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Volumn 29, Issue 1, 1999, Pages 121-135

Amyotrophic lateral sclerosis associated with mutations in superoxide dismutase: A putative mechanism of degeneration

Author keywords

Excitotoxicity; Neurofilament; Transgenic

Indexed keywords

ALPHA TOCOPHEROL; AMPA RECEPTOR; CALCIUM; CALCIUM CHANNEL; CALPAIN; GLUTAMATE RECEPTOR; KAINIC ACID RECEPTOR; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; PEROXYNITRITE; PROTEINASE; SUPEROXIDE DISMUTASE;

EID: 0032908774     PISSN: 01650173     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0165-0173(98)00049-6     Document Type: Article
Times cited : (78)

References (140)
  • 1
    • 0028971936 scopus 로고
    • Induction of nitrotyrosine-like immunoreactivity in the lower motor neuron of amyotrophic lateral sclerosis
    • K. Abe, L.-H. Pan, M. Watanabe, T. Kato, Y. Itoyama, Induction of nitrotyrosine-like immunoreactivity in the lower motor neuron of amyotrophic lateral sclerosis, Neurosci. Lett. 199 (1995) 152-154.
    • (1995) Neurosci. Lett. , vol.199 , pp. 152-154
    • Abe, K.1    Pan, L.-H.2    Watanabe, M.3    Kato, T.4    Itoyama, Y.5
  • 4
    • 0027946813 scopus 로고
    • The role of calcium-binding proteins in selective motoneuron vulnerability in amyotrophic lateral sclerosis
    • M.E. Alexianu, B.-K. Ho, A.H. Mohamed, V. La Bella, R.G. Smith, S.H. Appel, The role of calcium-binding proteins in selective motoneuron vulnerability in amyotrophic lateral sclerosis, Ann. Neurol. 36 (1994) 846-858.
    • (1994) Ann. Neurol. , vol.36 , pp. 846-858
    • Alexianu, M.E.1    Ho, B.-K.2    Mohamed, A.H.3    La Bella, V.4    Smith, R.G.5    Appel, S.H.6
  • 5
    • 0027447304 scopus 로고
    • Calcium-binding proteins: Selective markers of nerve cells
    • C. Andressen, I. Blümcke, M.R. Celio, Calcium-binding proteins: selective markers of nerve cells, Cell Tissue Res. 271 (1993) 181-208.
    • (1993) Cell Tissue Res. , vol.271 , pp. 181-208
    • Andressen, C.1    Blümcke, I.2    Celio, M.R.3
  • 6
    • 0025371643 scopus 로고
    • Calcium-binding proteins, parvalbumin- and calbindin-D28k-immunoreactive neurons in the rat spinal cord and dorsal root ganglia: A light and electron microscopic study
    • M. Antal, T.F. Freund, E. Polgar, Calcium-binding proteins, parvalbumin- and calbindin-D28k-immunoreactive neurons in the rat spinal cord and dorsal root ganglia: a light and electron microscopic study, J. Comp. Neurol. 295 (1990) 467-484.
    • (1990) J. Comp. Neurol. , vol.295 , pp. 467-484
    • Antal, M.1    Freund, T.F.2    Polgar, E.3
  • 7
    • 0029843713 scopus 로고    scopus 로고
    • AMPA-selective glutamate receptor subtype immunoreactivity in the hippocampal dentate gyrus of patients with Alzheimer's disease - Evidence for hippocampal plasticity
    • D.M. Armstrong, M.D. Ikonomovic, AMPA-selective glutamate receptor subtype immunoreactivity in the hippocampal dentate gyrus of patients with Alzheimer's disease - evidence for hippocampal plasticity, Mol. Chem. Neuropathol. 28 (1996) 59-64.
    • (1996) Mol. Chem. Neuropathol. , vol.28 , pp. 59-64
    • Armstrong, D.M.1    Ikonomovic, M.D.2
  • 8
    • 0028350662 scopus 로고
    • AMPA-selective glutamate receptor subtype immunoreactivity in the entorhinal cortex of non-demented elderly and patients with Alzheimer's disease
    • D.M. Armstrong, M.D. Ikonomovic, R. Sheffield, R.J. Wenthold, AMPA-selective glutamate receptor subtype immunoreactivity in the entorhinal cortex of non-demented elderly and patients with Alzheimer's disease, Brain Res. 639 (1994) 207-216.
    • (1994) Brain Res. , vol.639 , pp. 207-216
    • Armstrong, D.M.1    Ikonomovic, M.D.2    Sheffield, R.3    Wenthold, R.J.4
  • 14
    • 0029884012 scopus 로고    scopus 로고
    • Glutamate transporter gene expression in amyotrophic lateral sclerosis motor cortex
    • L.A. Bristol, J.D. Rothstein, Glutamate transporter gene expression in amyotrophic lateral sclerosis motor cortex, Ann. Neurol. 39 (1996) 676-679.
    • (1996) Ann. Neurol. , vol.39 , pp. 676-679
    • Bristol, L.A.1    Rothstein, J.D.2
  • 15
    • 0028341877 scopus 로고
    • Differential assembly of coexpressed glutamate receptor subunits in neurons of rat cerebral cortex
    • N. Brose, G.W. Huntley, Y. Stern-Bach, G. Sharma, J.H. Morrison, S.F. Heinemann, Differential assembly of coexpressed glutamate receptor subunits in neurons of rat cerebral cortex, J. Biol. Chem. 269 (1994) 16780-16784.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16780-16784
    • Brose, N.1    Huntley, G.W.2    Stern-Bach, Y.3    Sharma, G.4    Morrison, J.H.5    Heinemann, S.F.6
  • 16
    • 0030806228 scopus 로고    scopus 로고
    • Elevated free nitrotyrosine levels, but not protein-bound nitrotyrosine or hydroxyl radicals, throughout amyotrophic lateral sclerosis (ALS)-like disease implicate tyrosine nitration as an aberrant in vivo property of one familial ALS-linked superoxide dismutase 1 mutant
    • L.I. Bruijn, M.F. Beal, M.W. Becher, J.B. Schulz, P.C. Wong, D.L. Price, D.W. Cleveland, Elevated free nitrotyrosine levels, but not protein-bound nitrotyrosine or hydroxyl radicals, throughout amyotrophic lateral sclerosis (ALS)-like disease implicate tyrosine nitration as an aberrant in vivo property of one familial ALS-linked superoxide dismutase 1 mutant, Proc. Natl. Acad. Sci. USA 94 (1997) 7606-7611.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7606-7611
    • Bruijn, L.I.1    Beal, M.F.2    Becher, M.W.3    Schulz, J.B.4    Wong, P.C.5    Price, D.L.6    Cleveland, D.W.7
  • 18
    • 0027251053 scopus 로고
    • The pecking order of free radicals and antioxidants: Lipid peroxidation, a-tocopherol, and ascorbate
    • G.R. Buettner, The pecking order of free radicals and antioxidants: lipid peroxidation, a-tocopherol, and ascorbate, Arch. Biochem. Biophys. 300 (1993) 535-543.
    • (1993) Arch. Biochem. Biophys. , vol.300 , pp. 535-543
    • Buettner, G.R.1
  • 19
    • 0028945978 scopus 로고
    • Activation of a neurofilament kinase, a tau kinase, and a tau phosphatase by decreased ATP levels in nerve growth factor-differentiated PC-12 cells
    • M.L. Bush, J.S. Miyashiro, V.M. Ingram, Activation of a neurofilament kinase, a tau kinase, and a tau phosphatase by decreased ATP levels in nerve growth factor-differentiated PC-12 cells, Proc. Natl. Acad. Sci. USA 92 (1995) 1861-1865.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1861-1865
    • Bush, M.L.1    Miyashiro, J.S.2    Ingram, V.M.3
  • 20
    • 0023069451 scopus 로고
    • Intracellular calcium homeostasis
    • E. Carafoli, Intracellular calcium homeostasis, Annu. Rev. Biochem. 56 (1987) 395-433.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 395-433
    • Carafoli, E.1
  • 22
    • 0030015076 scopus 로고    scopus 로고
    • Motor neurons are selectively vulnerable to AMPA/kainate receptor-mediated injury in vitro
    • S.G. Carriedo, H.Z. Yin, J.H. Weiss, Motor neurons are selectively vulnerable to AMPA/kainate receptor-mediated injury in vitro, J. Neurosci. 16 (1996) 4069-4079.
    • (1996) J. Neurosci. , vol.16 , pp. 4069-4079
    • Carriedo, S.G.1    Yin, H.Z.2    Weiss, J.H.3
  • 23
    • 0025358573 scopus 로고
    • Calbindin D-28k and parvalbumin in the rat nervous system
    • M.R. Celio, Calbindin D-28k and parvalbumin in the rat nervous system, Neuroscience 35 (1990) 375-475.
    • (1990) Neuroscience , vol.35 , pp. 375-475
    • Celio, M.R.1
  • 24
    • 0027730919 scopus 로고
    • Calcium buffering properties of calbindin D-28k and parvalbumin in rat sensory neurones
    • P.S. Chard, D. Bleakman, S. Christakos, C.S. Fullmer, R.J. Miller, Calcium buffering properties of calbindin D-28k and parvalbumin in rat sensory neurones, J. Physiol. 472 (1993) 341-357.
    • (1993) J. Physiol. , vol.472 , pp. 341-357
    • Chard, P.S.1    Bleakman, D.2    Christakos, S.3    Fullmer, C.S.4    Miller, R.J.5
  • 25
    • 0026490217 scopus 로고
    • Riluzole inhibits the release of glutamate in the caudate nucleus of the cat in vivo
    • A. Cheramy, L. Barbeito, G. Godeheu, J. Glowinski, Riluzole inhibits the release of glutamate in the caudate nucleus of the cat in vivo, Neurosci. Lett. 147 (1992) 209-212.
    • (1992) Neurosci. Lett. , vol.147 , pp. 209-212
    • Cheramy, A.1    Barbeito, L.2    Godeheu, G.3    Glowinski, J.4
  • 27
    • 0023137252 scopus 로고
    • Ionic dependence of glutamate neurotoxicity
    • D.W. Choi, Ionic dependence of glutamate neurotoxicity, J. Neurosci. 7 (1987) 369-379.
    • (1987) J. Neurosci. , vol.7 , pp. 369-379
    • Choi, D.W.1
  • 28
    • 0023870521 scopus 로고
    • Pharmacology of glutamate neurotoxicity in cortical cell culture: Attenuation by NMDA antagonists
    • D.W. Choi, J. Koh, S. Peters, Pharmacology of glutamate neurotoxicity in cortical cell culture: attenuation by NMDA antagonists, J. Neurosci. 8 (1988) 185-196.
    • (1988) J. Neurosci. , vol.8 , pp. 185-196
    • Choi, D.W.1    Koh, J.2    Peters, S.3
  • 29
    • 0029004898 scopus 로고
    • Defective axonal transport in a transgenic mouse model of amyotrophic lateral sclerosis
    • J.-F. Collard, F. Cote, J.-P. Julien, Defective axonal transport in a transgenic mouse model of amyotrophic lateral sclerosis, Nature 375 (1995) 61-64.
    • (1995) Nature , vol.375 , pp. 61-64
    • Collard, J.-F.1    Cote, F.2    Julien, J.-P.3
  • 30
    • 0027465098 scopus 로고
    • Progressive neuronopathy in transgenic mice expressing the human neurofilament heavy gene: A mouse model of amyotrophic lateral sclerosis
    • F. Côté, J.-F. Collard, J.-P. Julien, Progressive neuronopathy in transgenic mice expressing the human neurofilament heavy gene: a mouse model of amyotrophic lateral sclerosis, Cell 73 (1993) 35-46.
    • (1993) Cell , vol.73 , pp. 35-46
    • Côté, F.1    Collard, J.-F.2    Julien, J.-P.3
  • 31
    • 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
    • J.P. Crow, J.B. Sampson, Y. Zhuang, J.A. Thompson, J.S. Beckman, Decreased zinc affinity of amyotrophic lateral sclerosis-associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite, J. Neurochem. 69 (1997) 1936-1944.
    • (1997) J. Neurochem. , vol.69 , pp. 1936-1944
    • Crow, J.P.1    Sampson, J.B.2    Zhuang, Y.3    Thompson, J.A.4    Beckman, J.S.5
  • 32
    • 0027946294 scopus 로고
    • Development of central nervous system pathology in a murine transgenic model of human amyotrophic lateral sclerosis
    • M.C. Dal Canto, M.E. Gurney, Development of central nervous system pathology in a murine transgenic model of human amyotrophic lateral sclerosis, Am. J. Pathol. 145 (1994) 1271-1279.
    • (1994) Am. J. Pathol. , vol.145 , pp. 1271-1279
    • Dal Canto, M.C.1    Gurney, M.E.2
  • 33
    • 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)
    • M.C. Dal Canto, M.E. Gurney, 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 (1995) 25-40.
    • (1995) Brain Res. , vol.676 , pp. 25-40
    • Dal Canto, M.C.1    Gurney, M.E.2
  • 34
    • 0030916609 scopus 로고    scopus 로고
    • A low expressor line of transgenic mice carrying a mutant human Cu,Zn superoxide dismutase (SOD1) gene develops pathological changes that most closely resemble those in human amyotrophic lateral sclerosis
    • M.C. Dal Canto, M.E. Gurney, A low expressor line of transgenic mice carrying a mutant human Cu,Zn superoxide dismutase (SOD1) gene develops pathological changes that most closely resemble those in human amyotrophic lateral sclerosis, Acta Neuropathol. 93 (1997) 537-550.
    • (1997) Acta Neuropathol. , vol.93 , pp. 537-550
    • Dal Canto, M.C.1    Gurney, M.E.2
  • 36
    • 0030995802 scopus 로고    scopus 로고
    • Programmed cell death in neurons: Focus on the pathway of nerve growth factor deprivation-induced death of sympathetic neurons
    • M. Deshmukh, E.M. Johnson Jr., Programmed cell death in neurons: focus on the pathway of nerve growth factor deprivation-induced death of sympathetic neurons, Mol. Pharmacol. 51 (1997) 897-906.
    • (1997) Mol. Pharmacol. , vol.51 , pp. 897-906
    • Deshmukh, M.1    Johnson E.M., Jr.2
  • 37
    • 0029753270 scopus 로고    scopus 로고
    • The pharmacology and mechanism of action of riluzole
    • A. Doble, The pharmacology and mechanism of action of riluzole, Neurology 47 (1996) S233-S241, (Suppl.).
    • (1996) Neurology , vol.47 , Issue.SUPPL.
    • Doble, A.1
  • 39
    • 0030777650 scopus 로고    scopus 로고
    • Aggregation of mutant Cu/Zn superoxide dismutase proteins in a culture model of ALS
    • H.D. Durham, J. Roy, L. Dong, D.A. Figlewicz, Aggregation of mutant Cu/Zn superoxide dismutase proteins in a culture model of ALS, J. Neuropathol. Exp. Neurol. 56 (1997) 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
  • 40
    • 0031972719 scopus 로고    scopus 로고
    • Splice variant-specific interaction of the NMDA receptor subunit NR1 with neuronal intermediate filaments
    • M.D. Ehlers, E.T. Fung, R.J. O'Brien, R.L. Huganir, Splice variant-specific interaction of the NMDA receptor subunit NR1 with neuronal intermediate filaments, J. Neurosci. 18 (1998) 720-730.
    • (1998) J. Neurosci. , vol.18 , pp. 720-730
    • Ehlers, M.D.1    Fung, E.T.2    O'Brien, R.J.3    Huganir, R.L.4
  • 42
    • 0029347075 scopus 로고
    • Lysyl-tRNA synthetase
    • Hoppe-Seyler
    • W. Freist, D.H. Gauss, Lysyl-tRNA synthetase, Biol. Chem. Hoppe-Seyler 376 (1995) 451-472.
    • (1995) Biol. Chem. , vol.376 , pp. 451-472
    • Freist, W.1    Gauss, D.H.2
  • 45
    • 0028955472 scopus 로고
    • Characterization of wild-type and amyotrophic lateral sclerosis-related mutant Cu,Zn-superoxide dismutases overproduced in baculovirus-infected insect cells
    • J. Fujii, T. Myint, H.G. Seo, Y. Kayanoki, Y. Ikeda, N. Taniguchi, Characterization of wild-type and amyotrophic lateral sclerosis-related mutant Cu,Zn-superoxide dismutases overproduced in baculovirus-infected insect cells, J. Neurochem. 64 (1995) 1456-1461.
    • (1995) J. Neurochem. , vol.64 , pp. 1456-1461
    • Fujii, J.1    Myint, T.2    Seo, H.G.3    Kayanoki, Y.4    Ikeda, Y.5    Taniguchi, N.6
  • 47
    • 0028286279 scopus 로고
    • Calcium-mediated degeneration of the axonal cytoskeleton in the Ola mouse
    • J.D. Glass, B.L. Schryer, J.W. Griffen, Calcium-mediated degeneration of the axonal cytoskeleton in the Ola mouse, J. Neurochem. 62 (1994) 2472-2475.
    • (1994) J. Neurochem. , vol.62 , pp. 2472-2475
    • Glass, J.D.1    Schryer, B.L.2    Griffen, J.W.3
  • 49
    • 0030050727 scopus 로고    scopus 로고
    • Benefit of vitamin E, riluzole, and gabapentin in a transgenic model of familial amyotrophic lateral sclerosis
    • M.E. Gurney, F.B. Cuttings, P. Zhai, A. Doble, C.P. Taylor, P.K. Andrus, E.D. Hall, Benefit of vitamin E, riluzole, and gabapentin in a transgenic model of familial amyotrophic lateral sclerosis, Ann. Neurol. 39 (1996) 147-157.
    • (1996) Ann. Neurol. , vol.39 , pp. 147-157
    • Gurney, M.E.1    Cuttings, F.B.2    Zhai, P.3    Doble, A.4    Taylor, C.P.5    Andrus, P.K.6    Hall, E.D.7
  • 52
    • 0026636441 scopus 로고
    • Free radicals, antioxidants, and human disease: Where are we now?
    • B. Halliwell, J.M.C. Gutteridge, C.E. Cross, Free radicals, antioxidants, and human disease: where are we now?, J. Lab. Clin. Med. 119 (1992) 598-620.
    • (1992) J. Lab. Clin. Med. , vol.119 , pp. 598-620
    • Halliwell, B.1    Gutteridge, J.M.C.2    Cross, C.E.3
  • 54
    • 0024370364 scopus 로고
    • Two classes of cortical GABA neurons defined by differential calcium binding protein immunoreactivities
    • S.H. Hendry, E.G. Jones, P.C. Emson, D.E. Lawson, C.W. Heizmann, P. Streit, Two classes of cortical GABA neurons defined by differential calcium binding protein immunoreactivities, Exp. Brain Res. 76 (1989) 467-472.
    • (1989) Exp. Brain Res. , vol.76 , pp. 467-472
    • Hendry, S.H.1    Jones, E.G.2    Emson, P.C.3    Lawson, D.E.4    Heizmann, C.W.5    Streit, P.6
  • 56
    • 0026042995 scopus 로고
    • Cytopathology of amyotrophic lateral sclerosis
    • L.P. Rowland (Ed.), Raven Press, New York
    • A. Hirano, Cytopathology of amyotrophic lateral sclerosis, in: L.P. Rowland (Ed.), Amyotrophic Lateral Sclerosis and Other Motor Neuron Diseases, Vol. 56, Raven Press, New York, 1991, pp. 91-101.
    • (1991) Amyotrophic Lateral Sclerosis and Other Motor Neuron Diseases , vol.56 , pp. 91-101
    • Hirano, A.1
  • 57
    • 0014063240 scopus 로고
    • Familial amyotrophic lateral sclerosis
    • A. Hirano, L.T. Kurland, G.P. Sayre, Familial amyotrophic lateral sclerosis, Arch. Neurol. 16 (1967) 232-243.
    • (1967) Arch. Neurol. , vol.16 , pp. 232-243
    • Hirano, A.1    Kurland, L.T.2    Sayre, G.P.3
  • 58
    • 0021261943 scopus 로고
    • Organization of mammalian neurofilament polypeptides within the neuronal cytoskeleton
    • N. Hirokawa, M.A. Glicksman, M.B. Willard, Organization of mammalian neurofilament polypeptides within the neuronal cytoskeleton, J. Cell Biol. 98 (1984) 1523-1536.
    • (1984) J. Cell Biol. , vol.98 , pp. 1523-1536
    • Hirokawa, N.1    Glicksman, M.A.2    Willard, M.B.3
  • 59
    • 0029665882 scopus 로고    scopus 로고
    • Expression of calbindin-D28k in motoneuron hybrid cells after retroviral infection with calbindin-D28k cDNA prevents amyotrophic lateral sclerosis IgG-mediated toxicity
    • B.-K. Ho, M.E. Alexianu, L.V. Colom, A.H. Mohamed, F. Serrano, S.H. Appel, Expression of calbindin-D28k in motoneuron hybrid cells after retroviral infection with calbindin-D28k cDNA prevents amyotrophic lateral sclerosis IgG-mediated toxicity, Proc. Natl. Acad. Sci. USA 93 (1996) 6796-6801.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6796-6801
    • Ho, B.-K.1    Alexianu, M.E.2    Colom, L.V.3    Mohamed, A.H.4    Serrano, F.5    Appel, S.H.6
  • 60
    • 0027231535 scopus 로고
    • Calretinin-immunoreactive neocortical interneurons are unaffected in Alzheimer's disease
    • P.R. Hof, E.A. Nimchinsky, M.R. Celio, C. Bouras, J.H. Morrison, Calretinin-immunoreactive neocortical interneurons are unaffected in Alzheimer's disease, Neurosci. Lett. 152 (1993) 145-149.
    • (1993) Neurosci. Lett. , vol.152 , pp. 145-149
    • Hof, P.R.1    Nimchinsky, E.A.2    Celio, M.R.3    Bouras, C.4    Morrison, J.H.5
  • 63
    • 0024367836 scopus 로고
    • Cloning by functional expression of a member of the glutamate receptor family
    • M. Hollmann, A. O'Shea-Greenfield, S.W. Rogers, S. Heinemann, Cloning by functional expression of a member of the glutamate receptor family, Nature 342 (1989) 643-648.
    • (1989) Nature , vol.342 , pp. 643-648
    • Hollmann, M.1    O'Shea-Greenfield, A.2    Rogers, S.W.3    Heinemann, S.4
  • 64
    • 0030862630 scopus 로고    scopus 로고
    • The copper chelator D-penicillamine delays onset of disease and extends survival in a transgenic mouse model of familial amyotrophic lateral sclerosis
    • A.F. Hottinger, E.G. Fine, M.E. Gurney, A.D. Zurn, P. Acbischer, The copper chelator D-penicillamine delays onset of disease and extends survival in a transgenic mouse model of familial amyotrophic lateral sclerosis, Eur. J. Neurosci. 9 (1997) 1548-1551.
    • (1997) Eur. J. Neurosci. , vol.9 , pp. 1548-1551
    • Hottinger, A.F.1    Fine, E.G.2    Gurney, M.E.3    Zurn, A.D.4    Acbischer, P.5
  • 65
    • 0025169140 scopus 로고
    • Abnormal distribution of phosphorylated neurofilaments in neuronal degeneration induced by kainic acid
    • J. Hugon, J.M. Vallat, Abnormal distribution of phosphorylated neurofilaments in neuronal degeneration induced by kainic acid, Neurosci. Lett. 119 (1990) 45-48.
    • (1990) Neurosci. Lett. , vol.119 , pp. 45-48
    • Hugon, J.1    Vallat, J.M.2
  • 66
    • 13344261949 scopus 로고    scopus 로고
    • Motor neuron degeneration induced by excitotoxin agonists has features in common with those seen in the SOD-1 transgenic mouse model of amyotrophic lateral sclerosis
    • C. Ikonomidou, Y. Qin Qin, J. Labruyere, J.W. Olney, Motor neuron degeneration induced by excitotoxin agonists has features in common with those seen in the SOD-1 transgenic mouse model of amyotrophic lateral sclerosis, J. Neuropath. Exp. Neurol. 55 (1996) 211-224.
    • (1996) J. Neuropath. Exp. Neurol. , vol.55 , pp. 211-224
    • Ikonomidou, C.1    Qin Qin, Y.2    Labruyere, J.3    Olney, J.W.4
  • 68
    • 0030015296 scopus 로고    scopus 로고
    • The chemistry and antioxidant properties of tocopherols and tocotrienols
    • A. Kamal-Eldin, L.-A. Appelqvist, The chemistry and antioxidant properties of tocopherols and tocotrienols, Lipids 31 (1996) 671-701.
    • (1996) Lipids , vol.31 , pp. 671-701
    • Kamal-Eldin, A.1    Appelqvist, L.-A.2
  • 70
    • 0032079517 scopus 로고    scopus 로고
    • Massive mitochondrial degeneration in motor neurons triggers the onset of amyotrophic lateral sclerosis in mice expressing a mutant SOD-1
    • J. Kong, Z. Xu, Massive mitochondrial degeneration in motor neurons triggers the onset of amyotrophic lateral sclerosis in mice expressing a mutant SOD-1, J. Neurosci. 18 (1998) 3241-3250.
    • (1998) J. Neurosci. , vol.18 , pp. 3241-3250
    • Kong, J.1    Xu, Z.2
  • 71
    • 0029983162 scopus 로고    scopus 로고
    • Peroxynitrite disables the tyrosine phosphorylation regulatory mechanism: Lymphocyte-specific tyrosine kinase fails to phosphorylate nitrated cdc2(6-20)NH2 peptide
    • S.-K. Kong, M.B. Yim, E.R. Stadtman, P.B. Chock, Peroxynitrite disables the tyrosine phosphorylation regulatory mechanism: lymphocyte-specific tyrosine kinase fails to phosphorylate nitrated cdc2(6-20)NH2 peptide, Proc. Natl. Acad. Sci. USA 93 (1996) 3377-3382.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3377-3382
    • Kong, S.-K.1    Yim, M.B.2    Stadtman, E.R.3    Chock, P.B.4
  • 72
    • 0030756459 scopus 로고    scopus 로고
    • BCL-2: Prolonging life in a transgenic mouse model of familial amyotrophic lateral sclerosis
    • V. Kostic, V. Jackson-Lewis, F. de Bilbao, M. Dubois-Dauphin, S. Przedborski, BCL-2: prolonging life in a transgenic mouse model of familial amyotrophic lateral sclerosis, Science 277 (1997) 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
  • 73
    • 0028085696 scopus 로고
    • The role of intracellular free calcium in motor neuron disease
    • C. Krieger, K. Jones, S.U. Kim, A.A. Eisen, The role of intracellular free calcium in motor neuron disease, J. Neurol. Sci. 124 (1994) 27-32, (Suppl.).
    • (1994) J. Neurol. Sci. , vol.124 , Issue.SUPPL. , pp. 27-32
    • Krieger, C.1    Jones, K.2    Kim, S.U.3    Eisen, A.A.4
  • 74
    • 0023931776 scopus 로고
    • Identification and quantification of calcium-binding proteins in squid axoplasm
    • M.H. Krinks, C.B. Klee, H.C. Pant, H. Gainer, Identification and quantification of calcium-binding proteins in squid axoplasm, J. Neurosci. 8 (1988) 2172-2182.
    • (1988) J. Neurosci. , vol.8 , pp. 2172-2182
    • Krinks, M.H.1    Klee, C.B.2    Pant, H.C.3    Gainer, H.4
  • 75
    • 0031012304 scopus 로고    scopus 로고
    • Mutations in SOD1 associated with amyotrophic lateral sclerosis cause novel protein interactions
    • C.B. Kunst, E. Mezey, M.J. Brownstein, D. Patterson, Mutations in SOD1 associated with amyotrophic lateral sclerosis cause novel protein interactions, Nature Genet. 15 (1997) 91-94.
    • (1997) Nature Genet. , vol.15 , pp. 91-94
    • Kunst, C.B.1    Mezey, E.2    Brownstein, M.J.3    Patterson, D.4
  • 77
    • 0028116467 scopus 로고
    • A mutant neurofilament subunit causes massive, selective motor neuron death: Implication for the pathogenesis of human motor neuron disease
    • M.K. Lee, J.R. Marszalek, D.W. Cleveland, A mutant neurofilament subunit causes massive, selective motor neuron death: implication for the pathogenesis of human motor neuron disease, Neuron 13 (1994) 975-988.
    • (1994) Neuron , vol.13 , pp. 975-988
    • Lee, M.K.1    Marszalek, J.R.2    Cleveland, D.W.3
  • 78
    • 0027293898 scopus 로고
    • Neurofilaments are obligate heteropolymers in vivo
    • M.K. Lee, Z. Xu, P.C. Wong, D.W. Cleveland, Neurofilaments are obligate heteropolymers in vivo, J. Cell Biol. 122 (1993) 1337-1350.
    • (1993) J. Cell Biol. , vol.122 , pp. 1337-1350
    • Lee, M.K.1    Xu, Z.2    Wong, P.C.3    Cleveland, D.W.4
  • 79
    • 0023668121 scopus 로고
    • Calcium binding to untreated and dephosphorylated porcine neurofilaments
    • S. Lefebvre, W.E. Mushynski, Calcium binding to untreated and dephosphorylated porcine neurofilaments, Biochem. Biophys. Res. Commun. 145 (1987) 1006-1011.
    • (1987) Biochem. Biophys. Res. Commun. , vol.145 , pp. 1006-1011
    • Lefebvre, S.1    Mushynski, W.E.2
  • 80
    • 0023733105 scopus 로고
    • Characterization of the cation-binding properties of porcine neurofilaments
    • S. Lefebvre, W.E. Mushynski, Characterization of the cation-binding properties of porcine neurofilaments, Biochemistry 27 (1988) 8503-8508.
    • (1988) Biochemistry , vol.27 , pp. 8503-8508
    • Lefebvre, S.1    Mushynski, W.E.2
  • 81
    • 0025999463 scopus 로고
    • Cytoskeletal pathology in motor neuron disease
    • L.P. Rowland (Ed.), Raven Press, New York
    • P.N. Leigh, M. Swash, Cytoskeletal pathology in motor neuron disease, in: L.P. Rowland (Ed.), Amyotrophic Lateral Sclerosis and Other Motor Neuron Diseases, Vol. 56, Raven Press, New York, 1991, pp. 115-124.
    • (1991) Amyotrophic Lateral Sclerosis and Other Motor Neuron Diseases , vol.56 , pp. 115-124
    • Leigh, P.N.1    Swash, M.2
  • 82
    • 0032032013 scopus 로고    scopus 로고
    • Aberrant RNa processing in a neurodegenerative disease: The cause for absent EAAT2, a glutamate transporter, in amyotrophic lateral sclerosis
    • C.-L.G. Lin, L.A. Bristol, L. Jin, M. Dykes-Hoberg, T. Crawford, L. Clawson, J.D. Rothstein, Aberrant RNA processing in a neurodegenerative disease: the cause for absent EAAT2, a glutamate transporter, in amyotrophic lateral sclerosis, Neuron 20 (1998) 589-602.
    • (1998) Neuron , vol.20 , pp. 589-602
    • Lin, C.-L.G.1    Bristol, L.A.2    Jin, L.3    Dykes-Hoberg, M.4    Crawford, T.5    Clawson, L.6    Rothstein, J.D.7
  • 83
    • 0026486270 scopus 로고
    • Stable transfection of calbindin-D28k into the GH3 cell line alters calcium currents and intracellular calcium homeostasis
    • P.-M. Lledo, B. Somasundaram, A.J. Morton, P.C. Emson, W.T. Mason, Stable transfection of calbindin-D28k into the GH3 cell line alters calcium currents and intracellular calcium homeostasis, Neuron 9 (1992) 943-954.
    • (1992) Neuron , vol.9 , pp. 943-954
    • Lledo, P.-M.1    Somasundaram, B.2    Morton, A.J.3    Emson, P.C.4    Mason, W.T.5
  • 85
    • 0027730298 scopus 로고
    • Decreased GluR2(B) receptor subunit mRNA expression in cerebellar neurons at risk for degeneration
    • J.E. Margulies, R.W. Cohen, M.S. Levine, J.B. Watson, Decreased GluR2(B) receptor subunit mRNA expression in cerebellar neurons at risk for degeneration, Dev. Neurosci. 15 (1993) 110-120.
    • (1993) Dev. Neurosci. , vol.15 , pp. 110-120
    • Margulies, J.E.1    Cohen, R.W.2    Levine, M.S.3    Watson, J.B.4
  • 86
    • 0026069449 scopus 로고
    • Evidence for calcium-reducing and excitoprotective roles for the calcium-binding protein calbindin-D28k in cultured hippocampal neurons
    • M.P. Mattson, B. Rychlik, C. Chu, S. Christakos, Evidence for calcium-reducing and excitoprotective roles for the calcium-binding protein calbindin-D28k in cultured hippocampal neurons, Neuron 6 (1991) 41-51.
    • (1991) Neuron , vol.6 , pp. 41-51
    • Mattson, M.P.1    Rychlik, B.2    Chu, C.3    Christakos, S.4
  • 87
    • 0028301325 scopus 로고
    • Calcium channels: Cellular roles and molecular mechanisms
    • E.W. McCleskey, Calcium channels: cellular roles and molecular mechanisms, Curr. Opin. Neurobiol. 4 (1994) 304-312.
    • (1994) Curr. Opin. Neurobiol. , vol.4 , pp. 304-312
    • McCleskey, E.W.1
  • 88
    • 0025063609 scopus 로고
    • Excitatory amino acid neurotoxicity and neurodegenerative disease
    • B. Meldrum, J. Garthwaite, Excitatory amino acid neurotoxicity and neurodegenerative disease, Trends Pharmacol. Sci. 11 (1990) 379-387.
    • (1990) Trends Pharmacol. Sci. , vol.11 , pp. 379-387
    • Meldrum, B.1    Garthwaite, J.2
  • 89
    • 0024428392 scopus 로고
    • Focal accumulation of phosphorylated neurofilaments within anterior horn cell in familial amyotrophic lateral sclerosis
    • H. Mizusawa, S. Matsumoto, S.-H. Yen, A. Hirano, R.R. Rojas-Corona, H. Donnenfeld, Focal accumulation of phosphorylated neurofilaments within anterior horn cell in familial amyotrophic lateral sclerosis, Acta Neuropathol. 79 (1989) 37-43.
    • (1989) Acta Neuropathol. , vol.79 , pp. 37-43
    • Mizusawa, H.1    Matsumoto, S.2    Yen, S.-H.3    Hirano, A.4    Rojas-Corona, R.R.5    Donnenfeld, H.6
  • 90
    • 0029793872 scopus 로고    scopus 로고
    • Quantitative immunocytochemical analysis of the spinal cord in G86R superoxide dismutase transgenic mice: Neurochemical correlates of selective vulnerability
    • B.M. Morrison, J.W. Gordon, M.E. Ripps, J.H. Morrison, Quantitative immunocytochemical analysis of the spinal cord in G86R superoxide dismutase transgenic mice: neurochemical correlates of selective vulnerability, J. Comp. Neurol. 373 (1996) 619-631.
    • (1996) J. Comp. Neurol. , vol.373 , pp. 619-631
    • Morrison, B.M.1    Gordon, J.W.2    Ripps, M.E.3    Morrison, J.H.4
  • 91
    • 0032472831 scopus 로고    scopus 로고
    • Time course of neuropathology in the spinal cord of G86R superoxide dismutase transgenic mice
    • B.M. Morrison, W.G. Janssen, J.W. Gordon, J.H. Morrison, Time course of neuropathology in the spinal cord of G86R superoxide dismutase transgenic mice, J. Comp. Neurol. 391 (1998) 64-77.
    • (1998) J. Comp. Neurol. , vol.391 , pp. 64-77
    • Morrison, B.M.1    Janssen, W.G.2    Gordon, J.W.3    Morrison, J.H.4
  • 92
    • 0032527065 scopus 로고    scopus 로고
    • Light and electron microscopic distribution of the AMPA receptor subunit, GluR2, in the spinal cord of control and G86R mutant superoxide dismutase transgenic mice
    • B.M. Morrison, W.G.M. Janssen, J.W. Gordon, J.H. Morrison, Light and electron microscopic distribution of the AMPA receptor subunit, GluR2, in the spinal cord of control and G86R mutant superoxide dismutase transgenic mice, J. Comp. Neurol. 395 (1998) 523-534.
    • (1998) J. Comp. Neurol. , vol.395 , pp. 523-534
    • Morrison, B.M.1    Janssen, W.G.M.2    Gordon, J.W.3    Morrison, J.H.4
  • 93
    • 0029890685 scopus 로고    scopus 로고
    • The Golgi apparatus of spinal cord motor neurons in transgenic mice expressing mutant Cu,Zn superoxide dismutase becomes fragmented in early, preclinical stages of the disease
    • Z. Mourelatos, N.K. Gonatas, A. Stieber, M.E. Gurney, M.C. Dal Canto, The Golgi apparatus of spinal cord motor neurons in transgenic mice expressing mutant Cu,Zn superoxide dismutase becomes fragmented in early, preclinical stages of the disease, Proc. Natl. Acad. Sci. USA 93 (1996) 5472-5477.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5472-5477
    • Mourelatos, Z.1    Gonatas, N.K.2    Stieber, A.3    Gurney, M.E.4    Dal Canto, M.C.5
  • 94
    • 0006035446 scopus 로고    scopus 로고
    • Riluzole treatment following spinal cord injury improves mitochondrial function and increases glutamate and glucose uptake
    • X. Mu, R.D. Azbill, J.E. Springer, Riluzole treatment following spinal cord injury improves mitochondrial function and increases glutamate and glucose uptake, Soc. Neurosci. Abstr. 23 (1997) 541.516.
    • (1997) Soc. Neurosci. Abstr. , vol.23 , pp. 541516
    • Mu, X.1    Azbill, R.D.2    Springer, J.E.3
  • 95
    • 0023738527 scopus 로고
    • Accumulation of phosphorylated neurofilaments in anterior horn motoneurons of amyotrophic lateral sclerosis patients
    • D.G. Munoz, C. Greene, D.P. Perl, D.J. Selkoe, Accumulation of phosphorylated neurofilaments in anterior horn motoneurons of amyotrophic lateral sclerosis patients, J. Neuropathol. Exp. Neurol. 47 (1988) 9-18.
    • (1988) J. Neuropathol. Exp. Neurol. , vol.47 , pp. 9-18
    • Munoz, D.G.1    Greene, C.2    Perl, D.P.3    Selkoe, D.J.4
  • 96
    • 0028149084 scopus 로고
    • Characterization of three yeast copper-zinc superoxide dismutase mutants analogous to those coded for in familial amyotrophic lateral sclerosis
    • C.R. Nishida, E.B. Gralla, J.S. Valentine, Characterization of three yeast copper-zinc superoxide dismutase mutants analogous to those coded for in familial amyotrophic lateral sclerosis, Proc. Natl. Acad. Sci. USA 91 (1994) 9906-9910.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9906-9910
    • Nishida, C.R.1    Gralla, E.B.2    Valentine, J.S.3
  • 97
    • 0027944855 scopus 로고
    • Metals and free radicals in neurodegeneration
    • C.W. Olanow, G.W. Arendash, Metals and free radicals in neurodegeneration, Curr. Opin. Neurol. 7 (1994) 548-558.
    • (1994) Curr. Opin. Neurol. , vol.7 , pp. 548-558
    • Olanow, C.W.1    Arendash, G.W.2
  • 98
    • 0028815433 scopus 로고
    • Superoxide dismutase is an abundant component in cell bodies, dendrites, and axons of motor neurons and in a subset of other neurons
    • C.A. Pardo, Z. Xu, D.R. Borchelt, D.L. Price, S.S. Sisodia, D.W. Cleveland, Superoxide dismutase is an abundant component in cell bodies, dendrites, and axons of motor neurons and in a subset of other neurons, Proc. Natl. Acad. Sci. USA 92 (1995) 954-958.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 954-958
    • Pardo, C.A.1    Xu, Z.2    Borchelt, D.R.3    Price, D.L.4    Sisodia, S.S.5    Cleveland, D.W.6
  • 99
    • 0026452868 scopus 로고
    • Switch in glutamate receptor subunit gene expression in CA1 subfield of hippocampus following global ischemia in rats
    • D.E. Pellegrini-Giampietro, R.S. Zukin, M.V.L. Bennett, S. Cho, W.A. Pulsinelli, Switch in glutamate receptor subunit gene expression in CA1 subfield of hippocampus following global ischemia in rats, Proc. Natl. Acad. Sci. USA 89 (1992) 10499-10503.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10499-10503
    • Pellegrini-Giampietro, D.E.1    Zukin, R.S.2    Bennett, M.V.L.3    Cho, S.4    Pulsinelli, W.A.5
  • 100
    • 0023607666 scopus 로고
    • Brain glutamate deficiency in amyotrophic lateral sclerosis
    • T.L. Perry, S. Hansen, K. Jones, Brain glutamate deficiency in amyotrophic lateral sclerosis, Neurology 37 (1987) 1845-1848.
    • (1987) Neurology , vol.37 , pp. 1845-1848
    • Perry, T.L.1    Hansen, S.2    Jones, K.3
  • 101
    • 0023617392 scopus 로고
    • Abnormal glutamate metabolism in amyotrophic lateral sclerosis
    • A. Plaitakis, J.T. Caroscio, Abnormal glutamate metabolism in amyotrophic lateral sclerosis, Ann. Neurol. 22 (1987) 575-579.
    • (1987) Ann. Neurol. , vol.22 , pp. 575-579
    • Plaitakis, A.1    Caroscio, J.T.2
  • 102
    • 0023804850 scopus 로고
    • The neuroexcitotoxic amino acids glutamate and aspartate are altered in the spinal cord and brain in amyotrophic lateral sclerosis
    • A. Plaitakis, E. Constantakakis, J. Smith, The neuroexcitotoxic amino acids glutamate and aspartate are altered in the spinal cord and brain in amyotrophic lateral sclerosis, Ann. Neurol. 24 (1988) 446-449.
    • (1988) Ann. Neurol. , vol.24 , pp. 446-449
    • Plaitakis, A.1    Constantakakis, E.2    Smith, J.3
  • 104
    • 0028873958 scopus 로고
    • Calcium-activated proteolysis of neurofilament proteins in goldfish Mauthner axons
    • T.D. Raabe, T. Nguyen, G.D. Bittner, Calcium-activated proteolysis of neurofilament proteins in goldfish Mauthner axons, J. Neurobiol. 26 (1995) 253-261.
    • (1995) J. Neurobiol. , vol.26 , pp. 253-261
    • Raabe, T.D.1    Nguyen, T.2    Bittner, G.D.3
  • 105
    • 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
    • S. Rabizadeh, E.B. Gralla, D.R. Borchelt, R. Gwinn, J.S. Valentine, S. Sisodia, P. Wong, M. Lee, H. Hahn, D.E. Bredesen, 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 (1995) 3024-3028.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3024-3028
    • Rabizadeh, S.1    Gralla, E.B.2    Borchelt, D.R.3    Gwinn, R.4    Valentine, J.S.5    Sisodia, S.6    Wong, P.7    Lee, M.8    Hahn, H.9    Bredesen, D.E.10
  • 107
    • 0028303110 scopus 로고
    • A comparative study of the calcium-binding proteins calbindin-D28k, calretinin, calmodulin and parvalbumin in the rat spinal cord
    • K. Ren, M.A. Ruda, A comparative study of the calcium-binding proteins calbindin-D28k, calretinin, calmodulin and parvalbumin in the rat spinal cord, Brain Res. Rev. 19 (1994) 163-179.
    • (1994) Brain Res. Rev. , vol.19 , pp. 163-179
    • Ren, K.1    Ruda, M.A.2
  • 108
    • 0028888945 scopus 로고
    • Transgenic mice expressing an altered murine superoxide dismutase gene provide an animal model of amyotrophic lateral sclerosis
    • M.E. Ripps, G.W. Huntley, P.R. Hof, J.H. Morrison, J.W. Gordon, Transgenic mice expressing an altered murine superoxide dismutase gene provide an animal model of amyotrophic lateral sclerosis, Proc. Natl. Acad. Sci. USA 92 (1995) 689-693.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 689-693
    • Ripps, M.E.1    Huntley, G.W.2    Hof, P.R.3    Morrison, J.H.4    Gordon, J.W.5
  • 111
    • 0027274623 scopus 로고
    • Chronic inhibition of glutamate uptake produces a model of slow neurotoxicity
    • J.D. Rothstein, L. Jin, M. Dykes-Hoberg, R.W. Kuncl, Chronic inhibition of glutamate uptake produces a model of slow neurotoxicity, Proc. Natl. Acad. Sci. USA 90 (1993) 6591-6595.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6591-6595
    • Rothstein, J.D.1    Jin, L.2    Dykes-Hoberg, M.3    Kuncl, R.W.4
  • 112
    • 0029113872 scopus 로고
    • Neuroprotective strategies in a model of chronic glutamate-mediated motor neurons toxicity
    • J.D. Rothstein, R.W. Kuncl, Neuroprotective strategies in a model of chronic glutamate-mediated motor neurons toxicity, J. Neurochem. 65 (1995) 643-651.
    • (1995) J. Neurochem. , vol.65 , pp. 643-651
    • Rothstein, J.D.1    Kuncl, R.W.2
  • 114
    • 0026597010 scopus 로고
    • Decreased glutamate transport by the brain and spinal cord in amyotrophic lateral sclerosis
    • J.D. Rothstein, L.J. Martin, R.W. Kuncl, Decreased glutamate transport by the brain and spinal cord in amyotrophic lateral sclerosis, N. Engl. J. Med. 326 (1992) 1464-1468.
    • (1992) N. Engl. J. Med. , vol.326 , pp. 1464-1468
    • Rothstein, J.D.1    Martin, L.J.2    Kuncl, R.W.3
  • 115
    • 0029030610 scopus 로고
    • Selective loss of glial glutamate transporter GLT-1 in amyotrophic lateral sclerosis
    • J.D. Rothstein, M. Van Kammen, A.I. Levey, L.J. Martin, R.W. Kuncl, Selective loss of glial glutamate transporter GLT-1 in amyotrophic lateral sclerosis, Ann. Neurol. 38 (1995) 73-84.
    • (1995) Ann. Neurol. , vol.38 , pp. 73-84
    • Rothstein, J.D.1    Van Kammen, M.2    Levey, A.I.3    Martin, L.J.4    Kuncl, R.W.5
  • 116
    • 0030900944 scopus 로고    scopus 로고
    • Mechanisms of apoptotic cell death
    • S. Rowan, D.E. Fisher, Mechanisms of apoptotic cell death, Leukemia 11 (1997) 457-465.
    • (1997) Leukemia , vol.11 , pp. 457-465
    • Rowan, S.1    Fisher, D.E.2
  • 117
    • 0345007554 scopus 로고    scopus 로고
    • Blockade of non-NMDA glutamate receptors protects motor neurons from toxicity of SOD-1 mutants linked to familial ALS
    • J. Roy, S. Minotti, L. Dong, D.A. Figlewicz, H.D. Durham, Blockade of non-NMDA glutamate receptors protects motor neurons from toxicity of SOD-1 mutants linked to familial ALS, Soc. Neurosci. Abstr. 23 (1997) 742-749.
    • (1997) Soc. Neurosci. Abstr. , vol.23 , pp. 742-749
    • Roy, J.1    Minotti, S.2    Dong, L.3    Figlewicz, D.A.4    Durham, H.D.5
  • 118
    • 0029884711 scopus 로고    scopus 로고
    • Bcl-2 blocks loss of mitochondrial membrane potential while ICE inhibitors act at a different step during inhibition of death induced by respiratory chain inhibitors
    • S. Shimuzu, Y. Eguchi, W. Kamiike, S. Waguri, Y. Uchiyama, H. Matsuda, Y. Tsujimoto, Bcl-2 blocks loss of mitochondrial membrane potential while ICE inhibitors act at a different step during inhibition of death induced by respiratory chain inhibitors, Oncogene 13 (1996) 21-29.
    • (1996) Oncogene , vol.13 , pp. 21-29
    • Shimuzu, S.1    Eguchi, Y.2    Kamiike, W.3    Waguri, S.4    Uchiyama, Y.5    Matsuda, H.6    Tsujimoto, Y.7
  • 119
    • 0029810307 scopus 로고    scopus 로고
    • Genetics of amyotrophic lateral sclerosis
    • T. Siddique, H.-X. Deng, Genetics of amyotrophic lateral sclerosis, Hum. Mol. Genet. 5 (1996) 1465-1470.
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 1465-1470
    • Siddique, T.1    Deng, H.-X.2
  • 121
    • 0025995296 scopus 로고
    • RNa editing in brain controls a determinant of ion flow in glutamate-gated channels
    • B. Sommer, M. Kohler, R. Sprengel, P.H. Seeburg, RNA editing in brain controls a determinant of ion flow in glutamate-gated channels, Cell 67 (1991) 11-19.
    • (1991) Cell , vol.67 , pp. 11-19
    • Sommer, B.1    Kohler, M.2    Sprengel, R.3    Seeburg, P.H.4
  • 123
    • 0002634911 scopus 로고
    • Clinical features and differential diagnosis of classical motor neuron disease
    • A.C. Williams (Ed.), Chapman & Hall, London
    • R. Tandan, Clinical features and differential diagnosis of classical motor neuron disease, in: A.C. Williams (Ed.), Motor Neuron Disease, Chapman & Hall, London, 1994, pp. 3-28.
    • (1994) Motor Neuron Disease , pp. 3-28
    • Tandan, R.1
  • 124
    • 0026452101 scopus 로고
    • Neurofilament and glial alterations in the cerebral cortex in amyotrophic lateral sclerosis
    • D. Troost, P.A.E. Sillevis Smitt, J.M.B.V. de Jong, D.F. Swaab, Neurofilament and glial alterations in the cerebral cortex in amyotrophic lateral sclerosis, Acta Neuropathol. 84 (1992) 664-673.
    • (1992) Acta Neuropathol. , vol.84 , pp. 664-673
    • Troost, D.1    Sillevis Smitt, P.A.E.2    De Jong, J.M.B.V.3    Swaab, D.F.4
  • 127
    • 0029966363 scopus 로고    scopus 로고
    • Transgenic mice carrying a human mutant superoxide dismutase transgene develop neuronal cytoskeletal pathology resembling human amyotrophic lateral sclerosis lesions
    • P.-H. Tu, P. Raju, K.A. Robinson, M.E. Gurney, J.Q. Trojanowski, V.M.-Y. Lee, 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 (1996) 3155-3160.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3155-3160
    • Tu, P.-H.1    Raju, P.2    Robinson, K.A.3    Gurney, M.E.4    Trojanowski, J.Q.5    Lee, V.M.-Y.6
  • 128
    • 0027292287 scopus 로고
    • Molecular pharmacology of vitamin E: Structural aspects of antioxidant activity
    • S.A.B.E. van Acker, L.M.H. Koymans, A. Bast, Molecular pharmacology of vitamin E: structural aspects of antioxidant activity, Free Rad. Biol. Med. 15 (1993) 311-328.
    • (1993) Free Rad. Biol. Med. , vol.15 , pp. 311-328
    • Van Acker, S.A.B.E.1    Koymans, L.M.H.2    Bast, A.3
  • 131
    • 0028057395 scopus 로고
    • Changes in neurofilament protein NF-L and NF-H immunoreactivity following kainic acid-induced seizures
    • S. Wang, A. Hamberger, Q. Yang, K.G. Haglid, Changes in neurofilament protein NF-L and NF-H immunoreactivity following kainic acid-induced seizures, J. Neurochem. 62 (1994) 739-748.
    • (1994) J. Neurochem. , vol.62 , pp. 739-748
    • Wang, S.1    Hamberger, A.2    Yang, Q.3    Haglid, K.G.4
  • 132
    • 0026041623 scopus 로고
    • Slow non-NMDA receptor mediated neurotoxicity and amyotrophic lateral sclerosis
    • L.P. Rowland (Ed.), Raven Press
    • J.H. Weiss, D.W. Choi, Slow non-NMDA receptor mediated neurotoxicity and amyotrophic lateral sclerosis, in: L.P. Rowland (Ed.), Amyotrophic Lateral Sclerosis and Other Motor Neuron Diseases, Vol. 56, Raven Press, 1991, pp. 311-318.
    • (1991) Amyotrophic Lateral Sclerosis and Other Motor Neuron Diseases , vol.56 , pp. 311-318
    • Weiss, J.H.1    Choi, D.W.2
  • 133
    • 0028137817 scopus 로고
    • Mitochondria buffer physiological calcium loads in cultured rat dorsal root ganglion neurons
    • J.L. Werth, S.A. Thayer, Mitochondria buffer physiological calcium loads in cultured rat dorsal root ganglion neurons, J. Neurosci. 14 (1994) 348-356.
    • (1994) J. Neurosci. , vol.14 , pp. 348-356
    • Werth, J.L.1    Thayer, S.A.2
  • 134
    • 0028985491 scopus 로고
    • 2+ exchange buffer glutamate-induced calcium loads in cultured cortical neurons
    • 2+ exchange buffer glutamate-induced calcium loads in cultured cortical neurons, J. Neurosci. 15 (1995) 1318-1328.
    • (1995) J. Neurosci. , vol.15 , pp. 1318-1328
    • White, R.J.1    Reynolds, I.J.2
  • 137
    • 0029053881 scopus 로고
    • An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria
    • P.C. Wong, C.A. Pardo, D.R. Borchelt, M.K. Lee, N.G. Copeland, N.A. Jenkins, S.S. Sisodia, D.W. Cleveland, D.L. Price, An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria, Neuron 14 (1995) 1105-1116.
    • (1995) Neuron , vol.14 , pp. 1105-1116
    • Wong, P.C.1    Pardo, C.A.2    Borchelt, D.R.3    Lee, M.K.4    Copeland, N.G.5    Jenkins, N.A.6    Sisodia, S.S.7    Cleveland, D.W.8    Price, D.L.9
  • 138
    • 0027410516 scopus 로고
    • Increased expression of neurofilament subunit NF-L produces morphological alterations that resemble the pathology of human motor neuron disease
    • Z. Xu, L.C. Cork, J.W. Griffin, D.W. Cleveland, Increased expression of neurofilament subunit NF-L produces morphological alterations that resemble the pathology of human motor neuron disease, Cell 73 (1993) 23-33.
    • (1993) Cell , vol.73 , pp. 23-33
    • Xu, Z.1    Cork, L.C.2    Griffin, J.W.3    Cleveland, D.W.4
  • 140
    • 0030817291 scopus 로고    scopus 로고
    • Neurofilaments and orthograde transport are reduced in ventral root axons of transgenic mice that express human SOD1 with a G93a mutation
    • B. Zhang, P.-H. Tu, F. Abtahian, J.Q. Trojanowski, V.M.-Y. Lee, Neurofilaments and orthograde transport are reduced in ventral root axons of transgenic mice that express human SOD1 with a G93A mutation, J. Cell Biol. 139 (1997) 1307-1315.
    • (1997) J. Cell Biol. , vol.139 , pp. 1307-1315
    • Zhang, B.1    Tu, P.-H.2    Abtahian, F.3    Trojanowski, J.Q.4    Lee, V.M.-Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.