메뉴 건너뛰기




Volumn 16, Issue 3, 2018, Pages 125-142

Rewiring cellular networks by members of the Flaviviridae family

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; LIPID; UBIQUITIN; ANTIVIRUS AGENT; VIRAL PROTEIN; VIRUS RNA;

EID: 85041860975     PISSN: 17401526     EISSN: 17401534     Source Type: Journal    
DOI: 10.1038/nrmicro.2017.170     Document Type: Review
Times cited : (266)

References (176)
  • 2
    • 85041113760 scopus 로고    scopus 로고
    • [No authors listed.], World Health Organization
    • [No authors listed.] Hepatitis C fact sheet. World Health Organization http://www.who.int/mediacentre/factsheets/fs164/en/(2017).
    • (2017) Hepatitis C Fact Sheet.
  • 3
    • 85014543450 scopus 로고    scopus 로고
    • Hepatitis C virus infection
    • Manns, M. P. et al. Hepatitis C virus infection. Nat. Rev. Dis. Primers. 3, 17006 (2017).
    • (2017) Nat. Rev. Dis. Primers. , vol.3 , pp. 17006
    • Manns, M.P.1
  • 4
    • 84971394553 scopus 로고    scopus 로고
    • The global burden of dengue: An analysis from the Global Burden of Disease Study 2013
    • Stanaway, J. D. et al. The global burden of dengue: an analysis from the Global Burden of Disease Study 2013. Lancet Infect. Dis. 16, 712-723 (2016).
    • (2016) Lancet Infect. Dis. , vol.16 , pp. 712-723
    • Stanaway, J.D.1
  • 5
    • 84942436806 scopus 로고    scopus 로고
    • Efficacy and long-term safety of a dengue vaccine in regions of endemic disease
    • Hadinegoro, S. R. et al. Efficacy and long-term safety of a dengue vaccine in regions of endemic disease. N. Engl. J. Med. 373, 1195-1206 (2015).
    • (2015) N. Engl. J. Med. , vol.373 , pp. 1195-1206
    • Hadinegoro, S.R.1
  • 6
    • 84973582916 scopus 로고    scopus 로고
    • Zika virus: History of a newly emerging arbovirus
    • Wikan, N. & Smith, D. R. Zika virus: history of a newly emerging arbovirus. Lancet Infect. Dis. 16, e119-e126 (2016).
    • (2016) Lancet Infect. Dis. , vol.16 , pp. e119-e126
    • Wikan, N.1    Smith, D.R.2
  • 7
    • 85011891106 scopus 로고    scopus 로고
    • Zika virus pathogenesis and tissue tropism
    • Miner, J. J. & Diamond, M. S. Zika virus pathogenesis and tissue tropism. Cell Host Microbe 21, 134-142 (2017).
    • (2017) Cell Host Microbe , vol.21 , pp. 134-142
    • Miner, J.J.1    Diamond, M.S.2
  • 8
    • 84969248482 scopus 로고    scopus 로고
    • Flaviviridae replication organelles: Oh, what a tangled web we weave
    • Paul, D. & Bartenschlager, R. Flaviviridae replication organelles: oh, what a tangled web we weave. Annu. Rev. Virol. 2, 289-310 (2015).
    • (2015) Annu. Rev. Virol. , vol.2 , pp. 289-310
    • Paul, D.1    Bartenschlager, R.2
  • 9
    • 64649097038 scopus 로고    scopus 로고
    • Composition and three-dimensional architecture of the dengue virus replication and assembly sites
    • Welsch, S. et al. Composition and three-dimensional architecture of the dengue virus replication and assembly sites. Cell Host Microbe 5, 365-375 (2009).
    • (2009) Cell Host Microbe , vol.5 , pp. 365-375
    • Welsch, S.1
  • 10
    • 85014114807 scopus 로고    scopus 로고
    • Ultrastructural characterization of Zika virus replication factories
    • Cortese, M. et al. Ultrastructural characterization of Zika virus replication factories. Cell Rep. 18, 2113-2123 (2017).
    • (2017) Cell Rep. , vol.18 , pp. 2113-2123
    • Cortese, M.1
  • 11
    • 77957201605 scopus 로고    scopus 로고
    • The endoplasmic reticulum provides the membrane platform for biogenesis of the flavivirus replication complex
    • Gillespie, L. K., Hoenen, A., Morgan, G. & Mackenzie, J. M. The endoplasmic reticulum provides the membrane platform for biogenesis of the flavivirus replication complex. J. Virol. 84, 10438-10447 (2010).
    • (2010) J. Virol. , vol.84 , pp. 10438-10447
    • Gillespie, L.K.1    Hoenen, A.2    Morgan, G.3    Mackenzie, J.M.4
  • 12
    • 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, E. G., Mackenzie, J. M., Kenney, M. T., Jones, M. K. & Khromykh, A. A. 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
  • 13
    • 80052281413 scopus 로고    scopus 로고
    • Mitochondrial-associated endoplasmic reticulum membranes (MAM) form innate immune synapses and are targeted by hepatitis C virus
    • Horner, S. M., Liu, H. M., Park, H. S., Briley, J. & Gale, M. Jr. Mitochondrial-associated endoplasmic reticulum membranes (MAM) form innate immune synapses and are targeted by hepatitis C virus. Proc. Natl Acad. Sci. USA 108, 14590-14595 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 14590-14595
    • Horner, S.M.1    Liu, H.M.2    Park, H.S.3    Briley, J.4    Gale, M.5
  • 14
    • 84995550705 scopus 로고    scopus 로고
    • Dengue virus perturbs mitochondrial morphodynamics to dampen innate immune responses
    • Chatel-Chaix, L. et al. Dengue virus perturbs mitochondrial morphodynamics to dampen innate immune responses. Cell Host Microbe 20, 342-356 (2016).
    • (2016) Cell Host Microbe , vol.20 , pp. 342-356
    • Chatel-Chaix, L.1
  • 15
    • 84897546853 scopus 로고    scopus 로고
    • Ultrastructural characterization and three-dimensional architecture of replication sites in dengue virus-infected mosquito cells
    • Junjhon, J. et al. Ultrastructural characterization and three-dimensional architecture of replication sites in dengue virus-infected mosquito cells. J. Virol. 88, 4687-4697 (2014).
    • (2014) J. Virol. , vol.88 , pp. 4687-4697
    • Junjhon, J.1
  • 16
    • 84872010602 scopus 로고    scopus 로고
    • Three-dimensional architecture and biogenesis of membrane structures associated with hepatitis C virus replication
    • Romero-Brey, I. et al. Three-dimensional architecture and biogenesis of membrane structures associated with hepatitis C virus replication. PLOS Pathog. 8, e1003056 (2012).
    • (2012) PLOS Pathog. , vol.8 , pp. e1003056
    • Romero-Brey, I.1
  • 17
    • 84874475890 scopus 로고    scopus 로고
    • Analysis of hepatitis C virus resistance to silibinin in vitro and in vivo points to a novel mechanism involving nonstructural protein 4B
    • Esser-Nobis, K. et al. Analysis of hepatitis C virus resistance to silibinin in vitro and in vivo points to a novel mechanism involving nonstructural protein 4B. Hepatology 57, 953-963 (2013).
    • (2013) Hepatology , vol.57 , pp. 953-963
    • Esser-Nobis, K.1
  • 18
    • 84885995316 scopus 로고    scopus 로고
    • Morphological and biochemical characterization of the membranous hepatitis C virus replication compartment
    • Paul, D., Hoppe, S., Saher, G., Krijnse-Locker, J. & Bartenschlager, R. Morphological and biochemical characterization of the membranous hepatitis C virus replication compartment. J. Virol. 87, 10612-10627 (2013).
    • (2013) J. Virol. , vol.87 , pp. 10612-10627
    • Paul, D.1    Hoppe, S.2    Saher, G.3    Krijnse-Locker, J.4    Bartenschlager, R.5
  • 19
    • 27144513392 scopus 로고    scopus 로고
    • Quantitative analysis of the hepatitis C virus replication complex
    • Quinkert, D., Bartenschlager, R. & Lohmann, V. Quantitative analysis of the hepatitis C virus replication complex. J. Virol. 79, 13594-13605 (2005).
    • (2005) J. Virol. , vol.79 , pp. 13594-13605
    • Quinkert, D.1    Bartenschlager, R.2    Lohmann, V.3
  • 20
    • 0346118919 scopus 로고    scopus 로고
    • Hepatitis C virus non-structural proteins in the probable membranous compartment function in viral genome replication
    • Miyanari, Y. et al. Hepatitis C virus non-structural proteins in the probable membranous compartment function in viral genome replication. J. Biol. Chem. 278, 50301-50308 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 50301-50308
    • Miyanari, Y.1
  • 21
    • 84959562427 scopus 로고    scopus 로고
    • The hepatitis C virus-induced membranous web and associated nuclear transport machinery limit access of pattern recognition receptors to viral replication sites
    • Neufeldt, C. J. et al. The hepatitis C virus-induced membranous web and associated nuclear transport machinery limit access of pattern recognition receptors to viral replication sites. PLOS Pathog. 12, e1005428 (2016).
    • (2016) PLOS Pathog. , vol.12 , pp. e1005428
    • Neufeldt, C.J.1
  • 22
    • 84887275344 scopus 로고    scopus 로고
    • Hepatitis C virus-induced cytoplasmic organelles use the nuclear transport machinery to establish an environment conducive to virus replication
    • Neufeldt, C. J. et al. Hepatitis C virus-induced cytoplasmic organelles use the nuclear transport machinery to establish an environment conducive to virus replication. PLOS Pathog. 9, e1003744 (2013).
    • (2013) PLOS Pathog. , vol.9 , pp. e1003744
    • Neufeldt, C.J.1
  • 23
    • 84894587388 scopus 로고    scopus 로고
    • Dimerization of flavivirus NS4B protein
    • Zou, J. et al. Dimerization of flavivirus NS4B protein. J. Virol. 88, 3379-3391 (2014).
    • (2014) J. Virol. , vol.88 , pp. 3379-3391
    • Zou, J.1
  • 24
    • 79955426289 scopus 로고    scopus 로고
    • Assembly of alphavirus replication complexes from RNA and protein components in a novel trans-replication system in mammalian cells
    • Spuul, P. et al. Assembly of alphavirus replication complexes from RNA and protein components in a novel trans-replication system in mammalian cells. J. Virol. 85, 4739-4751 (2011).
    • (2011) J. Virol. , vol.85 , pp. 4739-4751
    • Spuul, P.1
  • 25
    • 84958087646 scopus 로고    scopus 로고
    • RNA replication and membrane modification require the same functions of alphavirus nonstructural proteins
    • Kallio, K., Hellstrom, K., Jokitalo, E. & Ahola, T. RNA replication and membrane modification require the same functions of alphavirus nonstructural proteins. J. Virol. 90, 1687-1692 (2015).
    • (2015) J. Virol. , vol.90 , pp. 1687-1692
    • Kallio, K.1    Hellstrom, K.2    Jokitalo, E.3    Ahola, T.4
  • 26
    • 85027173207 scopus 로고    scopus 로고
    • Cryo-electron tomography reveals novel features of a viral RNA replication compartment
    • Ertel, K. J. et al. Cryo-electron tomography reveals novel features of a viral RNA replication compartment. eLife 6, e25940 (2017).
    • (2017) ELife , vol.6 , pp. e25940
    • Ertel, K.J.1
  • 27
    • 84894277002 scopus 로고    scopus 로고
    • Flavivirus NS1 structures reveal surfaces for associations with membranes and the immune system
    • Akey, D. L. et al. Flavivirus NS1 structures reveal surfaces for associations with membranes and the immune system. Science 343, 881-885 (2014).
    • (2014) Science , vol.343 , pp. 881-885
    • Akey, D.L.1
  • 28
    • 84980367600 scopus 로고    scopus 로고
    • Extended surface for membrane association in Zika virus NS1 structure
    • Brown, W. C. et al. Extended surface for membrane association in Zika virus NS1 structure. Nat. Struct. Mol. Biol. 23, 865-867 (2016).
    • (2016) Nat. Struct. Mol. Biol. , vol.23 , pp. 865-867
    • Brown, W.C.1
  • 29
    • 84908416018 scopus 로고    scopus 로고
    • Coupling of replication and assembly in flaviviruses
    • Apte-Sengupta, S., Sirohi, D. & Kuhn, R. J. Coupling of replication and assembly in flaviviruses. Curr. Opin. Virol. 9, 134-142 (2014).
    • (2014) Curr. Opin. Virol. , vol.9 , pp. 134-142
    • Apte-Sengupta, S.1    Sirohi, D.2    Kuhn, R.J.3
  • 30
    • 84989961920 scopus 로고    scopus 로고
    • Unique requirement for ESCRT factors in flavivirus particle formation on the endoplasmic reticulum
    • Tabata, K. et al. Unique requirement for ESCRT factors in flavivirus particle formation on the endoplasmic reticulum. Cell Rep. 16, 2339-2347 (2016).
    • (2016) Cell Rep. , vol.16 , pp. 2339-2347
    • Tabata, K.1
  • 31
    • 84940870232 scopus 로고    scopus 로고
    • NS5A domain 1 and polyprotein cleavage kinetics are critical for induction of double-membrane vesicles associated with hepatitis C virus replication
    • Romero-Brey, I. et al. NS5A domain 1 and polyprotein cleavage kinetics are critical for induction of double-membrane vesicles associated with hepatitis C virus replication. mBio 6, e00759 (2015).
    • (2015) MBio , vol.6 , pp. e00759
    • Romero-Brey, I.1
  • 32
    • 0036100578 scopus 로고    scopus 로고
    • Expression of hepatitis C virus proteins induces distinct membrane alterations including a candidate viral replication complex
    • Egger, D. et al. Expression of hepatitis C virus proteins induces distinct membrane alterations including a candidate viral replication complex. J. Virol. 76, 5974-5984 (2002).
    • (2002) J. Virol. , vol.76 , pp. 5974-5984
    • Egger, D.1
  • 33
    • 79960406328 scopus 로고    scopus 로고
    • NS4B self-interaction through conserved C-terminal elements is required for the establishment of functional hepatitis C virus replication complexes
    • Paul, D. et al. NS4B self-interaction through conserved C-terminal elements is required for the establishment of functional hepatitis C virus replication complexes. J. Virol. 85, 6963-6976 (2011).
    • (2011) J. Virol. , vol.85 , pp. 6963-6976
    • Paul, D.1
  • 34
    • 84899430502 scopus 로고    scopus 로고
    • Inhibition of HCV replication by cyclophilin antagonists is linked to replication fitness and occurs by inhibition of membranous web formation
    • Madan, V., Paul, D., Lohmann, V. & Bartenschlager, R. Inhibition of HCV replication by cyclophilin antagonists is linked to replication fitness and occurs by inhibition of membranous web formation. Gastroenterology 146, 1361-1372.e9 (2014).
    • (2014) Gastroenterology , vol.146 , pp. 1361-1361e9
    • Madan, V.1    Paul, D.2    Lohmann, V.3    Bartenschlager, R.4
  • 35
    • 78751512667 scopus 로고    scopus 로고
    • Recruitment and activation of a lipid kinase by hepatitis C virus NS5A is essential for integrity of the membranous replication compartment
    • Reiss, S. et al. Recruitment and activation of a lipid kinase by hepatitis C virus NS5A is essential for integrity of the membranous replication compartment. Cell Host Microbe 9, 32-45 (2011).
    • (2011) Cell Host Microbe , vol.9 , pp. 32-45
    • Reiss, S.1
  • 36
    • 84876520299 scopus 로고    scopus 로고
    • Hepatitis C virus proteins: From structure to function
    • Moradpour, D. & Penin, F. Hepatitis C virus proteins: from structure to function. Curr. Top. Microbiol. Immunol. 369, 113-142 (2013).
    • (2013) Curr. Top. Microbiol. Immunol. , vol.369 , pp. 113-142
    • Moradpour, D.1    Penin, F.2
  • 37
    • 84908295905 scopus 로고    scopus 로고
    • Daclatasvir-like inhibitors of NS5A block early biogenesis of hepatitis C virus-induced membranous replication factories, independent of RNA replication
    • Berger, C. et al. Daclatasvir-like inhibitors of NS5A block early biogenesis of hepatitis C virus-induced membranous replication factories, independent of RNA replication. Gastroenterology 147, 1094-1105. e25 (2014).
    • (2014) Gastroenterology , vol.147 , pp. 1094-1105e25
    • Berger, C.1
  • 38
    • 84891084459 scopus 로고    scopus 로고
    • Revisiting dengue virus-host cell interaction: New insights into molecular and cellular virology
    • Acosta, E. G., Kumar, A. & Bartenschlager, R. Revisiting dengue virus-host cell interaction: new insights into molecular and cellular virology. Adv. Virus Res. 88, 1-109 (2014).
    • (2014) Adv. Virus Res. , vol.88 , pp. 1-109
    • Acosta, E.G.1    Kumar, A.2    Bartenschlager, R.3
  • 39
    • 84879420038 scopus 로고    scopus 로고
    • The molecular and structural basis of advanced antiviral therapy for hepatitis C virus infection
    • Bartenschlager, R., Lohmann, V. & Penin, F. The molecular and structural basis of advanced antiviral therapy for hepatitis C virus infection. Nat. Rev. Microbiol. 11, 482-496 (2013).
    • (2013) Nat. Rev. Microbiol. , vol.11 , pp. 482-496
    • Bartenschlager, R.1    Lohmann, V.2    Penin, F.3
  • 40
    • 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, C. E. & Lobigs, M. 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, 2141-2149 (1998).
    • (1998) J. Virol. , vol.72 , pp. 2141-2149
    • Stocks, C.E.1    Lobigs, M.2
  • 41
    • 0032845108 scopus 로고    scopus 로고
    • Mutagenesis of the NS2B-NS3-mediated cleavage site in the flavivirus capsid protein demonstrates a requirement for coordinated processing
    • Amberg, S. M. & Rice, C. M. Mutagenesis of the NS2B-NS3-mediated cleavage site in the flavivirus capsid protein demonstrates a requirement for coordinated processing. J. Virol. 73, 8083-8094 (1999).
    • (1999) J. Virol. , vol.73 , pp. 8083-8094
    • Amberg, S.M.1    Rice, C.M.2
  • 42
    • 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, C. E., Amberg, S. M., Rice, C. M. & Lobigs, M. 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).
    • (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
  • 43
    • 0345734203 scopus 로고    scopus 로고
    • Inefficient signalase cleavage promotes efficient nucleocapsid incorporation into budding flavivirus membranes
    • Lobigs, M. & Lee, E. Inefficient signalase cleavage promotes efficient nucleocapsid incorporation into budding flavivirus membranes. J. Virol. 78, 178-186 (2004).
    • (2004) J. Virol. , vol.78 , pp. 178-186
    • Lobigs, M.1    Lee, E.2
  • 44
    • 84977606002 scopus 로고    scopus 로고
    • A CRISPR screen defines a signal peptide processing pathway required by flaviviruses
    • Zhang, R. et al. A CRISPR screen defines a signal peptide processing pathway required by flaviviruses. Nature 535, 164-168 (2016).
    • (2016) Nature , vol.535 , pp. 164-168
    • Zhang, R.1
  • 45
    • 85017646246 scopus 로고    scopus 로고
    • The natural product cavinafungin selectively interferes with Zika and dengue virus replication by inhibition of the host signal peptidase
    • Estoppey, D. et al. The natural product cavinafungin selectively interferes with Zika and dengue virus replication by inhibition of the host signal peptidase. Cell Rep. 19, 451-460 (2017).
    • (2017) Cell Rep. , vol.19 , pp. 451-460
    • Estoppey, D.1
  • 46
    • 84962909517 scopus 로고    scopus 로고
    • Glycosylation of dengue virus glycoproteins and their interactions with carbohydrate receptors: Possible targets for antiviral therapy
    • Idris, F., Muharram, S. H. & Diah, S. Glycosylation of dengue virus glycoproteins and their interactions with carbohydrate receptors: possible targets for antiviral therapy. Arch. Virol. 161, 1751-1760 (2016).
    • (2016) Arch. Virol. , vol.161 , pp. 1751-1760
    • Idris, F.1    Muharram, S.H.2    Diah, S.3
  • 47
    • 84890909380 scopus 로고    scopus 로고
    • Post-translational modifications of hepatitis C viral proteins and their biological significance
    • Hundt, J., Li, Z. & Liu, Q. Post-translational modifications of hepatitis C viral proteins and their biological significance. World J. Gastroenterol. 19, 8929-8939 (2013).
    • (2013) World J. Gastroenterol. , vol.19 , pp. 8929-8939
    • Hundt, J.1    Li, Z.2    Liu, Q.3
  • 48
    • 84977639708 scopus 로고    scopus 로고
    • Genetic dissection of Flaviviridae host factors through genome-scale CRISPR screens
    • Marceau, C. D. et al. Genetic dissection of Flaviviridae host factors through genome-scale CRISPR screens. Nature 535, 159-163 (2016).
    • (2016) Nature , vol.535 , pp. 159-163
    • Marceau, C.D.1
  • 49
    • 85029110393 scopus 로고    scopus 로고
    • Dengue virus hijacks a noncanonical oxidoreductase function of a cellular oligosaccharyltransferase complex
    • Lin, D. L. et al. Dengue virus hijacks a noncanonical oxidoreductase function of a cellular oligosaccharyltransferase complex. mBio 8, e00939-17 (2017).
    • (2017) MBio , vol.8 , pp. e00939-e009117
    • Lin, D.L.1
  • 50
    • 84947922826 scopus 로고    scopus 로고
    • Defining Hsp70 subnetworks in dengue virus replication reveals key vulnerability in Flavivirus infection
    • Taguwa, S. et al. Defining Hsp70 subnetworks in dengue virus replication reveals key vulnerability in Flavivirus infection. Cell 163, 1108-1123 (2015).
    • (2015) Cell , vol.163 , pp. 1108-1123
    • Taguwa, S.1
  • 51
    • 85016403131 scopus 로고    scopus 로고
    • The significance of Hsp70 subnetwork for dengue virus lifecycle
    • Taguwa, S. & Frydman, J. The significance of Hsp70 subnetwork for dengue virus lifecycle. Uirusu 65, 179-186 (2015).
    • (2015) Uirusu , vol.65 , pp. 179-186
    • Taguwa, S.1    Frydman, J.2
  • 52
    • 79551513993 scopus 로고    scopus 로고
    • Identification and characterization of the host protein DNAJC14 as a broadly active flavivirus replication modulator
    • Yi, Z. et al. Identification and characterization of the host protein DNAJC14 as a broadly active flavivirus replication modulator. PLOS Pathog. 7, e1001255 (2011).
    • (2011) PLOS Pathog. , vol.7 , pp. e1001255
    • Yi, Z.1
  • 53
    • 84961133909 scopus 로고    scopus 로고
    • Chaperone-assisted protein folding is critical for yellow fever virus NS3/4A cleavage and replication
    • Bozzacco, L. et al. Chaperone-assisted protein folding is critical for yellow fever virus NS3/4A cleavage and replication. J. Virol. 90, 3212-3228 (2016).
    • (2016) J. Virol. , vol.90 , pp. 3212-3228
    • Bozzacco, L.1
  • 54
    • 73149090363 scopus 로고    scopus 로고
    • The heat shock protein inhibitor Quercetin attenuates hepatitis C virus production
    • Gonzalez, O. et al. The heat shock protein inhibitor Quercetin attenuates hepatitis C virus production. Hepatology 50, 1756-1764 (2009).
    • (2009) Hepatology , vol.50 , pp. 1756-1764
    • Gonzalez, O.1
  • 55
    • 77956641825 scopus 로고    scopus 로고
    • Small molecular compounds that inhibit hepatitis C virus replication through destabilizing heat shock cognate 70 messenger RNA
    • Peng, Z. G. et al. Small molecular compounds that inhibit hepatitis C virus replication through destabilizing heat shock cognate 70 messenger RNA. Hepatology 52, 845-853 (2010).
    • (2010) Hepatology , vol.52 , pp. 845-853
    • Peng, Z.G.1
  • 56
    • 84961266484 scopus 로고    scopus 로고
    • Allosteric heat shock protein 70 inhibitors block hepatitis C virus assembly
    • Khachatoorian, R. et al. Allosteric heat shock protein 70 inhibitors block hepatitis C virus assembly. Int. J. Antimicrob. Agents 47, 289-296 (2016).
    • (2016) Int. J. Antimicrob. Agents , vol.47 , pp. 289-296
    • Khachatoorian, R.1
  • 57
    • 84896891900 scopus 로고    scopus 로고
    • The NS5A-binding heat shock proteins HSC70 and HSP70 play distinct roles in the hepatitis C viral life cycle
    • Khachatoorian, R. et al. The NS5A-binding heat shock proteins HSC70 and HSP70 play distinct roles in the hepatitis C viral life cycle. Virology 454-455, 118-127 (2014).
    • (2014) Virology , vol.454-455 , pp. 118-127
    • Khachatoorian, R.1
  • 59
    • 84885772855 scopus 로고    scopus 로고
    • Host-targeting agents in the treatment of hepatitis C: A beginning and an end?
    • Baugh, J. M., Garcia-Rivera, J. A. & Gallay, P. A. Host-targeting agents in the treatment of hepatitis C: a beginning and an end? Antiviral Res. 100, 555-561 (2013).
    • (2013) Antiviral Res. , vol.100 , pp. 555-561
    • Baugh, J.M.1    Garcia-Rivera, J.A.2    Gallay, P.A.3
  • 60
  • 61
    • 84951096003 scopus 로고    scopus 로고
    • Effect of modulation of unfolded protein response pathway on dengue virus infection
    • Diwaker, D., Mishra, K. P. & Ganju, L. Effect of modulation of unfolded protein response pathway on dengue virus infection. Acta Biochim. Biophys. Sin. 47, 960-968 (2015).
    • (2015) Acta Biochim. Biophys. Sin. , vol.47 , pp. 960-968
    • Diwaker, D.1    Mishra, K.P.2    Ganju, L.3
  • 62
    • 84904995477 scopus 로고    scopus 로고
    • A new paradigm: Innate immune sensing of viruses via the unfolded protein response
    • Smith, J. A. A new paradigm: innate immune sensing of viruses via the unfolded protein response. Front. Microbiol. 5, 222 (2014).
    • (2014) Front. Microbiol. , vol.5 , pp. 222
    • Smith, J.A.1
  • 63
    • 66449115318 scopus 로고    scopus 로고
    • Cannabinoid action induces autophagy-mediated cell death through stimulation of ER stress in human glioma cells
    • Salazar, M. et al. Cannabinoid action induces autophagy-mediated cell death through stimulation of ER stress in human glioma cells. J. Clin. Invest. 119, 1359-1372 (2009).
    • (2009) J. Clin. Invest. , vol.119 , pp. 1359-1372
    • Salazar, M.1
  • 64
    • 33845480131 scopus 로고    scopus 로고
    • Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response
    • Bernales, S., McDonald, K. L. & Walter, P. Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response. PLOS Biol. 4, e423 (2006).
    • (2006) PLOS Biol. , vol.4 , pp. e423
    • Bernales, S.1    McDonald, K.L.2    Walter, P.3
  • 65
    • 33845459165 scopus 로고    scopus 로고
    • Autophagy is activated for cell survival after endoplasmic reticulum stress
    • Ogata, M. et al. Autophagy is activated for cell survival after endoplasmic reticulum stress. Mol. Cell. Biol. 26, 9220-9231 (2006).
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 9220-9231
    • Ogata, M.1
  • 66
    • 33749579383 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress triggers autophagy
    • Yorimitsu, T., Nair, U., Yang, Z. & Klionsky, D. J. Endoplasmic reticulum stress triggers autophagy. J. Biol. Chem. 281, 30299-30304 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 30299-30304
    • Yorimitsu, T.1    Nair, U.2    Yang, Z.3    Klionsky, D.J.4
  • 67
    • 0033611157 scopus 로고    scopus 로고
    • RNA-binding proteins TIA-1 and TIAR link the phosphorylation of eIF-2 alpha to the assembly of mammalian stress granules
    • Kedersha, N. L., Gupta, M., Li, W., Miller, I. & Anderson, P. RNA-binding proteins TIA-1 and TIAR link the phosphorylation of eIF-2 alpha to the assembly of mammalian stress granules. J. Cell Biol. 147, 1431-1442 (1999).
    • (1999) J. Cell Biol. , vol.147 , pp. 1431-1442
    • Kedersha, N.L.1    Gupta, M.2    Li, W.3    Miller, I.4    Anderson, P.5
  • 68
    • 65549169178 scopus 로고    scopus 로고
    • Discovery of insect and human dengue virus host factors
    • Sessions, O. M. et al. Discovery of insect and human dengue virus host factors. Nature 458, 1047-1050 (2009).
    • (2009) Nature , vol.458 , pp. 1047-1050
    • Sessions, O.M.1
  • 69
    • 84904875418 scopus 로고    scopus 로고
    • Unfolded protein response in hepatitis C virus infection
    • Chan, S. W. Unfolded protein response in hepatitis C virus infection. Front. Microbiol. 5, 233 (2014).
    • (2014) Front. Microbiol. , vol.5 , pp. 233
    • Chan, S.W.1
  • 70
    • 85014683016 scopus 로고    scopus 로고
    • The role of the unfolded protein response in dengue virus pathogenesis
    • Perera, N., Miller, J. L. & Zitzmann, N. The role of the unfolded protein response in dengue virus pathogenesis. Cell. Microbiol. 19, e12734 (2017).
    • (2017) Cell. Microbiol. , vol.19 , pp. e12734
    • Perera, N.1    Miller, J.L.2    Zitzmann, N.3
  • 71
    • 79954601093 scopus 로고    scopus 로고
    • Dengue virus modulates the unfolded protein response in a time-dependent manner
    • Pena, J. & Harris, E. Dengue virus modulates the unfolded protein response in a time-dependent manner. J. Biol. Chem. 286, 14226-14236 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 14226-14236
    • Pena, J.1    Harris, E.2
  • 72
    • 85014764249 scopus 로고    scopus 로고
    • Flavivirus infection uncouples translation suppression from cellular stress responses
    • Roth, H. et al. Flavivirus infection uncouples translation suppression from cellular stress responses. mBio 8, e02150-16 (2017).
    • (2017) MBio , vol.8 , pp. e02150-e021116
    • Roth, H.1
  • 73
    • 84867167962 scopus 로고    scopus 로고
    • Dynamic oscillation of translation and stress granule formation mark the cellular response to virus infection
    • Ruggieri, A. et al. Dynamic oscillation of translation and stress granule formation mark the cellular response to virus infection. Cell Host Microbe 12, 71-85 (2012).
    • (2012) Cell Host Microbe , vol.12 , pp. 71-85
    • Ruggieri, A.1
  • 74
    • 33644778763 scopus 로고    scopus 로고
    • Dengue virus utilizes a novel strategy for translation initiation when cap-dependent translation is inhibited
    • Edgil, D., Polacek, C. & Harris, E. Dengue virus utilizes a novel strategy for translation initiation when cap-dependent translation is inhibited. J. Virol. 80, 2976-2986 (2006).
    • (2006) J. Virol. , vol.80 , pp. 2976-2986
    • Edgil, D.1    Polacek, C.2    Harris, E.3
  • 75
    • 84923001727 scopus 로고    scopus 로고
    • Understanding the potential of hepatitis C virus internal ribosome entry site domains to modulate translation initiation via their structure and function
    • Khawaja, A., Vopalensky, V. & Pospisek, M. Understanding the potential of hepatitis C virus internal ribosome entry site domains to modulate translation initiation via their structure and function. Wiley Interdiscip. Rev. RNA 6, 211-224 (2015).
    • (2015) Wiley Interdiscip. Rev. RNA , vol.6 , pp. 211-224
    • Khawaja, A.1    Vopalensky, V.2    Pospisek, M.3
  • 76
    • 81255160914 scopus 로고    scopus 로고
    • Viral subversion of the host protein synthesis machinery
    • Walsh, D. & Mohr, I. Viral subversion of the host protein synthesis machinery. Nat. Rev. Microbiol. 9, 860-875 (2011).
    • (2011) Nat. Rev. Microbiol. , vol.9 , pp. 860-875
    • Walsh, D.1    Mohr, I.2
  • 77
    • 84855281405 scopus 로고    scopus 로고
    • UPR-mediated membrane biogenesis in B cells
    • Brewer, J. W. & Jackowski, S. UPR-mediated membrane biogenesis in B cells. Biochem. Res. Int. 2012, 738471 (2012).
    • (2012) Biochem. Res. Int. , vol.2012 , pp. 738471
    • Brewer, J.W.1    Jackowski, S.2
  • 78
    • 0037320265 scopus 로고    scopus 로고
    • A time-dependent phase shift in the mammalian unfolded protein response
    • Yoshida, H. et al. A time-dependent phase shift in the mammalian unfolded protein response. Dev. Cell 4, 265-271 (2003).
    • (2003) Dev. Cell , vol.4 , pp. 265-271
    • Yoshida, H.1
  • 79
    • 78650961487 scopus 로고    scopus 로고
    • Activation of the unfolded protein response and autophagy after hepatitis C virus infection suppresses innate antiviral immunity in vitro
    • Ke, P. Y. & Chen, S. S. Activation of the unfolded protein response and autophagy after hepatitis C virus infection suppresses innate antiviral immunity in vitro. J. Clin. Invest. 121, 37-56 (2011).
    • (2011) J. Clin. Invest. , vol.121 , pp. 37-56
    • Ke, P.Y.1    Chen, S.S.2
  • 80
    • 84899757673 scopus 로고    scopus 로고
    • Hepatitis C virus core protein activates autophagy through EIF2AK3 and ATF6 UPR pathway-mediated MAP1LC3B and ATG12 expression
    • Wang, J. et al. Hepatitis C virus core protein activates autophagy through EIF2AK3 and ATF6 UPR pathway-mediated MAP1LC3B and ATG12 expression. Autophagy 10, 766-784 (2014).
    • (2014) Autophagy , vol.10 , pp. 766-784
    • Wang, J.1
  • 81
    • 0035966269 scopus 로고    scopus 로고
    • XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor
    • Yoshida, H., Matsui, T., Yamamoto, A., Okada, T. & Mori, K. XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell 107, 881-891 (2001).
    • (2001) Cell , vol.107 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 82
    • 84988697134 scopus 로고    scopus 로고
    • Identification of RNA binding proteins associated with dengue virus RNA in infected cells reveals temporally distinct host factor requirements
    • Viktorovskaya, O. V., Greco, T. M., Cristea, I. M. & Thompson, S. R. Identification of RNA binding proteins associated with dengue virus RNA in infected cells reveals temporally distinct host factor requirements. PLOS Negl. Trop. Dis. 10, e0004921 (2016).
    • (2016) PLOS Negl. Trop. Dis. , vol.10 , pp. e0004921
    • Viktorovskaya, O.V.1    Greco, T.M.2    Cristea, I.M.3    Thompson, S.R.4
  • 83
    • 47649089914 scopus 로고    scopus 로고
    • Host gene expression profiling of dengue virus infection in cell lines and patients
    • Fink, J. et al. Host gene expression profiling of dengue virus infection in cell lines and patients. PLOS Negl. Trop. Dis. 1, e86 (2007).
    • (2007) PLOS Negl. Trop. Dis. , vol.1 , pp. e86
    • Fink, J.1
  • 84
    • 84949494650 scopus 로고    scopus 로고
    • Production of infectious dengue virus in Aedes aegypti is dependent on the ubiquitin proteasome pathway
    • Choy, M. M., Sessions, O. M., Gubler, D. J. & Ooi, E. E. Production of infectious dengue virus in Aedes aegypti is dependent on the ubiquitin proteasome pathway. PLOS Negl. Trop. Dis. 9, e0004227 (2015).
    • (2015) PLOS Negl. Trop. Dis. , vol.9 , pp. e0004227
    • Choy, M.M.1    Sessions, O.M.2    Gubler, D.J.3    Ooi, E.E.4
  • 85
    • 85019659633 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of mosquito C6/36 cells reveals host proteins involved in Zika virus infection
    • Xin, Q. L. et al. Quantitative proteomic analysis of mosquito C6/36 cells reveals host proteins involved in Zika virus infection. J. Virol. 91, e00554-17 (2017).
    • (2017) J. Virol. , vol.91 , pp. e00554-e005117
    • Xin, Q.L.1
  • 86
    • 84949514477 scopus 로고    scopus 로고
    • Proteasome inhibition suppresses dengue virus egress in antibody dependent infection
    • Choy, M. M. et al. Proteasome inhibition suppresses dengue virus egress in antibody dependent infection. PLOS Negl. Trop. Dis. 9, e0004058 (2015).
    • (2015) PLOS Negl. Trop. Dis. , vol.9 , pp. e0004058
    • Choy, M.M.1
  • 87
    • 79952427119 scopus 로고    scopus 로고
    • Appraising the roles of CBLL1 and the ubiquitin/proteasome system for flavivirus entry and replication
    • Fernandez-Garcia, M. D. et al. Appraising the roles of CBLL1 and the ubiquitin/proteasome system for flavivirus entry and replication. J. Virol. 85, 2980-2989 (2011).
    • (2011) J. Virol. , vol.85 , pp. 2980-2989
    • Fernandez-Garcia, M.D.1
  • 88
    • 84978985593 scopus 로고    scopus 로고
    • Dengue virus genome uncoating requires ubiquitination
    • Byk, L. A. et al. Dengue virus genome uncoating requires ubiquitination. mBio 7, e00804-16 (2016).
    • (2016) MBio , vol.7 , pp. e00804-e00816
    • Byk, L.A.1
  • 89
    • 84923848394 scopus 로고    scopus 로고
    • Identification of HNRNPK as regulator of hepatitis C virus particle production
    • Poenisch, M. et al. Identification of HNRNPK as regulator of hepatitis C virus particle production. PLOS Pathog. 11, e1004573 (2015).
    • (2015) PLOS Pathog. , vol.11 , pp. e1004573
    • Poenisch, M.1
  • 90
    • 70349513508 scopus 로고    scopus 로고
    • A genome-wide genetic screen for host factors required for hepatitis C virus propagation
    • Li, Q. et al. A genome-wide genetic screen for host factors required for hepatitis C virus propagation. Proc. Natl Acad. Sci. USA 106, 16410-16415 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 16410-16415
    • Li, Q.1
  • 91
    • 0037378613 scopus 로고    scopus 로고
    • Interaction with a ubiquitin-like protein enhances the ubiquitination and degradation of hepatitis C virus RNA-dependent RNA polymerase
    • Gao, L. et al. Interaction with a ubiquitin-like protein enhances the ubiquitination and degradation of hepatitis C virus RNA-dependent RNA polymerase. J. Virol. 77, 4149-4159 (2003).
    • (2003) J. Virol. , vol.77 , pp. 4149-4159
    • Gao, L.1
  • 92
    • 17144382003 scopus 로고    scopus 로고
    • Hepatitis C virus expression suppresses interferon signaling by degrading STAT1
    • Lin, W. et al. Hepatitis C virus expression suppresses interferon signaling by degrading STAT1. Gastroenterology 128, 1034-1041 (2005).
    • (2005) Gastroenterology , vol.128 , pp. 1034-1041
    • Lin, W.1
  • 93
    • 33748488244 scopus 로고    scopus 로고
    • Hepatitis C virus core protein blocks interferon signaling by interaction with the STAT1 SH2 domain
    • Lin, W. et al. Hepatitis C virus core protein blocks interferon signaling by interaction with the STAT1 SH2 domain. J. Virol. 80, 9226-9235 (2006).
    • (2006) J. Virol. , vol.80 , pp. 9226-9235
    • Lin, W.1
  • 94
    • 77952728703 scopus 로고    scopus 로고
    • Suppressor of cytokine signaling 3 suppresses hepatitis C virus replication in an mTOR-dependent manner
    • Shao, R. X. et al. Suppressor of cytokine signaling 3 suppresses hepatitis C virus replication in an mTOR-dependent manner. J. Virol. 84, 6060-6069 (2010).
    • (2010) J. Virol. , vol.84 , pp. 6060-6069
    • Shao, R.X.1
  • 95
    • 85018286074 scopus 로고    scopus 로고
    • GP73 represses host innate immune response to promote virus replication by facilitating MAVS and TRAF6 degradation
    • Zhang, X. et al. GP73 represses host innate immune response to promote virus replication by facilitating MAVS and TRAF6 degradation. PLOS Pathog. 13, e1006321 (2017).
    • (2017) PLOS Pathog. , vol.13 , pp. e1006321
    • Zhang, X.1
  • 96
    • 84877790291 scopus 로고    scopus 로고
    • Hepatitis C virus targets the interferon-alpha JAK/STAT pathway by promoting proteasomal degradation in immune cells and hepatocytes
    • Stevenson, N. J. et al. Hepatitis C virus targets the interferon-alpha JAK/STAT pathway by promoting proteasomal degradation in immune cells and hepatocytes. FEBS Lett. 587, 1571-1578 (2013).
    • (2013) FEBS Lett. , vol.587 , pp. 1571-1578
    • Stevenson, N.J.1
  • 97
    • 84973446526 scopus 로고    scopus 로고
    • Zika virus targets human STAT2 to inhibit type i interferon signaling
    • Grant, A. et al. Zika virus targets human STAT2 to inhibit type I interferon signaling. Cell Host Microbe 19, 882-890 (2016).
    • (2016) Cell Host Microbe , vol.19 , pp. 882-890
    • Grant, A.1
  • 98
    • 84996836490 scopus 로고    scopus 로고
    • Zika virus inhibits type-I interferon production and downstream signaling
    • Kumar, A. et al. Zika virus inhibits type-I interferon production and downstream signaling. EMBO Rep. 17, 1766-1775 (2016).
    • (2016) EMBO Rep. , vol.17 , pp. 1766-1775
    • Kumar, A.1
  • 99
    • 66149146738 scopus 로고    scopus 로고
    • NS5 of dengue virus mediates STAT2 binding and degradation
    • Ashour, J., Laurent-Rolle, M., Shi, P. Y. & Garcia-Sastre, A. NS5 of dengue virus mediates STAT2 binding and degradation. J. Virol. 83, 5408-5418 (2009).
    • (2009) J. Virol. , vol.83 , pp. 5408-5418
    • Ashour, J.1    Laurent-Rolle, M.2    Shi, P.Y.3    Garcia-Sastre, A.4
  • 100
    • 84937699264 scopus 로고    scopus 로고
    • Dengue virus inhibition of autophagic flux and dependency of viral replication on proteasomal degradation of the autophagy receptor p62
    • Metz, P. et al. Dengue virus inhibition of autophagic flux and dependency of viral replication on proteasomal degradation of the autophagy receptor p62. J. Virol. 89, 8026-8041 (2015).
    • (2015) J. Virol. , vol.89 , pp. 8026-8041
    • Metz, P.1
  • 101
    • 84926451754 scopus 로고    scopus 로고
    • HCV induces the expression of Rubicon and UVRAG to temporally regulate the maturation of autophagosomes and viral replication
    • Wang, L., Tian, Y. & Ou, J. H. HCV induces the expression of Rubicon and UVRAG to temporally regulate the maturation of autophagosomes and viral replication. PLOS Pathog. 11, e1004764 (2015).
    • (2015) PLOS Pathog. , vol.11 , pp. e1004764
    • Wang, L.1    Tian, Y.2    Ou, J.H.3
  • 102
    • 79959344614 scopus 로고    scopus 로고
    • Flavivirus NS4A-induced autophagy protects cells against death and enhances virus replication
    • McLean, J. E., Wudzinska, A., Datan, E., Quaglino, D. & Zakeri, Z. Flavivirus NS4A-induced autophagy protects cells against death and enhances virus replication. J. Biol. Chem. 286, 22147-22159 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 22147-22159
    • McLean, J.E.1    Wudzinska, A.2    Datan, E.3    Quaglino, D.4    Zakeri, Z.5
  • 103
    • 84975072206 scopus 로고    scopus 로고
    • Dengue-induced autophagy, virus replication and protection from cell death require ER stress (PERK) pathway activation
    • Datan, E. et al. Dengue-induced autophagy, virus replication and protection from cell death require ER stress (PERK) pathway activation. Cell Death Dis. 7, e2127 (2016).
    • (2016) Cell Death Dis. , vol.7 , pp. e2127
    • Datan, E.1
  • 104
    • 84981742269 scopus 로고    scopus 로고
    • Zika virus NS4A and NS4B proteins deregulate Akt-mTOR signaling in human fetal neural stem cells to inhibit neurogenesis and induce autophagy
    • Liang, Q. et al. Zika virus NS4A and NS4B proteins deregulate Akt-mTOR signaling in human fetal neural stem cells to inhibit neurogenesis and induce autophagy. Cell Stem Cell 19, 663-671 (2016).
    • (2016) Cell Stem Cell , vol.19 , pp. 663-671
    • Liang, Q.1
  • 105
    • 84983732425 scopus 로고    scopus 로고
    • Autophagy-associated dengue vesicles promote viral transmission avoiding antibody neutralization
    • Wu, Y. W. et al. Autophagy-associated dengue vesicles promote viral transmission avoiding antibody neutralization. Sci. Rep. 6, 32243 (2016).
    • (2016) Sci. Rep. , vol.6 , pp. 32243
    • Wu, Y.W.1
  • 106
    • 62749134544 scopus 로고    scopus 로고
    • Co-localization of constituents of the dengue virus translation and replication machinery with amphisomes
    • Panyasrivanit, M., Khakpoor, A., Wikan, N. & Smith, D. R. Co-localization of constituents of the dengue virus translation and replication machinery with amphisomes. J. Gen. Virol. 90, 448-456 (2009).
    • (2009) J. Gen. Virol. , vol.90 , pp. 448-456
    • Panyasrivanit, M.1    Khakpoor, A.2    Wikan, N.3    Smith, D.R.4
  • 107
    • 84861556595 scopus 로고    scopus 로고
    • Replication of hepatitis C virus RNA on autophagosomal membranes
    • Sir, D. et al. Replication of hepatitis C virus RNA on autophagosomal membranes. J. Biol. Chem. 287, 18036-18043 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 18036-18043
    • Sir, D.1
  • 108
    • 85008929952 scopus 로고    scopus 로고
    • The autophagy elongation complex (ATG5-12/16L1) positively regulates HCV replication and is required for wild-type membranous web formation
    • Fahmy, A. M. & Labonte, P. The autophagy elongation complex (ATG5-12/16L1) positively regulates HCV replication and is required for wild-type membranous web formation. Sci. Rep. 7, 40351 (2017).
    • (2017) Sci. Rep. , vol.7 , pp. 40351
    • Fahmy, A.M.1    Labonte, P.2
  • 109
    • 77955515860 scopus 로고    scopus 로고
    • Autophagy protein ATG5 interacts transiently with the hepatitis C virus RNA polymerase (NS5B) early during infection
    • Guevin, C. et al. Autophagy protein ATG5 interacts transiently with the hepatitis C virus RNA polymerase (NS5B) early during infection. Virology 405, 1-7 (2010).
    • (2010) Virology , vol.405 , pp. 1-7
    • Guevin, C.1
  • 110
    • 69549135689 scopus 로고    scopus 로고
    • The autophagy machinery is required to initiate hepatitis C virus replication
    • Dreux, M., Gastaminza, P., Wieland, S. F. & Chisari, F. V. The autophagy machinery is required to initiate hepatitis C virus replication. Proc. Natl Acad. Sci. USA 106, 14046-14051 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 14046-14051
    • Dreux, M.1    Gastaminza, P.2    Wieland, S.F.3    Chisari, F.V.4
  • 111
    • 73449117507 scopus 로고    scopus 로고
    • Autophagy proteins promote hepatitis C virus replication
    • Dreux, M. & Chisari, F. V. Autophagy proteins promote hepatitis C virus replication. Autophagy 5, 1224-1225 (2009).
    • (2009) Autophagy , vol.5 , pp. 1224-1225
    • Dreux, M.1    Chisari, F.V.2
  • 112
    • 84958073576 scopus 로고    scopus 로고
    • Knockdown of autophagy inhibits infectious hepatitis C virus release by the exosomal pathway
    • Shrivastava, S. et al. Knockdown of autophagy inhibits infectious hepatitis C virus release by the exosomal pathway. J. Virol. 90, 1387-1396 (2015).
    • (2015) J. Virol. , vol.90 , pp. 1387-1396
    • Shrivastava, S.1
  • 113
    • 70349634804 scopus 로고    scopus 로고
    • Knockdown of autophagy-related gene decreases the production of infectious hepatitis C virus particles
    • Tanida, I. et al. Knockdown of autophagy-related gene decreases the production of infectious hepatitis C virus particles. Autophagy 5, 937-945 (2009).
    • (2009) Autophagy , vol.5 , pp. 937-945
    • Tanida, I.1
  • 114
    • 85010636696 scopus 로고    scopus 로고
    • Dengue and Zika viruses subvert reticulophagy by NS2B3-mediated cleavage of FAM134B
    • Lennemann, N. J. & Coyne, C. B. Dengue and Zika viruses subvert reticulophagy by NS2B3-mediated cleavage of FAM134B. Autophagy 13, 322-332 (2017).
    • (2017) Autophagy , vol.13 , pp. 322-332
    • Lennemann, N.J.1    Coyne, C.B.2
  • 115
    • 78349237370 scopus 로고    scopus 로고
    • Dengue virus-induced autophagy regulates lipid metabolism
    • Heaton, N. S. & Randall, G. Dengue virus-induced autophagy regulates lipid metabolism. Cell Host Microbe 8, 422-432 (2010).
    • (2010) Cell Host Microbe , vol.8 , pp. 422-432
    • Heaton, N.S.1    Randall, G.2
  • 116
    • 85016104361 scopus 로고    scopus 로고
    • Host-virus interaction of ZIKA virus in modulating disease pathogenesis
    • Routhu, N. K. & Byrareddy, S. N. Host-virus interaction of ZIKA virus in modulating disease pathogenesis. J. Neuroimmune Pharmacol. 12, 219-232 (2017).
    • (2017) J. Neuroimmune Pharmacol. , vol.12 , pp. 219-232
    • Routhu, N.K.1    Byrareddy, S.N.2
  • 117
    • 85019254450 scopus 로고    scopus 로고
    • Dengue virus activates the AMP kinase-mTOR axis to stimulate a proviral lipophagy
    • Jordan, T. X. & Randall, G. Dengue virus activates the AMP kinase-mTOR axis to stimulate a proviral lipophagy. J. Virol. 91, e02020-16 (2017).
    • (2017) J. Virol. , vol.91 , pp. e02020-e020116
    • Jordan, T.X.1    Randall, G.2
  • 118
    • 84899634895 scopus 로고    scopus 로고
    • Hepatitis C virus triggers mitochondrial fission and attenuates apoptosis to promote viral persistence
    • Kim, S. J. et al. Hepatitis C virus triggers mitochondrial fission and attenuates apoptosis to promote viral persistence. Proc. Natl Acad. Sci. USA 111, 6413-6418 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 6413-6418
    • Kim, S.J.1
  • 119
    • 84910629145 scopus 로고    scopus 로고
    • Hepatitis C virus RNA replication and assembly: Living on the fat of the land
    • Paul, D., Madan, V. & Bartenschlager, R. Hepatitis C virus RNA replication and assembly: living on the fat of the land. Cell Host. Microbe 16, 569-579 (2014).
    • (2014) Cell Host. Microbe , vol.16 , pp. 569-579
    • Paul, D.1    Madan, V.2    Bartenschlager, R.3
  • 120
    • 84991509153 scopus 로고    scopus 로고
    • Lipids and flaviviruses, present and future perspectives for the control of dengue, Zika, and West Nile viruses
    • Martin-Acebes, M. A., Vazquez-Calvo, A. & Saiz, J. C. Lipids and flaviviruses, present and future perspectives for the control of dengue, Zika, and West Nile viruses. Prog. Lipid Res. 64, 123-137 (2016).
    • (2016) Prog. Lipid Res. , vol.64 , pp. 123-137
    • Martin-Acebes, M.A.1    Vazquez-Calvo, A.2    Saiz, J.C.3
  • 121
    • 84957889595 scopus 로고    scopus 로고
    • Modification of the host cell lipid metabolism induced by hypolipidemic drugs targeting the acetyl coenzyme A carboxylase impairs West Nile virus replication
    • Merino-Ramos, T. et al. Modification of the host cell lipid metabolism induced by hypolipidemic drugs targeting the acetyl coenzyme A carboxylase impairs West Nile virus replication. Antimicrob. Agents Chemother. 60, 307-315 (2015).
    • (2015) Antimicrob. Agents Chemother. , vol.60 , pp. 307-315
    • Merino-Ramos, T.1
  • 122
    • 85018291520 scopus 로고    scopus 로고
    • DENV up-regulates the HMG-CoA reductase activity through the impairment of AMPK phosphorylation: A potential antiviral target
    • Soto-Acosta, R., Bautista-Carbajal, P., Cervantes-Salazar, M., Angel-Ambrocio, A. H. & Del Angel, R. M. DENV up-regulates the HMG-CoA reductase activity through the impairment of AMPK phosphorylation: a potential antiviral target. PLOS Pathog. 13, e1006257 (2017).
    • (2017) PLOS Pathog. , vol.13 , pp. e1006257
    • Soto-Acosta, R.1    Bautista-Carbajal, P.2    Cervantes-Salazar, M.3    Angel-Ambrocio, A.H.4    Del Angel, R.M.5
  • 123
    • 84880290533 scopus 로고    scopus 로고
    • Hepatitis C virus infection activates an innate pathway involving IKK-alpha in lipogenesis and viral assembly
    • Li, Q., Pene, V., Krishnamurthy, S., Cha, H. & Liang, T. J. Hepatitis C virus infection activates an innate pathway involving IKK-alpha in lipogenesis and viral assembly. Nat. Med. 19, 722-729 (2013).
    • (2013) Nat. Med. , vol.19 , pp. 722-729
    • Li, Q.1    Pene, V.2    Krishnamurthy, S.3    Cha, H.4    Liang, T.J.5
  • 124
    • 84861204033 scopus 로고    scopus 로고
    • Dengue virus infection perturbs lipid homeostasis in infected mosquito cells
    • Perera, R. et al. Dengue virus infection perturbs lipid homeostasis in infected mosquito cells. PLOS Pathog. 8, e1002584 (2012).
    • (2012) PLOS Pathog. , vol.8 , pp. e1002584
    • Perera, R.1
  • 125
    • 84907445590 scopus 로고    scopus 로고
    • The composition of West Nile virus lipid envelope unveils a role of sphingolipid metabolism in flavivirus biogenesis
    • Martin-Acebes, M. A. et al. The composition of West Nile virus lipid envelope unveils a role of sphingolipid metabolism in flavivirus biogenesis. J. Virol. 88, 12041-12054 (2014).
    • (2014) J. Virol. , vol.88 , pp. 12041-12054
    • Martin-Acebes, M.A.1
  • 126
    • 76349125478 scopus 로고    scopus 로고
    • Temporal proteome and lipidome profiles reveal hepatitis C virus-associated reprogramming of hepatocellular metabolism and bioenergetics
    • Diamond, D. L. et al. Temporal proteome and lipidome profiles reveal hepatitis C virus-associated reprogramming of hepatocellular metabolism and bioenergetics. PLOS Pathog. 6, e1000719 (2010).
    • (2010) PLOS Pathog. , vol.6 , pp. e1000719
    • Diamond, D.L.1
  • 127
    • 84959248504 scopus 로고    scopus 로고
    • Positive-strand RNA viruses stimulate host phosphatidylcholine synthesis at viral replication sites
    • Zhang, J. et al. Positive-strand RNA viruses stimulate host phosphatidylcholine synthesis at viral replication sites. Proc. Natl Acad. Sci. USA 113, E1064-E1073 (2016).
    • (2016) Proc. Natl Acad. Sci. USA , vol.113 , pp. E1064-E1073
    • Zhang, J.1
  • 128
    • 84898981360 scopus 로고    scopus 로고
    • Oxysterol-binding protein is a phosphatidylinositol 4-kinase effector required for HCV replication membrane integrity and cholesterol trafficking
    • Wang, H. et al. Oxysterol-binding protein is a phosphatidylinositol 4-kinase effector required for HCV replication membrane integrity and cholesterol trafficking. Gastroenterology 146, 1373-1385.e11 (2014).
    • (2014) Gastroenterology , vol.146 , pp. 1373-1385e11
    • Wang, H.1
  • 129
    • 85037987072 scopus 로고    scopus 로고
    • Hepatitis C virus replication depends on endosomal cholesterol homeostasis
    • Stoeck, I. K. et al. Hepatitis C virus replication depends on endosomal cholesterol homeostasis. J. Virol. 92, e01196-17 (2017).
    • (2017) J. Virol. , vol.92 , pp. e01196-e011117
    • Stoeck, I.K.1
  • 130
    • 84915739732 scopus 로고    scopus 로고
    • Mapping of functional domains of the lipid kinase phosphatidylinositol 4-kinase type III alpha involved in enzymatic activity and hepatitis C virus replication
    • Harak, C. et al. Mapping of functional domains of the lipid kinase phosphatidylinositol 4-kinase type III alpha involved in enzymatic activity and hepatitis C virus replication. J. Virol. 88, 9909-9926 (2014).
    • (2014) J. Virol. , vol.88 , pp. 9909-9926
    • Harak, C.1
  • 131
    • 84908004653 scopus 로고    scopus 로고
    • Modulation of hepatitis C virus genome replication by glycosphingolipids and four-phosphate adaptor protein 2
    • Khan, I. et al. Modulation of hepatitis C virus genome replication by glycosphingolipids and four-phosphate adaptor protein 2. J. Virol. 88, 12276-12295 (2014).
    • (2014) J. Virol. , vol.88 , pp. 12276-12295
    • Khan, I.1
  • 132
    • 84964031103 scopus 로고    scopus 로고
    • Small G Rac1 is involved in replication cycle of dengue serotype 2 virus in EAhy926 cells via the regulation of actin cytoskeleton
    • Zhang, J. et al. Small G Rac1 is involved in replication cycle of dengue serotype 2 virus in EAhy926 cells via the regulation of actin cytoskeleton. Sci. China Life Sci. 59, 487-494 (2016).
    • (2016) Sci. China Life Sci. , vol.59 , pp. 487-494
    • Zhang, J.1
  • 133
    • 70849088745 scopus 로고    scopus 로고
    • Cross-talk between Rac1 and Cdc42 GTPases regulates formation of filopodia required for dengue virus type-2 entry into HMEC-1 cells
    • Zamudio-Meza, H., Castillo-Alvarez, A., Gonzalez-Bonilla, C. & Meza, I. Cross-talk between Rac1 and Cdc42 GTPases regulates formation of filopodia required for dengue virus type-2 entry into HMEC-1 cells. J. Gen. Virol. 90, 2902-2911 (2009).
    • (2009) J. Gen. Virol. , vol.90 , pp. 2902-2911
    • Zamudio-Meza, H.1    Castillo-Alvarez, A.2    Gonzalez-Bonilla, C.3    Meza, I.4
  • 134
    • 84893469407 scopus 로고    scopus 로고
    • Cellular vimentin regulates construction of dengue virus replication complexes through interaction with NS4A protein
    • Teo, C. S. & Chu, J. J. Cellular vimentin regulates construction of dengue virus replication complexes through interaction with NS4A protein. J. Virol. 88, 1897-1913 (2014).
    • (2014) J. Virol. , vol.88 , pp. 1897-1913
    • Teo, C.S.1    Chu, J.J.2
  • 135
    • 50849093525 scopus 로고    scopus 로고
    • Vimentin is required for dengue virus serotype 2 infection but microtubules are not necessary for this process
    • Chen, W. et al. Vimentin is required for dengue virus serotype 2 infection but microtubules are not necessary for this process. Arch. Virol. 153, 1777-1781 (2008).
    • (2008) Arch. Virol. , vol.153 , pp. 1777-1781
    • Chen, W.1
  • 136
    • 67649400809 scopus 로고    scopus 로고
    • Initiation of hepatitis C virus infection requires the dynamic microtubule network: Role of the viral nucleocapsid protein
    • Roohvand, F. et al. Initiation of hepatitis C virus infection requires the dynamic microtubule network: role of the viral nucleocapsid protein. J. Biol. Chem. 284, 13778-13791 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 13778-13791
    • Roohvand, F.1
  • 137
    • 0037377744 scopus 로고    scopus 로고
    • Cytoskeletal requirements for hepatitis C virus (HCV) RNA synthesis in the HCV replicon cell culture system
    • Bost, A. G., Venable, D., Liu, L. & Heinz, B. A. Cytoskeletal requirements for hepatitis C virus (HCV) RNA synthesis in the HCV replicon cell culture system. J. Virol. 77, 4401-4408 (2003).
    • (2003) J. Virol. , vol.77 , pp. 4401-4408
    • Bost, A.G.1    Venable, D.2    Liu, L.3    Heinz, B.A.4
  • 138
    • 84978764257 scopus 로고    scopus 로고
    • Septin 9 induces lipid droplets growth by a phosphatidylinositol-5-phosphate and microtubule-dependent mechanism hijacked by HCV
    • Akil, A. et al. Septin 9 induces lipid droplets growth by a phosphatidylinositol-5-phosphate and microtubule-dependent mechanism hijacked by HCV. Nat. Commun. 7, 12203 (2016).
    • (2016) Nat. Commun. , vol.7 , pp. 12203
    • Akil, A.1
  • 139
    • 84960873341 scopus 로고    scopus 로고
    • Breaching the barrier-The nuclear envelope in virus infection
    • Mettenleiter, T. C. Breaching the barrier-the nuclear envelope in virus infection. J. Mol. Biol. 428, 1949-1961 (2016).
    • (2016) J. Mol. Biol. , vol.428 , pp. 1949-1961
    • Mettenleiter, T.C.1
  • 140
    • 84992079423 scopus 로고    scopus 로고
    • Properties and functions of the dengue virus capsid protein
    • Byk, L. A. & Gamarnik, A. V. Properties and functions of the dengue virus capsid protein. Annu. Rev. Virol. 3, 263-281 (2016).
    • (2016) Annu. Rev. Virol. , vol.3 , pp. 263-281
    • Byk, L.A.1    Gamarnik, A.V.2
  • 141
    • 84875802186 scopus 로고    scopus 로고
    • Nuclear localization of dengue virus nonstructural protein 5 does not strictly correlate with efficient viral RNA replication and inhibition of type i interferon signaling
    • Kumar, A. et al. Nuclear localization of dengue virus nonstructural protein 5 does not strictly correlate with efficient viral RNA replication and inhibition of type I interferon signaling. J. Virol. 87, 4545-4557 (2013).
    • (2013) J. Virol. , vol.87 , pp. 4545-4557
    • Kumar, A.1
  • 142
    • 84881238516 scopus 로고    scopus 로고
    • Serotype-specific differences in dengue virus non-structural protein 5 nuclear localization
    • Hannemann, H. et al. Serotype-specific differences in dengue virus non-structural protein 5 nuclear localization. J. Biol. Chem. 288, 22621-22635 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 22621-22635
    • Hannemann, H.1
  • 143
    • 84936993283 scopus 로고    scopus 로고
    • Hepatitis C virus and host cell nuclear transport machinery: A clandestine affair
    • Bonamassa, B. et al. Hepatitis C virus and host cell nuclear transport machinery: a clandestine affair. Front. Microbiol. 6, 619 (2015).
    • (2015) Front. Microbiol. , vol.6 , pp. 619
    • Bonamassa, B.1
  • 144
    • 84915748288 scopus 로고    scopus 로고
    • Functional characterization of nuclear localization and export signals in hepatitis C virus proteins and their role in the membranous web
    • Levin, A. et al. Functional characterization of nuclear localization and export signals in hepatitis C virus proteins and their role in the membranous web. PLOS ONE 9, e114629 (2014).
    • (2014) PLOS ONE , vol.9 , pp. e114629
    • Levin, A.1
  • 145
    • 85011940678 scopus 로고    scopus 로고
    • Hiding from intracellular pattern recognition receptors, a passive strategy of flavivirus immune evasion
    • Overby, A. K. & Weber, F. Hiding from intracellular pattern recognition receptors, a passive strategy of flavivirus immune evasion. Virulence 2, 238-240 (2011).
    • (2011) Virulence , vol.2 , pp. 238-240
    • Overby, A.K.1    Weber, F.2
  • 146
    • 84959284546 scopus 로고    scopus 로고
    • Proteomics of HCV virions reveals an essential role for the nucleoporin Nup98 in virus morphogenesis
    • Lussignol, M. et al. Proteomics of HCV virions reveals an essential role for the nucleoporin Nup98 in virus morphogenesis. Proc. Natl Acad. Sci. USA 113, 2484-2489 (2016).
    • (2016) Proc. Natl Acad. Sci. USA , vol.113 , pp. 2484-2489
    • Lussignol, M.1
  • 147
    • 85016549700 scopus 로고    scopus 로고
    • Japanese encephalitis virus NS5 inhibits type i interferon (IFN) production by blocking the nuclear translocation of IFN regulatory factor 3 and NF-kappaB
    • Ye, J. et al. Japanese encephalitis virus NS5 inhibits type I interferon (IFN) production by blocking the nuclear translocation of IFN regulatory factor 3 and NF-kappaB. J. Virol. 91, e00039-17 (2017).
    • (2017) J. Virol. , vol.91 , pp. e00039-e000117
    • Ye, J.1
  • 148
    • 85018979408 scopus 로고    scopus 로고
    • Importin beta1 targeting by hepatitis C virus NS3/4A protein restricts IRF3 and NF-kappaB signaling of IFNB1 antiviral response
    • Gagne, B., Tremblay, N., Park, A. Y., Baril, M. & Lamarre, D. Importin beta1 targeting by hepatitis C virus NS3/4A protein restricts IRF3 and NF-kappaB signaling of IFNB1 antiviral response. Traffic 18, 362-377 (2017).
    • (2017) Traffic , vol.18 , pp. 362-377
    • Gagne, B.1    Tremblay, N.2    Park, A.Y.3    Baril, M.4    Lamarre, D.5
  • 149
    • 34548316984 scopus 로고    scopus 로고
    • The lipid droplet is an important organelle for hepatitis C virus production
    • Miyanari, Y. et al. The lipid droplet is an important organelle for hepatitis C virus production. Nat. Cell Biol. 9, 1089-1097 (2007).
    • (2007) Nat. Cell Biol. , vol.9 , pp. 1089-1097
    • Miyanari, Y.1
  • 150
    • 84896871426 scopus 로고    scopus 로고
    • MAM (mitochondria-associated membranes) in mammalian cells: Lipids and beyond
    • Vance, J. E. MAM (mitochondria-associated membranes) in mammalian cells: lipids and beyond. Biochim. Biophys. Acta 1841, 595-609 (2014).
    • (2014) Biochim. Biophys. Acta , vol.1841 , pp. 595-609
    • Vance, J.E.1
  • 151
    • 84995632275 scopus 로고    scopus 로고
    • Dengue virus induces mitochondrial elongation through impairment of Drp1-triggered mitochondrial fission
    • Barbier, V., Lang, D., Valois, S., Rothman, A. L. & Medin, C. L. Dengue virus induces mitochondrial elongation through impairment of Drp1-triggered mitochondrial fission. Virology 500, 149-160 (2017).
    • (2017) Virology , vol.500 , pp. 149-160
    • Barbier, V.1    Lang, D.2    Valois, S.3    Rothman, A.L.4    Medin, C.L.5
  • 152
    • 84953227308 scopus 로고    scopus 로고
    • Dengue virus impairs mitochondrial fusion by cleaving mitofusins
    • Yu, C. Y. et al. Dengue virus impairs mitochondrial fusion by cleaving mitofusins. PLOS Pathog. 11, e1005350 (2015).
    • (2015) PLOS Pathog. , vol.11 , pp. e1005350
    • Yu, C.Y.1
  • 153
    • 85016277255 scopus 로고    scopus 로고
    • Dengue virus NS2B protein targets cGAS for degradation and prevents mitochondrial DNA sensing during infection
    • Aguirre, S. et al. Dengue virus NS2B protein targets cGAS for degradation and prevents mitochondrial DNA sensing during infection. Nat. Microbiol. 2, 17037 (2017).
    • (2017) Nat. Microbiol. , vol.2 , pp. 17037
    • Aguirre, S.1
  • 154
    • 84962234015 scopus 로고    scopus 로고
    • Hepatitis C virus NS5A protein cooperates with phosphatidylinositol 4-kinase IIIalpha to induce mitochondrial fragmentation
    • Siu, G. K. et al. Hepatitis C virus NS5A protein cooperates with phosphatidylinositol 4-kinase IIIalpha to induce mitochondrial fragmentation. Sci. Rep. 6, 23464 (2016).
    • (2016) Sci. Rep. , vol.6 , pp. 23464
    • Siu, G.K.1
  • 155
    • 84896851743 scopus 로고    scopus 로고
    • Hepatitis C virus, mitochondria and auto/mitophagy: Exploiting a host defense mechanism
    • Ruggieri, V. et al. Hepatitis C virus, mitochondria and auto/mitophagy: exploiting a host defense mechanism. World J. Gastroenterol. 20, 2624-2633 (2014).
    • (2014) World J. Gastroenterol. , vol.20 , pp. 2624-2633
    • Ruggieri, V.1
  • 156
    • 84885998217 scopus 로고    scopus 로고
    • Architecture and biogenesis of plus-strand RNA virus replication factories
    • Paul, D. & Bartenschlager, R. Architecture and biogenesis of plus-strand RNA virus replication factories. World J. Virol. 2, 32-48 (2013).
    • (2013) World J. Virol. , vol.2 , pp. 32-48
    • Paul, D.1    Bartenschlager, R.2
  • 158
    • 51649095289 scopus 로고    scopus 로고
    • RNA interference screen for human genes associated with West Nile virus infection
    • Krishnan, M. N. et al. RNA interference screen for human genes associated with West Nile virus infection. Nature 455, 242-245 (2008).
    • (2008) Nature , vol.455 , pp. 242-245
    • Krishnan, M.N.1
  • 159
    • 1642499388 scopus 로고    scopus 로고
    • Structure of the dengue virus envelope protein after membrane fusion
    • Modis, Y., Ogata, S., Clements, D. & Harrison, S. C. Structure of the dengue virus envelope protein after membrane fusion. Nature 427, 313-319 (2004).
    • (2004) Nature , vol.427 , pp. 313-319
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 160
    • 84919459596 scopus 로고    scopus 로고
    • Structure of acidic pH dengue virus showing the fusogenic glycoprotein trimers
    • Zhang, X. et al. Structure of acidic pH dengue virus showing the fusogenic glycoprotein trimers. J. Virol. 89, 743-750 (2015).
    • (2015) J. Virol. , vol.89 , pp. 743-750
    • Zhang, X.1
  • 161
    • 84948988051 scopus 로고    scopus 로고
    • Dengue virus non-structural protein 1 modulates infectious particle production via interaction with the structural proteins
    • Scaturro, P., Cortese, M., Chatel-Chaix, L., Fischl, W. & Bartenschlager, R. Dengue virus non-structural protein 1 modulates infectious particle production via interaction with the structural proteins. PLOS Pathog. 11, e1005277 (2015).
    • (2015) PLOS Pathog. , vol.11 , pp. e1005277
    • Scaturro, P.1    Cortese, M.2    Chatel-Chaix, L.3    Fischl, W.4    Bartenschlager, R.5
  • 162
    • 41349112304 scopus 로고    scopus 로고
    • Structure of the immature dengue virus at low pH primes proteolytic maturation
    • Yu, I. M. et al. Structure of the immature dengue virus at low pH primes proteolytic maturation. Science 319, 1834-1837 (2008).
    • (2008) Science , vol.319 , pp. 1834-1837
    • Yu, I.M.1
  • 163
    • 84956722368 scopus 로고    scopus 로고
    • Coordination of hepatitis C virus assembly by distinct regulatory regions in nonstructural protein 5A
    • Zayas, M., Long, G., Madan, V. & Bartenschlager, R. Coordination of hepatitis C virus assembly by distinct regulatory regions in nonstructural protein 5A. PLOS Pathog. 12, e1005376 (2016).
    • (2016) PLOS Pathog. , vol.12 , pp. e1005376
    • Zayas, M.1    Long, G.2    Madan, V.3    Bartenschlager, R.4
  • 164
    • 84908010481 scopus 로고    scopus 로고
    • Apolipoprotein e likely contributes to a maturation step of infectious hepatitis C virus particles and interacts with viral envelope glycoproteins
    • Lee, J. Y. et al. Apolipoprotein E likely contributes to a maturation step of infectious hepatitis C virus particles and interacts with viral envelope glycoproteins. J. Virol. 88, 12422-12437 (2014).
    • (2014) J. Virol. , vol.88 , pp. 12422-12437
    • Lee, J.Y.1
  • 165
    • 85021792257 scopus 로고    scopus 로고
    • Host-derived apolipoproteins play comparable roles with viral secretory proteins Erns and NS1 in the infectious particle formation of Flaviviridae
    • Fukuhara, T. et al. Host-derived apolipoproteins play comparable roles with viral secretory proteins Erns and NS1 in the infectious particle formation of Flaviviridae. PLOS Pathog. 13, e1006475 (2017).
    • (2017) PLOS Pathog. , vol.13 , pp. e1006475
    • Fukuhara, T.1
  • 166
    • 84991773772 scopus 로고    scopus 로고
    • Ultrastructural organisation of HCV from the bloodstream of infected patients revealed by electron microscopy after specific immunocapture
    • Piver, E. et al. Ultrastructural organisation of HCV from the bloodstream of infected patients revealed by electron microscopy after specific immunocapture. Gut 66, 1487-1495 (2016).
    • (2016) Gut , vol.66 , pp. 1487-1495
    • Piver, E.1
  • 167
    • 84994045380 scopus 로고    scopus 로고
    • Neglected but important role of apolipoprotein e exchange in hepatitis C virus infection
    • Yang, Z. et al. Neglected but important role of apolipoprotein E exchange in hepatitis C virus infection. J. Virol. 90, 9632-9643 (2016).
    • (2016) J. Virol. , vol.90 , pp. 9632-9643
    • Yang, Z.1
  • 168
    • 85020642109 scopus 로고    scopus 로고
    • Maturation of secreted HCV particles by incorporation of secreted ApoE protects from antibodies by enhancing infectivity
    • Bankwitz, D. et al. Maturation of secreted HCV particles by incorporation of secreted ApoE protects from antibodies by enhancing infectivity. J. Hepatol. 67, 480-489 (2017).
    • (2017) J. Hepatol. , vol.67 , pp. 480-489
    • Bankwitz, D.1
  • 169
    • 84987916117 scopus 로고    scopus 로고
    • The quest for host targets to combat dengue virus infections
    • Acosta, E. G. & Bartenschlager, R. The quest for host targets to combat dengue virus infections. Curr. Opin. Virol. 20, 47-54 (2016).
    • (2016) Curr. Opin. Virol. , vol.20 , pp. 47-54
    • Acosta, E.G.1    Bartenschlager, R.2
  • 170
    • 84946593124 scopus 로고    scopus 로고
    • Host-targeting agents to prevent and cure hepatitis C virus infection
    • Zeisel, M. B., Crouchet, E., Baumert, T. F. & Schuster, C. Host-targeting agents to prevent and cure hepatitis C virus infection. Viruses 7, 5659-5685 (2015).
    • (2015) Viruses , vol.7 , pp. 5659-5685
    • Zeisel, M.B.1    Crouchet, E.2    Baumert, T.F.3    Schuster, C.4
  • 171
    • 84942553557 scopus 로고    scopus 로고
    • Alisporivir plus ribavirin, interferon free or in combination with pegylated interferon, for hepatitis C virus genotype 2 or 3 infection
    • Pawlotsky, J. M. et al. Alisporivir plus ribavirin, interferon free or in combination with pegylated interferon, for hepatitis C virus genotype 2 or 3 infection. Hepatology 62, 1013-1023 (2015).
    • (2015) Hepatology , vol.62 , pp. 1013-1023
    • Pawlotsky, J.M.1
  • 172
    • 84940788102 scopus 로고    scopus 로고
    • Randomised clinical trial: Alisporivir combined with peginterferon and ribavirin in treatment-naive patients with chronic HCV genotype 1 infection (ESSENTIAL II)
    • Zeuzem, S. et al. Randomised clinical trial: alisporivir combined with peginterferon and ribavirin in treatment-naive patients with chronic HCV genotype 1 infection (ESSENTIAL II). Aliment. Pharmacol. Ther. 42, 829-844 (2015).
    • (2015) Aliment. Pharmacol. Ther. , vol.42 , pp. 829-844
    • Zeuzem, S.1
  • 173
    • 84904762644 scopus 로고    scopus 로고
    • Efficacy and safety of celgosivir in patients with dengue fever (CELADEN): A phase 1b, randomised, double-blind, placebo-controlled, proof-of-concept trial
    • Low, J. G. et al. Efficacy and safety of celgosivir in patients with dengue fever (CELADEN): a phase 1b, randomised, double-blind, placebo-controlled, proof-of-concept trial. Lancet Infect. Dis. 14, 706-715 (2014).
    • (2014) Lancet Infect. Dis. , vol.14 , pp. 706-715
    • Low, J.G.1
  • 174
    • 84988691039 scopus 로고    scopus 로고
    • Extended evaluation of virological, immunological and pharmacokinetic endpoints of CELADEN: A randomized, placebo-controlled trial of celgosivir in dengue fever patients
    • Sung, C. et al. Extended evaluation of virological, immunological and pharmacokinetic endpoints of CELADEN: a randomized, placebo-controlled trial of celgosivir in dengue fever patients. PLOS Negl. Trop. Dis. 10, e0004851 (2016).
    • (2016) PLOS Negl. Trop. Dis. , vol.10 , pp. e0004851
    • Sung, C.1
  • 175
    • 84955113692 scopus 로고    scopus 로고
    • Optimizing celgosivir therapy in mouse models of dengue virus infection of serotypes 1 and 2: The search for a window for potential therapeutic efficacy
    • Watanabe, S. et al. Optimizing celgosivir therapy in mouse models of dengue virus infection of serotypes 1 and 2: the search for a window for potential therapeutic efficacy. Antiviral Res. 127, 10-19 (2016).
    • (2016) Antiviral Res. , vol.127 , pp. 10-19
    • Watanabe, S.1
  • 176
    • 85041843355 scopus 로고    scopus 로고
    • US National Library of Medicine, ClinicalTrials.gov
    • US National Library of Medicine. ClinicalTrials.gov http://www.clinicaltrials.gov/ct2/show/NCT02569827 (2017).
    • (2017)


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.