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Volumn 45, Issue 1, 2011, Pages 110-122

Cell defense systems against oxidative stress and endoplasmic reticulum stress: Mechanisms of regulation and the effect of hepatitis C virus

Author keywords

endoplasmic reticulum stress; hepatitis C virus; oxidative stress; regulation; transcription factor

Indexed keywords

HEPATITIS C VIRUS;

EID: 79951977937     PISSN: 00268933     EISSN: 16083245     Source Type: Journal    
DOI: 10.1134/S0026893311010122     Document Type: Review
Times cited : (4)

References (139)
  • 1
    • 0003171299 scopus 로고    scopus 로고
    • Report of a WHO Consultation organized in collaboration with the Viral Hepatitis Prevention Board, Antwerp, Belgium
    • Global surveillancecontrol of hepatitis C
    • Global surveillance and control of hepatitis C. Report of a WHO Consultation organized in collaboration with the Viral Hepatitis Prevention Board, Antwerp, Belgium. 1999. J. Viral. Hepat. 6, 35-47.
    • (1999) J. Viral. Hepat. , vol.6 , pp. 35-47
  • 2
    • 0026538287 scopus 로고
    • Hepatitis C virus (HCV) circulates as a population of different but closely related genomes: Quasispecies nature of HCV genome distribution
    • Martell M., Esteban J. I., Quer J., Genesca J., Weiner A., Esteban R., Guardia J., Gomez J. 1992. Hepatitis C virus (HCV) circulates as a population of different but closely related genomes: Quasispecies nature of HCV genome distribution. J. Virol. 66, 3225-3229.
    • (1992) J. Virol. , vol.66 , pp. 3225-3229
    • Martell, M.1    Esteban, J.I.2    Quer, J.3    Genesca, J.4    Weiner, A.5    Esteban, R.6    Guardia, J.7    Gomez, J.8
  • 3
    • 77950648470 scopus 로고    scopus 로고
    • An overview about hepatitis C: A devastating virus
    • Bostan N., Mahmood T. 2010. An overview about hepatitis C: A devastating virus. Crit. Rev. Microbiol. 36, 91-133.
    • (2010) Crit. Rev. Microbiol. , vol.36 , pp. 91-133
    • Bostan, N.1    Mahmood, T.2
  • 4
    • 34547094367 scopus 로고    scopus 로고
    • Hepatitis C virus
    • D. M. Knipe and P. M. Howley (Eds.), Philadelphia, PA.: Lippincott Williams & Wilkins
    • Lemon S. A., Walker C. M., Alter M. J., Yi M.-K. 2007. Hepatitis C virus. In: Fields Virology, vol. 1. Eds. Knipe D. M., Howley P. M. Philadelphia, PA.: Lippincott Williams & Wilkins, pp. 1253-1304.
    • (2007) Fields Virology , pp. 1253-1304
    • Lemon, S.A.1    Walker, C.M.2    Alter, M.J.3    Yi, M.-K.4
  • 5
    • 0032768206 scopus 로고    scopus 로고
    • Hepatitis C virus: Current understanding and prospects for future therapies
    • Rosen H. R., Gretch D. R. 1999. Hepatitis C virus: Current understanding and prospects for future therapies. Mol. Med. Today. 5, 393-399.
    • (1999) Mol. Med. Today. , vol.5 , pp. 393-399
    • Rosen, H.R.1    Gretch, D.R.2
  • 8
    • 33747797031 scopus 로고    scopus 로고
    • Treating viral hepatitis C: Efficacy, side effects, and complications
    • Manns M. P., Wedemeyer H., Cornberg M. 2006. Treating viral hepatitis C: Efficacy, side effects, and complications. Gut. 55, 1350-1359.
    • (2006) Gut. , vol.55 , pp. 1350-1359
    • Manns, M.P.1    Wedemeyer, H.2    Cornberg, M.3
  • 9
    • 43849091636 scopus 로고    scopus 로고
    • New developments in the discovery of agents to treat hepatitis C
    • Ronn R., Sandstrom A. 2008. New developments in the discovery of agents to treat hepatitis C. Curr. Top. Med. Chem. 8, 533-562.
    • (2008) Curr. Top. Med. Chem. , vol.8 , pp. 533-562
    • Ronn, R.1    Sandstrom, A.2
  • 12
    • 33750344724 scopus 로고    scopus 로고
    • Different transformation pathways of murine fibroblast NIH 3T3 cells by hepatitis C virus core and NS3 proteins
    • Smirnova I. S., Aksenov N. D., Vonsky M. S., Isaguliants M. G. 2006. Different transformation pathways of murine fibroblast NIH 3T3 cells by hepatitis C virus core and NS3 proteins. Cell Biol. Int. 30, 915-919.
    • (2006) Cell Biol. Int. , vol.30 , pp. 915-919
    • Smirnova, I.S.1    Aksenov, N.D.2    Vonsky, M.S.3    Isaguliants, M.G.4
  • 13
    • 0034684968 scopus 로고    scopus 로고
    • Hepatitis C virus nonstructural protein NS4B transforms NIH3T3 cells in cooperation with the Ha-ras oncogene
    • Park J. S., Yang J. M., Min M. K. 2000. Hepatitis C virus nonstructural protein NS4B transforms NIH3T3 cells in cooperation with the Ha-ras oncogene. Biochem. Biophys. Res. Commun. 267, 581-587.
    • (2000) Biochem. Biophys. Res. Commun. , vol.267 , pp. 581-587
    • Park, J.S.1    Yang, J.M.2    Min, M.K.3
  • 15
    • 0036314483 scopus 로고    scopus 로고
    • Hepatitis C virus subgenomic replicons induce endoplasmic reticulum stress activating an intracellular signaling pathway
    • Tardif K. D., Mori K., Siddiqui A. 2002. Hepatitis C virus subgenomic replicons induce endoplasmic reticulum stress activating an intracellular signaling pathway. J. Virol. 76, 7453-7459.
    • (2002) J. Virol. , vol.76 , pp. 7453-7459
    • Tardif, K.D.1    Mori, K.2    Siddiqui, A.3
  • 16
    • 0034625351 scopus 로고    scopus 로고
    • Template requirement and initiation site selection by hepatitis C virus polymerase on a minimal viral RNA template
    • Oh J. W., Sheu G. T., Lai M. M. 2000. Template requirement and initiation site selection by hepatitis C virus polymerase on a minimal viral RNA template. J. Biol. Chem. 275, 17710-17717.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17710-17717
    • Oh, J.W.1    Sheu, G.T.2    Lai, M.M.3
  • 19
    • 0034712884 scopus 로고    scopus 로고
    • Selective binding of hepatitis C virus core protein to synthetic oligonucleotides corresponding to the 5′ untranslated region of the viral genome
    • Tanaka Y., Shimoike T., Ishii K., Suzuki R., Suzuki T., Ushijima H., Matsuura Y., Miyamura T. 2000. Selective binding of hepatitis C virus core protein to synthetic oligonucleotides corresponding to the 5′ untranslated region of the viral genome. Virology. 270, 229-236.
    • (2000) Virology. , vol.270 , pp. 229-236
    • Tanaka, Y.1    Shimoike, T.2    Ishii, K.3    Suzuki, R.4    Suzuki, T.5    Ushijima, H.6    Matsuura, Y.7    Miyamura, T.8
  • 20
    • 1942436893 scopus 로고    scopus 로고
    • Modulation of p53 transcription regulatory activity and post-translational modification by hepatitis C virus core protein
    • Kao C. F., Chen S. Y., Chen J. Y., Wu Lee Y. H. 2004. Modulation of p53 transcription regulatory activity and post-translational modification by hepatitis C virus core protein. Oncogene. 23, 2472-2483.
    • (2004) Oncogene. , vol.23 , pp. 2472-2483
    • Kao, C.F.1    Chen, S.Y.2    Chen, J.Y.3    Wu Lee, Y.H.4
  • 21
    • 0033016472 scopus 로고    scopus 로고
    • Hepatitis C virus core protein binds to a DEAD box RNA helicase
    • Mamiya N., Worman H. J. 1999. Hepatitis C virus core protein binds to a DEAD box RNA helicase. J. Biol. Chem. 274, 15751-15756.
    • (1999) J. Biol. Chem. , vol.274 , pp. 15751-15756
    • Mamiya, N.1    Worman, H.J.2
  • 22
    • 0141785229 scopus 로고    scopus 로고
    • Differential activation of interferon-inducible genes by hepatitis C virus core protein mediated by the interferon stimulated response element
    • Dansako H., Naganuma A., Nakamura T., Ikeda F., Nozaki A., Kato N. 2003. Differential activation of interferon-inducible genes by hepatitis C virus core protein mediated by the interferon stimulated response element. Virus Res. 97, 17-30.
    • (2003) Virus Res. , vol.97 , pp. 17-30
    • Dansako, H.1    Naganuma, A.2    Nakamura, T.3    Ikeda, F.4    Nozaki, A.5    Kato, N.6
  • 23
    • 27844604269 scopus 로고    scopus 로고
    • Hepatitis C virus core protein inhibits mitochondrial electron transport and increases reactive oxygen species (ROS) production
    • Korenaga M., Wang T., Li Y., Showalter L. A., Chan T., Sun J., Weinman S. A. 2005. Hepatitis C virus core protein inhibits mitochondrial electron transport and increases reactive oxygen species (ROS) production. J. Biol. Chem. 280, 37481-37488.
    • (2005) J. Biol. Chem. , vol.280 , pp. 37481-37488
    • Korenaga, M.1    Wang, T.2    Li, Y.3    Showalter, L.A.4    Chan, T.5    Sun, J.6    Weinman, S.A.7
  • 25
    • 34547775736 scopus 로고    scopus 로고
    • Characterization of fusion determinants points to the involvement of three discrete regions of both E1 and E2 glycoproteins in the membrane fusion process of hepatitis C virus
    • Lavillette D., Pecheur E. I., Donot P., Fresquet J., Molle J., Corbau R., Dreux M., Penin F., Cosset F. L. 2007. Characterization of fusion determinants points to the involvement of three discrete regions of both E1 and E2 glycoproteins in the membrane fusion process of hepatitis C virus. J. Virol. 81, 8752-8765.
    • (2007) J. Virol. , vol.81 , pp. 8752-8765
    • Lavillette, D.1    Pecheur, E.I.2    Donot, P.3    Fresquet, J.4    Molle, J.5    Corbau, R.6    Dreux, M.7    Penin, F.8    Cosset, F.L.9
  • 27
    • 24644495622 scopus 로고    scopus 로고
    • Hepatitis C virus envelope proteins regulate CHOP via induction of the unfolded protein response
    • Chan S. W., Egan P. A. 2005. Hepatitis C virus envelope proteins regulate CHOP via induction of the unfolded protein response. FASEB J. 19, 1510-1512.
    • (2005) FASEB J. , vol.19 , pp. 1510-1512
    • Chan, S.W.1    Egan, P.A.2
  • 30
    • 0029970903 scopus 로고    scopus 로고
    • The helicase activity associated with hepatitis C virus nonstructural protein 3 (NS3)
    • Tai C. L., Chi W. K., Chen D. S., Hwang L. H. 1996. The helicase activity associated with hepatitis C virus nonstructural protein 3 (NS3). J. Virol. 70, 8477-8484.
    • (1996) J. Virol. , vol.70 , pp. 8477-8484
    • Tai, C.L.1    Chi, W.K.2    Chen, D.S.3    Hwang, L.H.4
  • 32
    • 0344373790 scopus 로고    scopus 로고
    • Topology of the membrane-associated hepatitis C virus protein NS4B
    • Lundin M., Monne M., Widell A., Von Heijne G., Persson M. A. 2003. Topology of the membrane-associated hepatitis C virus protein NS4B. J. Virol. 77, 5428-5438.
    • (2003) J. Virol. , vol.77 , pp. 5428-5438
    • Lundin, M.1    Monne, M.2    Widell, A.3    von Heijne, G.4    Persson, M.A.5
  • 33
    • 30744475504 scopus 로고    scopus 로고
    • Hepatitis C virus non-structural protein NS4B can modulate an unfolded protein response
    • Zheng Y., Gao B., Ye L., Kong L., Jing W., Yang X., Wu Z. 2005. Hepatitis C virus non-structural protein NS4B can modulate an unfolded protein response. J. Microbiol. 43, 529-536.
    • (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
  • 34
    • 4544336360 scopus 로고    scopus 로고
    • Hepatitis C virus NS5A: tales of a promiscuous protein
    • Macdonald A., Harris M. 2004. Hepatitis C virus NS5A: tales of a promiscuous protein. J. Gen. Virol. 85, 2485-2502.
    • (2004) J. Gen. Virol. , vol.85 , pp. 2485-2502
    • Macdonald, A.1    Harris, M.2
  • 36
    • 1642441710 scopus 로고    scopus 로고
    • Two-step affinity purification of the hepatitis C virus ribonucleoprotein complex
    • Waris G., Sarker S., Siddiqui A. 2004. Two-step affinity purification of the hepatitis C virus ribonucleoprotein complex. RNA. 10, 321-329.
    • (2004) RNA. , vol.10 , pp. 321-329
    • Waris, G.1    Sarker, S.2    Siddiqui, A.3
  • 38
    • 0035859871 scopus 로고    scopus 로고
    • Human hepatitis C virus NS5A protein alters intracellular calcium levels, induces oxidative stress, and activates STAT-3 and NF-kappa B
    • Gong G., Waris G., Tanveer R., Siddiqui A. 2001. Human hepatitis C virus NS5A protein alters intracellular calcium levels, induces oxidative stress, and activates STAT-3 and NF-kappa B. Proc. Natl. Acad. Sci. U. S. A. 98, 9599-5604.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 9599-5604
    • Gong, G.1    Waris, G.2    Tanveer, R.3    Siddiqui, A.4
  • 39
    • 0242422098 scopus 로고    scopus 로고
    • Expression of hepatitis C virus proteins interferes with the antiviral action of interferon independently of PKR-mediated control of protein synthesis
    • Francois C., Duverlie G., Rebouillat D., Khorsi H., Castelain S., Blum H. E., Gatignol A., Wychowski C., Moradpour D., Meurs E. F. 2000. Expression of hepatitis C virus proteins interferes with the antiviral action of interferon independently of PKR-mediated control of protein synthesis. J. Virol. 74, 5587-5596.
    • (2000) J. Virol. , vol.74 , pp. 5587-5596
    • Francois, C.1    Duverlie, G.2    Rebouillat, D.3    Khorsi, H.4    Castelain, S.5    Blum, H.E.6    Gatignol, A.7    Wychowski, C.8    Moradpour, D.9    Meurs, E.F.10
  • 40
    • 1842289764 scopus 로고    scopus 로고
    • Biochemical properties of hepatitis C virus NS5B RNA-dependent RNA polymerase and identification of amino acid sequence motifs essential for enzymatic activity
    • Lohmann V., Korner F., Herian U., Bartenschlager R. 1997. Biochemical properties of hepatitis C virus NS5B RNA-dependent RNA polymerase and identification of amino acid sequence motifs essential for enzymatic activity. J. Virol. 71, 8416-8428.
    • (1997) J. Virol. , vol.71 , pp. 8416-8428
    • Lohmann, V.1    Korner, F.2    Herian, U.3    Bartenschlager, R.4
  • 42
    • 77951970555 scopus 로고    scopus 로고
    • Potential roles for cellular cofactors in hepatitis C virus replication complex formation
    • Berger K. L., Randall G. 2009. Potential roles for cellular cofactors in hepatitis C virus replication complex formation. Commun. Integr. Biol. 2, 471-473.
    • (2009) Commun. Integr. Biol. , vol.2 , pp. 471-473
    • Berger, K.L.1    Randall, G.2
  • 43
    • 0347457077 scopus 로고    scopus 로고
    • Modulation of the hepatitis C virus RNA-dependent RNA polymerase activity by the non-structural (NS) 3 helicase and the NS4B membrane protein
    • Piccininni S., Varaklioti A., Nardelli M., Dave B., Raney K. D., McCarthy J. E. 2002. Modulation of the hepatitis C virus RNA-dependent RNA polymerase activity by the non-structural (NS) 3 helicase and the NS4B membrane protein. J. Biol. Chem. 277, 45670-45679.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45670-45679
    • Piccininni, S.1    Varaklioti, A.2    Nardelli, M.3    Dave, B.4    Raney, K.D.5    McCarthy, J.E.6
  • 45
    • 77954350897 scopus 로고    scopus 로고
    • Animal models for hepatitis C and related liver disease
    • Koike K., Moriya K., Matsuura Y. 2010. Animal models for hepatitis C and related liver disease. Hepatol. Res. 40, 69-82.
    • (2010) Hepatol. Res. , vol.40 , pp. 69-82
    • Koike, K.1    Moriya, K.2    Matsuura, Y.3
  • 47
    • 44649093803 scopus 로고    scopus 로고
    • Mouse models for the study of HCV infection and virus-host interactions
    • Barth H., Robinet E., Liang T. J., Baumert T. F. 2008. Mouse models for the study of HCV infection and virus-host interactions. J. Hepatol. 49, 134-142.
    • (2008) J. Hepatol. , vol.49 , pp. 134-142
    • Barth, H.1    Robinet, E.2    Liang, T.J.3    Baumert, T.F.4
  • 48
    • 0024509701 scopus 로고
    • Isolation of a cDNA clone derived from a blood-borne non-A, non-B viral hepatitis genome
    • Choo Q. L., Kuo G., Weiner A. J., Overby L. R., Bradley D. W., Houghton M. 1989. Isolation of a cDNA clone derived from a blood-borne non-A, non-B viral hepatitis genome. Science. 244, 359-362.
    • (1989) Science , vol.244 , pp. 359-362
    • Choo, Q.L.1    Kuo, G.2    Weiner, A.J.3    Overby, L.R.4    Bradley, D.W.5    Houghton, M.6
  • 50
    • 0037370622 scopus 로고    scopus 로고
    • Efficient replication of hepatitis C virus genotype 1a RNAs in cell culture
    • Blight K. J., McKeating J. A., Marcotrigiano J., Rice C. M. 2003. Efficient replication of hepatitis C virus genotype 1a RNAs in cell culture. J. Virol. 77, 3181-3190.
    • (2003) J. Virol. , vol.77 , pp. 3181-3190
    • Blight, K.J.1    McKeating, J.A.2    Marcotrigiano, J.3    Rice, C.M.4
  • 51
    • 0344443242 scopus 로고    scopus 로고
    • Replication of the hepatitis C virus in cell culture
    • Bartenschlager R., Kaul A., Sparacio S. 2003. Replication of the hepatitis C virus in cell culture. Antiviral Res. 60, 91-102.
    • (2003) Antiviral Res. , vol.60 , pp. 91-102
    • Bartenschlager, R.1    Kaul, A.2    Sparacio, S.3
  • 56
    • 0034785349 scopus 로고    scopus 로고
    • The benefits and hazards of antioxidants: Controlling apoptosis and other protective mechanisms in cancer patients and the human population
    • Salganik R. I. 2001. The benefits and hazards of antioxidants: Controlling apoptosis and other protective mechanisms in cancer patients and the human population. J. Am. Coll. Nutr. 20, 464S-472S.
    • (2001) J. Am. Coll. Nutr. , vol.20
    • Salganik, R.I.1
  • 58
    • 0030809576 scopus 로고    scopus 로고
    • Reactive oxygen species, mitochondria, apoptosis and aging
    • Papa S., Skulachev V. P. 1997. Reactive oxygen species, mitochondria, apoptosis and aging. Mol. Cell. Biochem. 174, 305-319.
    • (1997) Mol. Cell. Biochem. , vol.174 , pp. 305-319
    • Papa, S.1    Skulachev, V.P.2
  • 59
    • 2342514015 scopus 로고    scopus 로고
    • An important role of Nrf2-ARE pathway in the cellular defense mechanism
    • Lee J. M., Johnson J. A. 2004. An important role of Nrf2-ARE pathway in the cellular defense mechanism. J. Biochem. Mol. Biol. 37, 139-143.
    • (2004) J. Biochem. Mol. Biol. , vol.37 , pp. 139-143
    • Lee, J.M.1    Johnson, J.A.2
  • 60
    • 34250359779 scopus 로고    scopus 로고
    • Emerging role of Nrf2 in protecting against hepatic and gastrointestinal disease
    • Aleksunes L. M., Manautou J. E. 2007. Emerging role of Nrf2 in protecting against hepatic and gastrointestinal disease. Toxicol. Pathol. 35, 459-473.
    • (2007) Toxicol. Pathol. , vol.35 , pp. 459-473
    • Aleksunes, L.M.1    Manautou, J.E.2
  • 61
    • 0034685897 scopus 로고    scopus 로고
    • Transcriptional regulation of the antioxidant response element. Activation by Nrf2 and repression by MafK
    • Nguyen T., Huang H. C., Pickett C. B. 2000. Transcriptional regulation of the antioxidant response element. Activation by Nrf2 and repression by MafK. J. Biol. Chem. 275, 15466-15473.
    • (2000) J. Biol. Chem. , vol.275 , pp. 15466-15473
    • Nguyen, T.1    Huang, H.C.2    Pickett, C.B.3
  • 62
    • 36749013169 scopus 로고    scopus 로고
    • The NHB1 (N-terminal homology box 1) sequence in transcription factor Nrf1 is required to anchor it to the endoplasmic reticulum and also to enable its asparagine-glycosylation
    • Zhang Y., Lucocq J. M., Yamamoto M., Hayes J. D. 2007. The NHB1 (N-terminal homology box 1) sequence in transcription factor Nrf1 is required to anchor it to the endoplasmic reticulum and also to enable its asparagine-glycosylation. Biochem. J. 408, 161-172.
    • (2007) Biochem. J. , vol.408 , pp. 161-172
    • Zhang, Y.1    Lucocq, J.M.2    Yamamoto, M.3    Hayes, J.D.4
  • 63
    • 33745807575 scopus 로고    scopus 로고
    • Nrf1 is targeted to the endoplasmic reticulum membrane by an N-terminal transmembrane domain. Inhibition of nuclear translocation and transacting function
    • Wang W., Chan J. Y. 2006. Nrf1 is targeted to the endoplasmic reticulum membrane by an N-terminal transmembrane domain. Inhibition of nuclear translocation and transacting function. J. Biol. Chem. 281, 19676-19687.
    • (2006) J. Biol. Chem. , vol.281 , pp. 19676-19687
    • Wang, W.1    Chan, J.Y.2
  • 64
    • 61449180332 scopus 로고    scopus 로고
    • The Nrf1 CNC/bZIP protein is a nuclear envelope-bound transcription factor that is activated by t-butyl hydroquinone but not by endoplasmic reticulum stressors
    • Zhang Y., Lucocq J. M., Hayes J. D. 2009. The Nrf1 CNC/bZIP protein is a nuclear envelope-bound transcription factor that is activated by t-butyl hydroquinone but not by endoplasmic reticulum stressors. Biochem. J. 418, 293-310.
    • (2009) Biochem. J. , vol.418 , pp. 293-310
    • Zhang, Y.1    Lucocq, J.M.2    Hayes, J.D.3
  • 65
    • 77958115724 scopus 로고    scopus 로고
    • Regulation of the Nrf2-Keap1 antioxidant response by the ubiquitin proteasome system: An insight into cullin-ring ubiquitin ligases
    • doi: 10. 1089/ars. 2010. 3211
    • Villeneuve N. F., Lau A., Zhang D. D. 2010. Regulation of the Nrf2-Keap1 antioxidant response by the ubiquitin proteasome system: An insight into cullin-ring ubiquitin ligases. Antioxid. Redox Signal. doi: 10. 1089/ars. 2010. 3211.
    • (2010) Antioxid. Redox Signal.
    • Villeneuve, N.F.1    Lau, A.2    Zhang, D.D.3
  • 66
    • 57749120460 scopus 로고    scopus 로고
    • Nrf1 and Nrf2 play distinct roles in activation of antioxidant response element-dependent genes
    • Ohtsuji M., Katsuoka F., Kobayashi A., Aburatani H., Hayes J. D., Yamamoto M. 2008. Nrf1 and Nrf2 play distinct roles in activation of antioxidant response element-dependent genes. J. Biol. Chem. 283, 33554-33562.
    • (2008) J. Biol. Chem. , vol.283 , pp. 33554-33562
    • Ohtsuji, M.1    Katsuoka, F.2    Kobayashi, A.3    Aburatani, H.4    Hayes, J.D.5    Yamamoto, M.6
  • 67
    • 0032536783 scopus 로고    scopus 로고
    • Targeted disruption of the ubiquitous CNC-bZIP transcription factor, Nrf-1, results in anemia and embryonic lethality in mice
    • Chan J. Y., Kwong M., Lu R., Chang J., Wang B., Yen T. S., Kan Y. W. 1998. Targeted disruption of the ubiquitous CNC-bZIP transcription factor, Nrf-1, results in anemia and embryonic lethality in mice. EMBO J. 17, 1779-1787.
    • (1998) EMBO J. , vol.17 , pp. 1779-1787
    • Chan, J.Y.1    Kwong, M.2    Lu, R.3    Chang, J.4    Wang, B.5    Yen, T.S.6    Kan, Y.W.7
  • 69
    • 0034704137 scopus 로고    scopus 로고
    • Small maf (MafG and MafK) proteins negatively regulate antioxidant response element-mediated expression and antioxidant induction of the NAD(P)H:Quinone oxidoreductase1 gene
    • Dhakshinamoorthy S., Jaiswal A. K. 2000. Small maf (MafG and MafK) proteins negatively regulate antioxidant response element-mediated expression and antioxidant induction of the NAD(P)H: Quinone oxidoreductase1 gene. J. Biol. Chem. 275, 40134-40141.
    • (2000) J. Biol. Chem. , vol.275 , pp. 40134-40141
    • Dhakshinamoorthy, S.1    Jaiswal, A.K.2
  • 70
    • 2342511435 scopus 로고    scopus 로고
    • Small Maf proteins serve as transcriptional cofactors for keratinocyte differentiation in the Keap1-Nrf2 regulatory pathway
    • Motohashi H., Katsuoka F., Engel J. D., Yamamoto M. 2004. Small Maf proteins serve as transcriptional cofactors for keratinocyte differentiation in the Keap1-Nrf2 regulatory pathway. Proc. Natl. Acad. Sci. U. S. A. 101, 6379-6384.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 6379-6384
    • Motohashi, H.1    Katsuoka, F.2    Engel, J.D.3    Yamamoto, M.4
  • 71
    • 1642282736 scopus 로고    scopus 로고
    • Cellular mechanisms of redox cell signalling: role of cysteine modification in controlling antioxidant defences in response to electrophilic lipid oxidation products
    • Levonen A. L., Landar A., Ramachandran A., Ceaser E. K., Dickinson D. A., Zanoni G., Morrow J. D., Darley-Usmar V. M. 2004. Cellular mechanisms of redox cell signalling: role of cysteine modification in controlling antioxidant defences in response to electrophilic lipid oxidation products. Biochem. J. 378, 373-382.
    • (2004) Biochem. J. , vol.378 , pp. 373-382
    • Levonen, A.L.1    Landar, A.2    Ramachandran, A.3    Ceaser, E.K.4    Dickinson, D.A.5    Zanoni, G.6    Morrow, J.D.7    Darley-Usmar, V.M.8
  • 72
    • 1942520367 scopus 로고    scopus 로고
    • Nrf2 signaling in coordinated activation of antioxidant gene expression
    • Jaiswal A. K. 2004. Nrf2 signaling in coordinated activation of antioxidant gene expression. Free Radic. Biol. Med. 36, 1199-1207.
    • (2004) Free Radic. Biol. Med. , vol.36 , pp. 1199-1207
    • Jaiswal, A.K.1
  • 73
    • 66349129338 scopus 로고    scopus 로고
    • Acetylation of Nrf2 by p300/CBP augments promoter-specific DNA binding of Nrf2 during the antioxidant response
    • Sun Z., Chin Y. E., Zhang D. D. 2009. Acetylation of Nrf2 by p300/CBP augments promoter-specific DNA binding of Nrf2 during the antioxidant response. Mol. Cell Biol. 29, 2658-2672.
    • (2009) Mol. Cell Biol. , vol.29 , pp. 2658-2672
    • Sun, Z.1    Chin, Y.E.2    Zhang, D.D.3
  • 74
    • 77956282020 scopus 로고    scopus 로고
    • Redox-dependent signaling system Nrf2/ARE in inflammation
    • Menshikova E. B., Tkachev V. O., Zenkov N. K. 2010. Redox-dependent signaling system Nrf2/ARE in inflammation. Mol. Biol. (Moscow). 44, 343-357.
    • (2010) Mol. Biol. (Moscow). , vol.44 , pp. 343-357
    • Menshikova, E.B.1    Tkachev, V.O.2    Zenkov, N.K.3
  • 75
    • 0032128150 scopus 로고    scopus 로고
    • Assembly, sorting, and exit of oligomeric proteins from the endoplasmic reticulum
    • Reddy P. S., Corley R. B. 1998. Assembly, sorting, and exit of oligomeric proteins from the endoplasmic reticulum. BioEssays. 20, 546-554.
    • (1998) BioEssays. , vol.20 , pp. 546-554
    • Reddy, P.S.1    Corley, R.B.2
  • 76
    • 35848957485 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and oxidative stress: A vicious cycle or a double-edged sword?
    • Malhotra J. D., Kaufman R. J. 2007. Endoplasmic reticulum stress and oxidative stress: A vicious cycle or a double-edged sword? Antioxid. Redox Signal. 9, 2277-2293.
    • (2007) Antioxid. Redox Signal. , vol.9 , pp. 2277-2293
    • Malhotra, J.D.1    Kaufman, R.J.2
  • 77
    • 34047192683 scopus 로고    scopus 로고
    • Review. The endoplasmic reticulum: A target for new anticancer drugs
    • Boelens J., Lust S., Offner F., Bracke M. E., Vanhoecke B. W. 2007. Review. The endoplasmic reticulum: A target for new anticancer drugs. In Vivo. 21, 215-226.
    • (2007) In Vivo. , vol.21 , pp. 215-226
    • Boelens, J.1    Lust, S.2    Offner, F.3    Bracke, M.E.4    Vanhoecke, B.W.5
  • 78
    • 0042691414 scopus 로고    scopus 로고
    • Unfolding the toxicity of cholesterol
    • Zhang K., Kaufman R. J. 2003. Unfolding the toxicity of cholesterol. Nature Cell Biol. 5, 769-770.
    • (2003) Nature Cell Biol. , vol.5 , pp. 769-770
    • Zhang, K.1    Kaufman, R.J.2
  • 79
    • 0035966320 scopus 로고    scopus 로고
    • The unfolding tale of the unfolded protein response
    • Ma Y., Hendershot L. M. 2001. The unfolding tale of the unfolded protein response. Cell. 107, 827-830.
    • (2001) Cell. , vol.107 , pp. 827-830
    • Ma, Y.1    Hendershot, L.M.2
  • 80
    • 0010625474 scopus 로고
    • Glucose depletion accounts for the induction of two transformation-sensitive membrane proteins in Rous sarcoma virus-transformed chick embryo fibroblasts
    • Shiu R. P., Pouyssegur J., Pastan I. 1977. Glucose depletion accounts for the induction of two transformation-sensitive membrane proteins in Rous sarcoma virus-transformed chick embryo fibroblasts. Proc. Natl. Acad. Sci. U. S. A. 74, 3840-3844.
    • (1977) Proc. Natl. Acad. Sci. U.S.A. , vol.74 , pp. 3840-3844
    • Shiu, R.P.1    Pouyssegur, J.2    Pastan, I.3
  • 81
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething M. J., Sambrook J. 1992. Protein folding in the cell. Nature. 355, 33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 82
    • 10444226462 scopus 로고    scopus 로고
    • ER stress and the unfolded protein response
    • Schroder M., Kaufman R. J. 2005. ER stress and the unfolded protein response. Mutat. Res. 569, 29-63.
    • (2005) Mutat. Res. , vol.569 , pp. 29-63
    • Schroder, M.1    Kaufman, R.J.2
  • 83
    • 0030053047 scopus 로고    scopus 로고
    • Activation of transcription factor NF-kappaB by the adenovirus E3/19K protein requires its ER retention
    • Pahl H. L., Sester M., Burgert H. G., Baeuerle P. A. 1996. Activation of transcription factor NF-kappaB by the adenovirus E3/19K protein requires its ER retention. J. Cell Biol. 132, 511-522.
    • (1996) J. Cell Biol. , vol.132 , pp. 511-522
    • Pahl, H.L.1    Sester, M.2    Burgert, H.G.3    Baeuerle, P.A.4
  • 84
    • 0029001576 scopus 로고
    • A novel signal transduction pathway from the endoplasmic reticulum to the nucleus is mediated by transcription factor NF-kappa B
    • Pahl H. L., Baeuerle P. A. 1995. A novel signal transduction pathway from the endoplasmic reticulum to the nucleus is mediated by transcription factor NF-kappa B. EMBO J. 14, 2580-2588.
    • (1995) EMBO J. , vol.14 , pp. 2580-2588
    • Pahl, H.L.1    Baeuerle, P.A.2
  • 85
    • 77951290227 scopus 로고    scopus 로고
    • TLR activation of the transcription factor XBP1 regulates innate immune responses in macrophages
    • Martinon F., Chen X., Lee A. H., Glimcher L. H. 2010. TLR activation of the transcription factor XBP1 regulates innate immune responses in macrophages. Nature Immunol. 11, 411-418.
    • (2010) Nature Immunol. , vol.11 , pp. 411-418
    • Martinon, F.1    Chen, X.2    Lee, A.H.3    Glimcher, L.H.4
  • 86
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmicreticulum-resident kinase
    • Harding H. P., Zhang Y., Ron D. 1999. Protein translation and folding are coupled by an endoplasmicreticulum-resident kinase. Nature. 397, 271-274.
    • (1999) Nature. , vol.397 , pp. 271-274
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 87
    • 0031755020 scopus 로고    scopus 로고
    • Identification and characterization of pancreatic eukaryotic initiation factor 2 alpha-subunit kinase, PEK, involved in translational control
    • Shi Y., Vattem K. M., Sood R., An J., Liang J., Stramm L., Wek R. C. 1998. Identification and characterization of pancreatic eukaryotic initiation factor 2 alpha-subunit kinase, PEK, involved in translational control. Mol. Cell Biol. 18, 7499-7509.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 7499-7509
    • Shi, Y.1    Vattem, K.M.2    Sood, R.3    An, J.4    Liang, J.5    Stramm, L.6    Wek, R.C.7
  • 88
    • 0033782015 scopus 로고    scopus 로고
    • Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response
    • Bertolotti A., Zhang Y., Hendershot L. M., Harding H. P., Ron D. 2000. Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response. Nature Cell Biol. 2, 326-332.
    • (2000) Nature Cell Biol. , vol.2 , pp. 326-332
    • Bertolotti, A.1    Zhang, Y.2    Hendershot, L.M.3    Harding, H.P.4    Ron, D.5
  • 89
    • 0036713724 scopus 로고    scopus 로고
    • Distinct roles of activating transcription factor 6 (ATF6) and double-stranded RNA-activated protein kinase-like endoplasmic reticulum kinase (PERK) in transcription during the mammalian unfolded protein response
    • Okada T., Yoshida H., Akazawa R., Negishi M., Mori K. 2002. Distinct roles of activating transcription factor 6 (ATF6) and double-stranded RNA-activated protein kinase-like endoplasmic reticulum kinase (PERK) in transcription during the mammalian unfolded protein response. Biochem. J. 366, 585-594.
    • (2002) Biochem. J. , vol.366 , pp. 585-594
    • Okada, T.1    Yoshida, H.2    Akazawa, R.3    Negishi, M.4    Mori, K.5
  • 90
    • 0033634654 scopus 로고    scopus 로고
    • Regulated translation initiation controls stress-induced gene expression in mammalian cells
    • Harding H. P., Novoa I., Zhang Y., Zeng H., Wek R., Schapira M., Ron D. 2000. Regulated translation initiation controls stress-induced gene expression in mammalian cells. Mol. Cell. 6, 1099-1108.
    • (2000) Mol. Cell. , vol.6 , pp. 1099-1108
    • Harding, H.P.1    Novoa, I.2    Zhang, Y.3    Zeng, H.4    Wek, R.5    Schapira, M.6    Ron, D.7
  • 91
    • 3843117589 scopus 로고    scopus 로고
    • Reinitiation involving upstream ORFs regulates ATF4 mRNA translation in mammalian cells
    • Vattem K. M., Wek R. C. 2004. Reinitiation involving upstream ORFs regulates ATF4 mRNA translation in mammalian cells. Proc. Natl. Acad. Sci. U. S. A. 101, 11269-11274.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 11269-11274
    • Vattem, K.M.1    Wek, R.C.2
  • 92
    • 2442542312 scopus 로고    scopus 로고
    • PERK-dependent activation of Nrf2 contributes to redox homeostasis and cell survival following endoplasmic reticulum stress
    • Cullinan S. B., Diehl J. A. 2004. PERK-dependent activation of Nrf2 contributes to redox homeostasis and cell survival following endoplasmic reticulum stress. J. Biol. Chem. 279, 20108-20117.
    • (2004) J. Biol. Chem. , vol.279 , pp. 20108-20117
    • Cullinan, S.B.1    Diehl, J.A.2
  • 93
    • 0036314984 scopus 로고    scopus 로고
    • Two distinct stress signaling pathways converge upon the CHOP promoter during the mammalian unfolded protein response
    • Ma Y., Brewer J. W., Diehl J. A., Hendershot L. M. 2002. Two distinct stress signaling pathways converge upon the CHOP promoter during the mammalian unfolded protein response. J. Mol. Biol. 318, 1351-1365.
    • (2002) J. Mol. Biol. , vol.318 , pp. 1351-1365
    • Ma, Y.1    Brewer, J.W.2    Diehl, J.A.3    Hendershot, L.M.4
  • 94
    • 1642442467 scopus 로고    scopus 로고
    • Underglycosylation of ATF6 as a novel sensing mechanism for activation of the unfolded protein response
    • Hong M., Luo S., Baumeister P., Huang J. M., Gogia R. K., Li M., Lee A. S. 2004. Underglycosylation of ATF6 as a novel sensing mechanism for activation of the unfolded protein response. J. Biol. Chem. 279, 11354-11363.
    • (2004) J. Biol. Chem. , vol.279 , pp. 11354-11363
    • Hong, M.1    Luo, S.2    Baumeister, P.3    Huang, J.M.4    Gogia, R.K.5    Li, M.6    Lee, A.S.7
  • 95
    • 0033815971 scopus 로고    scopus 로고
    • ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response
    • Yoshida H., Okada T., Haze K., Yanagi H., Yura T., Negishi M., Mori K. 2000. ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response. Mol. Cell Biol. 20, 6755-6767.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 6755-6767
    • Yoshida, H.1    Okada, T.2    Haze, K.3    Yanagi, H.4    Yura, T.5    Negishi, M.6    Mori, K.7
  • 96
    • 0035966269 scopus 로고    scopus 로고
    • XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor
    • Yoshida H., Matsui T., Yamamoto A., Okada T., Mori K. 2001. XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell. 107, 881-891.
    • (2001) Cell. , vol.107 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 98
    • 0032509216 scopus 로고    scopus 로고
    • Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors
    • Yoshida H., Haze K., Yanagi H., Yura T., Mori K. 1998. Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors. J. Biol. Chem. 273, 33741-33749.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33741-33749
    • Yoshida, H.1    Haze, K.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 99
    • 0035937721 scopus 로고    scopus 로고
    • Identification of ERSE-II, a new cis-acting element responsible for the ATF6-dependent mammalian unfolded protein response
    • Kokame K., Kato H., Miyata T. 2001. Identification of ERSE-II, a new cis-acting element responsible for the ATF6-dependent mammalian unfolded protein response. J. Biol. Chem. 276, 9199-9205.
    • (2001) J. Biol. Chem. , vol.276 , pp. 9199-9205
    • Kokame, K.1    Kato, H.2    Miyata, T.3
  • 100
    • 35348951126 scopus 로고    scopus 로고
    • How transmembrane proteins sense endoplasmic reticulum stress
    • Kohno K. 2007. How transmembrane proteins sense endoplasmic reticulum stress. Antioxid. Redox Signal. 9, 2295-2303.
    • (2007) Antioxid. Redox Signal. , vol.9 , pp. 2295-2303
    • Kohno, K.1
  • 101
    • 0034637605 scopus 로고    scopus 로고
    • Ligandindependent dimerization activates the stress response kinases IRE1 and PERK in the lumen of the endoplasmic reticulum
    • Liu C. Y., Schroder M., Kaufman R. J. 2000. Ligandindependent dimerization activates the stress response kinases IRE1 and PERK in the lumen of the endoplasmic reticulum. J. Biol. Chem. 275, 24881-24885.
    • (2000) J. Biol. Chem. , vol.275 , pp. 24881-24885
    • Liu, C.Y.1    Schroder, M.2    Kaufman, R.J.3
  • 103
  • 104
    • 0037083755 scopus 로고    scopus 로고
    • IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response
    • Lee K., Tirasophon W., Shen X., Michalak M., Prywes R., Okada T., Yoshida H., Mori K., Kaufman R. J. 2002. IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response. Genes Dev. 16, 452-466.
    • (2002) Genes Dev. , vol.16 , pp. 452-466
    • Lee, K.1    Tirasophon, W.2    Shen, X.3    Michalak, M.4    Prywes, R.5    Okada, T.6    Yoshida, H.7    Mori, K.8    Kaufman, R.J.9
  • 105
    • 9144228073 scopus 로고    scopus 로고
    • Differential contributions of ATF6 and XBP1 to the activation of endoplasmic reticulum stress-responsive cis-acting elements ERSE, UPRE and ERSE-II
    • Yamamoto K., Yoshida H., Kokame K., Kaufman R. J., Mori K. 2004. Differential contributions of ATF6 and XBP1 to the activation of endoplasmic reticulum stress-responsive cis-acting elements ERSE, UPRE and ERSE-II. J. Biochem. 136, 343-350.
    • (2004) J. Biochem. , vol.136 , pp. 343-350
    • Yamamoto, K.1    Yoshida, H.2    Kokame, K.3    Kaufman, R.J.4    Mori, K.5
  • 106
    • 0142059951 scopus 로고    scopus 로고
    • XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response
    • Lee A. H., Iwakoshi N. N., Glimcher L. H. 2003. XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response. Mol. Cell Biol. 23, 7448-7459.
    • (2003) Mol. Cell Biol. , vol.23 , pp. 7448-7459
    • Lee, A.H.1    Iwakoshi, N.N.2    Glimcher, L.H.3
  • 107
    • 0034632033 scopus 로고    scopus 로고
    • The unfolded protein response regulates multiple aspects of secretory and membrane protein biogenesis and endoplasmic reticulum quality control
    • Ng D. T., Spear E. D., Walter P. 2000. The unfolded protein response regulates multiple aspects of secretory and membrane protein biogenesis and endoplasmic reticulum quality control. J. Cell Biol. 150, 77-88.
    • (2000) J. Cell Biol. , vol.150 , pp. 77-88
    • Ng, D.T.1    Spear, E.D.2    Walter, P.3
  • 109
    • 0037058574 scopus 로고    scopus 로고
    • Control of PERK eIF2alpha kinase activity by the endoplasmic reticulum stress-induced molecular chaperone P58IPK
    • Yan W., Frank C. L., Korth M. J., Sopher B. L., Novoa I., Ron D., Katze M. G. 2002. Control of PERK eIF2alpha kinase activity by the endoplasmic reticulum stress-induced molecular chaperone P58IPK. Proc. Natl. Acad. Sci. U. S. A. 99, 15920-15925.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 15920-15925
    • Yan, W.1    Frank, C.L.2    Korth, M.J.3    Sopher, B.L.4    Novoa, I.5    Ron, D.6    Katze, M.G.7
  • 111
    • 0343924357 scopus 로고    scopus 로고
    • Evidence that hepatitis C virus resistance to interferon is mediated through repression of the PKR protein kinase by the nonstructural 5A protein
    • Gale M. J., Jr., Korth M. J., Tang N. M., Tan S. L., Hopkins D. A., Dever T. E., Polyak S. J., Gretch D. R., Katze M. G. 1997. Evidence that hepatitis C virus resistance to interferon is mediated through repression of the PKR protein kinase by the nonstructural 5A protein. Virology. 230, 217-227.
    • (1997) Virology. , vol.230 , pp. 217-227
    • Gale Jr., M.J.1    Korth, M.J.2    Tang, N.M.3    Tan, S.L.4    Hopkins, D.A.5    Dever, T.E.6    Polyak, S.J.7    Gretch, D.R.8    Katze, M.G.9
  • 112
    • 0033516497 scopus 로고    scopus 로고
    • Inhibition of the interferon-inducible protein kinase PKR by HCV E2 protein
    • Taylor D. R., Shi S. T., Romano P. R., Barber G. N., Lai M. M. 1999. Inhibition of the interferon-inducible protein kinase PKR by HCV E2 protein. Science. 285, 107-110.
    • (1999) Science , vol.285 , pp. 107-110
    • Taylor, D.R.1    Shi, S.T.2    Romano, P.R.3    Barber, G.N.4    Lai, M.M.5
  • 113
    • 0037333913 scopus 로고    scopus 로고
    • Protein synthesis and endoplasmic reticulum stress can be modulated by the hepatitis C virus envelope protein E2 through the eukaryotic initiation factor 2-alpha kinase PERK
    • Pavio N., Romano P. R., Graczyk T. M., Feinstone S. M., Taylor D. R. 2003. Protein synthesis and endoplasmic reticulum stress can be modulated by the hepatitis C virus envelope protein E2 through the eukaryotic initiation factor 2-alpha kinase PERK. J. Virol. 77, 3578-3585.
    • (2003) J. Virol. , vol.77 , pp. 3578-3585
    • Pavio, N.1    Romano, P.R.2    Graczyk, T.M.3    Feinstone, S.M.4    Taylor, D.R.5
  • 114
    • 2342435179 scopus 로고    scopus 로고
    • Hepatitis C virus suppresses the IRE1-XBP1 pathway of the unfolded protein response
    • Tardif K. D., Mori K., Kaufman R. J., Siddiqui A. 2004. Hepatitis C virus suppresses the IRE1-XBP1 pathway of the unfolded protein response. J. Biol. Chem. 279, 17158-17164.
    • (2004) J. Biol. Chem. , vol.279 , pp. 17158-17164
    • Tardif, K.D.1    Mori, K.2    Kaufman, R.J.3    Siddiqui, A.4
  • 115
    • 0033562966 scopus 로고    scopus 로고
    • Stress signaling from the lumen of the endoplasmic reticulum: Coordination of gene transcriptional and translational controls
    • Kaufman R. J. 1999. Stress signaling from the lumen of the endoplasmic reticulum: Coordination of gene transcriptional and translational controls. Genes Dev. 13, 1211-1233.
    • (1999) Genes Dev. , vol.13 , pp. 1211-1233
    • Kaufman, R.J.1
  • 116
    • 0142124130 scopus 로고    scopus 로고
    • Cell surface expression of major histocompatibility complex class I molecules is reduced in hepatitis C virus subgenomic repliconexpressing cells
    • Tardif K. D., Siddiqui A. 2003. Cell surface expression of major histocompatibility complex class I molecules is reduced in hepatitis C virus subgenomic repliconexpressing cells. J. Virol. 77, 11644-11650.
    • (2003) J. Virol. , vol.77 , pp. 11644-11650
    • Tardif, K.D.1    Siddiqui, A.2
  • 118
    • 0031868427 scopus 로고    scopus 로고
    • Enhanced expression of a new class of liver-enriched b-Zip transcription factors, hepatocarcinogenesis-related transcription factor, in hepatocellular carcinomas of rats and humans
    • Kishimoto T., Kokura K., Ohkawa N., Makino Y., Yoshida M., Hirohashi S., Niwa S., Muramatsu M., Tamura T. 1998. Enhanced expression of a new class of liver-enriched b-Zip transcription factors, hepatocarcinogenesis-related transcription factor, in hepatocellular carcinomas of rats and humans. Cell Growth Diff. 9, 337-344.
    • (1998) Cell Growth Diff. , vol.9 , pp. 337-344
    • Kishimoto, T.1    Kokura, K.2    Ohkawa, N.3    Makino, Y.4    Yoshida, M.5    Hirohashi, S.6    Niwa, S.7    Muramatsu, M.8    Tamura, T.9
  • 122
    • 0036165333 scopus 로고    scopus 로고
    • Mitochondrial injury, oxidative stress, and antioxidant gene expression are induced by hepatitis C virus core protein
    • Okuda M., Li K., Beard M. R., Showalter L. A., Scholle F., Lemon S. M., Weinman S. A. 2002. Mitochondrial injury, oxidative stress, and antioxidant gene expression are induced by hepatitis C virus core protein. Gastroenterology. 122, 366-375.
    • (2002) Gastroenterology. , vol.122 , pp. 366-375
    • Okuda, M.1    Li, K.2    Beard, M.R.3    Showalter, L.A.4    Scholle, F.5    Lemon, S.M.6    Weinman, S.A.7
  • 123
    • 77954236285 scopus 로고    scopus 로고
    • Hepatocyte NAD(P)H oxidases as an endogenous source of reactive oxygen species during hepatitis C virus infection
    • de Mochel N. S., Seronello S., Wang S. H., Ito C., Zheng J. X., Liang T. J., Lambeth J. D., Choi J. 2010. Hepatocyte NAD(P)H oxidases as an endogenous source of reactive oxygen species during hepatitis C virus infection. Hepatology. 52, 47-59.
    • (2010) Hepatology. , vol.52 , pp. 47-59
    • de Mochel, N.S.1    Seronello, S.2    Wang, S.H.3    Ito, C.4    Zheng, J.X.5    Liang, T.J.6    Lambeth, J.D.7    Choi, J.8
  • 124
    • 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
    • Boudreau H. E., Emerson S. U., Korzeniowska A., Jendrysik M. A., Leto T. L. 2009. 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. 83, 12934-12946.
    • (2009) J. Virol. , vol.83 , pp. 12934-12946
    • Boudreau, H.E.1    Emerson, S.U.2    Korzeniowska, A.3    Jendrysik, M.A.4    Leto, T.L.5
  • 125
    • 70349352744 scopus 로고    scopus 로고
    • Mechanisms and implications of reactive oxygen species generation during the unfolded protein response: Roles of endoplasmic reticulum oxidoreductases, mitochondrial electron transport and nadph oxidase
    • Santos C. X., Tanaka L. Y., Wosniak J. J., Laurindo F. R. 2009. Mechanisms and implications of reactive oxygen species generation during the unfolded protein response: Roles of endoplasmic reticulum oxidoreductases, mitochondrial electron transport and nadph oxidase. Antioxid. Redox Signal. 11, 2409-2427.
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 2409-2427
    • Santos, C.X.1    Tanaka, L.Y.2    Wosniak, J.J.3    Laurindo, F.R.4
  • 127
    • 40049085583 scopus 로고    scopus 로고
    • Evidence of oxidative stress as a cofactor in the development of insulin resistance in patients with chronic hepatitis C
    • Mitsuyoshi H., Itoh Y., Sumida Y., Minami M., Yasui K., Nakashima T., Okanoue T. 2008. Evidence of oxidative stress as a cofactor in the development of insulin resistance in patients with chronic hepatitis C. Hepatol. Res. 38, 348-353.
    • (2008) Hepatol. Res. , vol.38 , pp. 348-353
    • Mitsuyoshi, H.1    Itoh, Y.2    Sumida, Y.3    Minami, M.4    Yasui, K.5    Nakashima, T.6    Okanoue, T.7
  • 128
    • 33745580391 scopus 로고    scopus 로고
    • Oxidative stress inhibits IFN-alpha-induced antiviral gene expression by blocking the JAK-STAT pathway
    • Di Bona D., Cippitelli M., Fionda C., Camma C., Licata A., Santoni A., Craxi A. 2006. Oxidative stress inhibits IFN-alpha-induced antiviral gene expression by blocking the JAK-STAT pathway. J. Hepatol. 45, 271-279.
    • (2006) J. Hepatol. , vol.45 , pp. 271-279
    • Di Bona, D.1    Cippitelli, M.2    Fionda, C.3    Camma, C.4    Licata, A.5    Santoni, A.6    Craxi, A.7
  • 131
    • 22544447811 scopus 로고    scopus 로고
    • Hepatitis C virus stimulates the expression of cyclooxygenase-2 via oxidative stress: Role of prostaglandin E2 in RNA replication
    • Waris G., Siddiqui A. 2005. Hepatitis C virus stimulates the expression of cyclooxygenase-2 via oxidative stress: Role of prostaglandin E2 in RNA replication. J. Virol. 79, 9725-9734.
    • (2005) J. Virol. , vol.79 , pp. 9725-9734
    • Waris, G.1    Siddiqui, A.2
  • 132
  • 134
    • 0142039960 scopus 로고    scopus 로고
    • Hepatitis C virus NS5A and subgenomic replicon activate NF-kappaB via tyrosine phosphorylation of IkappaBalpha and its degradation by calpain protease
    • Waris G., Livolsi A., Imbert V., Peyron J. F., Siddiqui A. 2003. Hepatitis C virus NS5A and subgenomic replicon activate NF-kappaB via tyrosine phosphorylation of IkappaBalpha and its degradation by calpain protease. J. Biol. Chem. 278, 40778-40787.
    • (2003) J. Biol. Chem. , vol.278 , pp. 40778-40787
    • Waris, G.1    Livolsi, A.2    Imbert, V.3    Peyron, J.F.4    Siddiqui, A.5
  • 135
    • 76849085285 scopus 로고    scopus 로고
    • Activation of transcription factor Nrf2 by hepatitis C virus induces the cell-survival pathway
    • Burdette D., Olivarez M., Waris G. 2010. Activation of transcription factor Nrf2 by hepatitis C virus induces the cell-survival pathway. J. Gen. Virol. 91, 681-690.
    • (2010) J. Gen. Virol. , vol.91 , pp. 681-690
    • Burdette, D.1    Olivarez, M.2    Waris, G.3
  • 136
    • 33746658598 scopus 로고    scopus 로고
    • Oxidative stress and antioxidant defense in patients with chronic hepatitis C patients before and after pegylated interferon alfa-2b plus ribavirin therapy
    • Levent G., Ali A., Ahmet A., Polat E. C., Aytac C., Ayse E., Ahmet S. 2006. Oxidative stress and antioxidant defense in patients with chronic hepatitis C patients before and after pegylated interferon alfa-2b plus ribavirin therapy. J. Transl. Med. 4, 25. doi: 10. 1186/1479-5876-4-25.
    • (2006) J. Transl. Med. , vol.4 , pp. 25
    • Levent, G.1    Ali, A.2    Ahmet, A.3    Polat, E.C.4    Aytac, C.5    Ayse, E.6    Ahmet, S.7
  • 137
    • 0031088467 scopus 로고    scopus 로고
    • Reduced glutathione concentration in erythrocytes of patients with acute and chronic viral hepatitis
    • Swietek K., Juszczyk J. 1997. Reduced glutathione concentration in erythrocytes of patients with acute and chronic viral hepatitis. J. Viral Hepat. 4, 139-141.
    • (1997) J. Viral Hepat. , vol.4 , pp. 139-141
    • Swietek, K.1    Juszczyk, J.2
  • 138
    • 0029903665 scopus 로고    scopus 로고
    • Hepatic glutathione deficiency in chronic hepatitis C: Quantitative evaluation in patients who are HIV positive and HIV negative and correlations with plasmatic and lymphocytic concentrations and with the activity of the liver disease
    • Barbaro G., Di Lorenzo G., Soldini M., Parrotto S., Bellomo G., Belloni G., Grisorio B., Barbarini G. 1996. Hepatic glutathione deficiency in chronic hepatitis C: Quantitative evaluation in patients who are HIV positive and HIV negative and correlations with plasmatic and lymphocytic concentrations and with the activity of the liver disease. Am. J. Gastroenterol. 91, 2569-2573.
    • (1996) Am. J. Gastroenterol. , vol.91 , pp. 2569-2573
    • Barbaro, G.1    Di Lorenzo, G.2    Soldini, M.3    Parrotto, S.4    Bellomo, G.5    Belloni, G.6    Grisorio, B.7    Barbarini, G.8


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