, Falgout B, Hanley KA et al.: A live, attenuated dengue virus type 1 vaccine candidate with a 30-nucleotide deletion in the 3' untranslated region is highly attenuated and immunogenic in monkeys. J. Virol. 77, 1653-1657 (2003).
    • (2003) J. Virol. , vol.77 , pp. 1653-1657
    • Whitehead, S.S.1    Falgout, B.2    Hanley, K.A.3
  • 71
    • 0031849664 scopus 로고    scopus 로고
    • Identification of specific nucleotide sequences within the conserved 3"-SL in the dengue type 2 virus genome required for replication
    • □ This study determines that the conservation of the secondary structure and the last 11 nt of the 3-stem loop in DENV genome is required for replication
    • Zeng L, Falgout B, Markoff L: Identification of specific nucleotide sequences within the conserved 3"-SL in the dengue type 2 virus genome required for replication. J. Virol. 72, 7510-7522 (1998). □ This study determines that the conservation of the secondary structure and the last 11 nt of the 3-stem loop in DENV genome is required for replication.
    • (1998) J. Virol. , vol.72 , pp. 7510-7522
    • Zeng, L.1    Falgout, B.2    Markoff, L.3
  • 72
    • 3242740948 scopus 로고    scopus 로고
    • Structure and function of the 3' terminal six nucleotides of the West Nile virus genome in viral replication
    • Tilgner M, Shi PY: Structure and function of the 3' terminal six nucleotides of the West Nile virus genome in viral replication. J. Virol. 78, 8159-8171 (2004).
    • (2004) J. Virol. , vol.78 , pp. 8159-8171
    • Tilgner, M.1    Shi, P.Y.2
  • 73
    • 0141856225 scopus 로고    scopus 로고
    • Significance in replication of the terminal nucleotides of the flavivirus genome
    • Khromykh AA, Kondratieva N, Sgro JY et al.: significance in replication of the terminal nucleotides of the flavivirus genome. J. Virol. 77, 10623-10629 (2003).
    • (2003) J. Virol. , vol.77 , pp. 10623-10629
    • Khromykh, A.A.1    Kondratieva, N.2    Sgro, J.Y.3
  • 74
    • 0041707804 scopus 로고    scopus 로고
    • De novo synthesis of negative-strand RNA by dengue virus RNA-dependent RNA polymerase in vitro: Nucleotide, primer, and template parameters
    • Nomaguchi M, Ackermann M, Yon C et al.: De novo synthesis of negative-strand RNA by dengue virus RNA-dependent RNA polymerase in vitro: nucleotide, primer, and template parameters. J. Virol. 77, 8831-8842 (2003).
    • (2003) J. Virol. , vol.77 , pp. 8831-8842
    • Nomaguchi, M.1    Ackermann, M.2    Yon, C.3
  • 75
    • 57049157140 scopus 로고    scopus 로고
    • Genome 3"-end repair in dengue virus type 2
    • Teramoto T, Kohno Y, Mattoo P et al.: Genome 3"-end repair in dengue virus type 2. RNA 14, 2645-2656 (2008).
    • (2008) RNA , vol.14 , pp. 2645-2656
    • Teramoto, T.1    Kohno, Y.2    Mattoo, P.3
  • 76
    • 72949095115 scopus 로고    scopus 로고
    • Identification and characterization of small sub-genomic RNAs in dengue 1-4 virus-infected cell cultures and tissues
    • Ran L, Yue L, Li X et al.: Identification and characterization of small sub-genomic RNAs in dengue 1-4 virus-infected cell cultures and tissues. Biochem. Biophys. Res. Comm. 391, 1099-1103 (2010).
    • (2010) Biochem. Biophys. Res. Comm. , vol.391 , pp. 1099-1103
    • Ran, L.1    Yue, L.2    Li, X.3
  • 77
    • 0018078321 scopus 로고
    • Studies on virus-specific nucleic acids synthesized in vertebrate and mosquito cells infected with flaviviruses
    • Wengler G, Gross HJ: Studies on virus-specific nucleic acids synthesized in vertebrate and mosquito cells infected with flaviviruses. Virology 89, 423-437 (1978).
    • (1978) Virology , vol.89 , pp. 423-437
    • Wengler, G.1    Gross, H.J.2
  • 78
    • 57049096375 scopus 로고    scopus 로고
    • A highly structured, nuclease resistant, noncoding RNA produced by flaviviruses is required for pathogenicity
    • Pijlman GP, Funk A, Kondratieva N et al.: A highly structured, nuclease resistant, noncoding RNA produced by flaviviruses is required for pathogenicity. Cell Host Microbe 4, 579-591 (2008).
    • (2008) Cell. Host Microbe , vol.4 , pp. 579-591
    • Pijlman, G.P.1    Funk, A.2    Kondratieva, N.3
  • 79
    • 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: Immunolocalization of the dengue virus nonstructural glycoprotein NS1 suggests a role in viral RNA replication. Virology 220, 232-240 (1996).
    • (1996) Virology , vol.220 , pp. 232-240
    • Mackenzie, J.M.1    Jones, M.K.2    Young, P.R.3
  • 80
    • 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: Subcellular localization and membrane topology of the dengue virus type 2 non-structural protein 4B. J. Biol. Chem. 281, 8854-8863 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 8854-8863
    • Miller, S.1    Sparacio, S.2    Bartenschlager, R.3
  • 81
    • 34247848008 scopus 로고    scopus 로고
    • The nonstructural protein 4A of dengue virus is an integral membrane protein inducing membrane alteration in a 2K-regulated manner
    • Miller S, Kastner S, Krijne-Locker J, Buhler S, Bartenschlager R: The nonstructural protein 4A of dengue virus is an integral membrane protein inducing membrane alteration in a 2K-regulated manner. J. Biol. Chem. 282, 8873-8882 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 8873-8882
    • Miller, S.1    Kastner, S.2    Krijne-Locker, J.3    Buhler, S.4    Bartenschlager, R.5
  • 82
    • 0033034992 scopus 로고    scopus 로고
    • Genetic interaction of flavivirus nonstructural proteins NS1 and NS4A as a determinant of replicase function
    • Lindenbach BD, Rice CM: Genetic interaction of flavivirus nonstructural proteins NS1 and NS4A as a determinant of replicase function. J. Virol. 73, 4611-4621 (1999).
    • (1999) J. Virol. , vol.73 , pp. 4611-4621
    • Lindenbach, B.D.1    Rice, C.M.2
  • 83
    • 33747338217 scopus 로고    scopus 로고
    • Dengue virus NS4B interacts with NS3 and dissociates it from singlestranded RNA
    • Umareddy I, Chao A, Sampath A, Gu F, Vasudevan SG: Dengue virus NS4B interacts with NS3 and dissociates it from singlestranded RNA. J. Gen. Virol. 87, 2605-2614 (2006).
    • (2006) J. Gen. Virol. , vol.87 , pp. 2605-2614
    • Umareddy, I.1    Chao, A.2    Sampath, A.3    Gu, F.4    Vasudevan, S.G.5
  • 84
    • 0035104617 scopus 로고    scopus 로고
    • Purification and characterization of West Nile virus nucleoside triphosphatase (NTPase)/helicase: Evidence for dissociation of the NTPase and helicase activities of the enzyme
    • Borowski P, Niebuhr A, Mueller O et al.: Purification and characterization of West Nile virus nucleoside triphosphatase (NTPase)/helicase: evidence for dissociation of the NTPase and helicase activities of the enzyme. J. Virol. 75, 3220-3229 (2001).
    • (2001) J. Virol. , vol.75 , pp. 3220-3229
    • Borowski, P.1    Niebuhr, A.2    Mueller, O.3
  • 86
    • 33745025763 scopus 로고    scopus 로고
    • Structural basis for the activation of flaviviral NS3 proteases from dengue and West Nile virus
    • Erbel P, Schiering N, D'Arcy A et al.: Structural basis for the activation of flaviviral NS3 proteases from dengue and West Nile virus. Nat. Struct. Mol. Biol. 13, 372-373 (2006).
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 372-373
    • Erbel, P.1    Schiering, N.2    D'Arcy, A.3
  • 87
    • 34247625945 scopus 로고    scopus 로고
    • Structural evidence for regulation and specificity of flaviviral proteases and evolution of the Flaviviridae fold
    • Aleshin AE, Shiryaev SA, Strongin AY, Liddington RC: Structural evidence for regulation and specificity of flaviviral proteases and evolution of the Flaviviridae fold. Protein Sci. 16, 795-806 (2007).
    • (2007) Protein Sci. , vol.16 , pp. 795-806
    • Aleshin, A.E.1    Shiryaev, S.A.2    Strongin, A.Y.3    Liddington, R.C.4
  • 88
    • 0034802008 scopus 로고    scopus 로고
    • Mutagenesis of the dengue virus type 2 NS3 protein within and outside helicase motifs: Effects on enzyme activity and virus replication
    • Matusan AE, Pryor MJ, Davidson AD, Wright PJ: Mutagenesis of the dengue virus type 2 NS3 protein within and outside helicase motifs: effects on enzyme activity and virus replication. J. Virol. 75, 9633-9643 (2001).
    • (2001) J. Virol. , vol.75 , pp. 9633-9643
    • Matusan, A.E.1    Pryor, M.J.2    Davidson, A.D.3    Wright, P.J.4
  • 89
    • 34748873170 scopus 로고    scopus 로고
    • Knipe DM, Howley PM Eds. Lippincott-Raven Publishers, PA, USA
    • Lindenbach BD, Thiel HJ, Rice CM: Fields Virology. Knipe DM, Howley PM (Eds). Lippincott-Raven Publishers, PA, USA 1101-1152 (2007).
    • (2007) Fields Virology , pp. 1101-1152
    • Lindenbach, B.D.1    Thiel, H.J.2    Rice, C.M.3
  • 90
    • 0027474037 scopus 로고
    • Computer-assisted identification of a putative methyltransferase domain in NS5 protein of aviviruses and λ protein of reovirus
    • Koonin EV: Computer-assisted identification of a putative methyltransferase domain in NS5 protein of aviviruses and λ protein of reovirus. J. Gen. Virol. 74, 733-740 (1993).
    • (1993) J. Gen. Virol. , vol.74 , pp. 733-740
    • Koonin, E.V.1
  • 91
    • 0037013858 scopus 로고    scopus 로고
    • An RNA cap (nucleoside-2"-O)-methyltransferase in the avivirus RNA polymerase NS5: Crystal structure and functional characterization
    • Egloff MP, Benarroch D, Selisko B, Romette JL, Canard B: An RNA cap (nucleoside-2"-O)-methyltransferase in the avivirus RNA polymerase NS5: crystal structure and functional characterization. EMBO J. 21, 2757-2768 (2002).
    • (2002) EMBO J. , vol.21 , pp. 2757-2768
    • Egloff, M.P.1    Benarroch, D.2    Selisko, B.3    Romette, J.L.4    Canard, B.5
  • 92
    • 73249127604 scopus 로고    scopus 로고
    • The flavivirus NS5 protein is a true RNA guanylyltransferase that catalyzes a two-step reaction to form the RNA cap structure
    • Issur O, Geiss BJ, Bougie I et al.: The flavivirus NS5 protein is a true RNA guanylyltransferase that catalyzes a two-step reaction to form the RNA cap structure. RNA 15, 2340-2350 (2009).
    • (2009) RNA , vol.15 , pp. 2340-2350
    • Issur, O.1    Geiss, B.J.2    Bougie, I.3
  • 93
    • 0029863798 scopus 로고    scopus 로고
    • Recombinant dengue type 1 virus Ns5 protein expressed in Escherichia coli exhibits RNA-dependent RNA polymerase activity
    • Tan BH, Fu J, Sugrue RJ, Yap EH, Chan YC, Tan YH: Recombinant dengue type 1 virus Ns5 protein expressed in Escherichia coli exhibits RNA-dependent RNA polymerase activity. Virology 216, 317-325 (1996).
    • (1996) Virology , vol.216 , pp. 317-325
    • Tan, B.H.1    Fu, J.2    Sugrue, R.J.3    Yap, E.H.4    Chan, Y.C.5    Tan, Y.H.6
  • 94
    • 34247113349 scopus 로고    scopus 로고
    • Structure and function of flavivirus NS5 methyltransferase
    • Zhou Y, Ray D, Zhao y et al.: Structure and function of flavivirus NS5 methyltransferase. J. Virol. 81, 3891-3903 (2007).
    • (2007) J. Virol. , vol.81 , pp. 3891-3903
    • Zhou, Y.1    Ray, D.2    Zhao, Y.3
  • 95
    • 33748669852 scopus 로고    scopus 로고
    • West Nile virus 5-cap structure is formed by sequential guanine N-7 and ribose 2-O methylations by nonstructural protein 5
    • Ray D, Shah A, Tilgner M et al.: West Nile virus 5-cap structure is formed by sequential guanine N-7 and ribose 2-O methylations by nonstructural protein 5. J. Virol. 80, 8362-8370 (2006).
    • (2006) J. Virol. , vol.80 , pp. 8362-8370
    • Ray, D.1    Shah, A.2    Tilgner, M.3
  • 96
    • 50049109958 scopus 로고    scopus 로고
    • Flavivirus methyltransferase: A novel antiviral target
    • □ Comprehensive review of the methyltransferase activity in West Nile virus
    • Dong H, Zhang B, Shi PY: Flavivirus methyltransferase: a novel antiviral target. Antiviral Res. 80, 1-10 (2008). □ Comprehensive review of the methyltransferase activity in West Nile virus.
    • (2008) Antiviral Res. , vol.80 , pp. 1-10
    • Dong, H.1    Zhang, B.2    Shi, P.Y.3
  • 97
    • 67650106549 scopus 로고    scopus 로고
    • CRM1-mediated nuclear export of dengue virus RNA polymerase NS5 modulates interleukin-8 induction and virus production
    • □ Describes that NS5 is able to be exported from the nucleus by the exportin CRM1 and, hence, can shuttle between the nucleus and cytoplasm. The nuclear accumulation of NS5 during infection due to CRM1 inhibition coincided with altered kinetics of virus production and decreased induction of the antiviral chemokine IL-8
    • Rawlinson SM, Pryor MJ, Wright PJ, Jans DA: CRM1-mediated nuclear export of dengue virus RNA polymerase NS5 modulates interleukin-8 induction and virus production. J. Biol. Chem. 284, 15589-15597 (2009). □ Describes that NS5 is able to be exported from the nucleus by the exportin CRM1 and, hence, can shuttle between the nucleus and cytoplasm. The nuclear accumulation of NS5 during infection due to CRM1 inhibition coincided with altered kinetics of virus production and decreased induction of the antiviral chemokine IL-8.
    • (2009) J. Biol. Chem. , vol.284 , pp. 15589-15597
    • Rawlinson, S.M.1    Pryor, M.J.2    Wright, P.J.3    Jans, D.A.4
  • 98
    • 0029027850 scopus 로고
    • Association between NS3 and NS5 proteins of dengue virus type-2 in the putative RNA replicase is linked to differential phosphorylation of NS5
    • Kapoor ML, Zhang W, Ramachandra M, Kusukawa J, Ebner KE, Padmanabhan R: Association between NS3 and NS5 proteins of dengue virus type-2 in the putative RNA replicase is linked to differential phosphorylation of NS5. J. Biol. Chem. 270, 19100-19106 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 19100-19106
    • Kapoor, M.L.1    Zhang, W.2    Ramachandra, M.3    Kusukawa, J.4    Ebner, K.E.5    Padmanabhan, R.6
  • 99
    • 0032486596 scopus 로고    scopus 로고
    • Recombinant dengue virus type 1 NS3 protein exhibits specific viral RNA binding and NTPase activity regulated by the NS5 protein
    • □ Reports the binding of NS3 to the 3"-untranslated region UTR of DENV serotype 1 and provides the first evidence that the NTPAase activity of NS3 is regulated by NS5, suggesting a functional association between these two proteins during virus replication
    • Cui T, Sugrue RJ, Xu Q, Lee AK, Chan YC, Fu J: Recombinant dengue virus type 1 NS3 protein exhibits specific viral RNA binding and NTPase activity regulated by the NS5 protein. Virology 246 409-417 (1998). □ Reports the binding of NS3 to the 3"-untranslated region (UTR) of DENV serotype 1 and provides the first evidence that the NTPAase activity of NS3 is regulated by NS5, suggesting a functional association between these two proteins during virus replication.
    • (1998) Virology , vol.246 , pp. 409-417
    • Cui, T.1    Sugrue, R.J.2    Xu, Q.3    Lee, A.K.4    Chan, Y.C.5    Fu, J.6
  • 100
    • 0027349993 scopus 로고
    • Synthesis of dengue virus RNA in vitro: Initiation and the involvement of proteins NS3 and NS5
    • □□ Reports the inhibition of the conversion of RNA form RF to replicative intermediate RI using antibodies against NS3 and NS5 in an in vitro replication assay using cell extracts from DENV-infected cells
    • Bartholomeusz AI, Wright PJ: Synthesis of dengue virus RNA in vitro: initiation and the involvement of proteins NS3 and NS5. Arch. Virol. 128, 111-121 (1993). □□ Reports the inhibition of the conversion of RNA form (RF) to replicative intermediate (RI) using antibodies against NS3 and NS5 in an in vitro replication assay using cell extracts from DENV-infected cells.
    • (1993) Arch. Virol. , vol.128 , pp. 111-121
    • Bartholomeusz, A.I.1    Wright, P.J.2
  • 101
    • 0031953007 scopus 로고    scopus 로고
    • Conversion of dengue virus replicative form RNA (RF) to replicative intermediate (RI) by nonstructural proteins NS-5 and NS-3
    • □□ Reports the conversion of RF to RI of DENV by NS3 and NS5 and the additive effect when both proteins are present in the reaction
    • Raviprakash K, Sinha M, Hayes CG, Porter KR: Conversion of dengue virus replicative form RNA (RF) to replicative intermediate (RI) by nonstructural proteins NS-5 and NS-3. Am. J. Trop. Med. Hyg. 58, 90-95 (1998). □□ Reports the conversion of RF to RI of DENV by NS3 and NS5 and the additive effect when both proteins are present in the reaction.
    • (1998) Am. J. Trop. Med. Hyg. , vol.58 , pp. 90-95
    • Raviprakash, K.1    Sinha, M.2    Hayes, C.G.3    Porter, K.R.4
  • 102
    • 23844440838 scopus 로고    scopus 로고
    • Dengue virus nonstructural protein NS5 induces interleukin-8 transcription and secretion
    • □ Describes that transfection of a p las mid expressing NS5 or a DENV replicon induced IL-8 gene expression and secretion; however, RANTES expression was not induced under these conditions
    • Medin CL, Fitzgerald KA, Rothman AL: Dengue virus nonstructural protein NS5 induces interleukin-8 transcription and secretion. J. Virol. 79, 11053-11061 (2005). □ Describes that transfection of a p las mid expressing NS5 or a DENV replicon induced IL-8 gene expression and secretion; however, RANTES expression was not induced under these conditions.
    • (2005) J. Virol. , vol.79 , pp. 11053-11061
    • Medin, C.L.1    Fitzgerald, K.A.2    Rothman, A.L.3
  • 103
    • 0030882340 scopus 로고    scopus 로고
    • The α chemokine, interleukin 8, inhibits the antiviral action of interferon α
    • Khabar KS, Al-Zoghaibi F, Al-Ahdal MN et al.: The α chemokine, interleukin 8, inhibits the antiviral action of interferon α. J. Exp. Med. 186, 1077-1085 (1997).
    • (1997) J. Exp. Med. , vol.186 , pp. 1077-1085
    • Khabar, K.S.1    Al-Zoghaibi, F.2    Al-Ahdal, M.N.3
  • 104
    • 0027948136 scopus 로고
    • Enhancement human cytomegalovirus replication in a human lung fibroblast cell line by interleukin-8
    • Murayama T, Kuno K, Jisaki F et al.: Enhancement human cytomegalovirus replication in a human lung fibroblast cell line by interleukin-8. J. Virol. 68, 7582-7585 (1994).
    • (1994) J. Virol. , vol.68 , pp. 7582-7585
    • Murayama, T.1    Kuno, K.2    Jisaki, F.3
  • 105
    • 0034879050 scopus 로고    scopus 로고
    • Interleukin-8 stimulates human immunodeficiency virus type 1 replication and is a potential new target for antiretroviral therapy
    • Lane BR, Lore K, Bock PJ et al.: Interleukin-8 stimulates human immunodeficiency virus type 1 replication and is a potential new target for antiretroviral therapy. J. Virol. 75, 8195-8202 (2001).
    • (2001) J. Virol. , vol.75 , pp. 8195-8202
    • Lane, B.R.1    Lore, K.2    Bock, P.J.3
  • 106
    • 0034969251 scopus 로고    scopus 로고
    • Hepatitis C virus nonstructural 5a protein induces interleukin-8, leading to partial inhibition of the interferon-induced antiviral response
    • Polyak SJ, Khalid SA, Khabar DM et al.: Hepatitis C virus nonstructural 5a protein induces interleukin-8, leading to partial inhibition of the interferon-induced antiviral response. J. Virol. 75, 6095-6106 (2001).
    • (2001) J. Virol. , vol.75 , pp. 6095-6106
    • Polyak, S.J.1    Khalid, S.A.2    Khabar, D.M.3
  • 107
    • 33746840523 scopus 로고    scopus 로고
    • Relationships between hepatitis C virus replication and CXCL-8 production in vitro
    • Koo BC, McPoland P, Wagoner JP, Kane OJ, Lohmann V, Polyak SJ: Relationships between hepatitis C virus replication and CXCL-8 production in vitro. J. Virol. 80, 7885-7893 (2006).
    • (2006) J. Virol. , vol.80 , pp. 7885-7893
    • Koo, B.C.1    McPoland, P.2    Wagoner, J.P.3    Kane, O.J.4    Lohmann, V.5    Polyak, S.J.6
  • 108
    • 34250899898 scopus 로고    scopus 로고
    • Nuclear localization of dengue virus nonstructural protein 5 through its importin a/b-recognized nuclear localization sequences is integral to viral infection
    • Pryor M, Rawlinso SM, Butcher RE et al.: Nuclear localization of dengue virus nonstructural protein 5 through its importin a/b-recognized nuclear localization sequences is integral to viral infection. Traffic 8, 795-807 (2007).
    • (2007) Traffic , vol.8 , pp. 795-807
    • Pryor, M.1    Rawlinso, S.M.2    Butcher, R.E.3
  • 109
    • 0030761459 scopus 로고    scopus 로고
    • Translation elongation factor-1 α interacts with the 3' stem-loop region of West Nile virus genomic RNA
    • Blackwell JL, Brinton MA: Translation elongation factor-1 α interacts with the 3' stem-loop region of West Nile virus genomic RNA. J. Virol. 71, 6433-6444 (1997).
    • (1997) J. Virol. , vol.71 , pp. 6433-6444
    • Blackwell, J.L.1    Brinton, M.A.2
  • 110
    • 0036061536 scopus 로고    scopus 로고
    • Translation elongation factor-1 α, La, and PTB interact with the 3' untranslated region of dengue 4 virus RNA
    • □ First paper to report the specific interaction of the cellular proteins La, polypyrimidine tract binding protein PTB and translation elongation factor-1 α to the 3-UTR of DENV
    • De Nova-Ocampo M, Villegas-Sepuveda N, del Angel RM: Translation elongation factor-1 α, La, and PTB interact with the 3' untranslated region of dengue 4 virus RNA. Virology 295, 337-347 (2002). □ First paper to report the specific interaction of the cellular proteins La, polypyrimidine tract binding protein (PTB) and translation elongation factor-1 α to the 3-UTR of DENV.
    • (2002) Virology , vol.295 , pp. 337-347
    • De Nova-Ocampo, M.1    Villegas-Sepuveda, N.2    Del Angel, R.M.3
  • 111
    • 0036888883 scopus 로고    scopus 로고
    • Cell proteins TIA-1 and TIAR interact with the 3' stem-loop of the West Nile virus complementary minus-strand RNA and facilitate virus replication
    • Li W, Kedersha N, Anderson M et al.: Cell proteins TIA-1 and TIAR interact with the 3' stem-loop of the West Nile virus complementary minus-strand RNA and facilitate virus replication. J. Virol. 76, 11989-12000 (2002).
    • (2002) J. Virol. , vol.76 , pp. 11989-12000
    • Li, W.1    Kedersha, N.2    Anderson, M.3
  • 112
    • 0037372070 scopus 로고    scopus 로고
    • Cellular proteins from human monocytes bind to dengue 4 virus minus-strand 3' untranslated region RNA
    • Yocupicio-Monroy RME, Medina F, Reyes-del Valle J et al.: Cellular proteins from human monocytes bind to dengue 4 virus minus-strand 3' untranslated region RNA. J. Virol. 77, 3067-3076 (2003).
    • (2003) J. Virol. , vol.77 , pp. 3067-3076
    • Yocupicio-Monroy, R.M.E.1    Medina, F.2    Reyes-del Valle, J.3
  • 113
    • 1842861928 scopus 로고    scopus 로고
    • La protein binds to NS5 and NS3 and to the 5' and 3' ends of dengue 4 virus RNA
    • □ Reports the interaction of the cellular protein la to the 5-and 3-UTR of DENV
    • Garcia-Montalvo BM, Medina F, del Angel RM: La protein binds to NS5 and NS3 and to the 5' and 3' ends of dengue 4 virus RNA. Virus Res. 102, 141-150 (2004). □ Reports the interaction of the cellular protein la to the 5-and 3-UTR of DENV.
    • (2004) Virus Res. , vol.102 , pp. 141-150
    • Garcia-Montalvo, B.M.1    Medina, F.2    Del Angel, R.M.3
  • 114
    • 35648946315 scopus 로고    scopus 로고
    • Y box-binding protein-1 binds to the dengue virus 3"-untranslated region and mediates antiviral effects
    • □ Describes the isolation and identification of several host cell factors from BHK cells that bind to the UTR of DENV One identified protein, YB-1, shows a repressive role on DENV translation via a mechanism that requires viral genomic sequences
    • Paranjape SM, Harris E: Y box-binding protein-1 binds to the dengue virus 3"-untranslated region and mediates antiviral effects. J. Biol. Chem. 282, 30497-30508 (2007). □ Describes the isolation and identification of several host cell factors from BHK cells that bind to the UTR of DENV One identified protein, YB-1, shows a repressive role on DENV translation via a mechanism that requires viral genomic sequences.
    • (2007) J. Biol. Chem. , vol.282 , pp. 30497-30508
    • Paranjape, S.M.1    Harris, E.2
  • 115
    • 4143091385 scopus 로고    scopus 로고
    • The translation elongation factor 1A in tumorigenesis, signal transduction and apoptosis
    • Lamberti A, Longo O, Marra M et al.: The translation elongation factor 1A in tumorigenesis, signal transduction and apoptosis. Amino Acids 26, 443-448 (2004).
    • (2004) Amino Acids , vol.26 , pp. 443-448
    • Lamberti, A.1    Longo, O.2    Marra, M.3
  • 116
    • 0029149642 scopus 로고
    • BHK cell proteins that bind to the 3' stem-loop structure of the West Nile virus genome RNA
    • Blackwell JL, Brinton MA: BHK cell proteins that bind to the 3' stem-loop structure of the West Nile virus genome RNA. J. Virol. 69, 5650-5658 (1995).
    • (1995) J. Virol. , vol.69 , pp. 5650-5658
    • Blackwell, J.L.1    Brinton, M.A.2
  • 117
    • 0032539680 scopus 로고    scopus 로고
    • RNA polymerase of vesicular stomatitis virus specifically associates with translation elongation factor-1 a for its activity
    • Das T, Mathur M, Gupta AK et al.: RNA polymerase of vesicular stomatitis virus specifically associates with translation elongation factor-1 a for its activity. Proc. Natl Acad. Sci. USA 95, 1449-1454 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1449-1454
    • Das, T.1    Mathur, M.2    Gupta, A.K.3
  • 118
    • 0035941296 scopus 로고    scopus 로고
    • Polypyrimidine tract-binding protein represses splicing of a fibroblast growth factor receptor-2 gene alternative exon through exon sequences
    • Le Guiner C, Plet A, Galiana D et al.: Polypyrimidine tract-binding protein represses splicing of a fibroblast growth factor receptor-2 gene alternative exon through exon sequences. J. Biol. Chem. 276, 43677-43687 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 43677-43687
    • Le Guiner, C.1    Plet, A.2    Galiana, D.3
  • 119
    • 2942629589 scopus 로고    scopus 로고
    • Polypyrimidine tract binding protein modulates efficiency of polyadenylation
    • Castelo-Branco P, Furger A, Wollerton M et al.: Polypyrimidine tract binding protein modulates efficiency of polyadenylation. Mol. Cell. Biol. 24, 4174-4183 (2004).
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4174-4183
    • Castelo-Branco, P.1    Furger, A.2    Wollerton, M.3
  • 120
    • 49349112872 scopus 로고    scopus 로고
    • Polypyrimidine-tract-binding protein: A multifunctional RNA-binding protein
    • Sawicka K, Bushell M, Spriggs KA et al.: Polypyrimidine-tract-binding protein: a multifunctional RNA-binding protein. Biochem. Soc. Trans. 36, 641-647 (2008).
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 641-647
    • Sawicka, K.1    Bushell, M.2    Spriggs, K.A.3
  • 121
    • 33845961718 scopus 로고    scopus 로고
    • The polypyrimidine tract-binding protein (PTB) is involved in the post-transcriptional regulation of human inducible nitric oxide synthase expression
    • Pautz A, Linker K, Hubrich T et al.: The polypyrimidine tract-binding protein (PTB) is involved in the post-transcriptional regulation of human inducible nitric oxide synthase expression. J. Biol. Chem. 281, 32294-32302 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 32294-32302
    • Pautz, A.1    Linker, K.2    Hubrich, T.3
  • 122
    • 0036168869 scopus 로고    scopus 로고
    • Translation of polioviral mRNA is inhibited by cleavage of polypyrimidine tract-binding proteins executed by polioviral 3Cpro
    • Back SH, Kim YK, Kim WJ et al.: Translation of polioviral mRNA is inhibited by cleavage of polypyrimidine tract-binding proteins executed by polioviral 3Cpro. J. Virol. 76, 2529-2542 (2002).
    • (2002) J. Virol. , vol.76 , pp. 2529-2542
    • Back, S.H.1    Kim, Y.K.2    Kim, W.J.3
  • 123
    • 28344442948 scopus 로고    scopus 로고
    • Evidence for an RNA chaperone function of polypyrimidine tract-binding protein in picornavirus translation
    • Song, Y, Tzima E, Ochs K et al.: Evidence for an RNA chaperone function of polypyrimidine tract-binding protein in picornavirus translation. RNA 11, 1809-1824 (2005).
    • (2005) RNA , vol.11 , pp. 1809-1824
    • Song, Y.1    Tzima, E.2    Ochs, K.3
  • 124
    • 33750228022 scopus 로고    scopus 로고
    • Feline calicivirus replication: Requirement for polypyrimidine tract-binding protein is temperature-dependent
    • Karakasiliotis I, Chaudhry Y, Roberts LO et al.: Feline calicivirus replication: requirement for polypyrimidine tract-binding protein is temperature-dependent. J. Gen. Virol. 87, 3339-3347 (2006).
    • (2006) J. Gen. Virol. , vol.87 , pp. 3339-3347
    • Karakasiliotis, I.1    Chaudhry, Y.2    Roberts, L.O.3
  • 125
    • 0029166747 scopus 로고
    • Interaction of polypyrimidine tract-binding protein with the 5' noncoding region of the hepatitis C virus RNA genome and its functional requirement in internal initiation of translation
    • Ali N, Siddiqui A: Interaction of polypyrimidine tract-binding protein with the 5' noncoding region of the hepatitis C virus RNA genome and its functional requirement in internal initiation of translation. J. Virol. 69, 6367-6375 (1995).
    • (1995) J. Virol. , vol.69 , pp. 6367-6375
    • Ali, N.1    Siddiqui, A.2
  • 126
    • 0031746507 scopus 로고    scopus 로고
    • The polypyrimidine tract binding protein (PTB) requirement for internal initiation of translation of cardiovirus RNAs is conditional rather than absolute
    • Kaminski A, Jackson RJ: The polypyrimidine tract binding protein (PTB) requirement for internal initiation of translation of cardiovirus RNAs is conditional rather than absolute. RNA 4, 626-638 (1998).
    • (1998) RNA , vol.4 , pp. 626-638
    • Kaminski, A.1    Jackson, R.J.2
  • 127
    • 0342614202 scopus 로고    scopus 로고
    • Transient expression of cellular polypyrimidine-tract binding protein stimulates cap-independent translation directed by both picornaviral and flaviviral internal ribosome entry sites in vivo
    • Gosert KH, Rijnbrand R, Yi M et al.: Transient expression of cellular polypyrimidine-tract binding protein stimulates cap-independent translation directed by both picornaviral and flaviviral internal ribosome entry sites in vivo. Mol. Cell. Biol. 20, 1583-1595 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1583-1595
    • Gosert, K.H.1    Rijnbrand, R.2    Yi, M.3
  • 128
    • 0033559870 scopus 로고    scopus 로고
    • HnRNP C and polypyrimidine tract-binding protein specifically interact with the pyrimidine-rich region within the 3'NTR of the HCV RNA genome
    • Gontarek RR, Gutshall LL, Herold KM et al.: hnRNP C and polypyrimidine tract-binding protein specifically interact with the pyrimidine-rich region within the 3'NTR of the HCV RNA genome. Nucleic Acids Res. 27, 1457-1463 (1999).
    • (1999) Nucleic Acids Res. , vol.27 , pp. 1457-1463
    • Gontarek, R.R.1    Gutshall, L.L.2    Herold, K.M.3
  • 129
    • 30644468137 scopus 로고    scopus 로고
    • Polypyrimidine tract-binding protein interacts with the 3' stem-loop region of Japanese encephalitis virus negative-strand RNA
    • Kim SM, Jeong YS: Polypyrimidine tract-binding protein interacts with the 3' stem-loop region of Japanese encephalitis virus negative-strand RNA. Virus Res. 115, 131-140 (2006).
    • (2006) Virus Res. , vol.115 , pp. 131-140
    • Kim, S.M.1    Jeong, Y.S.2
  • 130
    • 33745713127 scopus 로고    scopus 로고
    • Polypyrimidine-tract-binding protein is a component of the HCV RNA replication complex and necessary for RNA synthesis
    • Aizaki H, Choi KS, Liu M et al.: Polypyrimidine-tract-binding protein is a component of the HCV RNA replication complex and necessary for RNA synthesis. J. Biomed. Sci. 13, 469-480 (2006).
    • (2006) J. Biomed. Sci. , vol.13 , pp. 469-480
    • Aizaki, H.1    Choi, K.S.2    Liu, M.3
  • 131
    • 70849127442 scopus 로고    scopus 로고
    • Polypyrimidine tract-binding protein is relocated to the cytoplasm and is required during dengue virus infection in Vero cells
    • □ Provides evidence that, during DENV infection, PTB moves from the nucleus to the cytoplasm and plays an important role in the DENV replicative cycle
    • Agis-Juárez RA, Galván I, Medina F et al.: Polypyrimidine tract-binding protein is relocated to the cytoplasm and is required during dengue virus infection in Vero cells. J. Gen. Virol. 90, 2893-2901 (2009). □ Provides evidence that, during DENV infection, PTB moves from the nucleus to the cytoplasm and plays an important role in the DENV replicative cycle.
    • (2009) J. Gen. Virol. , vol.90 , pp. 2893-2901
    • Agis-Juárez, R.A.1    Galván, I.2    Medina, F.3
  • 132
    • 67650520190 scopus 로고    scopus 로고
    • The polypyrimidine tract-binding protein is required for effcient dengue virus propagation and associates with the viral replication machinery
    • □ Provides evidence that PTB interacts with the replication complex of DENV and is acting at the level of viral RNA replication
    • Anwar A, Leong KM, Ng L et al.: The polypyrimidine tract-binding protein is required for effcient dengue virus propagation and associates with the viral replication machinery. J Biol. Chem. 284, 17021-17029 (2009). □ Provides evidence that PTB interacts with the replication complex of DENV and is acting at the level of viral RNA replication.
    • (2009) J. Biol. Chem. , vol.284 , pp. 17021-17029
    • Anwar, A.1    Leong, K.M.2    Ng, L.3
  • 133
    • 67349133117 scopus 로고    scopus 로고
    • Polypyrimidine tract-binding protein influences negative strand RNA synthesis of dengue virus
    • □ Shows the interaction of DENV NS4A protein with PTB and its role in DENV replication
    • Jiang L, Yao H, Duan X et al.: Polypyrimidine tract-binding protein influences negative strand RNA synthesis of dengue virus. Biochem. Biophys. Res. Com. 385, 187-192 (2009). □ Shows the interaction of DENV NS4A protein with PTB and its role in DENV replication.
    • (2009) Biochem. Biophys. Res. Com , vol.385 , pp. 187-192
    • Jiang, L.1    Yao, H.2    Duan, X.3
  • 134
    • 18144404977 scopus 로고    scopus 로고
    • The polypyrimidine tract binding protein is required for efficient picornavirus gene expression and propagation
    • Florez PM, Sessions OM, Wagner EJ et al.: The polypyrimidine tract binding protein is required for efficient picornavirus gene expression and propagation. J. Virol. 79, 6172-6179 (2005).
    • (2005) J. Virol. , vol.79 , pp. 6172-6179
    • Florez, P.M.1    Sessions, O.M.2    Wagner, E.J.3
  • 135
    • 77949714892 scopus 로고    scopus 로고
    • Polypyrimidine tract binding protein functions as a negative regulator of feline calicivirus translation
    • Karakasiliotis I, Vashist S, Bailey D et al.: Polypyrimidine tract binding protein functions as a negative regulator of feline calicivirus translation. PLoS One 5, e9562 (2010).
    • (2010) PLoS One , vol.5
    • Karakasiliotis, I.1    Vashist, S.2    Bailey, D.3
  • 136
    • 0036920155 scopus 로고    scopus 로고
    • Polypyrimidinetract-binding protein affects transcription but not translation of mouse hepatitis virus RNA
    • Choi KS, Huang P, Lai MM: Polypyrimidinetract-binding protein affects transcription but not translation of mouse hepatitis virus RNA. Virology 303, 58-68 (2002).
    • (2002) Virology , vol.303 , pp. 58-68
    • Choi, K.S.1    Huang, P.2    Lai, M.M.3
  • 137
    • 77951026051 scopus 로고    scopus 로고
    • Polypyrimidine tract-binding protein interacts with coxsackievirus B3 RNA and influences its translation
    • Verma B, Bhattacharyya S, Das S: Polypyrimidine tract-binding protein interacts with coxsackievirus B3 RNA and influences its translation. J. Gen. Virol. 91, 1245-1255 (2010).
    • (2010) J. Gen. Virol. , vol.91 , pp. 1245-1255
    • Verma, B.1    Bhattacharyya, S.2    Das, S.3
  • 138
    • 0029126581 scopus 로고
    • Fasactivated serine/threonine kinase (FAST) phosphorylates TIA-1 during Fas-mediated apoptosis
    • Tian Q, Taupin J, Elledge S et al.: Fasactivated serine/threonine kinase (FAST) phosphorylates TIA-1 during Fas-mediated apoptosis. J. Exp. Med. 182, 865-874 (1995).
    • (1995) J. Exp. Med. , vol.182 , pp. 865-874
    • Tian, Q.1    Taupin, J.2    Elledge, S.3
  • 139
    • 5444257942 scopus 로고    scopus 로고
    • Regulation of cytoplasmic stress granules by apoptosis-inducing factor
    • Candé C, Vahsen N, Métivier D et al.: Regulation of cytoplasmic stress granules by apoptosis-inducing factor. J. Cell Sci. 117, 4461-4468 (2004).
    • (2004) J. Cell. Sci. , vol.117 , pp. 4461-4468
    • Candé, C.1    Vahsen, N.2    Métivier, D.3
  • 140
    • 1942512174 scopus 로고    scopus 로고
    • Post-transcriptional regulation of proinflammatory proteins
    • Anderson P, Phillips K, Stoecklin G et al.: Post-transcriptional regulation of proinflammatory proteins. J. Leukoc. Biol. 76, 42-47 (2004).
    • (2004) J. Leukoc. Biol. , vol.76 , pp. 42-47
    • Anderson, P.1    Phillips, K.2    Stoecklin, G.3
  • 141
    • 0034638837 scopus 로고    scopus 로고
    • Dynamic shuttling of Tia-1 accompanies the recruitment of mRNA to mammalian stress granules
    • Kedersha N, Cho MR, Li W et al.: Dynamic shuttling of Tia-1 accompanies the recruitment of mRNA to mammalian stress granules. J. Cell Biol. 151, 1257-1268 (2000).
    • (2000) J. Cell. Biol. , vol.151 , pp. 1257-1268
    • Kedersha, N.1    Cho, M.R.2    Li, W.3
  • 142
    • 35648933435 scopus 로고    scopus 로고
    • T-cell intracellular antigen-1 (TIA-1)-induced translational silencing promotes the decay of selected mRNAs
    • Yamasaki S, Stoecklin G, Kedersha N et al.: T-cell intracellular antigen-1 (TIA-1)-induced translational silencing promotes the decay of selected mRNAs. J. Biol. Chem. 282, 30070-30077 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 30070-30077
    • Yamasaki, S.1    Stoecklin, G.2    Kedersha, N.3
  • 143
    • 34547456097 scopus 로고    scopus 로고
    • Interaction of TIA-1/TIAR with West Nile and dengue virus products in infected cells interferes with stress granule formation and processing body assembly
    • Emara MM, Brinton MA: Interaction of TIA-1/TIAR with West Nile and dengue virus products in infected cells interferes with stress granule formation and processing body assembly. Proc. Natl Acad. Sci. USA 104, 9041-9046 (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 9041-9046
    • Emara, M.M.1    Brinton, M.A.2
  • 144
    • 9444259316 scopus 로고    scopus 로고
    • The role of nuclear Y-box binding protein 1 as a global marker in drug resistance
    • Kuwano M, Oda Y, Izumi H et al.: The role of nuclear Y-box binding protein 1 as a global marker in drug resistance. Mol. Cancer Ther. 3, 1485-1492 (2004).
    • (2004) Mol. Cancer Ther. , vol.3 , pp. 1485-1492
    • Kuwano, M.1    Oda, Y.2    Izumi, H.3
  • 145
    • 7544225495 scopus 로고    scopus 로고
    • Novel roles of TLR3 tyrosine phosphorylation and PI3 kinase in double-stranded RNA signaling
    • Sarkar SN, Peters KL, Elco CP et al.: Novel roles of TLR3 tyrosine phosphorylation and PI3 kinase in double-stranded RNA signaling. Nat. Struct. Mol. Biol. 11, 1060-1067 (2004).
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 1060-1067
    • Sarkar, S.N.1    Peters, K.L.2    Elco, C.P.3
  • 146
    • 0035858877 scopus 로고    scopus 로고
    • La protein and the trafficking of nascent RNA polymerase III transcripts
    • Maraia RJ: La protein and the trafficking of nascent RNA polymerase III transcripts. J. Cell Biol. 153, F13-F18 (2001).
    • (2001) J. Cell. Biol. , vol.153
    • Maraia, R.J.1
  • 147
    • 0021253722 scopus 로고
    • Nucleotide sequence and host la protein interactions of rabies virus leader RNA
    • Kurilla MG, Cabradilla CD, Holloway BP et al.: Nucleotide sequence and host la protein interactions of rabies virus leader RNA. J. Virol. 50, 773-778 (1984).
    • (1984) J. Virol. , vol.50 , pp. 773-778
    • Kurilla, M.G.1    Cabradilla, C.D.2    Holloway, B.P.3
  • 148
    • 0027193593 scopus 로고
    • La autoantigen enhances and corrects aberrant translation of poliovirus RNA in reticulocyte lysate
    • Meerovitch K, Svitkin y V, Lee HS et al.: La autoantigen enhances and corrects aberrant translation of poliovirus RNA in reticulocyte lysate. J. Virol. 67, 3798-3807 (1993).
    • (1993) J. Virol. , vol.67 , pp. 3798-3807
    • Meerovitch, K.1    Svitkin, Y.V.2    Lee, H.S.3
  • 149
    • 0029760743 scopus 로고    scopus 로고
    • Specific Interaction in vitro and in vivo of glyceraldehyde-3-phosphate dehydrogenase and la protein with cis-acting RNAs of human parainfluenza virus type 3
    • De BP, Gupta S, Zhao H et al.: Specific Interaction in vitro and in vivo of glyceraldehyde-3-phosphate dehydrogenase and la protein with cis-acting RNAs of human parainfluenza virus type 3. J. Biol. Chem. 271, 24728-24735 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 24728-24735
    • De, B.P.1    Gupta, S.2    Zhao, H.3
  • 150
    • 0035830704 scopus 로고    scopus 로고
    • Pyrimidine tract binding protein and la autoantigen interact differently with the 5' untranslated regions of lentiviruses and oncoretrovirus mRNAs
    • Waysbort A, Bonnal S, Audigier S et al.: Pyrimidine tract binding protein and la autoantigen interact differently with the 5' untranslated regions of lentiviruses and oncoretrovirus mRNAs. FEBS Lett. 490, 54-58 (2001).
    • (2001) FEBS Lett. , vol.490 , pp. 54-58
    • Waysbort, A.1    Bonnal, S.2    Audigier, S.3
  • 151
    • 6344262259 scopus 로고    scopus 로고
    • Functional characterization of the interaction between human la and hepatitis B virus RNA
    • Ehlers I, Horke S, Reumann K et al.: Functional characterization of the interaction between human la and hepatitis B virus RNA. J. Biol. Chem. 279, 43437-43447 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 43437-43447
    • Ehlers, I.1    Horke, S.2    Reumann, K.3
  • 152
    • 3042787712 scopus 로고    scopus 로고
    • Leader RNA of Rinderpest virus binds specifically with cellular la protein: A possible role in virus replication
    • Raha T, Pudi R, Das S et al.: Leader RNA of Rinderpest virus binds specifically with cellular la protein: a possible role in virus replication. Virus Res. 104, 101-109 (2004).
    • (2004) Virus Res. , vol.104 , pp. 101-109
    • Raha, T.1    Pudi, R.2    Das, S.3
  • 153
    • 0038485613 scopus 로고    scopus 로고
    • Hepatitis C virus internal ribosome entry site-mediated translation is stimulated by specific interaction of independent regions of human la autoantigen
    • Pudi R, Abhiman S, Srinivasan N et al.: Hepatitis C virus internal ribosome entry site-mediated translation is stimulated by specific interaction of independent regions of human la autoantigen. J. Biol. Chem. 278, 12231-12240 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 12231-12240
    • Pudi, R.1    Abhiman, S.2    Srinivasan, N.3
  • 154
    • 49149128081 scopus 로고    scopus 로고
    • Cellular la protein shields nonsegmented negative-strand RNA viral leader RNA from RIG-I and enhances virus growth by diverse mechanisms
    • Bitko V, Musiyenko A, Bayfield MA et al.: Cellular la protein shields nonsegmented negative-strand RNA viral leader RNA from RIG-I and enhances virus growth by diverse mechanisms. J. Virol. 82, 7977-7987 (2008).
    • (2008) J. Virol. , vol.82 , pp. 7977-7987
    • Bitko, V.1    Musiyenko, A.2    Bayfield, M.A.3
  • 155
    • 67649230014 scopus 로고    scopus 로고
    • La protein binds the predicted loop structures in the 3' non-coding region of Japanese encephalitis virus genome: Role in virus replication
    • Vashist S, Anantpadma M, Sharma H et al.: La protein binds the predicted loop structures in the 3' non-coding region of Japanese encephalitis virus genome: role in virus replication. J. Gen. Virol. 90:1343-1352 (2009).
    • (2009) J. Gen. Virol. , vol.90 , pp. 1343-1352
    • Vashist, S.1    Anantpadma, M.2    Sharma, H.3
  • 156
    • 35548989664 scopus 로고    scopus 로고
    • Mosquito la protein binds to the 3' untranslated region of the positive and negative polarity dengue virus RNAs and relocates to the cytoplasm of infected cells
    • □ Describes that la protein is redistributed in DENV-infected cells from the nucleus to the cytoplasm and the presence of la protein in an in vitro replication system inhibit RNA synthesis in a dose-dependent manner
    • Yocupicio-Monroy M, Padmanabhan R, Medina F et al.: Mosquito la protein binds to the 3' untranslated region of the positive and negative polarity dengue virus RNAs and relocates to the cytoplasm of infected cells. Virology 357, 29-40 (2007). □ Describes that la protein is redistributed in DENV-infected cells from the nucleus to the cytoplasm and the presence of la protein in an in vitro replication system inhibit RNA synthesis in a dose-dependent manner.
    • (2007) Virology , vol.357 , pp. 29-40
    • Yocupicio-Monroy, M.1    Padmanabhan, R.2    Medina, F.3
  • 158
    • 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: Subcellular localization and membrane topology of the dengue virus type 2 non-structural protein 4B. J. Biol. Chem. 281, 8854-8863 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 8854-8863
    • Miller, S.1    Sparacio, S.2    Bartenschlager, R.3
  • 159
    • 0033840553 scopus 로고    scopus 로고
    • Syntaxin 17 is abundant in steroigogenic cells and implicated in smooth endoplasmic reticulum membrane dynamics
    • Steegmaier M, Oorschot V, Klumperman J, Scheller RH: Syntaxin 17 is abundant in steroigogenic cells and implicated in smooth endoplasmic reticulum membrane dynamics Mol. Biol. Cell 11, 2719-2731 (2000).
    • (2000) Mol. Biol. Cell. , vol.11 , pp. 2719-2731
    • Steegmaier, M.1    Oorschot, V.2    Klumperman, J.3    Scheller, R.H.4
  • 160
    • 0032863958 scopus 로고    scopus 로고
    • Markers for trans-Golgi membranes and the intermediate compartment localize to induced membranes with distinct replication functions in flavivirus-infected cells
    • □ Determines the cellular origins of viral-induced membranous structures associated with flaviviral RNA synthesis
    • Mackenzie JM, Jones MK, Westaway EG: Markers for trans-Golgi membranes and the intermediate compartment localize to induced membranes with distinct replication functions in flavivirus-infected cells. J. Virol.. 73, 9555-9567 (1999). □ Determines the cellular origins of viral-induced membranous structures associated with flaviviral RNA synthesis.
    • (1999) J. Virol. , vol.73 , pp. 9555-9567
    • Mackenzie, J.M.1    Jones, M.K.2    Westaway, E.G.3
  • 161
    • 1842850947 scopus 로고    scopus 로고
    • The nonstructural 3 (NS3) protein of dengue virus type 2 interacts with human nuclear receptor binding protein and is associated with alterations in membrane structure
    • Chua JJ, Ng MM, Chow VT: The nonstructural 3 (NS3) protein of dengue virus type 2 interacts with human nuclear receptor binding protein and is associated with alterations in membrane structure. Virus Res. 102, 151-163 (2004).
    • (2004) Virus Res. , vol.102 , pp. 151-163
    • Chua, J.J.1    Ng, M.M.2    Chow, V.T.3
  • 162
    • 33646167045 scopus 로고    scopus 로고
    • Regulated cleavage at the West Nile virus NS4A-2K-NS4B junction play a major role in rearranging cytoplasmic membranes and Golgi trafficking of the NS4A protein
    • Roosendaal J, Westaway EG, Khromykh A, Mackenzie J: Regulated cleavage at the West Nile virus NS4A-2K-NS4B junction play a major role in rearranging cytoplasmic membranes and Golgi trafficking of the NS4A protein. J. Virol. 80, 4623-4632 (2006).
    • (2006) J. Virol. , vol.80 , pp. 4623-4632
    • Roosendaal, J.1    Westaway, E.G.2    Khromykh, A.3    Mackenzie, J.4
  • 163
    • 34247848008 scopus 로고    scopus 로고
    • The nonstructural protein 4A of dengue virus is an integral membrane protein inducing membrane alteration in a 2K-regulated manner
    • Miller S, Kastner S, Krijne-Locker J, Buhler S, Bartenschlager R: The nonstructural protein 4A of dengue virus is an integral membrane protein inducing membrane alteration in a 2K-regulated manner. J. Biol. Chem. 282, 8873-8882 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 8873-8882
    • Miller, S.1    Kastner, S.2    Krijne-Locker, J.3    Buhler, S.4    Bartenschlager, R.5
  • 164
    • 64649097038 scopus 로고    scopus 로고
    • Composition and three-dimensional architecture of the dengue virus replication and assembly sites
    • □□ Describes the composition and 3D structure of DENV-induced membranes involved in replication and assembly. It is worth noting that the electron tomography figures showing high quality images of membranous compartments where the replicative cycle takes place
    • Welsch S, Miller S, Romero-Brey I et al.: Composition and three-dimensional architecture of the dengue virus replication and assembly sites. Cell Host Microbe 5, 365-375 (2009). □□ Describes the composition and 3D structure of DENV-induced membranes involved in replication and assembly. It is worth noting that the electron tomography figures showing high quality images of membranous compartments where the replicative cycle takes place.
    • (2009) Cell. Host Microbe , vol.5 , pp. 365-375
    • Welsch, S.1    Miller, S.2    Romero-Brey, I.3
  • 165
    • 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: Proteins C and NS4B of the flavivirus Kunjin translocate independently into the nucleus. Virology 234, 31-41 (1997).
    • (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
  • 166
    • 0030846512 scopus 로고    scopus 로고
    • Ultrastructure of Kunjin virus-infected cells: Colocalization of NS1 and NS3 with double-stranded RNA and of NS2B with NS3, in virus-induced membrane structures
    • Westaway EG, Mackenzie JM, Kenney MT, Jones MK, Khromykh AA: Ultrastructure of Kunjin virus-infected cells: colocalization of NS1 and NS3 with double-stranded RNA and of NS2B with NS3, in virus-induced membrane structures. J. Virol. 71, 6650-6661 (1997).
    • (1997) J. Virol. , vol.71 , pp. 6650-6661
    • Westaway, E.G.1    Mackenzie, J.M.2    Kenney, M.T.3    Jones, M.K.4    Khromykh, A.A.5
  • 167
    • 73449101533 scopus 로고    scopus 로고
    • Dengue virus capsid protein USURPS lipid droplets for viral particle formation
    • □ Proposes that lipid droplets play multiple roles during the viral lifecycle; they could sequester the viral capsid protein early during infection and provide a scaffold for genome encapsidation
    • Samsa MM, Mondotte JA, Iglesias NG et al.: dengue virus capsid protein USURPS lipid droplets for viral particle formation. PLoS Pathog. 5(10), e1000632 (2009). □ Proposes that lipid droplets play multiple roles during the viral lifecycle; they could sequester the viral capsid protein early during infection and provide a scaffold for genome encapsidation.
    • (2009) PLoS Pathog , vol.5 , Issue.10
    • Samsa, M.M.1    Mondotte, J.A.2    Iglesias, N.G.3
  • 168
    • 34548420660 scopus 로고    scopus 로고
    • Reliance of host cholesterol metabolic pathways for the life cycle of hepatitis C virus
    • Ye J: Reliance of host cholesterol metabolic pathways for the life cycle of hepatitis C virus. PLoS Pathog 3(8), e108 (2007)
    • (2007) PLoS Pathog , vol.3 , Issue.8
    • Ye, J.1
  • 170
    • 67349187399 scopus 로고    scopus 로고
    • Cholesterol biosynthesis modulation regulates dengue viral replication
    • □ Describes that genetic and pharmacological modulation of cholesterol biosynthesis can regulate DENV replication
    • Rothwell C, Lebreton A, Young Ng C et al.: Cholesterol biosynthesis modulation regulates dengue viral replication. Virology 389, 8-19 (2009). □ Describes that genetic and pharmacological modulation of cholesterol biosynthesis can regulate DENV replication.
    • (2009) Virology , vol.389 , pp. 8-19
    • Rothwell, C.1    Lebreton, A.2    Young Ng, C.3
  • 171
    • 70649086972 scopus 로고    scopus 로고
    • JNK phosphorylation, induced during dengue virus infection, is important for viral infection and requires the presence of cholesterol
    • Ceballos-Olvera I, Chávez-Salinas S, Medina F, Ludert JE, del Angel RM: JNK phosphorylation, induced during dengue virus infection, is important for viral infection and requires the presence of cholesterol. Virology 396, 30-36 (2010).
    • (2010) Virology , vol.396 , pp. 30-36
    • Ceballos-Olvera, I.1    Chávez-Salinas, S.2    Medina, F.3    Ludert, J.E.4    Del Angel, R.M.5
  • 172
    • 76249120963 scopus 로고    scopus 로고
    • Antibody-dependent enhancement of dengue virus infection in U937 cells requires cholesterol-rich membrane microdomains
    • Puerta-Guardo H, Mosso C, Medina F, Liprandi F, Ludert JE, del Angel RM: Antibody-dependent enhancement of dengue virus infection in U937 cells requires cholesterol-rich membrane microdomains. J. Gen. Virol. 91, 394-403 (2010).
    • (2010) J. Gen. Virol. , vol.91 , pp. 394-403
    • Puerta-Guardo, H.1    Mosso, C.2    Medina, F.3    Liprandi, F.4    Ludert, J.E.5    Del Angel, R.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.