메뉴 건너뛰기




Volumn 111, Issue 2, 2003, Pages 153-161

Programmed cell death in amyotrophic lateral sclerosis

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMICAL MARKER; CASPASE; DNA FRAGMENT; PROTEIN BCL 2; SUPEROXIDE DISMUTASE;

EID: 0037240427     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI200317610     Document Type: Review
Times cited : (160)

References (77)
  • 1
    • 0002768765 scopus 로고
    • Hereditary and acquired motor neuron diseases
    • L.P. Rowland, editor. Williams & Wilkins. Philadelphia, Pennsylvania, USA
    • Rowland, L.P. 1995. Hereditary and acquired motor neuron diseases. In Merritt's textbook of neurology. L.P. Rowland, editor. Williams & Wilkins. Philadelphia, Pennsylvania, USA. 742-749.
    • (1995) Merritt's Textbook of Neurology , pp. 742-749
    • Rowland, L.P.1
  • 2
    • 0028960506 scopus 로고
    • Amyotrophic lateral sclerosis: Recent insights from genetics and transgenic mice
    • Brown, R.H., Jr. 1995. Amyotrophic lateral sclerosis: recent insights from genetics and transgenic mice. Cell. 80:687-692.
    • (1995) Cell , vol.80 , pp. 687-692
    • Brown R.H., Jr.1
  • 3
    • 0027426169 scopus 로고
    • Amyotrophic lateral sclerosis and structural defects in Cu,Zn superoxide dismutase
    • Deng, H.-X., et al. 1993. Amyotrophic lateral sclerosis and structural defects in Cu,Zn superoxide dismutase. Science. 261:1047-1051.
    • (1993) Science , vol.261 , pp. 1047-1051
    • Deng, H.-X.1
  • 4
    • 0027401203 scopus 로고
    • Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis
    • Rosen, D.R., et al. 1993. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature. 362:59-62.
    • (1993) Nature , vol.362 , pp. 59-62
    • Rosen, D.R.1
  • 5
    • 0031057003 scopus 로고    scopus 로고
    • Epidemiology of mutations in superoxide dismutase in amyotrophic lateral sclerosis
    • Cudkowicz, M.E., et al. 1997. Epidemiology of mutations in superoxide dismutase in amyotrophic lateral sclerosis. Ann. Neurol. 41:210-221.
    • (1997) Ann. Neurol. , vol.41 , pp. 210-221
    • Cudkowicz, M.E.1
  • 6
    • 0029881166 scopus 로고    scopus 로고
    • Blood superoxide dismutase, catalase and glutathione peroxidase activities in familial and sporadic amyotrophic lateral sclerosis
    • Przedborski, S., et al. 1996. Blood superoxide dismutase, catalase and glutathione peroxidase activities in familial and sporadic amyotrophic lateral sclerosis. Neurodegeneration. 5:57-64.
    • (1996) Neurodegeneration , vol.5 , pp. 57-64
    • Przedborski, S.1
  • 7
    • 0028221169 scopus 로고
    • Down-regulation of copper/zinc superoxide dismutase causes apoptotic death in PC12 neuronal cells
    • Troy, C.M., and Shelanski, M.L. 1994. Down-regulation of copper/zinc superoxide dismutase causes apoptotic death in PC12 neuronal cells. Proc. Natl. Acad. Sci. USA. 91:6384-6387.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6384-6387
    • Troy, C.M.1    Shelanski, M.L.2
  • 9
    • 15844393658 scopus 로고    scopus 로고
    • Motor neurons in Cu/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury
    • Reaume, A.G., et al. 1996. Motor neurons in Cu/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury. Nat. Genet. 13:43-47.
    • (1996) Nat. Genet. , vol.13 , pp. 43-47
    • Reaume, A.G.1
  • 10
    • 0028284779 scopus 로고
    • Motor neuron degeneration in mice that express a human Cu, Zn superoxide dismutase mutation
    • Gurney, M.E., et al. 1994. Motor neuron degeneration in mice that express a human Cu, Zn superoxide dismutase mutation. Science. 264:1772-1775.
    • (1994) Science , vol.264 , pp. 1772-1775
    • Gurney, M.E.1
  • 11
    • 0029053881 scopus 로고
    • An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria
    • Wong, P.C., et al. 1995. An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria. Neuron. 14:1105-1116.
    • (1995) Neuron , vol.14 , pp. 1105-1116
    • Wong, P.C.1
  • 12
    • 0031051485 scopus 로고    scopus 로고
    • ALS-linked SOD1 mutant G85R mediated damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions
    • Bruijn, L.I., et al. 1997. ALS-linked SOD1 mutant G85R mediated damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions. Neuron. 18:327-338.
    • (1997) Neuron , vol.18 , pp. 327-338
    • Bruijn, L.I.1
  • 13
    • 0035575761 scopus 로고    scopus 로고
    • Rats expressing human cytosolic copper-zinc superoxide dismutase transgenes with amyotrophic lateral sclerosis: Associated mutations develop motor neuron disease
    • Nagai, M., et al. 2001. Rats expressing human cytosolic copper-zinc superoxide dismutase transgenes with amyotrophic lateral sclerosis: associated mutations develop motor neuron disease. J. Neurosci. 21:9246-9254.
    • (2001) J. Neurosci. , vol.21 , pp. 9246-9254
    • Nagai, M.1
  • 14
    • 0036212119 scopus 로고    scopus 로고
    • Mutant SOD1 causes motor neuron disease independent of copper chaperone-mediated copper loading
    • Subramaniam, J.R., et al. 2002. Mutant SOD1 causes motor neuron disease independent of copper chaperone-mediated copper loading. Nat. Neurosci. 5:301-307.
    • (2002) Nat. Neurosci. , vol.5 , pp. 301-307
    • Subramaniam, J.R.1
  • 15
    • 0029584941 scopus 로고
    • Superoxide dismutase in familial amyocrophic lateral sclerosis: Models for gain of function
    • Brown, R.H., Jr. 1995. Superoxide dismutase in familial amyocrophic lateral sclerosis: models for gain of function. Curr. Opin. Neurobiol. 5:841-846.
    • (1995) Curr. Opin. Neurobiol. , vol.5 , pp. 841-846
    • Brown R.H., Jr.1
  • 16
    • 0029096114 scopus 로고
    • Age-dependent penetrance of disease in a transgenic mouse model of familial amyotrophic lateral sclerosis
    • Chiu, A.Y., et al. 1995. Age-dependent penetrance of disease in a transgenic mouse model of familial amyotrophic lateral sclerosis. Mol. Cell. Neurosci. 6:349-362.
    • (1995) Mol. Cell. Neurosci. , vol.6 , pp. 349-362
    • Chiu, A.Y.1
  • 17
    • 0028933344 scopus 로고
    • Neuropathological changes in two lines of mice carrying a transgene for mutant human Cu,Zn SOD, and in mice overexpressing wild type human SOD: A model of familial amyotrophic lateral sclerosis (FALS)
    • Dal Canto, M.C., and Gurney, M.E. 1995. Neuropathological changes in two lines of mice carrying a transgene for mutant human Cu,Zn SOD, and in mice overexpressing wild type human SOD: a model of familial amyotrophic lateral sclerosis (FALS). Brain Res. 676:25-40.
    • (1995) Brain Res. , vol.676 , pp. 25-40
    • Dal Canto, M.C.1    Gurney, M.E.2
  • 18
    • 0033018506 scopus 로고    scopus 로고
    • Inducible nitric oxide synthase upregulation in a transgenic mouse model of familial amyotrophic lateral sclerosis
    • Almer, G., Vukosavic, S., Romero, N., and Przedborski, S. 1999. Inducible nitric oxide synthase upregulation in a transgenic mouse model of familial amyotrophic lateral sclerosis. J. Neurochem. 72:2415-2425.
    • (1999) J. Neurochem. , vol.72 , pp. 2415-2425
    • Almer, G.1    Vukosavic, S.2    Romero, N.3    Przedborski, S.4
  • 19
    • 0029966363 scopus 로고    scopus 로고
    • Transgenic mice carrying a human mutant superoxide dismutase transgene develop neuronal cytoskeletal pathology resembling human amyotrophic lateral sclerosis lesions
    • Tu, P.H., et al. 1996. Transgenic mice carrying a human mutant superoxide dismutase transgene develop neuronal cytoskeletal pathology resembling human amyotrophic lateral sclerosis lesions. Proc. Natl. Acad. Sci. USA. 93:3155-3160.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3155-3160
    • Tu, P.H.1
  • 20
    • 0035516124 scopus 로고    scopus 로고
    • From Charcor to Lou Gehrig: Deciphering selective motor neuron death in ALS
    • Cleveland, D.W., and Rothstein, J.D. 2001. From Charcor to Lou Gehrig: deciphering selective motor neuron death in ALS. Nat. Rev. Neurosci. 2:806-819.
    • (2001) Nat. Rev. Neurosci. , vol.2 , pp. 806-819
    • Cleveland, D.W.1    Rothstein, J.D.2
  • 22
    • 0029671220 scopus 로고    scopus 로고
    • Altered reactivity of superoxide dismutase in familial amyotrophic lateral sclerosis
    • Wiedau-Pazos, M., et al. 1996. Altered reactivity of superoxide dismutase in familial amyotrophic lateral sclerosis. Science. 271:515-518.
    • (1996) Science , vol.271 , pp. 515-518
    • Wiedau-Pazos, M.1
  • 23
    • 0030833449 scopus 로고    scopus 로고
    • Decreased zinc affinity of amyotrophic lateral sclerosis-associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite
    • Crow, J.P., Sampson, J.B., Zhuang, Y.X., Thompson, J.A., and Beckman, J.S. 1997. Decreased zinc affinity of amyotrophic lateral sclerosis-associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite. J. Neurochem. 69:1936-1944.
    • (1997) J. Neurochem. , vol.69 , pp. 1936-1944
    • Crow, J.P.1    Sampson, J.B.2    Zhuang, Y.X.3    Thompson, J.A.4    Beckman, J.S.5
  • 24
    • 0039251419 scopus 로고    scopus 로고
    • Induction of nitric oxide-dependent apoptosis in motor neurons by zinc-deficient superoxide dismutase
    • Estevez, A.G., et al. 1999. Induction of nitric oxide-dependent apoptosis in motor neurons by zinc-deficient superoxide dismutase. Science. 286:2498-2500.
    • (1999) Science , vol.286 , pp. 2498-2500
    • Estevez, A.G.1
  • 25
    • 0032544674 scopus 로고    scopus 로고
    • Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1
    • Bruijn, L.I., et al. 1998. Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1. Science. 281:1851-1854.
    • (1998) Science , vol.281 , pp. 1851-1854
    • Bruijn, L.I.1
  • 26
    • 0030777650 scopus 로고    scopus 로고
    • Aggregation of mutant Cu/Zn superoxide dismutase proteins in a culture model of ALS
    • Durham, H.D., Roy, J., Dong, L., and Figlewicz, D.A. 1997. Aggregation of mutant Cu/Zn superoxide dismutase proteins in a culture model of ALS: J. Neuropathol. Exp. Neurol. 56:523-530.
    • (1997) J. Neuropathol. Exp. Neurol. , vol.56 , pp. 523-530
    • Durham, H.D.1    Roy, J.2    Dong, L.3    Figlewicz, D.A.4
  • 27
    • 0033940437 scopus 로고    scopus 로고
    • Late-onset neurodegenerative diseases: The role of protein insolubility
    • Johnson, W.G. 2000. Late-onset neurodegenerative diseases: the role of protein insolubility. J. Anat. 196:609-616.
    • (2000) J. Anat. , vol.196 , pp. 609-616
    • Johnson, W.G.1
  • 28
    • 0028915976 scopus 로고
    • Mutations associated with amyotrophic lateral sclerosis convert superoxide dismutase from an antiapoptotic gene to a proapoptotic gene: Studies in yeast and neural cells
    • Rabizadeh, S., et al. 1995. Mutations associated with amyotrophic lateral sclerosis convert superoxide dismutase from an antiapoptotic gene to a proapoptotic gene: studies in yeast and neural cells. Proc. Natl. Acad. Sci. USA. 92:3024-3028.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3024-3028
    • Rabizadeh, S.1
  • 29
    • 0030831352 scopus 로고    scopus 로고
    • Mutant superoxide dismutase-1-linked familial amyotrophic lateral sclerosis: Molecular mechanisms of neuronal death and protection
    • Ghadge, G.D., et al. 1997. Mutant superoxide dismutase-1-linked familial amyotrophic lateral sclerosis: molecular mechanisms of neuronal death and protection. J. Neurosci. 17:8756-8766.
    • (1997) J. Neurosci. , vol.17 , pp. 8756-8766
    • Ghadge, G.D.1
  • 30
    • 0030943110 scopus 로고    scopus 로고
    • Effects of wild-type and mutated copper/zinc superoxide dismutase on neuronal survival and L-DOPA-induced toxicity in postnatal midbrain culture
    • Mena, M.A., et al. 1997. Effects of wild-type and mutated copper/zinc superoxide dismutase on neuronal survival and L-DOPA-induced toxicity in postnatal midbrain culture. J. Neurochem. 69:21-33.
    • (1997) J. Neurochem. , vol.69 , pp. 21-33
    • Mena, M.A.1
  • 31
    • 0028896092 scopus 로고
    • The gene for neuronal apoptosis inhibitory protein is partially deleted in individuals with spinal muscular atrophy
    • Roy, N., et al. 1995. The gene for neuronal apoptosis inhibitory protein is partially deleted in individuals with spinal muscular atrophy. Cell. 80:167-178.
    • (1995) Cell , vol.80 , pp. 167-178
    • Roy, N.1
  • 32
    • 0032863462 scopus 로고    scopus 로고
    • Lack ofapoptosis in mice with ALS
    • Migheli, A., et al. 1999. Lack ofapoptosis in mice with ALS. Nat. Med. 5:966-967.
    • (1999) Nat. Med. , vol.5 , pp. 966-967
    • Migheli, A.1
  • 33
    • 0034610328 scopus 로고    scopus 로고
    • Caspase-1 and -3 are sequentially activated in motor neuron death in Cu,Zn superoxide dismutase-mediated familial amyotrophic lateral sclerosis
    • Pasinelli, P., Houseweart, M.K., Brown, R.H., Jr., and Cleveland, D.W. 2000. Caspase-1 and -3 are sequentially activated in motor neuron death in Cu,Zn superoxide dismutase-mediated familial amyotrophic lateral sclerosis. Proc. Natl. Acad. Sci. USA. 97:13901-13906.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13901-13906
    • Pasinelli, P.1    Houseweart, M.K.2    Brown R.H., Jr.3    Cleveland, D.W.4
  • 34
    • 0034671376 scopus 로고    scopus 로고
    • Delaying caspase activation by Bcl-2: A clue to disease retardation in a transgenic mouse model of amyotrophic lateral sclerosis
    • Vukosavic, S., et al. 2000. Delaying caspase activation by Bcl-2: a clue to disease retardation in a transgenic mouse model of amyotrophic lateral sclerosis. J. Neurosci. 20:9119-9125.
    • (2000) J. Neurosci. , vol.20 , pp. 9119-9125
    • Vukosavic, S.1
  • 35
    • 0002023977 scopus 로고    scopus 로고
    • Apoptosis versus necrosis
    • V.E. Koliatsos and R.R. Ratan, editors. Humana Press. Totowa, New Jersey, USA
    • Clarke, P.G.H. 1999. Apoptosis versus necrosis. In Cell death and diseases of the nervous system. V.E. Koliatsos and R.R. Ratan, editors. Humana Press. Totowa, New Jersey, USA. 3-28.
    • (1999) Cell Death and Diseases of the Nervous System , pp. 3-28
    • Clarke, P.G.H.1
  • 36
    • 0029981892 scopus 로고    scopus 로고
    • A novel type of programmed neuronal death in the cervical spinal cord of the chick embryo
    • Yaginuma, H., et al. 1996. A novel type of programmed neuronal death in the cervical spinal cord of the chick embryo. J. Neurosci. 16:3685-3703.
    • (1996) J. Neurosci. , vol.16 , pp. 3685-3703
    • Yaginuma, H.1
  • 37
    • 0034687754 scopus 로고    scopus 로고
    • An alternative, nonapoptotic form of programmed cell death
    • Sperandio, S., de Belle, I., and Bredesen, D.E. 2000. An alternative, nonapoptotic form of programmed cell death. Proc. Natl. Acad. Sci. USA. 97:14376-14381.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 14376-14381
    • Sperandio, S.1    De Belle, I.2    Bredesen, D.E.3
  • 38
    • 0032896327 scopus 로고    scopus 로고
    • Neuronal death in amyotrophic lateral sclerosis is apoptosis: Possible contribution of a programmed cell death mechanism
    • Martin, L.J. 1999. Neuronal death in amyotrophic lateral sclerosis is apoptosis: possible contribution of a programmed cell death mechanism. J. Neuropathol. Exp. Neurol. 58:459-471.
    • (1999) J. Neuropathol. Exp. Neurol. , vol.58 , pp. 459-471
    • Martin, L.J.1
  • 39
    • 0028101227 scopus 로고
    • Apoptosis related antigen, Le(Y) and nick-end labeling are positive in spinal motor neurons in amyotrophic lateral sclerosis
    • Yoshiyama, Y., Yamada, T., Asanuma, K., and Asahi, T. 1994. Apoptosis related antigen, Le(Y) and nick-end labeling are positive in spinal motor neurons in amyotrophic lateral sclerosis. Acta Neuropathol. (Berl.) 88:207-211.
    • (1994) Acta Neuropathol. (Berl.) , vol.88 , pp. 207-211
    • Yoshiyama, Y.1    Yamada, T.2    Asanuma, K.3    Asahi, T.4
  • 40
    • 0032862513 scopus 로고    scopus 로고
    • Upregulation of Bax protein and increased DNA degradation in ALS spinal cord motor neurons
    • Ekegren, T., Grundstrom, E., Lindholm, D., and Aquilonius, S.M. 1999. Upregulation of Bax protein and increased DNA degradation in ALS spinal cord motor neurons. Acta Neurol. Scand. 100:317-321.
    • (1999) Acta Neurol. Scand. , vol.100 , pp. 317-321
    • Ekegren, T.1    Grundstrom, E.2    Lindholm, D.3    Aquilonius, S.M.4
  • 41
    • 0027985477 scopus 로고
    • A study of apoptosis in normal and pathologic nervous tissue after in situ endlabeling of DNA strand breaks
    • Migheli, A., Cavalla, P., Marino, S., and Schiffer, D. 1994. A study of apoptosis in normal and pathologic nervous tissue after in situ endlabeling of DNA strand breaks. J. Neuropathol. Exp. Neurol. 53:606-616.
    • (1994) J. Neuropathol. Exp. Neurol. , vol.53 , pp. 606-616
    • Migheli, A.1    Cavalla, P.2    Marino, S.3    Schiffer, D.4
  • 42
    • 0033625507 scopus 로고    scopus 로고
    • Motor neuronal death in sporadic amyotrophic lateral sclerosis (ALS) is not apoptotic. A comparative study of ALS and chronic aluminium chloride neurotoxicity in New Zealand white rabbits
    • He, B.P., and Strong, M.J. 2000. Motor neuronal death in sporadic amyotrophic lateral sclerosis (ALS) is not apoptotic. A comparative study of ALS and chronic aluminium chloride neurotoxicity in New Zealand white rabbits. Neuropathol. Appl. Neurobiol. 26:150-160.
    • (2000) Neuropathol. Appl. Neurobiol. , vol.26 , pp. 150-160
    • He, B.P.1    Strong, M.J.2
  • 43
    • 0027338125 scopus 로고
    • Le(y) antigen expression is correlated with apoptosis (programmed cell death)
    • Hiraishi, K., Suzuki, K., Hakomori, S., and Adachi, M. 1993. Le(y) antigen expression is correlated with apoptosis (programmed cell death). Glycobiology. 3:381-390.
    • (1993) Glycobiology , vol.3 , pp. 381-390
    • Hiraishi, K.1    Suzuki, K.2    Hakomori, S.3    Adachi, M.4
  • 44
    • 0032963464 scopus 로고    scopus 로고
    • Fractin immunostaining for the detection of apoptotic cells and apoptotic bodies in formalin-fixed and paraffin-embedded tissue
    • Suurmeijer, A.J., van der Wijk, J., van Veldhuisen, D.J., Yang, F., and Cole, G.M. 1999. Fractin immunostaining for the detection of apoptotic cells and apoptotic bodies in formalin-fixed and paraffin-embedded tissue. Lab. Invest. 79:619-620.
    • (1999) Lab. Invest. , vol.79 , pp. 619-620
    • Suurmeijer, A.J.1    Van der Wijk, J.2    Van Veldhuisen, D.J.3    Yang, F.4    Cole, G.M.5
  • 45
    • 0002571491 scopus 로고    scopus 로고
    • Apoptosis mediated by a novel leucine zipper protein Par-4
    • Rangnekar, V.M. 1998. Apoptosis mediated by a novel leucine zipper protein Par-4. Apoptosis. 3:61-66.
    • (1998) Apoptosis , vol.3 , pp. 61-66
    • Rangnekar, V.M.1
  • 46
    • 0034012013 scopus 로고    scopus 로고
    • The prostate apoptosis response-4 protein participates in motor neuron degeneration in amyotrophic lateral sclerosis
    • Pedersen, W.A., Luo, H., Kruman, I., Kasarskis, E., and Mattson, M.P. 2000. The prostate apoptosis response-4 protein participates in motor neuron degeneration in amyotrophic lateral sclerosis. FASEB J. 14:913-924.
    • (2000) FASEB J. , vol.14 , pp. 913-924
    • Pedersen, W.A.1    Luo, H.2    Kruman, I.3    Kasarskis, E.4    Mattson, M.P.5
  • 47
    • 0035033952 scopus 로고    scopus 로고
    • Signaling for survival and death in neurones. The role of stress-activated kinases, JNK and p38
    • Harper, S.J., and LoGrasso, P. 2001. Signaling for survival and death in neurones. The role of stress-activated kinases, JNK and p38. Cell. Signal. 13:299-310.
    • (2001) Cell. Signal , vol.13 , pp. 299-310
    • Harper, S.J.1    LoGrasso, P.2
  • 48
    • 0035834279 scopus 로고    scopus 로고
    • Molecular steps of death receptor and mitochondrial pathways of apoptosis
    • Gupta, S. 2001. Molecular steps of death receptor and mitochondrial pathways of apoptosis. Life Sci. 69:2957-2964.
    • (2001) Life Sci. , vol.69 , pp. 2957-2964
    • Gupta, S.1
  • 49
    • 0037068836 scopus 로고    scopus 로고
    • Motoneuron death triggered by a specific pathway downstream of Fas. Potentiation by ALS-Linked SOD1 mutations
    • Raoul, C., et al. 2002. Motoneuron death triggered by a specific pathway downstream of Fas. Potentiation by ALS-Linked SOD1 mutations. Neuron. 35:1067-1083.
    • (2002) Neuron , vol.35 , pp. 1067-1083
    • Raoul, C.1
  • 50
    • 0037088793 scopus 로고    scopus 로고
    • Mutant Cu, Zn superoxide dismutase that causes motoneuron degeneration is present in mitochondria in the CNS
    • Higgins, C.M., Jung, C., Ding, H., and Xu, Z. 2002. Mutant Cu, Zn superoxide dismutase that causes motoneuron degeneration is present in mitochondria in the CNS. J. Neurosci. 22:RC215.
    • (2002) J. Neurosci. , vol.22
    • Higgins, C.M.1    Jung, C.2    Ding, H.3    Xu, Z.4
  • 51
    • 0032079517 scopus 로고    scopus 로고
    • Massive mitochondrial degeneration in motor neurons triggers the onset of amyotrophic lateral sclerosis in mice expressing a mutant SOD1
    • Kong, J.M., and Xu, Z.S. 1998. Massive mitochondrial degeneration in motor neurons triggers the onset of amyotrophic lateral sclerosis in mice expressing a mutant SOD1. J. Neurosci. 18:3241-3250.
    • (1998) J. Neurosci. , vol.18 , pp. 3241-3250
    • Kong, J.M.1    Xu, Z.S.2
  • 52
    • 0031865772 scopus 로고    scopus 로고
    • Metabolic dysfunction in familial, but not sporadic, amyotrophic lateral sclerosis
    • Browne, S.E., et al. 1998. Metabolic dysfunction in familial, but not sporadic, amyotrophic lateral sclerosis. J. Neurochem. 71:281-287.
    • (1998) J. Neurochem. , vol.71 , pp. 281-287
    • Browne, S.E.1
  • 53
    • 0034068601 scopus 로고    scopus 로고
    • Mitochondrial control of cell death
    • Kroemer, G., and Reed, J.C. 2000. Mitochondrial control of cell death. Nat. Med. 6:513-519.
    • (2000) Nat. Med. , vol.6 , pp. 513-519
    • Kroemer, G.1    Reed, J.C.2
  • 54
    • 0034811953 scopus 로고    scopus 로고
    • Early decrease of survival signal-related proteins in spinal motor neurons of presymptomatic transgenic mice with a mutant SOD1 gene
    • Warita, H., et al. 2001. Early decrease of survival signal-related proteins in spinal motor neurons of presymptomatic transgenic mice with a mutant SOD1 gene. Apoptosis. 6:345-352.
    • (2001) Apoptosis , vol.6 , pp. 345-352
    • Warita, H.1
  • 55
    • 0035833937 scopus 로고    scopus 로고
    • Immune reactivity in a mouse model of familial ALS correlates with disease progression
    • Alexianu, M.E., Kozovska, M., and Appel, S.H. 2001. Immune reactivity in a mouse model of familial ALS correlates with disease progression. Neurology. 57:1282-1289.
    • (2001) Neurology , vol.57 , pp. 1282-1289
    • Alexianu, M.E.1    Kozovska, M.2    Appel, S.H.3
  • 56
    • 0034765498 scopus 로고    scopus 로고
    • Induction of proinflammatory molecules in mice with amyotrophic lateral sclerosis: No requirement for proapoptotic interleukin-1beta in neurodegeneration
    • Nguyen, M.D., Julien, J.P., and Rivest, S. 2001. Induction of proinflammatory molecules in mice with amyotrophic lateral sclerosis: no requirement for proapoptotic interleukin-1beta in neurodegeneration. Ann. Neurol. 50:630-639.
    • (2001) Ann. Neurol. , vol.50 , pp. 630-639
    • Nguyen, M.D.1    Julien, J.P.2    Rivest, S.3
  • 57
    • 0034647003 scopus 로고    scopus 로고
    • Functional role of caspase-1 and caspase-3 in an ALS transgenic mouse model
    • Li, M., et al. 2000. Functional role of caspase-1 and caspase-3 in an ALS transgenic mouse model. Science. 288:335-339.
    • (2000) Science , vol.288 , pp. 335-339
    • Li, M.1
  • 58
    • 0031918223 scopus 로고    scopus 로고
    • BCL-2 family: Regulators of cell death
    • Chao, D.T., and Korsmeyer, S.J. 1998. BCL-2 family: regulators of cell death. Annu. Rev. Immunol. 16:395-419.
    • (1998) Annu. Rev. Immunol. , vol.16 , pp. 395-419
    • Chao, D.T.1    Korsmeyer, S.J.2
  • 59
    • 0029787513 scopus 로고    scopus 로고
    • Altered expression of bcl-2 and bax mRNA in amyotrophic lateral sclerosis spinal cord motor neurons
    • Mu, X., He, J., Anderson, D.W., Trojanowski, J.Q., and Springer, J. E. 1996. Altered expression of bcl-2 and bax mRNA in amyotrophic lateral sclerosis spinal cord motor neurons. Ann. Neurol. 40:379-386.
    • (1996) Ann. Neurol. , vol.40 , pp. 379-386
    • Mu, X.1    He, J.2    Anderson, D.W.3    Trojanowski, J.Q.4    Springer, J.E.5
  • 60
    • 0032750753 scopus 로고    scopus 로고
    • Bax and Bcl-2 interaction in a transgenic mouse model of familial amyotrophic lateral sclerosis
    • Vukosavic, S., Dubois-Dauphin, M., Romero, N., and Przedborski, S. 1999. Bax and Bcl-2 interaction in a transgenic mouse model of familial amyotrophic lateral sclerosis. J. Neurochem. 73:2460-2468.
    • (1999) J. Neurochem. , vol.73 , pp. 2460-2468
    • Vukosavic, S.1    Dubois-Dauphin, M.2    Romero, N.3    Przedborski, S.4
  • 61
    • 0029563461 scopus 로고
    • Apoptosis in amyotrophic lateral sclerosis is not restricted to motor neurons. Bcl-2 expression is increased in unaffected post-central gyrus
    • Troost, D., Aten, J., Morsink, F., and De Jong, J.M.B.V. 1995. Apoptosis in amyotrophic lateral sclerosis is not restricted to motor neurons. Bcl-2 expression is increased in unaffected post-central gyrus. Neuropathol. Appl. Neurobiol. 21:498-504.
    • (1995) Neuropathol. Appl. Neurobiol. , vol.21 , pp. 498-504
    • Troost, D.1    Aten, J.2    Morsink, F.3    De Jong, J.M.B.V.4
  • 62
    • 0033826143 scopus 로고    scopus 로고
    • Alteration of the Bcl-x/Bax ratio in a transgenic mouse model ofamyotrophic lateral sclerosis: Evidence for the implication of the p53 signaling pathway
    • Gonzalez de Aguilar, J.L., et al. 2000. Alteration of the Bcl-x/Bax ratio in a transgenic mouse model ofamyotrophic lateral sclerosis: evidence for the implication of the p53 signaling pathway. Neurobiol. Dis. 7:406-415.
    • (2000) Neurobiol. Dis. , vol.7 , pp. 406-415
    • Gonzalez de Aguilar, J.L.1
  • 63
    • 0035437866 scopus 로고    scopus 로고
    • Recruitment of the mitochondrial-dependent apoptotic pathway in amyotrophic lateral sclerosis
    • Guégan, C., Vila, M., Rosoklija, G., Hays, A.P., and Przedborski, S. 2001. Recruitment of the mitochondrial-dependent apoptotic pathway in amyotrophic lateral sclerosis. J. Neurosci. 21:6569-6576.
    • (2001) J. Neurosci. , vol.21 , pp. 6569-6576
    • Guégan, C.1    Vila, M.2    Rosoklija, G.3    Hays, A.P.4    Przedborski, S.5
  • 64
    • 0030756459 scopus 로고    scopus 로고
    • Bcl-2: Prolonging life in a transgenic mouse model of familial amyotrophic lateral sclerosis
    • Kostic, V., Jackson-Lewis, V., De Bilbao, F., Dubois-Dauphin, M., and Przedborski, S. 1997. Bcl-2: prolonging life in a transgenic mouse model of familial amyotrophic lateral sclerosis. Science. 277:559-562.
    • (1997) Science , vol.277 , pp. 559-562
    • Kostic, V.1    Jackson-Lewis, V.2    De Bilbao, F.3    Dubois-Dauphin, M.4    Przedborski, S.5
  • 65
    • 0036385720 scopus 로고    scopus 로고
    • Instrumental activation of Bid by caspase-1 in a transgenic mouse model of ALS
    • Guégan, C., et al. 2002. Instrumental activation of Bid by caspase-1 in a transgenic mouse model of ALS. Mol. Cell. Neurosci. 20:553-562.
    • (2002) Mol. Cell. Neurosci. , vol.20 , pp. 553-562
    • Guégan, C.1
  • 66
    • 0035834274 scopus 로고    scopus 로고
    • Upregulation of the pro-apoptotic BH3-only peptide harakiri in spinal neurons of amyotrophic lateral sclerosis patients
    • Shinoe, T., et al. 2001. Upregulation of the pro-apoptotic BH3-only peptide harakiri in spinal neurons of amyotrophic lateral sclerosis patients. Neurosci. Lett. 313:153-157.
    • (2001) Neurosci. Lett. , vol.313 , pp. 153-157
    • Shinoe, T.1
  • 67
    • 0028335717 scopus 로고
    • Tumor suppressor p53 is a regulator of bcl-2 and bax gene expression in vitro and in vivo
    • Miyashita, T., et al. 1994. Tumor suppressor p53 is a regulator of bcl-2 and bax gene expression in vitro and in vivo. Oncogene. 9:1799-1805.
    • (1994) Oncogene , vol.9 , pp. 1799-1805
    • Miyashita, T.1
  • 68
    • 0034818446 scopus 로고    scopus 로고
    • Post-translational modifications and activation of p53 by genotoxic stresses
    • Appella, E., and Anderson, C.W. 2001. Post-translational modifications and activation of p53 by genotoxic stresses. Eur. J. Biochem. 268:2764-2772.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2764-2772
    • Appella, E.1    Anderson, C.W.2
  • 69
    • 0034517935 scopus 로고    scopus 로고
    • p53 is abnormally elevated and active in the CNS of patients with amyotrophic lateral sclerosis
    • Martin, L.J. 2000. p53 is abnormally elevated and active in the CNS of patients with amyotrophic lateral sclerosis. Neurobiol. Dis. 7:613-622.
    • (2000) Neurobiol. Dis. , vol.7 , pp. 613-622
    • Martin, L.J.1
  • 70
    • 0034613225 scopus 로고    scopus 로고
    • Motor neuron cell death in a mouse model of FALS is not mediated by the p53 cell survival regulator
    • Prudlo, J., et al. 2000. Motor neuron cell death in a mouse model of FALS is not mediated by the p53 cell survival regulator. Brain Res. 879:183-187.
    • (2000) Brain Res. , vol.879 , pp. 183-187
    • Prudlo, J.1
  • 71
    • 0033834503 scopus 로고    scopus 로고
    • Absence of p53: No effect in a transgenic mouse model of familial amyotrophic lateral sclerosis
    • Kuntz, C., Kinoshita, Y., Beal, M.F., Donehower, L.A., and Morrison, R.S. 2000. Absence of p53: no effect in a transgenic mouse model of familial amyotrophic lateral sclerosis. Exp. Neurol. 165:184-190.
    • (2000) Exp. Neurol. , vol.165 , pp. 184-190
    • Kuntz, C.1    Kinoshita, Y.2    Beal, M.F.3    Donehower, L.A.4    Morrison, R.S.5
  • 72
    • 0032430185 scopus 로고    scopus 로고
    • Caspase-1 is activated in neural cells and tissue with amyotrophic lateral sclerosis-associated mutations in copper-zinc superoxide dismutase
    • Pasinelli, P., Borchelt, D.R., Houseweart, M.K., Cleveland, D.W., and Brown, R.H.J. 1998. Caspase-1 is activated in neural cells and tissue with amyotrophic lateral sclerosis-associated mutations in copper-zinc superoxide dismutase. Proc. Natl. Acad Sci. USA. 95:15763-15768.
    • (1998) Proc. Natl. Acad Sci. USA , vol.95 , pp. 15763-15768
    • Pasinelli, P.1    Borchelt, D.R.2    Houseweart, M.K.3    Cleveland, D.W.4    Brown, R.H.J.5
  • 74
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta
    • Nakagawa, T., et al. 2000. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature. 403:98-103.
    • (2000) Nature , vol.403 , pp. 98-103
    • Nakagawa, T.1
  • 75
    • 0032080197 scopus 로고    scopus 로고
    • Defects in regulation of apoptosis in caspase-2-deficient mice
    • Bergeron, L., et al. 1998. Defects in regulation of apoptosis in caspase-2-deficient mice. Genes Dev. 12:1304-1314.
    • (1998) Genes Dev. , vol.12 , pp. 1304-1314
    • Bergeron, L.1
  • 76
    • 0037007645 scopus 로고    scopus 로고
    • Minocycline inhibits cytochrome c release and delays progression of amyotrophic lateral sclerosis in mice
    • Zhu, S., et al. 2002. Minocycline inhibits cytochrome c release and delays progression of amyotrophic lateral sclerosis in mice. Nature. 417:74-78.
    • (2002) Nature , vol.417 , pp. 74-78
    • Zhu, S.1
  • 77
    • 0033709907 scopus 로고    scopus 로고
    • Deficiency in caspase-9 or caspase-3 induces compensatory caspase activation
    • Zheng, T.S., et al. 2000. Deficiency in caspase-9 or caspase-3 induces compensatory caspase activation. Nat. Med. 6:1241-1247.
    • (2000) Nat. Med. , vol.6 , pp. 1241-1247
    • Zheng, T.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.