메뉴 건너뛰기




Volumn 347, Issue 1, 2016, Pages 83-94

Rabies virus matrix protein induces apoptosis by targeting mitochondria

Author keywords

Apoptosis; Matrix protein; Mitochondria; Rabies virus

Indexed keywords

ADENOSINE TRIPHOSPHATE; AMINO ACID; APOPTOSIS INDUCING FACTOR; CASPASE 3; CASPASE 8; CASPASE 9; CYTOCHROME C; LACTATE DEHYDROGENASE; M PROTEIN; MATRIX PROTEIN; PROTEIN BAX; UNCLASSIFIED DRUG; VIRAL PROTEIN; VIRAL PROTEIN N;

EID: 84997610375     PISSN: 00144827     EISSN: 10902422     Source Type: Journal    
DOI: 10.1016/j.yexcr.2016.07.008     Document Type: Article
Times cited : (31)

References (64)
  • 1
    • 0036852215 scopus 로고    scopus 로고
    • To kill or be killed: viral evasion of apoptosis
    • [1] Benedict, C.A., Norris, P.S., Ware, C.F., To kill or be killed: viral evasion of apoptosis. Nat. Immunol. 3:11 (2002), 1013–1018.
    • (2002) Nat. Immunol. , vol.3 , Issue.11 , pp. 1013-1018
    • Benedict, C.A.1    Norris, P.S.2    Ware, C.F.3
  • 2
    • 0032575714 scopus 로고    scopus 로고
    • Death receptors: signaling and modulation
    • [2] Ashkenazi, A., Dixit, V.M., Death receptors: signaling and modulation. Science 281:5381 (1998), 1305–1308.
    • (1998) Science , vol.281 , Issue.5381 , pp. 1305-1308
    • Ashkenazi, A.1    Dixit, V.M.2
  • 3
    • 0042575744 scopus 로고    scopus 로고
    • Mitochondria: regulators of cell death and survival
    • [3] Granville, D.J., Gottlieb, R.A., Mitochondria: regulators of cell death and survival. Sci. World J. 2 (2002), 1569–1578.
    • (2002) Sci. World J. , vol.2 , pp. 1569-1578
    • Granville, D.J.1    Gottlieb, R.A.2
  • 4
    • 0033280669 scopus 로고    scopus 로고
    • Biochemical pathways of caspase activation during apoptosis
    • [4] Budihardjo, I., et al. Biochemical pathways of caspase activation during apoptosis. Annu Rev. Cell Dev. Biol. 15 (1999), 269–290.
    • (1999) Annu Rev. Cell Dev. Biol. , vol.15 , pp. 269-290
    • Budihardjo, I.1
  • 5
    • 84859760175 scopus 로고    scopus 로고
    • Mitochondrial dynamics: Functional link with apoptosis
    • [5] Otera, H., Mihara, K., Mitochondrial dynamics: Functional link with apoptosis. Int. J. Cell Biol., 2012, 2012, 821676.
    • (2012) Int. J. Cell Biol. , vol.2012 , pp. 821676
    • Otera, H.1    Mihara, K.2
  • 6
    • 0035957653 scopus 로고    scopus 로고
    • Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and death
    • [6] Wei, M.C., et al. Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and death. Science 292:5517 (2001), 727–730.
    • (2001) Science , vol.292 , Issue.5517 , pp. 727-730
    • Wei, M.C.1
  • 7
    • 0035928830 scopus 로고    scopus 로고
    • Conformation of the C-terminal domain of the pro-apoptotic protein Bax and mutants and its interaction with membranes
    • [7] del Mar Martinez-Senac, M., Corbalan-Garcia, S., Gomez-Fernandez, J.C., Conformation of the C-terminal domain of the pro-apoptotic protein Bax and mutants and its interaction with membranes. Biochemistry 40:33 (2001), 9983–9992.
    • (2001) Biochemistry , vol.40 , Issue.33 , pp. 9983-9992
    • del Mar Martinez-Senac, M.1    Corbalan-Garcia, S.2    Gomez-Fernandez, J.C.3
  • 8
    • 37549048249 scopus 로고    scopus 로고
    • The BCL-2 protein family: opposing activities that mediate cell death
    • [8] Youle, R.J., Strasser, A., The BCL-2 protein family: opposing activities that mediate cell death. Nat. Rev. Mol. Cell Biol. 9:1 (2008), 47–59.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , Issue.1 , pp. 47-59
    • Youle, R.J.1    Strasser, A.2
  • 9
    • 27544446991 scopus 로고    scopus 로고
    • Life in the balance: how BH3-only proteins induce apoptosis
    • [9] Willis, S.N., Adams, J.M., Life in the balance: how BH3-only proteins induce apoptosis. Curr. Opin. Cell Biol. 17:6 (2005), 617–625.
    • (2005) Curr. Opin. Cell Biol. , vol.17 , Issue.6 , pp. 617-625
    • Willis, S.N.1    Adams, J.M.2
  • 10
    • 84867691699 scopus 로고    scopus 로고
    • Mitochondrial control of cellular life, stress, and death
    • [10] Galluzzi, L., et al. Mitochondrial control of cellular life, stress, and death. Circ. Res. 111:9 (2012), 1198–1207.
    • (2012) Circ. Res. , vol.111 , Issue.9 , pp. 1198-1207
    • Galluzzi, L.1
  • 11
    • 44949151607 scopus 로고    scopus 로고
    • Viral control of mitochondrial apoptosis
    • e1000018-e1000018
    • [11] Galluzzi, L., et al. Viral control of mitochondrial apoptosis. PLoS Pathog., 4(5), 2008 e1000018-e1000018.
    • (2008) PLoS Pathog. , vol.4 , Issue.5
    • Galluzzi, L.1
  • 12
    • 18944390116 scopus 로고    scopus 로고
    • Re-evaluating the burden of rabies in Africa and Asia
    • [12] Knobel, D.L., et al. Re-evaluating the burden of rabies in Africa and Asia. Bull. World Health Organ. 83:5 (2005), 360–368.
    • (2005) Bull. World Health Organ. , vol.83 , Issue.5 , pp. 360-368
    • Knobel, D.L.1
  • 14
    • 0030842595 scopus 로고    scopus 로고
    • Rabies virus infects mouse and human lymphocytes and induces apoptosis
    • [14] Thoulouze, M.I., et al. Rabies virus infects mouse and human lymphocytes and induces apoptosis. J. Virol. 71:10 (1997), 7372–7380.
    • (1997) J. Virol. , vol.71 , Issue.10 , pp. 7372-7380
    • Thoulouze, M.I.1
  • 15
    • 65449161836 scopus 로고    scopus 로고
    • Pathology of the spinal cord of C57BL/6J mice infected with rabies virus (CVS-11 strain)
    • [15] Kojima, D., et al. Pathology of the spinal cord of C57BL/6J mice infected with rabies virus (CVS-11 strain). J. Vet. Med. Sci. 71:3 (2009), 319–324.
    • (2009) J. Vet. Med. Sci. , vol.71 , Issue.3 , pp. 319-324
    • Kojima, D.1
  • 16
    • 0242690437 scopus 로고    scopus 로고
    • Apoptosis and rabies virus neuroinvasion
    • [16] Baloul, L., Lafon, M., Apoptosis and rabies virus neuroinvasion. Biochimie 85:8 (2003), 777–788.
    • (2003) Biochimie , vol.85 , Issue.8 , pp. 777-788
    • Baloul, L.1    Lafon, M.2
  • 17
    • 77957677128 scopus 로고    scopus 로고
    • Lesions of the central nervous system induced by intracerebral inoculation of BALB/c mice with rabies virus (CVS-11)
    • [17] Kojima, D., et al. Lesions of the central nervous system induced by intracerebral inoculation of BALB/c mice with rabies virus (CVS-11). J. Vet. Med. Sci. 72:8 (2010), 1011–1016.
    • (2010) J. Vet. Med. Sci. , vol.72 , Issue.8 , pp. 1011-1016
    • Kojima, D.1
  • 18
    • 77950866191 scopus 로고    scopus 로고
    • Cytotoxicity and inhibition of DNA topoisomerase I of polyhydroxylated triterpenoids and triterpenoid glycosides
    • [18] Wang, P., et al. Cytotoxicity and inhibition of DNA topoisomerase I of polyhydroxylated triterpenoids and triterpenoid glycosides. Bioorg. Med. Chem. Lett. 20:9 (2010), 2790–2796.
    • (2010) Bioorg. Med. Chem. Lett. , vol.20 , Issue.9 , pp. 2790-2796
    • Wang, P.1
  • 19
    • 0032143449 scopus 로고    scopus 로고
    • Rabies virus replication induces Bax-related, caspase dependent apoptosis in mouse neuroblastoma cells
    • [19] Ubol, S., Sukwattanapan, C., Utaisincharoen, P., Rabies virus replication induces Bax-related, caspase dependent apoptosis in mouse neuroblastoma cells. Virus Res. 56:2 (1998), 207–215.
    • (1998) Virus Res. , vol.56 , Issue.2 , pp. 207-215
    • Ubol, S.1    Sukwattanapan, C.2    Utaisincharoen, P.3
  • 20
    • 37349019017 scopus 로고    scopus 로고
    • Structural abnormalities in neurons are sufficient to explain the clinical disease and fatal outcome of experimental rabies in yellow fluorescent protein-expressing transgenic mice
    • [20] Scott, C.A., et al. Structural abnormalities in neurons are sufficient to explain the clinical disease and fatal outcome of experimental rabies in yellow fluorescent protein-expressing transgenic mice. J. Virol. 82:1 (2008), 513–521.
    • (2008) J. Virol. , vol.82 , Issue.1 , pp. 513-521
    • Scott, C.A.1
  • 21
    • 0031858436 scopus 로고    scopus 로고
    • Apoptosis induction in brain during the fixed strain of rabies virus infection correlates with onset and severity of illness
    • [21] Theerasurakarn, S., Ubol, S., Apoptosis induction in brain during the fixed strain of rabies virus infection correlates with onset and severity of illness. J. Neurovirol. 4:4 (1998), 407–414.
    • (1998) J. Neurovirol. , vol.4 , Issue.4 , pp. 407-414
    • Theerasurakarn, S.1    Ubol, S.2
  • 22
    • 0035853811 scopus 로고    scopus 로고
    • Bax is present as a high molecular weight oligomer/complex in the mitochondrial membrane of apoptotic cells
    • [22] Antonsson, B., et al. Bax is present as a high molecular weight oligomer/complex in the mitochondrial membrane of apoptotic cells. J. Biol. Chem. 276:15 (2001), 11615–11623.
    • (2001) J. Biol. Chem. , vol.276 , Issue.15 , pp. 11615-11623
    • Antonsson, B.1
  • 23
    • 0038025230 scopus 로고    scopus 로고
    • Association of Bax and Bak homo-oligomers in mitochondria. Bax requirement for Bak reorganization and cytochrome c release
    • [23] Mikhailov, V., et al. Association of Bax and Bak homo-oligomers in mitochondria. Bax requirement for Bak reorganization and cytochrome c release. J. Biol. Chem. 278:7 (2003), 5367–5376.
    • (2003) J. Biol. Chem. , vol.278 , Issue.7 , pp. 5367-5376
    • Mikhailov, V.1
  • 24
    • 79952221290 scopus 로고    scopus 로고
    • The Rubella virus capsid is an anti-apoptotic protein that attenuates the pore-forming ability of Bax
    • [24] Ilkow, C.S., Goping, I.S., Hobman, T.C., The Rubella virus capsid is an anti-apoptotic protein that attenuates the pore-forming ability of Bax. PLoS Pathog., 7(2), 2011, e1001291.
    • (2011) PLoS Pathog. , vol.7 , Issue.2 , pp. e1001291
    • Ilkow, C.S.1    Goping, I.S.2    Hobman, T.C.3
  • 25
    • 0036124248 scopus 로고    scopus 로고
    • Overexpression of the rabies virus glycoprotein results in enhancement of apoptosis and antiviral immune response
    • [25] Faber, M., et al. Overexpression of the rabies virus glycoprotein results in enhancement of apoptosis and antiviral immune response. J. Virol. 76:7 (2002), 3374–3381.
    • (2002) J. Virol. , vol.76 , Issue.7 , pp. 3374-3381
    • Faber, M.1
  • 26
    • 9844226204 scopus 로고    scopus 로고
    • Caspase-dependent apoptosis of COS-7 cells induced by Bax overexpression: differential effects of Bcl-2 and Bcl-xL on Bax-induced caspase activation and apoptosis
    • [26] Kitanaka, C., et al. Caspase-dependent apoptosis of COS-7 cells induced by Bax overexpression: differential effects of Bcl-2 and Bcl-xL on Bax-induced caspase activation and apoptosis. Oncogene 15:15 (1997), 1763–1772.
    • (1997) Oncogene , vol.15 , Issue.15 , pp. 1763-1772
    • Kitanaka, C.1
  • 27
    • 0035194166 scopus 로고    scopus 로고
    • Matrix protein and another viral component contribute to induction of apoptosis in cells infected with vesicular stomatitis virus
    • [27] Kopecky, S.A., Willingham, M.C., Lyles, D.S., Matrix protein and another viral component contribute to induction of apoptosis in cells infected with vesicular stomatitis virus. J. Virol. 75:24 (2001), 12169–12181.
    • (2001) J. Virol. , vol.75 , Issue.24 , pp. 12169-12181
    • Kopecky, S.A.1    Willingham, M.C.2    Lyles, D.S.3
  • 28
    • 2642566701 scopus 로고    scopus 로고
    • Lyssavirus matrix protein induces apoptosis by a TRAIL-dependent mechanism involving caspase-8 activation
    • [28] Kassis, R., et al. Lyssavirus matrix protein induces apoptosis by a TRAIL-dependent mechanism involving caspase-8 activation. J. Virol. 78:12 (2004), 6543–6555.
    • (2004) J. Virol. , vol.78 , Issue.12 , pp. 6543-6555
    • Kassis, R.1
  • 29
    • 77956866156 scopus 로고    scopus 로고
    • Two overlapping domains of a lyssavirus matrix protein that acts on different cell death pathways
    • [29] Larrous, F., et al. Two overlapping domains of a lyssavirus matrix protein that acts on different cell death pathways. J. Virol. 84:19 (2010), 9897–9906.
    • (2010) J. Virol. , vol.84 , Issue.19 , pp. 9897-9906
    • Larrous, F.1
  • 30
    • 17344368263 scopus 로고    scopus 로고
    • Pathogenicity of different rabies virus variants inversely correlates with apoptosis and rabies virus glycoprotein expression in infected primary neuron cultures
    • [30] Morimoto, K., et al. Pathogenicity of different rabies virus variants inversely correlates with apoptosis and rabies virus glycoprotein expression in infected primary neuron cultures. J. Virol. 73:1 (1999), 510–518.
    • (1999) J. Virol. , vol.73 , Issue.1 , pp. 510-518
    • Morimoto, K.1
  • 31
    • 0031884996 scopus 로고    scopus 로고
    • Apoptotic cell death in experimental rabies in suckling mice
    • [31] Jackson, A.C., Park, H., Apoptotic cell death in experimental rabies in suckling mice. Acta Neuropathol. 95:2 (1998), 159–164.
    • (1998) Acta Neuropathol. , vol.95 , Issue.2 , pp. 159-164
    • Jackson, A.C.1    Park, H.2
  • 32
    • 78650532560 scopus 로고    scopus 로고
    • Amino acids at positions 273 and 394 in rabies virus nucleoprotein are important for both evasion of host RIG-I-mediated antiviral response and pathogenicity
    • [32] Masatani, T., et al. Amino acids at positions 273 and 394 in rabies virus nucleoprotein are important for both evasion of host RIG-I-mediated antiviral response and pathogenicity. Virus Res. 155:1 (2011), 168–174.
    • (2011) Virus Res. , vol.155 , Issue.1 , pp. 168-174
    • Masatani, T.1
  • 33
    • 39749142655 scopus 로고    scopus 로고
    • The glycoprotein and the matrix protein of rabies virus affect pathogenicity by regulating viral replication and facilitating cell-to-cell spread
    • [33] Pulmanausahakul, R., et al. The glycoprotein and the matrix protein of rabies virus affect pathogenicity by regulating viral replication and facilitating cell-to-cell spread. J. Virol. 82:5 (2008), 2330–2338.
    • (2008) J. Virol. , vol.82 , Issue.5 , pp. 2330-2338
    • Pulmanausahakul, R.1
  • 34
    • 52649094943 scopus 로고    scopus 로고
    • PPEY motif within the rabies virus (RV) matrix protein is essential for efficient virion release and RV pathogenicity
    • [34] Wirblich, C., et al. PPEY motif within the rabies virus (RV) matrix protein is essential for efficient virion release and RV pathogenicity. J. Virol. 82:19 (2008), 9730–9738.
    • (2008) J. Virol. , vol.82 , Issue.19 , pp. 9730-9738
    • Wirblich, C.1
  • 35
    • 0242568964 scopus 로고    scopus 로고
    • Glycoprotein of nonpathogenic rabies viruses is a key determinant of human cell apoptosis
    • [35] Prehaud, C., et al. Glycoprotein of nonpathogenic rabies viruses is a key determinant of human cell apoptosis. J. Virol. 77:19 (2003), 10537–10547.
    • (2003) J. Virol. , vol.77 , Issue.19 , pp. 10537-10547
    • Prehaud, C.1
  • 36
    • 0034123026 scopus 로고    scopus 로고
    • Cleavage of BID during cytotoxic drug and UV radiation-induced apoptosis occurs downstream of the point of Bcl-2 action and is catalysed by caspase-3: a potential feedback loop for amplification of apoptosis-associated mitochondrial cytochrome c release
    • [36] Slee, E.A., Keogh, S.A., Martin, S.J., Cleavage of BID during cytotoxic drug and UV radiation-induced apoptosis occurs downstream of the point of Bcl-2 action and is catalysed by caspase-3: a potential feedback loop for amplification of apoptosis-associated mitochondrial cytochrome c release. Cell Death Differ. 7:6 (2000), 556–565.
    • (2000) Cell Death Differ. , vol.7 , Issue.6 , pp. 556-565
    • Slee, E.A.1    Keogh, S.A.2    Martin, S.J.3
  • 37
    • 0035283079 scopus 로고    scopus 로고
    • Activation of caspase-8 in drug-induced apoptosis of B-lymphoid cells is independent of CD95/Fas receptor-ligand interaction and occurs downstream of caspase-3
    • [37] Wieder, T., et al. Activation of caspase-8 in drug-induced apoptosis of B-lymphoid cells is independent of CD95/Fas receptor-ligand interaction and occurs downstream of caspase-3. Blood 97:5 (2001), 1378–1387.
    • (2001) Blood , vol.97 , Issue.5 , pp. 1378-1387
    • Wieder, T.1
  • 38
    • 33748932322 scopus 로고    scopus 로고
    • Rabies virus-induced apoptosis involves caspase-dependent and caspase-independent pathways
    • [38] Sarmento, L., et al. Rabies virus-induced apoptosis involves caspase-dependent and caspase-independent pathways. Virus Res. 121:2 (2006), 144–151.
    • (2006) Virus Res. , vol.121 , Issue.2 , pp. 144-151
    • Sarmento, L.1
  • 39
    • 0035967169 scopus 로고    scopus 로고
    • Essential role of the mitochondrial apoptosis-inducing factor in programmed cell death
    • [39] Joza, N., et al. Essential role of the mitochondrial apoptosis-inducing factor in programmed cell death. Nature 410:6828 (2001), 549–554.
    • (2001) Nature , vol.410 , Issue.6828 , pp. 549-554
    • Joza, N.1
  • 40
    • 0034676090 scopus 로고    scopus 로고
    • Apoptosis control in syncytia induced by the HIV type 1-envelope glycoprotein complex: role of mitochondria and caspases
    • [40] Ferri, K.F., et al. Apoptosis control in syncytia induced by the HIV type 1-envelope glycoprotein complex: role of mitochondria and caspases. J. Exp. Med. 192:8 (2000), 1081–1092.
    • (2000) J. Exp. Med. , vol.192 , Issue.8 , pp. 1081-1092
    • Ferri, K.F.1
  • 41
    • 13844276111 scopus 로고    scopus 로고
    • Early activation of the mitochondrial apoptotic pathway in vesicular stomatitis virus-infected cells
    • [41] Gadaleta, P., et al. Early activation of the mitochondrial apoptotic pathway in vesicular stomatitis virus-infected cells. Virus Res. 109:1 (2005), 65–69.
    • (2005) Virus Res. , vol.109 , Issue.1 , pp. 65-69
    • Gadaleta, P.1
  • 42
    • 0033799242 scopus 로고    scopus 로고
    • Wild-type herpes simplex virus 1 blocks programmed cell death and release of cytochrome c but not the translocation of mitochondrial apoptosis-inducing factor to the nuclei of human embryonic lung fibroblasts
    • [42] Zhou, G., Roizman, B., Wild-type herpes simplex virus 1 blocks programmed cell death and release of cytochrome c but not the translocation of mitochondrial apoptosis-inducing factor to the nuclei of human embryonic lung fibroblasts. J. Virol. 74:19 (2000), 9048–9053.
    • (2000) J. Virol. , vol.74 , Issue.19 , pp. 9048-9053
    • Zhou, G.1    Roizman, B.2
  • 43
    • 67649576965 scopus 로고    scopus 로고
    • Bovine ephemeral fever virus-induced apoptosis requires virus gene expression and activation of Fas and mitochondrial signaling pathway
    • [43] Lin, C.H., et al. Bovine ephemeral fever virus-induced apoptosis requires virus gene expression and activation of Fas and mitochondrial signaling pathway. Apoptosis 14:7 (2009), 864–877.
    • (2009) Apoptosis , vol.14 , Issue.7 , pp. 864-877
    • Lin, C.H.1
  • 44
    • 41149152733 scopus 로고    scopus 로고
    • How do BCL-2 proteins induce mitochondrial outer membrane permeabilization?
    • [44] Chipuk, J.E., Green, D.R., How do BCL-2 proteins induce mitochondrial outer membrane permeabilization?. Trends Cell Biol. 18:4 (2008), 157–164.
    • (2008) Trends Cell Biol. , vol.18 , Issue.4 , pp. 157-164
    • Chipuk, J.E.1    Green, D.R.2
  • 45
    • 55249099620 scopus 로고    scopus 로고
    • Hepatitis C virus infection induces apoptosis through a Bax-triggered, mitochondrion-mediated, caspase 3-dependent pathway
    • [45] Deng, L., et al. Hepatitis C virus infection induces apoptosis through a Bax-triggered, mitochondrion-mediated, caspase 3-dependent pathway. J. Virol. 82:21 (2008), 10375–10385.
    • (2008) J. Virol. , vol.82 , Issue.21 , pp. 10375-10385
    • Deng, L.1
  • 46
    • 0035968079 scopus 로고    scopus 로고
    • West Nile virus-induced bax-dependent apoptosis
    • [46] del Carmen Parquet, M., et al. West Nile virus-induced bax-dependent apoptosis. FEBS Lett. 500:1 (2001), 17–24.
    • (2001) FEBS Lett. , vol.500 , Issue.1 , pp. 17-24
    • del Carmen Parquet, M.1
  • 47
    • 69449099385 scopus 로고    scopus 로고
    • Vesicular stomatitis virus induces apoptosis primarily through Bak rather than Bax by inactivating Mcl-1 and Bcl-XL
    • [47] Pearce, A.F., Lyles, D.S., Vesicular stomatitis virus induces apoptosis primarily through Bak rather than Bax by inactivating Mcl-1 and Bcl-XL. J. Virol. 83:18 (2009), 9102–9112.
    • (2009) J. Virol. , vol.83 , Issue.18 , pp. 9102-9112
    • Pearce, A.F.1    Lyles, D.S.2
  • 48
    • 77952578865 scopus 로고    scopus 로고
    • Viral apoptosis is induced by IRF‐3–mediated activation of Bax
    • [48] Chattopadhyay, S., et al. Viral apoptosis is induced by IRF‐3–mediated activation of Bax. EMBO J. 29:10 (2010), 1762–1773.
    • (2010) EMBO J. , vol.29 , Issue.10 , pp. 1762-1773
    • Chattopadhyay, S.1
  • 49
    • 19944370132 scopus 로고    scopus 로고
    • Identification of the rabies virus alpha/beta interferon antagonist: phosphoprotein P interferes with phosphorylation of interferon regulatory factor 3
    • [49] Brzozka, K., Finke, S., Conzelmann, K.K., Identification of the rabies virus alpha/beta interferon antagonist: phosphoprotein P interferes with phosphorylation of interferon regulatory factor 3. J. Virol. 79:12 (2005), 7673–7681.
    • (2005) J. Virol. , vol.79 , Issue.12 , pp. 7673-7681
    • Brzozka, K.1    Finke, S.2    Conzelmann, K.K.3
  • 50
    • 78650675607 scopus 로고    scopus 로고
    • Genetic dissection of interferon-antagonistic functions of rabies virus phosphoprotein: Inhibition of interferon regulatory factor 3 activation is important for pathogenicity
    • [50] Rieder, M., et al. Genetic dissection of interferon-antagonistic functions of rabies virus phosphoprotein: Inhibition of interferon regulatory factor 3 activation is important for pathogenicity. J. Virol. 85:2 (2011), 842–852.
    • (2011) J. Virol. , vol.85 , Issue.2 , pp. 842-852
    • Rieder, M.1
  • 51
    • 77950501526 scopus 로고    scopus 로고
    • Rabies virus nucleoprotein functions to evade activation of the RIG-I-mediated antiviral response
    • [51] Masatani, T., et al. Rabies virus nucleoprotein functions to evade activation of the RIG-I-mediated antiviral response. J. Virol. 84:8 (2010), 4002–4012.
    • (2010) J. Virol. , vol.84 , Issue.8 , pp. 4002-4012
    • Masatani, T.1
  • 52
    • 31144454896 scopus 로고    scopus 로고
    • Myxoma virus M11L blocks apoptosis through inhibition of conformational activation of Bax at the mitochondria
    • [52] Su, J., et al. Myxoma virus M11L blocks apoptosis through inhibition of conformational activation of Bax at the mitochondria. J. Virol. 80:3 (2006), 1140–1151.
    • (2006) J. Virol. , vol.80 , Issue.3 , pp. 1140-1151
    • Su, J.1
  • 53
    • 79551716137 scopus 로고    scopus 로고
    • Deerpox virus encodes an inhibitor of apoptosis that regulates Bak and Bax
    • [53] Banadyga, L., et al. Deerpox virus encodes an inhibitor of apoptosis that regulates Bak and Bax. J. Virol. 85:5 (2011), 1922–1934.
    • (2011) J. Virol. , vol.85 , Issue.5 , pp. 1922-1934
    • Banadyga, L.1
  • 54
    • 84938414375 scopus 로고    scopus 로고
    • Rabies virus phosphoprotein interacts with mitochondrial Complex I and induces mitochondrial dysfunction and oxidative stress
    • [54] Kammouni, W., et al. Rabies virus phosphoprotein interacts with mitochondrial Complex I and induces mitochondrial dysfunction and oxidative stress. J. Neurovirol., 2015, 1–13.
    • (2015) J. Neurovirol. , pp. 1-13
    • Kammouni, W.1
  • 55
    • 0342905085 scopus 로고    scopus 로고
    • Hepatitis B virus X protein colocalizes to mitochondria with a human voltage-dependent anion channel, HVDAC3, and alters its transmembrane potential
    • [55] Rahmani, Z., et al. Hepatitis B virus X protein colocalizes to mitochondria with a human voltage-dependent anion channel, HVDAC3, and alters its transmembrane potential. J. Virol. 74:6 (2000), 2840–2846.
    • (2000) J. Virol. , vol.74 , Issue.6 , pp. 2840-2846
    • Rahmani, Z.1
  • 56
    • 10044257654 scopus 로고    scopus 로고
    • Mitochondrial targeting sequence of the influenza A virus PB1-F2 protein and its function in mitochondria
    • [56] Yamada, H., et al. Mitochondrial targeting sequence of the influenza A virus PB1-F2 protein and its function in mitochondria. FEBS Lett. 578:3 (2004), 331–336.
    • (2004) FEBS Lett. , vol.578 , Issue.3 , pp. 331-336
    • Yamada, H.1
  • 57
    • 0036385502 scopus 로고    scopus 로고
    • Avian encephalomyelitis virus induces apoptosis via major structural protein VP3
    • [57] Liu, J., Wei, T., Kwang, J., Avian encephalomyelitis virus induces apoptosis via major structural protein VP3. Virology 300:1 (2002), 39–49.
    • (2002) Virology , vol.300 , Issue.1 , pp. 39-49
    • Liu, J.1    Wei, T.2    Kwang, J.3
  • 58
    • 84867425710 scopus 로고    scopus 로고
    • Rotaviral enterotoxin nonstructural protein 4 targets mitochondria for activation of apoptosis during infection
    • [58] Bhowmick, R., et al. Rotaviral enterotoxin nonstructural protein 4 targets mitochondria for activation of apoptosis during infection. J. Biol. Chem. 287:42 (2012), 35004–35020.
    • (2012) J. Biol. Chem. , vol.287 , Issue.42 , pp. 35004-35020
    • Bhowmick, R.1
  • 59
    • 77953445303 scopus 로고    scopus 로고
    • Sequencing of complete genome of rabies virus CVS-11 strain
    • [59] WANG, L., CAO, S.-c, Du, J.-l, Sequencing of complete genome of rabies virus CVS-11 strain. Chin. J. Biol., 5, 2010, 005.
    • (2010) Chin. J. Biol. , vol.5 , pp. 005
    • WANG, L.1    CAO, S.-C.2    Du, J.-L.3
  • 60
    • 0025392013 scopus 로고
    • Monoclonal antibody studies of rabies viruses isolated from Thailand
    • [60] Thongcharoen, P., et al. Monoclonal antibody studies of rabies viruses isolated from Thailand. Southeast Asian J. Trop. Med. Public Health 21:1 (1990), 129–133.
    • (1990) Southeast Asian J. Trop. Med. Public Health , vol.21 , Issue.1 , pp. 129-133
    • Thongcharoen, P.1
  • 61
    • 43249084547 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in lyssavirus-induced apoptosis
    • [61] Gholami, A., et al. Mitochondrial dysfunction in lyssavirus-induced apoptosis. J. Virol. 82:10 (2008), 4774–4784.
    • (2008) J. Virol. , vol.82 , Issue.10 , pp. 4774-4784
    • Gholami, A.1
  • 62
    • 33750231542 scopus 로고    scopus 로고
    • Matrix protein of Vesicular stomatitis virus harbours a cryptic mitochondrial-targeting motif
    • [62] Lichty, B.D., et al. Matrix protein of Vesicular stomatitis virus harbours a cryptic mitochondrial-targeting motif. J. Gen. Virol. 87:11 (2006), 3379–3384.
    • (2006) J. Gen. Virol. , vol.87 , Issue.11 , pp. 3379-3384
    • Lichty, B.D.1
  • 63
    • 0033761842 scopus 로고    scopus 로고
    • The matrix protein of vesicular stomatitis virus inhibits nucleocytoplasmic transport when it is in the nucleus and associated with nuclear pore complexes
    • [63] Petersen, J.M., et al. The matrix protein of vesicular stomatitis virus inhibits nucleocytoplasmic transport when it is in the nucleus and associated with nuclear pore complexes. Mol. Cell. Biol. 20:22 (2000), 8590–8601.
    • (2000) Mol. Cell. Biol. , vol.20 , Issue.22 , pp. 8590-8601
    • Petersen, J.M.1
  • 64
    • 84903469577 scopus 로고    scopus 로고
    • Vesiculoviral matrix (M) protein occupies nucleic acid binding site at nucleoporin pair (Rae1* Nup98)
    • [64] Quan, B., et al. Vesiculoviral matrix (M) protein occupies nucleic acid binding site at nucleoporin pair (Rae1* Nup98). Proc. Natl. Acad. Sci. USA 111:25 (2014), 9127–9132.
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , Issue.25 , pp. 9127-9132
    • Quan, B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.