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Volumn 44, Issue 5, 2012, Pages 375-384

Interplay between the cellular autophagy machinery and positive-stranded RNA viruses

Author keywords

Autophagosome; Autophagy; Double membrane vesicle; P62 SQSTM1; Positive stranded RNA viruses; Xenophagy

Indexed keywords

ATG12 PROTEIN, HUMAN; ATG5 PROTEIN, HUMAN; MICROTUBULE ASSOCIATED PROTEIN; SUMO PROTEIN; TARGET OF RAPAMYCIN KINASE; VIRUS PROTEIN;

EID: 84860473144     PISSN: 16729145     EISSN: 17457270     Source Type: Journal    
DOI: 10.1093/abbs/gms010     Document Type: Review
Times cited : (49)

References (101)
  • 1
    • 77957957039 scopus 로고    scopus 로고
    • Organelle-like membrane compartmentalization of positive-strand RNA virus replication factories
    • den Boon JA and 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
  • 2
    • 42349086670 scopus 로고    scopus 로고
    • Modification of intracellular membrane structures for virus replication
    • DOI 10.1038/nrmicro1890, PII NRMICRO1890
    • Miller S and Krijnse-Locker J. Modification of intracellular membrane structures for virus replication. Nat Rev Microbiol 2008, 6: 363-374. (Pubitemid 351552657)
    • (2008) Nature Reviews Microbiology , vol.6 , Issue.5 , pp. 363-374
    • Miller, S.1    Krijnse-Locker, J.2
  • 4
    • 33646555141 scopus 로고    scopus 로고
    • Aggresomes and autophagy generate sites for virus replication
    • DOI 10.1126/science.1126766
    • Wileman T. Aggresomes and autophagy generate sites for virus replication. Science 2006, 312: 875-878. (Pubitemid 43727312)
    • (2006) Science , vol.312 , Issue.5775 , pp. 875-878
    • Wileman, T.1
  • 5
    • 35448981935 scopus 로고    scopus 로고
    • Autophagy: From phenomenology to molecular understanding in less than a decade
    • DOI 10.1038/nrm2245, PII NRM2245
    • Klionsky DJ. Autophagy: from phenomenology to molecular understanding in less than a decade. Nat Rev Mol Cell Biol 2007, 8: 931-937. (Pubitemid 47622558)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.11 , pp. 931-937
    • Klionsky, D.J.1
  • 6
    • 79960735619 scopus 로고    scopus 로고
    • Ubiquitination-mediated autophagy against invading bacteria
    • Fujita N and Yoshimori T. Ubiquitination-mediated autophagy against invading bacteria. Curr Opin Cell Biol 2011, 23: 492-497.
    • (2011) Curr Opin Cell Biol , vol.23 , pp. 492-497
    • Fujita, N.1    Yoshimori, T.2
  • 7
    • 79952355107 scopus 로고    scopus 로고
    • Selective autophagy mediated by autophagic adapter proteins
    • Johansen T and Lamark T. Selective autophagy mediated by autophagic adapter proteins. Autophagy 2011, 7: 279-296.
    • (2011) Autophagy , vol.7 , pp. 279-296
    • Johansen, T.1    Lamark, T.2
  • 8
    • 77955964664 scopus 로고    scopus 로고
    • Selective autophagy regulates various cellular functions
    • Komatsu M and Ichimura Y. Selective autophagy regulates various cellular functions. Genes Cells 2010, 15: 923-933.
    • (2010) Genes Cells , vol.15 , pp. 923-933
    • Komatsu, M.1    Ichimura, Y.2
  • 9
    • 75649122282 scopus 로고    scopus 로고
    • Subversion of the cellular autophagy pathway by viruses
    • Kirkegaard K. Subversion of the cellular autophagy pathway by viruses. Curr Top Microbiol Immunol 2009, 335: 323-333.
    • (2009) Curr Top Microbiol Immunol , vol.335 , pp. 323-333
    • Kirkegaard, K.1
  • 11
    • 39149117352 scopus 로고    scopus 로고
    • Autophagy and antiviral immunity
    • Lee HK and Iwasaki A. Autophagy and antiviral immunity. Curr Opin Immunol 2008, 20: 23-29.
    • (2008) Curr Opin Immunol , vol.20 , pp. 23-29
    • Lee, H.K.1    Iwasaki, A.2
  • 12
    • 74449088520 scopus 로고    scopus 로고
    • Autophagy in Mammalian antiviral immunity
    • Orvedahl A and Levine B. Autophagy in Mammalian antiviral immunity. Curr Top Microbiol Immunol 2009, 335: 267-285.
    • (2009) Curr Top Microbiol Immunol , vol.335 , pp. 267-285
    • Orvedahl, A.1    Levine, B.2
  • 13
    • 69449103157 scopus 로고    scopus 로고
    • Viruses and arrested autophagosome development
    • Taylor MP and Jackson WT. Viruses and arrested autophagosome development. Autophagy 2009, 5: 870-871.
    • (2009) Autophagy , vol.5 , pp. 870-871
    • Taylor, M.P.1    Jackson, W.T.2
  • 17
    • 0031883733 scopus 로고    scopus 로고
    • Lysosomes, a meeting point of proteins, chaperones, and proteases
    • Cuervo AM and Dice JF. Lysosomes, a meeting point of proteins, chaperones, and proteases. J Mol Med (Berl) 1998, 76: 6-12. (Pubitemid 28085056)
    • (1998) Journal of Molecular Medicine , vol.76 , Issue.1 , pp. 6-12
    • Cuervo, A.M.1    Dice, J.F.2
  • 18
    • 0028222874 scopus 로고
    • Autophagy and related mechanisms of lysosome-mediated protein degradation
    • DOI 10.1016/0962-8924(94)90069-8
    • Dunn WA, Jr. Autophagy and related mechanisms of lysosome-mediated protein degradation. Trends Cell Biol 1994, 4: 139-143. (Pubitemid 24107709)
    • (1994) Trends in Cell Biology , vol.4 , Issue.4 , pp. 139-143
    • Dunn Jr., W.A.1
  • 19
    • 57649195400 scopus 로고    scopus 로고
    • Autophagy and multivesicular bodies: Two closely related partners
    • Fader CM and Colombo MI. Autophagy and multivesicular bodies: two closely related partners. Cell Death Differ 2009, 16: 70-78.
    • (2009) Cell Death Differ , vol.16 , pp. 70-78
    • Fader, C.M.1    Colombo, M.I.2
  • 20
    • 72549095406 scopus 로고    scopus 로고
    • Regulation mechanisms and signaling pathways of autophagy
    • He C and Klionsky DJ. Regulation mechanisms and signaling pathways of autophagy. Annu Rev Genet 2009, 43: 67-93.
    • (2009) Annu Rev Genet , vol.43 , pp. 67-93
    • He, C.1    Klionsky, D.J.2
  • 21
    • 77956416339 scopus 로고    scopus 로고
    • Autophagy in mammalian development and differentiation
    • Mizushima N and Levine B. Autophagy in mammalian development and differentiation. Nat Cell Biol 2010, 12: 823-830.
    • (2010) Nat Cell Biol , vol.12 , pp. 823-830
    • Mizushima, N.1    Levine, B.2
  • 22
    • 0035286734 scopus 로고    scopus 로고
    • Molecular dissection of autophagy: Two ubiquitin-like systems
    • DOI 10.1038/35056522
    • Ohsumi Y. Molecular dissection of autophagy: two ubiquitin-like systems. Nat Rev Mol Cell Biol 2001, 2: 211-216. (Pubitemid 33675746)
    • (2001) Nature Reviews Molecular Cell Biology , vol.2 , Issue.3 , pp. 211-216
    • Ohsumi, Y.1
  • 23
    • 0034329418 scopus 로고    scopus 로고
    • LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing
    • Kabeya Y, Mizushima N, Ueno T, Yamamoto A, Kirisako T, Noda T and Kominami E, et al. LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing. EMBO J 2000, 19: 5720-5728.
    • (2000) EMBO J , vol.19 , pp. 5720-5728
    • Kabeya, Y.1    Mizushima, N.2    Ueno, T.3    Yamamoto, A.4    Kirisako, T.5    Noda, T.6    Kominami, E.7
  • 24
    • 0035032723 scopus 로고    scopus 로고
    • Beclin-phosphatidylinositol 3-kinase complex functions at the trans-Golgi network
    • DOI 10.1093/embo-reports/kve061
    • Kihara A, Kabeya Y, Ohsumi Y and Yoshimori T. Beclin-phosphatidylinositol 3-kinase complex functions at the trans-Golgi network. EMBO Rep 2001, 2: 330-335. (Pubitemid 32401529)
    • (2001) EMBO Reports , vol.2 , Issue.4 , pp. 330-335
    • Kihara, A.1    Kabeya, Y.2    Ohsumi, Y.3    Yoshimori, T.4
  • 25
    • 32244442749 scopus 로고    scopus 로고
    • Functional specificity of the mammalian Beclin-Vps34 PI 3-kinase complex in macroautophagy versus endocytosis and lysosomal enzyme trafficking
    • DOI 10.1242/jcs.02735
    • Zeng X, Overmeyer JH and Maltese WA. Functional specificity of the mammalian Beclin-Vps34 PI 3-kinase complex in macroautophagy versus endocytosis and lysosomal enzyme trafficking. J Cell Sci 2006, 119: 259-270. (Pubitemid 43210695)
    • (2006) Journal of Cell Science , vol.119 , Issue.2 , pp. 259-270
    • Zeng, X.1    Overmeyer, J.H.2    Maltese, W.A.3
  • 26
    • 27644466759 scopus 로고    scopus 로고
    • Autophagy and signaling: Their role in cell survival and cell death
    • DOI 10.1038/sj.cdd.4401751, PII 4401751
    • Codogno P and Meijer AJ. Autophagy and signaling: their role in cell survival and cell death. Cell Death Differ 2005, 12(Suppl. 2): 1509-1518. (Pubitemid 41553987)
    • (2005) Cell Death and Differentiation , vol.12 , Issue.SUPPL. 2 , pp. 1509-1518
    • Codogno, P.1    Meijer, A.J.2
  • 28
    • 77950495123 scopus 로고    scopus 로고
    • Physiological significance of selective degradation of p62 by autophagy
    • Komatsu M and Ichimura Y. Physiological significance of selective degradation of p62 by autophagy. FEBS Lett 2010, 584: 1374-1378.
    • (2010) FEBS Lett , vol.584 , pp. 1374-1378
    • Komatsu, M.1    Ichimura, Y.2
  • 29
    • 37649005234 scopus 로고    scopus 로고
    • Autophagy in the pathogenesis of disease
    • Levine B and Kroemer G. Autophagy in the pathogenesis of disease. Cell 2008, 132: 27-42.
    • (2008) Cell , vol.132 , pp. 27-42
    • Levine, B.1    Kroemer, G.2
  • 30
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • DOI 10.1038/nature06639, PII NATURE06639
    • Mizushima N, Levine B, Cuervo AM and Klionsky DJ. Autophagy fights disease through cellular self-digestion. Nature 2008, 451: 1069-1075. (Pubitemid 351317450)
    • (2008) Nature , vol.451 , Issue.7182 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 31
    • 8344242220 scopus 로고    scopus 로고
    • Autophagy in health and disease: A double-edged sword
    • DOI 10.1126/science.1099993
    • Shintani T and Klionsky DJ. Autophagy in health and disease: a doubleedged sword. Science 2004, 306: 990-995. (Pubitemid 39482894)
    • (2004) Science , vol.306 , Issue.5698 , pp. 990-995
    • Shintani, T.1    Klionsky, D.J.2
  • 32
    • 38049074222 scopus 로고    scopus 로고
    • Xenophagy in herpes simplex virus replication and pathogenesis
    • Alexander DE and Leib DA. Xenophagy in herpes simplex virus replication and pathogenesis. Autophagy 2008, 4: 101-103.
    • (2008) Autophagy , vol.4 , pp. 101-103
    • Alexander, D.E.1    Leib, D.A.2
  • 33
    • 12944308330 scopus 로고    scopus 로고
    • Eating oneself and uninvited guests: Autophagy-related pathways in cellular defense
    • DOI 10.1016/j.cell.2005.01.005, PII S0092867405000437
    • Levine B. Eating oneself and uninvited guests: autophagy-related pathways in cellular defense. Cell 2005, 120: 159-162. (Pubitemid 40174758)
    • (2005) Cell , vol.120 , Issue.2 , pp. 159-162
    • Levine, B.1
  • 34
    • 65249108735 scopus 로고    scopus 로고
    • Autophagy genes in immunity
    • Virgin HW and Levine B. Autophagy genes in immunity. Nat Immunol 2009, 10: 461-470.
    • (2009) Nat Immunol , vol.10 , pp. 461-470
    • Virgin, H.W.1    Levine, B.2
  • 35
    • 1642280930 scopus 로고    scopus 로고
    • Coronavirus Replication Complex Formation Utilizes Components of Cellular Autophagy
    • DOI 10.1074/jbc.M306124200
    • Prentice E, Jerome WG, Yoshimori T, Mizushima N and Denison MR. Coronavirus replication complex formation utilizes components of cellular autophagy. J Biol Chem 2004, 279: 10136-10141. (Pubitemid 38372618)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.11 , pp. 10136-10141
    • Prentice, E.1    Jerome, W.G.2    Yoshimori, T.3    Mizushima, N.4    Denison, M.R.5
  • 36
    • 78049513713 scopus 로고    scopus 로고
    • Coxsackievirus infection induces autophagy-like vesicles and megaphagosomes in pancreatic acinar cells in vivo
    • Kemball CC, Alirezaei M, Flynn CT, Wood MR, Harkins S, Kiosses WB and Whitton JL. Coxsackievirus infection induces autophagy-like vesicles and megaphagosomes in pancreatic acinar cells in vivo. J Virol 2010, 84: 12110-12124.
    • (2010) J Virol , vol.84 , 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    Whitton, J.L.7
  • 37
    • 50949133741 scopus 로고    scopus 로고
    • Autophagosome supports coxsackievirus B3 replication in host cells
    • Wong J, Zhang J, Si X, Gao G, Mao I, McManus BM and Luo H. Autophagosome supports coxsackievirus B3 replication in host cells. J Virol 2008, 82: 9143-9153.
    • (2008) J Virol , vol.82 , pp. 9143-9153
    • Wong, J.1    Zhang, J.2    Si, X.3    Gao, G.4    Mao, I.5    McManus, B.M.6    Luo, H.7
  • 39
    • 56449116096 scopus 로고    scopus 로고
    • Coxsackievirus B4 uses autophagy for replication after calpain activation in rat primary neurons
    • Yoon SY, Ha YE, Choi JE, Ahn J, Lee H, Kweon HS and Lee JY, et al. Coxsackievirus B4 uses autophagy for replication after calpain activation in rat primary neurons. J Virol 2008, 82: 11976-11978.
    • (2008) J Virol , vol.82 , pp. 11976-11978
    • Yoon, S.Y.1    Ha, Y.E.2    Choi, J.E.3    Ahn, J.4    Lee, H.5    Kweon, H.S.6    Lee, J.Y.7
  • 40
    • 67649989068 scopus 로고    scopus 로고
    • Enterovirus 71-induced autophagy detected in vitro and in vivo promotes viral replication
    • Huang SC, Chang CL, Wang PS, Tsai Y and Liu HS. Enterovirus 71-induced autophagy detected in vitro and in vivo promotes viral replication. J Med Virol 2009, 81: 1241-1252.
    • (2009) J Med Virol , vol.81 , pp. 1241-1252
    • Huang, S.C.1    Chang, C.L.2    Wang, P.S.3    Tsai, Y.4    Liu, H.S.5
  • 41
    • 80055099522 scopus 로고    scopus 로고
    • Autophagy inhibitor 3-MA decreases the production and release of infectious enterovirus 71 particles
    • Zhang XY, Xi XY and Zhao ZD. Autophagy inhibitor 3-MA decreases the production and release of infectious enterovirus 71 particles. Zhonghua Shi Yan He Lin Chuang Bing Du Xue Za Zhi 2011, 25: 176-178.
    • (2011) Zhonghua Shi Yan He Lin Chuang Bing du Xue Za Zhi , vol.25 , pp. 176-178
    • Zhang, X.Y.1    Xi, X.Y.2    Zhao, Z.D.3
  • 43
    • 79957926128 scopus 로고    scopus 로고
    • Autophagy promotes the replication of encephalomyocarditis virus in host cells
    • Zhang Y, Li Z, Xinna G, Xin G and Yang H. Autophagy promotes the replication of encephalomyocarditis virus in host cells. Autophagy 2011, 7: 613-628.
    • (2011) Autophagy , vol.7 , pp. 613-628
    • Zhang, Y.1    Li, Z.2    Xinna, G.3    Xin, G.4    Yang, H.5
  • 44
    • 80052428163 scopus 로고    scopus 로고
    • Human rhinovirus 2 induces the autophagic pathway and replicates more efficiently in autophagic cells
    • Klein KA and Jackson WT. Human rhinovirus 2 induces the autophagic pathway and replicates more efficiently in autophagic cells. J Virol 2011, 85: 9651-9654.
    • (2011) J Virol , vol.85 , pp. 9651-9654
    • Klein, K.A.1    Jackson, W.T.2
  • 45
    • 48749126160 scopus 로고    scopus 로고
    • Autophagy and viral neurovirulence
    • Orvedahl A and Levine B. Autophagy and viral neurovirulence. Cell Microbiol 2008, 10: 1747-1756.
    • (2008) Cell Microbiol , vol.10 , pp. 1747-1756
    • Orvedahl, A.1    Levine, B.2
  • 47
    • 80655124392 scopus 로고    scopus 로고
    • Coronavirus nsp6 proteins generate autophagosomes from the endoplasmic reticulum via an omegasome intermediate
    • Cottam EM, Maier HJ, Manifava M, Vaux LC, Chandra-Schoenfelder P, Gerner W and Britton P, et al. Coronavirus nsp6 proteins generate autophagosomes from the endoplasmic reticulum via an omegasome intermediate. Autophagy 2011, 7: 1335-1347.
    • (2011) Autophagy , vol.7 , pp. 1335-1347
    • Cottam, E.M.1    Maier, H.J.2    Manifava, M.3    Vaux, L.C.4    Chandra-Schoenfelder, P.5    Gerner, W.6    Britton, P.7
  • 48
    • 41449099088 scopus 로고    scopus 로고
    • Are nidoviruses hijacking the autophagy machinery?
    • de Haan CA and Reggiori F. Are nidoviruses hijacking the autophagy machinery? Autophagy 2008, 4: 276-279. (Pubitemid 351458086)
    • (2008) Autophagy , vol.4 , Issue.3 , pp. 276-279
    • De Haan, C.A.M.1    Reggiori, F.2
  • 49
    • 0036196634 scopus 로고    scopus 로고
    • RNA replication of mouse hepatitis virus takes place at double-membrane vesicles
    • DOI 10.1128/JVI.76.8.3697-3708.2002
    • Gosert R, Kanjanahaluethai A, Egger D, Bienz K and Baker SC. RNA replication of mouse hepatitis virus takes place at double-membrane vesicles. J Virol 2002, 76: 3697-3708. (Pubitemid 34250534)
    • (2002) Journal of Virology , vol.76 , Issue.8 , pp. 3697-3708
    • Gosert, R.1    Kanjanahaluethai, A.2    Egger, D.3    Bienz, K.4    Baker, S.C.5
  • 50
    • 77956525570 scopus 로고    scopus 로고
    • Coronaviruses Hijack the LC3-I-positive EDEMosomes, ER-derived vesicles exporting short-lived ERAD regulators, for replication
    • Reggiori F, Monastyrska I, Verheije MH, Cali T, Ulasli M, Bianchi S and Bernasconi R, et al. Coronaviruses Hijack the LC3-I-positive EDEMosomes, ER-derived vesicles exporting short-lived ERAD regulators, for replication. Cell Host Microbe 2010, 7: 500-508.
    • (2010) Cell Host Microbe , vol.7 , pp. 500-508
    • Reggiori, F.1    Monastyrska, I.2    Verheije, M.H.3    Cali, T.4    Ulasli, M.5    Bianchi, S.6    Bernasconi, R.7
  • 51
    • 0033017866 scopus 로고    scopus 로고
    • Open reading frame 1a-encoded subunits of the arterivirus replicase induce endoplasmic reticulum-derived double-membrane vesicles which carry the viral replication complex
    • Pedersen KW, van der Meer Y, Roos N and Snijder EJ. Open reading frame 1a-encoded subunits of the arterivirus replicase induce endoplasmic reticulum-derived double-membrane vesicles which carry the viral replication complex. J Virol 1999, 73: 2016-2026. (Pubitemid 29098104)
    • (1999) Journal of Virology , vol.73 , Issue.3 , pp. 2016-2026
    • Pedersen, K.W.1    Van Der Meer, Y.2    Roos, N.3    Snijder, E.J.4
  • 52
    • 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 EJ, van Tol H, Roos N and Pedersen KW. 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. (Pubitemid 32454599)
    • (2001) Journal of General Virology , vol.82 , Issue.5 , pp. 985-994
    • Snijder, E.J.1    Van Tol, H.2    Roos, N.3    Pedersen, K.W.4
  • 53
    • 78349237370 scopus 로고    scopus 로고
    • Dengue virus-induced autophagy regulates lipid metabolism
    • Heaton NS and 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
  • 54
    • 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 PY and Chen SS. 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
  • 55
    • 67449086380 scopus 로고    scopus 로고
    • A role for autophagolysosomes in dengue virus 3 production in HepG2 cells
    • Khakpoor A, Panyasrivanit M, Wikan N and Smith DR. 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
    • 79959344614 scopus 로고    scopus 로고
    • Flavivirus NS4A-induced autophagy protects cells against death and enhances virus replication
    • McLean JE, Wudzinska A, Datan E, Quaglino D and 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
  • 59
    • 65249100786 scopus 로고    scopus 로고
    • Linking dengue virus entry and translation/replication through amphisomes
    • Panyasrivanit M, Khakpoor A, Wikan N and Smith DR. Linking dengue virus entry and translation/replication through amphisomes. Autophagy 2009, 5: 434-435.
    • (2009) Autophagy , vol.5 , pp. 434-435
    • Panyasrivanit, M.1    Khakpoor, A.2    Wikan, N.3    Smith, D.R.4
  • 60
    • 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 and Smith DR. 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
  • 61
  • 62
    • 69549135689 scopus 로고    scopus 로고
    • The autophagy machinery is required to initiate hepatitis C virus replication
    • Dreux M, Gastaminza P, Wieland SF and Chisari FV. The autophagy machinery is required to initiate hepatitis C virus replication. Proc Natl Acad Sci USA 2009, 106: 14046-14051.
    • (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
  • 63
    • 77956294587 scopus 로고    scopus 로고
    • Ultrastructural and biochemical analyses of hepatitis C virus-associated host cell membranes
    • Ferraris P, Blanchard E and 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
  • 64
    • 77949264265 scopus 로고    scopus 로고
    • Inhibition of hepatitis C virus replication by chloroquine targeting virus-associated autophagy
    • Mizui T, Yamashina S, Tanida I, Takei Y, Ueno T, Sakamoto N and Ikejima K, et al. Inhibition of hepatitis C virus replication by chloroquine targeting virus-associated autophagy. J Gastroenterol 2010, 45: 195-203.
    • (2010) J Gastroenterol , vol.45 , pp. 195-203
    • Mizui, T.1    Yamashina, S.2    Tanida, I.3    Takei, Y.4    Ueno, T.5    Sakamoto, N.6    Ikejima, K.7
  • 65
    • 54449101892 scopus 로고    scopus 로고
    • Induction of incomplete autophagic response by hepatitis C virus via the unfolded protein response
    • Sir D, Chen WL, Choi J, Wakita T, Yen TS and Ou JH. Induction of incomplete autophagic response by hepatitis C virus via the unfolded protein response. Hepatology 2008, 48: 1054-1061.
    • (2008) Hepatology , vol.48 , pp. 1054-1061
    • Sir, D.1    Chen, W.L.2    Choi, J.3    Wakita, T.4    Yen, T.S.5    Ou, J.H.6
  • 66
    • 80054978956 scopus 로고    scopus 로고
    • Rab5 and class III phosphoinositide 3-kinase Vps34 are involved in hepatitis C virus NS4B-induced autophagy
    • Su WC, Chao TC, Huang YL, Weng SC, Jeng KS and Lai MM. Rab5 and class III phosphoinositide 3-kinase Vps34 are involved in hepatitis C virus NS4B-induced autophagy. J Virol 2011, 85: 10561-10571.
    • (2011) J Virol , vol.85 , pp. 10561-10571
    • Su, W.C.1    Chao, T.C.2    Huang, Y.L.3    Weng, S.C.4    Jeng, K.S.5    Lai, M.M.6
  • 67
    • 84855827121 scopus 로고    scopus 로고
    • Dysfunction of autophagy participates in vacuole formation and cell death in cells replicating hepatitis C virus
    • Taguwa S, Kambara H, Fujita N, Noda T, Yoshimori T, Koike K and Moriishi K, et al. Dysfunction of autophagy participates in vacuole formation and cell death in cells replicating hepatitis C virus. J Virol 2011, 85: 13185-13194.
    • (2011) J Virol , vol.85 , pp. 13185-13194
    • Taguwa, S.1    Kambara, H.2    Fujita, N.3    Noda, T.4    Yoshimori, T.5    Koike, K.6    Moriishi, K.7
  • 68
    • 84855997100 scopus 로고    scopus 로고
    • Autophagy is involved in the early step of Japanese encephalitis virus infection
    • Li JK, Liang JJ, Liao CL and Lin YL. Autophagy is involved in the early step of Japanese encephalitis virus infection. Microbes Infect 2012, 14: 159-168.
    • (2012) Microbes Infect , vol.14 , pp. 159-168
    • Li, J.K.1    Liang, J.J.2    Liao, C.L.3    Lin, Y.L.4
  • 69
    • 77952766891 scopus 로고    scopus 로고
    • Autophagy: Assays and artifacts
    • Barth S, Glick D and Macleod KF. Autophagy: assays and artifacts. J Pathol 2010, 221: 117-124.
    • (2010) J Pathol , vol.221 , pp. 117-124
    • Barth, S.1    Glick, D.2    MacLeod, K.F.3
  • 71
    • 50249087889 scopus 로고    scopus 로고
    • Perturbation of autophagic pathway by hepatitis C virus
    • Sir D, Liang C, Chen WL, Jung JU and Ou JH. Perturbation of autophagic pathway by hepatitis C virus. Autophagy 2008, 4: 830-831.
    • (2008) Autophagy , vol.4 , pp. 830-831
    • Sir, D.1    Liang, C.2    Chen, W.L.3    Jung, J.U.4    Ou, J.H.5
  • 72
    • 34548077575 scopus 로고    scopus 로고
    • Dissection of the autophagosome maturation process by a novel reporter protein, tandem fluorescent-tagged LC3
    • Kimura S, Noda T and Yoshimori T. Dissection of the autophagosome maturation process by a novel reporter protein, tandem fluorescent-tagged LC3. Autophagy 2007, 3: 452-460. (Pubitemid 47293726)
    • (2007) Autophagy , vol.3 , Issue.5 , pp. 452-460
    • Kimura, S.1    Noda, T.2    Yoshimori, T.3
  • 73
    • 59749086561 scopus 로고    scopus 로고
    • The unfolded protein response and autophagy: Herpesviruses rule!
    • Lee DY, Lee J and Sugden B. The unfolded protein response and autophagy: herpesviruses rule! J Virol 2009, 83: 1168-1172.
    • (2009) J Virol , vol.83 , pp. 1168-1172
    • Lee, D.Y.1    Lee, J.2    Sugden, B.3
  • 74
    • 32044465506 scopus 로고    scopus 로고
    • TOR signaling in growth and metabolism
    • DOI 10.1016/j.cell.2006.01.016, PII S0092867406001085
    • Wullschleger S, Loewith R and Hall MN. TOR signaling in growth and metabolism. Cell 2006, 124: 471-484. (Pubitemid 43199434)
    • (2006) Cell , vol.124 , Issue.3 , pp. 471-484
    • Wullschleger, S.1    Loewith, R.2    Hall, M.N.3
  • 75
    • 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 DA, Giddings TH, Jr and 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 Jr., T.H.2    Kirkegaard, K.3
  • 76
    • 36049014444 scopus 로고    scopus 로고
    • Modification of cellular autophagy protein LC3 by poliovirus
    • DOI 10.1128/JVI.00755-07
    • Taylor MP and Kirkegaard K. Modification of cellular autophagy protein LC3 by poliovirus. J Virol 2007, 81: 12543-12553. (Pubitemid 350085868)
    • (2007) Journal of Virology , vol.81 , Issue.22 , pp. 12543-12553
    • Taylor, M.P.1    Kirkegaard, K.2
  • 77
    • 34648816108 scopus 로고    scopus 로고
    • Induction of autophagy does not affect human rhinovirus type 2 production
    • DOI 10.1128/JVI.00143-07
    • Brabec-Zaruba M, Berka U, Blaas D and Fuchs R. Induction of autophagy does not affect human rhinovirus type 2 production. J Virol 2007, 81: 10815-10817. (Pubitemid 47463354)
    • (2007) Journal of Virology , vol.81 , Issue.19 , pp. 10815-10817
    • Brabec-Zaruba, M.1    Berka, U.2    Blaas, D.3    Fuchs, R.4
  • 78
    • 70349634804 scopus 로고    scopus 로고
    • Knockdown of autophagy-related gene decreases the production of infectious hepatitis C virus particles
    • Tanida I, Fukasawa M, Ueno T, Kominami E, Wakita T and Hanada K. Knockdown of autophagy-related gene decreases the production of infectious hepatitis C virus particles. Autophagy 2009, 5: 937-945.
    • (2009) Autophagy , vol.5 , pp. 937-945
    • Tanida, I.1    Fukasawa, M.2    Ueno, T.3    Kominami, E.4    Wakita, T.5    Hanada, K.6
  • 79
    • 0028037893 scopus 로고
    • Membrane rearrangement and vesicle induction by recombinant poliovirus 2C and 2BC in human cells
    • DOI 10.1006/viro.1994.1329
    • Cho MW, Teterina N, Egger D, Bienz K and Ehrenfeld E. Membrane rearrangement and vesicle induction by recombinant poliovirus 2C and 2BC in human cells. Virology 1994, 202: 129-145. (Pubitemid 24241985)
    • (1994) Virology , vol.202 , Issue.1 , pp. 129-145
    • Cho, M.W.1    Teterina, N.2    Egger, D.3    Bienz, K.4    Ehrenfeld, E.5
  • 82
    • 0027246363 scopus 로고
    • Vectorial release of poliovirus from polarized human intestinal epithelial cells
    • Tucker SP, Thornton CL, Wimmer E and Compans RW. Vectorial release of poliovirus from polarized human intestinal epithelial cells. J Virol 1993, 67: 4274-4282. (Pubitemid 23180754)
    • (1993) Journal of Virology , vol.67 , Issue.7 , pp. 4274-4282
    • Tucker, S.P.1    Thornton, C.L.2    Wimmer, E.3    Compans, R.W.4
  • 83
    • 33846594517 scopus 로고    scopus 로고
    • Topology of double-membraned vesicles and the opportunity for non-lytic release of cytoplasm
    • Kirkegaard K and Jackson WT. Topology of double-membraned vesicles and the opportunity for non-lytic release of cytoplasm. Autophagy 2005, 1: 182-184.
    • (2005) Autophagy , vol.1 , pp. 182-184
    • Kirkegaard, K.1    Jackson, W.T.2
  • 84
    • 79251512287 scopus 로고    scopus 로고
    • Knockdown of autophagy enhances the innate immune response in hepatitis C virus-infected hepatocytes
    • Shrivastava S, Raychoudhuri A, Steele R, Ray R and Ray RB. Knockdown of autophagy enhances the innate immune response in hepatitis C virus-infected hepatocytes. Hepatology 2011, 53: 406-414.
    • (2011) Hepatology , vol.53 , pp. 406-414
    • Shrivastava, S.1    Raychoudhuri, A.2    Steele, R.3    Ray, R.4    Ray, R.B.5
  • 85
    • 79958828558 scopus 로고    scopus 로고
    • Regulation of lipid droplets by autophagy
    • Dong H and Czaja MJ. Regulation of lipid droplets by autophagy. Trends Endocrinol Metab 2011, 22: 234-240.
    • (2011) Trends Endocrinol Metab , vol.22 , pp. 234-240
    • Dong, H.1    Czaja, M.J.2
  • 87
    • 77950252174 scopus 로고    scopus 로고
    • Cross talk between apoptosis and autophagy by caspase-mediated cleavage of Beclin 1
    • Djavaheri-Mergny M, Maiuri MC and Kroemer G. Cross talk between apoptosis and autophagy by caspase-mediated cleavage of Beclin 1. Oncogene 2010, 29: 1717-1719.
    • (2010) Oncogene , vol.29 , pp. 1717-1719
    • Djavaheri-Mergny, M.1    Maiuri, M.C.2    Kroemer, G.3
  • 88
    • 28544435485 scopus 로고    scopus 로고
    • Lysosomes and autophagy in cell death control
    • DOI 10.1038/nrc1738
    • Kroemer G and Jaattela M. Lysosomes and autophagy in cell death control. Nat Rev Cancer 2005, 5: 886-897. (Pubitemid 41746033)
    • (2005) Nature Reviews Cancer , vol.5 , Issue.11 , pp. 886-897
    • Kroemer, G.1    Jaattela, M.2
  • 89
    • 48249092267 scopus 로고    scopus 로고
    • Bcl-2 family members: Dual regulators of apoptosis and autophagy
    • Levine B, Sinha S and Kroemer G. Bcl-2 family members: dual regulators of apoptosis and autophagy. Autophagy 2008, 4: 600-606.
    • (2008) Autophagy , vol.4 , pp. 600-606
    • Levine, B.1    Sinha, S.2    Kroemer, G.3
  • 90
    • 34548188741 scopus 로고    scopus 로고
    • Self-eating and self-killing: Crosstalk between autophagy and apoptosis
    • DOI 10.1038/nrm2239, PII NRM2239
    • Maiuri MC, Zalckvar E, Kimchi A and Kroemer G. Self-eating and selfkilling: crosstalk between autophagy and apoptosis. Nat Rev Mol Cell Biol 2007, 8: 741-752. (Pubitemid 47312826)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.9 , pp. 741-752
    • Maiuri, M.C.1    Zalckvar, E.2    Kimchi, A.3    Kroemer, G.4
  • 91
    • 33645823654 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway in viral infections
    • DOI 10.1139/y05-144
    • Gao G and Luo H. The ubiquitin-proteasome pathway in viral infections. Can J Physiol Pharmacol 2006, 84: 5-14. (Pubitemid 44011945)
    • (2006) Canadian Journal of Physiology and Pharmacology , vol.84 , Issue.1 , pp. 5-14
    • Gao, G.1    Luo, H.2
  • 92
    • 4143118915 scopus 로고    scopus 로고
    • Regulation of poliovirus 3C protease by the 2C polypeptide
    • DOI 10.1128/JVI.78.17.9243-9256.2004
    • Banerjee R, Weidman MK, Echeverri A, Kundu P and Dasgupta A. Regulation of poliovirus 3C protease by the 2C polypeptide. J Virol 2004, 78: 9243-9256. (Pubitemid 39096534)
    • (2004) Journal of Virology , vol.78 , Issue.17 , pp. 9243-9256
    • Banerjee, R.1    Weidman, M.K.2    Echeverri, A.3    Kundu, P.4    Dasgupta, A.5
  • 93
    • 78049473996 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system regulates the accumulation of Turnip yellow mosaic virus RNA-dependent RNA polymerase during viral infection
    • Camborde L, Planchais S, Tournier V, Jakubiec A, Drugeon G, Lacassagne E and Pflieger S, et al. The ubiquitin-proteasome system regulates the accumulation of Turnip yellow mosaic virus RNA-dependent RNA polymerase during viral infection. Plant Cell 2010, 22: 3142-3152.
    • (2010) Plant Cell , vol.22 , pp. 3142-3152
    • Camborde, L.1    Planchais, S.2    Tournier, V.3    Jakubiec, A.4    Drugeon, G.5    Lacassagne, E.6    Pflieger, S.7
  • 94
    • 78650048951 scopus 로고    scopus 로고
    • Antiviral effects of a transgenic RNA-dependent RNA polymerase
    • Kerkvliet J, Papke L and Rodriguez M. Antiviral effects of a transgenic RNA-dependent RNA polymerase. J Virol 2011, 85: 621-625.
    • (2011) J Virol , vol.85 , pp. 621-625
    • Kerkvliet, J.1    Papke, L.2    Rodriguez, M.3
  • 96
    • 0031559756 scopus 로고    scopus 로고
    • Evaluation of the susceptibility of the 3C proteases of hepatitis A virus and poliovirus to degradation by the ubiquitin-mediated proteolytic system
    • DOI 10.1006/bbrc.1997.7251
    • Gladding RL, Haas AL, Gronros DL and Lawson TG. Evaluation of the susceptibility of the 3C proteases of hepatitis A virus and poliovirus to degradation by the ubiquitin-mediated proteolytic system. Biochem Biophys Res Commun 1997, 238: 119-125. (Pubitemid 27453285)
    • (1997) Biochemical and Biophysical Research Communications , vol.238 , Issue.1 , pp. 119-125
    • Gladding, R.L.1    Haas, A.L.2    Gronros, D.L.3    Lawson, T.G.4
  • 97
    • 0033515486 scopus 로고    scopus 로고
    • Identification and characterization of a protein destruction signal in the encephalomyocarditis virus 3C protease
    • Lawson TG, Gronros DL, Evans PE, Bastien MC, Michalewich KM, Clark JK and Edmonds JH, et al. Identification and characterization of a protein destruction signal in the encephalomyocarditis virus 3C protease. J Biol Chem 1999, 274: 9904-9980.
    • (1999) J Biol Chem , vol.274 , pp. 9904-9980
    • Lawson, T.G.1    Gronros, D.L.2    Evans, P.E.3    Bastien, M.C.4    Michalewich, K.M.5    Clark, J.K.6    Edmonds, J.H.7
  • 98
    • 0037903343 scopus 로고    scopus 로고
    • Signals in hepatitis A virus P3 region proteins recognized by the ubiquitin-mediated proteolytic system
    • DOI 10.1016/S0042-6822(03)00071-0
    • Losick VP, Schlax PE, Emmons RA and Lawson TG. Signals in hepatitis A virus P3 region proteins recognized by the ubiquitin-mediated proteolytic system. Virology 2003, 309: 306-319. (Pubitemid 36579224)
    • (2003) Virology , vol.309 , Issue.2 , pp. 306-319
    • Losick, V.P.1    Schlax, P.E.2    Emmons, R.A.3    Lawson, T.G.4
  • 99
    • 67449096521 scopus 로고    scopus 로고
    • Investigation of a role for lysine residues in non-structural proteins 2 and 2/3 of the hepatitis C virus for their degradation and virus assembly
    • Welbourn S, Jirasko V, Breton V, Reiss S, Penin F, Bartenschlager R and Pause A. Investigation of a role for lysine residues in non-structural proteins 2 and 2/3 of the hepatitis C virus for their degradation and virus assembly. J Gen Virol 2009, 90: 1071-1080.
    • (2009) J Gen Virol , vol.90 , pp. 1071-1080
    • Welbourn, S.1    Jirasko, V.2    Breton, V.3    Reiss, S.4    Penin, F.5    Bartenschlager, R.6    Pause, A.7
  • 100
    • 66349128242 scopus 로고    scopus 로고
    • Viral myocarditis: From the perspective of the virus
    • Yajima T and Knowlton KU. Viral myocarditis: from the perspective of the virus. Circulation 2009, 119: 2615-2624.
    • (2009) Circulation , vol.119 , pp. 2615-2624
    • Yajima, T.1    Knowlton, K.U.2
  • 101
    • 77954892280 scopus 로고    scopus 로고
    • A role for Toll-like receptor 3 variants in host susceptibility to enteroviral myocarditis and dilated cardiomyopathy
    • Gorbea C, Makar KA, Pauschinger M, Pratt G, Bersola JL, Varela J and David RM, et al. A role for Toll-like receptor 3 variants in host susceptibility to enteroviral myocarditis and dilated cardiomyopathy. J Biol Chem 2010, 285: 23208-23223.
    • (2010) J Biol Chem , vol.285 , pp. 23208-23223
    • Gorbea, C.1    Makar, K.A.2    Pauschinger, M.3    Pratt, G.4    Bersola, J.L.5    Varela, J.6    David, R.M.7


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