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Volumn 1787, Issue 5, 2009, Pages 539-546

HCV infection induces mitochondrial bioenergetic unbalance: Causes and effects

Author keywords

Ca2+ homeostasis; Hepatitis C virus; Mitochondria; Redox signaling

Indexed keywords

CALCIUM ION; DANTROLENE; HYPOXIA INDUCIBLE FACTOR; NITROGEN; REACTIVE OXYGEN METABOLITE; RUTHENIUM RED;

EID: 67349286520     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2008.11.008     Document Type: Review
Times cited : (63)

References (71)
  • 1
    • 23944506014 scopus 로고    scopus 로고
    • Global epidemiology of hepatitis C virus infection
    • Shepard C.W., Finelli L., and Alter M.J. Global epidemiology of hepatitis C virus infection. Lancet Infect. Dis. 5 (2005) 558-567
    • (2005) Lancet Infect. Dis. , vol.5 , pp. 558-567
    • Shepard, C.W.1    Finelli, L.2    Alter, M.J.3
  • 3
    • 16244405250 scopus 로고    scopus 로고
    • Hepatitis C virus, ER stress, and oxidative stress
    • Tardif K.D., Waris G., and Siddiqui A. Hepatitis C virus, ER stress, and oxidative stress. Trends Microbiol. 13 (2005) 159-163
    • (2005) Trends Microbiol. , vol.13 , pp. 159-163
    • Tardif, K.D.1    Waris, G.2    Siddiqui, A.3
  • 5
    • 34547415672 scopus 로고    scopus 로고
    • Hepatitis C virus protein expression causes calcium-mediated mitochondrial bioenergetic dysfunction and nitro-oxidative stress
    • Piccoli C., Scrima R., Quarato G., D'Aprile A., Ripoli M., Lecce L., Boffoli D., Moradpour D., and Capitanio N. Hepatitis C virus protein expression causes calcium-mediated mitochondrial bioenergetic dysfunction and nitro-oxidative stress. Hepatology 46 (2007) 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
  • 6
    • 33747600880 scopus 로고    scopus 로고
    • Causes and consequences of mitochondrial reactive oxygen species generation in hepatitis C
    • Wang T., and Weinman S.A. Causes and consequences of mitochondrial reactive oxygen species generation in hepatitis C. J. Gastroenterol. Hepatol. 21 Suppl 3 (2006) S34-37
    • (2006) J. Gastroenterol. Hepatol. , vol.21 , Issue.SUPPL. 3
    • Wang, T.1    Weinman, S.A.2
  • 8
    • 23844558266 scopus 로고    scopus 로고
    • A mitochondrial paradigm of metabolic and degenerative diseases, aging, and cancer: a dawn for evolutionary medicine
    • Wallace D.C. A mitochondrial paradigm of metabolic and degenerative diseases, aging, and cancer: a dawn for evolutionary medicine. Annu. Rev. Genet. 39 (2005) 359-407
    • (2005) Annu. Rev. Genet. , vol.39 , pp. 359-407
    • Wallace, D.C.1
  • 9
    • 0033525924 scopus 로고    scopus 로고
    • Oxidative phosphorylation at the fin de siecle
    • Saraste M. Oxidative phosphorylation at the fin de siecle. Science 283 (1999) 1488-1493
    • (1999) Science , vol.283 , pp. 1488-1493
    • Saraste, M.1
  • 11
    • 27144440476 scopus 로고    scopus 로고
    • Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus
    • Meylan E., Curran J., Hofmann K., Moradpour D., Binder M., Bartenschlager R., and Tschopp J. Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus. Nature 437 (2005) 1167-1172
    • (2005) Nature , vol.437 , pp. 1167-1172
    • Meylan, E.1    Curran, J.2    Hofmann, K.3    Moradpour, D.4    Binder, M.5    Bartenschlager, R.6    Tschopp, J.7
  • 17
    • 29744467205 scopus 로고    scopus 로고
    • Signal peptide cleavage and internal targeting signals direct the hepatitis C virus p7 protein to distinct intracellular membranes
    • Griffin S., Clarke D., McCormick C., Rowlands D., and Harris M. Signal peptide cleavage and internal targeting signals direct the hepatitis C virus p7 protein to distinct intracellular membranes. J. Virol. 79 (2005) 15525-15536
    • (2005) J. Virol. , vol.79 , pp. 15525-15536
    • Griffin, S.1    Clarke, D.2    McCormick, C.3    Rowlands, D.4    Harris, M.5
  • 19
    • 33745624260 scopus 로고    scopus 로고
    • Non-structural protein 4A of Hepatitis C virus accumulates on mitochondria and renders the cells prone to undergoing mitochondria-mediated apoptosis
    • Nomura-Takigawa Y., Nagano-Fujii M., Deng L., Kitazawa S., Ishido S., Sada K., and Hotta H. Non-structural protein 4A of Hepatitis C virus accumulates on mitochondria and renders the cells prone to undergoing mitochondria-mediated apoptosis. J. Gen. Virol. 87 (2006) 1935-1945
    • (2006) J. Gen. Virol. , vol.87 , pp. 1935-1945
    • Nomura-Takigawa, Y.1    Nagano-Fujii, M.2    Deng, L.3    Kitazawa, S.4    Ishido, S.5    Sada, K.6    Hotta, H.7
  • 20
    • 33644847375 scopus 로고    scopus 로고
    • Microdomains of intracellular Ca2+: molecular determinants and functional consequences
    • Rizzuto R., and Pozzan T. Microdomains of intracellular Ca2+: molecular determinants and functional consequences. Physiol. Rev. 86 (2006) 369-408
    • (2006) Physiol. Rev. , vol.86 , pp. 369-408
    • Rizzuto, R.1    Pozzan, T.2
  • 21
    • 84934442833 scopus 로고    scopus 로고
    • Chaperones as parts of organelle networks
    • Szabadkai G., and Rizzuto R. Chaperones as parts of organelle networks. Adv. Exp. Med. Biol. 594 (2007) 64-77
    • (2007) Adv. Exp. Med. Biol. , vol.594 , pp. 64-77
    • Szabadkai, G.1    Rizzuto, R.2
  • 22
    • 67349230617 scopus 로고    scopus 로고
    • Mitochondrial calcium transport systems: properties, regulation, and taxonomic features
    • Deryabina Y.I., Isakova E.P., and Zvyagilskaya R.A. Mitochondrial calcium transport systems: properties, regulation, and taxonomic features. Biochemistry (Moscow) 26 (2004) 190-195
    • (2004) Biochemistry (Moscow) , vol.26 , pp. 190-195
    • Deryabina, Y.I.1    Isakova, E.P.2    Zvyagilskaya, R.A.3
  • 23
    • 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., and Weinman S.A. Mitochondrial injury, oxidative stress, and antioxidant gene expression are induced by hepatitis C virus core protein. Gastroenterology 122 (2002) 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
  • 24
    • 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., and Weinman SA. Hepatitis C virus core protein inhibits mitochondrial electron transport and increases reactive oxygen species (ROS) production. J. Biol. Chem. 280 (2005) 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, SA.7
  • 26
    • 33745797050 scopus 로고    scopus 로고
    • Hepatitis C virus triggers mitochondrial permeability transition with production of reactive oxygen species, leading to DNA damage and STAT3 activation
    • Machida K., Cheng K.T., Lai C.K., Jeng K.S., Sung V.M., and Lai M.M. Hepatitis C virus triggers mitochondrial permeability transition with production of reactive oxygen species, leading to DNA damage and STAT3 activation. J. Virol. 80 (2006) 7199-7207
    • (2006) J. Virol. , vol.80 , pp. 7199-7207
    • Machida, K.1    Cheng, K.T.2    Lai, C.K.3    Jeng, K.S.4    Sung, V.M.5    Lai, M.M.6
  • 27
    • 34547739644 scopus 로고    scopus 로고
    • Hepatitis C virus core protein increases mitochondrial ROS production by stimulation of Ca2+ uniporter activity
    • Li Y., Boehning D.F., Qian T., Popov V.L., and Weinman S.A. Hepatitis C virus core protein increases mitochondrial ROS production by stimulation of Ca2+ uniporter activity. FASEB J. 21 (2007) 2474-2485
    • (2007) FASEB J. , vol.21 , pp. 2474-2485
    • Li, Y.1    Boehning, D.F.2    Qian, T.3    Popov, V.L.4    Weinman, S.A.5
  • 28
    • 0031862855 scopus 로고    scopus 로고
    • Continuous human cell lines inducibly expressing hepatitis C virus structural and non-structural proteins
    • Moradpour D., Kary P., Rice C.M., and Blum H.E. Continuous human cell lines inducibly expressing hepatitis C virus structural and non-structural proteins. Hepatology 28 (2005) 192-201
    • (2005) Hepatology , vol.28 , pp. 192-201
    • Moradpour, D.1    Kary, P.2    Rice, C.M.3    Blum, H.E.4
  • 29
    • 1842844355 scopus 로고    scopus 로고
    • Dantrolene-a review of its pharmacology, therapeutic use and new developments
    • Krause T., Gerbershagen M.U., Fiege M., Weisshorn R., and Wappler F. Dantrolene-a review of its pharmacology, therapeutic use and new developments. Anaesthesia 59 (2004) 364-373
    • (2004) Anaesthesia , vol.59 , pp. 364-373
    • Krause, T.1    Gerbershagen, M.U.2    Fiege, M.3    Weisshorn, R.4    Wappler, F.5
  • 30
    • 41749108854 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress in disease pathogenesis
    • Lin J.H., Walter P., and Yen T.S. Endoplasmic reticulum stress in disease pathogenesis. Annu. Rev. Pathol. 3 (2008) 399-425
    • (2008) Annu. Rev. Pathol. , vol.3 , pp. 399-425
    • Lin, J.H.1    Walter, P.2    Yen, T.S.3
  • 31
    • 0037111954 scopus 로고    scopus 로고
    • Endoplasmic reticulum (ER) stress: hepatitis C virus induces an ER-nucleus signal transduction pathway and activates NF-kappaB and STAT-3
    • Waris G., Tardif K.D., and Siddiqui A. Endoplasmic reticulum (ER) stress: hepatitis C virus induces an ER-nucleus signal transduction pathway and activates NF-kappaB and STAT-3. Biochem. Pharmacol. 64 (2002) 1425-1430
    • (2002) Biochem. Pharmacol. , vol.64 , pp. 1425-1430
    • Waris, G.1    Tardif, K.D.2    Siddiqui, A.3
  • 32
    • 2342435179 scopus 로고    scopus 로고
    • A Hepatitis C virus suppresses the IRE1-XBP1 pathway of the unfolded protein response
    • Tardif K.D., Mori K., Kaufman R.J., and Siddiqui A. A Hepatitis C virus suppresses the IRE1-XBP1 pathway of the unfolded protein response. J. Biol. Chem. 279 (2004) 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
  • 36
    • 34247631514 scopus 로고    scopus 로고
    • Analysis of hepatitis C virus superinfection exclusion by using novel fluorochrome gene-tagged viral genomes
    • Schaller T., Appel N., Koutsoudakis G., Kallis S., Lohmann V., Pietschmann T., and Bartenschlager R. Analysis of hepatitis C virus superinfection exclusion by using novel fluorochrome gene-tagged viral genomes. J. Virol. 81 (2007) 4591-4603
    • (2007) J. Virol. , vol.81 , pp. 4591-4603
    • Schaller, T.1    Appel, N.2    Koutsoudakis, G.3    Kallis, S.4    Lohmann, V.5    Pietschmann, T.6    Bartenschlager, R.7
  • 37
    • 33845341103 scopus 로고    scopus 로고
    • Interaction of HCV core protein with 14-3-3epsilon protein releases Bax to activate apoptosis
    • Lee S.K., Park S.O., Joe C.O., and Kim Y.S. Interaction of HCV core protein with 14-3-3epsilon protein releases Bax to activate apoptosis. Biochem. Biophys. Res. Commun. 352 (2007) 756-762
    • (2007) Biochem. Biophys. Res. Commun. , vol.352 , pp. 756-762
    • Lee, S.K.1    Park, S.O.2    Joe, C.O.3    Kim, Y.S.4
  • 38
    • 33646394110 scopus 로고    scopus 로고
    • HCV E2 may induce apoptosis of Huh-7 cells via a mitochondrial-related caspase pathway
    • Chiou H.L., Hsieh Y.S., Hsieh M.R., and Chen T.Y. HCV E2 may induce apoptosis of Huh-7 cells via a mitochondrial-related caspase pathway. Biochem. Biophys. Res. Commun. 345 (2006) 453-458
    • (2006) Biochem. Biophys. Res. Commun. , vol.345 , pp. 453-458
    • Chiou, H.L.1    Hsieh, Y.S.2    Hsieh, M.R.3    Chen, T.Y.4
  • 39
    • 13544269612 scopus 로고    scopus 로고
    • Hepatitis C virus core protein modulates TRAIL-mediated apoptosis by enhancing Bid cleavage and activation of mitochondria apoptosis signaling pathway
    • Chou A.H., Tsai H.F., Wu Y.Y., Hu C.Y., Hwang L.H., Hsu P.I., and Hsu P.N. Hepatitis C virus core protein modulates TRAIL-mediated apoptosis by enhancing Bid cleavage and activation of mitochondria apoptosis signaling pathway. J. Immunol. 174 (2005) 2160-2216
    • (2005) J. Immunol. , vol.174 , pp. 2160-2216
    • Chou, A.H.1    Tsai, H.F.2    Wu, Y.Y.3    Hu, C.Y.4    Hwang, L.H.5    Hsu, P.I.6    Hsu, P.N.7
  • 40
    • 42449088547 scopus 로고    scopus 로고
    • Inhibition of hepatitis C virus (HCV) core protein-induced cell growth by non-structural protein 4A (NS4A) is mediated by mitochondrial dysregulation
    • Selimović D., and Hassan M. Inhibition of hepatitis C virus (HCV) core protein-induced cell growth by non-structural protein 4A (NS4A) is mediated by mitochondrial dysregulation. Bosn. J. Basic Med. Sci. 8 (2008) 4-11
    • (2008) Bosn. J. Basic Med. Sci. , vol.8 , pp. 4-11
    • Selimović, D.1    Hassan, M.2
  • 41
    • 33746367134 scopus 로고    scopus 로고
    • Hepatitis C virus non-structural protein NS5A interacts with FKBP38 and inhibits apoptosis in Huh7 hepatoma cells
    • Wang J., Tong W., Zhang X., Chen L., Yi Z., Pan T., Hu Y., Xiang L., and Yuan Z. Hepatitis C virus non-structural protein NS5A interacts with FKBP38 and inhibits apoptosis in Huh7 hepatoma cells. FEBS Lett. 580 (2006) 4392-4400
    • (2006) FEBS Lett. , vol.580 , pp. 4392-4400
    • Wang, J.1    Tong, W.2    Zhang, X.3    Chen, L.4    Yi, Z.5    Pan, T.6    Hu, Y.7    Xiang, L.8    Yuan, Z.9
  • 44
    • 18844416914 scopus 로고    scopus 로고
    • Inhibition of hepatitis C virus core protein expression in immortalized human hepatocytes induces cytochrome c-independent increase in Apaf-1 and caspase-9 activation for cell death
    • Meyer K., Basu A., Saito K., Ray R.B., and Ray R. Inhibition of hepatitis C virus core protein expression in immortalized human hepatocytes induces cytochrome c-independent increase in Apaf-1 and caspase-9 activation for cell death. Virology 336 (2005) 198-207
    • (2005) Virology , vol.336 , pp. 198-207
    • Meyer, K.1    Basu, A.2    Saito, K.3    Ray, R.B.4    Ray, R.5
  • 46
    • 27844612117 scopus 로고    scopus 로고
    • Hypoxia-inducible factor as a physiological regulator
    • Maxwell P.H. Hypoxia-inducible factor as a physiological regulator. Exp. Physiol. 90 (2005) 791-797
    • (2005) Exp. Physiol. , vol.90 , pp. 791-797
    • Maxwell, P.H.1
  • 47
    • 22244440847 scopus 로고    scopus 로고
    • Proline hydroxylation and gene expression
    • Kaelin W.G. Proline hydroxylation and gene expression. Annu. Rev. Biochem. 74 (2005) 115-128
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 115-128
    • Kaelin, W.G.1
  • 48
    • 11144337759 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1: regulation by hypoxic and non-hypoxic activators
    • Déry M.A., Michaud M.D., and Richard D.E. Hypoxia-inducible factor 1: regulation by hypoxic and non-hypoxic activators. Int. J. Biochem. Cell Biol. 37 (2005) 535-540
    • (2005) Int. J. Biochem. Cell Biol. , vol.37 , pp. 535-540
    • Déry, M.A.1    Michaud, M.D.2    Richard, D.E.3
  • 49
    • 34648830896 scopus 로고    scopus 로고
    • Hepatitis C virus stabilizes hypoxia-inducible factor 1alpha and stimulates the synthesis of vascular endothelial growth factor
    • Nasimuzzaman M., Waris G., Mikolon D., Stupack D.G., and Siddiqui A. Hepatitis C virus stabilizes hypoxia-inducible factor 1alpha and stimulates the synthesis of vascular endothelial growth factor. J. Virol. 81 (2007) 10249-10257
    • (2007) J. Virol. , vol.81 , pp. 10249-10257
    • Nasimuzzaman, M.1    Waris, G.2    Mikolon, D.3    Stupack, D.G.4    Siddiqui, A.5
  • 50
    • 49649108032 scopus 로고    scopus 로고
    • Regulation of gene expression by hypoxia
    • Kenneth N.S., and Rocha S. Regulation of gene expression by hypoxia. Biochem. J. 414 (2008) 19-29
    • (2008) Biochem. J. , vol.414 , pp. 19-29
    • Kenneth, N.S.1    Rocha, S.2
  • 52
    • 24644462789 scopus 로고    scopus 로고
    • Mitochondria and calcium signalling
    • Nicholls D.G. Mitochondria and calcium signalling. Cell Calcium 38 (2005) 311-317
    • (2005) Cell Calcium , vol.38 , pp. 311-317
    • Nicholls, D.G.1
  • 54
    • 46649120115 scopus 로고    scopus 로고
    • The versatility of mitochondrial calcium signals: from stimulation of cell metabolism to induction of cell death
    • Rimessi A., Giorgi C., Pinton P., and Rizzuto R. The versatility of mitochondrial calcium signals: from stimulation of cell metabolism to induction of cell death. Biochim. Biophys. Acta 1777 (2008) 808-816
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 808-816
    • Rimessi, A.1    Giorgi, C.2    Pinton, P.3    Rizzuto, R.4
  • 55
    • 34250789163 scopus 로고    scopus 로고
    • Role of cardiolipin in cytochrome c release from mitochondria
    • Ott M., Zhivotovsky B., and Orrenius S. Role of cardiolipin in cytochrome c release from mitochondria. Cell Death Differ. 14 (2007) 1243-1247
    • (2007) Cell Death Differ. , vol.14 , pp. 1243-1247
    • Ott, M.1    Zhivotovsky, B.2    Orrenius, S.3
  • 57
    • 0142150051 scopus 로고    scopus 로고
    • Mitochondrial formation of reactive oxygen species
    • Turrens J.F. Mitochondrial formation of reactive oxygen species. J. Physiol. 552 (2003) 335-344
    • (2003) J. Physiol. , vol.552 , pp. 335-344
    • Turrens, J.F.1
  • 58
    • 0038462137 scopus 로고    scopus 로고
    • Nitric oxide and calcium together inactivate mitochondrial complex I and induce cytochrome c release
    • Jekabsone A., Ivanoviene L., Brown G.C., and Borutaite V. Nitric oxide and calcium together inactivate mitochondrial complex I and induce cytochrome c release. J. Mol. Cell Cardiol. 35 (2003) 803-809
    • (2003) J. Mol. Cell Cardiol. , vol.35 , pp. 803-809
    • Jekabsone, A.1    Ivanoviene, L.2    Brown, G.C.3    Borutaite, V.4
  • 59
    • 33745603712 scopus 로고    scopus 로고
    • S-nitrosothiol inhibition of mitochondrial complex I causes a reversible increase in mitochondrial hydrogen peroxide production
    • Borutaite V., and Brown G.C. S-nitrosothiol inhibition of mitochondrial complex I causes a reversible increase in mitochondrial hydrogen peroxide production. Biochim. Biophys. Acta 1757 (2006) 562-566
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 562-566
    • Borutaite, V.1    Brown, G.C.2
  • 60
    • 33745635338 scopus 로고    scopus 로고
    • Mitochondrial NADPH, transhydrogenase and disease
    • Rydström J. Mitochondrial NADPH, transhydrogenase and disease. Biochim. Biophys. Acta 1757 (2006) 721-726
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 721-726
    • Rydström, J.1
  • 61
    • 9144249116 scopus 로고    scopus 로고
    • Glutaredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins: implications for mitochondrial redox regulation and antioxidant DEFENSE
    • Beer S.M., Taylor E.R., Brown S.E., Dahm C.C., Costa N.J., Runswick M.J., and Murphy M.P. Glutaredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins: implications for mitochondrial redox regulation and antioxidant DEFENSE. J. Biol. Chem. 279 (2004) 47939-47951
    • (2004) J. Biol. Chem. , vol.279 , pp. 47939-47951
    • Beer, S.M.1    Taylor, E.R.2    Brown, S.E.3    Dahm, C.C.4    Costa, N.J.5    Runswick, M.J.6    Murphy, M.P.7
  • 62
    • 0036260697 scopus 로고    scopus 로고
    • Cellular response to oxidative stress: signaling for suicide and survival
    • Martindale J.L., and Holbrook N.J. Cellular response to oxidative stress: signaling for suicide and survival. J. Cell Physiol. 192 (2002) 1-15
    • (2002) J. Cell Physiol. , vol.192 , pp. 1-15
    • Martindale, J.L.1    Holbrook, N.J.2
  • 63
    • 3242752786 scopus 로고    scopus 로고
    • Molecular events associated with reactive oxygen species and cell cycle progression in mammalian cells
    • Boonstra J., and Post J.A. Molecular events associated with reactive oxygen species and cell cycle progression in mammalian cells. Gene 337 (2004) 1-13
    • (2004) Gene , vol.337 , pp. 1-13
    • Boonstra, J.1    Post, J.A.2
  • 64
    • 17244367828 scopus 로고    scopus 로고
    • Reactive oxygen species in tumor progression
    • Storz P. Reactive oxygen species in tumor progression. Front Biosci. 10 (2005) 1881-1896
    • (2005) Front Biosci. , vol.10 , pp. 1881-1896
    • Storz, P.1
  • 65
    • 33751372117 scopus 로고    scopus 로고
    • Mechanisms and significance of liver steatosis in hepatitis C virus infection
    • Negro F. Mechanisms and significance of liver steatosis in hepatitis C virus infection. World J. Gastroenterol. 12 (2006) 6756-6765
    • (2006) World J. Gastroenterol. , vol.12 , pp. 6756-6765
    • Negro, F.1
  • 66
    • 46749146865 scopus 로고    scopus 로고
    • Carnitine palmitoyltransferase 1: central to cell function
    • Zammit V.A. Carnitine palmitoyltransferase 1: central to cell function. IUBMB Life 60 (2008) 347-354
    • (2008) IUBMB Life , vol.60 , pp. 347-354
    • Zammit, V.A.1
  • 67
    • 0028053663 scopus 로고
    • Recent progress on regulation of the mitochondrial permeability transition pore; a cyclosporin-sensitive pore in the inner mitochondrial membrane
    • Bernardi P., Broekemeier K.M., and Pfeiffer D.R. Recent progress on regulation of the mitochondrial permeability transition pore; a cyclosporin-sensitive pore in the inner mitochondrial membrane. J. Bioenerg. Biomembr. 26 (1994) 509-517
    • (1994) J. Bioenerg. Biomembr. , vol.26 , pp. 509-517
    • Bernardi, P.1    Broekemeier, K.M.2    Pfeiffer, D.R.3
  • 68
    • 0031008145 scopus 로고    scopus 로고
    • Role of the mitochondrial permeability transition pore in apoptosis
    • Hirsch T., Marzo I., and Kroemer G. Role of the mitochondrial permeability transition pore in apoptosis. Biosci. Rep. 17 (1997) 67-76
    • (1997) Biosci. Rep. , vol.17 , pp. 67-76
    • Hirsch, T.1    Marzo, I.2    Kroemer, G.3
  • 69
    • 38849184816 scopus 로고    scopus 로고
    • PPARalpha activation is essential for HCV core protein-induced hepatic steatosis and hepatocellular carcinoma in mice
    • Tanaka N., Moriya K., Kiyosawa K., Koike K., Gonzalez F.J., and Aoyama T. PPARalpha activation is essential for HCV core protein-induced hepatic steatosis and hepatocellular carcinoma in mice. J. Clin. Invest. 118 (2008) 683-694
    • (2008) J. Clin. Invest. , vol.118 , pp. 683-694
    • Tanaka, N.1    Moriya, K.2    Kiyosawa, K.3    Koike, K.4    Gonzalez, F.J.5    Aoyama, T.6
  • 70
    • 33845977959 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization in cell death
    • Kroemer G., Galluzzi L., and Brenner C. Mitochondrial membrane permeabilization in cell death. Physiol. Rev. 87 (2007) 99-163
    • (2007) Physiol. Rev. , vol.87 , pp. 99-163
    • Kroemer, G.1    Galluzzi, L.2    Brenner, C.3
  • 71
    • 42449123761 scopus 로고    scopus 로고
    • Expansion and evolution of cell death programmes
    • Degterev A., and Yuan J. Expansion and evolution of cell death programmes. Nat. Rev. Mol. Cell Biol. 9 (2008) 378-390
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 378-390
    • Degterev, A.1    Yuan, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.