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Volumn 69-70, Issue 1, 2014, Pages 45-52

Role of intracellular events in the pathogenesis of dengue; An overview

Author keywords

Autophagy; Dengue; Lipid droplets; Processing bodies; Stress granules

Indexed keywords

ADENOSINE TRIPHOSPHATE; FAT DROPLET; INITIATION FACTOR 2ALPHA; MESSENGER RNA;

EID: 84898893842     PISSN: 08824010     EISSN: 10961208     Source Type: Journal    
DOI: 10.1016/j.micpath.2014.03.004     Document Type: Review
Times cited : (27)

References (101)
  • 3
    • 48449100077 scopus 로고    scopus 로고
    • Vascular endothelium: the battlefield of dengue viruses
    • Basu A., Chaturvedi U.C. Vascular endothelium: the battlefield of dengue viruses. FEMS Immunol Med Microbiol 2008, 53:287-299.
    • (2008) FEMS Immunol Med Microbiol , vol.53 , pp. 287-299
    • Basu, A.1    Chaturvedi, U.C.2
  • 6
    • 0642287817 scopus 로고    scopus 로고
    • Neutralization and antibody-dependent enhancement of dengue viruses
    • Halstead S.B. Neutralization and antibody-dependent enhancement of dengue viruses. Adv Virus Res 2003, 60:421-467.
    • (2003) Adv Virus Res , vol.60 , pp. 421-467
    • Halstead, S.B.1
  • 7
    • 70350452043 scopus 로고    scopus 로고
    • Antibodies determine virulence in dengue
    • Halstead S.B. Antibodies determine virulence in dengue. Ann N Y Acad Sci 2009, 1171(Suppl. 1):E48-E56.
    • (2009) Ann N Y Acad Sci , vol.1171 , Issue.SUPPL. 1
    • Halstead, S.B.1
  • 10
    • 0028808189 scopus 로고
    • Dengue virus-induced human cytotoxic factor: production by peripheral blood leucocytes in vitro
    • Mukerjee R., Chaturvedi U.C., Dhawan R. Dengue virus-induced human cytotoxic factor: production by peripheral blood leucocytes in vitro. Clin Exp Immunol 1995, 101:261-267.
    • (1995) Clin Exp Immunol , vol.101 , pp. 261-267
    • Mukerjee, R.1    Chaturvedi, U.C.2    Dhawan, R.3
  • 11
    • 0001085886 scopus 로고    scopus 로고
    • Purification and pathogenicity of the cytotoxic factor from the cases of dengue haemorrhagic fever
    • Mukerjee R., Chaturvedi U.C., Vaughn D.W., Kalayanarooj S. Purification and pathogenicity of the cytotoxic factor from the cases of dengue haemorrhagic fever. Curr Sci 1997, 72:494-501.
    • (1997) Curr Sci , vol.72 , pp. 494-501
    • Mukerjee, R.1    Chaturvedi, U.C.2    Vaughn, D.W.3    Kalayanarooj, S.4
  • 13
    • 84871425559 scopus 로고    scopus 로고
    • Cytokine expression profile of dengue patients at different phases of illness
    • Rathakrishnan A., Wang S.M., Hu Y., Khan A.M., Ponnampalavanar S., Lum L.C., et al. Cytokine expression profile of dengue patients at different phases of illness. PLoS One 2012, 7(12):e52215. 10.1371/journal.pone.0052215.
    • (2012) PLoS One , vol.7 , Issue.12
    • Rathakrishnan, A.1    Wang, S.M.2    Hu, Y.3    Khan, A.M.4    Ponnampalavanar, S.5    Lum, L.C.6
  • 14
    • 33645472158 scopus 로고    scopus 로고
    • Dengue and dengue haemorrhagic fever: implications of host genetics
    • Chaturvedi U.C., Nagar R., Shrivastava S. Dengue and dengue haemorrhagic fever: implications of host genetics. FEMS Immunol Med Microbiol 2006, 47:155-166.
    • (2006) FEMS Immunol Med Microbiol , vol.47 , pp. 155-166
    • Chaturvedi, U.C.1    Nagar, R.2    Shrivastava, S.3
  • 15
    • 77952251551 scopus 로고    scopus 로고
    • Recent advances in understanding the intracellular responses to dengue virus infection
    • (Invited editorial)
    • Basu A., Chaturvedi U.C. Recent advances in understanding the intracellular responses to dengue virus infection. Future Virol 2010, 5:255-257. (Invited editorial).
    • (2010) Future Virol , vol.5 , pp. 255-257
    • Basu, A.1    Chaturvedi, U.C.2
  • 17
    • 47249142841 scopus 로고    scopus 로고
    • Molecular aspects of dengue virus replication
    • Bartenachlager R., Miller S. Molecular aspects of dengue virus replication. Future Microbiol 2008 Apr, 3:155-165.
    • (2008) Future Microbiol , vol.3 , pp. 155-165
    • Bartenachlager, R.1    Miller, S.2
  • 18
    • 11144348130 scopus 로고    scopus 로고
    • A structural perspective of the flavivirus life cycle
    • Mukhopadhyay S., Kuhn R.J., Rossmann M.G. A structural perspective of the flavivirus life cycle. Nat Rev Microbiol. 2005 Jan, 3(1):13-22.
    • (2005) Nat Rev Microbiol. , vol.3 , Issue.1 , pp. 13-22
    • Mukhopadhyay, S.1    Kuhn, R.J.2    Rossmann, M.G.3
  • 19
    • 0032863958 scopus 로고    scopus 로고
    • Markers for trans Golgi membranes and the intermediate compartment localize to induced membranes with distinct replication functions in flavivirus-infected cells
    • Mackenzie J.M., Jones M.K., Westaway E.G. Markers for trans Golgi membranes and the intermediate compartment localize to induced membranes with distinct replication functions in flavivirus-infected cells. J Virol 1999 Nov, 73(11):9555-9567.
    • (1999) J Virol , vol.73 , Issue.11 , pp. 9555-9567
    • Mackenzie, J.M.1    Jones, M.K.2    Westaway, E.G.3
  • 21
    • 1542283812 scopus 로고    scopus 로고
    • In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker
    • Mizushima N., Yamamoto A., Matsui M., Yoshimori T., Ohsumi Y. In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker. Mol Biol Cell 2004, 15:1101-1111.
    • (2004) Mol Biol Cell , vol.15 , pp. 1101-1111
    • Mizushima, N.1    Yamamoto, A.2    Matsui, M.3    Yoshimori, T.4    Ohsumi, Y.5
  • 22
    • 84856734124 scopus 로고    scopus 로고
    • Autophagy promotes T-cell survival through degradation of proteins of the cell death machinery
    • Kovacs J.R., Li C., Yang Q., Li G., Garcia I.G., Ju S., et al. Autophagy promotes T-cell survival through degradation of proteins of the cell death machinery. Cell Death Differ 2012, 19:144-152.
    • (2012) Cell Death Differ , vol.19 , pp. 144-152
    • Kovacs, J.R.1    Li, C.2    Yang, Q.3    Li, G.4    Garcia, I.G.5    Ju, S.6
  • 23
    • 80053303830 scopus 로고    scopus 로고
    • Autophagy and cytokines
    • Harris J. Autophagy and cytokines. Cytokine 2011, 56:140-144.
    • (2011) Cytokine , vol.56 , pp. 140-144
    • Harris, J.1
  • 24
    • 36249025723 scopus 로고    scopus 로고
    • Autophagy: process and function
    • Mizushima N. Autophagy: process and function. Genes Dev 2007, 21:2861-2873.
    • (2007) Genes Dev , vol.21 , pp. 2861-2873
    • Mizushima, N.1
  • 25
    • 84883717351 scopus 로고    scopus 로고
    • Autophagy and autoimmunity crosstalks
    • Bhattacharya A., Eissa N.T. Autophagy and autoimmunity crosstalks. Front Immunol 2013, 15(4):88. 10.3389/fimmu.2013.00088.
    • (2013) Front Immunol , vol.15 , Issue.4 , pp. 88
    • Bhattacharya, A.1    Eissa, N.T.2
  • 26
    • 84880152406 scopus 로고    scopus 로고
    • Divergent roles of autophagy in virus infection
    • Chiramel A.I., Brady N.R., Bartenschlager R. Divergent roles of autophagy in virus infection. Cells 2013, 2:83-104. 10.3390/cells2010083.
    • (2013) Cells , vol.2 , pp. 83-104
    • Chiramel, A.I.1    Brady, N.R.2    Bartenschlager, R.3
  • 28
    • 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 2011, 121:37-56.
    • (2011) J Clin Invest , vol.121 , pp. 37-56
    • Ke, P.Y.1    Chen, S.S.2
  • 31
    • 84859991798 scopus 로고    scopus 로고
    • Virus recognition by Toll-7 activates antiviral autophagy in Drosophila
    • Nakamoto M., Moy R.H., Xu J., Bambina S., Yasunaga A., Shelly S.S., et al. Virus recognition by Toll-7 activates antiviral autophagy in Drosophila. Immunity 2012, 36:658-667.
    • (2012) Immunity , vol.36 , pp. 658-667
    • Nakamoto, M.1    Moy, R.H.2    Xu, J.3    Bambina, S.4    Yasunaga, A.5    Shelly, S.S.6
  • 32
    • 78649338141 scopus 로고    scopus 로고
    • Autophagy and the integrated stress response
    • Kroemer G., Marino G., Levine B. Autophagy and the integrated stress response. Mol Cell 2010, 40:280-293.
    • (2010) Mol Cell , vol.40 , pp. 280-293
    • Kroemer, G.1    Marino, G.2    Levine, B.3
  • 33
    • 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 2011, 286:22147-22159.
    • (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
  • 34
    • 41449098293 scopus 로고    scopus 로고
    • Downregulation of autophagy by herpesvirus Bcl-2 homologs
    • Liang C.E.X., Jung J.U. Downregulation of autophagy by herpesvirus Bcl-2 homologs. Autophagy 2008, 4:268-272.
    • (2008) Autophagy , vol.4 , pp. 268-272
    • Liang, C.E.X.1    Jung, J.U.2
  • 35
    • 40449127353 scopus 로고    scopus 로고
    • Structural and biochemical bases for the inhibition of autophagy and apoptosis by viral BCL-2 of murine gamma-herpesvirus 68
    • Ku B., Woo J.S., Liang C., Lee K.H., Hong H.S., E X., et al. Structural and biochemical bases for the inhibition of autophagy and apoptosis by viral BCL-2 of murine gamma-herpesvirus 68. PLoS Pathog 2008, 4:e25.
    • (2008) PLoS Pathog , vol.4
    • Ku, B.1    Woo, J.S.2    Liang, C.3    Lee, K.H.4    Hong, H.S.5
  • 36
    • 33947715151 scopus 로고    scopus 로고
    • HSV-1 ICP34.5 confers neurovirulence by targeting the Beclin 1 autophagy protein
    • Orvedahl A., Alexander D., Talloczy Z., Sun Q., Wei Y., Zhang W., et al. HSV-1 ICP34.5 confers neurovirulence by targeting the Beclin 1 autophagy protein. Cell Host Microbe 2007, 1:23-35.
    • (2007) Cell Host Microbe , vol.1 , pp. 23-35
    • Orvedahl, A.1    Alexander, D.2    Talloczy, Z.3    Sun, Q.4    Wei, Y.5    Zhang, W.6
  • 37
    • 67649585835 scopus 로고    scopus 로고
    • Autophagy pathway intersects with HIV-1 biosynthesis and regulates viral yields in macrophages
    • Kyei G.B., Dinkins C., Davis A.S., Roberts E., Singh S.B., Dong C., et al. Autophagy pathway intersects with HIV-1 biosynthesis and regulates viral yields in macrophages. J Cell Biol 2009, 186:255-268.
    • (2009) J Cell Biol , vol.186 , pp. 255-268
    • Kyei, G.B.1    Dinkins, C.2    Davis, A.S.3    Roberts, E.4    Singh, S.B.5    Dong, C.6
  • 39
    • 78049513713 scopus 로고    scopus 로고
    • Coxsackievirus infection induces autophagy-like vesicles and megaphagosomes in pancreatic acinar cells in vivo
    • Kemball C.C., Alirezaei M., Flynn C.T., Wood M.R., Harkins S., Kiosses W.B., et al. Coxsackievirus infection induces autophagy-like vesicles and megaphagosomes in pancreatic acinar cells in vivo. J Virol 2010, I84:12110-12124.
    • (2010) J Virol , vol.I84 , pp. 12110-12124
    • Kemball, C.C.1    Alirezaei, M.2    Flynn, C.T.3    Wood, M.R.4    Harkins, S.5    Kiosses, W.B.6
  • 41
    • 82555187810 scopus 로고    scopus 로고
    • Image-based genome-wide siRNA screen identifies selective autophagy factors
    • Orvedahl A., Sumpter R., Xiao G., Ng A., Zou Z., Tang Y., et al. Image-based genome-wide siRNA screen identifies selective autophagy factors. Nature 2011, 480:113-117.
    • (2011) Nature , vol.480 , pp. 113-117
    • Orvedahl, A.1    Sumpter, R.2    Xiao, G.3    Ng, A.4    Zou, Z.5    Tang, Y.6
  • 42
    • 67349269904 scopus 로고    scopus 로고
    • Autophagy enhances the presentation of endogenous viral antigens on MHC class I molecules during HSV-1 infection
    • English L., Chemali M., Duron J., Rondeau C., Laplante A., Gingras D., et al. Autophagy enhances the presentation of endogenous viral antigens on MHC class I molecules during HSV-1 infection. Nat Immunol 2009, 10:480-487.
    • (2009) Nat Immunol , vol.10 , pp. 480-487
    • English, L.1    Chemali, M.2    Duron, J.3    Rondeau, C.4    Laplante, A.5    Gingras, D.6
  • 43
    • 12844275079 scopus 로고    scopus 로고
    • Endogenous MHC class II processing of a viral nuclear antigen after autophagy
    • Paludan C., Schmid D., Landthaler M., Vockerodt M., Kube D., Tuschl T., et al. Endogenous MHC class II processing of a viral nuclear antigen after autophagy. Science 2005, 307:593-596.
    • (2005) Science , vol.307 , pp. 593-596
    • Paludan, C.1    Schmid, D.2    Landthaler, M.3    Vockerodt, M.4    Kube, D.5    Tuschl, T.6
  • 44
    • 33846224369 scopus 로고    scopus 로고
    • Antigen-loading compartments for major histocompatibility complex class II molecules continuously receive input from autophagosomes
    • Schmid D., Pypaert M., Munz C. Antigen-loading compartments for major histocompatibility complex class II molecules continuously receive input from autophagosomes. Immunity 2007, 26:79-92.
    • (2007) Immunity , vol.26 , pp. 79-92
    • Schmid, D.1    Pypaert, M.2    Munz, C.3
  • 45
    • 0029794678 scopus 로고    scopus 로고
    • Cellular origin and ultrastructure of membranes induced during poliovirus infection
    • Schlegel A., Giddings T.H., Ladinsky M.S., Kirkegaard K. Cellular origin and ultrastructure of membranes induced during poliovirus infection. J Virol 1996, 70:6576-6588.
    • (1996) J Virol , vol.70 , pp. 6576-6588
    • Schlegel, A.1    Giddings, T.H.2    Ladinsky, M.S.3    Kirkegaard, K.4
  • 46
    • 84861556595 scopus 로고    scopus 로고
    • Replication of hepatitis C virus RNA on autophagosomal membranes
    • Sir D., Kuo C.F., Tian Y., Liu H.M., Huang E.J., Jung J.U., et al. Replication of hepatitis C virus RNA on autophagosomal membranes. J Biol Chem 2012, 287:18036-18043.
    • (2012) J Biol Chem , vol.287 , pp. 18036-18043
    • Sir, D.1    Kuo, C.F.2    Tian, Y.3    Liu, H.M.4    Huang, E.J.5    Jung, J.U.6
  • 47
    • 33744935521 scopus 로고    scopus 로고
    • Rotavirus NSP4 induces a novel vesicular compartment regulated by calcium and associated with viroplasms
    • Berkova Z., Crawford S.E., Trugnan G., Yoshimori T., Morris A.P., Estes M.K. Rotavirus NSP4 induces a novel vesicular compartment regulated by calcium and associated with viroplasms. J Virol 2006, 80:6061-6071.
    • (2006) J Virol , vol.80 , pp. 6061-6071
    • Berkova, Z.1    Crawford, S.E.2    Trugnan, G.3    Yoshimori, T.4    Morris, A.P.5    Estes, M.K.6
  • 48
    • 80052148073 scopus 로고    scopus 로고
    • Dengue virus and autophagy
    • Heaton N.S., Randall G. Dengue virus and autophagy. Viruses 2011, 3(8):1332-1341.
    • (2011) Viruses , vol.3 , Issue.8 , pp. 1332-1341
    • Heaton, N.S.1    Randall, G.2
  • 49
    • 80052045217 scopus 로고    scopus 로고
    • Subversion of cellular autophagy machinery by hepatitis B virus for viral envelopment
    • Li J., Liu Y., Wang Z., Liu K., Wang Y., Liu J., et al. Subversion of cellular autophagy machinery by hepatitis B virus for viral envelopment. J Virol 2011, 85:6319-6333.
    • (2011) J Virol , vol.85 , pp. 6319-6333
    • Li, J.1    Liu, Y.2    Wang, Z.3    Liu, K.4    Wang, Y.5    Liu, J.6
  • 54
    • 42649105438 scopus 로고    scopus 로고
    • Autophagic machinery activated by dengue virus enhances virus replication
    • Lee Y.R., Lei H.Y., Liu M.T., Wang J.R., Chen S.H., Jiang-Shieh Y.F., et al. Autophagic machinery activated by dengue virus enhances virus replication. Virology 2008, 374:240-248.
    • (2008) Virology , vol.374 , pp. 240-248
    • Lee, Y.R.1    Lei, H.Y.2    Liu, M.T.3    Wang, J.R.4    Chen, S.H.5    Jiang-Shieh, Y.F.6
  • 55
    • 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 2009, 90:448-456.
    • (2009) J Gen Virol , vol.90 , pp. 448-456
    • Panyasrivanit, M.1    Khakpoor, A.2    Wikan, N.3    Smith, D.R.4
  • 56
    • 67449086380 scopus 로고    scopus 로고
    • A role for autophagolysosomes in dengue virus 3 production in HepG2 cells
    • Khakpoor A., Panyasrivanit M., Wikan N., Smith D.R. A role for autophagolysosomes in dengue virus 3 production in HepG2 cells. J Gen Virol 2009, 90:1093-1103.
    • (2009) J Gen Virol , vol.90 , pp. 1093-1103
    • Khakpoor, A.1    Panyasrivanit, M.2    Wikan, N.3    Smith, D.R.4
  • 57
    • 64649097038 scopus 로고    scopus 로고
    • Composition and three-dimensional architecture of the dengue virus replication and assembly sites
    • Welsch S., Miller S., Romero-Brey I., Merz A., Bleck C.K., Walther P., et al. Composition and three-dimensional architecture of the dengue virus replication and assembly sites. Cell Host Microbe 2009, 5:365-375.
    • (2009) Cell Host Microbe , vol.5 , pp. 365-375
    • Welsch, S.1    Miller, S.2    Romero-Brey, I.3    Merz, A.4    Bleck, C.K.5    Walther, P.6
  • 58
    • 84873031729 scopus 로고    scopus 로고
    • Inhibition of cellular autophagy deranges dengue virion maturation
    • Mateo R., Nagamine C.M., Spagnolo J., Méndez E., Rahe M., Gale M., et al. Inhibition of cellular autophagy deranges dengue virion maturation. J Virol 2013, 87(3):1312-1321.
    • (2013) J Virol , vol.87 , Issue.3 , pp. 1312-1321
    • Mateo, R.1    Nagamine, C.M.2    Spagnolo, J.3    Méndez, E.4    Rahe, M.5    Gale, M.6
  • 59
    • 77957160633 scopus 로고    scopus 로고
    • Intrinsic antibody-dependent enhancement of microbial infection in macrophages: disease regulation by immune complexes
    • Halstead S.B., Mahalingam S., Marovich M.A., Ubol S., Mosser D.M. Intrinsic antibody-dependent enhancement of microbial infection in macrophages: disease regulation by immune complexes. Lancet Infect Dis 2010, 10(10):712-722.
    • (2010) Lancet Infect Dis , vol.10 , Issue.10 , pp. 712-722
    • Halstead, S.B.1    Mahalingam, S.2    Marovich, M.A.3    Ubol, S.4    Mosser, D.M.5
  • 61
    • 79955448291 scopus 로고    scopus 로고
    • The birth and life of lipid droplets: learning from the hepatitis C virus
    • Roingeard P., Depla M. The birth and life of lipid droplets: learning from the hepatitis C virus. Biol Cell 2011, 103:223-231.
    • (2011) Biol Cell , vol.103 , pp. 223-231
    • Roingeard, P.1    Depla, M.2
  • 62
    • 50249107793 scopus 로고    scopus 로고
    • Hepatitis C virus budding at lipid droplet-associated ER membrane visualized by 3D electron microscopy
    • Roingeard P., Hourioux C., Blanchard E., Prensier G. Hepatitis C virus budding at lipid droplet-associated ER membrane visualized by 3D electron microscopy. Histochem Cell Biol 2008, 130:561-566.
    • (2008) Histochem Cell Biol , vol.130 , pp. 561-566
    • Roingeard, P.1    Hourioux, C.2    Blanchard, E.3    Prensier, G.4
  • 63
    • 47649114826 scopus 로고    scopus 로고
    • Hepatitis C virus core protein induces lipid droplet redistribution in a microtubule- and dynein-dependent manner
    • Boulant S., Douglas M.W., Moody L., Budkowska A., Targett-Adams P., McLauchlan J. Hepatitis C virus core protein induces lipid droplet redistribution in a microtubule- and dynein-dependent manner. Traffic 2008, 9:1268-1282.
    • (2008) Traffic , vol.9 , pp. 1268-1282
    • Boulant, S.1    Douglas, M.W.2    Moody, L.3    Budkowska, A.4    Targett-Adams, P.5    McLauchlan, J.6
  • 64
    • 34548316984 scopus 로고    scopus 로고
    • The lipid droplet is an important organelle for hepatitis C virus production
    • Miyanari Y., Atsuzawa K., Usuda N., Watashi K., Hishiki T., Zayas R., et al. The lipid droplet is an important organelle for hepatitis C virus production. Nat Cell Biol 2007, 9:1089-1097.
    • (2007) Nat Cell Biol , vol.9 , pp. 1089-1097
    • Miyanari, Y.1    Atsuzawa, K.2    Usuda, N.3    Watashi, K.4    Hishiki, T.5    Zayas, R.6
  • 65
    • 79959370167 scopus 로고    scopus 로고
    • Is fat so bad? Modulation of endoplasmic reticulum stress by lipid droplet formation
    • Hapala I., Marza E., Ferreira T. Is fat so bad? Modulation of endoplasmic reticulum stress by lipid droplet formation. Biol Cell 2011, 103:271-285.
    • (2011) Biol Cell , vol.103 , pp. 271-285
    • Hapala, I.1    Marza, E.2    Ferreira, T.3
  • 67
    • 84872749486 scopus 로고    scopus 로고
    • Early dengue virus protein synthesis induces extensive rearrangement of the endoplasmic reticulum independent of the UPR and SREBP-2 pathway
    • Peña J., Harris E. Early dengue virus protein synthesis induces extensive rearrangement of the endoplasmic reticulum independent of the UPR and SREBP-2 pathway. PLoS One 2012, 6:e38202. 10.1371/journal.pone.0038202.
    • (2012) PLoS One , vol.6
    • Peña, J.1    Harris, E.2
  • 68
    • 84870995648 scopus 로고    scopus 로고
    • Regulation of lipid stores and metabolism by lipophagy
    • Liu K., Czaja M.J. Regulation of lipid stores and metabolism by lipophagy. Cell Death Differ 2013, 20:3-11.
    • (2013) Cell Death Differ , vol.20 , pp. 3-11
    • Liu, K.1    Czaja, M.J.2
  • 70
    • 77749292148 scopus 로고    scopus 로고
    • The early autophagic pathway is activated by hepatitis B virus and required for viral DNA replication
    • Sir D., Tian Y., Chen W.L., Ann D.K., Yen T.S., Ou J.H. The early autophagic pathway is activated by hepatitis B virus and required for viral DNA replication. Proc Natl Acad Sci U S A 2010, 107:4383-4388.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 4383-4388
    • Sir, D.1    Tian, Y.2    Chen, W.L.3    Ann, D.K.4    Yen, T.S.5    Ou, J.H.6
  • 71
    • 70350142577 scopus 로고    scopus 로고
    • Hepatitis C virus: viral proteins on the move
    • McLauchlan J. Hepatitis C virus: viral proteins on the move. Biochem Soc Trans 2009, 37:986-990.
    • (2009) Biochem Soc Trans , vol.37 , pp. 986-990
    • McLauchlan, J.1
  • 72
    • 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 2010, 8:422-432.
    • (2010) Cell Host Microbe , vol.8 , pp. 422-432
    • Heaton, N.S.1    Randall, G.2
  • 73
    • 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., et al. 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
  • 74
    • 84878237457 scopus 로고    scopus 로고
    • Virus-induced ER stress and the unfolded protein response
    • Zhang L., Wang A. Virus-induced ER stress and the unfolded protein response. Front Plant Sci 2012, 3:293. 10.3389/fpls.2012.00293.
    • (2012) Front Plant Sci , vol.3 , pp. 293
    • Zhang, L.1    Wang, A.2
  • 75
    • 59749086561 scopus 로고    scopus 로고
    • The unfolded protein response and autophagy: herpesviruses rule!
    • Lee D.Y., Lee J., Sugden B. The unfolded protein response and autophagy: herpesviruses rule!. J Virol 2009, 83(3):1168-1172.
    • (2009) J Virol , vol.83 , Issue.3 , pp. 1168-1172
    • Lee, D.Y.1    Lee, J.2    Sugden, B.3
  • 76
    • 43249109174 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress responses
    • Schroder M. Endoplasmic reticulum stress responses. Cell Mol Life Sci 2008, 65(6):862-894.
    • (2008) Cell Mol Life Sci , vol.65 , Issue.6 , pp. 862-894
    • Schroder, M.1
  • 77
    • 65249187333 scopus 로고    scopus 로고
    • Enhancing immunity through autophagy
    • Munz C. Enhancing immunity through autophagy. Annu Rev Immunol 2009, 27:423-449.
    • (2009) Annu Rev Immunol , vol.27 , pp. 423-449
    • Munz, C.1
  • 78
    • 35748966391 scopus 로고    scopus 로고
    • Dengue virus serotype infection specifies the activation of the unfolded protein response
    • Umareddy I., Pluquet O., Wang Q.Y., Vasudevan S.G., Chevet E., Gu F. Dengue virus serotype infection specifies the activation of the unfolded protein response. Virol J 2007, 4:91.
    • (2007) Virol J , vol.4 , pp. 91
    • Umareddy, I.1    Pluquet, O.2    Wang, Q.Y.3    Vasudevan, S.G.4    Chevet, E.5    Gu, F.6
  • 79
    • 79954601093 scopus 로고    scopus 로고
    • Dengue virus modulates the unfolded protein response in a time-dependent manner
    • Peña J., Harris E. Dengue virus modulates the unfolded protein response in a time-dependent manner. J Biol Chem 2011, 286(16):14226-14236.
    • (2011) J Biol Chem , vol.286 , Issue.16 , pp. 14226-14236
    • Peña, J.1    Harris, E.2
  • 80
    • 79955663893 scopus 로고    scopus 로고
    • Unfolded protein response (UPR) gene expression during antibody-dependent enhanced infection of cultured monocytes correlates with dengue disease severity
    • Paradkar P.N., Ooi E.E., Hanson B.J., Gubler D.J., Vasudevan S.G. Unfolded protein response (UPR) gene expression during antibody-dependent enhanced infection of cultured monocytes correlates with dengue disease severity. Biosci Rep 2011, 31(3):221-230.
    • (2011) Biosci Rep , vol.31 , Issue.3 , pp. 221-230
    • Paradkar, P.N.1    Ooi, E.E.2    Hanson, B.J.3    Gubler, D.J.4    Vasudevan, S.G.5
  • 81
    • 66249103703 scopus 로고    scopus 로고
    • RNA granules: post-transcriptional and epigenetic modulators of gene expression
    • Anderson P., Kedersha N. RNA granules: post-transcriptional and epigenetic modulators of gene expression. Nat Rev Mol Cell Biol 2009, 10:430-436.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 430-436
    • Anderson, P.1    Kedersha, N.2
  • 83
    • 56149086182 scopus 로고    scopus 로고
    • P bodies promote stress granule assembly in Saccharomyces cerevisiae
    • Buchan J.R., Muhlrad D., Parker R. P bodies promote stress granule assembly in Saccharomyces cerevisiae. J Cell Biol 2008, 183:441-455.
    • (2008) J Cell Biol , vol.183 , pp. 441-455
    • Buchan, J.R.1    Muhlrad, D.2    Parker, R.3
  • 84
    • 84864032746 scopus 로고    scopus 로고
    • How do viruses interact with stress-associated RNA granules?
    • Lloyd R.E. How do viruses interact with stress-associated RNA granules?. PLoS Pathog 2012, 8(6):e1002741. 10.1371/journal.ppat.1002741.
    • (2012) PLoS Pathog , vol.8 , Issue.6
    • Lloyd, R.E.1
  • 85
    • 84863407268 scopus 로고    scopus 로고
    • Regulation of stress granules in virus systems
    • White J.P., Lloyd R.E. Regulation of stress granules in virus systems. Trends Microbiol 2012, 20:175-183.
    • (2012) Trends Microbiol , vol.20 , pp. 175-183
    • White, J.P.1    Lloyd, R.E.2
  • 86
    • 77949389673 scopus 로고    scopus 로고
    • Stable formation of compositionally unique stress granules in virus-infected cells
    • Piotrowska J., Hansen S.J., Park N., Jamka K., Sarnow P., Gustin K.E. Stable formation of compositionally unique stress granules in virus-infected cells. J Virol 2010, 84:3654-3665.
    • (2010) J Virol , vol.84 , pp. 3654-3665
    • Piotrowska, J.1    Hansen, S.J.2    Park, N.3    Jamka, K.4    Sarnow, P.5    Gustin, K.E.6
  • 87
    • 18844419215 scopus 로고    scopus 로고
    • Human cytomegalovirus infection activates and regulates the unfolded protein response
    • Isler J.A., Skalet A.H., Alwine J.C. Human cytomegalovirus infection activates and regulates the unfolded protein response. J Virol 2005, 79:6890-6899.
    • (2005) J Virol , vol.79 , pp. 6890-6899
    • Isler, J.A.1    Skalet, A.H.2    Alwine, J.C.3
  • 88
    • 38349138566 scopus 로고    scopus 로고
    • Rotavirus infection induces the phosphorylation of eIF2alpha but prevents the formation of stress granules
    • Montero H., Rojas M., Arias C.F., Lopez S. Rotavirus infection induces the phosphorylation of eIF2alpha but prevents the formation of stress granules. J Virol 2008, 82:1496-1504.
    • (2008) J Virol , vol.82 , pp. 1496-1504
    • Montero, H.1    Rojas, M.2    Arias, C.F.3    Lopez, S.4
  • 89
    • 84860900591 scopus 로고    scopus 로고
    • Influenza A virus inhibits cytoplasmic stress granule formation
    • Khaperskyy D.A., Hatchette T.F., McCormick C. Influenza A virus inhibits cytoplasmic stress granule formation. Faseb J 2011, 10.1096/fj.11-196915.
    • (2011) Faseb J
    • Khaperskyy, D.A.1    Hatchette, T.F.2    McCormick, C.3
  • 90
    • 32444441933 scopus 로고    scopus 로고
    • Reovirus induces and benefits from an integrated cellular stress response
    • Smith J.A., Schmechel S.C., Raghavan A., Abelson M., Reilly C., Katze M.G., et al. Reovirus induces and benefits from an integrated cellular stress response. J Virol 2006, 80:2019-2033.
    • (2006) J Virol , vol.80 , pp. 2019-2033
    • Smith, J.A.1    Schmechel, S.C.2    Raghavan, A.3    Abelson, M.4    Reilly, C.5    Katze, M.G.6
  • 91
    • 70350678748 scopus 로고    scopus 로고
    • Mammalian orthoreovirus particles induce and are recruited into stress granules at early times postinfection
    • Qin Q., Hastings C., Miller C.L. Mammalian orthoreovirus particles induce and are recruited into stress granules at early times postinfection. J Virol 2009, 83:11090-11101.
    • (2009) J Virol , vol.83 , pp. 11090-11101
    • Qin, Q.1    Hastings, C.2    Miller, C.L.3
  • 92
    • 84872791019 scopus 로고    scopus 로고
    • Differential unfolded protein response during Chikungunya and Sindbis virus infection: CHIKV nsP4 suppresses eIF2α phosphorylation
    • Rathore A.P., Ng M.L., Vasudevan S.G. Differential unfolded protein response during Chikungunya and Sindbis virus infection: CHIKV nsP4 suppresses eIF2α phosphorylation. Virol J 2013, 10:36.
    • (2013) Virol J , vol.10 , pp. 36
    • Rathore, A.P.1    Ng, M.L.2    Vasudevan, S.G.3
  • 93
    • 35848929915 scopus 로고    scopus 로고
    • Inhibition of cytoplasmic mRNA stress granule formation by a viral proteinase
    • White J.P., Cardenas A.M., Marissen W.E., Lloyd R.E. Inhibition of cytoplasmic mRNA stress granule formation by a viral proteinase. Cell Host Microbe 2007, 2:295-305.
    • (2007) Cell Host Microbe , vol.2 , pp. 295-305
    • White, J.P.1    Cardenas, A.M.2    Marissen, W.E.3    Lloyd, R.E.4
  • 94
    • 34547456097 scopus 로고    scopus 로고
    • Interaction of TIA-1/TIAR with West Nile and dengue virus products in infected cells interferes with stress granule formation and processing body assembly
    • Emara M.M., Brinton M.A. Interaction of TIA-1/TIAR with West Nile and dengue virus products in infected cells interferes with stress granule formation and processing body assembly. Proc Natl Acad Sci U S A 2007, 104(21):9041-9046.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , Issue.21 , pp. 9041-9046
    • Emara, M.M.1    Brinton, M.A.2
  • 95
    • 81255210913 scopus 로고    scopus 로고
    • Quantitative mass spectrometry of DENV-2 RNA-interacting proteins reveals that the DEAD-box RNA helicase DDX6 binds the DB1 and DB2 3' UTR structures
    • Ward A.M., Bidet K., Yinglin A., Ler S.G., Hogue K., Blackstock W., et al. Quantitative mass spectrometry of DENV-2 RNA-interacting proteins reveals that the DEAD-box RNA helicase DDX6 binds the DB1 and DB2 3' UTR structures. RNA Biol 2011, 8:1173-1186.
    • (2011) RNA Biol , vol.8 , pp. 1173-1186
    • Ward, A.M.1    Bidet, K.2    Yinglin, A.3    Ler, S.G.4    Hogue, K.5    Blackstock, W.6
  • 96
    • 11144223347 scopus 로고    scopus 로고
    • The UL41 protein of herpes simplex virus mediates selective stabilization or degradation of cellular mRNAs
    • Esclatine A., Taddeo B., Roizman B. The UL41 protein of herpes simplex virus mediates selective stabilization or degradation of cellular mRNAs. Proc Natl Acad Sci U S A 2004, 101:18165-18170.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 18165-18170
    • Esclatine, A.1    Taddeo, B.2    Roizman, B.3
  • 97
    • 80052963807 scopus 로고    scopus 로고
    • The HTLV-1 Tax protein inhibits formation of stress granules by interacting with histone deacetylase 6
    • Legros S., Boxus M., Gatot J.S., Van Lint C., Kruys V., Kettmann R., et al. The HTLV-1 Tax protein inhibits formation of stress granules by interacting with histone deacetylase 6. Oncogene 2011, 30:4050-4062.
    • (2011) Oncogene , vol.30 , pp. 4050-4062
    • Legros, S.1    Boxus, M.2    Gatot, J.S.3    Van Lint, C.4    Kruys, V.5    Kettmann, R.6
  • 98
    • 76649143385 scopus 로고    scopus 로고
    • Novel Staufen1 ribonucleoproteins prevent formation of stress granules but favour encapsidation of HIV-1 genomic RNA
    • Abrahamyan L.G., Chatel-Chaix L., Ajamian L., Milev M.P., Monette A., Clement J.F., et al. Novel Staufen1 ribonucleoproteins prevent formation of stress granules but favour encapsidation of HIV-1 genomic RNA. J Cell Sci 2010, 123:369-383.
    • (2010) J Cell Sci , vol.123 , pp. 369-383
    • Abrahamyan, L.G.1    Chatel-Chaix, L.2    Ajamian, L.3    Milev, M.P.4    Monette, A.5    Clement, J.F.6
  • 99
    • 79960389571 scopus 로고    scopus 로고
    • Hepatitis C virus hijacks P-body and stress granule components around lipid droplets
    • Ariumi Y., Kuroki M., Kushima Y., Osugi K., Hijikata M., Maki M., et al. Hepatitis C virus hijacks P-body and stress granule components around lipid droplets. J Virol 2011, 85:6882-6892.
    • (2011) J Virol , vol.85 , pp. 6882-6892
    • Ariumi, Y.1    Kuroki, M.2    Kushima, Y.3    Osugi, K.4    Hijikata, M.5    Maki, M.6
  • 100
    • 79953107370 scopus 로고    scopus 로고
    • Activation of protein kinase R is required for induction of stress granules by respiratory syncytial virus but dispensable for viral replication
    • Lindquist M.E., Mainou B.A., Dermody T.S., Crowe J.E. Activation of protein kinase R is required for induction of stress granules by respiratory syncytial virus but dispensable for viral replication. Virology 2011, 413:103-110.
    • (2011) Virology , vol.413 , pp. 103-110
    • Lindquist, M.E.1    Mainou, B.A.2    Dermody, T.S.3    Crowe, J.E.4


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