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Volumn 23, Issue 7, 2000, Pages 284-290

Altruistic cell suicide and the specialized case of the virus-infected nervous system

Author keywords

[No Author keywords available]

Indexed keywords

APOPTOSIS; CELL DEATH; HUMAN; NERVOUS SYSTEM INFLAMMATION; PERSISTENT VIRUS INFECTION; PRIORITY JOURNAL; REVIEW; VIRUS INFECTION; VIRUS INHIBITION; VIRUS REPLICATION;

EID: 0034237303     PISSN: 01662236     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-2236(00)01591-5     Document Type: Note
Times cited : (45)

References (77)
  • 1
    • 0002171705 scopus 로고    scopus 로고
    • Cellular interactions that regulate programmed cell death in the developing vertebrate nervous system
    • V. Koliatsos, & R.R. Ratan. Humana Press
    • Burek M.J., Oppenheim R.W. Cellular interactions that regulate programmed cell death in the developing vertebrate nervous system. Koliatsos V., Ratan R.R. Cell Death and Diseases of the Nervous System. 1998;145-179 Humana Press.
    • (1998) Cell Death and Diseases of the Nervous System , pp. 145-179
    • Burek, M.J.1    Oppenheim, R.W.2
  • 2
    • 0022398502 scopus 로고
    • Slow, persistent replication of lentiviruses: Role of tissue macrophages and macrophage precursors in bone marrow
    • Gendelman H.E.et al. Slow, persistent replication of lentiviruses. role of tissue macrophages and macrophage precursors in bone marrow Proc. Natl. Acad. Sci. U. S. A. 82:1985;7086-7090.
    • (1985) Proc. Natl. Acad. Sci. U. S. A. , vol.82 , pp. 7086-7090
    • Gendelman, H.E.1
  • 3
    • 0029079852 scopus 로고
    • Induction of MHC class I genes in neurones
    • Neumann H.et al. Induction of MHC class I genes in neurones. Science. 269:1995;549-552.
    • (1995) Science , vol.269 , pp. 549-552
    • Neumann, H.1
  • 4
    • 0342460565 scopus 로고    scopus 로고
    • Transneuronal spread of Semliki Forest virus in the developing mouse olfactory system is determined by neuronal maturity
    • Oliver K.R., Fazakerley J.K. Transneuronal spread of Semliki Forest virus in the developing mouse olfactory system is determined by neuronal maturity. Neuroscience. 82:1998;867-877.
    • (1998) Neuroscience , vol.82 , pp. 867-877
    • Oliver, K.R.1    Fazakerley, J.K.2
  • 5
    • 0031855304 scopus 로고    scopus 로고
    • Virus infection induces neuronal apoptosis: A comparison with trophic factor withdrawal
    • Allsopp T.E.et al. Virus infection induces neuronal apoptosis. a comparison with trophic factor withdrawal Cell Death Differ. 5:1998;50-59.
    • (1998) Cell Death Differ. , vol.5 , pp. 50-59
    • Allsopp, T.E.1
  • 6
    • 0030994226 scopus 로고    scopus 로고
    • Apoptosis plays an important role in experimental rabies virus infection
    • Jackson A.C., Rossiter J.P. Apoptosis plays an important role in experimental rabies virus infection. J. Virol. 71:1997;5603-5607.
    • (1997) J. Virol. , vol.71 , pp. 5603-5607
    • Jackson, A.C.1    Rossiter, J.P.2
  • 7
    • 0030825748 scopus 로고    scopus 로고
    • Regulators of apoptosis on the road to persistent alphavirus infection
    • Griffin D.E., Hardwick J.M. Regulators of apoptosis on the road to persistent alphavirus infection. Annu. Rev. Microbiol. 51:1997;565-592.
    • (1997) Annu. Rev. Microbiol. , vol.51 , pp. 565-592
    • Griffin, D.E.1    Hardwick, J.M.2
  • 8
    • 0031726882 scopus 로고    scopus 로고
    • A review of alphavirus replication in neurones
    • Griffin D.E. A review of alphavirus replication in neurones. Neurosci. Biobehav. Rev. 22:1998;721-723.
    • (1998) Neurosci. Biobehav. Rev. , vol.22 , pp. 721-723
    • Griffin, D.E.1
  • 9
    • 0032819096 scopus 로고    scopus 로고
    • The molecular pathogenesis of Semliki Forest virus: A model made useful
    • Atkins G.J.et al. The molecular pathogenesis of Semliki Forest virus. a model made useful J. Gen. Virol. 80:1999;2287-2297.
    • (1999) J. Gen. Virol. , vol.80 , pp. 2287-2297
    • Atkins, G.J.1
  • 10
    • 0031660130 scopus 로고    scopus 로고
    • The Semliki Forest virus vector induces p53-independent apoptosis
    • Glasgow G.M.et al. The Semliki Forest virus vector induces p53-independent apoptosis. J. Gen. Virol. 79:1998;2405-2410.
    • (1998) J. Gen. Virol. , vol.79 , pp. 2405-2410
    • Glasgow, G.M.1
  • 11
    • 2642706678 scopus 로고    scopus 로고
    • The transmembrane domains of Sindbis virus envelope glycoproteins induce cell death
    • Joe A.K.et al. The transmembrane domains of Sindbis virus envelope glycoproteins induce cell death. J. Virol. 72:1998;3935-3943.
    • (1998) J. Virol. , vol.72 , pp. 3935-3943
    • Joe, A.K.1
  • 12
    • 0032710836 scopus 로고    scopus 로고
    • Induction of apoptosis by Sindbis virus occurs at cell entry and does not require virus replication
    • Jan J.-T., Griffin D.E. Induction of apoptosis by Sindbis virus occurs at cell entry and does not require virus replication. J. Virol. 73:1999;10296-10302.
    • (1999) J. Virol. , vol.73 , pp. 10296-10302
    • Jan, J.-T.1    Griffin, D.E.2
  • 13
    • 1842456916 scopus 로고    scopus 로고
    • Inactivation of BCL2 results in progressive degeneration of motoneurones, sympathetic and sensory neurones during early postnatal development
    • Michaelidis T.M.et al. Inactivation of BCL2 results in progressive degeneration of motoneurones, sympathetic and sensory neurones during early postnatal development. Neuron. 17:1996;75-89.
    • (1996) Neuron , vol.17 , pp. 75-89
    • Michaelidis, T.M.1
  • 14
    • 0028922885 scopus 로고
    • Massive cell death of immature hematopoietic cells and neurones in bcl-x-deficient mice
    • Motoyama N.et al. Massive cell death of immature hematopoietic cells and neurones in bcl-x-deficient mice. Science. 267:1995;1506-1510.
    • (1995) Science , vol.267 , pp. 1506-1510
    • Motoyama, N.1
  • 15
    • 0028859541 scopus 로고
    • Bax-deficient mice with lymphoid hyperplasia and male germ cell death
    • Knudson C.M.et al. Bax-deficient mice with lymphoid hyperplasia and male germ cell death. Science. 270:1995;96-99.
    • (1995) Science , vol.270 , pp. 96-99
    • Knudson, C.M.1
  • 16
    • 0029956641 scopus 로고    scopus 로고
    • Decreased apoptosis in the brain and premature lethality in CPP32-deficient mice
    • Kuida K.et al. Decreased apoptosis in the brain and premature lethality in CPP32-deficient mice. Nature. 384:1996;368-372.
    • (1996) Nature , vol.384 , pp. 368-372
    • Kuida, K.1
  • 17
    • 0032493910 scopus 로고    scopus 로고
    • Reduced apoptosis and cytochrome-C-mediated caspase activation in mice lacking caspase 9
    • Kuida K.et al. Reduced apoptosis and cytochrome-C-mediated caspase activation in mice lacking caspase 9. Cell. 94:1998;325-337.
    • (1998) Cell , vol.94 , pp. 325-337
    • Kuida, K.1
  • 18
    • 0032493870 scopus 로고    scopus 로고
    • Differential requirement for caspase 9 in apoptotic pathways in vivo
    • Hakem R.et al. Differential requirement for caspase 9 in apoptotic pathways in vivo. Cell. 94:1998;339-352.
    • (1998) Cell , vol.94 , pp. 339-352
    • Hakem, R.1
  • 19
    • 0032575688 scopus 로고    scopus 로고
    • The BCL2 protein family: Arbiters of cell survival
    • Adams J.M., Cory S. The BCL2 protein family. arbiters of cell survival Science. 281:1998;1322-1326.
    • (1998) Science , vol.281 , pp. 1322-1326
    • Adams, J.M.1    Cory, S.2
  • 20
    • 0028797781 scopus 로고
    • The role of the dsRNA-activated kinase, PKR, in signal transduction
    • Williams B.R.G. The role of the dsRNA-activated kinase, PKR, in signal transduction. Semin. Virol. 6:1995;191-202.
    • (1995) Semin. Virol. , vol.6 , pp. 191-202
    • Williams, B.R.G.1
  • 21
    • 0032488661 scopus 로고    scopus 로고
    • BCL-XL cooperatively associates with the bap31 complex in the endoplasmic reticulum dependent on procaspase 8 and ced-4 adaptor
    • Ng F.W.H., Shore G.C. BCL-XL cooperatively associates with the bap31 complex in the endoplasmic reticulum dependent on procaspase 8 and ced-4 adaptor. J. Biol. Chem. 273:1998;3140-3143.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3140-3143
    • Ng, F.W.H.1    Shore, G.C.2
  • 22
    • 0031464542 scopus 로고    scopus 로고
    • Induction of TNF-sensitive cellular phenotype by c-Myc involves p53 and impaired NF-kappaB activation
    • Klefstrom J.et al. Induction of TNF-sensitive cellular phenotype by c-Myc involves p53 and impaired NF-kappaB activation. EMBO J. 16:1997;7382-7392.
    • (1997) EMBO J. , vol.16 , pp. 7382-7392
    • Klefstrom, J.1
  • 23
    • 0032577979 scopus 로고    scopus 로고
    • Suppression of steady-state, but not stimulus-induced NF-kappa B activity inhibits alphavirus-induced apoptosis
    • Lin K.I.et al. Suppression of steady-state, but not stimulus-induced NF-kappa B activity inhibits alphavirus-induced apoptosis. J. Cell Biol. 141:1998;1479-1487.
    • (1998) J. Cell Biol. , vol.141 , pp. 1479-1487
    • Lin, K.I.1
  • 24
    • 0032501426 scopus 로고    scopus 로고
    • Acute infection of Sindbis virus induces phosphorylation and intracellular translocation of small heat shock protein HSP27 and activation of p38 MAP kinase signaling pathway
    • Nakatsue T.et al. Acute infection of Sindbis virus induces phosphorylation and intracellular translocation of small heat shock protein HSP27 and activation of p38 MAP kinase signaling pathway. Biochem. Biophys. Res. Commun. 253:1998;59-64.
    • (1998) Biochem. Biophys. Res. Commun. , vol.253 , pp. 59-64
    • Nakatsue, T.1
  • 25
    • 0027532285 scopus 로고
    • Conversion of lytic to persistent alphavirus infection by the BCL2 cellular oncogene
    • Levine B.et al. Conversion of lytic to persistent alphavirus infection by the BCL2 cellular oncogene. Nature. 361:1993;739-742.
    • (1993) Nature , vol.361 , pp. 739-742
    • Levine, B.1
  • 26
    • 0029664298 scopus 로고    scopus 로고
    • BCL2 protects mice against fatal alphavirus encephalitis
    • Levine B.et al. BCL2 protects mice against fatal alphavirus encephalitis. Proc. Natl. Acad. Sci. U. S. A. 93:1996;4810-4815.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 4810-4815
    • Levine, B.1
  • 27
    • 0031974917 scopus 로고    scopus 로고
    • Sindbis virus induces apoptosis through a caspase-dependent crmA-sensitive pathway
    • Levine B.et al. Sindbis virus induces apoptosis through a caspase-dependent crmA-sensitive pathway. J. Virol. 72:1998;452-459.
    • (1998) J. Virol. , vol.72 , pp. 452-459
    • Levine, B.1
  • 28
    • 0028234786 scopus 로고
    • Neurovirulent strains of alphavirus induce apoptosis in BCL2- expressing cells - Role of a single amino-acid change in the E2 glycoprotein
    • Ubol S.et al. Neurovirulent strains of alphavirus induce apoptosis in BCL2- expressing cells - role of a single amino-acid change in the E2 glycoprotein. Proc. Natl. Acad. Sci. U. S. A. 91:1994;5202-5206.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 5202-5206
    • Ubol, S.1
  • 29
    • 0031034802 scopus 로고    scopus 로고
    • BCL2 acts early to restrict Semliki Forest virus replication and delays virus-induced programmed cell death
    • Scallan M.F. BCL2 acts early to restrict Semliki Forest virus replication and delays virus-induced programmed cell death. J. Virol. 71:1997;1583-1590.
    • (1997) J. Virol. , vol.71 , pp. 1583-1590
    • Scallan, M.F.1
  • 30
    • 0031974917 scopus 로고    scopus 로고
    • Sindbis virus induces apoptosis through a caspase-dependent, CrmA-sensitive pathway
    • Nava V.E.et al. Sindbis virus induces apoptosis through a caspase-dependent, CrmA-sensitive pathway. J. Virol. 72:1998;452-459.
    • (1998) J. Virol. , vol.72 , pp. 452-459
    • Nava, V.E.1
  • 31
    • 0032473496 scopus 로고    scopus 로고
    • Alphaviruses induce apoptosis in BCL2-overexpressing cells: Evidence for a caspase-mediated, proteolytic inactivation of BCL2
    • Grandgirard D.et al. Alphaviruses induce apoptosis in BCL2-overexpressing cells. evidence for a caspase-mediated, proteolytic inactivation of BCL2 EMBO J. 17:1998;1268-1278.
    • (1998) EMBO J. , vol.17 , pp. 1268-1278
    • Grandgirard, D.1
  • 32
    • 0001488499 scopus 로고    scopus 로고
    • Protection against fatal Sindbis virus encephalitis by Beclin, a novel BCL2-interacting protein
    • Liang X.H.et al. Protection against fatal Sindbis virus encephalitis by Beclin, a novel BCL2-interacting protein. J. Virol. 72:1998;8586-8596.
    • (1998) J. Virol. , vol.72 , pp. 8586-8596
    • Liang, X.H.1
  • 33
    • 0031465443 scopus 로고    scopus 로고
    • Conversion of BCL2 to a bax-like death effector by caspases
    • Cheng E.H.et al. Conversion of BCL2 to a bax-like death effector by caspases. Science. 278:1997;1966-1968.
    • (1997) Science , vol.278 , pp. 1966-1968
    • Cheng, E.H.1
  • 34
    • 0033597785 scopus 로고    scopus 로고
    • Caspase 3 dependent cleavage of BCL2 promotes release of cytochrome-C
    • Kirsch D.G.et al. Caspase 3 dependent cleavage of BCL2 promotes release of cytochrome-C. J. Biol. Chem. 274:1999;21155-21161.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21155-21161
    • Kirsch, D.G.1
  • 35
    • 0032517786 scopus 로고    scopus 로고
    • P53 is essential for developmental neuron death as regulated by the TrkA and p75 neurotrophin receptors
    • Aloyz R.S.et al. P53 is essential for developmental neuron death as regulated by the TrkA and p75 neurotrophin receptors. J. Cell Biol. 143:1998;1691-1703.
    • (1998) J. Cell Biol. , vol.143 , pp. 1691-1703
    • Aloyz, R.S.1
  • 36
    • 0032032404 scopus 로고    scopus 로고
    • Role of the jun kinase pathway in the regulation of c-jun expression and apoptosis in sympathetic neurons
    • Eilers A.et al. Role of the jun kinase pathway in the regulation of c-jun expression and apoptosis in sympathetic neurons. J. Neurosci. 18:1998;1713-1724.
    • (1998) J. Neurosci. , vol.18 , pp. 1713-1724
    • Eilers, A.1
  • 37
    • 0033103344 scopus 로고    scopus 로고
    • Fas/Apo-1 and associated proteins in the differentiating cerebral cortex: Induction of caspase-dependent cell death and activation of NF-kappaB
    • Cheema Z.F.et al. Fas/Apo-1 and associated proteins in the differentiating cerebral cortex. induction of caspase-dependent cell death and activation of NF-kappaB J. Neurosci. 19:1999;1754-1770.
    • (1999) J. Neurosci. , vol.19 , pp. 1754-1770
    • Cheema, Z.F.1
  • 38
    • 0032520195 scopus 로고    scopus 로고
    • Widespread elimination of naturally occurring neuronal death in bax-deficient mice
    • White F.A.et al. Widespread elimination of naturally occurring neuronal death in bax-deficient mice. J. Neurosci. 18:1998;1428-1439.
    • (1998) J. Neurosci. , vol.18 , pp. 1428-1439
    • White, F.A.1
  • 39
    • 0029990550 scopus 로고    scopus 로고
    • Immunohistochemical analysis of in vivo patterns of Bak expression, a proapoptotic member of the Bcl-2 protein family
    • Krajewski S.et al. Immunohistochemical analysis of in vivo patterns of Bak expression, a proapoptotic member of the Bcl-2 protein family. Cancer Res. 56:1996;2849-2855.
    • (1996) Cancer Res. , vol.56 , pp. 2849-2855
    • Krajewski, S.1
  • 40
    • 0033535976 scopus 로고    scopus 로고
    • Characterization of the cell death promoter, Bad, in the developing rat retina and forebrain
    • Rickman D.W.et al. Characterization of the cell death promoter, Bad, in the developing rat retina and forebrain. Dev. Brain Res. 115:1999;41-47.
    • (1999) Dev. Brain Res. , vol.115 , pp. 41-47
    • Rickman, D.W.1
  • 41
    • 0032080197 scopus 로고    scopus 로고
    • Defects in regulation of apoptosis in caspase-2-deficient mice
    • Bergeron L.et al. Defects in regulation of apoptosis in caspase-2-deficient mice. Genes Dev. 12:1998;1304-1314.
    • (1998) Genes Dev. , vol.12 , pp. 1304-1314
    • Bergeron, L.1
  • 42
    • 0029915857 scopus 로고    scopus 로고
    • Loss of the p53 tumor suppressor gene protects neurons from kainate-induced cell death
    • Morrison R.S.et al. Loss of the p53 tumor suppressor gene protects neurons from kainate-induced cell death. J. Neurosci. 16:1996;1337-1345.
    • (1996) J. Neurosci. , vol.16 , pp. 1337-1345
    • Morrison, R.S.1
  • 43
    • 0029086989 scopus 로고
    • The role of free radicals and p53 in neuron apoptosis in vivo
    • Wood K.A.et al. The role of free radicals and p53 in neuron apoptosis in vivo. J. Neurosci. 15:1995;5851-5857.
    • (1995) J. Neurosci. , vol.15 , pp. 5851-5857
    • Wood, K.A.1
  • 44
    • 0030780804 scopus 로고    scopus 로고
    • Absence of excitotoxicity-induced apoptosis in the hippocampus of mice lacking the Jnk3 gene
    • Yang D.D.et al. Absence of excitotoxicity-induced apoptosis in the hippocampus of mice lacking the Jnk3 gene. Nature. 389:1997;865-870.
    • (1997) Nature , vol.389 , pp. 865-870
    • Yang, D.D.1
  • 45
    • 0029918952 scopus 로고    scopus 로고
    • Apoptosis and c-Jun in the thalamus of the rat following cortical infarction
    • Soriano M.A.et al. Apoptosis and c-Jun in the thalamus of the rat following cortical infarction. NeuroReport. 7:1996;425-428.
    • (1996) NeuroReport , vol.7 , pp. 425-428
    • Soriano, M.A.1
  • 46
    • 0033593608 scopus 로고    scopus 로고
    • Free radical scavenger OPC-14117 attenuates quinolinic acid-induced NF-kappaB activation and apoptosis in rat striatum
    • Nakai M.et al. Free radical scavenger OPC-14117 attenuates quinolinic acid-induced NF-kappaB activation and apoptosis in rat striatum. Mol. Brain Res. 64:1999;59-68.
    • (1999) Mol. Brain Res. , vol.64 , pp. 59-68
    • Nakai, M.1
  • 47
    • 0033562658 scopus 로고    scopus 로고
    • CD95 ligand (Fas-L/Apo-1L) and tumor necrosis factor-related apoptosis-inducing ligand mediate ischemia-induced apoptosis in neurons
    • Martin-Villalba A.et al. CD95 ligand (Fas-L/Apo-1L) and tumor necrosis factor-related apoptosis-inducing ligand mediate ischemia-induced apoptosis in neurons. J. Neurosci. 19:1999;3809-3817.
    • (1999) J. Neurosci. , vol.19 , pp. 3809-3817
    • Martin-Villalba, A.1
  • 48
    • 0033535771 scopus 로고    scopus 로고
    • Reciprocal changes in the expression of Bcl-2 and Bax in hypoglossal nucleus after axotomy in adult rats: Possible involvement in the induction of neuronal cell death
    • Baba N.et al. Reciprocal changes in the expression of Bcl-2 and Bax in hypoglossal nucleus after axotomy in adult rats. possible involvement in the induction of neuronal cell death Brain Res. 827:1999;122-129.
    • (1999) Brain Res. , vol.827 , pp. 122-129
    • Baba, N.1
  • 49
    • 0032862513 scopus 로고    scopus 로고
    • Upregulation of bax protein and increased DNA degradation in ALS spinal cord motor neurons
    • Ekegren T.et al. Upregulation of bax protein and increased DNA degradation in ALS spinal cord motor neurons. Acta Neurol. Scand. 100:1999;317-321.
    • (1999) Acta Neurol. Scand. , vol.100 , pp. 317-321
    • Ekegren, T.1
  • 50
    • 0028973310 scopus 로고
    • Upregulation of bax protein levels in neurons following cerebral ischemia
    • Krajewski S.et al. Upregulation of bax protein levels in neurons following cerebral ischemia. J. Neurosci. 15:1995;6364-6376.
    • (1995) J. Neurosci. , vol.15 , pp. 6364-6376
    • Krajewski, S.1
  • 51
    • 0031983648 scopus 로고    scopus 로고
    • Differential regulation of Bax, Bcl-2, and Bcl-X proteins in focal cortical ischemia in the rat
    • Isenmann S.et al. Differential regulation of Bax, Bcl-2, and Bcl-X proteins in focal cortical ischemia in the rat. Brain Pathol. 8:1998;49-62.
    • (1998) Brain Pathol. , vol.8 , pp. 49-62
    • Isenmann, S.1
  • 52
    • 0033537768 scopus 로고    scopus 로고
    • 2+ induced apoptosis through calcineurin dephosphorylation of BAD
    • 2+ induced apoptosis through calcineurin dephosphorylation of BAD. Science. 284:1999;339-343.
    • (1999) Science , vol.284 , pp. 339-343
    • Wang, H.G.1
  • 53
    • 0345049629 scopus 로고    scopus 로고
    • Inhibition of ICE slows ALS in mice
    • Friedlander R.M.et al. Inhibition of ICE slows ALS in mice. Nature. 388:1997;31.
    • (1997) Nature , vol.388 , pp. 31
    • Friedlander, R.M.1
  • 54
    • 0033587128 scopus 로고    scopus 로고
    • Inhibition of caspase-1 slows disease progression in a mouse model of Huntington's disease
    • Ona V.O.et al. Inhibition of caspase-1 slows disease progression in a mouse model of Huntington's disease. Nature. 399:1999;263-267.
    • (1999) Nature , vol.399 , pp. 263-267
    • Ona, V.O.1
  • 55
    • 0033565587 scopus 로고    scopus 로고
    • Caspase 8 and caspase 3 are expressed by different populations of cortical neurons undergoing delayed cell death after focal stroke in the rat
    • Velier J.L.et al. Caspase 8 and caspase 3 are expressed by different populations of cortical neurons undergoing delayed cell death after focal stroke in the rat. J. Neurosci. 19:1999;5932-5941.
    • (1999) J. Neurosci. , vol.19 , pp. 5932-5941
    • Velier, J.L.1
  • 56
    • 0032950235 scopus 로고    scopus 로고
    • Increases in bcl-2 and cleavage of caspase 1 and caspase 3 in human brain after head injury
    • Clark R.S.B.et al. Increases in bcl-2 and cleavage of caspase 1 and caspase 3 in human brain after head injury. FASEB J. 13:1999;813-821.
    • (1999) FASEB J. , vol.13 , pp. 813-821
    • Clark, R.S.B.1
  • 57
    • 0033617402 scopus 로고    scopus 로고
    • Involvement of caspases in proteolytic cleavage of Alzheimer's amyloid-β precursor protein and amyloidogenic Aβ peptide formation
    • Gervais F.G.et al. Involvement of caspases in proteolytic cleavage of Alzheimer's amyloid-β precursor protein and amyloidogenic Aβ peptide formation. Cell. 97:1999;395-406.
    • (1999) Cell , vol.97 , pp. 395-406
    • Gervais, F.G.1
  • 58
    • 0033103523 scopus 로고    scopus 로고
    • Caspase 8 is required for cell death induced by expanded polyglutamine repeats
    • Sanchez I.et al. Caspase 8 is required for cell death induced by expanded polyglutamine repeats. Neuron. 22:1999;623-633.
    • (1999) Neuron , vol.22 , pp. 623-633
    • Sanchez, I.1
  • 59
    • 13044305983 scopus 로고    scopus 로고
    • Release of caspase-9 from mitochondria during neuronal apoptosis and cerebral ischemia
    • Krajewski S.et al. Release of caspase-9 from mitochondria during neuronal apoptosis and cerebral ischemia. Proc. Natl. Acad. Sci. U. S. A. 96:1999;5752-5757.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 5752-5757
    • Krajewski, S.1
  • 60
    • 0032548919 scopus 로고    scopus 로고
    • Murine caspase 11, an ICE-interacting protease, is essential for the activation of ICE
    • Wang S.et al. Murine caspase 11, an ICE-interacting protease, is essential for the activation of ICE. Cell. 92:1998;501-509.
    • (1998) Cell , vol.92 , pp. 501-509
    • Wang, S.1
  • 61
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta
    • Nakagawa T.et al. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature. 403:1999;98-103.
    • (1999) Nature , vol.403 , pp. 98-103
    • Nakagawa, T.1
  • 62
    • 0031438851 scopus 로고    scopus 로고
    • Analysis of the mechanism of loss of trophic factor dependence associated with neuronal maturation: A phenotype indistinguishable from bax deletion
    • Easton R.M.et al. Analysis of the mechanism of loss of trophic factor dependence associated with neuronal maturation. a phenotype indistinguishable from bax deletion J. Neurosci. 17:1997;9656-9666.
    • (1997) J. Neurosci. , vol.17 , pp. 9656-9666
    • Easton, R.M.1
  • 63
    • 0030760873 scopus 로고    scopus 로고
    • Death mechanisms in cultured cells infected by Semliki Forest virus
    • Glasgow G.M.et al. Death mechanisms in cultured cells infected by Semliki Forest virus. J. Gen. Virol. 78:1997;1559-1563.
    • (1997) J. Gen. Virol. , vol.78 , pp. 1559-1563
    • Glasgow, G.M.1
  • 64
    • 0033040722 scopus 로고    scopus 로고
    • Cell death mechanisms in the olfactory bulb of rats infected intranasally with Semliki Forest virus
    • Sammin D.J.et al. Cell death mechanisms in the olfactory bulb of rats infected intranasally with Semliki Forest virus. Neuropathol. Appl. Neurobiol. 25:1999;236-243.
    • (1999) Neuropathol. Appl. Neurobiol. , vol.25 , pp. 236-243
    • Sammin, D.J.1
  • 65
    • 0031555644 scopus 로고    scopus 로고
    • Sindbis virus infection of neonatal mice results in a severe stress response
    • Trgovcich J.et al. Sindbis virus infection of neonatal mice results in a severe stress response. Virology. 227:1997;234-238.
    • (1997) Virology , vol.227 , pp. 234-238
    • Trgovcich, J.1
  • 66
    • 0033093689 scopus 로고    scopus 로고
    • Resistance of interleukin-1 beta-deficient mice to fatal Sindbis virus encephalitis
    • Liang X.H.et al. Resistance of interleukin-1 beta-deficient mice to fatal Sindbis virus encephalitis. J. Virol. 73:1999;2563-2567.
    • (1999) J. Virol. , vol.73 , pp. 2563-2567
    • Liang, X.H.1
  • 67
    • 0029656251 scopus 로고    scopus 로고
    • Bcl-2 alters influenza virus yield, spread and hemagglutinin glycosylation
    • Olsen C.W.et al. Bcl-2 alters influenza virus yield, spread and hemagglutinin glycosylation. J. Virol. 70:1996;663-666.
    • (1996) J. Virol. , vol.70 , pp. 663-666
    • Olsen, C.W.1
  • 68
    • 0032192529 scopus 로고    scopus 로고
    • Evidence of a novel event during neuronal death:development of competence-to-die in response to cytoplasmic cytochrome-C
    • Deshmukh M., Johnson E.M. Jr. Evidence of a novel event during neuronal death:development of competence-to-die in response to cytoplasmic cytochrome-C. Neuron. 21:1998;695-705.
    • (1998) Neuron , vol.21 , pp. 695-705
    • Deshmukh, M.1    Johnson E.M., Jr.2
  • 69
    • 0030810926 scopus 로고    scopus 로고
    • X-linked IAP is a direct inhibitor of cell-death proteases
    • Deveraux Q.L.et al. X-linked IAP is a direct inhibitor of cell-death proteases. Nature. 388:1997;300-304.
    • (1997) Nature , vol.388 , pp. 300-304
    • Deveraux, Q.L.1
  • 70
    • 0032522738 scopus 로고    scopus 로고
    • IAPs block apoptotic events induced by caspase-8 and cytochrome-C by direct inhibition of distinct caspases
    • Deveraux Q.L.et al. IAPs block apoptotic events induced by caspase-8 and cytochrome-C by direct inhibition of distinct caspases. EMBO J. 17:1998;2215-2223.
    • (1998) EMBO J. , vol.17 , pp. 2215-2223
    • Deveraux, Q.L.1
  • 71
    • 0030698127 scopus 로고    scopus 로고
    • The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases
    • Roy N.et al. The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases. EMBO J. 16:1997;6914-6925.
    • (1997) EMBO J. , vol.16 , pp. 6914-6925
    • Roy, N.1
  • 72
    • 0030051388 scopus 로고    scopus 로고
    • Role of immune responses in protection and pathogenesis during Semliki Forest virus encephalitis
    • Amor S.et al. Role of immune responses in protection and pathogenesis during Semliki Forest virus encephalitis. J. Gen. Virol. 77:1996;281-291.
    • (1996) J. Gen. Virol. , vol.77 , pp. 281-291
    • Amor, S.1
  • 73
    • 0031051779 scopus 로고    scopus 로고
    • Susceptibility to a neurotropic virus and its changing distribution in the developing brain is a function of CNS maturity
    • Oliver K.R.et al. Susceptibility to a neurotropic virus and its changing distribution in the developing brain is a function of CNS maturity. J. Neurovirol. 3:1997;38-48.
    • (1997) J. Neurovirol. , vol.3 , pp. 38-48
    • Oliver, K.R.1
  • 74
    • 0023921032 scopus 로고
    • Viral infection of neurons can depress neurotransmitter mRNA levels without histologic injury
    • Lipkin W.I.et al. Viral infection of neurons can depress neurotransmitter mRNA levels without histologic injury. Brain Res. 451:1988;333-339.
    • (1988) Brain Res. , vol.451 , pp. 333-339
    • Lipkin, W.I.1
  • 75
    • 0025785045 scopus 로고
    • High resolution in situ hybridisation to determine the cellular distribution of lymphocytic choriomeningitis virus RNA in the tissues of persistently infected mice: Relevance to arenavirus disease and mechanisms of viral persistence
    • Fazakerley J.K.et al. High resolution in situ hybridisation to determine the cellular distribution of lymphocytic choriomeningitis virus RNA in the tissues of persistently infected mice: relevance to arenavirus disease and mechanisms of viral persistence. J. Gen. Virol. 72:1991;1611-1625.
    • (1991) J. Gen. Virol. , vol.72 , pp. 1611-1625
    • Fazakerley, J.K.1
  • 76
    • 0023156706 scopus 로고
    • Semliki Forest virus-induced immune-mediated demyelination: Adoptive transfer studies and viral persistence in nude mice
    • Fazakerley J.K., Webb H.E. Semliki Forest virus-induced immune-mediated demyelination. adoptive transfer studies and viral persistence in nude mice J. Gen. Virol. 68:1987;377-385.
    • (1987) J. Gen. Virol. , vol.68 , pp. 377-385
    • Fazakerley, J.K.1    Webb, H.E.2
  • 77
    • 0026354236 scopus 로고
    • Antibody-mediated clearance of alphavirus infection from neurones
    • Levine B.et al. Antibody-mediated clearance of alphavirus infection from neurones. Science. 254:1991;856-860.
    • (1991) Science , vol.254 , pp. 856-860
    • Levine, B.1


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