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Volumn 32, Issue , 2016, Pages 82-88

(+) RNA virus replication compartments: A safe home for (most) viral replication

Author keywords

[No Author keywords available]

Indexed keywords

RNA VIRUS; VIRUS REPLICATION; BIOSYNTHESIS; EXOSOME; GENETICS; GROWTH, DEVELOPMENT AND AGING; LIPID METABOLISM; METABOLISM; PHYSIOLOGY; VIROLOGY;

EID: 84971389562     PISSN: 13695274     EISSN: 18790364     Source Type: Journal    
DOI: 10.1016/j.mib.2016.05.003     Document Type: Review
Times cited : (59)

References (81)
  • 1
    • 42349086670 scopus 로고    scopus 로고
    • Modification of intracellular membrane structures for virus replication
    • Miller S., Krijnse-Locker J. Modification of intracellular membrane structures for virus replication. Nat Rev Microbiol 2008, 6:363-374.
    • (2008) Nat Rev Microbiol , vol.6 , pp. 363-374
    • Miller, S.1    Krijnse-Locker, J.2
  • 2
    • 0242300174 scopus 로고    scopus 로고
    • Engineered retargeting of viral RNA replication complexes to an alternative intracellular membrane
    • Miller D.J., Schwartz M.D., Dye B.T., Ahlquist P. Engineered retargeting of viral RNA replication complexes to an alternative intracellular membrane. J Virol 2003, 77:12193-12202.
    • (2003) J Virol , vol.77 , pp. 12193-12202
    • Miller, D.J.1    Schwartz, M.D.2    Dye, B.T.3    Ahlquist, P.4
  • 4
    • 84926459204 scopus 로고    scopus 로고
    • Spatiotemporal analysis of hepatitis C virus infection
    • Shulla A., Randall G. Spatiotemporal analysis of hepatitis C virus infection. PLoS Pathog 2015, 11:e1004758.
    • (2015) PLoS Pathog , vol.11
    • Shulla, A.1    Randall, G.2
  • 5
    • 34548679815 scopus 로고    scopus 로고
    • Three-dimensional analysis of a viral RNA replication complex reveals a virus-induced mini-organelle
    • Kopek B.G., Perkins G., Miller D.J., Ellisman M.H., Ahlquist P. Three-dimensional analysis of a viral RNA replication complex reveals a virus-induced mini-organelle. PLoS Biol 2007, 5:e220.
    • (2007) PLoS Biol , vol.5
    • Kopek, B.G.1    Perkins, G.2    Miller, D.J.3    Ellisman, M.H.4    Ahlquist, P.5
  • 6
    • 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 1997, 71:6650-6661.
    • (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
  • 9
    • 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 2013, 87:10612-10627.
    • (2013) J Virol , vol.87 , pp. 10612-10627
    • Paul, D.1    Hoppe, S.2    Saher, G.3    Krijnse-Locker, J.4    Bartenschlager, R.5
  • 10
    • 77956294587 scopus 로고    scopus 로고
    • Ultrastructural and biochemical analyses of hepatitis C virus-associated host cell membranes
    • Ferraris P., Blanchard E., Roingeard P. Ultrastructural and biochemical analyses of hepatitis C virus-associated host cell membranes. J Gen Virol 2010, 91:2230-2237.
    • (2010) J Gen Virol , vol.91 , pp. 2230-2237
    • Ferraris, P.1    Blanchard, E.2    Roingeard, P.3
  • 12
    • 85010222358 scopus 로고    scopus 로고
    • Three-dimensional imaging of the intracellular assembly of a functional viral RNA replicase complex
    • de Castro I.F., Fernandez J.J., Barajas D., Nagy P.D., Risco C. Three-dimensional imaging of the intracellular assembly of a functional viral RNA replicase complex. J Cell Sci 2016, 10.1242/jcs.181586.
    • (2016) J Cell Sci
    • de Castro, I.F.1    Fernandez, J.J.2    Barajas, D.3    Nagy, P.D.4    Risco, C.5
  • 13
    • 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 2010, 84:10438-10447.
    • (2010) J Virol , vol.84 , pp. 10438-10447
    • Gillespie, L.K.1    Hoenen, A.2    Morgan, G.3    Mackenzie, J.M.4
  • 15
    • 80455132064 scopus 로고    scopus 로고
    • The transformation of enterovirus replication structures: a three-dimensional study of single- and double-membrane compartments
    • Limpens R.W., van der Schaar H.M., Kumar D., Koster A.J., Snijder E.J., van Kuppeveld F.J., Barcena M. The transformation of enterovirus replication structures: a three-dimensional study of single- and double-membrane compartments. MBio 2011, 2.
    • (2011) MBio , pp. 2
    • Limpens, R.W.1    van der Schaar, H.M.2    Kumar, D.3    Koster, A.J.4    Snijder, E.J.5    van Kuppeveld, F.J.6    Barcena, M.7
  • 16
    • 84857815535 scopus 로고    scopus 로고
    • Ultrastructural characterization of arterivirus replication structures: reshaping the endoplasmic reticulum to accommodate viral RNA synthesis
    • Knoops K., Barcena M., Limpens R.W., Koster A.J., Mommaas A.M., Snijder E.J. Ultrastructural characterization of arterivirus replication structures: reshaping the endoplasmic reticulum to accommodate viral RNA synthesis. J Virol 2012, 86:2474-2487.
    • (2012) J Virol , vol.86 , pp. 2474-2487
    • Knoops, K.1    Barcena, M.2    Limpens, R.W.3    Koster, A.J.4    Mommaas, A.M.5    Snijder, E.J.6
  • 17
    • 84868117555 scopus 로고    scopus 로고
    • A three-dimensional comparison of tick-borne flavivirus infection in mammalian and tick cell lines
    • Offerdahl D.K., Dorward D.W., Hansen B.T., Bloom M.E. A three-dimensional comparison of tick-borne flavivirus infection in mammalian and tick cell lines. PLoS One 2012, 7:e47912.
    • (2012) PLoS One , vol.7
    • Offerdahl, D.K.1    Dorward, D.W.2    Hansen, B.T.3    Bloom, M.E.4
  • 18
    • 84878209731 scopus 로고    scopus 로고
    • Three-dimensional architecture of tick-borne encephalitis virus replication sites and trafficking of the replicated RNA
    • Miorin L., Romero-Brey I., Maiuri P., Hoppe S., Krijnse-Locker J., Bartenschlager R., Marcello A. Three-dimensional architecture of tick-borne encephalitis virus replication sites and trafficking of the replicated RNA. J Virol 2013, 87:6469-6481.
    • (2013) J Virol , vol.87 , pp. 6469-6481
    • Miorin, L.1    Romero-Brey, I.2    Maiuri, P.3    Hoppe, S.4    Krijnse-Locker, J.5    Bartenschlager, R.6    Marcello, A.7
  • 19
    • 84897546853 scopus 로고    scopus 로고
    • Ultrastructural characterization and three-dimensional architecture of replication sites in dengue virus-infected mosquito cells
    • Junjhon J., Pennington J.G., Edwards T.J., Perera R., Lanman J., Kuhn R.J. Ultrastructural characterization and three-dimensional architecture of replication sites in dengue virus-infected mosquito cells. J Virol 2014, 88:4687-4697.
    • (2014) J Virol , vol.88 , pp. 4687-4697
    • Junjhon, J.1    Pennington, J.G.2    Edwards, T.J.3    Perera, R.4    Lanman, J.5    Kuhn, R.J.6
  • 20
    • 84929589847 scopus 로고    scopus 로고
    • Morphogenesis of endoplasmic reticulum membrane-invaginated vesicles during beet black scorch virus infection: role of auxiliary replication protein and new implications of three-dimensional architecture
    • Cao X., Jin X., Zhang X., Li Y., Wang C., Wang X., Hong J., Wang X., Li D., Zhang Y. Morphogenesis of endoplasmic reticulum membrane-invaginated vesicles during beet black scorch virus infection: role of auxiliary replication protein and new implications of three-dimensional architecture. J Virol 2015, 89:6184-6195.
    • (2015) J Virol , vol.89 , pp. 6184-6195
    • Cao, X.1    Jin, X.2    Zhang, X.3    Li, Y.4    Wang, C.5    Wang, X.6    Hong, J.7    Wang, X.8    Li, D.9    Zhang, Y.10
  • 21
    • 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 2013, 2:32-48.
    • (2013) World J Virol , vol.2 , pp. 32-48
    • Paul, D.1    Bartenschlager, R.2
  • 22
    • 77957957039 scopus 로고    scopus 로고
    • Organelle-like membrane compartmentalization of positive-strand RNA virus replication factories
    • den Boon J.A., Ahlquist P. Organelle-like membrane compartmentalization of positive-strand RNA virus replication factories. Annu Rev Microbiol 2010, 64:241-256.
    • (2010) Annu Rev Microbiol , vol.64 , pp. 241-256
    • den Boon, J.A.1    Ahlquist, P.2
  • 24
    • 78049491884 scopus 로고    scopus 로고
    • Functional Sindbis virus replicative complexes are formed at the plasma membrane
    • Frolova E.I., Gorchakov R., Pereboeva L., Atasheva S., Frolov I. Functional Sindbis virus replicative complexes are formed at the plasma membrane. J Virol 2010, 84:11679-11695.
    • (2010) J Virol , vol.84 , pp. 11679-11695
    • Frolova, E.I.1    Gorchakov, R.2    Pereboeva, L.3    Atasheva, S.4    Frolov, I.5
  • 25
    • 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., Joyce M.A., Levin A., Steenbergen R.H., Pang D., Shields J., Tyrrell D.L., Wozniak R.W. Hepatitis C virus-induced cytoplasmic organelles use the nuclear transport machinery to establish an environment conducive to virus replication. PLoS Pathog 2013, 9:e1003744.
    • (2013) PLoS Pathog , vol.9
    • Neufeldt, C.J.1    Joyce, M.A.2    Levin, A.3    Steenbergen, R.H.4    Pang, D.5    Shields, J.6    Tyrrell, D.L.7    Wozniak, R.W.8
  • 26
    • 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., Joyce M.A., Van Buuren N., Levin A., Kirkegaard K., Gale M., Tyrrell D.L., Wozniak R.W. The hepatitis C virus-induced membranous web and associated nuclear transport machinery limit access of pattern recognition receptors to viral replication sites. PLoS Pathog 2016, 12:e1005428.
    • (2016) PLoS Pathog , vol.12
    • Neufeldt, C.J.1    Joyce, M.A.2    Van Buuren, N.3    Levin, A.4    Kirkegaard, K.5    Gale, M.6    Tyrrell, D.L.7    Wozniak, R.W.8
  • 27
    • 34247559591 scopus 로고    scopus 로고
    • Participation of rab5, an early endosome protein, in hepatitis C virus RNA replication machinery
    • Stone M., Jia S., Heo W.D., Meyer T., Konan K.V. Participation of rab5, an early endosome protein, in hepatitis C virus RNA replication machinery. J Virol 2007, 81:4551-4563.
    • (2007) J Virol , vol.81 , pp. 4551-4563
    • Stone, M.1    Jia, S.2    Heo, W.D.3    Meyer, T.4    Konan, K.V.5
  • 28
  • 30
    • 84870612538 scopus 로고    scopus 로고
    • Biogenesis and dynamics of the coronavirus replicative structures
    • Hagemeijer M.C., Rottier P.J., de Haan C.A. Biogenesis and dynamics of the coronavirus replicative structures. Viruses 2012, 4:3245-3269.
    • (2012) Viruses , vol.4 , pp. 3245-3269
    • Hagemeijer, M.C.1    Rottier, P.J.2    de Haan, C.A.3
  • 31
  • 32
    • 77958004276 scopus 로고    scopus 로고
    • Membrane-shaping host reticulon proteins play crucial roles in viral RNA replication compartment formation and function
    • Diaz A., Wang X., Ahlquist P. Membrane-shaping host reticulon proteins play crucial roles in viral RNA replication compartment formation and function. Proc Natl Acad Sci U S A 2010, 107:16291-16296.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 16291-16296
    • Diaz, A.1    Wang, X.2    Ahlquist, P.3
  • 34
    • 0036204740 scopus 로고    scopus 로고
    • A positive-strand RNA virus replication complex parallels form and function of retrovirus capsids
    • Schwartz M., Chen J., Janda M., Sullivan M., den Boon J., Ahlquist P. A positive-strand RNA virus replication complex parallels form and function of retrovirus capsids. Mol Cell 2002, 9:505-514.
    • (2002) Mol Cell , vol.9 , pp. 505-514
    • Schwartz, M.1    Chen, J.2    Janda, M.3    Sullivan, M.4    den Boon, J.5    Ahlquist, P.6
  • 35
    • 74549189980 scopus 로고    scopus 로고
    • A unique role for the host ESCRT proteins in replication of Tomato bushy stunt virus
    • Barajas D., Jiang Y., Nagy P.D. A unique role for the host ESCRT proteins in replication of Tomato bushy stunt virus. PLoS Pathog 2009, 5:e1000705.
    • (2009) PLoS Pathog , vol.5
    • Barajas, D.1    Jiang, Y.2    Nagy, P.D.3
  • 36
    • 84960142886 scopus 로고    scopus 로고
    • Role of viral RNA and co-opted cellular ESCRT-I and ESCRT-III factors in formation of tombusvirus spherules harboring the tombusvirus replicase
    • Kovalev N., de Castro Martin I.F., Pogany J., Barajas D., Pathak K., Risco C., Nagy P.D. Role of viral RNA and co-opted cellular ESCRT-I and ESCRT-III factors in formation of tombusvirus spherules harboring the tombusvirus replicase. J Virol 2016, 90:3611-3626.
    • (2016) J Virol , vol.90 , pp. 3611-3626
    • Kovalev, N.1    de Castro Martin, I.F.2    Pogany, J.3    Barajas, D.4    Pathak, K.5    Risco, C.6    Nagy, P.D.7
  • 37
    • 84901361971 scopus 로고    scopus 로고
    • Noncanonical role for the host Vps4 AAA+ ATPase ESCRT protein in the formation of Tomato bushy stunt virus replicase
    • Barajas D., Martin I.F., Pogany J., Risco C., Nagy P.D. Noncanonical role for the host Vps4 AAA+ ATPase ESCRT protein in the formation of Tomato bushy stunt virus replicase. PLoS Pathog 2014, 10:e1004087.
    • (2014) PLoS Pathog , vol.10
    • Barajas, D.1    Martin, I.F.2    Pogany, J.3    Risco, C.4    Nagy, P.D.5
  • 38
    • 84926507804 scopus 로고    scopus 로고
    • Host ESCRT proteins are required for bromovirus RNA replication compartment assembly and function
    • Diaz A., Zhang J., Ollwerther A., Wang X., Ahlquist P. Host ESCRT proteins are required for bromovirus RNA replication compartment assembly and function. PLoS Pathog 2015, 11:e1004742.
    • (2015) PLoS Pathog , vol.11
    • Diaz, A.1    Zhang, J.2    Ollwerther, A.3    Wang, X.4    Ahlquist, P.5
  • 39
    • 77958100661 scopus 로고    scopus 로고
    • Dengue virus nonstructural protein 3 redistributes fatty acid synthase to sites of viral replication and increases cellular fatty acid synthesis
    • Heaton N.S., Perera R., Berger K.L., Khadka S., Lacount D.J., Kuhn R.J., Randall G. Dengue virus nonstructural protein 3 redistributes fatty acid synthase to sites of viral replication and increases cellular fatty acid synthesis. Proc Natl Acad Sci U S A 2010, 107:17345-17350.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 17345-17350
    • Heaton, N.S.1    Perera, R.2    Berger, K.L.3    Khadka, S.4    Lacount, D.J.5    Kuhn, R.J.6    Randall, G.7
  • 40
    • 0142092456 scopus 로고    scopus 로고
    • Membrane requirements for uridylylation of the poliovirus VPg protein and viral RNA synthesis in vitro
    • Fogg M.H., Teterina N.L., Ehrenfeld E. Membrane requirements for uridylylation of the poliovirus VPg protein and viral RNA synthesis in vitro. J Virol 2003, 77:11408-11416.
    • (2003) J Virol , vol.77 , pp. 11408-11416
    • Fogg, M.H.1    Teterina, N.L.2    Ehrenfeld, E.3
  • 42
    • 84856427709 scopus 로고    scopus 로고
    • West Nile virus replication requires fatty acid synthesis but is independent on phosphatidylinositol-4-phosphate lipids
    • Martin-Acebes M.A., Blazquez A.B., Jimenez de Oya N., Escribano-Romero E., Saiz J.C. West Nile virus replication requires fatty acid synthesis but is independent on phosphatidylinositol-4-phosphate lipids. PLoS One 2011, 6:e24970.
    • (2011) PLoS One , vol.6
    • Martin-Acebes, M.A.1    Blazquez, A.B.2    Jimenez de Oya, N.3    Escribano-Romero, E.4    Saiz, J.C.5
  • 43
    • 84876461949 scopus 로고    scopus 로고
    • Modulation of fatty acid synthase enzyme activity and expression during hepatitis C virus replication
    • Nasheri N., Joyce M., Rouleau Y., Yang P., Yao S., Tyrrell D.L., Pezacki J.P. Modulation of fatty acid synthase enzyme activity and expression during hepatitis C virus replication. Chem Biol 2013, 20:570-582.
    • (2013) Chem Biol , vol.20 , pp. 570-582
    • Nasheri, N.1    Joyce, M.2    Rouleau, Y.3    Yang, P.4    Yao, S.5    Tyrrell, D.L.6    Pezacki, J.P.7
  • 44
    • 33750459353 scopus 로고    scopus 로고
    • COPI activity coupled with fatty acid biosynthesis is required for viral replication
    • Cherry S., Kunte A., Wang H., Coyne C., Rawson R.B., Perrimon N. COPI activity coupled with fatty acid biosynthesis is required for viral replication. PLoS Pathog 2006, 2:e102.
    • (2006) PLoS Pathog , vol.2
    • Cherry, S.1    Kunte, A.2    Wang, H.3    Coyne, C.4    Rawson, R.B.5    Perrimon, N.6
  • 45
    • 84901296162 scopus 로고    scopus 로고
    • Rab18 facilitates dengue virus infection by targeting fatty acid synthase to sites of viral replication
    • Tang W.C., Lin R.J., Liao C.L., Lin Y.L. Rab18 facilitates dengue virus infection by targeting fatty acid synthase to sites of viral replication. J Virol 2014, 88:6793-6804.
    • (2014) J Virol , vol.88 , pp. 6793-6804
    • Tang, W.C.1    Lin, R.J.2    Liao, C.L.3    Lin, Y.L.4
  • 46
    • 84879513998 scopus 로고    scopus 로고
    • Increased long chain acyl-Coa synthetase activity and fatty acid import is linked to membrane synthesis for development of picornavirus replication organelles
    • Nchoutmboube J.A., Viktorova E.G., Scott A.J., Ford L.A., Pei Z., Watkins P.A., Ernst R.K., Belov G.A. Increased long chain acyl-Coa synthetase activity and fatty acid import is linked to membrane synthesis for development of picornavirus replication organelles. PLoS Pathog 2013, 9:e1003401.
    • (2013) PLoS Pathog , vol.9
    • Nchoutmboube, J.A.1    Viktorova, E.G.2    Scott, A.J.3    Ford, L.A.4    Pei, Z.5    Watkins, P.A.6    Ernst, R.K.7    Belov, G.A.8
  • 49
    • 84928558965 scopus 로고    scopus 로고
    • RNA virus replication depends on enrichment of phosphatidylethanolamine at replication sites in subcellular membranes
    • Xu K., Nagy P.D. RNA virus replication depends on enrichment of phosphatidylethanolamine at replication sites in subcellular membranes. Proc Natl Acad Sci U S A 2015, 112:E1782-E1791.
    • (2015) Proc Natl Acad Sci U S A , vol.112 , pp. E1782-E1791
    • Xu, K.1    Nagy, P.D.2
  • 53
    • 80052284074 scopus 로고    scopus 로고
    • Hepatitis C virus stimulates the phosphatidylinositol 4-kinase III alpha-dependent phosphatidylinositol 4-phosphate production that is essential for its replication
    • Berger K.L., Kelly S.M., Jordan T.X., Tartell M.A., Randall G. Hepatitis C virus stimulates the phosphatidylinositol 4-kinase III alpha-dependent phosphatidylinositol 4-phosphate production that is essential for its replication. J Virol 2011, 85:8870-8883.
    • (2011) J Virol , vol.85 , pp. 8870-8883
    • Berger, K.L.1    Kelly, S.M.2    Jordan, T.X.3    Tartell, M.A.4    Randall, G.5
  • 54
    • 80053962863 scopus 로고    scopus 로고
    • The role of the phosphatidylinositol 4-kinase PI4KA in hepatitis C virus-induced host membrane rearrangement
    • Tai A.W., Salloum S. The role of the phosphatidylinositol 4-kinase PI4KA in hepatitis C virus-induced host membrane rearrangement. PLoS One 2011, 6:e26300.
    • (2011) PLoS One , vol.6
    • Tai, A.W.1    Salloum, S.2
  • 56
    • 84898981360 scopus 로고    scopus 로고
    • Oxysterol-binding protein is a phosphatidylinositol 4-kinase effector required for HCV replication membrane integrity and cholesterol trafficking
    • e1371-1311
    • Wang H., Perry J.W., Lauring A.S., Neddermann P., De Francesco R., Tai A.W. Oxysterol-binding protein is a phosphatidylinositol 4-kinase effector required for HCV replication membrane integrity and cholesterol trafficking. Gastroenterology 2014, 146:1373-1385. e1371-1311.
    • (2014) Gastroenterology , vol.146 , pp. 1373-1385
    • Wang, H.1    Perry, J.W.2    Lauring, A.S.3    Neddermann, P.4    De Francesco, R.5    Tai, A.W.6
  • 57
    • 69549113556 scopus 로고    scopus 로고
    • Role of oxysterol binding protein in hepatitis C virus infection
    • Amako Y., Sarkeshik A., Hotta H., Yates J., Siddiqui A. Role of oxysterol binding protein in hepatitis C virus infection. J Virol 2009, 83:9237-9246.
    • (2009) J Virol , vol.83 , pp. 9237-9246
    • Amako, Y.1    Sarkeshik, A.2    Hotta, H.3    Yates, J.4    Siddiqui, A.5
  • 58
    • 79953215325 scopus 로고    scopus 로고
    • Protein kinase D negatively regulates hepatitis C virus secretion through phosphorylation of oxysterol-binding protein and ceramide transfer protein
    • Amako Y., Syed G.H., Siddiqui A. Protein kinase D negatively regulates hepatitis C virus secretion through phosphorylation of oxysterol-binding protein and ceramide transfer protein. J Biol Chem 2011, 286:11265-11274.
    • (2011) J Biol Chem , vol.286 , pp. 11265-11274
    • Amako, Y.1    Syed, G.H.2    Siddiqui, A.3
  • 59
    • 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., Radujkovic D., Taveneau C., Reiss S., Klein R., Bressanelli S., Lohmann V. 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 2014, 88:9909-9926.
    • (2014) J Virol , vol.88 , pp. 9909-9926
    • Harak, C.1    Radujkovic, D.2    Taveneau, C.3    Reiss, S.4    Klein, R.5    Bressanelli, S.6    Lohmann, V.7
  • 62
    • 84910620039 scopus 로고    scopus 로고
    • Rhinovirus uses a phosphatidylinositol 4-phosphate/cholesterol counter-current for the formation of replication compartments at the ER-Golgi interface
    • Roulin P.S., Lotzerich M., Torta F., Tanner L.B., van Kuppeveld F.J., Wenk M.R., Greber U.F. Rhinovirus uses a phosphatidylinositol 4-phosphate/cholesterol counter-current for the formation of replication compartments at the ER-Golgi interface. Cell Host Microbe 2014, 16:677-690.
    • (2014) Cell Host Microbe , vol.16 , pp. 677-690
    • Roulin, P.S.1    Lotzerich, M.2    Torta, F.3    Tanner, L.B.4    van Kuppeveld, F.J.5    Wenk, M.R.6    Greber, U.F.7
  • 65
    • 84875504620 scopus 로고    scopus 로고
    • An N-terminal amphipathic helix in dengue virus nonstructural protein 4A mediates oligomerization and is essential for replication
    • Stern O., Hung Y.F., Valdau O., Yaffe Y., Harris E., Hoffmann S., Willbold D., Sklan E.H. An N-terminal amphipathic helix in dengue virus nonstructural protein 4A mediates oligomerization and is essential for replication. J Virol 2013, 87:4080-4085.
    • (2013) J Virol , vol.87 , pp. 4080-4085
    • Stern, O.1    Hung, Y.F.2    Valdau, O.3    Yaffe, Y.4    Harris, E.5    Hoffmann, S.6    Willbold, D.7    Sklan, E.H.8
  • 66
    • 34247848008 scopus 로고    scopus 로고
    • The non-structural protein 4A of dengue virus is an integral membrane protein inducing membrane alterations in a 2K-regulated manner
    • Miller S., Kastner S., Krijnse-Locker J., Buhler S., Bartenschlager R. The non-structural protein 4A of dengue virus is an integral membrane protein inducing membrane alterations in a 2K-regulated manner. J Biol Chem 2007, 282:8873-8882.
    • (2007) J Biol Chem , vol.282 , pp. 8873-8882
    • Miller, S.1    Kastner, S.2    Krijnse-Locker, J.3    Buhler, S.4    Bartenschlager, R.5
  • 67
  • 68
    • 33646167045 scopus 로고    scopus 로고
    • Regulated cleavages at the West Nile virus NS4A-2K-NS4B junctions play a major role in rearranging cytoplasmic membranes and Golgi trafficking of the NS4A protein
    • Roosendaal J., Westaway E.G., Khromykh A., Mackenzie J.M. Regulated cleavages at the West Nile virus NS4A-2K-NS4B junctions play a major role in rearranging cytoplasmic membranes and Golgi trafficking of the NS4A protein. J Virol 2006, 80:4623-4632.
    • (2006) J Virol , vol.80 , pp. 4623-4632
    • Roosendaal, J.1    Westaway, E.G.2    Khromykh, A.3    Mackenzie, J.M.4
  • 69
    • 84905184081 scopus 로고    scopus 로고
    • Induction of endoplasmic reticulum-derived replication-competent membrane structures by West Nile virus non-structural protein 4B
    • Kaufusi P.H., Kelley J.F., Yanagihara R., Nerurkar V.R. Induction of endoplasmic reticulum-derived replication-competent membrane structures by West Nile virus non-structural protein 4B. PLoS One 2014, 9:e84040.
    • (2014) PLoS One , vol.9
    • Kaufusi, P.H.1    Kelley, J.F.2    Yanagihara, R.3    Nerurkar, V.R.4
  • 70
    • 0036776626 scopus 로고    scopus 로고
    • Flock house virus RNA polymerase is a transmembrane protein with amino-terminal sequences sufficient for mitochondrial localization and membrane insertion
    • Miller D.J., Ahlquist P. Flock house virus RNA polymerase is a transmembrane protein with amino-terminal sequences sufficient for mitochondrial localization and membrane insertion. J Virol 2002, 76:9856-9867.
    • (2002) J Virol , vol.76 , pp. 9856-9867
    • Miller, D.J.1    Ahlquist, P.2
  • 71
    • 0037301423 scopus 로고    scopus 로고
    • Properly folded nonstructural polyprotein directs the semliki forest virus replication complex to the endosomal compartment
    • Salonen A., Vasiljeva L., Merits A., Magden J., Jokitalo E., Kaariainen L. Properly folded nonstructural polyprotein directs the semliki forest virus replication complex to the endosomal compartment. J Virol 2003, 77:1691-1702.
    • (2003) J Virol , vol.77 , pp. 1691-1702
    • Salonen, A.1    Vasiljeva, L.2    Merits, A.3    Magden, J.4    Jokitalo, E.5    Kaariainen, L.6
  • 73
    • 84876437083 scopus 로고    scopus 로고
    • Host factors with regulatory roles in tombusvirus replication
    • Nagy P.D., Barajas D., Pogany J. Host factors with regulatory roles in tombusvirus replication. Curr Opin Virol 2012, 2:691-698.
    • (2012) Curr Opin Virol , vol.2 , pp. 691-698
    • Nagy, P.D.1    Barajas, D.2    Pogany, J.3
  • 74
    • 42449116994 scopus 로고    scopus 로고
    • Formation of the arterivirus replication/transcription complex: a key role for nonstructural protein 3 in the remodeling of intracellular membranes
    • Posthuma C.C., Pedersen K.W., Lu Z., Joosten R.G., Roos N., Zevenhoven-Dobbe J.C., Snijder E.J. Formation of the arterivirus replication/transcription complex: a key role for nonstructural protein 3 in the remodeling of intracellular membranes. J Virol 2008, 82:4480-4491.
    • (2008) J Virol , vol.82 , pp. 4480-4491
    • Posthuma, C.C.1    Pedersen, K.W.2    Lu, Z.3    Joosten, R.G.4    Roos, N.5    Zevenhoven-Dobbe, J.C.6    Snijder, E.J.7
  • 75
    • 0035008260 scopus 로고    scopus 로고
    • Non-structural proteins 2 and 3 interact to modify host cell membranes during the formation of the arterivirus replication complex
    • Snijder E.J., van Tol H., Roos N., Pedersen K.W. Non-structural proteins 2 and 3 interact to modify host cell membranes during the formation of the arterivirus replication complex. J Gen Virol 2001, 82:985-994.
    • (2001) J Gen Virol , vol.82 , pp. 985-994
    • Snijder, E.J.1    van Tol, H.2    Roos, N.3    Pedersen, K.W.4
  • 76
    • 84883321889 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome coronavirus nonstructural proteins 3, 4, and 6 induce double-membrane vesicles
    • Angelini M.M., Akhlaghpour M., Neuman B.W., Buchmeier M.J. Severe acute respiratory syndrome coronavirus nonstructural proteins 3, 4, and 6 induce double-membrane vesicles. MBio 2013, 4.
    • (2013) MBio , pp. 4
    • Angelini, M.M.1    Akhlaghpour, M.2    Neuman, B.W.3    Buchmeier, M.J.4
  • 77
    • 0036100578 scopus 로고    scopus 로고
    • Expression of hepatitis C virus proteins induces distinct membrane alterations including a candidate viral replication complex
    • Egger D., Wolk B., Gosert R., Bianchi L., Blum H.E., Moradpour D., Bienz K. Expression of hepatitis C virus proteins induces distinct membrane alterations including a candidate viral replication complex. J Virol 2002, 76:5974-5984.
    • (2002) J Virol , vol.76 , pp. 5974-5984
    • Egger, D.1    Wolk, B.2    Gosert, R.3    Bianchi, L.4    Blum, H.E.5    Moradpour, D.6    Bienz, K.7
  • 78
    • 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., Berger C., Kallis S., Kolovou A., Paul D., Lohmann V., Bartenschlager R. NS5A domain 1 and polyprotein cleavage kinetics are critical for induction of double-membrane vesicles associated with hepatitis C virus replication. MBio 2015, 6:e00759.
    • (2015) MBio , vol.6
    • Romero-Brey, I.1    Berger, C.2    Kallis, S.3    Kolovou, A.4    Paul, D.5    Lohmann, V.6    Bartenschlager, R.7
  • 79
    • 0028037893 scopus 로고
    • Membrane rearrangement and vesicle induction by recombinant poliovirus 2C and 2BC in human cells
    • Cho M.W., Teterina N., Egger D., Bienz K., Ehrenfeld E. Membrane rearrangement and vesicle induction by recombinant poliovirus 2C and 2BC in human cells. Virology 1994, 202:129-145.
    • (1994) Virology , vol.202 , pp. 129-145
    • Cho, M.W.1    Teterina, N.2    Egger, D.3    Bienz, K.4    Ehrenfeld, E.5
  • 80
    • 0033798416 scopus 로고    scopus 로고
    • Remodeling the endoplasmic reticulum by poliovirus infection and by individual viral proteins: an autophagy-like origin for virus-induced vesicles
    • Suhy D.A., Giddings T.H., Kirkegaard K. Remodeling the endoplasmic reticulum by poliovirus infection and by individual viral proteins: an autophagy-like origin for virus-induced vesicles. J Virol 2000, 74:8953-8965.
    • (2000) J Virol , vol.74 , pp. 8953-8965
    • Suhy, D.A.1    Giddings, T.H.2    Kirkegaard, K.3


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