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Volumn 19, Issue 3, 2009, Pages 147-164

Access of viral proteins to mitochondria via mitochondria-associated membranes

Author keywords

[No Author keywords available]

Indexed keywords

ANTIVIRUS AGENT; CALCIUM ION; CERAMIDE; CORE PROTEIN; F ACTIN; PROTEIN UL37; SERINE PROTEINASE; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 67449119450     PISSN: 10529276     EISSN: None     Source Type: Journal    
DOI: 10.1002/rmv.611     Document Type: Review
Times cited : (55)

References (148)
  • 2
    • 0014461483 scopus 로고
    • Continuities between mitochondria and endoplasmic reticulum in the mammalian ovary
    • Ruby JR, Dyer RF, Skalko RG. Continuities between mitochondria and endoplasmic reticulum in the mammalian ovary. Z Zellforsch Mikrosk Anat 1969; 97: 30-37.
    • (1969) Z Zellforsch Mikrosk Anat , vol.97 , pp. 30-37
    • Ruby, J.R.1    Dyer, R.F.2    Skalko, R.G.3
  • 3
    • 0019225889 scopus 로고
    • Relationships between mitochondrial outer membranes and agranular reticulum in nervous tissue: Ultrastructural observations and a new interpretation
    • Spacek J, Lieberman AR. Relationships between mitochondrial outer membranes and agranular reticulum in nervous tissue: ultrastructural observations and a new interpretation. J Cell Sci 1980; 46: 129-147.
    • (1980) J Cell Sci , vol.46 , pp. 129-147
    • Spacek, J.1    Lieberman, A.R.2
  • 4
    • 0014995330 scopus 로고
    • Continuity between cytoplasmic endomembranes and outer mitochondrial membranes in fungi
    • Bracker CE, Grove SN. Continuity between cytoplasmic endomembranes and outer mitochondrial membranes in fungi. Protoplasma 1971; 73: 15-34.
    • (1971) Protoplasma , vol.73 , pp. 15-34
    • Bracker, C.E.1    Grove, S.N.2
  • 5
    • 0015791478 scopus 로고
    • A rapidly sedimenting fraction of rat liver endoplasmic reticulum
    • Lewis JA, Tata JR. A rapidly sedimenting fraction of rat liver endoplasmic reticulum. J Cell Sci 1973; 13: 447-459.
    • (1973) J Cell Sci , vol.13 , pp. 447-459
    • Lewis, J.A.1    Tata, J.R.2
  • 6
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • Schroder M, Kaufman RJ. The mammalian unfolded protein response. Annu Rev Biochem 2005; 74: 739-789.
    • (2005) Annu Rev Biochem , vol.74 , pp. 739-789
    • Schroder, M.1    Kaufman, R.J.2
  • 7
    • 7444240833 scopus 로고    scopus 로고
    • The ER function BiP is a master regulator of ER function
    • Hendershot LM. The ER function BiP is a master regulator of ER function. Mt Sinai J Med 2004; 71: 289-297.
    • (2004) Mt Sinai J Med , vol.71 , pp. 289-297
    • Hendershot, L.M.1
  • 8
    • 33750523442 scopus 로고    scopus 로고
    • Mitochondrial calcium signalling and cell death: Approaches for assessing the role of mitochondrial Ca2+ uptake in apoptosis
    • Hajnoczky G, Csordas G, Das S, et al. Mitochondrial calcium signalling and cell death: approaches for assessing the role of mitochondrial Ca2+ uptake in apoptosis. Cell Calcium 2006; 40: 553-560.
    • (2006) Cell Calcium , vol.40 , pp. 553-560
    • Hajnoczky, G.1    Csordas, G.2    Das, S.3
  • 9
    • 0036830474 scopus 로고    scopus 로고
    • Mitochondrial function and dysfunction in the cell: Its relevance to aging and agingrelated disease
    • Nicholls DG. Mitochondrial function and dysfunction in the cell: its relevance to aging and agingrelated disease. Int J Biochem Cell Biol 2002; 34: 1372-1381.
    • (2002) Int J Biochem Cell Biol , vol.34 , pp. 1372-1381
    • Nicholls, D.G.1
  • 10
    • 1542350631 scopus 로고    scopus 로고
    • Rizzuto R, Duchen MR, Pozzan T. Flirting in little space: the ER/ mitochondria Ca2+ liaison. Sci STKE 2004; 2004: re1.
    • Rizzuto R, Duchen MR, Pozzan T. Flirting in little space: the ER/ mitochondria Ca2+ liaison. Sci STKE 2004; 2004: re1.
  • 11
    • 0019885304 scopus 로고
    • Isolation and characterization of rough endoplasmic reticulum associated with mitochondria from normal rat liver
    • Meier PJ, Spycher MA, Meyer UA. Isolation and characterization of rough endoplasmic reticulum associated with mitochondria from normal rat liver. Biochim Biophys Acta 1981; 646: 283-297.
    • (1981) Biochim Biophys Acta , vol.646 , pp. 283-297
    • Meier, P.J.1    Spycher, M.A.2    Meyer, U.A.3
  • 12
    • 0035956989 scopus 로고    scopus 로고
    • Organellar relationships in the Golgi region of the pancreatic beta cell line, HIT-T15, visualized by high resolution electron tomography
    • Marsh BJ, Mastronarde DN, Buttle KF, Howell KE, McIntosh JR. Organellar relationships in the Golgi region of the pancreatic beta cell line, HIT-T15, visualized by high resolution electron tomography. Proc Natl Acad Sci USA 2001; 98: 2399-2406.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 2399-2406
    • Marsh, B.J.1    Mastronarde, D.N.2    Buttle, K.F.3    Howell, K.E.4    McIntosh, J.R.5
  • 13
    • 0019161684 scopus 로고    scopus 로고
    • Pickett CB, Montisano D, Eisner D, Cascarano J. The physical association between rat liver mitochondria and rough endoplasmic reticulum. I. Isolation, electron microscopic examination and sedimentation equilibrium centrifugation analyses of rough endoplasmic reticulum-mitochondrial complexes. Exp Cell Res 1980; 128: 343-352.
    • Pickett CB, Montisano D, Eisner D, Cascarano J. The physical association between rat liver mitochondria and rough endoplasmic reticulum. I. Isolation, electron microscopic examination and sedimentation equilibrium centrifugation analyses of rough endoplasmic reticulum-mitochondrial complexes. Exp Cell Res 1980; 128: 343-352.
  • 14
    • 35549006797 scopus 로고    scopus 로고
    • Sigma-1 receptor chaperones at the ER-mitochondrion interface regulate Ca(2+) signaling and cell survival
    • Hayashi T, Su TP. Sigma-1 receptor chaperones at the ER-mitochondrion interface regulate Ca(2+) signaling and cell survival. Cell 2007; 131: 596-610.
    • (2007) Cell , vol.131 , pp. 596-610
    • Hayashi, T.1    Su, T.P.2
  • 15
    • 33845692166 scopus 로고    scopus 로고
    • Chaperonemediated coupling of endoplasmic reticulum and mitochondrial Ca2+ channels
    • Szabadkai G, Bianchi K, Varnai P, et al. Chaperonemediated coupling of endoplasmic reticulum and mitochondrial Ca2+ channels. J Cell Biol 2006; 175: 901-911.
    • (2006) J Cell Biol , vol.175 , pp. 901-911
    • Szabadkai, G.1    Bianchi, K.2    Varnai, P.3
  • 16
    • 2542448093 scopus 로고    scopus 로고
    • Participation of endoplasmic reticulum and mitochondrial calcium handling in apoptosis: More than just neighborhood?
    • Szabadkai G, Rizzuto R. Participation of endoplasmic reticulum and mitochondrial calcium handling in apoptosis: more than just neighborhood? FEBS Lett 2004; 567: 111-115.
    • (2004) FEBS Lett , vol.567 , pp. 111-115
    • Szabadkai, G.1    Rizzuto, R.2
  • 17
    • 35248824214 scopus 로고    scopus 로고
    • Mitochondria-endoplasmic reticulum choreography: Structure and signaling dynamics
    • Pizzo P, Pozzan T. Mitochondria-endoplasmic reticulum choreography: structure and signaling dynamics. Trends Cell Biol 2007; 17: 511-517.
    • (2007) Trends Cell Biol , vol.17 , pp. 511-517
    • Pizzo, P.1    Pozzan, T.2
  • 18
    • 0025273937 scopus 로고
    • Phospholipid synthesis in a membrane fraction associated with mitochondria
    • Vance JE. Phospholipid synthesis in a membrane fraction associated with mitochondria. J Biol Chem 1990; 265: 7248-7256.
    • (1990) J Biol Chem , vol.265 , pp. 7248-7256
    • Vance, J.E.1
  • 19
    • 26444593029 scopus 로고    scopus 로고
    • Mitochondria and endoplasmic reticulum: The lethal interorganelle crosstalk
    • Walter L, Hajnoczky G. Mitochondria and endoplasmic reticulum: the lethal interorganelle crosstalk. J Bioenerg Biomembr 2005; 37: 191-206.
    • (2005) J Bioenerg Biomembr , vol.37 , pp. 191-206
    • Walter, L.1    Hajnoczky, G.2
  • 20
    • 0017325162 scopus 로고
    • Two fractions of rough endoplasmic reticulum from rat liver. I. Recovery of rapidly sedimenting endoplasmic reticulum in association with mitochondria
    • Shore GC, Tata JR. Two fractions of rough endoplasmic reticulum from rat liver. I. Recovery of rapidly sedimenting endoplasmic reticulum in association with mitochondria. J Cell Biol 1977; 72: 714-725.
    • (1977) J Cell Biol , vol.72 , pp. 714-725
    • Shore, G.C.1    Tata, J.R.2
  • 21
    • 0027377058 scopus 로고
    • Involvement of mitochondrial contact sites in the subcellular compartmentalization of phospholipid biosynthetic enzymes
    • Ardail D, Gasnier F, Lerme F, Simonot C, Louisot P, Gateau-Roesch O. Involvement of mitochondrial contact sites in the subcellular compartmentalization of phospholipid biosynthetic enzymes. J Biol Chem 1993; 268: 25985-25992.
    • (1993) J Biol Chem , vol.268 , pp. 25985-25992
    • Ardail, D.1    Gasnier, F.2    Lerme, F.3    Simonot, C.4    Louisot, P.5    Gateau-Roesch, O.6
  • 22
    • 33749022800 scopus 로고    scopus 로고
    • Structural and functional features and significance of the physical linkage between ER and mitochondria
    • Csordas G, Renken C, Varnai P, et al. Structural and functional features and significance of the physical linkage between ER and mitochondria. J Cell Biol 2006; 174: 915-921.
    • (2006) J Cell Biol , vol.174 , pp. 915-921
    • Csordas, G.1    Renken, C.2    Varnai, P.3
  • 23
    • 0033521586 scopus 로고    scopus 로고
    • Quasi-synaptic calcium signal transmission between endoplasmic reticulum and mitochondria
    • Csordas G, Thomas AP, Hajnoczky G. Quasi-synaptic calcium signal transmission between endoplasmic reticulum and mitochondria. EMBO J 1999; 18: 96-108.
    • (1999) EMBO J , vol.18 , pp. 96-108
    • Csordas, G.1    Thomas, A.P.2    Hajnoczky, G.3
  • 24
    • 42949105726 scopus 로고    scopus 로고
    • Ceramide synthesis in the endoplasmic reticulum can permeabilize mitochondria to proapoptotic proteins
    • Stiban J, Caputo L, Colombini M. Ceramide synthesis in the endoplasmic reticulum can permeabilize mitochondria to proapoptotic proteins. J Lipid Res 2008; 49: 625-634.
    • (2008) J Lipid Res , vol.49 , pp. 625-634
    • Stiban, J.1    Caputo, L.2    Colombini, M.3
  • 25
    • 0034602158 scopus 로고    scopus 로고
    • Phosphatidylserine synthase-1 and -2 are localized to mitochondria-associated membranes
    • Stone SJ, Vance JE. Phosphatidylserine synthase-1 and -2 are localized to mitochondria-associated membranes. J Biol Chem 2000; 275: 34534-34540.
    • (2000) J Biol Chem , vol.275 , pp. 34534-34540
    • Stone, S.J.1    Vance, J.E.2
  • 26
    • 0032511112 scopus 로고    scopus 로고
    • Close contacts with the endoplasmic reticulum as determinants of mitochondrial Ca2+ responses
    • Rizzuto R, Pinton P, Carrington W, et al. Close contacts with the endoplasmic reticulum as determinants of mitochondrial Ca2+ responses. Science 1998; 280: 1763-1766.
    • (1998) Science , vol.280 , pp. 1763-1766
    • Rizzuto, R.1    Pinton, P.2    Carrington, W.3
  • 27
    • 40949104848 scopus 로고    scopus 로고
    • Bozidis P, Williamson CD, Colberg-Poley AM. Isolation of endoplasmic reticulum, mitochondria, and mitochondria-associated membrane fractions from transfected cells and from human cytomegalovirus-infected primary fibroblasts. In Current Protocols in Cell Biology. 2007; 3.27: 1-23
    • Bozidis P, Williamson CD, Colberg-Poley AM. Isolation of endoplasmic reticulum, mitochondria, and mitochondria-associated membrane fractions from transfected cells and from human cytomegalovirus-infected primary fibroblasts. In Current Protocols in Cell Biology. 2007; 3.27: 1-23
  • 28
    • 4544261024 scopus 로고    scopus 로고
    • Subcellular compartmentalization of ceramide metabolism: MAM (mitochondria-associated membrane) and/or mitochondria?
    • Bionda C, Portoukalian J, Schmitt D, Rodriguez-Lafrasse C, Ardail D. Subcellular compartmentalization of ceramide metabolism: MAM (mitochondria-associated membrane) and/or mitochondria? Biochem J 2004; 382: 527-533.
    • (2004) Biochem J , vol.382 , pp. 527-533
    • Bionda, C.1    Portoukalian, J.2    Schmitt, D.3    Rodriguez-Lafrasse, C.4    Ardail, D.5
  • 29
    • 0038662790 scopus 로고    scopus 로고
    • The mitochondria-associated endoplasmic-reticulum subcompartment (MAM fraction) of rat liver contains highly active sphingolipid-specific glycosyltransferases
    • Ardail D, Popa I, Bodennec J, Louisot P, Schmitt D, Portoukalian J. The mitochondria-associated endoplasmic-reticulum subcompartment (MAM fraction) of rat liver contains highly active sphingolipid-specific glycosyltransferases. Biochem J 2003; 371: 1013-1019.
    • (2003) Biochem J , vol.371 , pp. 1013-1019
    • Ardail, D.1    Popa, I.2    Bodennec, J.3    Louisot, P.4    Schmitt, D.5    Portoukalian, J.6
  • 30
    • 21744445061 scopus 로고    scopus 로고
    • Bridging gaps in phospholipid transport
    • Voelker DR. Bridging gaps in phospholipid transport. Trends Biochem Sci 2005; 30: 396-404.
    • (2005) Trends Biochem Sci , vol.30 , pp. 396-404
    • Voelker, D.R.1
  • 31
    • 50949084838 scopus 로고    scopus 로고
    • Phosphatidylserine and phosphatidy-lethanolamine in mammalian cells: Two metabolically related aminophospholipids
    • Vance JE. Phosphatidylserine and phosphatidy-lethanolamine in mammalian cells: two metabolically related aminophospholipids. J Lipid Res 2008; 49: 1377-1387.
    • (2008) J Lipid Res , vol.49 , pp. 1377-1387
    • Vance, J.E.1
  • 32
    • 20144385980 scopus 로고    scopus 로고
    • PACS-2 controls endoplasmic reticulum-mitochondria communication and Bid-mediated apoptosis
    • Simmen T, Aslan JE, Blagoveshchenskaya AD, et al. PACS-2 controls endoplasmic reticulum-mitochondria communication and Bid-mediated apoptosis. EMBO J 2005; 24: 717-729.
    • (2005) EMBO J , vol.24 , pp. 717-729
    • Simmen, T.1    Aslan, J.E.2    Blagoveshchenskaya, A.D.3
  • 33
    • 0032006885 scopus 로고    scopus 로고
    • FACL4, a new gene encoding long-chain acyl-CoA synthetase 4, is deleted in a family with Alport syndrome, elliptocytosis, and mental retardation
    • Piccini M, Vitelli F, Bruttini M, et al. FACL4, a new gene encoding long-chain acyl-CoA synthetase 4, is deleted in a family with Alport syndrome, elliptocytosis, and mental retardation. Genomics 1998; 47: 350-358.
    • (1998) Genomics , vol.47 , pp. 350-358
    • Piccini, M.1    Vitelli, F.2    Bruttini, M.3
  • 34
    • 0027973135 scopus 로고
    • A unique mitochondria-associated membrane fraction from rat liver has a high capacity for lipid synthesis and contains pre-Golgi secretory proteins including nascent lipoproteins
    • Rusiñol AE, Cui Z, Chen MH, Vance JE. A unique mitochondria-associated membrane fraction from rat liver has a high capacity for lipid synthesis and contains pre-Golgi secretory proteins including nascent lipoproteins. J Biol Chem 1994; 269: 27494-27502.
    • (1994) J Biol Chem , vol.269 , pp. 27494-27502
    • Rusiñol, A.E.1    Cui, Z.2    Chen, M.H.3    Vance, J.E.4
  • 35
    • 11144357274 scopus 로고    scopus 로고
    • Hepatitis C virus core protein shows a cytoplasmic localization and associates to cellular lipid storage droplets
    • Barba G, Harper F, Harada T, et al. Hepatitis C virus core protein shows a cytoplasmic localization and associates to cellular lipid storage droplets. Proc Natl Acad Sci USA 1997; 94: 1200-1205.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 1200-1205
    • Barba, G.1    Harper, F.2    Harada, T.3
  • 36
    • 0036683052 scopus 로고    scopus 로고
    • Intramembrane proteolysis promotes trafficking of hepatitis C virus core protein to lipid droplets
    • McLauchlan J, Lemberg MK, Hope G, Martoglio B. Intramembrane proteolysis promotes trafficking of hepatitis C virus core protein to lipid droplets. EMBO J 2002; 21: 3980-3988.
    • (2002) EMBO J , vol.21 , pp. 3980-3988
    • McLauchlan, J.1    Lemberg, M.K.2    Hope, G.3    Martoglio, B.4
  • 37
    • 0030859121 scopus 로고    scopus 로고
    • Hepatitis C virus core protein induces hepatic steatosis in transgenic mice
    • Moriya K, Yotsuyanagi H, Shintani Y, et al. Hepatitis C virus core protein induces hepatic steatosis in transgenic mice. J Gen Virol 1997; 78: 1527-1531.
    • (1997) J Gen Virol , vol.78 , pp. 1527-1531
    • Moriya, K.1    Yotsuyanagi, H.2    Shintani, Y.3
  • 38
    • 0032883325 scopus 로고    scopus 로고
    • Hepatitis C virus core protein binds to apolipoprotein AII and its secretion is modulated by fibrates
    • Sabile A, Perlemuter G, Bono F, et al. Hepatitis C virus core protein binds to apolipoprotein AII and its secretion is modulated by fibrates. Hepatology 1999; 30: 1064-1076.
    • (1999) Hepatology , vol.30 , pp. 1064-1076
    • Sabile, A.1    Perlemuter, G.2    Bono, F.3
  • 39
    • 18244365866 scopus 로고    scopus 로고
    • Hepatitis C virus core protein inhibits microsomal triglyceride transfer protein activity and very low density lipo-protein secretion: A model of viral-related steatosis
    • Perlemuter G, Sabile A, Letteron P, et al. Hepatitis C virus core protein inhibits microsomal triglyceride transfer protein activity and very low density lipo-protein secretion: a model of viral-related steatosis. Faseb J 2002; 16: 185-194.
    • (2002) Faseb J , vol.16 , pp. 185-194
    • Perlemuter, G.1    Sabile, A.2    Letteron, P.3
  • 40
    • 34548316984 scopus 로고    scopus 로고
    • The lipid droplet is an important organelle for hepatitis C virus production
    • Miyanari Y, Atsuzawa K, Usuda N, et al. The lipid droplet is an important organelle for hepatitis C virus production. Nat Cell Biol 2007; 9: 1089-1097.
    • (2007) Nat Cell Biol , vol.9 , pp. 1089-1097
    • Miyanari, Y.1    Atsuzawa, K.2    Usuda, N.3
  • 41
    • 54449086337 scopus 로고    scopus 로고
    • Human cytomegalovirus regulates bioactive sphingolipids
    • Machesky NJ, Zhang G, Raghavan B, et al. Human cytomegalovirus regulates bioactive sphingolipids. J Biol Chem 2008; 283: 26148-26160.
    • (2008) J Biol Chem , vol.283 , pp. 26148-26160
    • Machesky, N.J.1    Zhang, G.2    Raghavan, B.3
  • 42
    • 40149104688 scopus 로고    scopus 로고
    • Mitochondrial and secretory human cytomegalovirus UL37 proteins traffic into mitochondrion-associated membranes of human cells
    • Bozidis P, Williamson CD, Colberg-Poley AM. Mitochondrial and secretory human cytomegalovirus UL37 proteins traffic into mitochondrion-associated membranes of human cells. J Virol 2008; 82: 2715-2726.
    • (2008) J Virol , vol.82 , pp. 2715-2726
    • Bozidis, P.1    Williamson, C.D.2    Colberg-Poley, A.M.3
  • 43
    • 0032055479 scopus 로고    scopus 로고
    • A mitochondrial membrane protein is required for translocation of phosphatidylserine from mitochondria-associated membranes to mitochondria
    • Shiao YJ, Balcerzak B, Vance JE. A mitochondrial membrane protein is required for translocation of phosphatidylserine from mitochondria-associated membranes to mitochondria. Biochem J 1998; 331: 217-223.
    • (1998) Biochem J , vol.331 , pp. 217-223
    • Shiao, Y.J.1    Balcerzak, B.2    Vance, J.E.3
  • 44
    • 0026508561 scopus 로고
    • Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages
    • Fadok VA, Voelker DR, Campbell PA, Cohen JJ, Bratton DL, Henson PM. Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages. J Immunol 1992; 148: 2207-2216.
    • (1992) J Immunol , vol.148 , pp. 2207-2216
    • Fadok, V.A.1    Voelker, D.R.2    Campbell, P.A.3    Cohen, J.J.4    Bratton, D.L.5    Henson, P.M.6
  • 45
    • 0026451081 scopus 로고
    • Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C
    • Nishizuka Y. Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C. Science 1992; 258: 607-614.
    • (1992) Science , vol.258 , pp. 607-614
    • Nishizuka, Y.1
  • 46
    • 34547138164 scopus 로고    scopus 로고
    • Regulated externalization of phosphatidylserine at the cell surface: Implications for apoptosis
    • Balasubramanian K, Mirnikjoo B, Schroit AJ. Regulated externalization of phosphatidylserine at the cell surface: implications for apoptosis. J Biol Chem 2007; 282: 18357-18364.
    • (2007) J Biol Chem , vol.282 , pp. 18357-18364
    • Balasubramanian, K.1    Mirnikjoo, B.2    Schroit, A.J.3
  • 47
    • 0037203317 scopus 로고    scopus 로고
    • Serine palmitoyltransferase: Role in apoptotic de novo ceramide synthesis and other stress responses
    • Perry DK. Serine palmitoyltransferase: role in apoptotic de novo ceramide synthesis and other stress responses. Biochim Biophys Acta 2002; 1585: 146-152.
    • (2002) Biochim Biophys Acta , vol.1585 , pp. 146-152
    • Perry, D.K.1
  • 48
    • 27344459492 scopus 로고    scopus 로고
    • Lipid microdomains contribute to apoptosis-associated modifications of mitochondria in T cells
    • Garofalo T, Giammarioli AM, Misasi R, et al. Lipid microdomains contribute to apoptosis-associated modifications of mitochondria in T cells. Cell Death Differ 2005; 12: 1378-1389.
    • (2005) Cell Death Differ , vol.12 , pp. 1378-1389
    • Garofalo, T.1    Giammarioli, A.M.2    Misasi, R.3
  • 50
    • 0029143569 scopus 로고
    • Decoding of cytosolic calcium oscillations in the mitochondria
    • Hajnoczky G, Robb-Gaspers LD, Seitz MB, Thomas AP. Decoding of cytosolic calcium oscillations in the mitochondria. Cell 1995; 82: 415-424.
    • (1995) Cell , vol.82 , pp. 415-424
    • Hajnoczky, G.1    Robb-Gaspers, L.D.2    Seitz, M.B.3    Thomas, A.P.4
  • 51
    • 0141754206 scopus 로고    scopus 로고
    • Stable interactions between mitochondria and endoplasmic reticulum allow rapid accumulation of calcium in a subpopulation of mitochondria
    • Filippin L, Magalhaes PJ, Di Benedetto G, Colella M, Pozzan T. Stable interactions between mitochondria and endoplasmic reticulum allow rapid accumulation of calcium in a subpopulation of mitochondria. J Biol Chem 2003; 278: 39224-39234.
    • (2003) J Biol Chem , vol.278 , pp. 39224-39234
    • Filippin, L.1    Magalhaes, P.J.2    Di Benedetto, G.3    Colella, M.4    Pozzan, T.5
  • 52
    • 1642540210 scopus 로고    scopus 로고
    • The mitochondrial calcium uniporter is a highly selective ion channel
    • Kirichok Y, Krapivinsky G, Clapham DE. The mitochondrial calcium uniporter is a highly selective ion channel. Nature 2004; 427: 360-364.
    • (2004) Nature , vol.427 , pp. 360-364
    • Kirichok, Y.1    Krapivinsky, G.2    Clapham, D.E.3
  • 53
    • 0037924355 scopus 로고    scopus 로고
    • Sigma-1 receptors (sigma(1) binding sites) form raft-like microdomains and target lipid droplets on the endoplasmic reticulum: Roles in endoplasmic reticulum lipid compartmentalization and export
    • Hayashi T, Su TP. Sigma-1 receptors (sigma(1) binding sites) form raft-like microdomains and target lipid droplets on the endoplasmic reticulum: roles in endoplasmic reticulum lipid compartmentalization and export. J Pharmacol Exp Ther 2003; 306: 718-725.
    • (2003) J Pharmacol Exp Ther , vol.306 , pp. 718-725
    • Hayashi, T.1    Su, T.P.2
  • 54
    • 0034683749 scopus 로고    scopus 로고
    • Calcium regulates the association between mitochondria and a smooth subdomain of the endoplasmic reticulum
    • Wang HJ, Guay G, Pogan L, Sauve R, Nabi IR. Calcium regulates the association between mitochondria and a smooth subdomain of the endoplasmic reticulum. J Cell Biol 2000; 150: 1489-1498.
    • (2000) J Cell Biol , vol.150 , pp. 1489-1498
    • Wang, H.J.1    Guay, G.2    Pogan, L.3    Sauve, R.4    Nabi, I.R.5
  • 55
    • 29144463168 scopus 로고    scopus 로고
    • Agonist-induced regulation of mitochondrial and endoplasmic reticulum motility
    • Brough D, Schell MJ, Irvine RF. Agonist-induced regulation of mitochondrial and endoplasmic reticulum motility. Biochem J 2005; 392: 291-297.
    • (2005) Biochem J , vol.392 , pp. 291-297
    • Brough, D.1    Schell, M.J.2    Irvine, R.F.3
  • 56
    • 9444226972 scopus 로고    scopus 로고
    • Control of mitochondrial motility and distribution by the calcium signal: A homeostatic circuit
    • Yi M, Weaver D, Hajnoczky G. Control of mitochondrial motility and distribution by the calcium signal: a homeostatic circuit. J Cell Biol 2004; 167: 661-672.
    • (2004) J Cell Biol , vol.167 , pp. 661-672
    • Yi, M.1    Weaver, D.2    Hajnoczky, G.3
  • 57
    • 57349100367 scopus 로고    scopus 로고
    • Mitofusin 2 tethers endoplasmic reticulum to mitochondria
    • de Brito OM, Scorrano L. Mitofusin 2 tethers endoplasmic reticulum to mitochondria. Nature 2008; 456: 605-610.
    • (2008) Nature , vol.456 , pp. 605-610
    • de Brito, O.M.1    Scorrano, L.2
  • 58
    • 11844295416 scopus 로고    scopus 로고
    • Incidence and outcome of congenital cytomegalovirus infection in selected groups of preterm and full-term neonates under intensive care
    • Nagy A, Endreffy E, Streitman K, Pinter S, Pusztai R. Incidence and outcome of congenital cytomegalovirus infection in selected groups of preterm and full-term neonates under intensive care. In Vivo 2004; 18: 819-823.
    • (2004) In Vivo , vol.18 , pp. 819-823
    • Nagy, A.1    Endreffy, E.2    Streitman, K.3    Pinter, S.4    Pusztai, R.5
  • 60
    • 67449129414 scopus 로고    scopus 로고
    • Mocarski ES, Jr., Shenk T, Pass RF. Cytomegaloviruses. In Fields Virology (5th edn), 2, Knipe DM, Howley PM (eds). Wolters Kluwer Health, Lippincott Williams & Wilkins: Philadelphia; 2007; 2701-2772.
    • Mocarski ES, Jr., Shenk T, Pass RF. Cytomegaloviruses. In Fields Virology (5th edn), Vol. 2, Knipe DM, Howley PM (eds). Wolters Kluwer Health, Lippincott Williams & Wilkins: Philadelphia; 2007; 2701-2772.
  • 61
    • 0019756318 scopus 로고
    • Prenatal cytomegalovirus infection: Epidemiology, pathology and pathogenesis
    • Becroft DM. Prenatal cytomegalovirus infection: epidemiology, pathology and pathogenesis. Perspect Pediatr Pathol 1981; 6: 203-241.
    • (1981) Perspect Pediatr Pathol , vol.6 , pp. 203-241
    • Becroft, D.M.1
  • 62
    • 0026544277 scopus 로고
    • Lethal cytomegalovirus infection in preterm infants: Clinical, radiological, and neuropathological findings
    • Perlman JM, Argyle C. Lethal cytomegalovirus infection in preterm infants: clinical, radiological, and neuropathological findings. Ann Neurol 1992; 31: 64-68.
    • (1992) Ann Neurol , vol.31 , pp. 64-68
    • Perlman, J.M.1    Argyle, C.2
  • 63
    • 1542373665 scopus 로고    scopus 로고
    • The impact of cytomegalovirus serostatus of donor and recipient before hematopoietic stem cell transplantation in the era of antiviral prophylaxis and preemptive therapy
    • Boeckh M, Nichols WG. The impact of cytomegalovirus serostatus of donor and recipient before hematopoietic stem cell transplantation in the era of antiviral prophylaxis and preemptive therapy. Blood 2004; 103: 2003-2008.
    • (2004) Blood , vol.103 , pp. 2003-2008
    • Boeckh, M.1    Nichols, W.G.2
  • 64
    • 15044343276 scopus 로고    scopus 로고
    • From clinical trials to clinical practice: An overview of Certican (everolimus) in heart transplantation
    • discussion S210-S181
    • Valantine H, Zuckermann A. From clinical trials to clinical practice: an overview of Certican (everolimus) in heart transplantation. J Heart Lung Transplant 2005; 24: S185-S190; discussion S210-S181.
    • (2005) J Heart Lung Transplant , vol.24
    • Valantine, H.1    Zuckermann, A.2
  • 65
    • 0029840904 scopus 로고    scopus 로고
    • Association between prior cytomegalovirus infection and the risk of restenosis after coronary atherectomy
    • Zhou YF, Leon MB, Waclawiw MA, et al. Association between prior cytomegalovirus infection and the risk of restenosis after coronary atherectomy. N Engl J Med 1996; 335: 624-630.
    • (1996) N Engl J Med , vol.335 , pp. 624-630
    • Zhou, Y.F.1    Leon, M.B.2    Waclawiw, M.A.3
  • 66
    • 0032054987 scopus 로고    scopus 로고
    • High anticytomegalovirus (CMV) IgG antibody titer is associated with coronary artery disease and may predict post-coronary balloon angioplasty restenosis
    • Blum A, Giladi M, Weinberg M, et al. High anticytomegalovirus (CMV) IgG antibody titer is associated with coronary artery disease and may predict post-coronary balloon angioplasty restenosis. Am J Cardiol 1998; 81: 866-868.
    • (1998) Am J Cardiol , vol.81 , pp. 866-868
    • Blum, A.1    Giladi, M.2    Weinberg, M.3
  • 67
    • 0023736949 scopus 로고
    • An immediate early gene of human cytomegalovirus encodes a potential membrane glycoprotein
    • Kouzarides T, Bankier AT, Satchwell SC, Preddy E, Barrell BG. An immediate early gene of human cytomegalovirus encodes a potential membrane glycoprotein. Virology 1988; 165: 151-164.
    • (1988) Virology , vol.165 , pp. 151-164
    • Kouzarides, T.1    Bankier, A.T.2    Satchwell, S.C.3    Preddy, E.4    Barrell, B.G.5
  • 68
    • 13044276250 scopus 로고    scopus 로고
    • A cytomegalovirus-encoded mitochondria-localized inhibitor of apoptosis structurally unrelated to Bcl-2
    • Goldmacher VS, Bartle LM, Skaletskaya A, et al. A cytomegalovirus-encoded mitochondria-localized inhibitor of apoptosis structurally unrelated to Bcl-2. Proc Natl Acad Sci USA 1999; 96: 12536-12541.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 12536-12541
    • Goldmacher, V.S.1    Bartle, L.M.2    Skaletskaya, A.3
  • 70
    • 0029814503 scopus 로고    scopus 로고
    • The human cytomegalovirus UL37 immediate-early regulatory protein is an integral membrane N-glycoprotein which traffics through the endoplasmic reticulum and Golgi apparatus
    • Al-Barazi HO, Colberg-Poley AM. The human cytomegalovirus UL37 immediate-early regulatory protein is an integral membrane N-glycoprotein which traffics through the endoplasmic reticulum and Golgi apparatus. J Virol 1996; 70: 7198-7208.
    • (1996) J Virol , vol.70 , pp. 7198-7208
    • Al-Barazi, H.O.1    Colberg-Poley, A.M.2
  • 71
    • 1342289076 scopus 로고    scopus 로고
    • Dual targeting of the human cytomegalovirus UL37 exon 1 protein during permissive infection
    • Mavinakere MS, Colberg-Poley AM. Dual targeting of the human cytomegalovirus UL37 exon 1 protein during permissive infection. J Gen Virol 2004; 85: 323-329.
    • (2004) J Gen Virol , vol.85 , pp. 323-329
    • Mavinakere, M.S.1    Colberg-Poley, A.M.2
  • 72
    • 33947418741 scopus 로고    scopus 로고
    • Human cytomegalovirus pUL37×1 induces the release of endoplasmic reticulum calcium stores
    • Sharon-Friling R, Goodhouse J, Colberg-Poley AM, Shenk T. Human cytomegalovirus pUL37×1 induces the release of endoplasmic reticulum calcium stores. Proc Natl Acad Sci USA 2006; 103: 19117-19122.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 19117-19122
    • Sharon-Friling, R.1    Goodhouse, J.2    Colberg-Poley, A.M.3    Shenk, T.4
  • 73
    • 0025909411 scopus 로고
    • Expression of the human cytomegalovirus UL36-38 immediate early region during permissive infection
    • Tenney DJ, Colberg-Poley AM. Expression of the human cytomegalovirus UL36-38 immediate early region during permissive infection. Virology 1991; 182: 199-210.
    • (1991) Virology , vol.182 , pp. 199-210
    • Tenney, D.J.1    Colberg-Poley, A.M.2
  • 74
    • 0347382540 scopus 로고    scopus 로고
    • Complex alternative processing of human cytomegalovirus UL37 pre-mRNA
    • Adair R, Liebisch GW, Colberg-Poley AM. Complex alternative processing of human cytomegalovirus UL37 pre-mRNA. J Gen Virol 2003; 84: 3353-3358.
    • (2003) J Gen Virol , vol.84 , pp. 3353-3358
    • Adair, R.1    Liebisch, G.W.2    Colberg-Poley, A.M.3
  • 75
    • 3342969701 scopus 로고    scopus 로고
    • Internal cleavage of the human cytomegalovirus UL37 immediate-early glycoprotein and divergent trafficking of its proteolytic fragments
    • Mavinakere MS, Colberg-Poley AM. Internal cleavage of the human cytomegalovirus UL37 immediate-early glycoprotein and divergent trafficking of its proteolytic fragments. J Gen Virol 2004; 85: 1989-1994.
    • (2004) J Gen Virol , vol.85 , pp. 1989-1994
    • Mavinakere, M.S.1    Colberg-Poley, A.M.2
  • 76
    • 0025344377 scopus 로고
    • Analysis of the protein-coding content of the sequence of human cytomegalovirus strain AD169
    • Chee MS, Bankier AT, Beck S, et al. Analysis of the protein-coding content of the sequence of human cytomegalovirus strain AD169. Curr Top Microbiol Immunol 1990; 154: 125-169.
    • (1990) Curr Top Microbiol Immunol , vol.154 , pp. 125-169
    • Chee, M.S.1    Bankier, A.T.2    Beck, S.3
  • 77
    • 33644644202 scopus 로고    scopus 로고
    • Human cytomegalovirus temporally regulated gene expression in differentiated, immortalized retinal pigment epithelial cells
    • Adair R, Liebisch GW, Lerman BJ, Colberg-Poley AM. Human cytomegalovirus temporally regulated gene expression in differentiated, immortalized retinal pigment epithelial cells. J Clin Virol 2006; 35: 478-484.
    • (2006) J Clin Virol , vol.35 , pp. 478-484
    • Adair, R.1    Liebisch, G.W.2    Lerman, B.J.3    Colberg-Poley, A.M.4
  • 78
    • 0035916014 scopus 로고    scopus 로고
    • The sequence and antiapoptotic functional domains of the human cytomegalovirus UL37 exon 1 immediate early protein are conserved in multiple primary strains
    • Hayajneh WA, Colberg-Poley AM, Skaletskaya A, et al. The sequence and antiapoptotic functional domains of the human cytomegalovirus UL37 exon 1 immediate early protein are conserved in multiple primary strains. Virology 2001; 279: 233-240.
    • (2001) Virology , vol.279 , pp. 233-240
    • Hayajneh, W.A.1    Colberg-Poley, A.M.2    Skaletskaya, A.3
  • 79
    • 33745755471 scopus 로고    scopus 로고
    • Induction of apoptosis limits cytomegalovirus cross-species infection
    • Jurak I, Brune W. Induction of apoptosis limits cytomegalovirus cross-species infection. EMBO J 2006; 25: 2634-2642.
    • (2006) EMBO J , vol.25 , pp. 2634-2642
    • Jurak, I.1    Brune, W.2
  • 80
    • 0142091343 scopus 로고    scopus 로고
    • Functional map of human cytomegalovirus AD169 defined by global mutational analysis
    • Yu D, Silva MC, Shenk T. Functional map of human cytomegalovirus AD169 defined by global mutational analysis. Proc Natl Acad Sci USA 2003; 100: 12396-12401.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 12396-12401
    • Yu, D.1    Silva, M.C.2    Shenk, T.3
  • 81
    • 9944262385 scopus 로고    scopus 로고
    • Human cytomegalovirus proteins encoded by UL37 exon 1 protect infected fibroblasts against virus-induced apoptosis and are required for efficient virus replication
    • Reboredo M, Greaves RF, Hahn G. Human cytomegalovirus proteins encoded by UL37 exon 1 protect infected fibroblasts against virus-induced apoptosis and are required for efficient virus replication. J Gen Virol 2004; 85: 3555-3567.
    • (2004) J Gen Virol , vol.85 , pp. 3555-3567
    • Reboredo, M.1    Greaves, R.F.2    Hahn, G.3
  • 82
    • 0345060878 scopus 로고    scopus 로고
    • Functional profiling of a human cytomegalovirus genome
    • Dunn W, Chou C, Li H, et al. Functional profiling of a human cytomegalovirus genome. Proc Natl Acad Sci USA 2003; 100: 14223-14228.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 14223-14228
    • Dunn, W.1    Chou, C.2    Li, H.3
  • 83
    • 25144449148 scopus 로고    scopus 로고
    • Mitochondrial cell death suppressors carried by human and murine cytomegalovirus confer resistance to proteasome inhibitor-induced apoptosis
    • McCormick AL, Meiering CD, Smith GB, Mocarski ES. Mitochondrial cell death suppressors carried by human and murine cytomegalovirus confer resistance to proteasome inhibitor-induced apoptosis. J Virol 2005; 79: 12205-12217.
    • (2005) J Virol , vol.79 , pp. 12205-12217
    • McCormick, A.L.1    Meiering, C.D.2    Smith, G.B.3    Mocarski, E.S.4
  • 84
    • 33745792770 scopus 로고    scopus 로고
    • Processing of human cytomegalovirus UL37 mutant glycoproteins in the endoplasmic reticulum lumen prior to mitochondrial importation
    • Mavinakere MS, Williamson CD, Goldmacher VS, Colberg-Poley AM. Processing of human cytomegalovirus UL37 mutant glycoproteins in the endoplasmic reticulum lumen prior to mitochondrial importation. J Virol 2006; 80: 6771-6783.
    • (2006) J Virol , vol.80 , pp. 6771-6783
    • Mavinakere, M.S.1    Williamson, C.D.2    Goldmacher, V.S.3    Colberg-Poley, A.M.4
  • 85
    • 35848946411 scopus 로고    scopus 로고
    • Structure-function analysis of the interaction between Bax and the cytomegalovirus-encoded protein vMIA
    • Pauleau A-L, Larochette N, Giordanetto F, et al. Structure-function analysis of the interaction between Bax and the cytomegalovirus-encoded protein vMIA. Oncogene 2007; 26: 7067-7080.
    • (2007) Oncogene , vol.26 , pp. 7067-7080
    • Pauleau, A.-L.1    Larochette, N.2    Giordanetto, F.3
  • 86
    • 33749003497 scopus 로고    scopus 로고
    • Cytopathic effects of the cytomegalovirus-encoded apoptosis inhibitory protein vMIA
    • Poncet D, Pauleau AL, Szabadkai G, et al. Cytopathic effects of the cytomegalovirus-encoded apoptosis inhibitory protein vMIA. J Cell Biol 2006; 174: 985-996.
    • (2006) J Cell Biol , vol.174 , pp. 985-996
    • Poncet, D.1    Pauleau, A.L.2    Szabadkai, G.3
  • 87
    • 2542437627 scopus 로고    scopus 로고
    • An antiapoptotic viral protein that recruits Bax to mitochondria
    • Poncet D, Larochette N, Pauleau AL, et al. An antiapoptotic viral protein that recruits Bax to mitochondria. J Biol Chem 2004; 279: 22605-22614.
    • (2004) J Biol Chem , vol.279 , pp. 22605-22614
    • Poncet, D.1    Larochette, N.2    Pauleau, A.L.3
  • 88
    • 0037213306 scopus 로고    scopus 로고
    • Disruption of mitochondrial networks by the human cytomegalovirus UL37 gene product viral mitochondrion-localized inhibitor of apoptosis
    • McCormick AL, Smith VL, Chow D, Mocarski ES. Disruption of mitochondrial networks by the human cytomegalovirus UL37 gene product viral mitochondrion-localized inhibitor of apoptosis. J Virol 2003; 77: 631-641.
    • (2003) J Virol , vol.77 , pp. 631-641
    • McCormick, A.L.1    Smith, V.L.2    Chow, D.3    Mocarski, E.S.4
  • 89
    • 27744439412 scopus 로고    scopus 로고
    • Contribution of GADD45 family members to cell death suppression by cellular bcl-xL and cytomegalovirus vMIA
    • Smith G, Mocarski ES. Contribution of GADD45 family members to cell death suppression by cellular bcl-xL and cytomegalovirus vMIA. J Virol 2005; 79: 14923-14932.
    • (2005) J Virol , vol.79 , pp. 14923-14932
    • Smith, G.1    Mocarski, E.S.2
  • 90
    • 2542629734 scopus 로고    scopus 로고
    • Cytomegalovirus cell death suppressor vMIA blocks Baxbut not Bak-mediated apoptosis by binding and sequestering Bax at mitochondria
    • Arnoult D, Bartle LM, Skaletskaya A, et al. Cytomegalovirus cell death suppressor vMIA blocks Baxbut not Bak-mediated apoptosis by binding and sequestering Bax at mitochondria. Proc Natl Acad Sci USA 2004; 101: 7988-7993.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 7988-7993
    • Arnoult, D.1    Bartle, L.M.2    Skaletskaya, A.3
  • 91
    • 0035913190 scopus 로고    scopus 로고
    • The adenine nucleotide translocator: A target of nitric oxide, peroxynitrite, and 4-hydroxynonenal
    • Vieira HL, Belzacq AS, Haouzi D, et al. The adenine nucleotide translocator: a target of nitric oxide, peroxynitrite, and 4-hydroxynonenal. Oncogene 2001; 20: 4305-4316.
    • (2001) Oncogene , vol.20 , pp. 4305-4316
    • Vieira, H.L.1    Belzacq, A.S.2    Haouzi, D.3
  • 93
    • 0344982847 scopus 로고    scopus 로고
    • Differential function and expression of the viral inhibitor of caspase 8-induced apoptosis (vICA) and the viral mitochondria-localized inhibitor of apoptosis (vMIA) cell death suppressors conserved in primate and rodent cytomegaloviruses
    • McCormick AL, Skaletskaya A, Barry PA, Mocarski ES, Goldmacher VS. Differential function and expression of the viral inhibitor of caspase 8-induced apoptosis (vICA) and the viral mitochondria-localized inhibitor of apoptosis (vMIA) cell death suppressors conserved in primate and rodent cytomegaloviruses. Virology 2003; 316: 221-233.
    • (2003) Virology , vol.316 , pp. 221-233
    • McCormick, A.L.1    Skaletskaya, A.2    Barry, P.A.3    Mocarski, E.S.4    Goldmacher, V.S.5
  • 94
    • 43249095547 scopus 로고    scopus 로고
    • Murine cytomegalovirus m38.5 protein inhibits Bax-mediated cell death
    • Jurak I, Schumacher U, Simic H, Voigt S, Brune W. Murine cytomegalovirus m38.5 protein inhibits Bax-mediated cell death. J Virol 2008; 82: 4812-4822.
    • (2008) J Virol , vol.82 , pp. 4812-4822
    • Jurak, I.1    Schumacher, U.2    Simic, H.3    Voigt, S.4    Brune, W.5
  • 95
    • 45749140887 scopus 로고    scopus 로고
    • Cytomegalovirus proteins vMIA and m38.5 link mitochondrial morphogenesis to Bcl-2 family proteins
    • Norris KL, Youle RJ. Cytomegalovirus proteins vMIA and m38.5 link mitochondrial morphogenesis to Bcl-2 family proteins. J Virol 2008; 82: 6232-6243.
    • (2008) J Virol , vol.82 , pp. 6232-6243
    • Norris, K.L.1    Youle, R.J.2
  • 96
    • 33947399734 scopus 로고    scopus 로고
    • Human cytomegalovirus UL38 protein blocks apoptosis
    • Terhune S, Torigoi E, Moorman N, et al. Human cytomegalovirus UL38 protein blocks apoptosis. J Virol 2007; 81: 3109-3123.
    • (2007) J Virol , vol.81 , pp. 3109-3123
    • Terhune, S.1    Torigoi, E.2    Moorman, N.3
  • 97
    • 41849101685 scopus 로고    scopus 로고
    • Human cytomegalovirus protein UL38 inhibits host cell stress responses by antagonizing the tuberous sclerosis protein complex
    • Moorman NJ, Cristea IM, Terhune SS, Rout MP, Chait BT, Shenk T. Human cytomegalovirus protein UL38 inhibits host cell stress responses by antagonizing the tuberous sclerosis protein complex. Cell Host Microbe 2008; 3: 253-262.
    • (2008) Cell Host Microbe , vol.3 , pp. 253-262
    • Moorman, N.J.1    Cristea, I.M.2    Terhune, S.S.3    Rout, M.P.4    Chait, B.T.5    Shenk, T.6
  • 98
    • 44949139608 scopus 로고    scopus 로고
    • McCormick AL, Roback L, Mocarski ES. HtrA2/Omi terminates cytomegalovirus infection and is controlled by the viral mitochondrial inhibitor of apoptosis (vMIA). PLoS Pathog 2008; 4: e1000063.
    • McCormick AL, Roback L, Mocarski ES. HtrA2/Omi terminates cytomegalovirus infection and is controlled by the viral mitochondrial inhibitor of apoptosis (vMIA). PLoS Pathog 2008; 4: e1000063.
  • 99
    • 30844440999 scopus 로고    scopus 로고
    • HIV-1 protease inhibitors and cytomegalovirus vMIA induce mitochondrial fragmentation without triggering apoptosis
    • Roumier T, Szabadkai G, Simoni AM, et al. HIV-1 protease inhibitors and cytomegalovirus vMIA induce mitochondrial fragmentation without triggering apoptosis. Cell Death Differ 2006; 13: 348-351.
    • (2006) Cell Death Differ , vol.13 , pp. 348-351
    • Roumier, T.1    Szabadkai, G.2    Simoni, A.M.3
  • 101
    • 0027417232 scopus 로고
    • Open reading frames UL44, IRS1/TRS1, and UL36-38 are required for transient complementation of human cytomegalovirus oriLyt-dependent DNA synthesis
    • Pari GS, Kacica MA, Anders DG. Open reading frames UL44, IRS1/TRS1, and UL36-38 are required for transient complementation of human cytomegalovirus oriLyt-dependent DNA synthesis. J Virol 1993; 67: 2575-2582.
    • (1993) J Virol , vol.67 , pp. 2575-2582
    • Pari, G.S.1    Kacica, M.A.2    Anders, D.G.3
  • 102
    • 0028821027 scopus 로고
    • Expression of human cytomegalovirus UL36 and UL37 genes is required for viral DNA replication
    • Smith JA, Pari GS. Expression of human cytomegalovirus UL36 and UL37 genes is required for viral DNA replication. J Virol 1995; 69: 1925-1931.
    • (1995) J Virol , vol.69 , pp. 1925-1931
    • Smith, J.A.1    Pari, G.S.2
  • 103
    • 0029655255 scopus 로고    scopus 로고
    • Four of eleven loci required for transient complementation of human cytomegalovirus DNA replication cooperate to activate expression of replication genes
    • Iskenderian AC, Huang L, Reilly A, Stenberg RM, Anders DG. Four of eleven loci required for transient complementation of human cytomegalovirus DNA replication cooperate to activate expression of replication genes. J Virol 1996; 70: 383-392.
    • (1996) J Virol , vol.70 , pp. 383-392
    • Iskenderian, A.C.1    Huang, L.2    Reilly, A.3    Stenberg, R.M.4    Anders, D.G.5
  • 104
    • 0037431210 scopus 로고    scopus 로고
    • An analysis of the requirements for human cytomegalovirus oriLyt-dependent DNA synthesis in the presence of the herpes simplex virus type 1 replication fork proteins
    • Reid GG, Ellsmore V, Stow ND. An analysis of the requirements for human cytomegalovirus oriLyt-dependent DNA synthesis in the presence of the herpes simplex virus type 1 replication fork proteins. Virology 2003; 308: 303-316.
    • (2003) Virology , vol.308 , pp. 303-316
    • Reid, G.G.1    Ellsmore, V.2    Stow, N.D.3
  • 105
    • 0034953928 scopus 로고    scopus 로고
    • The carboxyl terminus of the human cytomegalovirus UL37 immediate-early glycoprotein is conserved in primary strains and is important for transactivation
    • Hayajneh WA, Contopoulos-Ioannidis DG, Lesperance MM, Venegas AM, Colberg-Poley AM. The carboxyl terminus of the human cytomegalovirus UL37 immediate-early glycoprotein is conserved in primary strains and is important for transactivation. J Gen Virol 2001; 82: 1569-1579.
    • (2001) J Gen Virol , vol.82 , pp. 1569-1579
    • Hayajneh, W.A.1    Contopoulos-Ioannidis, D.G.2    Lesperance, M.M.3    Venegas, A.M.4    Colberg-Poley, A.M.5
  • 106
    • 34247859153 scopus 로고    scopus 로고
    • Ectopic expression of HCMV IE72 and IE86 proteins is sufficient to induce early gene expression but not production of infectious virus in undifferentiated promonocytic THP-1 cells
    • Yee LF, Lin PL, Stinski MF. Ectopic expression of HCMV IE72 and IE86 proteins is sufficient to induce early gene expression but not production of infectious virus in undifferentiated promonocytic THP-1 cells. Virology 2007; 363: 174-188.
    • (2007) Virology , vol.363 , pp. 174-188
    • Yee, L.F.1    Lin, P.L.2    Stinski, M.F.3
  • 107
    • 17444435232 scopus 로고    scopus 로고
    • The acidic domain of pUL37x1 and gpUL37 plays a key role in transactivation of HCMV DNA replication gene promoter constructions
    • Colberg-Poley AM, Huang L, Soltero VE, Iskenderian AC, Schumacher RF, Anders DG. The acidic domain of pUL37x1 and gpUL37 plays a key role in transactivation of HCMV DNA replication gene promoter constructions. Virology 1998; 246: 400-408.
    • (1998) Virology , vol.246 , pp. 400-408
    • Colberg-Poley, A.M.1    Huang, L.2    Soltero, V.E.3    Iskenderian, A.C.4    Schumacher, R.F.5    Anders, D.G.6
  • 108
    • 0033199998 scopus 로고    scopus 로고
    • Human cytomegalovirus US3 gene expression is regulated by a complex network of positive and negative regulators
    • Biegalke BJ. Human cytomegalovirus US3 gene expression is regulated by a complex network of positive and negative regulators. Virology 1999; 261: 155-164.
    • (1999) Virology , vol.261 , pp. 155-164
    • Biegalke, B.J.1
  • 109
    • 0024511734 scopus 로고
    • An assay for circulating antibodies to a major etiologic virus of human non-A, non-B hepatitis
    • Kuo G, Choo QL, Alter HJ, et al. An assay for circulating antibodies to a major etiologic virus of human non-A, non-B hepatitis. Science 1989; 244: 362-364.
    • (1989) Science , vol.244 , pp. 362-364
    • Kuo, G.1    Choo, Q.L.2    Alter, H.J.3
  • 110
    • 0024509701 scopus 로고
    • Isolation of a cDNA clone derived from a blood-borne non-A, non-B viral hepatitis genome
    • Choo QL, Kuo G, Weiner AJ, Overby LR, Bradley DW, Houghton M. Isolation of a cDNA clone derived from a blood-borne non-A, non-B viral hepatitis genome. Science 1989; 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
  • 111
    • 17344381535 scopus 로고    scopus 로고
    • Hepatitis C virus biology
    • Giannini C, Brechot C. Hepatitis C virus biology. Cell Death Differ 2003; 10(Suppl 1): S27-S38.
    • (2003) Cell Death Differ , vol.10 , Issue.SUPPL. 1
    • Giannini, C.1    Brechot, C.2
  • 112
    • 34547094367 scopus 로고    scopus 로고
    • Hepatitis C Virus
    • 5th edn, eds, Wolters Kluwer Health, Lippincott Williams & Wilkins: Philadelphia
    • Lemon S, Walker C, Alter M, Yi M. Hepatitis C Virus. In Fields Virology (5th edn), Vol. I, Knipe DM, Howley PM (eds). Wolters Kluwer Health, Lippincott Williams & Wilkins: Philadelphia, 2007; 1253-1304.
    • (2007) Fields Virology , pp. 1253-1304
    • Lemon, S.1    Walker, C.2    Alter, M.3    Yi, M.4
  • 114
    • 0025968921 scopus 로고
    • Genetic organization and diversity of the hepatitis C virus
    • Choo QL, Richman KH, Han JH, et al. Genetic organization and diversity of the hepatitis C virus. Proc Natl Acad Sci USA 1991; 88: 2451-2455.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 2451-2455
    • Choo, Q.L.1    Richman, K.H.2    Han, J.H.3
  • 115
    • 0026084948 scopus 로고
    • Structure and organization of the hepatitis C virus genome isolated from human carriers
    • Takamizawa A, Mori C, Fuke I, et al. Structure and organization of the hepatitis C virus genome isolated from human carriers. J Virol 1991; 65: 1105-1113.
    • (1991) J Virol , vol.65 , pp. 1105-1113
    • Takamizawa, A.1    Mori, C.2    Fuke, I.3
  • 116
    • 35348925573 scopus 로고    scopus 로고
    • 5th edn, Knipe DM, Howley PM eds, & Wilkins: Philadelphia
    • Gubler D, Kuno G, Markoff L. Flaviviruses. In Fields Virology (5th edn), Vol. 1, Knipe DM, Howley PM (eds). Wolters Kluwer Heatlh, Lippincott Williams & Wilkins: Philadelphia, 2007; 1153-1252.
    • (2007) Fields Virology , vol.1 , pp. 1153-1252
    • Gubler, D.1    Kuno, G.2    Flaviviruses, M.L.3
  • 117
    • 0033880575 scopus 로고    scopus 로고
    • Sequence motifs required for lipid droplet association and protein stability are unique to the hepatitis C virus core protein
    • Hope RG, McLauchlan J. Sequence motifs required for lipid droplet association and protein stability are unique to the hepatitis C virus core protein. J Gen Virol 2000; 81: 1913-1925.
    • (2000) J Gen Virol , vol.81 , pp. 1913-1925
    • Hope, R.G.1    McLauchlan, J.2
  • 118
    • 0036385501 scopus 로고    scopus 로고
    • Phosphorylation of hepatitis C virus core protein by protein kinase A and protein kinase C
    • Lu W, Ou JH. Phosphorylation of hepatitis C virus core protein by protein kinase A and protein kinase C. Virology 2002; 300: 20-30.
    • (2002) Virology , vol.300 , pp. 20-30
    • Lu, W.1    Ou, J.H.2
  • 119
    • 0036809216 scopus 로고    scopus 로고
    • Requirements for signal peptide peptidase-catalyzed intramembrane proteolysis
    • Lemberg MK, Martoglio B. Requirements for signal peptide peptidase-catalyzed intramembrane proteolysis. Mol Cell 2002; 10: 735-744.
    • (2002) Mol Cell , vol.10 , pp. 735-744
    • Lemberg, M.K.1    Martoglio, B.2
  • 120
    • 0037150672 scopus 로고    scopus 로고
    • Identification of signal peptide peptidase, a presenilin-type aspartic protease
    • Weihofen A, Binns K, Lemberg MK, Ashman K, Martoglio B. Identification of signal peptide peptidase, a presenilin-type aspartic protease. Science 2002; 296: 2215-2218.
    • (2002) Science , vol.296 , pp. 2215-2218
    • Weihofen, A.1    Binns, K.2    Lemberg, M.K.3    Ashman, K.4    Martoglio, B.5
  • 121
    • 0030218609 scopus 로고    scopus 로고
    • Characterization of cell lines allowing tightly regulated expression of hepatitis C virus core protein
    • Moradpour D, Englert C, Wakita T, Wands JR. Characterization of cell lines allowing tightly regulated expression of hepatitis C virus core protein. Virology 1996; 222: 51-63.
    • (1996) Virology , vol.222 , pp. 51-63
    • Moradpour, D.1    Englert, C.2    Wakita, T.3    Wands, J.R.4
  • 122
    • 0031780716 scopus 로고    scopus 로고
    • The native form and maturation process of hepatitis C virus core protein
    • Yasui K, Wakita T, Tsukiyama-Kohara K, et al. The native form and maturation process of hepatitis C virus core protein. J Virol 1998; 72: 6048-6055.
    • (1998) J Virol , vol.72 , pp. 6048-6055
    • Yasui, K.1    Wakita, T.2    Tsukiyama-Kohara, K.3
  • 123
    • 0028840840 scopus 로고
    • Differential subcellular localization of hepatitis C virus core gene products
    • Lo SY, Masiarz F, Hwang SB, Lai MM, Ou JH. Differential subcellular localization of hepatitis C virus core gene products. Virology 1995; 213: 455-461.
    • (1995) Virology , vol.213 , pp. 455-461
    • Lo, S.Y.1    Masiarz, F.2    Hwang, S.B.3    Lai, M.M.4    Ou, J.H.5
  • 124
    • 0028131243 scopus 로고
    • Characterization of HCV structural proteins expressed in various animal cells
    • Matsuura Y, Harada T, Makimura M, et al. Characterization of HCV structural proteins expressed in various animal cells. Intervirology 1994; 37: 114-118.
    • (1994) Intervirology , vol.37 , pp. 114-118
    • Matsuura, Y.1    Harada, T.2    Makimura, M.3
  • 125
    • 0031712813 scopus 로고    scopus 로고
    • Moriya K, Fujie H, Shintani Y, et al. The core protein of hepatitis C virus induces hepatocellular carcinoma in transgenic mice. Nat Med 1998; 4: b 1065-1067.
    • Moriya K, Fujie H, Shintani Y, et al. The core protein of hepatitis C virus induces hepatocellular carcinoma in transgenic mice. Nat Med 1998; 4: b 1065-1067.
  • 126
    • 0028304566 scopus 로고
    • Intracellular localization of full-length and truncated hepatitis C virus core protein expressed in mammalian cells
    • Ravaggi A, Natoli G, Primi D, Albertini A, Levrero M, Cariani E. Intracellular localization of full-length and truncated hepatitis C virus core protein expressed in mammalian cells. J Hepatol 1994; 20: 833-836.
    • (1994) J Hepatol , vol.20 , pp. 833-836
    • Ravaggi, A.1    Natoli, G.2    Primi, D.3    Albertini, A.4    Levrero, M.5    Cariani, E.6
  • 127
    • 0035866317 scopus 로고    scopus 로고
    • Hepatitis C virus structural proteins reside in the endoplasmic reticulum as well as in the intermediate compartment/cis-Golgi complex region of stably transfected cells
    • Martire G, Viola A, Iodice L, Lotti LV, Gradini R, Bonatti S. Hepatitis C virus structural proteins reside in the endoplasmic reticulum as well as in the intermediate compartment/cis-Golgi complex region of stably transfected cells. Virology 2001; 280: 176-182.
    • (2001) Virology , vol.280 , pp. 176-182
    • Martire, G.1    Viola, A.2    Iodice, L.3    Lotti, L.V.4    Gradini, R.5    Bonatti, S.6
  • 128
    • 3242673323 scopus 로고    scopus 로고
    • Targeting of hepatitis C virus core protein to mitochondria through a novel C-terminal localization motif
    • Schwer B, Ren S, Pietschmann T, et al. Targeting of hepatitis C virus core protein to mitochondria through a novel C-terminal localization motif. J Virol 2004; 78: 7958-7968.
    • (2004) J Virol , vol.78 , pp. 7958-7968
    • Schwer, B.1    Ren, S.2    Pietschmann, T.3
  • 129
    • 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 MR, et al. Mitochondrial injury, oxidative stress, and antioxidant gene expression are induced by hepatitis C virus core protein. Gastroenterology 2002; 122: 366-375.
    • (2002) Gastroenterology , vol.122 , pp. 366-375
    • Okuda, M.1    Li, K.2    Beard, M.R.3
  • 130
    • 19944428289 scopus 로고    scopus 로고
    • Molecular determinants for subcellular localization of hepatitis C virus core protein
    • Suzuki R, Sakamoto S, Tsutsumi T, et al. Molecular determinants for subcellular localization of hepatitis C virus core protein. J Virol 2005; 79: 1271-1281.
    • (2005) J Virol , vol.79 , pp. 1271-1281
    • Suzuki, R.1    Sakamoto, S.2    Tsutsumi, T.3
  • 131
    • 2642539953 scopus 로고    scopus 로고
    • Intramembrane proteolysis and endoplasmic reticulum retention of hepatitis C virus core protein
    • Okamoto K, Moriishi K, Miyamura T, Matsuura Y. Intramembrane proteolysis and endoplasmic reticulum retention of hepatitis C virus core protein. J Virol 2004; 78: 6370-6380.
    • (2004) J Virol , vol.78 , pp. 6370-6380
    • Okamoto, K.1    Moriishi, K.2    Miyamura, T.3    Matsuura, Y.4
  • 132
    • 58149136255 scopus 로고    scopus 로고
    • Cellular vimentin content regulates the protein level of hepatitis C virus core protein and the hepatitis C virus production in cultured cells
    • Nitahara-Kasahara Y, Fukasawa M, Shinkai-Ouchi F, et al. Cellular vimentin content regulates the protein level of hepatitis C virus core protein and the hepatitis C virus production in cultured cells. Virology 2009; 383: 319-327.
    • (2009) Virology , vol.383 , pp. 319-327
    • Nitahara-Kasahara, Y.1    Fukasawa, M.2    Shinkai-Ouchi, F.3
  • 133
    • 0028233530 scopus 로고
    • Biosynthesis and biochemical properties of the hepatitis C virus core protein
    • Santolini E, Migliaccio G, La Monica N. Biosynthesis and biochemical properties of the hepatitis C virus core protein. J Virol 1994; 68: 3631-3641.
    • (1994) J Virol , vol.68 , pp. 3631-3641
    • Santolini, E.1    Migliaccio, G.2    La Monica, N.3
  • 134
    • 0031957325 scopus 로고    scopus 로고
    • Hepatitis C virus core protein binds to the cytoplasmic domain of tumor necrosis factor (TNF) receptor 1 and enhances TNF-induced apoptosis
    • Zhu N, Khoshnan A, Schneider R, et al. Hepatitis C virus core protein binds to the cytoplasmic domain of tumor necrosis factor (TNF) receptor 1 and enhances TNF-induced apoptosis. J Virol 1998; 72: 3691-3697.
    • (1998) J Virol , vol.72 , pp. 3691-3697
    • Zhu, N.1    Khoshnan, A.2    Schneider, R.3
  • 135
    • 0032504223 scopus 로고    scopus 로고
    • Hepatitis C virus core protein interacts with heterogeneous nuclear ribonucleoprotein K
    • Hsieh TY, Matsumoto M, Chou HC, et al. Hepatitis C virus core protein interacts with heterogeneous nuclear ribonucleoprotein K. J Biol Chem 1998; 273: 17651-17659.
    • (1998) J Biol Chem , vol.273 , pp. 17651-17659
    • Hsieh, T.Y.1    Matsumoto, M.2    Chou, H.C.3
  • 136
    • 0032975740 scopus 로고    scopus 로고
    • Hepatitis C virus core protein interacts with cellular putative RNA helicase
    • You LR, Chen CM, Yeh TS, et al. Hepatitis C virus core protein interacts with cellular putative RNA helicase. J Virol 1999; 73: 2841-2853.
    • (1999) J Virol , vol.73 , pp. 2841-2853
    • You, L.R.1    Chen, C.M.2    Yeh, T.S.3
  • 137
    • 8944262349 scopus 로고    scopus 로고
    • Hepatitis C virus core protein cooperates with ras and transforms primary rat embryo fibroblasts to tumorigenic phenotype
    • Ray RB, Lagging LM, Meyer K, Ray R. Hepatitis C virus core protein cooperates with ras and transforms primary rat embryo fibroblasts to tumorigenic phenotype. J Virol 1996; 70: 4438-4443.
    • (1996) J Virol , vol.70 , pp. 4438-4443
    • Ray, R.B.1    Lagging, L.M.2    Meyer, K.3    Ray, R.4
  • 138
    • 0034651869 scopus 로고    scopus 로고
    • Hepatitis C virus core protein-induced loss of LZIP function correlates with cellular transformation
    • Jin DY, Wang HL, Zhou Y, et al. Hepatitis C virus core protein-induced loss of LZIP function correlates with cellular transformation. EMBO J 2000; 19: 729-740.
    • (2000) EMBO J , vol.19 , pp. 729-740
    • Jin, D.Y.1    Wang, H.L.2    Zhou, Y.3
  • 139
    • 0036717295 scopus 로고    scopus 로고
    • Activation of STAT3 by the hepatitis C virus core protein leads to cellular transformation
    • Yoshida T,Hanada T, Tokuhisa T, et al. Activation of STAT3 by the hepatitis C virus core protein leads to cellular transformation. J Exp Med 2002; 196: 641-653.
    • (2002) J Exp Med , vol.196 , pp. 641-653
    • Yoshida, T.1    Hanada, T.2    Tokuhisa, T.3
  • 140
    • 0031901556 scopus 로고    scopus 로고
    • Hepatitis C virus core from two different genotypes has an oncogenic potential but is not sufficient for transforming primary rat embryo fibroblasts in cooperation with the H-ras oncogene
    • Chang J, Yang SH, Cho YG, Hwang SB, Hahn YS, Sung YC. Hepatitis C virus core from two different genotypes has an oncogenic potential but is not sufficient for transforming primary rat embryo fibroblasts in cooperation with the H-ras oncogene. J Virol 1998; 72: 3060-3065.
    • (1998) J Virol , vol.72 , pp. 3060-3065
    • Chang, J.1    Yang, S.H.2    Cho, Y.G.3    Hwang, S.B.4    Hahn, Y.S.5    Sung, Y.C.6
  • 141
    • 33748376920 scopus 로고    scopus 로고
    • Enhancement of de novo fatty acid biosynthesis in hepatic cell line Huh7 expressing hepatitis C virus core protein
    • Fukasawa M, Tanaka Y, Sato S, et al. Enhancement of de novo fatty acid biosynthesis in hepatic cell line Huh7 expressing hepatitis C virus core protein. Biol Pharm Bull 2006; 29: 1958-1961.
    • (2006) Biol Pharm Bull , vol.29 , pp. 1958-1961
    • Fukasawa, M.1    Tanaka, Y.2    Sato, S.3
  • 142
    • 19444385812 scopus 로고    scopus 로고
    • Metabolic aspects of hepatitis C viral infection: Steatohepatitis resembling but distinct from NASH
    • Koike K, Moriya K. Metabolic aspects of hepatitis C viral infection: steatohepatitis resembling but distinct from NASH. J Gastroenterol 2005; 40: 329-336.
    • (2005) J Gastroenterol , vol.40 , pp. 329-336
    • Koike, K.1    Moriya, K.2
  • 143
    • 23744461982 scopus 로고    scopus 로고
    • Hepatitis C virus core triggers apoptosis in liver cells by inducing ER stress and ER calcium depletion
    • Benali-Furet NL, Chami M, Houel L, et al. Hepatitis C virus core triggers apoptosis in liver cells by inducing ER stress and ER calcium depletion. Oncogene 2005; 24: 4921-4933.
    • (2005) Oncogene , vol.24 , pp. 4921-4933
    • Benali-Furet, N.L.1    Chami, M.2    Houel, L.3
  • 144
    • 0038819966 scopus 로고    scopus 로고
    • The hepatitis C virus core protein modulates T cell responses by inducing spontaneous and altering T-cell receptor-triggered Ca2 oscillations
    • Bergqvist A, Sundstrom S, Dimberg LY, Gylfe E, Masucci MG. The hepatitis C virus core protein modulates T cell responses by inducing spontaneous and altering T-cell receptor-triggered Ca2 oscillations. J Biol Chem 2003; 278: 18877-18883.
    • (2003) J Biol Chem , vol.278 , pp. 18877-18883
    • Bergqvist, A.1    Sundstrom, S.2    Dimberg, L.Y.3    Gylfe, E.4    Masucci, M.G.5
  • 145
    • 1842843854 scopus 로고    scopus 로고
    • hsp70-DnaJ chaperone pair prevents nitric oxide- and CHOP-induced apoptosis by inhibiting translocation of Bax to mitochondria
    • Gotoh T, Terada K, Oyadomari S,MoriM. hsp70-DnaJ chaperone pair prevents nitric oxide- and CHOP-induced apoptosis by inhibiting translocation of Bax to mitochondria. Cell Death Differ 2004; 11: 390-402.
    • (2004) Cell Death Differ , vol.11 , pp. 390-402
    • Gotoh, T.1    Terada, K.2    Oyadomari, S.3    Mori, M.4
  • 146
    • 0035943698 scopus 로고    scopus 로고
    • Synergistic movements of Ca(2+) and Bax in cells undergoing apoptosis
    • Pan Z, Bhat MB, Nieminen AL, Ma J. Synergistic movements of Ca(2+) and Bax in cells undergoing apoptosis. J Biol Chem 2001; 276: 32257-32263.
    • (2001) J Biol Chem , vol.276 , pp. 32257-32263
    • Pan, Z.1    Bhat, M.B.2    Nieminen, A.L.3    Ma, J.4
  • 147
    • 55249099620 scopus 로고    scopus 로고
    • Hepatitis C virus infection induces apoptosis through a Bax-triggered, mitochondrion-mediated, caspase 3-dependent pathway
    • Deng L, Adachi T, Kitayama K, et al. Hepatitis C virus infection induces apoptosis through a Bax-triggered, mitochondrion-mediated, caspase 3-dependent pathway. J Virol 2008; 82: 10375-10385.
    • (2008) J Virol , vol.82 , pp. 10375-10385
    • Deng, L.1    Adachi, T.2    Kitayama, K.3
  • 148
    • 67449157167 scopus 로고    scopus 로고
    • Gene expression profile of Huh-7 cells expressing hepatitis C virus genotype 1b or 3a core proteins
    • Sep 18 [Epub ahead of print
    • Pazienza V, Clement S, Pugnale P, et al. Gene expression profile of Huh-7 cells expressing hepatitis C virus genotype 1b or 3a core proteins. Liver Int 2008 Sep 18 [Epub ahead of print].
    • (2008) Liver Int
    • Pazienza, V.1    Clement, S.2    Pugnale, P.3


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