메뉴 건너뛰기




Volumn 33, Issue 3, 2017, Pages 211-231

Look who’s talking—the crosstalk between oxidative stress and autophagy supports exosomal-dependent release of HCV particles

Author keywords

Autophagy; Endosomal exosomal trafficking; Hepatitis C virus; Nrf2 Keap1 signaling; p62; Reactive oxygen species (ROS)

Indexed keywords

EXOSOME MULTIENZYME RIBONUCLEASE COMPLEX; REACTIVE OXYGEN METABOLITE;

EID: 85006454823     PISSN: 07422091     EISSN: 15736822     Source Type: Journal    
DOI: 10.1007/s10565-016-9376-3     Document Type: Review
Times cited : (30)

References (225)
  • 1
    • 39749116856 scopus 로고    scopus 로고
    • Hepatitis C virus genotype 1a growth and induction of autophagy
    • COI: 1:CAS:528:DC%2BD1cXitlyhtLs%3D, PID: 18077704
    • Ait-Goughoulte M, Kanda T, Meyer K, Ryerse J, Ray R, Ray R. Hepatitis C virus genotype 1a growth and induction of autophagy. J Virol. 2008;82:2241–9.
    • (2008) J Virol , vol.82 , pp. 2241-2249
    • Ait-Goughoulte, M.1    Kanda, T.2    Meyer, K.3    Ryerse, J.4    Ray, R.5    Ray, R.6
  • 2
    • 33745280280 scopus 로고    scopus 로고
    • TIP47 is a key effector for Rab9 localization
    • COI: 1:CAS:528:DC%2BD28Xmt1aqsLk%3D, PID: 16769818
    • Aivazian D, Serrano R, Pfeffer S. TIP47 is a key effector for Rab9 localization. J Cell Biol. 2006;173:917–26.
    • (2006) J Cell Biol , vol.173 , pp. 917-926
    • Aivazian, D.1    Serrano, R.2    Pfeffer, S.3
  • 3
    • 84856800302 scopus 로고    scopus 로고
    • Role of AMPK-mTOR-Ulk1/2 in the regulation of autophagy: cross talk, shortcuts, and feedbacks
    • COI: 1:CAS:528:DC%2BC38Xjt12msro%3D, PID: 22025673
    • Alers S, Löffler A, Wesselborg S, Stork B. Role of AMPK-mTOR-Ulk1/2 in the regulation of autophagy: cross talk, shortcuts, and feedbacks. Mol Cell Biol. 2012;32:2–11.
    • (2012) Mol Cell Biol , vol.32 , pp. 2-11
    • Alers, S.1    Löffler, A.2    Wesselborg, S.3    Stork, B.4
  • 4
    • 67650531887 scopus 로고    scopus 로고
    • Microvesicles: messengers and mediators of tumor progression
    • COI: 1:CAS:528:DC%2BC3cXovFyrtg%3D%3D, PID: 19535896
    • Al-Nedawi K, Meehan B, Rak J. Microvesicles: messengers and mediators of tumor progression. Cell Cycle. 2009;8:2014–8.
    • (2009) Cell Cycle , vol.8 , pp. 2014-2018
    • Al-Nedawi, K.1    Meehan, B.2    Rak, J.3
  • 5
    • 84975215693 scopus 로고    scopus 로고
    • Exosomes in viral disease
    • COI: 1:CAS:528:DC%2BC28XhtVyiu77J, PID: 27324390
    • Anderson M, Kashanchi F, Jacobson S. Exosomes in viral disease. Neurotherapeutics. 2016;13:535–46.
    • (2016) Neurotherapeutics , vol.13 , pp. 535-546
    • Anderson, M.1    Kashanchi, F.2    Jacobson, S.3
  • 6
    • 48949103979 scopus 로고    scopus 로고
    • Mitochondrial electron transport inhibition in full genomic hepatitis C virus replicon cells is restored by reducing viral replication
    • COI: 1:CAS:528:DC%2BD1cXhtFWmsLzF, PID: 18410284
    • Ando M, Korenaga M, Hino K, Ikeda M, Kato N, Nishina S, Hidaka I, Sakaida I. Mitochondrial electron transport inhibition in full genomic hepatitis C virus replicon cells is restored by reducing viral replication. Liver Int. 2008;28:1158–66.
    • (2008) Liver Int , vol.28 , pp. 1158-1166
    • Ando, M.1    Korenaga, M.2    Hino, K.3    Ikeda, M.4    Kato, N.5    Nishina, S.6    Hidaka, I.7    Sakaida, I.8
  • 7
    • 84893823338 scopus 로고    scopus 로고
    • Regulation of autophagy by the Rab GTPase network
    • COI: 1:CAS:528:DC%2BC2cXhtVOltbk%3D, PID: 24440914
    • Ao X, Zou L, Wu Y. Regulation of autophagy by the Rab GTPase network. Cell Death Differ. 2014;21:348–58.
    • (2014) Cell Death Differ , vol.21 , pp. 348-358
    • Ao, X.1    Zou, L.2    Wu, Y.3
  • 8
    • 79251580950 scopus 로고    scopus 로고
    • The ESCRT system is required for hepatitis C virus production
    • COI: 1:CAS:528:DC%2BC3MXhtFWgtbc%3D, PID: 21264300
    • Ariumi Y, Kuroki M, Maki M, Ikeda M, Dansako H, Wakita T, Kato N. The ESCRT system is required for hepatitis C virus production. PLoS One. 2011;6:e14517.
    • (2011) PLoS One , vol.6
    • Ariumi, Y.1    Kuroki, M.2    Maki, M.3    Ikeda, M.4    Dansako, H.5    Wakita, T.6    Kato, N.7
  • 9
    • 80255136273 scopus 로고    scopus 로고
    • Bimodal targeting of cytochrome P450s to endoplasmic reticulum and mitochondria: the concept of chimeric signals
    • COI: 1:CAS:528:DC%2BC3MXhsFaksrnJ, PID: 21929726
    • Avadhani N, Sangar M, Bansal S, Bajpai P. Bimodal targeting of cytochrome P450s to endoplasmic reticulum and mitochondria: the concept of chimeric signals. FEBS J. 2011;278:4218–29.
    • (2011) FEBS J , vol.278 , pp. 4218-4229
    • Avadhani, N.1    Sangar, M.2    Bansal, S.3    Bajpai, P.4
  • 10
    • 50249084987 scopus 로고    scopus 로고
    • Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum
    • COI: 1:CAS:528:DC%2BD1cXhtV2rurzK, PID: 18725538
    • Axe E, Walker S, Manifava M, Chandra P, Roderick H, Habermann A, Griffiths G, Ktistakis N. Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum. J Cell Biol. 2008;182:685–701.
    • (2008) J Cell Biol , vol.182 , pp. 685-701
    • Axe, E.1    Walker, S.2    Manifava, M.3    Chandra, P.4    Roderick, H.5    Habermann, A.6    Griffiths, G.7    Ktistakis, N.8
  • 11
    • 84919465425 scopus 로고    scopus 로고
    • Exosomes and autophagy: coordinated mechanisms for the maintenance of cellular fitness
    • PID: 25191326
    • Baixauli F, Lopez-Otin C, Mittelbrunn M. Exosomes and autophagy: coordinated mechanisms for the maintenance of cellular fitness. Front Immunol. 2014;5:403.
    • (2014) Front Immunol , vol.5 , pp. 403
    • Baixauli, F.1    Lopez-Otin, C.2    Mittelbrunn, M.3
  • 12
    • 13944278132 scopus 로고    scopus 로고
    • Mitochondria, oxidants, and aging
    • COI: 1:CAS:528:DC%2BD2MXitVWnurg%3D, PID: 15734681
    • Balaban R, Nemoto S, Finkel T. Mitochondria, oxidants, and aging. Cell. 2005;120:483–95.
    • (2005) Cell , vol.120 , pp. 483-495
    • Balaban, R.1    Nemoto, S.2    Finkel, T.3
  • 13
    • 85000925904 scopus 로고    scopus 로고
    • Banning C
    • Wiltzer-Bach L, Schindler M. Hepatitis C virus is released via a non-canonical secretory route, J Virol
    • Bayer K, Banning C, Bruss V, Wiltzer-Bach L, Schindler M. Hepatitis C virus is released via a non-canonical secretory route. J Virol. 2016
    • (2016) Bruss , vol.5
    • Bayer, K.1
  • 14
    • 84866426167 scopus 로고    scopus 로고
    • Exosomes: vehicles for the transfer of toxic proteins associated with neurodegenerative diseases?
    • COI: 1:CAS:528:DC%2BC38Xns1Wqtbg%3D, PID: 22563321
    • Bellingham S, Guo B, Coleman B, Hill A. Exosomes: vehicles for the transfer of toxic proteins associated with neurodegenerative diseases? Front Physiol. 2012;3:124.
    • (2012) Front Physiol , vol.3 , pp. 124
    • Bellingham, S.1    Guo, B.2    Coleman, B.3    Hill, A.4
  • 16
    • 84953880644 scopus 로고    scopus 로고
    • Toward an understanding of autophagosome-lysosome fusion: the unsuspected role of ATG14
    • COI: 1:CAS:528:DC%2BC2MXhvVWqt7zF, PID: 25920502
    • Bernard A, Klionsky D. Toward an understanding of autophagosome-lysosome fusion: the unsuspected role of ATG14. Autophagy. 2015;11:583–4.
    • (2015) Autophagy , vol.11 , pp. 583-584
    • Bernard, A.1    Klionsky, D.2
  • 17
    • 84880871967 scopus 로고    scopus 로고
    • A unique hairpin-type tail-anchored SNARE starts to solve a long-time puzzle
    • PID: 23575358
    • Bernard A, Popelka H, Klionsky D. A unique hairpin-type tail-anchored SNARE starts to solve a long-time puzzle. Autophagy. 2013;9:813–4.
    • (2013) Autophagy , vol.9 , pp. 813-814
    • Bernard, A.1    Popelka, H.2    Klionsky, D.3
  • 19
    • 72849147487 scopus 로고    scopus 로고
    • Hepatitis C virus (HCV) proteins induce NADPH oxidase 4 expression in a transforming growth factor beta-dependent manner: a new contributor to HCV-induced oxidative stress
    • COI: 1:CAS:528:DC%2BD1MXhsF2gsLrN, PID: 19812163
    • Boudreau H, Emerson S, Korzeniowska A, Jendrysik M, Leto T. Hepatitis C virus (HCV) proteins induce NADPH oxidase 4 expression in a transforming growth factor beta-dependent manner: a new contributor to HCV-induced oxidative stress. J Virol. 2009;83:12934–46.
    • (2009) J Virol , vol.83 , pp. 12934-12946
    • Boudreau, H.1    Emerson, S.2    Korzeniowska, A.3    Jendrysik, M.4    Leto, T.5
  • 20
    • 84908349078 scopus 로고    scopus 로고
    • Exosomes from hepatitis C infected patients transmit HCV infection and contain replication competent viral RNA in complex with Ago2-miR122-HSP90
    • PID: 25275643
    • Bukong T, Momen-Heravi F, Kodys K, Bala S, Szabo G. Exosomes from hepatitis C infected patients transmit HCV infection and contain replication competent viral RNA in complex with Ago2-miR122-HSP90. PLoS Pathog. 2014;10:e1004424.
    • (2014) PLoS Pathog , vol.10
    • Bukong, T.1    Momen-Heravi, F.2    Kodys, K.3    Bala, S.4    Szabo, G.5
  • 21
    • 76849085285 scopus 로고    scopus 로고
    • Activation of transcription factor Nrf2 by hepatitis C virus induces the cell-survival pathway
    • COI: 1:CAS:528:DC%2BC3cXjsFalsro%3D, PID: 19889935
    • Burdette D, Olivarez M, Waris G. Activation of transcription factor Nrf2 by hepatitis C virus induces the cell-survival pathway. J. Gen. Virol. 2010;91:681–90.
    • (2010) J. Gen. Virol. , vol.91 , pp. 681-690
    • Burdette, D.1    Olivarez, M.2    Waris, G.3
  • 22
    • 34247623568 scopus 로고    scopus 로고
    • Coats, tethers, Rabs, and SNAREs work together to mediate the intracellular destination of a transport vesicle
    • COI: 1:CAS:528:DC%2BD2sXlsVajtLo%3D, PID: 17488620
    • Cai H, Reinisch K, Ferro-Novick S. Coats, tethers, Rabs, and SNAREs work together to mediate the intracellular destination of a transport vesicle. Dev Cell. 2007;12:671–82.
    • (2007) Dev Cell , vol.12 , pp. 671-682
    • Cai, H.1    Reinisch, K.2    Ferro-Novick, S.3
  • 23
    • 84875991598 scopus 로고    scopus 로고
    • Diacylglycerol acyltransferase-1 localizes hepatitis C virus NS5A protein to lipid droplets and enhances NS5A interaction with the viral capsid core
    • COI: 1:CAS:528:DC%2BC3sXlsVGgs78%3D, PID: 23420847
    • Camus G, Herker E, Modi A, Haas J, Ramage H, Farese R, Ott M. Diacylglycerol acyltransferase-1 localizes hepatitis C virus NS5A protein to lipid droplets and enhances NS5A interaction with the viral capsid core. J Biol Chem. 2013;288:9915–23.
    • (2013) J Biol Chem , vol.288 , pp. 9915-9923
    • Camus, G.1    Herker, E.2    Modi, A.3    Haas, J.4    Ramage, H.5    Farese, R.6    Ott, M.7
  • 24
    • 79953220445 scopus 로고    scopus 로고
    • Hepatitis C virus impairs the induction of cytoprotective Nrf2 target genes by delocalization of small Maf proteins
    • COI: 1:CAS:528:DC%2BC3MXjtFOju7c%3D, PID: 21216956
    • Carvajal-Yepes M, Himmelsbach K, Schaedler S, Ploen D, Krause J, Ludwig L, Weiss T, Klingel K, Hildt E. Hepatitis C virus impairs the induction of cytoprotective Nrf2 target genes by delocalization of small Maf proteins. J Biol Chem. 2011;286:8941–51.
    • (2011) J Biol Chem , vol.286 , pp. 8941-8951
    • Carvajal-Yepes, M.1    Himmelsbach, K.2    Schaedler, S.3    Ploen, D.4    Krause, J.5    Ludwig, L.6    Weiss, T.7    Klingel, K.8    Hildt, E.9
  • 25
    • 67349166918 scopus 로고    scopus 로고
    • Cholesterol synthesis inhibitor U18666A and the role of sterol metabolism and trafficking in numerous pathophysiological processes
    • COI: 1:CAS:528:DC%2BD1MXmtlOmtrc%3D, PID: 19440746
    • Cenedella R. Cholesterol synthesis inhibitor U18666A and the role of sterol metabolism and trafficking in numerous pathophysiological processes. Lipids. 2009;44:477–87.
    • (2009) Lipids , vol.44 , pp. 477-487
    • Cenedella, R.1
  • 26
    • 84934759283 scopus 로고    scopus 로고
    • Exosomes and their role in the life cycle and pathogenesis of RNA viruses
    • COI: 1:CAS:528:DC%2BC2MXhslOqt7%2FN, PID: 26102580
    • Chahar H, Bao X, Casola A. Exosomes and their role in the life cycle and pathogenesis of RNA viruses. Viruses. 2015;7:3204–25.
    • (2015) Viruses. , vol.7 , pp. 3204-3225
    • Chahar, H.1    Bao, X.2    Casola, A.3
  • 27
    • 24644495622 scopus 로고    scopus 로고
    • Hepatitis C virus envelope proteins regulate CHOP via induction of the unfolded protein response
    • COI: 1:CAS:528:DC%2BD2MXpvFKgsL8%3D, PID: 16006626
    • Chan S-W, Egan P. Hepatitis C virus envelope proteins regulate CHOP via induction of the unfolded protein response. FASEB J. 2005;19:1510–2.
    • (2005) FASEB J , vol.19 , pp. 1510-1512
    • Chan, S.-W.1    Egan, P.2
  • 28
    • 0035256978 scopus 로고    scopus 로고
    • SNARE-mediated membrane fusion
    • COI: 1:CAS:528:DC%2BD3MXivVSit7c%3D, PID: 11252968
    • Chen Y, Scheller R. SNARE-mediated membrane fusion. Nat Rev Mol Cell Biol. 2001;2:98–106.
    • (2001) Nat Rev Mol Cell Biol. , vol.2 , pp. 98-106
    • Chen, Y.1    Scheller, R.2
  • 29
    • 84874433733 scopus 로고    scopus 로고
    • Regulation of small GTPases by GEFs, GAPs, and GDIs
    • COI: 1:CAS:528:DC%2BC3sXhvFKns7s%3D, PID: 23303910
    • Cherfils J, Zeghouf M. Regulation of small GTPases by GEFs, GAPs, and GDIs. Physiol Rev. 2013;93:269–309.
    • (2013) Physiol Rev , vol.93 , pp. 269-309
    • Cherfils, J.1    Zeghouf, M.2
  • 30
    • 84880152406 scopus 로고    scopus 로고
    • Divergent roles of autophagy in virus infection
    • PID: 24709646
    • Chiramel A, Brady N, Bartenschlager R. Divergent roles of autophagy in virus infection. Cells. 2013;2:83–104.
    • (2013) Cells , vol.2 , pp. 83-104
    • Chiramel, A.1    Brady, N.2    Bartenschlager, R.3
  • 31
    • 1442306648 scopus 로고    scopus 로고
    • Reactive oxygen species suppress hepatitis C virus RNA replication in human hepatoma cells
    • COI: 1:CAS:528:DC%2BD2cXjtlCrur4%3D, PID: 14752826
    • Choi J, Lee K, Zheng Y, Yamaga A, Lai M, Ou J-H. Reactive oxygen species suppress hepatitis C virus RNA replication in human hepatoma cells. Hepatology. 2004;39:81–9.
    • (2004) Hepatology , vol.39 , pp. 81-89
    • Choi, J.1    Lee, K.2    Zheng, Y.3    Yamaga, A.4    Lai, M.5    Ou, J.-H.6
  • 32
    • 82555170658 scopus 로고    scopus 로고
    • Persistent expression of hepatitis C virus non-structural proteins leads to increased autophagy and mitochondrial injury in human hepatoma cells
    • COI: 1:CAS:528:DC%2BC3MXhs1Grur%2FF, PID: 22164304
    • Chu V, Bhattacharya S, Nomoto A, Lin J, Zaidi S, Oberley T, Weinman S, Azhar S, Huang T-T. Persistent expression of hepatitis C virus non-structural proteins leads to increased autophagy and mitochondrial injury in human hepatoma cells. PLoS One. 2011;6:e28551.
    • (2011) PLoS One , vol.6
    • Chu, V.1    Bhattacharya, S.2    Nomoto, A.3    Lin, J.4    Zaidi, S.5    Oberley, T.6    Weinman, S.7    Azhar, S.8    Huang, T.-T.9
  • 33
    • 80054758176 scopus 로고    scopus 로고
    • Involvement of members of the Rab family and related small GTPases in autophagosome formation and maturation
    • COI: 1:CAS:528:DC%2BC3MXht1eis7%2FI, PID: 21687989
    • Chua C, Gan B, Tang B. Involvement of members of the Rab family and related small GTPases in autophagosome formation and maturation. Cell Mol Life Sci. 2011;68:3349–58.
    • (2011) Cell Mol Life Sci , vol.68 , pp. 3349-3358
    • Chua, C.1    Gan, B.2    Tang, B.3
  • 34
    • 84929703770 scopus 로고    scopus 로고
    • Role of Rab GTPases and their interacting proteins in mediating metabolic signalling and regulation
    • COI: 1:CAS:528:DC%2BC2MXjtVeltLo%3D, PID: 25690707
    • Chua C, Tang B. Role of Rab GTPases and their interacting proteins in mediating metabolic signalling and regulation. Cell Mol Life Sci. 2015;72:2289–304.
    • (2015) Cell Mol Life Sci , vol.72 , pp. 2289-2304
    • Chua, C.1    Tang, B.2
  • 35
    • 77952781968 scopus 로고    scopus 로고
    • Physical and functional interaction of sequestosome 1 with Keap1 regulates the Keap1-Nrf2 cell defense pathway
    • COI: 1:CAS:528:DC%2BC3cXmtlygtr8%3D, PID: 20378532
    • Copple I, Lister A, Obeng A, Kitteringham N, Jenkins R, Layfield R, Foster B, Goldring C, Park B. Physical and functional interaction of sequestosome 1 with Keap1 regulates the Keap1-Nrf2 cell defense pathway. J Biol Chem. 2010;285:16782–8.
    • (2010) J Biol Chem , vol.285 , pp. 16782-16788
    • Copple, I.1    Lister, A.2    Obeng, A.3    Kitteringham, N.4    Jenkins, R.5    Layfield, R.6    Foster, B.7    Goldring, C.8    Park, B.9
  • 36
    • 76249128583 scopus 로고    scopus 로고
    • Vps4 and the ESCRT-III complex are required for the release of infectious hepatitis C virus particles
    • COI: 1:CAS:528:DC%2BC3cXis1equ7Y%3D, PID: 19828764
    • Corless L, Crump CM, Griffin SD, Harris M. Vps4 and the ESCRT-III complex are required for the release of infectious hepatitis C virus particles. J. Gen. Virol. 2010;91:362–72.
    • (2010) J. Gen. Virol. , vol.91 , pp. 362-372
    • Corless, L.1    Crump, C.M.2    Griffin, S.D.3    Harris, M.4
  • 37
    • 84894048545 scopus 로고    scopus 로고
    • HCV transmission by hepatic exosomes establishes a productive infection
    • PID: 24512825
    • Cosset F-L, Dreux M. HCV transmission by hepatic exosomes establishes a productive infection. J Hepatol. 2014;60:674–5.
    • (2014) J Hepatol , vol.60 , pp. 674-675
    • Cosset, F.-L.1    Dreux, M.2
  • 38
    • 84969555923 scopus 로고    scopus 로고
    • Hepatitis C virus infection induces autophagy as a prosurvival mechanism to alleviate hepatic ER-stress response
    • Dash S, Chava S, Aydin Y, Chandra P, Ferraris P, Chen W, Balart L, Wu T, Garry R. Hepatitis C virus infection induces autophagy as a prosurvival mechanism to alleviate hepatic ER-stress response. Viruses. 2016;8:150.
    • (2016) Viruses. , vol.8 , pp. 150
    • Dash, S.1    Chava, S.2    Aydin, Y.3    Chandra, P.4    Ferraris, P.5    Chen, W.6    Balart, L.7    Wu, T.8    Garry, R.9
  • 39
    • 77954236285 scopus 로고    scopus 로고
    • Hepatocyte NAD(P)H oxidases as an endogenous source of reactive oxygen species during hepatitis C virus infection
    • PID: 20578128
    • de Mochel NS, Seronello S, Wang S, Ito C, Zheng J, Liang T, Lambeth J, Choi J. Hepatocyte NAD(P)H oxidases as an endogenous source of reactive oxygen species during hepatitis C virus infection. Hepatology. 2010;52:47–59.
    • (2010) Hepatology , vol.52 , pp. 47-59
    • de Mochel, N.S.1    Seronello, S.2    Wang, S.3    Ito, C.4    Zheng, J.5    Liang, T.6    Lambeth, J.7    Choi, J.8
  • 40
    • 0035855632 scopus 로고    scopus 로고
    • Activation of the interferon-inducible protein kinase PKR by hepatocellular carcinoma derived-hepatitis C virus core protein
    • COI: 1:CAS:528:DC%2BD3MXntlSgtrc%3D, PID: 11593389
    • Delhem N, Sabile A, Gajardo R, Podevin P, Abadie A, Blaton M, Kremsdorf D, Beretta L, Brechot C. Activation of the interferon-inducible protein kinase PKR by hepatocellular carcinoma derived-hepatitis C virus core protein. Oncogene. 2001;20:5836–45.
    • (2001) Oncogene , vol.20 , pp. 5836-5845
    • Delhem, N.1    Sabile, A.2    Gajardo, R.3    Podevin, P.4    Abadie, A.5    Blaton, M.6    Kremsdorf, D.7    Beretta, L.8    Brechot, C.9
  • 42
    • 0040973364 scopus 로고    scopus 로고
    • A novel Rab9 effector required for endosome-to-TGN transport
    • PID: 9230071
    • Díaz E, Schimmöller F, Pfeffer S. A novel Rab9 effector required for endosome-to-TGN transport. J Cell Biol. 1997;138:283–90.
    • (1997) J Cell Biol , vol.138 , pp. 283-290
    • Díaz, E.1    Schimmöller, F.2    Pfeffer, S.3
  • 44
    • 73449117507 scopus 로고    scopus 로고
    • Autophagy proteins promote hepatitis C virus replication
    • PID: 19844160
    • Dreux M, Chisari F. Autophagy proteins promote hepatitis C virus replication. Autophagy. 2009a;5:1224–5.
    • (2009) Autophagy , vol.5 , pp. 1224-1225
    • Dreux, M.1    Chisari, F.2
  • 45
    • 80052166468 scopus 로고    scopus 로고
    • Impact of the autophagy machinery on hepatitis C virus infection
    • PID: 21994783
    • Dreux M, Chisari F. Impact of the autophagy machinery on hepatitis C virus infection. Viruses. 2011;3:1342–57.
    • (2011) Viruses. , vol.3 , pp. 1342-1357
    • Dreux, M.1    Chisari, F.2
  • 46
    • 84867653559 scopus 로고    scopus 로고
    • Short-range exosomal transfer of viral RNA from infected cells to plasmacytoid dendritic cells triggers innate immunity
    • COI: 1:CAS:528:DC%2BC38XhsFCksrzE, PID: 23084922
    • Dreux M, Garaigorta U, Boyd B, Décembre E, Chung J, Whitten-Bauer C, Wieland S, Chisari F. Short-range exosomal transfer of viral RNA from infected cells to plasmacytoid dendritic cells triggers innate immunity. Cell Host Microbe. 2012;12:558–70.
    • (2012) Cell Host Microbe , vol.12 , pp. 558-570
    • Dreux, M.1    Garaigorta, U.2    Boyd, B.3    Décembre, E.4    Chung, J.5    Whitten-Bauer, C.6    Wieland, S.7    Chisari, F.8
  • 47
    • 69549135689 scopus 로고    scopus 로고
    • The autophagy machinery is required to initiate hepatitis C virus replication
    • COI: 1:CAS:528:DC%2BD1MXhtFWksL%2FE, PID: 19666601
    • Dreux M, Gastaminza P, Wieland S, Chisari F. The autophagy machinery is required to initiate hepatitis C virus replication. Proc Natl Acad Sci U S A. 2009b;106:14046–51.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 14046-14051
    • Dreux, M.1    Gastaminza, P.2    Wieland, S.3    Chisari, F.4
  • 50
    • 85000995944 scopus 로고    scopus 로고
    • The intra-cellular cholesterol transport inhibitor U18666A inhibits the exosome-dependent release of mature hepatitis C virus
    • Elgner F, Ren H, Medvedev R, Ploen D, Himmelsbach K, Boller K, Hildt E. The intra-cellular cholesterol transport inhibitor U18666A inhibits the exosome-dependent release of mature hepatitis C virus. J Virol. 2016.
    • (2016) J Virol
    • Elgner, F.1    Ren, H.2    Medvedev, R.3    Ploen, D.4    Himmelsbach, K.5    Boller, K.6    Hildt, E.7
  • 51
    • 62949091373 scopus 로고    scopus 로고
    • Autophagy: a lysosomal degradation pathway with a central role in health and disease
    • COI: 1:CAS:528:DC%2BD1MXjslOlsbs%3D, PID: 18706940
    • Eskelinen E-L, Saftig P. Autophagy: a lysosomal degradation pathway with a central role in health and disease. Biochim Biophys Acta. 2009;1793:664–73.
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 664-673
    • Eskelinen, E.-L.1    Saftig, P.2
  • 53
    • 84870858655 scopus 로고    scopus 로고
    • ATP is released from autophagic vesicles to the extracellular space in a VAMP7-dependent manner
    • COI: 1:CAS:528:DC%2BC3sXitlCnsb4%3D, PID: 22951367
    • Fader C, Aguilera M, Colombo M. ATP is released from autophagic vesicles to the extracellular space in a VAMP7-dependent manner. Autophagy. 2012;8:1741–56.
    • (2012) Autophagy , vol.8 , pp. 1741-1756
    • Fader, C.1    Aguilera, M.2    Colombo, M.3
  • 54
    • 33645907831 scopus 로고    scopus 로고
    • Multivesicular bodies and autophagy in erythrocyte maturation
    • PID: 16874060
    • Fader C, Colombo M. Multivesicular bodies and autophagy in erythrocyte maturation. Autophagy. 2006;2:122–5.
    • (2006) Autophagy , vol.2 , pp. 122-125
    • Fader, C.1    Colombo, M.2
  • 55
    • 57649195400 scopus 로고    scopus 로고
    • Autophagy and multivesicular bodies: two closely related partners
    • COI: 1:CAS:528:DC%2BD1cXhsV2it7%2FO, PID: 19008921
    • Fader C, Colombo M. Autophagy and multivesicular bodies: two closely related partners. Cell Death Differ. 2009a;16:70–8.
    • (2009) Cell Death Differ , vol.16 , pp. 70-78
    • Fader, C.1    Colombo, M.2
  • 56
    • 38149044992 scopus 로고    scopus 로고
    • Induction of autophagy promotes fusion of multivesicular bodies with autophagic vacuoles in k562 cells
    • COI: 1:CAS:528:DC%2BD1cXit1SgsbY%3D, PID: 17999726
    • Fader C, Sanchez D, Furlan M, Colombo M. Induction of autophagy promotes fusion of multivesicular bodies with autophagic vacuoles in k562 cells. Traffic. 2008;9:230–50.
    • (2008) Traffic , vol.9 , pp. 230-250
    • Fader, C.1    Sanchez, D.2    Furlan, M.3    Colombo, M.4
  • 57
    • 72049088519 scopus 로고    scopus 로고
    • TI-VAMP/VAMP7 and VAMP3/cellubrevin: two v-SNARE proteins involved in specific steps of the autophagy/multivesicular body pathways
    • COI: 1:CAS:528:DC%2BD1MXhsV2gsbzE, PID: 19781582
    • Fader C, Sanchez D, Mestre M, Colombo M. TI-VAMP/VAMP7 and VAMP3/cellubrevin: two v-SNARE proteins involved in specific steps of the autophagy/multivesicular body pathways. Biochim Biophys Acta. 2009b;1793:1901–16.
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 1901-1916
    • Fader, C.1    Sanchez, D.2    Mestre, M.3    Colombo, M.4
  • 58
    • 0032430423 scopus 로고    scopus 로고
    • Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs
    • COI: 1:CAS:528:DyaK1MXhvFegtQ%3D%3D, PID: 9861047
    • Fasshauer D, Sutton R, Brunger A, Jahn R. Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs. Proc Natl Acad Sci U S A. 1998;95:15781–6.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 15781-15786
    • Fasshauer, D.1    Sutton, R.2    Brunger, A.3    Jahn, R.4
  • 59
    • 77956294587 scopus 로고    scopus 로고
    • Ultrastructural and biochemical analyses of hepatitis C virus-associated host cell membranes
    • COI: 1:CAS:528:DC%2BC3cXhtF2rtbvO, PID: 20484561
    • Ferraris P, Blanchard E, Roingeard P. Ultrastructural and biochemical analyses of hepatitis C virus-associated host cell membranes. J Gen Virol. 2010;91:2230–7.
    • (2010) J Gen Virol , vol.91 , pp. 2230-2237
    • Ferraris, P.1    Blanchard, E.2    Roingeard, P.3
  • 60
    • 35948983328 scopus 로고    scopus 로고
    • Functional multivesicular bodies are required for autophagic clearance of protein aggregates associated with neurodegenerative disease
    • COI: 1:CAS:528:DC%2BD2sXht12jsbzO, PID: 17984323
    • Filimonenko M, Stuffers S, Raiborg C, Yamamoto A, Malerød L, Fisher EMC, Isaacs A, Brech A, Stenmark H, Simonsen A. Functional multivesicular bodies are required for autophagic clearance of protein aggregates associated with neurodegenerative disease. J Cell Biol. 2007;179:485–500.
    • (2007) J Cell Biol , vol.179 , pp. 485-500
    • Filimonenko, M.1    Stuffers, S.2    Raiborg, C.3    Yamamoto, A.4    Malerød, L.5    Fisher, E.M.C.6    Isaacs, A.7    Brech, A.8    Stenmark, H.9    Simonsen, A.10
  • 62
    • 43949143804 scopus 로고    scopus 로고
    • The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy
    • COI: 1:CAS:528:DC%2BD1cXlslelsL0%3D, PID: 18321988
    • Fujita N, Itoh T, Omori H, Fukuda M, Noda T, Yoshimori T. The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy. Mol Biol Cell. 2008;19:2092–100.
    • (2008) Mol Biol Cell , vol.19 , pp. 2092-2100
    • Fujita, N.1    Itoh, T.2    Omori, H.3    Fukuda, M.4    Noda, T.5    Yoshimori, T.6
  • 63
    • 77949448601 scopus 로고    scopus 로고
    • Combinational soluble N-ethylmaleimide-sensitive factor attachment protein receptor proteins VAMP8 and Vti1b mediate fusion of antimicrobial and canonical autophagosomes with lysosomes
    • COI: 1:CAS:528:DC%2BC3cXjs1eqsLo%3D, PID: 20089838
    • Furuta N, Fujita N, Noda T, Yoshimori T, Amano A. Combinational soluble N-ethylmaleimide-sensitive factor attachment protein receptor proteins VAMP8 and Vti1b mediate fusion of antimicrobial and canonical autophagosomes with lysosomes. Mol Biol Cell. 2010;21:1001–10.
    • (2010) Mol Biol Cell , vol.21 , pp. 1001-1010
    • Furuta, N.1    Fujita, N.2    Noda, T.3    Yoshimori, T.4    Amano, A.5
  • 64
    • 77957933124 scopus 로고    scopus 로고
    • Ultrastructural and biophysical characterization of hepatitis C virus particles produced in cell culture
    • COI: 1:CAS:528:DC%2BC3cXhsVeisLbK, PID: 20686033
    • Gastaminza P, Dryden K, Boyd B, Wood M, Law M, Yeager M, Chisari F. Ultrastructural and biophysical characterization of hepatitis C virus particles produced in cell culture. J Virol. 2010;84:10999–1009.
    • (2010) J Virol , vol.84 , pp. 10999-11009
    • Gastaminza, P.1    Dryden, K.2    Boyd, B.3    Wood, M.4    Law, M.5    Yeager, M.6    Chisari, F.7
  • 65
    • 0141856621 scopus 로고    scopus 로고
    • The Trojan exosome hypothesis
    • COI: 1:CAS:528:DC%2BD3sXnslyns7o%3D, PID: 12947040
    • Gould S, Booth A, Hildreth J. The Trojan exosome hypothesis. Proc Natl Acad Sci U S A. 2003;100:10592–7.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 10592-10597
    • Gould, S.1    Booth, A.2    Hildreth, J.3
  • 67
    • 84866054964 scopus 로고    scopus 로고
    • Autophagy and RNA virus interactomes reveal IRGM as a common target
    • PID: 22722598
    • Grégoire I, Rabourdin-Combe C, Faure M. Autophagy and RNA virus interactomes reveal IRGM as a common target. Autophagy. 2012;8:1136–7.
    • (2012) Autophagy , vol.8 , pp. 1136-1137
    • Grégoire, I.1    Rabourdin-Combe, C.2    Faure, M.3
  • 68
    • 85117871479 scopus 로고    scopus 로고
    • Multiple roles of the small GTPase Rab7
    • Guerra F, Bucci C. Multiple roles of the small GTPase Rab7. Cells. 2016;5.
    • (2016) Cells , pp. 5
    • Guerra, F.1    Bucci, C.2
  • 69
    • 3242877218 scopus 로고    scopus 로고
    • Rab7 is required for the normal progression of the autophagic pathway in mammalian cells
    • COI: 1:CAS:528:DC%2BD2cXlvFeht74%3D, PID: 15138286
    • Gutierrez M, Munafo D, Beron W, Colombo M. Rab7 is required for the normal progression of the autophagic pathway in mammalian cells. J Cell Sci. 2004;117:2687–97.
    • (2004) J Cell Sci , vol.117 , pp. 2687-2697
    • Gutierrez, M.1    Munafo, D.2    Beron, W.3    Colombo, M.4
  • 70
    • 84938694329 scopus 로고    scopus 로고
    • Molecular mechanisms of Nrf2 regulation and how these influence chemical modulation for disease intervention
    • COI: 1:CAS:528:DC%2BC2MXhsVCrsb3F, PID: 26551712
    • Harder B, Jiang T, Wu T, Tao S, de la Vega Rojo M, Tian W, Chapman E, Zhang D. Molecular mechanisms of Nrf2 regulation and how these influence chemical modulation for disease intervention. Biochem Soc Trans. 2015;43:680–6.
    • (2015) Biochem Soc Trans , vol.43 , pp. 680-686
    • Harder, B.1    Jiang, T.2    Wu, T.3    Tao, S.4    de la Vega Rojo, M.5    Tian, W.6    Chapman, E.7    Zhang, D.8
  • 71
    • 84857833776 scopus 로고    scopus 로고
    • Cell signalling by reactive lipid species: new concepts and molecular mechanisms
    • COI: 1:CAS:528:DC%2BC38XivV2itbo%3D, PID: 22364280
    • Higdon A, Diers A, Oh J, Landar A, Darley-Usmar V. Cell signalling by reactive lipid species: new concepts and molecular mechanisms. Biochem J. 2012;442:453–64.
    • (2012) Biochem J , vol.442 , pp. 453-464
    • Higdon, A.1    Diers, A.2    Oh, J.3    Landar, A.4    Darley-Usmar, V.5
  • 72
    • 84893764764 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species as a mystery voice in hepatitis C
    • COI: 1:CAS:528:DC%2BC2cXit12ltL0%3D, PID: 24112394
    • Hino K, Hara Y, Nishina S. Mitochondrial reactive oxygen species as a mystery voice in hepatitis C. Hepatol Res. 2014;44:123–32.
    • (2014) Hepatol Res , vol.44 , pp. 123-132
    • Hino, K.1    Hara, Y.2    Nishina, S.3
  • 73
    • 68949214328 scopus 로고    scopus 로고
    • A small GTPase, human Rab32, is required for the formation of autophagic vacuoles under basal conditions
    • COI: 1:CAS:528:DC%2BD1MXps1Cqtrg%3D, PID: 19593531
    • Hirota Y, Tanaka Y. A small GTPase, human Rab32, is required for the formation of autophagic vacuoles under basal conditions. Cell Mol Life Sci. 2009;66:2913–32.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 2913-2932
    • Hirota, Y.1    Tanaka, Y.2
  • 74
    • 24744453945 scopus 로고    scopus 로고
    • Specific patterns of electrophile adduction trigger Keap1 ubiquitination and Nrf2 activation
    • COI: 1:CAS:528:DC%2BD2MXpslejsL0%3D, PID: 15985429
    • Hong F, Sekhar K, Freeman M, Liebler D. Specific patterns of electrophile adduction trigger Keap1 ubiquitination and Nrf2 activation. J Biol Chem. 2005;280:31768–75.
    • (2005) J Biol Chem , vol.280 , pp. 31768-31775
    • Hong, F.1    Sekhar, K.2    Freeman, M.3    Liebler, D.4
  • 75
    • 80052281413 scopus 로고    scopus 로고
    • Mitochondrial-associated endoplasmic reticulum membranes (MAM) form innate immune synapses and are targeted by hepatitis C virus
    • COI: 1:CAS:528:DC%2BC3MXhtFCltbfO, PID: 21844353
    • Horner S, Liu H, Park H, Briley J, Gale MJR. Mitochondrial-associated endoplasmic reticulum membranes (MAM) form innate immune synapses and are targeted by hepatitis C virus. Proc Natl Acad Sci U S A. 2011;108:14590–5.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 14590-14595
    • Horner, S.1    Liu, H.2    Park, H.3    Briley, J.4    Gale, M.J.R.5
  • 76
    • 36749054104 scopus 로고    scopus 로고
    • Inhibition of hepatitis C virus replication by peroxidation of arachidonate and restoration by vitamin E
    • COI: 1:CAS:528:DC%2BD2sXhtl2ku7bP, PID: 18003907
    • Huang H, Chen Y, Ye J. Inhibition of hepatitis C virus replication by peroxidation of arachidonate and restoration by vitamin E. Proc Natl Acad Sci U S A. 2007a;104:18666–70.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 18666-18670
    • Huang, H.1    Chen, Y.2    Ye, J.3
  • 77
    • 34250337631 scopus 로고    scopus 로고
    • Hepatitis C virus production by human hepatocytes dependent on assembly and secretion of very low-density lipoproteins
    • COI: 1:CAS:528:DC%2BD2sXkt1Kgt74%3D, PID: 17376867
    • Huang H, Sun F, Owen D, Li W, Chen Y, Gale M, Ye J. Hepatitis C virus production by human hepatocytes dependent on assembly and secretion of very low-density lipoproteins. Proc Natl Acad Sci U S A. 2007b;104:5848–53.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 5848-5853
    • Huang, H.1    Sun, F.2    Owen, D.3    Li, W.4    Chen, Y.5    Gale, M.6    Ye, J.7
  • 78
    • 84994047133 scopus 로고    scopus 로고
    • LAMP-2 is required for incorporating syntaxin-17 into autophagosomes and for their fusion with lysosomes
    • PID: 27628032
    • Hubert V, Peschel A, Langer B, Groger M, Rees A, Kain R. LAMP-2 is required for incorporating syntaxin-17 into autophagosomes and for their fusion with lysosomes. Biol Open. 2016;5:1516–29.
    • (2016) Biol Open , vol.5 , pp. 1516-1529
    • Hubert, V.1    Peschel, A.2    Langer, B.3    Groger, M.4    Rees, A.5    Kain, R.6
  • 79
    • 80052233389 scopus 로고    scopus 로고
    • Endosome maturation
    • COI: 1:CAS:528:DC%2BC3MXhtFSltb7L, PID: 21878991
    • Huotari J, Helenius A. Endosome maturation. EMBO J. 2011;30:3481–500.
    • (2011) EMBO J , vol.30 , pp. 3481-3500
    • Huotari, J.1    Helenius, A.2
  • 80
    • 78751656754 scopus 로고    scopus 로고
    • Role of Rab GTPases in membrane traffic and cell physiology
    • COI: 1:CAS:528:DC%2BC3MXisVCht74%3D, PID: 21248164
    • Hutagalung A, Novick P. Role of Rab GTPases in membrane traffic and cell physiology. Physiol Rev. 2011;91:119–49.
    • (2011) Physiol Rev , vol.91 , pp. 119-149
    • Hutagalung, A.1    Novick, P.2
  • 81
    • 84871903696 scopus 로고    scopus 로고
    • Maturation of autophagosomes and endosomes: a key role for Rab7
    • COI: 1:CAS:528:DC%2BC3sXht1OksLw%3D, PID: 23220125
    • Hyttinen J, Niittykoski M, Salminen A, Kaarniranta K. Maturation of autophagosomes and endosomes: a key role for Rab7. Biochim Biophys Acta. 2013;1833:503–10.
    • (2013) Biochim Biophys Acta , vol.1833 , pp. 503-510
    • Hyttinen, J.1    Niittykoski, M.2    Salminen, A.3    Kaarniranta, K.4
  • 83
    • 84978877010 scopus 로고    scopus 로고
    • Multiple types of guanine nucleotide exchange factors (GEFs) for Rab small GTPases
    • PID: 27246931
    • Ishida ME, Oguchi M, Fukuda M. Multiple types of guanine nucleotide exchange factors (GEFs) for Rab small GTPases. Cell Struct Funct. 2016;41:61–79.
    • (2016) Cell Struct Funct , vol.41 , pp. 61-79
    • Ishida, M.E.1    Oguchi, M.2    Fukuda, M.3
  • 84
    • 84870880174 scopus 로고    scopus 로고
    • The hairpin-type tail-anchored SNARE syntaxin 17 targets to autophagosomes for fusion with endosomes/lysosomes
    • COI: 1:CAS:528:DC%2BC38XhvVaisrvK, PID: 23217709
    • Itakura E, Kishi-Itakura C, Mizushima N. The hairpin-type tail-anchored SNARE syntaxin 17 targets to autophagosomes for fusion with endosomes/lysosomes. Cell. 2012;151:1256–69.
    • (2012) Cell , vol.151 , pp. 1256-1269
    • Itakura, E.1    Kishi-Itakura, C.2    Mizushima, N.3
  • 85
    • 84880907167 scopus 로고    scopus 로고
    • Syntaxin 17: the autophagosomal SNARE
    • COI: 1:CAS:528:DC%2BC3sXhvVOnsr%2FI, PID: 23466629
    • Itakura E, Mizushima N. Syntaxin 17: the autophagosomal SNARE. Autophagy. 2013;9:917–9.
    • (2013) Autophagy , vol.9 , pp. 917-919
    • Itakura, E.1    Mizushima, N.2
  • 86
    • 50249098491 scopus 로고    scopus 로고
    • Golgi-resident small GTPase Rab33B interacts with Atg16L and modulates autophagosome formation
    • COI: 1:CAS:528:DC%2BD1cXoslWitL0%3D, PID: 18448665
    • Itoh T, Fujita N, Kanno E, Yamamoto A, Yoshimori T, Fukuda M. Golgi-resident small GTPase Rab33B interacts with Atg16L and modulates autophagosome formation. Mol Biol Cell. 2008;19:2916–25.
    • (2008) Mol Biol Cell , vol.19 , pp. 2916-2925
    • Itoh, T.1    Fujita, N.2    Kanno, E.3    Yamamoto, A.4    Yoshimori, T.5    Fukuda, M.6
  • 88
    • 33747622293 scopus 로고    scopus 로고
    • SNAREs—engines for membrane fusion
    • COI: 1:CAS:528:DC%2BD28Xot12ju7g%3D, PID: 16912714
    • Jahn R, Scheller R. SNAREs—engines for membrane fusion. Nat Rev Mol Cell Biol. 2006;7:631–43.
    • (2006) Nat Rev Mol Cell Biol. , vol.7 , pp. 631-643
    • Jahn, R.1    Scheller, R.2
  • 89
    • 77954599053 scopus 로고    scopus 로고
    • p62/SQSTM1 is a target gene for transcription factor NRF2 and creates a positive feedback loop by inducing antioxidant response element-driven gene transcription
    • COI: 1:CAS:528:DC%2BC3cXos1WntLg%3D, PID: 20452972
    • Jain A, Lamark T, Sjøttem E, Larsen K, Awuh J, Øvervatn A, McMahon M, Hayes J, Johansen T. p62/SQSTM1 is a target gene for transcription factor NRF2 and creates a positive feedback loop by inducing antioxidant response element-driven gene transcription. J Biol Chem. 2010;285:22576–91.
    • (2010) J Biol Chem , vol.285 , pp. 22576-22591
    • Jain, A.1    Lamark, T.2    Sjøttem, E.3    Larsen, K.4    Awuh, J.5    Øvervatn, A.6    McMahon, M.7    Hayes, J.8    Johansen, T.9
  • 91
    • 84960971044 scopus 로고    scopus 로고
    • Subviral hepatitis B virus filaments are released like infectious viral particles via multivesicular bodies
    • PID: 26719264
    • Jiang B, Himmelsbach K, Ren H, Boller K, Hildt E. Subviral hepatitis B virus filaments are released like infectious viral particles via multivesicular bodies. J Virol. 2015a;90:3330–41.
    • (2015) J Virol , vol.90 , pp. 3330-3341
    • Jiang, B.1    Himmelsbach, K.2    Ren, H.3    Boller, K.4    Hildt, E.5
  • 92
    • 84901381389 scopus 로고    scopus 로고
    • The HOPS complex mediates autophagosome-lysosome fusion through interaction with syntaxin 17
    • PID: 24554770
    • Jiang P, Nishimura T, Sakamaki Y, Itakura E, Hatta T, Natsume T, Mizushima N. The HOPS complex mediates autophagosome-lysosome fusion through interaction with syntaxin 17. Mol Biol Cell. 2014;25:1327–37.
    • (2014) Mol Biol Cell , vol.25 , pp. 1327-1337
    • Jiang, P.1    Nishimura, T.2    Sakamaki, Y.3    Itakura, E.4    Hatta, T.5    Natsume, T.6    Mizushima, N.7
  • 94
    • 79952355107 scopus 로고    scopus 로고
    • Selective autophagy mediated by autophagic adapter proteins
    • COI: 1:CAS:528:DC%2BC3MXjvFOhsr0%3D, PID: 21189453
    • Johansen T, Lamark T. Selective autophagy mediated by autophagic adapter proteins. Autophagy. 2011;7:279–96.
    • (2011) Autophagy , vol.7 , pp. 279-296
    • Johansen, T.1    Lamark, T.2
  • 95
    • 0025890156 scopus 로고
    • Exosome formation during maturation of mammalian and avian reticulocytes: evidence that exosome release is a major route for externalization of obsolete membrane proteins
    • COI: 1:CAS:528:DyaK3MXks12iurg%3D, PID: 2037622
    • Johnstone R, Mathew A, Mason A, Teng K. Exosome formation during maturation of mammalian and avian reticulocytes: evidence that exosome release is a major route for externalization of obsolete membrane proteins. J Cell Physiol. 1991;147:27–36.
    • (1991) J Cell Physiol , vol.147 , pp. 27-36
    • Johnstone, R.1    Mathew, A.2    Mason, A.3    Teng, K.4
  • 96
    • 84878785993 scopus 로고    scopus 로고
    • The Keap1-Nrf2 pathway: mechanisms of activation and dysregulation in cancer
    • COI: 1:CAS:528:DC%2BC2cXptFygsw%3D%3D, PID: 24024136
    • Kansanen E, Kuosmanen S, Leinonen H, Levonen A-L. The Keap1-Nrf2 pathway: mechanisms of activation and dysregulation in cancer. Redox Biol. 2013;1:45–9.
    • (2013) Redox Biol , vol.1 , pp. 45-49
    • Kansanen, E.1    Kuosmanen, S.2    Leinonen, H.3    Levonen, A.-L.4
  • 97
    • 84964647174 scopus 로고    scopus 로고
    • The core of hepatitis C virus pathogenesis
    • COI: 1:CAS:528:DC%2BC28XhsFynt7w%3D, PID: 26851516
    • Kao C, Yi G, Huang H-C. The core of hepatitis C virus pathogenesis. Curr Opin Virol. 2016;17:66–73.
    • (2016) Curr Opin Virol , vol.17 , pp. 66-73
    • Kao, C.1    Yi, G.2    Huang, H.-C.3
  • 98
    • 22844442887 scopus 로고    scopus 로고
    • Intracellular localization of NS3 and C proteins in chronic hepatitis C
    • COI: 1:CAS:528:DC%2BD2MXpsVantLo%3D, PID: 15998442
    • Kasprzak A, Seidel J, Biczysko W, Wysocki J, Spachacz R, Zabel M. Intracellular localization of NS3 and C proteins in chronic hepatitis C. Liver Int. 2005;25:896–903.
    • (2005) Liver Int , vol.25 , pp. 896-903
    • Kasprzak, A.1    Seidel, J.2    Biczysko, W.3    Wysocki, J.4    Spachacz, R.5    Zabel, M.6
  • 99
    • 84954129051 scopus 로고    scopus 로고
    • p62/SQSTM1 functions as a signaling hub and an autophagy adaptor
    • COI: 1:CAS:528:DC%2BC2MXhs1KisbbO, PID: 26432171
    • Katsuragi Y, Ichimura Y, Komatsu M. p62/SQSTM1 functions as a signaling hub and an autophagy adaptor. FEBS J. 2015;282:4672–8.
    • (2015) FEBS J , vol.282 , pp. 4672-4678
    • Katsuragi, Y.1    Ichimura, Y.2    Komatsu, M.3
  • 100
    • 79955689690 scopus 로고    scopus 로고
    • Autophagy: a novel guardian of HCV against innate immune response
    • PID: 21242722
    • Ke P-Y, Chen S. Autophagy: a novel guardian of HCV against innate immune response. Autophagy. 2011;7:533–5.
    • (2011) Autophagy , vol.7 , pp. 533-535
    • Ke, P.-Y.1    Chen, S.2
  • 101
    • 84868119125 scopus 로고    scopus 로고
    • Hepatitis C virus and cellular stress response: implications to molecular pathogenesis of liver diseases
    • COI: 1:CAS:528:DC%2BC38Xhs1eqtbbJ, PID: 23202463
    • Ke P-Y, Chen S. Hepatitis C virus and cellular stress response: implications to molecular pathogenesis of liver diseases. Viruses. 2012;4:2251–90.
    • (2012) Viruses. , vol.4 , pp. 2251-2290
    • Ke, P.-Y.1    Chen, S.2
  • 102
    • 84901217944 scopus 로고    scopus 로고
    • Autophagy in hepatitis C virus-host interactions: potential roles and therapeutic targets for liver-associated diseases
    • PID: 24914338
    • Ke P-Y, Chen S. Autophagy in hepatitis C virus-host interactions: potential roles and therapeutic targets for liver-associated diseases. World J Gastroenterol. 2014;20:5773–93.
    • (2014) World J Gastroenterol , vol.20 , pp. 5773-5793
    • Ke, P.-Y.1    Chen, S.2
  • 103
    • 33847050801 scopus 로고    scopus 로고
    • Cell survival responses to environmental stresses via the Keap1-Nrf2-ARE pathway
    • COI: 1:CAS:528:DC%2BD2sXit1altrg%3D, PID: 16968214
    • Kensler T, Wakabayashi N, Biswal S. Cell survival responses to environmental stresses via the Keap1-Nrf2-ARE pathway. Annu Rev Pharmacol Toxicol. 2007a;47:89–116.
    • (2007) Annu Rev Pharmacol Toxicol , vol.47 , pp. 89-116
    • Kensler, T.1    Wakabayashi, N.2    Biswal, S.3
  • 104
    • 27844604269 scopus 로고    scopus 로고
    • Hepatitis C virus core protein inhibits mitochondrial electron transport and increases reactive oxygen species (ROS) production
    • COI: 1:CAS:528:DC%2BD2MXhtF2isrvE, PID: 16150732
    • Korenaga M, Wang T, Li Y, Showalter L, Chan T, Sun J, Weinman S. Hepatitis C virus core protein inhibits mitochondrial electron transport and increases reactive oxygen species (ROS) production. J Biol Chem. 2005;280:37481–8.
    • (2005) J Biol Chem , vol.280 , pp. 37481-37488
    • Korenaga, M.1    Wang, T.2    Li, Y.3    Showalter, L.4    Chan, T.5    Sun, J.6    Weinman, S.7
  • 105
    • 70349829157 scopus 로고    scopus 로고
    • Trans-synaptic transmission of vesicular Wnt signals through Evi/Wntless
    • COI: 1:CAS:528:DC%2BD1MXhsFWht73P, PID: 19837038
    • Korkut C, Ataman B, Ramachandran P, Ashley J, Barria R, Gherbesi N, Budnik V. Trans-synaptic transmission of vesicular Wnt signals through Evi/Wntless. Cell. 2009;139:393–404.
    • (2009) Cell , vol.139 , pp. 393-404
    • Korkut, C.1    Ataman, B.2    Ramachandran, P.3    Ashley, J.4    Barria, R.5    Gherbesi, N.6    Budnik, V.7
  • 106
    • 85014935810 scopus 로고    scopus 로고
    • The multiple roles of Rab9 in the endolysosomal system
    • PID: 27574541
    • Kucera A, Bakke O, Progida C. The multiple roles of Rab9 in the endolysosomal system. Commun Integr Biol. 2016;9:e1204498.
    • (2016) Commun Integr Biol , vol.9
    • Kucera, A.1    Bakke, O.2    Progida, C.3
  • 108
    • 77957944633 scopus 로고    scopus 로고
    • Hepatitis C virus egress and release depend on endosomal trafficking of core protein
    • COI: 1:CAS:528:DC%2BC3cXhsVeisbrJ, PID: 20739534
    • Lai C-K, Jeng K-S, Machida K, Lai MM. Hepatitis C virus egress and release depend on endosomal trafficking of core protein. J Virol. 2010a;84:11590–8.
    • (2010) J Virol , vol.84 , pp. 11590-11598
    • Lai, C.-K.1    Jeng, K.-S.2    Machida, K.3    Lai, M.M.4
  • 109
    • 84902579140 scopus 로고    scopus 로고
    • Nonstructural protein 5A is incorporated into hepatitis C virus low-density particle through interaction with core protein and microtubules during intracellular transport
    • PID: 24905011
    • Lai C-K, Saxena V, Tseng C-H, Jeng K-S, Kohara M, Lai M. Nonstructural protein 5A is incorporated into hepatitis C virus low-density particle through interaction with core protein and microtubules during intracellular transport. PLoS One. 2014;9:e99022.
    • (2014) PLoS One , vol.9
    • Lai, C.-K.1    Saxena, V.2    Tseng, C.-H.3    Jeng, K.-S.4    Kohara, M.5    Lai, M.6
  • 111
    • 19444370566 scopus 로고    scopus 로고
    • The lipid composition of autophagic vacuoles regulates expression of multilamellar bodies
    • COI: 1:CAS:528:DC%2BD2MXkslOgu7k%3D, PID: 15840653
    • Lajoie P, Guay G, Dennis J, Nabi I. The lipid composition of autophagic vacuoles regulates expression of multilamellar bodies. J Cell Sci. 2005;118:1991–2003.
    • (2005) J Cell Sci , vol.118 , pp. 1991-2003
    • Lajoie, P.1    Guay, G.2    Dennis, J.3    Nabi, I.4
  • 112
    • 84870984887 scopus 로고    scopus 로고
    • Endocytosis and autophagy: shared machinery for degradation
    • COI: 1:CAS:528:DC%2BC38XhvVCksrjL, PID: 23147242
    • Lamb C, Dooley H, Tooze S. Endocytosis and autophagy: shared machinery for degradation. BioEssays. 2013a;35:34–45.
    • (2013) BioEssays , vol.35 , pp. 34-45
    • Lamb, C.1    Dooley, H.2    Tooze, S.3
  • 113
    • 84991039873 scopus 로고    scopus 로고
    • Rabs and GAPs in starvation-induced autophagy
    • COI: 1:CAS:528:DC%2BC28XhslWjtL%2FP, PID: 27669114
    • Lamb C, Longatti A, Tooze S. Rabs and GAPs in starvation-induced autophagy. Small GTPases. 2016;7:265–9.
    • (2016) Small GTPases , vol.7 , pp. 265-269
    • Lamb, C.1    Longatti, A.2    Tooze, S.3
  • 114
    • 84888380983 scopus 로고    scopus 로고
    • The autophagosome: origins unknown, biogenesis complex
    • COI: 1:CAS:528:DC%2BC3sXhslCnur%2FJ, PID: 24201109
    • Lamb C, Yoshimori T, Tooze S. The autophagosome: origins unknown, biogenesis complex. Nat. Rev. Mol. Cell Biol. 2013b;14:759–74.
    • (2013) Nat. Rev. Mol. Cell Biol. , vol.14 , pp. 759-774
    • Lamb, C.1    Yoshimori, T.2    Tooze, S.3
  • 117
    • 37649005234 scopus 로고    scopus 로고
    • Autophagy in the pathogenesis of disease
    • COI: 1:CAS:528:DC%2BD1cXhtFehtb8%3D, PID: 18191218
    • Levine B, 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
  • 118
    • 84898785937 scopus 로고    scopus 로고
    • Redox regulation of antioxidants, autophagy, and the response to stress: implications for electrophile therapeutics
    • COI: 1:CAS:528:DC%2BC2cXovVKjt7s%3D, PID: 24681256
    • Levonen A-L, Hill B, Kansanen E, Zhang J, Darley-Usmar V. Redox regulation of antioxidants, autophagy, and the response to stress: implications for electrophile therapeutics. Free Radic Biol Med. 2014;71:196–207.
    • (2014) Free Radic Biol Med , vol.71 , pp. 196-207
    • Levonen, A.-L.1    Hill, B.2    Kansanen, E.3    Zhang, J.4    Darley-Usmar, V.5
  • 120
    • 29144462494 scopus 로고    scopus 로고
    • Hepatitis C virus protease NS3/4A cleaves mitochondrial antiviral signaling protein off the mitochondria to evade innate immunity
    • COI: 1:CAS:528:DC%2BD2MXhtlegs73O, PID: 16301520
    • Li X-D, Sun L, Seth R, Pineda G, Chen Z. Hepatitis C virus protease NS3/4A cleaves mitochondrial antiviral signaling protein off the mitochondria to evade innate immunity. Proc Natl Acad Sci U S A. 2005;102:17717–22.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 17717-17722
    • Li, X.-D.1    Sun, L.2    Seth, R.3    Pineda, G.4    Chen, Z.5
  • 121
    • 34547739644 scopus 로고    scopus 로고
    • Hepatitis C virus core protein increases mitochondrial ROS production by stimulation of Ca2+ uniporter activity
    • COI: 1:CAS:528:DC%2BD2sXptFKhurg%3D, PID: 17392480
    • Li Y, Boehning D, Qian T, Popov V, Weinman S. Hepatitis C virus core protein increases mitochondrial ROS production by stimulation of Ca2+ uniporter activity. FASEB J. 2007;21:2474–85.
    • (2007) FASEB J , vol.21 , pp. 2474-2485
    • Li, Y.1    Boehning, D.2    Qian, T.3    Popov, V.4    Weinman, S.5
  • 122
    • 84876570860 scopus 로고    scopus 로고
    • Virion assembly and release
    • COI: 1:CAS:528:DC%2BC3sXhs1ejtbbF, PID: 23463202
    • Lindenbach B. Virion assembly and release. Curr Top Microbiol Immunol. 2013;369:199–218.
    • (2013) Curr Top Microbiol Immunol , vol.369 , pp. 199-218
    • Lindenbach, B.1
  • 123
    • 84884283137 scopus 로고    scopus 로고
    • The ins and outs of hepatitis C virus entry and assembly
    • COI: 1:CAS:528:DC%2BC3sXhsVSku7rE
    • Lindenbach B, Rice C. The ins and outs of hepatitis C virus entry and assembly. Nat Rev Micro. 2013;11:688–700.
    • (2013) Nat Rev Micro , vol.11 , pp. 688-700
    • Lindenbach, B.1    Rice, C.2
  • 124
    • 84912113044 scopus 로고    scopus 로고
    • The role of reactive oxygen species (ROS) and cytochrome P-450 2E1 in the generation of carcinogenic etheno-DNA adducts
    • COI: 1:CAS:528:DC%2BC2cXhsFWlurvP, PID: 25462066
    • Linhart K, Bartsch H, Seitz H. The role of reactive oxygen species (ROS) and cytochrome P-450 2E1 in the generation of carcinogenic etheno-DNA adducts. Redox Biol. 2014;3:56–62.
    • (2014) Redox Biol , vol.3 , pp. 56-62
    • Linhart, K.1    Bartsch, H.2    Seitz, H.3
  • 125
    • 84914101527 scopus 로고    scopus 로고
    • Exosome-associated hepatitis C virus in cell cultures and patient plasma
    • COI: 1:CAS:528:DC%2BC2cXhvV2gsb%2FL, PID: 25449270
    • Liu Z, Zhang X, Yu Q, He J. Exosome-associated hepatitis C virus in cell cultures and patient plasma. Biochem Biophys Res Commun. 2014;455:218–22.
    • (2014) Biochem Biophys Res Commun , vol.455 , pp. 218-222
    • Liu, Z.1    Zhang, X.2    Yu, Q.3    He, J.4
  • 126
    • 84964402775 scopus 로고    scopus 로고
    • Role of Nrf2/HO-1 system in development, oxidative stress response and diseases: an evolutionarily conserved mechanism
    • COI: 1:CAS:528:DC%2BC28XmsFakurs%3D, PID: 27100828
    • Loboda A, Damulewicz M, Pyza E, Jozkowicz A, Dulak J. Role of Nrf2/HO-1 system in development, oxidative stress response and diseases: an evolutionarily conserved mechanism. Cell Mol Life Sci. 2016;73:3221–47.
    • (2016) Cell Mol Life Sci , vol.73 , pp. 3221-3247
    • Loboda, A.1    Damulewicz, M.2    Pyza, E.3    Jozkowicz, A.4    Dulak, J.5
  • 128
    • 84951012428 scopus 로고    scopus 로고
    • The dual role of exosomes in hepatitis a and C virus transmission and viral immune activation
    • COI: 1:CAS:528:DC%2BC28Xos1Ontrc%3D, PID: 26694453
    • Longatti A. The dual role of exosomes in hepatitis a and C virus transmission and viral immune activation. Viruses. 2015;7:6707–15.
    • (2015) Viruses , vol.7 , pp. 6707-6715
    • Longatti, A.1
  • 129
    • 84923051057 scopus 로고    scopus 로고
    • Virion-independent transfer of replication-competent hepatitis C virus RNA between permissive cells
    • PID: 25505060
    • Longatti A, Boyd B, Chisari F. Virion-independent transfer of replication-competent hepatitis C virus RNA between permissive cells. J Virol. 2015;89:2956–61.
    • (2015) J Virol , vol.89 , pp. 2956-2961
    • Longatti, A.1    Boyd, B.2    Chisari, F.3
  • 130
    • 84862611041 scopus 로고    scopus 로고
    • Yoshimura S-i, Barr F, Tooze S. TBC1D14 regulates autophagosome formation via Rab11- and ULK1-positive recycling endosomes
    • COI: 1:CAS:528:DC%2BC38XotFWgur8%3D, PID: 22613832
    • Longatti A, Lamb C, Razi M. Yoshimura S-i, Barr F, Tooze S. TBC1D14 regulates autophagosome formation via Rab11- and ULK1-positive recycling endosomes. J Cell Biol. 2012;197:659–75.
    • (2012) J Cell Biol , vol.197 , pp. 659-675
    • Longatti, A.1    Lamb, C.2    Razi, M.3
  • 131
    • 77049114949 scopus 로고    scopus 로고
    • Transcriptional responses to oxidative stress: pathological and toxicological implications
    • COI: 1:CAS:528:DC%2BC3cXit1Ogurc%3D, PID: 19945483
    • Ma Q. Transcriptional responses to oxidative stress: pathological and toxicological implications. Pharmacol Ther. 2010;125:376–93.
    • (2010) Pharmacol Ther , vol.125 , pp. 376-393
    • Ma, Q.1
  • 132
    • 79952708723 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress in liver disease
    • COI: 1:CAS:528:DC%2BC3MXjs12hsrw%3D, PID: 21145844
    • Malhi H, Kaufman R. Endoplasmic reticulum stress in liver disease. J Hepatol. 2011;54:795–809.
    • (2011) J Hepatol , vol.54 , pp. 795-809
    • Malhi, H.1    Kaufman, R.2
  • 133
    • 85000879798 scopus 로고    scopus 로고
    • Release of infectious hepatitis C virus from Huh7 cells occurs via a trans-Golgi network to endosome pathway independent of VLDL
    • Mankouri J, Walter C, Stewart H, Bentham M, Park W, Heo W, Fukuda M, Griffin S, Harris M. Release of infectious hepatitis C virus from Huh7 cells occurs via a trans-Golgi network to endosome pathway independent of VLDL. J Virol. 2016.
    • (2016) J Virol
    • Mankouri, J.1    Walter, C.2    Stewart, H.3    Bentham, M.4    Park, W.5    Heo, W.6    Fukuda, M.7    Griffin, S.8    Harris, M.9
  • 135
    • 77956404647 scopus 로고    scopus 로고
    • Exosomes: extracellular organelles important in intercellular communication
    • COI: 1:CAS:528:DC%2BC3cXhtFGjtr%2FJ
    • Mathivanan S, Ji H, Simpson R. Exosomes: extracellular organelles important in intercellular communication. J Proteome. 2010;73:1907–20.
    • (2010) J Proteome , vol.73 , pp. 1907-1920
    • Mathivanan, S.1    Ji, H.2    Simpson, R.3
  • 136
    • 84855855145 scopus 로고    scopus 로고
    • Microvesicles and viral infection
    • COI: 1:CAS:528:DC%2BC3MXhs1Shs7vM, PID: 21976651
    • Meckes DJR, Raab-Traub N. Microvesicles and viral infection. J Virol. 2011;85:12844–54.
    • (2011) J Virol , vol.85 , pp. 12844-12854
    • Meckes, D.J.R.1    Raab-Traub, N.2
  • 137
    • 84959431882 scopus 로고    scopus 로고
    • HCV and oxidative stress: implications for HCV life cycle and HCV-associated pathogenesis
    • Medvedev R, Ploen D, Hildt E. HCV and oxidative stress: implications for HCV life cycle and HCV-associated pathogenesis. Oxidative Med Cell Longev. 2016;2016:9012580.
    • (2016) Oxidative Med Cell Longev , vol.2016 , pp. 9012580
    • Medvedev, R.1    Ploen, D.2    Hildt, E.3
  • 139
    • 80052899192 scopus 로고    scopus 로고
    • HCV causes chronic endoplasmic reticulum stress leading to adaptation and interference with the unfolded protein response
    • COI: 1:CAS:528:DC%2BC3MXht1yqsrrM, PID: 21949742
    • Merquiol E, Uzi D, Mueller T, Goldenberg D, Nahmias Y, Xavier R, Tirosh B, Shibolet O. HCV causes chronic endoplasmic reticulum stress leading to adaptation and interference with the unfolded protein response. PLoS One. 2011;6:e24660.
    • (2011) PLoS One , vol.6
    • Merquiol, E.1    Uzi, D.2    Mueller, T.3    Goldenberg, D.4    Nahmias, Y.5    Xavier, R.6    Tirosh, B.7    Shibolet, O.8
  • 141
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • COI: 1:CAS:528:DC%2BD1cXisFWjt78%3D, PID: 18305538
    • Mizushima N, Levine B, Cuervo A, Klionsky D. Autophagy fights disease through cellular self-digestion. Nature. 2008;451:1069–75.
    • (2008) Nature , vol.451 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.3    Klionsky, D.4
  • 143
    • 84960342190 scopus 로고    scopus 로고
    • Early events in the generation of autophagosomes are required for the formation of membrane structures involved in hepatitis C virus genome replication
    • COI: 1:CAS:528:DC%2BC28Xht1CqsLrI, PID: 26727924
    • Mohl B-P, Bartlett C, Mankouri J, Harris M. Early events in the generation of autophagosomes are required for the formation of membrane structures involved in hepatitis C virus genome replication. J Gen Virol. 2016;97:680–93.
    • (2016) J Gen Virol , vol.97 , pp. 680-693
    • Mohl, B.-P.1    Bartlett, C.2    Mankouri, J.3    Harris, M.4
  • 144
    • 0344012048 scopus 로고    scopus 로고
    • Membrane association of hepatitis C virus nonstructural proteins and identification of the membrane alteration that harbors the viral replication complex
    • COI: 1:CAS:528:DC%2BD3sXpt1eqsrg%3D, PID: 14638405
    • Moradpour D, Gosert R, Egger D, Penin F, Blum H, Bienz K. Membrane association of hepatitis C virus nonstructural proteins and identification of the membrane alteration that harbors the viral replication complex. Antivir Res. 2003;60:103–9.
    • (2003) Antivir Res , vol.60 , pp. 103-109
    • Moradpour, D.1    Gosert, R.2    Egger, D.3    Penin, F.4    Blum, H.5    Bienz, K.6
  • 145
    • 34249024924 scopus 로고    scopus 로고
    • Replication of hepatitis C virus
    • COI: 1:CAS:528:DC%2BD2sXltlSqtb8%3D, PID: 17487147
    • Moradpour D, Penin F, Rice C. Replication of hepatitis C virus. Nat Rev Microbiol. 2007;5:453–63.
    • (2007) Nat Rev Microbiol , vol.5 , pp. 453-463
    • Moradpour, D.1    Penin, F.2    Rice, C.3
  • 146
    • 79960774898 scopus 로고    scopus 로고
    • Autophagosome precursor maturation requires homotypic fusion
    • COI: 1:CAS:528:DC%2BC3MXptlektrc%3D, PID: 21784250
    • Moreau K, Ravikumar B, Renna M, Puri C, Rubinsztein D. Autophagosome precursor maturation requires homotypic fusion. Cell. 2011;146:303–17.
    • (2011) Cell , vol.146 , pp. 303-317
    • Moreau, K.1    Ravikumar, B.2    Renna, M.3    Puri, C.4    Rubinsztein, D.5
  • 149
    • 50049122662 scopus 로고    scopus 로고
    • Decreased expression of cytochromes P450 1A2, 2E1, and 3A4 and drug transporters Na+-taurocholate-cotransporting polypeptide, organic cation transporter 1, and organic anion-transporting peptide-C correlates with the progression of liver fibrosis in chronic hepatitis C patients
    • COI: 1:CAS:528:DC%2BD1cXhtVGqsrrE, PID: 18515332
    • Nakai K, Tanaka H, Hanada K, Ogata H, Suzuki F, Kumada H, Miyajima A, Ishida S, Sunouchi M, Habano W, Kamikawa Y, Kubota K, Kita J, Ozawa S, Ohno Y. Decreased expression of cytochromes P450 1A2, 2E1, and 3A4 and drug transporters Na+-taurocholate-cotransporting polypeptide, organic cation transporter 1, and organic anion-transporting peptide-C correlates with the progression of liver fibrosis in chronic hepatitis C patients. Drug Metab Dispos. 2008;36:1786–93.
    • (2008) Drug Metab Dispos , vol.36 , pp. 1786-1793
    • Nakai, K.1    Tanaka, H.2    Hanada, K.3    Ogata, H.4    Suzuki, F.5    Kumada, H.6    Miyajima, A.7    Ishida, S.8    Sunouchi, M.9    Habano, W.10    Kamikawa, Y.11    Kubota, K.12    Kita, J.13    Ozawa, S.14    Ohno, Y.15
  • 150
    • 84902581331 scopus 로고    scopus 로고
    • Autophagy: close contact keeps out the uninvited
    • Nakatogawa H, Ohsum Y. Autophagy: close contact keeps out the uninvited. Curr Biol. 2014;24:R557–60.
    • (2014) Curr Biol , vol.24 , pp. R557-R560
    • Nakatogawa, H.1    Ohsum, Y.2
  • 152
    • 0037277404 scopus 로고    scopus 로고
    • Taxilin; a novel syntaxin-binding protein that is involved in Ca2+-dependent exocytosis in neuroendocrine cells
    • COI: 1:CAS:528:DC%2BD3sXmtFKmsQ%3D%3D, PID: 12558796
    • Nogami S, Satoh S, Nakano M, Shimizu H, Fukushima H, Maruyama A, Terano A, Shirataki H. Taxilin; a novel syntaxin-binding protein that is involved in Ca2+-dependent exocytosis in neuroendocrine cells. Genes Cells. 2003a;8:17–28.
    • (2003) Genes Cells , vol.8 , pp. 17-28
    • Nogami, S.1    Satoh, S.2    Nakano, M.3    Shimizu, H.4    Fukushima, H.5    Maruyama, A.6    Terano, A.7    Shirataki, H.8
  • 153
    • 0242521571 scopus 로고    scopus 로고
    • Interaction of taxilin with syntaxin which does not form the SNARE complex
    • COI: 1:CAS:528:DC%2BD3sXovVeisrg%3D, PID: 14623251
    • Nogami S, Satoh S, Nakano M, Terano A, Shirataki H. Interaction of taxilin with syntaxin which does not form the SNARE complex. Biochem Biophys Res Commun. 2003b;311:797–802.
    • (2003) Biochem Biophys Res Commun , vol.311 , pp. 797-802
    • Nogami, S.1    Satoh, S.2    Nakano, M.3    Terano, A.4    Shirataki, H.5
  • 154
    • 84982852199 scopus 로고    scopus 로고
    • Regulation of membrane traffic by Rab GEF and GAP cascades
    • Novick P. Regulation of membrane traffic by Rab GEF and GAP cascades. Small GTPases. 2016: 1–5.
    • (2016) Small GTPases , pp. 1-5
    • Novick, P.1
  • 155
    • 84938765962 scopus 로고    scopus 로고
    • The Keap1/Nrf2 pathway in health and disease: from the bench to the clinic
    • PID: 26551713
    • O’Connell M, Hayes J. The Keap1/Nrf2 pathway in health and disease: from the bench to the clinic. Biochem Soc Trans. 2015;43:687–9.
    • (2015) Biochem Soc Trans , vol.43 , pp. 687-689
    • O’Connell, M.1    Hayes, J.2
  • 156
    • 0036165333 scopus 로고    scopus 로고
    • Mitochondrial injury, oxidative stress, and antioxidant gene expression are induced by hepatitis C virus core protein
    • COI: 1:CAS:528:DC%2BD38XhsVGns7o%3D, PID: 11832451
    • Okuda M, Li K, Beard M, Showalter L, Scholle F, Lemon S, Weinman S. Mitochondrial injury, oxidative stress, and antioxidant gene expression are induced by hepatitis C virus core protein. Gastroenterology. 2002;122:366–75.
    • (2002) Gastroenterology , vol.122 , pp. 366-375
    • Okuda, M.1    Li, K.2    Beard, M.3    Showalter, L.4    Scholle, F.5    Lemon, S.6    Weinman, S.7
  • 157
    • 84949057575 scopus 로고    scopus 로고
    • FYCO1 contains a C-terminally extended, LC3A/B-preferring LC3-interacting region (LIR) motif required for efficient maturation of autophagosomes during basal autophagy
    • COI: 1:CAS:528:DC%2BC2MXhvFGku7%2FM, PID: 26468287
    • Olsvik H, Lamark T, Takagi K, Larsen K, Evjen G, Overvatn A, Mizushima T, Johansen T. FYCO1 contains a C-terminally extended, LC3A/B-preferring LC3-interacting region (LIR) motif required for efficient maturation of autophagosomes during basal autophagy. J Biol Chem. 2015;290:29361–74.
    • (2015) J Biol Chem , vol.290 , pp. 29361-29374
    • Olsvik, H.1    Lamark, T.2    Takagi, K.3    Larsen, K.4    Evjen, G.5    Overvatn, A.6    Mizushima, T.7    Johansen, T.8
  • 161
    • 76149086512 scopus 로고    scopus 로고
    • FYCO1 is a Rab7 effector that binds to LC3 and PI3P to mediate microtubule plus end-directed vesicle transport
    • COI: 1:CAS:528:DC%2BC3cXhsVyjsL0%3D, PID: 20100911
    • Pankiv S, Alemu E, Brech A, Bruun J-A, Lamark T, Overvatn A, Bjørkøy G, Johansen T. FYCO1 is a Rab7 effector that binds to LC3 and PI3P to mediate microtubule plus end-directed vesicle transport. J Cell Biol. 2010;188:253–69.
    • (2010) J Cell Biol , vol.188 , pp. 253-269
    • Pankiv, S.1    Alemu, E.2    Brech, A.3    Bruun, J.-A.4    Lamark, T.5    Overvatn, A.6    Bjørkøy, G.7    Johansen, T.8
  • 162
    • 66149149803 scopus 로고    scopus 로고
    • Hepatitis C virus nonstructural 4B protein modulates sterol regulatory element-binding protein signaling via the AKT pathway
    • COI: 1:CAS:528:DC%2BD1MXjs1ymsrY%3D, PID: 19204002
    • Park C-Y, Jun H-J, Wakita T, Cheong J, Hwang S. Hepatitis C virus nonstructural 4B protein modulates sterol regulatory element-binding protein signaling via the AKT pathway. J Biol Chem. 2009;284:9237–46.
    • (2009) J Biol Chem , vol.284 , pp. 9237-9246
    • Park, C.-Y.1    Jun, H.-J.2    Wakita, T.3    Cheong, J.4    Hwang, S.5
  • 163
    • 84885995316 scopus 로고    scopus 로고
    • Morphological and biochemical characterization of the membranous hepatitis C virus replication compartment
    • COI: 1:CAS:528:DC%2BC3sXhsVygtL7J, PID: 23885072
    • 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;87:10612–27.
    • (2013) J Virol , vol.87 , pp. 10612-10627
    • Paul, D.1    Hoppe, S.2    Saher, G.3    Krijnse-Locker, J.4    Bartenschlager, R.5
  • 164
    • 64749092296 scopus 로고    scopus 로고
    • Gene expression profile of Huh-7 cells expressing hepatitis C virus genotype 1b or 3a core proteins
    • COI: 1:CAS:528:DC%2BD1MXlvFSjtbo%3D, PID: 18803589
    • Pazienza V, Clement S, Pugnale P, Conzelmann S, Pascarella S, Mangia A, Negro F. Gene expression profile of Huh-7 cells expressing hepatitis C virus genotype 1b or 3a core proteins. Liver Int. 2009;29:661–9.
    • (2009) Liver Int , vol.29 , pp. 661-669
    • Pazienza, V.1    Clement, S.2    Pugnale, P.3    Conzelmann, S.4    Pascarella, S.5    Mangia, A.6    Negro, F.7
  • 166
    • 34547415672 scopus 로고    scopus 로고
    • Hepatitis C virus protein expression causes calcium-mediated mitochondrial bioenergetic dysfunction and nitro-oxidative stress
    • COI: 1:CAS:528:DC%2BD2sXosVyltrc%3D, PID: 17567832
    • Piccoli C, Scrima R, Quarato G, D’Aprile A, Ripoli M, Lecce L, Boffoli D, Moradpour D, Capitanio N. Hepatitis C virus protein expression causes calcium-mediated mitochondrial bioenergetic dysfunction and nitro-oxidative stress. Hepatology. 2007;46:58–65.
    • (2007) Hepatology , vol.46 , pp. 58-65
    • Piccoli, C.1    Scrima, R.2    Quarato, G.3    D’Aprile, A.4    Ripoli, M.5    Lecce, L.6    Boffoli, D.7    Moradpour, D.8    Capitanio, N.9
  • 168
    • 84893776013 scopus 로고    scopus 로고
    • TIP47 is associated with the hepatitis C virus and its interaction with Rab9 is required for release of viral particles
    • COI: 1:CAS:528:DC%2BC2cXhtlKgsbk%3D, PID: 24480419
    • Ploen D, Hafirassou M, Himmelsbach K, Schille S, Biniossek M, Baumert T, Schuster C, Hildt E. TIP47 is associated with the hepatitis C virus and its interaction with Rab9 is required for release of viral particles. Eur J Cell Biol. 2013b;92:374–82.
    • (2013) Eur J Cell Biol , vol.92 , pp. 374-382
    • Ploen, D.1    Hafirassou, M.2    Himmelsbach, K.3    Schille, S.4    Biniossek, M.5    Baumert, T.6    Schuster, C.7    Hildt, E.8
  • 169
    • 84937917960 scopus 로고    scopus 로고
    • Hepatitis C virus comes for dinner: how the hepatitis C virus interferes with autophagy
    • COI: 1:CAS:528:DC%2BC2MXhslGrsrbE, PID: 26229393
    • Ploen D, Hildt E. Hepatitis C virus comes for dinner: how the hepatitis C virus interferes with autophagy. World J Gastroenterol. 2015;21:8492–507.
    • (2015) World J Gastroenterol , vol.21 , pp. 8492-8507
    • Ploen, D.1    Hildt, E.2
  • 170
    • 84355162292 scopus 로고    scopus 로고
    • U18666A, an intra-cellular cholesterol transport inhibitor, inhibits dengue virus entry and replication
    • COI: 1:CAS:528:DC%2BC3MXhs1OrurnL, PID: 22146564
    • Poh M, Shui G, Xie X, Shi P-Y, Wenk M, Gu F. U18666A, an intra-cellular cholesterol transport inhibitor, inhibits dengue virus entry and replication. Antivir Res. 2012;93:191–8.
    • (2012) Antivir Res , vol.93 , pp. 191-198
    • Poh, M.1    Shui, G.2    Xie, X.3    Shi, P.-Y.4    Wenk, M.5    Gu, F.6
  • 171
    • 84865196725 scopus 로고    scopus 로고
    • Dynamics of Rab7b-dependent transport of sorting receptors
    • COI: 1:CAS:528:DC%2BC38XhtlOmtLjP, PID: 22708738
    • Progida C, Nielsen M, Koster G, Bucci C, Bakke O. Dynamics of Rab7b-dependent transport of sorting receptors. Traffic. 2012;13:1273–85.
    • (2012) Traffic , vol.13 , pp. 1273-1285
    • Progida, C.1    Nielsen, M.2    Koster, G.3    Bucci, C.4    Bakke, O.5
  • 173
    • 84874377202 scopus 로고    scopus 로고
    • Extracellular vesicles: exosomes, microvesicles, and friends
    • COI: 1:CAS:528:DC%2BC3sXjtFCnsbk%3D, PID: 23420871
    • Raposo G, Stoorvogel W. Extracellular vesicles: exosomes, microvesicles, and friends. J Cell Biol. 2013;200:373–83.
    • (2013) J Cell Biol , vol.200 , pp. 373-383
    • Raposo, G.1    Stoorvogel, W.2
  • 174
    • 33749496326 scopus 로고    scopus 로고
    • A functional role for the GCC185 golgin in mannose 6-phosphate receptor recycling
    • COI: 1:CAS:528:DC%2BD28XhtFSjt7bF, PID: 16885419
    • Reddy J, Burguete A, Sridevi K, Ganley I, Nottingham R, Pfeffer S. A functional role for the GCC185 golgin in mannose 6-phosphate receptor recycling. Mol Biol Cell. 2006;17:4353–63.
    • (2006) Mol Biol Cell , vol.17 , pp. 4353-4363
    • Reddy, J.1    Burguete, A.2    Sridevi, K.3    Ganley, I.4    Nottingham, R.5    Pfeffer, S.6
  • 175
    • 27644544004 scopus 로고    scopus 로고
    • Atg9 cycles between mitochondria and the pre-autophagosomal structure in yeasts
    • COI: 1:CAS:528:DC%2BD2MXhtVyktL7I, PID: 16874040
    • Reggiori F, Shintani T, Nair U, Klionsky D. Atg9 cycles between mitochondria and the pre-autophagosomal structure in yeasts. Autophagy. 2005;1:101–9.
    • (2005) Autophagy , vol.1 , pp. 101-109
    • Reggiori, F.1    Shintani, T.2    Nair, U.3    Klionsky, D.4
  • 177
    • 84975217888 scopus 로고    scopus 로고
    • The autophagosomal SNARE protein syntaxin 17 is an essential factor for the hepatitis C virus life cycle
    • COI: 1:CAS:528:DC%2BC28XhsFOrtbbE, PID: 27099307
    • Ren H, Elgner F, Jiang B, Himmelsbach K, Medvedev R, Ploen D, Hildt E. The autophagosomal SNARE protein syntaxin 17 is an essential factor for the hepatitis C virus life cycle. J Virol. 2016;90:5989–6000.
    • (2016) J Virol , vol.90 , pp. 5989-6000
    • Ren, H.1    Elgner, F.2    Jiang, B.3    Himmelsbach, K.4    Medvedev, R.5    Ploen, D.6    Hildt, E.7
  • 178
    • 0028224561 scopus 로고
    • Lysosome biogenesis requires Rab9 function and receptor recycling from endosomes to the trans-Golgi network
    • COI: 1:CAS:528:DyaK2cXis1Kmtr8%3D, PID: 7909812
    • Riederer M, Soldati T, Shapiro A, Lin J, Pfeffer S. Lysosome biogenesis requires Rab9 function and receptor recycling from endosomes to the trans-Golgi network. J Cell Biol. 1994;125:573–82.
    • (1994) J Cell Biol , vol.125 , pp. 573-582
    • Riederer, M.1    Soldati, T.2    Shapiro, A.3    Lin, J.4    Pfeffer, S.5
  • 179
    • 84896818399 scopus 로고    scopus 로고
    • Regulation of immune responses by extracellular vesicles
    • COI: 1:CAS:528:DC%2BC2cXivFyhtbg%3D, PID: 24566916
    • Robbins P, Morelli A. Regulation of immune responses by extracellular vesicles. Nat Rev Immunol. 2014;14:195–208.
    • (2014) Nat Rev Immunol. , vol.14 , pp. 195-208
    • Robbins, P.1    Morelli, A.2
  • 180
    • 67649600680 scopus 로고    scopus 로고
    • Cholesterol sensor ORP1L contacts the ER protein VAP to control Rab7-RILP-p150 glued and late endosome positioning
    • COI: 1:CAS:528:DC%2BD1MXot1aqt7k%3D, PID: 19564404
    • Rocha N, Kuijl C, van der Kant R, Janssen L, Houben D, Janssen H, Zwart W, Neefjes J. Cholesterol sensor ORP1L contacts the ER protein VAP to control Rab7-RILP-p150 glued and late endosome positioning. J Cell Biol. 2009;185:1209–25.
    • (2009) J Cell Biol , vol.185 , pp. 1209-1225
    • Rocha, N.1    Kuijl, C.2    van der Kant, R.3    Janssen, L.4    Houben, D.5    Janssen, H.6    Zwart, W.7    Neefjes, J.8
  • 183
    • 3242673323 scopus 로고    scopus 로고
    • Targeting of hepatitis C virus core protein to mitochondria through a novel C-terminal localization motif
    • COI: 1:CAS:528:DC%2BD2cXmtFequ7c%3D, PID: 15254168
    • Schwer B, Ren S, Pietschmann T, Kartenbeck J, Kaehlcke K, Bartenschlager R, Yen T, Ott M. Targeting of hepatitis C virus core protein to mitochondria through a novel C-terminal localization motif. J Virol. 2004;78:7958–68.
    • (2004) J Virol , vol.78 , pp. 7958-7968
    • Schwer, B.1    Ren, S.2    Pietschmann, T.3    Kartenbeck, J.4    Kaehlcke, K.5    Bartenschlager, R.6    Yen, T.7    Ott, M.8
  • 184
    • 0027531811 scopus 로고
    • Biochemical analysis of rab9, a ras-like GTPase involved in protein transport from late endosomes to the trans Golgi network
    • COI: 1:CAS:528:DyaK3sXit1ylsLo%3D, PID: 8463223
    • Shapiro A, Riederer M, Pfeffer S. Biochemical analysis of rab9, a ras-like GTPase involved in protein transport from late endosomes to the trans Golgi network. J Biol Chem. 1993;268:6925–31.
    • (1993) J Biol Chem , vol.268 , pp. 6925-6931
    • Shapiro, A.1    Riederer, M.2    Pfeffer, S.3
  • 185
    • 84865103087 scopus 로고    scopus 로고
    • Hepatitis C virus upregulates Beclin1 for induction of autophagy and activates mTOR signaling
    • COI: 1:CAS:528:DC%2BC38XhtF2jtb7K, PID: 22674982
    • Shrivastava S, Bhanja Chowdhury J, Steele R, Ray R, Ray R. Hepatitis C virus upregulates Beclin1 for induction of autophagy and activates mTOR signaling. J Virol. 2012;86:8705–12.
    • (2012) J Virol , vol.86 , pp. 8705-8712
    • Shrivastava, S.1    Bhanja Chowdhury, J.2    Steele, R.3    Ray, R.4    Ray, R.5
  • 186
    • 84958073576 scopus 로고    scopus 로고
    • Knockdown of autophagy inhibits infectious hepatitis C virus release by the exosomal pathway
    • COI: 1:CAS:528:DC%2BC28XosVClsbo%3D
    • Shrivastava S, Devhare P, Sujijantarat N, Steele R, Kwon Y-C, Ray R, Ray R. Knockdown of autophagy inhibits infectious hepatitis C virus release by the exosomal pathway. J Virol. 2016;90:1387–96.
    • (2016) J Virol , vol.90 , pp. 1387-1396
    • Shrivastava, S.1    Devhare, P.2    Sujijantarat, N.3    Steele, R.4    Kwon, Y.-C.5    Ray, R.6    Ray, R.7
  • 187
    • 84884814648 scopus 로고    scopus 로고
    • Modulation of the autophagy pathway by human tumor viruses
    • COI: 1:CAS:528:DC%2BC3sXpslGgsLc%3D, PID: 23727156
    • Silva L, Jung J. Modulation of the autophagy pathway by human tumor viruses. Semin Cancer Biol. 2013;23:323–8.
    • (2013) Semin Cancer Biol , vol.23 , pp. 323-328
    • Silva, L.1    Jung, J.2
  • 188
    • 70349919804 scopus 로고    scopus 로고
    • Coordination of membrane events during autophagy by multiple class III PI3-kinase complexes
    • COI: 1:CAS:528:DC%2BD1MXht1Srt7bO, PID: 19797076
    • Simonsen A, Tooze S. Coordination of membrane events during autophagy by multiple class III PI3-kinase complexes. J Cell Biol. 2009;186:773–82.
    • (2009) J Cell Biol , vol.186 , pp. 773-782
    • Simonsen, A.1    Tooze, S.2
  • 189
    • 54449101892 scopus 로고    scopus 로고
    • Induction of incomplete autophagic response by hepatitis C virus via the unfolded protein response
    • COI: 1:CAS:528:DC%2BD1cXht1Khu77P, PID: 18688877
    • Sir D, Chen W-L, Choi J, Wakita T, Yen TSB, J-h O. Induction of incomplete autophagic response by hepatitis C virus via the unfolded protein response. Hepatology. 2008;48:1054–61.
    • (2008) Hepatology , vol.48 , pp. 1054-1061
    • Sir, D.1    Chen, W.-L.2    Choi, J.3    Wakita, T.4    Yen, T.S.B.5    J-h, O.6
  • 190
    • 84861556595 scopus 로고    scopus 로고
    • Replication of hepatitis C virus RNA on autophagosomal membranes
    • COI: 1:CAS:528:DC%2BC38XnsF2ntro%3D, PID: 22496373
    • Sir D, C-f K, Tian Y, Liu H, Huang E, Jung J, Machida K, J-h O. Replication of hepatitis C virus RNA on autophagosomal membranes. J Biol Chem. 2012;287:18036–43.
    • (2012) J Biol Chem , vol.287 , pp. 18036-18043
    • Sir, D.1    C-f, K.2    Tian, Y.3    Liu, H.4    Huang, E.5    Jung, J.6    Machida, K.7    J-h, O.8
  • 191
    • 84962234015 scopus 로고    scopus 로고
    • Hepatitis C virus NS5A protein cooperates with phosphatidylinositol 4-kinase IIIalpha to induce mitochondrial fragmentation
    • COI: 1:CAS:528:DC%2BC28XkvVCgt7c%3D, PID: 27010100
    • Siu G, Zhou F, Yu M, Zhang L, Wang T, Liang Y, Chen Y, Chan H, Yu S. Hepatitis C virus NS5A protein cooperates with phosphatidylinositol 4-kinase IIIalpha to induce mitochondrial fragmentation. Sci Rep. 2016;6:23464.
    • (2016) Sci Rep , vol.6 , pp. 23464
    • Siu, G.1    Zhou, F.2    Yu, M.3    Zhang, L.4    Wang, T.5    Liang, Y.6    Chen, Y.7    Chan, H.8    Yu, S.9
  • 193
    • 68049105101 scopus 로고    scopus 로고
    • Rab GTPases as coordinators of vesicle traffic
    • COI: 1:CAS:528:DC%2BD1MXosFWhsrs%3D, PID: 19603039
    • Stenmark H. Rab GTPases as coordinators of vesicle traffic. Nat Rev Mol Cell Biol. 2009;10:513–25.
    • (2009) Nat Rev Mol Cell Biol. , vol.10 , pp. 513-525
    • Stenmark, H.1
  • 194
    • 34247559591 scopus 로고    scopus 로고
    • Participation of rab5, an early endosome protein, in hepatitis C virus RNA replication machinery
    • COI: 1:CAS:528:DC%2BD2sXkvFChsLg%3D, PID: 17301141
    • Stone M, Jia S, Heo W, Meyer T, Konan K. Participation of rab5, an early endosome protein, in hepatitis C virus RNA replication machinery. J Virol. 2007;81:4551–63.
    • (2007) J Virol , vol.81 , pp. 4551-4563
    • Stone, M.1    Jia, S.2    Heo, W.3    Meyer, T.4    Konan, K.5
  • 195
    • 80054978956 scopus 로고    scopus 로고
    • Rab5 and class III phosphoinositide 3-kinase Vps34 are involved in hepatitis C virus NS4B-induced autophagy
    • COI: 1:CAS:528:DC%2BC3MXhtl2nsLfI, PID: 21835792
    • Su W-C, Chao T-C, Huang Y-L, Weng S-C, Jeng K-S, Lai MM. Rab5 and class III phosphoinositide 3-kinase Vps34 are involved in hepatitis C virus NS4B-induced autophagy. J Virol. 2011;85:10561–71.
    • (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
  • 196
    • 33747335165 scopus 로고    scopus 로고
    • Roles of endogenously synthesized sterols in the endocytic pathway
    • COI: 1:CAS:528:DC%2BD28XnvVWjtbo%3D, PID: 16737966
    • Sugii S, Lin S, Ohgami N, Ohashi M, Chang C, Chang T-Y. Roles of endogenously synthesized sterols in the endocytic pathway. J Biol Chem. 2006;281:23191–206.
    • (2006) J Biol Chem , vol.281 , pp. 23191-23206
    • Sugii, S.1    Lin, S.2    Ohgami, N.3    Ohashi, M.4    Chang, C.5    Chang, T.-Y.6
  • 197
    • 80655134724 scopus 로고    scopus 로고
    • IFN-α/β and autophagy: tug-of-war between HCV and the host
    • COI: 1:CAS:528:DC%2BC38Xjs1Smt78%3D, PID: 21997372
    • Sun J, Desai M, Soong L, Ou JHJ. IFN-α/β and autophagy: tug-of-war between HCV and the host. Autophagy. 2011;7:1394–6.
    • (2011) Autophagy , vol.7 , pp. 1394-1396
    • Sun, J.1    Desai, M.2    Soong, L.3    Ou, J.H.J.4
  • 199
    • 80053962863 scopus 로고    scopus 로고
    • The role of the phosphatidylinositol 4-kinase PI4KA in hepatitis C virus-induced host membrane rearrangement
    • COI: 1:CAS:528:DC%2BC3MXhsVSgsbnP, PID: 22022594
    • Tai A, 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.1    Salloum, S.2
  • 202
    • 85019318795 scopus 로고    scopus 로고
    • Tang S, Buchkovich N, Henne W, Banjade S, Kim Y, Emr S.Exosome-mediated transmission of hepatitis C virus between human hepatoma Huh7.5 cells1 during MVB biogenesis. eLife. 2016; 5:
    • Tang S, Buchkovich N, Henne W, Banjade S, Kim Y, Emr S. ESCRT-III activation by parallel action of ESCRT-I/II and ESCRT-0/Bro. Exosome-mediated transmission of hepatitis C virus between human hepatoma Huh7.5 cells1 during MVB biogenesis. eLife. 2016; 5:
    • (2016) ESCRT-III activation by parallel action of ESCRT-I/II and ESCRT-0/Bro
  • 203
    • 84981711313 scopus 로고    scopus 로고
    • p62/SQSTM1-Dr. Jekyll and Mr. Hyde that prevents oxidative stress but promotes liver cancer
    • COI: 1:CAS:528:DC%2BC28XhsFOrt7rP, PID: 27404485
    • Taniguchi K, Yamachika S, He F, Karin M. p62/SQSTM1-Dr. Jekyll and Mr. Hyde that prevents oxidative stress but promotes liver cancer. FEBS Lett. 2016;590:2375–97.
    • (2016) FEBS Lett , vol.590 , pp. 2375-2397
    • Taniguchi, K.1    Yamachika, S.2    He, F.3    Karin, M.4
  • 204
    • 16244405250 scopus 로고    scopus 로고
    • Hepatitis C virus, ER stress, and oxidative stress
    • COI: 1:CAS:528:DC%2BD2MXjtVyqs7c%3D, PID: 15817385
    • Tardif K, Waris G, Siddiqui A. Hepatitis C virus, ER stress, and oxidative stress. Trends Microbiol. 2005;13:159–63.
    • (2005) Trends Microbiol , vol.13 , pp. 159-163
    • Tardif, K.1    Waris, G.2    Siddiqui, A.3
  • 205
    • 0036676445 scopus 로고    scopus 로고
    • Exosomes: composition, biogenesis and function
    • COI: 1:CAS:528:DC%2BD38XlslGru7k%3D, PID: 12154376
    • Thery C, Zitvogel L, Amigorena S. Exosomes: composition, biogenesis and function. Nat Rev Immunol. 2002;2:569–79.
    • (2002) Nat Rev Immunol , vol.2 , pp. 569-579
    • Thery, C.1    Zitvogel, L.2    Amigorena, S.3
  • 206
    • 0842266604 scopus 로고    scopus 로고
    • Oxidative protein folding in eukaryotes: mechanisms and consequences
    • COI: 1:CAS:528:DC%2BD2cXhtVaiu7g%3D, PID: 14757749
    • Tu B, Weissman J. Oxidative protein folding in eukaryotes: mechanisms and consequences. J Cell Biol. 2004;164:341–6.
    • (2004) J Cell Biol , vol.164 , pp. 341-346
    • Tu, B.1    Weissman, J.2
  • 207
    • 38549173564 scopus 로고    scopus 로고
    • Membrane lipids: where they are and how they behave
    • PID: 18216768
    • van Meer G, Voelker D, Feigenson G. Membrane lipids: where they are and how they behave. Nat Rev Mol Cell Biol. 2008;9:112–24.
    • (2008) Nat Rev Mol Cell Biol. , vol.9 , pp. 112-124
    • van Meer, G.1    Voelker, D.2    Feigenson, G.3
  • 209
    • 84876820482 scopus 로고    scopus 로고
    • Lipid droplet-binding protein TIP47 regulates hepatitis C virus RNA replication through interaction with the viral NS5A protein
    • COI: 1:CAS:528:DC%2BC3sXntlCruro%3D, PID: 23593007
    • Vogt D, Camus G, Herker E, Webster B, Tsou C-L, Greene W, Yen T-S, Ott M. Lipid droplet-binding protein TIP47 regulates hepatitis C virus RNA replication through interaction with the viral NS5A protein. PLoS Pathog. 2013;9:e1003302.
    • (2013) PLoS Pathog , vol.9
    • Vogt, D.1    Camus, G.2    Herker, E.3    Webster, B.4    Tsou, C.-L.5    Greene, W.6    Yen, T.-S.7    Ott, M.8
  • 210
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: from stress pathway to homeostatic regulation
    • COI: 1:CAS:528:DC%2BC3MXhsV2mu7jL, PID: 22116877
    • Walter P, Ron D. The unfolded protein response: from stress pathway to homeostatic regulation. Science. 2011;334:1081–6.
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 211
    • 79952197289 scopus 로고    scopus 로고
    • Role of hepatitis C virus core protein in viral-induced mitochondrial dysfunction
    • COI: 1:STN:280:DC%2BC3cbjsFOlsw%3D%3D, PID: 20002299
    • Wang T, Campbell R, Yi M, Lemon S, Weinman S. Role of hepatitis C virus core protein in viral-induced mitochondrial dysfunction. J Viral Hepat. 2010;17:784–93.
    • (2010) J Viral Hepat , vol.17 , pp. 784-793
    • Wang, T.1    Campbell, R.2    Yi, M.3    Lemon, S.4    Weinman, S.5
  • 212
    • 84896844772 scopus 로고    scopus 로고
    • Interactions between hepatitis C virus and mitochondria: impact on pathogenesis and innate immunity
    • PID: 23956955
    • Wang T, Weinman S. Interactions between hepatitis C virus and mitochondria: impact on pathogenesis and innate immunity. Curr Pathobiol Rep. 2013;1:179–87.
    • (2013) Curr Pathobiol Rep , vol.1 , pp. 179-187
    • Wang, T.1    Weinman, S.2
  • 216
    • 84974602682 scopus 로고    scopus 로고
    • Cholesterol and ORP1L-mediated ER contact sites control autophagosome transport and fusion with the endocytic pathway
    • COI: 1:CAS:528:DC%2BC28Xpslykurk%3D, PID: 27283760
    • Wijdeven R, Janssen H, Nahidiazar L, Janssen L, Jalink K, Berlin I, Neefjes J. Cholesterol and ORP1L-mediated ER contact sites control autophagosome transport and fusion with the endocytic pathway. Nat Commun. 2016;7:11808.
    • (2016) Nat Commun , vol.7 , pp. 11808
    • Wijdeven, R.1    Janssen, H.2    Nahidiazar, L.3    Janssen, L.4    Jalink, K.5    Berlin, I.6    Neefjes, J.7
  • 217
    • 34247342216 scopus 로고    scopus 로고
    • The emerging shape of the ESCRT machinery
    • COI: 1:CAS:528:DC%2BD2sXksFSjsrw%3D, PID: 17450176
    • Williams R, Urbe S. The emerging shape of the ESCRT machinery. Nat Rev Mol Cell Biol. 2007;8:355–68.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 355-368
    • Williams, R.1    Urbe, S.2
  • 219
    • 84903901688 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress links hepatitis C virus RNA replication to wild-type PGC-1alpha/liver-specific PGC-1alpha upregulation
    • PID: 24829353
    • Yao W, Cai H, Li X, Li T, Hu L, Peng T. Endoplasmic reticulum stress links hepatitis C virus RNA replication to wild-type PGC-1alpha/liver-specific PGC-1alpha upregulation. J Virol. 2014;88:8361–74.
    • (2014) J Virol , vol.88 , pp. 8361-8374
    • Yao, W.1    Cai, H.2    Li, X.3    Li, T.4    Hu, L.5    Peng, T.6
  • 221
    • 75749135725 scopus 로고    scopus 로고
    • The conserved oligomeric Golgi complex is involved in double-membrane vesicle formation during autophagy
    • COI: 1:CAS:528:DC%2BC3cXntFKhug%3D%3D, PID: 20065092
    • Yen W-L, Shintani T, Nair U, Cao Y, Richardson B, Li Z, Hughson F, Baba M, Klionsky D. The conserved oligomeric Golgi complex is involved in double-membrane vesicle formation during autophagy. J Cell Biol. 2010;188:101–14.
    • (2010) J Cell Biol , vol.188 , pp. 101-114
    • Yen, W.-L.1    Shintani, T.2    Nair, U.3    Cao, Y.4    Richardson, B.5    Li, Z.6    Hughson, F.7    Baba, M.8    Klionsky, D.9
  • 223
    • 0035257013 scopus 로고    scopus 로고
    • Rab proteins as membrane organizers
    • COI: 1:CAS:528:DC%2BD3MXivVSitL8%3D, PID: 11252952
    • Zerial M, McBride H. Rab proteins as membrane organizers. Nat Rev Mol Cell Biol. 2001;2:107–17.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 107-117
    • Zerial, M.1    McBride, H.2
  • 224
    • 84946037451 scopus 로고    scopus 로고
    • Cellular functions of Rab GTPases at a glance
    • COI: 1:CAS:528:DC%2BC28XmvVWmu78%3D, PID: 26272922
    • Zhen Y, Stenmark H. Cellular functions of Rab GTPases at a glance. J Cell Sci. 2015;128:3171–6.
    • (2015) J Cell Sci , vol.128 , pp. 3171-3176
    • Zhen, Y.1    Stenmark, H.2
  • 225
    • 30744475504 scopus 로고    scopus 로고
    • Hepatitis C virus non-structural protein NS4B can modulate an unfolded protein response
    • COI: 1:CAS:528:DC%2BD1cXitVSgt70%3D, PID: 16410770
    • Zheng Y, Gao B, Ye L, Kong L, Jing W, Yang X, Wu Z, Ye L. Hepatitis C virus non-structural protein NS4B can modulate an unfolded protein response. J Microbiol. 2005;43:529–36.
    • (2005) J Microbiol , vol.43 , pp. 529-536
    • Zheng, Y.1    Gao, B.2    Ye, L.3    Kong, L.4    Jing, W.5    Yang, X.6    Wu, Z.7    Ye, L.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.