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Volumn 2, Issue 11, 2001, Pages 806-819

From charcot to lou gehrig: deciphering selective motor neuron death in als

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE; COPPER; CPP32 PROTEIN; ENDOTHELIAL CELL GROWTH FACTOR; LYMPHOKINE; NEUROFILAMENT PROTEIN; SUPEROXIDE DISMUTASE; SUPEROXIDE DISMUTASE 1; VASCULOTROPIN; ZINC;

EID: 0035516124     PISSN: 1471003X     EISSN: 14710048     Source Type: Journal    
DOI: 10.1038/35097565     Document Type: Article
Times cited : (1228)

References (157)
  • 1
    • 0000280462 scopus 로고
    • Deux cas d'atrophie musculaire progressive avec lesions de la substance grise et des faisceaux antero-lateraux de la moelle epiniere
    • Charcot, J. M. & Joffory, A. Deux cas d'atrophie musculaire progressive avec lesions de la substance grise et des faisceaux antero-lateraux de la moelle epiniere. Arch. Physiol. Weurol. Pathol. 2, 744-754 (1869).
    • (1869) Arch. Physiol. Weurol. Pathol. , vol.2 , pp. 744-754
    • Charcot, J.M.1    Joffory, A.2
  • 2
    • 0023000254 scopus 로고
    • Follow-up study on amyotrophic lateral sclerosis in Rochester, Minn., 1925 through 1984
    • Yoshida, S., Mulder, D. W., Kurland, L. T., Chu, C. P & Okazaki, H. Follow-up study on amyotrophic lateral sclerosis in Rochester, Minn., 1925 through 1984. Weuroepidemiology 5, 61-70 (1986).
    • (1986) Weuroepidemiology , vol.5 , pp. 61-70
    • Yoshida, S.1    Mulder, D.W.2    Kurland, L.T.3    Chu, C.P.4    Okazaki, H.5
  • 3
    • 0027401203 scopus 로고
    • Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis
    • Rosen, D. R. et al. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Wature 362, 59-62 (1993).
    • (1993) Wature , vol.362 , pp. 59-62
    • Rosen, D.R.1
  • 4
    • 0021167918 scopus 로고
    • Fine structural observations of neurofilamentous changes in amyotrophic lateral sclerosis
    • Hirano, A., Donnenfeld, H., Sasaki, S. & Nakano, I. Fine structural observations of neurofilamentous changes in amyotrophic lateral sclerosis. J. Weuropathol. Exp. Weurol. 43, 461-470 (1984).
    • (1984) J. Weuropathol. Exp. Weurol. , vol.43 , pp. 461-470
    • Hirano, A.1    Donnenfeld, H.2    Sasaki, S.3    Nakano, I.4
  • 5
    • 0021157469 scopus 로고
    • Fine structural study of neurofibrillary changes in a family with amyotrophic lateral sclerosis
    • Hirano, A. et al. Fine structural study of neurofibrillary changes in a family with amyotrophic lateral sclerosis. J. Weuropathol. Exp. Weurol. 43, 471-480 (1984).
    • (1984) J. Weuropathol. Exp. Weurol. , vol.43 , pp. 471-480
    • Hirano, A.1
  • 6
    • 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. Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1. Science 281, 1851-1854 (1998).
    • (1998) Science , vol.281 , pp. 1851-1854
    • Bruijn, L.I.1
  • 7
    • 0022443737 scopus 로고
    • Familial adult motor neuron disease: Amyotrophic lateral sclerosis
    • Mulder, D. W., Kurland, L. T., Offord, K. P. & Beard, C. M. Familial adult motor neuron disease: amyotrophic lateral sclerosis. Neurology 36, 511-517 (1986).
    • (1986) Neurology , vol.36 , pp. 511-517
    • Mulder, D.W.1    Kurland, L.T.2    Offord, K.P.3    Beard, C.M.4
  • 8
    • 15844429977 scopus 로고    scopus 로고
    • Superoxide dismutase activity is essential for stationary phase survival in Saccharomyces cerevisiae. Mitochondrial production of toxic oxygen species in vivo
    • Longo, V. D., Gralla, E. B. & Valentine, J. S. Superoxide dismutase activity is essential for stationary phase survival in Saccharomyces cerevisiae. Mitochondrial production of toxic oxygen species in vivo. J. Biol. Chem. 271, 12275-12280 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 12275-12280
    • Longo, V.D.1    Gralla, E.B.2    Valentine, J.S.3
  • 9
    • 0347233829 scopus 로고    scopus 로고
    • (eds Brown, R. H., Meininger, V & Swash, M., Martin Dunitz, London
    • Andersen, P M., Morita, M. & Brown, R. H. Jr. in Amyotrophic Lateral Sclerosis (eds Brown, R. H., Meininger, V & Swash, M.) 223-250 (Martin Dunitz, London, 2000).
    • (2000) Amyotrophic Lateral Sclerosis , pp. 223-250
    • Andersen, P.M.1    Morita, M.2    Brown, R.H.3
  • 12
    • 0029010496 scopus 로고
    • Amyotrophic lateral sclerosis associated with homozygosity for an Asp90Ala mutation in CuZn-superoxide dismutase
    • Andersen, P M. et al. Amyotrophic lateral sclerosis associated with homozygosity for an Asp90Ala mutation in CuZn-superoxide dismutase. Wature Genet. 10, 61-66 (1995).
    • (1995) Wature Genet , vol.10 , pp. 61-66
    • Andersen, P.M.1
  • 13
    • 9544236295 scopus 로고    scopus 로고
    • Autosomal recessive adult-onset amyotrophic lateral sclerosis associated with homozygosity for Asp90Ala CuZn-superoxide dismutase mutation. A clinical and genealogical study of 36 patients
    • Andersen, P M. et al. Autosomal recessive adult-onset amyotrophic lateral sclerosis associated with homozygosity for Asp90Ala CuZn-superoxide dismutase mutation. A clinical and genealogical study of 36 patients. Brain 119, 1153-1172 (1996).
    • (1996) Brain , vol.119 , pp. 1153-1172
    • Andersen, P.M.1
  • 14
    • 0027426169 scopus 로고
    • Amyotrophic lateral sclerosis and structural defects in Cu, Zn superoxide dismutase
    • Deng, H. X. et al. Amyotrophic lateral sclerosis and structural defects in Cu, Zn superoxide dismutase. Science 261, 1047-1051 (1993).
    • (1993) Science , vol.261 , pp. 1047-1051
    • Deng, H.X.1
  • 16
    • 0028284779 scopus 로고
    • Motor neuron degeneration in mice that express a human Cu, Zn superoxide dismutase mutation
    • Gurney, M. E. et al. Motor neuron degeneration in mice that express a human Cu, Zn superoxide dismutase mutation. Science 264, 1772-1775 (1994).
    • (1994) Science , vol.264 , pp. 1772-1775
    • Gurney, M.E.1
  • 17
    • 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. An adverse property of a familial ALS- linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria. Weuron 14, 1105-1116 (1995).
    • (1995) Weuron , vol.14 , pp. 1105-1116
    • Wong, P.C.1
  • 18
    • 0028888945 scopus 로고
    • Transgenic mice expressing an altered murine superoxide dismutase gene provide an animal model of amyotrophic lateral sclerosis
    • Ripps, M. E., Huntley, G. W., Hof, P R., Morrison, J. H. & Gordon, J. W. Transgenic mice expressing an altered murine superoxide dismutase gene provide an animal model of amyotrophic lateral sclerosis. Proc. WatlAcad. Sci. USA 92, 689-693 (1995).
    • (1995) Proc. Watlacad. 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
  • 19
    • 0031051485 scopus 로고    scopus 로고
    • ALS-linked SOD1 mutant G85R mediates damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions
    • Bruijn, L. I. et al. ALS-linked SOD1 mutant G85R mediates damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions. Weuron 18, 327-338 (1997).
    • (1997) Weuron , vol.18 , pp. 327-338
    • Bruijn, L.I.1
  • 20
    • 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. Motor neurons in Cu/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury. Wature Genet. 13, 43-47 (1996).
    • (1996) Wature Genet , vol.13 , pp. 43-47
    • Reaume, A.G.1
  • 21
    • 0027965073 scopus 로고
    • Superoxide dismutase 1 with mutations linked to familial amyotrophic lateral sclerosis possesses significant activity
    • Borchelt, D. R. et al. Superoxide dismutase 1 with mutations linked to familial amyotrophic lateral sclerosis possesses significant activity. Proc. Watl Acad. Sci. USA 91, 8292-8296 (1994).
    • (1994) Proc. Watl Acad. Sci. USA , vol.91 , pp. 8292-8296
    • Borchelt, D.R.1
  • 22
    • 0028940996 scopus 로고
    • Superoxide dismutase concentration and activity in familial amyotrophic lateral sclerosis
    • Bowling, A. C. et al. Superoxide dismutase concentration and activity in familial amyotrophic lateral sclerosis. J. Weurochem. 64, 2366-2369 (1995).
    • (1995) J. Weurochem. , vol.64 , pp. 2366-2369
    • Bowling, A.C.1
  • 23
  • 24
    • 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. & Przedborski, S. Bcl-2: prolonging life in a transgenic mouse model of familial amyotrophic lateral sclerosis. Science 277, 559-562 (1997).
    • (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
  • 25
    • 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. Delaying caspase activation by Bcl-2: a clue to disease retardation in a transgenic mouse model of amyotrophic lateral sclerosis. J. Weurosci. 20, 9119-9125 (2000).
    • (2000) J. Weurosci. , vol.20 , pp. 9119-9125
    • Vukosavic, S.1
  • 26
    • 0034647003 scopus 로고    scopus 로고
    • Functional role of caspase-1 and caspase-3 in an ALS transgenic mouse model
    • Li, M. et al. Functional role of caspase-1 and caspase-3 in an ALS transgenic mouse model. Science 288, 335-339 (2000).
    • (2000) Science , vol.288 , pp. 335-339
    • Li, M.1
  • 27
    • 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 & Cleveland, D. W. Caspase-1 and -3 are sequentially activated in motor neuron death in Cu, Zn superoxide dismutase-mediated familial amyotrophic lateral sclerosis. Proc. Watl Acad. Sci. USA 97, 13901-13906 (2000).
    • (2000) Proc. Watl Acad. Sci. USA , vol.97 , pp. 13901-13906
    • Pasinelli, P.1    Houseweart, M.K.2    Brown, R.H.3    Cleveland, D.W.4
  • 28
    • 0035437866 scopus 로고    scopus 로고
    • Recruitment of the mitochondrial- dependent apoptotic pathway in amyotrophic lateral sclerosis
    • Guegan, C., Vila, M., Rosoklija, G., Hays, A. P & Przedborski, S. Recruitment of the mitochondrial- dependent apoptotic pathway in amyotrophic lateral sclerosis. J. Weurosci. 21, 6569-6576 (2001).
    • (2001) J. Weurosci. , vol.21 , pp. 6569-6576
    • Guegan, C.1    Vila, M.2    Rosoklija, G.3    Hays, A.P.4    Przedborski, S.5
  • 29
    • 0032568546 scopus 로고    scopus 로고
    • Chaperone-facilitated copper binding is a property common to several classes of familial amyotrophic lateral sclerosis- linked superoxide dismutase mutants
    • Corson, L. B., Strain, J. J., Culotta, V C. & Cleveland, D. W. Chaperone-facilitated copper binding is a property common to several classes of familial amyotrophic lateral sclerosis- linked superoxide dismutase mutants. Proc. Watl Acad. Sci. USA 95, 6361-6366 (1998).
    • (1998) Proc. Watl Acad. Sci. USA , vol.95 , pp. 6361-6366
    • Corson, L.B.1    Strain, J.J.2    Culotta, V.C.3    Cleveland, D.W.4
  • 31
    • 0030767498 scopus 로고    scopus 로고
    • Increased 3-nitrotyrosine and oxidative damage in mice with a human copper/zinc superoxide dismutase mutation
    • Ferrante, R. J. et al. Increased 3-nitrotyrosine and oxidative damage in mice with a human copper/zinc superoxide dismutase mutation. Ann. Weurol. 42, 326-334 (1997).
    • (1997) Ann. Weurol. , vol.42 , pp. 326-334
    • Ferrante, R.J.1
  • 32
    • 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
    • Bruijn, L. I. et al. 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. Watl Acad. Sci. USA 94, 7606-7611 (1997).
    • (1997) Proc. Watl Acad. Sci. USA 94 , pp. 7606-7611
    • Bruijn, L.I.1
  • 33
    • 0031784348 scopus 로고    scopus 로고
    • Protein oxidative damage in a transgenic mouse model of familial amyotrophic lateral sclerosis
    • Andrus, P K., Fleck, T J., Gurney, M. E. & Hall, E. D. Protein oxidative damage in a transgenic mouse model of familial amyotrophic lateral sclerosis. J. Weurochem. 71, 2041-2048 (1998).
    • (1998) J. Weurochem. , vol.71 , pp. 2041-2048
    • Andrus, P.K.1    Fleck, T.J.2    Gurney, M.E.3    Hall, E.D.4
  • 34
    • 0030851761 scopus 로고    scopus 로고
    • Increased 3-nitrotyrosine in both sporadic and familial amyotrophic lateral sclerosis
    • Beal, M. F. et al. Increased 3-nitrotyrosine in both sporadic and familial amyotrophic lateral sclerosis. Ann. Weurol. 42, 644-654 (1997).
    • (1997) Ann. Weurol. , vol.42 , pp. 644-654
    • Beal, M.F.1
  • 35
    • 0034520591 scopus 로고    scopus 로고
    • Human Cu/Zn superoxide dismutase (SOD1) overexpression in mice causes mitochondrial vacuolization, axonal degeneration, and premature motoneuron death and accelerates motoneuron disease in mice expressing a familial amyotrophic lateral sclerosis mutant SOD1
    • Jaarsma, D. et al. Human Cu/Zn superoxide dismutase (SOD1) overexpression in mice causes mitochondrial vacuolization, axonal degeneration, and premature motoneuron death and accelerates motoneuron disease in mice expressing a familial amyotrophic lateral sclerosis mutant SOD1. Weurobiol. Dis. 7, 623-643 (2000).
    • (2000) Weurobiol. Dis. , vol.7 , pp. 623-643
    • Jaarsma, D.1
  • 36
    • 0029671220 scopus 로고    scopus 로고
    • Altered reactivity of superoxide dismutase in familial amyotrophic lateral sclerosis
    • Wiedau-Pazos, M. et al. Altered reactivity of superoxide dismutase in familial amyotrophic lateral sclerosis. Science 271, 515-518 (1996).
    • (1996) Science , vol.271 , pp. 515-518
    • Wiedau-Pazos, M.1
  • 37
    • 0032499788 scopus 로고    scopus 로고
    • Reexamination of the mechanism of hydroxyl radical adducts formed from the reaction between familial amyotrophic lateral sclerosis-associated Cu, Zn superoxide dismutase mutants and H2O2
    • 2. Proc. Watl Acad. Sci. USA 95, 6675-6680 (1998).
    • (1998) Proc. Watl Acad. Sci. USA , vol.95 , pp. 6675-6680
    • Singh, R.J.1
  • 38
    • 0032127330 scopus 로고    scopus 로고
    • Relationship of oxygen radical-induced lipid peroxidative damage to disease onset and progression in a transgenic model of familial ALS
    • Hall, E. D., Andrus, P. K., Oostveen, J. A., Fleck, T J. & Gurney, M. E. Relationship of oxygen radical-induced lipid peroxidative damage to disease onset and progression in a transgenic model of familial ALS. J. Weurosci. Res. 53, 66-77 (1998).
    • (1998) J. Weurosci. Res. , vol.53 , pp. 66-77
    • Hall, E.D.1    Rus, P.K.2    Oostveen, J.A.3    Fleck, T.J.4    Gurney, M.E.5
  • 39
    • 0028813380 scopus 로고
    • Superoxide dismutase 1 subunits with mutations linked to familial amyotrophic lateral sclerosis do not affect wild-type subunit function
    • Borchelt, D. R. et al. Superoxide dismutase 1 subunits with mutations linked to familial amyotrophic lateral sclerosis do not affect wild-type subunit function. J. Biol. Chem. 270, 3234-3238 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 3234-3238
    • Borchelt, D.R.1
  • 40
    • 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, Thompson, J. A. & Beckman, J. S. Decreased zinc affinity of amyotrophic lateral sclerosis-associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite. J. Weurochem. 69, 1936-1944 (1997).
    • (1997) J. Weurochem. , vol.69 , pp. 1936-1944
    • Crow, J.P.1    Sampson, J.B.2    Zhuang, Y.3    Thompson, J.A.4    Beckman, J.S.5
  • 41
    • 0039251419 scopus 로고    scopus 로고
    • Induction of nitric oxide-dependent apoptosis in motor neurons by zinc-deficient superoxide dismutase
    • Estevez, A. G. et al. Induction of nitric oxide-dependent apoptosis in motor neurons by zinc-deficient superoxide dismutase. Science 286, 2498-2500 (1999).
    • (1999) Science , vol.286 , pp. 2498-2500
    • Estevez, A.G.1
  • 42
    • 0034696741 scopus 로고    scopus 로고
    • Toxicity of ALS-linked SOD1 mutants
    • Williamson, T. L. et al. Toxicity of ALS-linked SOD1 mutants. Science 288, 399-400 (2000).
    • (2000) Science , vol.288 , pp. 399-400
    • Williamson, T.L.1
  • 43
    • 0033977325 scopus 로고    scopus 로고
    • Loss of in vitro metal ion binding specificity in mutant copper-zinc superoxide dismutases associated with familial amyotrophic lateral sclerosis
    • Goto, J. J. et al. Loss of in vitro metal ion binding specificity in mutant copper-zinc superoxide dismutases associated with familial amyotrophic lateral sclerosis. J. Biol. Chem. 275, 1007-1014 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 1007-1014
    • Goto, J.J.1
  • 44
    • 0032954386 scopus 로고    scopus 로고
    • Lack of involvement of neuronal nitric oxide synthase in the pathogenesis of a transgenic mouse model of familial amyotrophic lateral sclerosis
    • Facchinetti, F. et al. Lack of involvement of neuronal nitric oxide synthase in the pathogenesis of a transgenic mouse model of familial amyotrophic lateral sclerosis. Weuroscience 90, 1483-1492 (1999).
    • (1999) Weuroscience , vol.90 , pp. 1483-1492
    • Facchinetti, F.1
  • 45
    • 0035826750 scopus 로고    scopus 로고
    • Nitrotyrosination contributes minimally to toxicity of mutant SOD1 associated with ALS
    • Doroudchi, M. M., Minotti, S., Figlewicz, D. A. & Durham, H. D. Nitrotyrosination contributes minimally to toxicity of mutant SOD1 associated with ALS. Weuroreport 12, 1239-1243 (2001).
    • (2001) Weuroreport , vol.12 , pp. 1239-1243
    • Doroudchi, M.M.1    Minotti, S.2    Figlewicz, D.A.3    Durham, H.D.4
  • 46
    • 0029082389 scopus 로고
    • Oxidative damage to protein in sporadic motor neuron disease spinal cord
    • Shaw, P J., Ince, P. G., Falkous, G. & Mantle, D. Oxidative damage to protein in sporadic motor neuron disease spinal cord. Ann. Weurol. 38, 691-695 (1995).
    • (1995) Ann. Weurol. , vol.38 , pp. 691-695
    • Shaw, P.J.1    Ince, P.G.2    Falkous, G.3    Mantle, D.4
  • 47
    • 0027359334 scopus 로고
    • Superoxide dismutase activity, oxidative damage, and mitochondrial energy metabolism in familial and sporadic amyotrophic lateral sclerosis
    • Bowling, A. C., Schulz, J. B., Brown, R. H. Jr & Beal, M. F. Superoxide dismutase activity, oxidative damage, and mitochondrial energy metabolism in familial and sporadic amyotrophic lateral sclerosis. J. Weurochem. 61, 2322-2325 (1993).
    • (1993) J. Weurochem. , vol.61 , pp. 2322-2325
    • Bowling, A.C.1    Schulz, J.B.2    Brown, R.H.3    Beal, M.F.4
  • 48
    • 0027946294 scopus 로고
    • Development of central nervous system pathology in a murine transgenic model of human amyotrophic lateral sclerosis
    • Dal Canto, M. C. & Gurney, M. E. Development of central nervous system pathology in a murine transgenic model of human amyotrophic lateral sclerosis. Am. J. Pathol. 145, 1271-1279 (1994).
    • (1994) Am. J. Pathol. , vol.145 , pp. 1271-1279
    • Dal Canto, M.C.1    Gurney, M.E.2
  • 49
    • 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. & Xu, Z. Massive mitochondrial degeneration in motor neurons triggers the onset of amyotrophic lateral sclerosis in mice expressing a mutant SOD1. J. Weurosci. 18, 3241-3250 (1998).
    • (1998) J. Weurosci. , vol.18 , pp. 3241-3250
    • Kong, J.1    Xu, Z.2
  • 50
    • 0030802648 scopus 로고    scopus 로고
    • The copper chaperone for superoxide dismutase
    • Culotta, V. C. et al. The copper chaperone for superoxide dismutase. J. Biol. Chem. 272, 23469-23472 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 23469-23472
    • Culotta, V.C.1
  • 51
    • 0034646410 scopus 로고    scopus 로고
    • Copper chaperone for superoxide dismutase is essential to activate mammalian Cu/Zn superoxide dismutase
    • Wong, P. C. et al. Copper chaperone for superoxide dismutase is essential to activate mammalian Cu/Zn superoxide dismutase. Proc. Watl Acad. Sci. USA 97, 2886-2891 (2000).
    • (2000) Proc. Watl Acad. Sci. USA , vol.97 , pp. 2886-2891
    • Wong, P.C.1
  • 52
    • 0030813067 scopus 로고    scopus 로고
    • Evidence of increased oxidative damage in both sporadic and familial amyotrophic lateral sclerosis
    • Ferrante, R. J. et al. Evidence of increased oxidative damage in both sporadic and familial amyotrophic lateral sclerosis. J. Weurochem. 69, 2064-2074 (1997).
    • (1997) J. Weurochem. , vol.69 , pp. 2064-2074
    • Ferrante, R.J.1
  • 53
    • 0033749379 scopus 로고    scopus 로고
    • Formation of high molecular weight complexes of mutant Cu, Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis
    • Johnston, J. A., Dalton, M. J., Gurney, M. E. & Kopito, R. R. Formation of high molecular weight complexes of mutant Cu, Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis. Proc. Watl Acad. Sci. USA 97, 12571-12576 (2000).
    • (2000) Proc. Watl Acad. Sci. USA , vol.97 , pp. 12571-12576
    • Johnston, J.A.1    Dalton, M.J.2    Gurney, M.E.3    Kopito, R.R.4
  • 54
    • 0027190478 scopus 로고
    • Histochemical and immunocytochemical study of ubiquitinated neuronal inclusions in amyotrophic lateral sclerosis
    • Mather, K. et al. Histochemical and immunocytochemical study of ubiquitinated neuronal inclusions in amyotrophic lateral sclerosis. Weuropathol.Appl. Weurobiol. 19, 141-145 (1993).
    • (1993) Weuropathol.Appl. Weurobiol. , vol.19 , pp. 141-145
    • Mather, K.1
  • 55
    • 0025729489 scopus 로고
    • Ubiquitin-immunoreactive intraneuronal inclusions in amyotrophic lateral sclerosis. Morphology, distribution, and specificity
    • Leigh, P N. et al. Ubiquitin-immunoreactive intraneuronal inclusions in amyotrophic lateral sclerosis. Morphology, distribution, and specificity. Brain 114, 775-788 (1991).
    • (1991) Brain , vol.114 , pp. 775-788
    • Leigh, P.N.1
  • 56
    • 0023823645 scopus 로고
    • Ubiquitin deposits in anterior horn cells in motor neurone disease
    • Leigh, P N. et al. Ubiquitin deposits in anterior horn cells in motor neurone disease. Weurosci. Lett. 93, 197-203 (1988).
    • (1988) Weurosci. Lett. , vol.93 , pp. 197-203
    • Leigh, P.N.1
  • 57
    • 0344507132 scopus 로고    scopus 로고
    • Up-regulation of protein chaperones preserves viability of cells expressing toxic Cu/Zn- superoxide dismutase mutants associated with amyotrophic lateral sclerosis
    • Bruening, W. et al. Up-regulation of protein chaperones preserves viability of cells expressing toxic Cu/Zn- superoxide dismutase mutants associated with amyotrophic lateral sclerosis. J. Weurochem. 72, 693-699 (1999).
    • (1999) J. Weurochem. , vol.72 , pp. 693-699
    • Bruening, W.1
  • 58
    • 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. & Figlewicz, D. A. Aggregation of mutant Cu/Zn superoxide dismutase proteins in a culture model of ALS. J. Weuropathol. Exp. Weurol. 56, 523-530 (1997).
    • (1997) J. Weuropathol. Exp. Weurol. , vol.56 , pp. 523-530
    • Durham, H.D.1    Roy, J.2    Dong, L.3    Figlewicz, D.A.4
  • 59
    • 13344286293 scopus 로고    scopus 로고
    • Knockout of glutamate transporters reveals a major role for astroglial transport in excitotoxicity and clearance of glutamate
    • Rothstein, J. D. et al. Knockout of glutamate transporters reveals a major role for astroglial transport in excitotoxicity and clearance of glutamate. Weuron 16, 675-686 (1996).
    • (1996) Weuron , vol.16 , pp. 675-686
    • Rothstein, J.D.1
  • 60
    • 0034651102 scopus 로고    scopus 로고
    • Restricted expression of G86R Cu/Zn superoxide dismutase in astrocytes results in astrocytosis but does not cause motoneuron degeneration
    • Gong, Y. H., Parsadanian, A. S., Andreeva, A., Snider, W. D. & Elliott, J. L. Restricted expression of G86R Cu/Zn superoxide dismutase in astrocytes results in astrocytosis but does not cause motoneuron degeneration. J. Weurosci. 20, 660-665 (2000).
    • (2000) J. Weurosci. , vol.20 , pp. 660-665
    • Gong, Y.H.1    Parsadanian, A.S.2    Reeva, A.3    Snider, W.D.4    Elliott, J.L.5
  • 61
    • 0032482976 scopus 로고    scopus 로고
    • Absence of neurofilaments reduces the selective vulnerability of motor neurons and slows disease caused by a familial amyotrophic lateral sclerosis- linked superoxide dismutase 1 mutant
    • Williamson, T. L. et al. Absence of neurofilaments reduces the selective vulnerability of motor neurons and slows disease caused by a familial amyotrophic lateral sclerosis- linked superoxide dismutase 1 mutant. Proc. Watl Acad. Sci. USA 95, 9631-9636 (1998).
    • (1998) Proc. Watl Acad. Sci. USA , vol.95 , pp. 9631-9636
    • Williamson, T.L.1
  • 62
    • 0032483016 scopus 로고    scopus 로고
    • Protective effect of neurofilament heavy gene overexpression in motor neuron disease induced by mutant superoxide dismutase
    • Couillard-Despres, S. et al. Protective effect of neurofilament heavy gene overexpression in motor neuron disease induced by mutant superoxide dismutase. Proc. Watl Acad. Sci. USA 95, 9626-9630 (1998).
    • (1998) Proc. Watl Acad. Sci. USA , vol.95 , pp. 9626-9630
    • Couillard-Despres, S.1
  • 63
    • 0035873076 scopus 로고    scopus 로고
    • Neuron-specific expression of mutant superoxide dismutase 1 in transgenic mice does not lead to motor impairment
    • Pramatarova, A., Laganiere, J., Roussel, J., Brisebois, K. & Rouleau, G. A. Neuron-specific expression of mutant superoxide dismutase 1 in transgenic mice does not lead to motor impairment. J. Weurosci. 21, 3369-3374 (2001).
    • (2001) J. Weurosci. , vol.21 , pp. 3369-3374
    • Pramatarova, A.1    Laganiere, J.2    Roussel, J.3    Brisebois, K.4    Rouleau, G.A.5
  • 64
    • 0014336826 scopus 로고
    • Proximal axonal enlargement in motor neuron disease
    • Carpenter, S. Proximal axonal enlargement in motor neuron disease. Weurology 18, 841-851 (1968).
    • (1968) Weurology , vol.18 , pp. 841-851
    • Carpenter, S.1
  • 65
    • 0027410516 scopus 로고
    • Increased expression of neurofilament subunit NF-L produces morphological alterations that resemble the pathology of human motor neuron disease
    • Xu, Z., Cork, L. C., Griffin, J. W. & Cleveland, D. W. Increased expression of neurofilament subunit NF-L produces morphological alterations that resemble the pathology of human motor neuron disease. Cell 73, 23-33 (1993).
    • (1993) Cell , vol.73 , pp. 23-33
    • Xu, Z.1    Cork, L.C.2    Griffin, J.W.3    Cleveland, D.W.4
  • 66
    • 0027465098 scopus 로고
    • P Progressive neuronopathy in transgenic mice expressing the human neurofilament heavy gene: A mouse model of amyotrophic lateral sclerosis
    • Cote, F., Collard, J. F. & Julien, J. P Progressive neuronopathy in transgenic mice expressing the human neurofilament heavy gene: a mouse model of amyotrophic lateral sclerosis. Cell 73, 35-46 (1993).
    • (1993) Cell , vol.73 , pp. 35-46
    • Cote, F.1    Collard, J.F.2    Julien, J.3
  • 67
    • 0033830020 scopus 로고    scopus 로고
    • Extra axonal neurofilaments do not exacerbate disease caused by mutant Cu, Zn superoxide dismutase
    • Couillard-Despres, S., Meier, J. & Julien, J. P. Extra axonal neurofilaments do not exacerbate disease caused by mutant Cu, Zn superoxide dismutase. Weurobiol. Dis. 7, 462-470 (2000).
    • (2000) Weurobiol. Dis. , vol.7 , pp. 462-470
    • Couillard-Despres, S.1    Meier, J.2    Julien, J.P.3
  • 68
    • 17744368458 scopus 로고    scopus 로고
    • Deregulation of Cdk5 in a mouse model of ALS: Toxicity alleviated by perikaryal neurofilament inclusions
    • Nguyen, M. D., Lariviere, R. C. & Julien, J. P. Deregulation of Cdk5 in a mouse model of ALS: toxicity alleviated by perikaryal neurofilament inclusions. Weuron 30, 135-147 (2001).
    • (2001) Weuron , vol.30 , pp. 135-147
    • Nguyen, M.D.1    Lariviere, R.C.2    Julien, J.P.3
  • 69
    • 0033953140 scopus 로고    scopus 로고
    • Overexpression of neurofilament subunit NF-L and NF-H extends survival of a mouse model for amyotrophic lateral sclerosis
    • Kong, J. & Xu, Z. Overexpression of neurofilament subunit NF-L and NF-H extends survival of a mouse model for amyotrophic lateral sclerosis. Weurosci. Lett. 281, 72-74 (2000).
    • (2000) Weurosci. Lett. , vol.281 , pp. 72-74
    • Kong, J.1    Xu, Z.2
  • 70
    • 0033366384 scopus 로고    scopus 로고
    • Slowing of axonal transport is a very early event in the toxicity of ALS-linked SOD1 mutants to motor neurons
    • Williamson, T L. & Cleveland, D. W. Slowing of axonal transport is a very early event in the toxicity of ALS-linked SOD1 mutants to motor neurons. Wature Weurosci. 2, 50-56 (1999).
    • (1999) Wature Weurosci , vol.2 , pp. 50-56
    • Williamson, T.L.1    Cleveland, D.W.2
  • 71
    • 0021087687 scopus 로고
    • Modulations of neurofilament axonal transport during the development of rabbit retinal ganglion cells
    • Willard, M. & Simon, C. Modulations of neurofilament axonal transport during the development of rabbit retinal ganglion cells. Cell 35, 551-559 (1983).
    • (1983) Cell , vol.35 , pp. 551-559
    • Willard, M.1    Simon, C.2
  • 72
    • 0032926368 scopus 로고    scopus 로고
    • Deletions of the heavy neurofilament subunit tail in amyotrophic lateral sclerosis
    • Al-Chalabi, A. et al. Deletions of the heavy neurofilament subunit tail in amyotrophic lateral sclerosis. Hum. Mol. Genet. 8, 157-164 (1999).
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 157-164
    • Al-Chalabi, A.1
  • 73
    • 0028001606 scopus 로고
    • Variants of the heavy neurofilament subunit are associated with the development of amyotrophic lateral sclerosis
    • Figlewicz, D. A. et al. Variants of the heavy neurofilament subunit are associated with the development of amyotrophic lateral sclerosis. Hum. Mol. Genet. 3, 1757-1761 (1994).
    • (1994) Hum. Mol. Genet. , vol.3 , pp. 1757-1761
    • Figlewicz, D.A.1
  • 74
    • 0032427646 scopus 로고    scopus 로고
    • Novel insertion in the KSP region of the neurofilament heavy gene in amyotrophic lateral sclerosis (ALS)
    • Tomkins, J. et al. Novel insertion in the KSP region of the neurofilament heavy gene in amyotrophic lateral sclerosis (ALS). Weuroreport 9, 3967-3970 (1998).
    • (1998) Weuroreport , vol.9 , pp. 3967-3970
    • Tomkins, J.1
  • 75
    • 0035136847 scopus 로고    scopus 로고
    • Further evidence that neurofilament light chain gene mutations can cause Charcot-Marie-Tooth disease type 2E
    • De Jonghe, P. et al. Further evidence that neurofilament light chain gene mutations can cause Charcot-Marie-Tooth disease type 2E. Ann. Weurol. 49, 245-249 (2001).
    • (2001) Ann. Weurol. , vol.49 , pp. 245-249
    • De Jonghe, P.1
  • 76
    • 0033911099 scopus 로고    scopus 로고
    • A new variant of Charcot-Marie-Tooth disease type 2 is probably the result of a mutation in the neurofilament-light gene
    • Mersiyanova, I. V. et al. A new variant of Charcot-Marie-Tooth disease type 2 is probably the result of a mutation in the neurofilament-light gene. Am. J. Hum. Genet. 67, 37-46 (2000).
    • (2000) Am. J. Hum. Genet. , vol.67 , pp. 37-46
    • Mersiyanova, I.V.1
  • 77
    • 0029894157 scopus 로고    scopus 로고
    • Subunit composition of neurofilaments specifies axonal diameter
    • Xu, Z. et al. Subunit composition of neurofilaments specifies axonal diameter. J. Cell Biol. 133, 1061-1069 (1996).
    • (1996) J. Cell Biol. , vol.133 , pp. 1061-1069
    • Xu, Z.1
  • 78
    • 0019784990 scopus 로고
    • Morphometric comparison of the vulnerability of peripheral motor and sensory neurons in amyotrophic lateral sclerosis
    • Kawamura, Y. et al. Morphometric comparison of the vulnerability of peripheral motor and sensory neurons in amyotrophic lateral sclerosis. J. Weuropathol. Exp. Weurol. 40, 667-675 (1981).
    • (1981) J. Weuropathol. Exp. Weurol. , vol.40 , pp. 667-675
    • Kawamura, Y.1
  • 79
    • 0028116467 scopus 로고
    • A mutant neurofilament subunit causes massive, selective motor neuron death: Implications for the pathogenesis of human motor neuron disease
    • Lee, M. K., Marszalek, J. R. & Cleveland, D. W. A mutant neurofilament subunit causes massive, selective motor neuron death: implications for the pathogenesis of human motor neuron disease. Weuron 13, 975-988 (1994).
    • (1994) Weuron , vol.13 , pp. 975-988
    • Lee, M.K.1    Marszalek, J.R.2    Cleveland, D.W.3
  • 80
    • 0030812843 scopus 로고    scopus 로고
    • Epilepsy and exacerbation of brain injury in mice lacking the glutamate transporter GLT-1
    • Tanaka, K. et al. Epilepsy and exacerbation of brain injury in mice lacking the glutamate transporter GLT-1. Science 276, 1699-1702 (1997).
    • (1997) Science , vol.276 , pp. 1699-1702
    • Tanaka, K.1
  • 81
    • 0025873777 scopus 로고
    • Excitatory amino acids in amyotrophic lateral sclerosis: An update
    • Rothstein, J. D. et al. Excitatory amino acids in amyotrophic lateral sclerosis: an update. Ann. Weurol. 30, 224-225 (1991).
    • (1991) Ann. Weurol. , vol.30 , pp. 224-225
    • Rothstein, J.D.1
  • 82
    • 0025299819 scopus 로고
    • Abnormal excitatory amino acid metabolism in amyotrophic lateral sclerosis
    • Rothstein, J. D. et al. Abnormal excitatory amino acid metabolism in amyotrophic lateral sclerosis. Ann. Weurol. 28, 18-25 (1990).
    • (1990) Ann. Weurol. , vol.28 , pp. 18-25
    • Rothstein, J.D.1
  • 83
    • 0029067210 scopus 로고
    • CSF and plasma amino acid levels in motor neuron disease — elevation of CSF glutamate in a subset of patients
    • Shaw, P J., Forrest, V, Ince, P. G., Richardson, J. P. & Wastell, H. J. CSF and plasma amino acid levels in motor neuron disease — elevation of CSF glutamate in a subset of patients. Weurodegeneration 4, 209-216 (1995).
    • (1995) Weurodegeneration , vol.4 , pp. 209-216
    • Shaw, P.J.1    Forrest, V.2    Ince, P.G.3    Richardson, J.P.4    Wastell, H.J.5
  • 84
    • 84984775131 scopus 로고    scopus 로고
    • Glutamate levels in cerebrospinal fluid in amyotrophic lateral sclerosis. A reapprasial using a new HPLC method with coulometric detection in a large cohort of patients
    • (in the press)
    • Spreux-Varoquaux, O. et al. Glutamate levels in cerebrospinal fluid in amyotrophic lateral sclerosis. A reapprasial using a new HPLC method with coulometric detection in a large cohort of patients. J. Weurol. Sci. (in the press).
    • J. Weurol. Sci
    • Spreux-Varoquaux, O.1
  • 85
    • 0029030610 scopus 로고
    • Selective loss of glial glutamate transporter GLT-1 in amyotrophic lateral sclerosis
    • Rothstein, J. D., Van Kammen, M., Levey, A. I., Martin, L. J. & Kuncl, R. W. Selective loss of glial glutamate transporter GLT-1 in amyotrophic lateral sclerosis. Ann. Weurol. 38, 73-84 (1995).
    • (1995) Ann. Weurol. , 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
  • 86
    • 0032032013 scopus 로고    scopus 로고
    • Aberrant RNA processing in a neurodegenerative disease: The cause for absent EAAT2, a glutamate transporter, in amyotrophic lateral sclerosis
    • Lin, C. L. et al. Aberrant RNA processing in a neurodegenerative disease: the cause for absent EAAT2, a glutamate transporter, in amyotrophic lateral sclerosis. Weuron 20, 589-602 (1998).
    • (1998) Weuron , vol.20 , pp. 589-602
    • Lin, C.L.1
  • 87
    • 0032716796 scopus 로고    scopus 로고
    • The RNA of the glutamate transporter EAAT2 is variably spliced in amyotrophic lateral sclerosis and normal individuals
    • Meyer, T. et al. The RNA of the glutamate transporter EAAT2 is variably spliced in amyotrophic lateral sclerosis and normal individuals. J. Weurol. Sci. 170, 45-50 (1999).
    • (1999) J. Weurol. Sci. , vol.170 , pp. 45-50
    • Meyer, T.1
  • 88
    • 0034711151 scopus 로고    scopus 로고
    • Glutamate transporter EAAT2 splice variants occur not only in ALS, but also in AD and controls
    • Honig, L. S., Chambliss, D. D., Bigio, E. H., Carroll, S. L. & Elliott, J. L. Glutamate transporter EAAT2 splice variants occur not only in ALS, but also in AD and controls. Weurology 55, 1082-1088 (2000).
    • (2000) Weurology , vol.55 , pp. 1082-1088
    • Honig, L.S.1    Chambliss, D.D.2    Bigio, E.H.3    Carroll, S.L.4    Elliott, J.L.5
  • 89
    • 0022973208 scopus 로고
    • Lathyrism: Evidence for the role of the neuroexcitatory amino acid BOAA
    • Spencer, P. S. et al. Lathyrism: evidence for the role of the neuroexcitatory amino acid BOAA. Lancet 2, 1066-1067 (1986).
    • (1986) Lancet , vol.2 , pp. 1066-1067
    • Spencer, P.S.1
  • 90
    • 0027741209 scopus 로고
    • Guam ALS-PDC: Possible causes
    • Spencer, P. S. et al. Guam ALS-PDC: possible causes. Science 262, 825-826 (1993).
    • (1993) Science , vol.262 , pp. 825-826
    • Spencer, P.S.1
  • 91
    • 0346604092 scopus 로고    scopus 로고
    • Nitration of glutamate transporters in transgenic mice with a familial amyotrophic lateral sclerosis-linked SOD1 mutation
    • Nagano, I., Wong, P. C. & Rothstein, J. D. Nitration of glutamate transporters in transgenic mice with a familial amyotrophic lateral sclerosis-linked SOD1 mutation. Ann. Weurol. 40, 542 (1996).
    • (1996) Ann. Weurol. , vol.40 , pp. 542
    • Nagano, I.1    Wong, P.C.2    Rothstein, J.D.3
  • 92
    • 0034978562 scopus 로고    scopus 로고
    • Deletion of the hypoxia-response element in the vascular endothelial growth factor promoter causes motor neuron degeneration
    • Oosthuyse, B. et al. Deletion of the hypoxia-response element in the vascular endothelial growth factor promoter causes motor neuron degeneration. Wature Genet. 28, 131-138 (2001).
    • (2001) Wature Genet , vol.28 , pp. 131-138
    • Oosthuyse, B.1
  • 93
    • 0032816137 scopus 로고    scopus 로고
    • Autosomal dominant juvenile amyotrophic lateral sclerosis
    • Rabin, B. A. et al. Autosomal dominant juvenile amyotrophic lateral sclerosis. Brain 122, 1539-1550 (1999).
    • (1999) Brain , vol.122 , pp. 1539-1550
    • Rabin, B.A.1
  • 94
    • 0031959591 scopus 로고    scopus 로고
    • Linkage of the gene for an autosomal dominant form of juvenile amyotrophic lateral sclerosis to chromosome 9q34
    • Chance, P. F. et al. Linkage of the gene for an autosomal dominant form of juvenile amyotrophic lateral sclerosis to chromosome 9q34. Am. J. Hum. Genet. 62, 633-640 (1998).
    • (1998) Am. J. Hum. Genet. , vol.62 , pp. 633-640
    • Chance, P.F.1
  • 95
    • 0032414948 scopus 로고    scopus 로고
    • Linkage of a commoner form of recessive amyotrophic lateral sclerosis to chromosome 15q15-q22 markers
    • Hentati, A. et al. Linkage of a commoner form of recessive amyotrophic lateral sclerosis to chromosome 15q15-q22 markers. Weurogenetics 2, 55-60 (1998).
    • (1998) Weurogenetics 2 , pp. 55-60
    • Hentati, A.1
  • 96
    • 0034785483 scopus 로고    scopus 로고
    • A gene encoding a putative GTPase regulator is mutated in familial amyotrophic lateral sclerosis 2
    • Hadano, S. et al. A gene encoding a putative GTPase regulator is mutated in familial amyotrophic lateral sclerosis 2. Wature Genet. 29, 166-173 (2001).
    • (2001) Wature Genet , vol.29 , pp. 166-173
    • Hadano, S.1
  • 97
    • 0034785509 scopus 로고    scopus 로고
    • The gene encoding alsin, a protein with three guanine-nucleotide exchange factor domains, is mutated in a form of recessive amyotrophic lateral sclerosis
    • Yang, Y. et al. The gene encoding alsin, a protein with three guanine-nucleotide exchange factor domains, is mutated in a form of recessive amyotrophic lateral sclerosis. Wature Genet. 29, 160-165 (2001).
    • (2001) Wature Genet , vol.29 , pp. 160-165
    • Yang, Y.1
  • 98
    • 0027210116 scopus 로고
    • Parvalbumin and calbindin D-28k in the human motor system and in motor neuron disease
    • Ince, P. et al. Parvalbumin and calbindin D-28k in the human motor system and in motor neuron disease. Weuropathol. Appl. Weurobiol. 19, 291-299 (1993).
    • (1993) Weuropathol. Appl. Weurobiol. , vol.19 , pp. 291-299
    • Ince, P.1
  • 99
    • 7844227669 scopus 로고    scopus 로고
    • Recessive amyotrophic lateral sclerosis families with the D90A SOD1 mutation share a common founder: Evidence for a linked protective factor
    • Al-Chalabi, A. et al. Recessive amyotrophic lateral sclerosis families with the D90A SOD1 mutation share a common founder: evidence for a linked protective factor. Hum. Mol. Genet. 7, 2045-2050 (1998).
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 2045-2050
    • Al-Chalabi, A.1
  • 100
    • 0034537966 scopus 로고    scopus 로고
    • Genetic mapping of a mouse modifier gene that can prevent ALS onset
    • Kunst, C. B., Messer, L., Gordon, J., Haines, J. & Patterson, D. Genetic mapping of a mouse modifier gene that can prevent ALS onset. Genomics 70, 181-189 (2000).
    • (2000) Genomics , vol.70 , pp. 181-189
    • Kunst, C.B.1    Messer, L.2    Gordon, J.3    Haines, J.4    Patterson, D.5
  • 101
    • 0001389279 scopus 로고    scopus 로고
    • A controlled trial of recombinant methionyl human BDNF in ALS: The BDNF Study Group (Phase III)
    • Kasarkis, E. J. et al. A controlled trial of recombinant methionyl human BDNF in ALS: The BDNF Study Group (Phase III). Weurology 52, 1427-1433 (1999).
    • (1999) Weurology , vol.52 , pp. 1427-1433
    • Kasarkis, E.J.1
  • 102
    • 0031562362 scopus 로고    scopus 로고
    • Expression of glial glutamate transporters GLT-1 and GLAST is unchanged in the hippocampus in fully kindled rats
    • Akbar, M. T. et al. Expression of glial glutamate transporters GLT-1 and GLAST is unchanged in the hippocampus in fully kindled rats. Weuroscience 78, 351-359 (1997).
    • (1997) Weuroscience , vol.78 , pp. 351-359
    • Akbar, M.T.1
  • 103
    • 0031722582 scopus 로고    scopus 로고
    • A placebo-controlled trial of insulin-like growth factor-I in amyotrophic lateral sclerosis. European ALS/IGF-I Study Group
    • Borasio, G. D. et al. A placebo-controlled trial of insulin-like growth factor-I in amyotrophic lateral sclerosis. European ALS/IGF-I Study Group. Weurology 51, 583-586 (1998).
    • (1998) Weurology , vol.51 , pp. 583-586
    • Borasio, G.D.1
  • 104
    • 6844266272 scopus 로고    scopus 로고
    • Effect of recombinant human insulin-like growth factor-I on progression of ALS. A placebo-controlled study. The North America ALS/IGF-I Study Group
    • Lai, E. C. et al. Effect of recombinant human insulin-like growth factor-I on progression of ALS. A placebo-controlled study. The North America ALS/IGF-I Study Group. Weurology 49, 1621-1630 (1997).
    • (1997) Weurology , vol.49 , pp. 1621-1630
    • Lai, E.C.1
  • 105
    • 0028097839 scopus 로고
    • A controlled trial of riluzole in amyotrophic lateral sclerosis
    • Bensimon, G., Lacomblez, L., Meininger, V. & The ALS/Riluzole Study Group. A controlled trial of riluzole in amyotrophic lateral sclerosis. W. Engl. J. Med. 330, 585-591 (1994).
    • (1994) W. Engl. J. Med. , vol.330 , pp. 585-591
    • Bensimon, G.1    Lacomblez, L.2    Meininger, V.3
  • 106
    • 0029977337 scopus 로고    scopus 로고
    • Dose-ranging study of riluzole in amyotrophic lateral sclerosis. Amyotrophic Lateral Sclerosis/Riluzole Study Group II
    • Lacomblez, L., Bensimon, G., Leigh, P. N., Guillet, P. & Meininger, V. Dose-ranging study of riluzole in amyotrophic lateral sclerosis. Amyotrophic Lateral Sclerosis/Riluzole Study Group II. Lancet 347, 1425-1431 (1996).
    • (1996) Lancet , vol.347 , pp. 1425-1431
    • Lacomblez, L.1    Bensimon, G.2    Leigh, P.N.3    Guillet, P.4    Meininger, V.5
  • 107
    • 0033051815 scopus 로고    scopus 로고
    • Neuroprotective effects of creatine in a transgenic animal model of amyotrophic lateral sclerosis
    • Klivenyi, P. et al. Neuroprotective effects of creatine in a transgenic animal model of amyotrophic lateral sclerosis. Mature Med. 5, 347-350 (1999).
    • (1999) Mature Med , vol.5 , pp. 347-350
    • Klivenyi, P.1
  • 108
    • 0035051503 scopus 로고    scopus 로고
    • Increases in cortical glutamate concentrations in transgenic amyotrophic lateral sclerosis mice are attenuated by creatine supplementation
    • Andreassen, O. A. et al. Increases in cortical glutamate concentrations in transgenic amyotrophic lateral sclerosis mice are attenuated by creatine supplementation. J. Weurochem. 77, 383-390 (2001).
    • (2001) J. Weurochem. , vol.77 , pp. 383-390
    • Andreassen, O.A.1
  • 109
    • 0035918258 scopus 로고    scopus 로고
    • Mutant Cu/Zn-superoxide dismutase proteins have altered solubility and interact with heat shock/stress proteins in models of amyotrophic lateral sclerosis
    • Shinder, G. A., Lacourse, M. C., Minotti, S. & Durham, H. D. Mutant Cu/Zn-superoxide dismutase proteins have altered solubility and interact with heat shock/stress proteins in models of amyotrophic lateral sclerosis. J. Biol. Chem. 276, 12791-12796 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 12791-12796
    • Shinder, G.A.1    Lacourse, M.C.2    Minotti, S.3    Durham, H.D.4
  • 110
    • 0034605478 scopus 로고    scopus 로고
    • Linkage of familial amyotrophic lateral sclerosis with frontotemporal dementia to chromosome 9q21 -q22
    • Hosler, B. A. et al. Linkage of familial amyotrophic lateral sclerosis with frontotemporal dementia to chromosome 9q21 -q22. J. Am. Med. Assoc. 284, 1664-1669 (2000).
    • (2000) J. Am. Med. Assoc. , vol.284 , pp. 1664-1669
    • Hosler, B.A.1
  • 111
    • 0007731688 scopus 로고    scopus 로고
    • X-linked dominant locus for late-onset familial amyotrophic lateral sclerosis
    • Siddique, T. et al. X-linked dominant locus for late-onset familial amyotrophic lateral sclerosis. Am. J. Hum. Genet. 63, A308 (1998).
    • (1998) Am. J. Hum. Genet. , vol.63 , pp. A308
    • Siddique, T.1
  • 112
    • 0035947221 scopus 로고    scopus 로고
    • Synthetic superoxide dismutase/catalase mimetics reduce oxidative stress and prolong survival in a mouse amyotrophic lateral sclerosis model
    • Jung, C. et al. Synthetic superoxide dismutase/catalase mimetics reduce oxidative stress and prolong survival in a mouse amyotrophic lateral sclerosis model. Weurosci. Lett. 304, 157-160 (2001).
    • (2001) Weurosci. Lett. , vol.304 , pp. 157-160
    • Jung, C.1
  • 113
    • 0032827346 scopus 로고    scopus 로고
    • Therapeutic benefits of putrescine-modified catalase in a transgenic mouse model of familial amyotrophic lateral sclerosis
    • Reinholz, M. M., Merkle, C. M. & Poduslo, J. F. Therapeutic benefits of putrescine-modified catalase in a transgenic mouse model of familial amyotrophic lateral sclerosis. Exp. Weurol. 159, 204-216 (1999).
    • (1999) Exp. Weurol. , vol.159 , pp. 204-216
    • Reinholz, M.M.1    Merkle, C.M.2    Poduslo, J.F.3
  • 114
    • 0035068202 scopus 로고    scopus 로고
    • Effects of an inhibitor of poly(ADP- ribose) polymerase, desmethylselegiline, trientine, and lipoic acid in transgenic ALS mice
    • Andreassen, O. A. et al. Effects of an inhibitor of poly(ADP- ribose) polymerase, desmethylselegiline, trientine, and lipoic acid in transgenic ALS mice. Exp. Weurol. 168, 419-424 (2001).
    • (2001) Exp. Weurol. , vol.168 , pp. 419-424
    • Andreassen, O.A.1
  • 115
    • 0034327293 scopus 로고    scopus 로고
    • Beneficial effect of ginseng root in SOD-1 (G93A) transgenic mice
    • Jiang, F., DeSilva, S. & Turnbull, J. Beneficial effect of ginseng root in SOD-1 (G93A) transgenic mice. J. Weurol. Sci. 180, 52-54 (2000).
    • (2000) J. Weurol. Sci. , vol.180 , pp. 52-54
    • Jiang, F.1    Desilva, S.2    Turnbull, J.3
  • 116
    • 0034601439 scopus 로고    scopus 로고
    • I. W-acetyl-L-cysteine improves survival and preserves motor performance in an animal model of familial amyotrophic lateral sclerosis
    • Andreassen, O. A., Dedeoglu, A., Klivenyi, P, Beal, M. F & Bush, A. I. W-acetyl-L-cysteine improves survival and preserves motor performance in an animal model of familial amyotrophic lateral sclerosis. Weuroreport 11, 2491-2493 (2000).
    • (2000) Weuroreport , vol.11 , pp. 2491-2493
    • Andreassen, O.A.1    Dedeoglu, A.2    Klivenyi, P.3    Beal, M.F.4    Bush, A.5
  • 117
    • 0035155759 scopus 로고    scopus 로고
    • Mice with a partial deficiency of manganese superoxide dismutase show increased vulnerability to the mitochondrial toxins malonate, 3-nitropropionic acid, and MPTP
    • Andreassen, O. A. et al. Mice with a partial deficiency of manganese superoxide dismutase show increased vulnerability to the mitochondrial toxins malonate, 3-nitropropionic acid, and MPTP. Exp. Weurol. 167, 189-195 (2001).
    • (2001) Exp. Weurol. , vol.167 , pp. 189-195
    • Andreassen, O.A.1
  • 118
    • 0034614353 scopus 로고    scopus 로고
    • A specific inhibitor of janus kinase-3 increases survival in a transgenic mouse model of amyotrophic lateral sclerosis
    • Trieu, V. N., Liu, R., Liu, X. P. & Uckun, F. M. A specific inhibitor of janus kinase-3 increases survival in a transgenic mouse model of amyotrophic lateral sclerosis. Biochem. Biophys. Res. Commun. 267, 22-25 (2000).
    • (2000) Biochem. Biophys. Res. Commun. , vol.267 , pp. 22-25
    • Trieu, V.N.1    Liu, R.2    Liu, X.P.3    Uckun, F.M.4
  • 119
    • 0033064535 scopus 로고    scopus 로고
    • Administration of nitric oxide synthase inhibitors does not alter disease course of amyotrophic lateral sclerosis SOD1 mutant transgenic mice
    • Upton-Rice, M. N., Cudkowicz, M. E., Mathew, R. K., Reif, D. & Brown, R. H. Jr. Administration of nitric oxide synthase inhibitors does not alter disease course of amyotrophic lateral sclerosis SOD1 mutant transgenic mice. Ann. Weurol. 45, 413-414 (1999).
    • (1999) Ann. Weurol. , vol.45 , pp. 413-414
    • Upton-Rice, M.N.1    Cudkowicz, M.E.2    Mathew, R.K.3    Reif, D.4    Brown, R.H.5
  • 120
    • 0033597218 scopus 로고    scopus 로고
    • Benefit of a combined treatment with trientine and ascorbate in familial amyotrophic lateral sclerosis model mice
    • Nagano, S., Ogawa, Y, Yanagihara, T. & Sakoda, S. Benefit of a combined treatment with trientine and ascorbate in familial amyotrophic lateral sclerosis model mice. Weurosci. Lett. 265, 159-162 (1999).
    • (1999) Weurosci. Lett. , vol.265 , pp. 159-162
    • Nagano, S.1    Ogawa, Y.2    Yanagihara, T.3    Sakoda, S.4
  • 121
    • 0030050727 scopus 로고    scopus 로고
    • Benefit of vitamin E, riluzole, and gabapentin in a transgenic model of familial amyotrophic lateral sclerosis
    • Gurney, M. E. et al. Benefit of vitamin E, riluzole, and gabapentin in a transgenic model of familial amyotrophic lateral sclerosis. Ann. Weurol. 39, 147-157 (1996).
    • (1996) Ann. Weurol. , vol.39 , pp. 147-157
    • Gurney, M.E.1
  • 122
    • 0001897915 scopus 로고    scopus 로고
    • Carboxyfullerenes as neuroprotective agents
    • Dugan, L. L. et al. Carboxyfullerenes as neuroprotective agents. Proc. Watl Acad. Sci. USA 94, 9434-9439 (1997).
    • (1997) Proc. Watl Acad. Sci. USA , vol.94 , pp. 9434-9439
    • Dugan, L.L.1
  • 123
    • 0035007860 scopus 로고    scopus 로고
    • Double-blind, placebo-controlled randomized clinical trial of a-tocopherol (Vitamin E) in the treatment of amyotrophic lateral sclerosis. ALS Riluzole-Tocopherol Study Group
    • Desnuelle, C., Dib, M., Garrel, C. & Favier, A. A double-blind, placebo-controlled randomized clinical trial of a-tocopherol (vitamin E) in the treatment of amyotrophic lateral sclerosis. ALS Riluzole-Tocopherol Study Group. Amyotroph. Lateral Scler. Other Motor Weuron Disord. 2, 9-18 (2001).
    • (2001) Amyotroph. Lateral Scler. Other Motor Weuron Disord. , vol.2 , pp. 9-18
    • Desnuelle, C.1    Dib, M.2    Garrel, C.3    Favier, A.A.4
  • 124
    • 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
    • Hottinger, A. F., Fine, E. G., Gurney M. E., Zurn, A. D. & Aebischer, P. The copper chelator D-penicillamine delays onset of disease and extends survival in a transgenic mouse model of familial amyotrophic lateral sclerosis. Eur. J. Weurosci. 9, 1548-1551 (1997).
    • (1997) Eur. J. Weurosci. , vol.9 , pp. 1548-1551
    • Hottinger, A.F.1    Fine, E.G.2    Gurney, M.E.3    Zurn, A.D.4    Aebischer, P.5
  • 125
    • 0035896440 scopus 로고    scopus 로고
    • Intrathecal cyclosporin prolongs survival of late-stage ALS mice
    • Keep, M., Elmer, E., Fong, K S. & Csiszar, K. Intrathecal cyclosporin prolongs survival of late-stage ALS mice. Brain Res. 894, 327-331 (2001).
    • (2001) Brain Res , vol.894 , pp. 327-331
    • Keep, M.1    Elmer, E.2    Fong, K.S.3    Csiszar, K.4
  • 126
    • 0344609220 scopus 로고    scopus 로고
    • Beneficial effects of lysine acetylsalicylate, a soluble salt of aspirin, on motor performance in a transgenic model of amyotrophic lateral sclerosis
    • Barneoud, P & Curet, O. Beneficial effects of lysine acetylsalicylate, a soluble salt of aspirin, on motor performance in a transgenic model of amyotrophic lateral sclerosis. Exp. Weurol. 155, 243-251 (1999).
    • (1999) Exp. Weurol. , vol.155 , pp. 243-251
    • Barneoud, P.1    Curet, O.2
  • 127
    • 84984755124 scopus 로고    scopus 로고
    • COX-2 inhibition prolongs survival in a transgenic mouse model of ALS
    • (in the press)
    • Frank, K. M., Coccia, C., Drachman, D. B. & Rothstein, J. D. COX-2 inhibition prolongs survival in a transgenic mouse model of ALS. Soc. Weurosci.Abstr. 27 (in the press).
    • Soc. Weurosci.Abstr , vol.27
    • Frank, K.M.1    Coccia, C.2    Drachman, D.B.3    Rothstein, J.D.4
  • 128
    • 0027997173 scopus 로고
    • Trial of immunosuppression in amyotrophic lateral sclerosis using total lymphoid irradiation
    • Haverkamp, L. J., Smith, R. G. & Appel, S. H. Trial of immunosuppression in amyotrophic lateral sclerosis using total lymphoid irradiation. Ann. Weurol. 36, 253-254 (1994).
    • (1994) Ann. Weurol. , vol.36 , pp. 253-254
    • Haverkamp, L.J.1    Smith, R.G.2    Appel, S.H.3
  • 129
    • 0023949295 scopus 로고
    • A double-blind study of the effectiveness of cyclosporine in amyotrophic lateral sclerosis
    • Appel, S. H. et al. A double-blind study of the effectiveness of cyclosporine in amyotrophic lateral sclerosis. Arch. Weurol. 45, 381-386 (1988).
    • (1988) Arch. Weurol. , vol.45 , pp. 381-386
    • Appel, S.H.1
  • 130
    • 0022521502 scopus 로고
    • Intrathecal administration of natural human interferon a in amyotrophic lateral sclerosis
    • Mora, J. S. et al. Intrathecal administration of natural human interferon a in amyotrophic lateral sclerosis. Weurology 36, 1137-1140 (1986).
    • (1986) Weurology , vol.36 , pp. 1137-1140
    • Mora, J.S.1
  • 131
    • 0022570201 scopus 로고
    • Therapeutic plasmapheresis and plasma exchange
    • Patten, E. Therapeutic plasmapheresis and plasma exchange. Crit. Rev. Clin. Lab. Sci. 23, 147-175 (1986).
    • (1986) Crit. Rev. Clin. Lab. Sci. , vol.23 , pp. 147-175
    • Patten, E.1
  • 132
    • 0021241929 scopus 로고
    • Ganglioside therapy for amyotrophic lateral sclerosis: A double-blind controlled trial
    • Harrington, H., Hallett, M. & Tyler, H. R. Ganglioside therapy for amyotrophic lateral sclerosis: a double-blind controlled trial. Weurology 34, 1083-1085 (1984).
    • (1984) Weurology , vol.34 , pp. 1083-1085
    • Harrington, H.1    Hallett, M.2    Tyler, H.R.3
  • 133
    • 0021253595 scopus 로고
    • A double-blind controlled trial of bovine brain gangliosides in amyotrophic lateral sclerosis
    • Bradley, W. G. et al. A double-blind controlled trial of bovine brain gangliosides in amyotrophic lateral sclerosis. Weurology 34, 1079-1082 (1984).
    • (1984) Weurology , vol.34 , pp. 1079-1082
    • Bradley, W.G.1
  • 134
    • 0021306178 scopus 로고
    • Trials of ganglioside therapy for amyotrophic lateral sclerosis and diabetic neuropathy
    • Hallett, M., Harrington, H., Tyler, H. R., Flood, T. & Slater, N. Trials of ganglioside therapy for amyotrophic lateral sclerosis and diabetic neuropathy. Adv. Exp. Med. Biol. 174, 575-579 (1984).
    • (1984) Adv. Exp. Med. Biol. , vol.174 , pp. 575-579
    • Hallett, M.1    Harrington, H.2    Tyler, H.R.3    Flood, T.4    Slater, N.5
  • 135
    • 0021298875 scopus 로고
    • Double-blind controlled trial of purified brain gangliosides in amyotrophic lateral sclerosis and experience with peripheral neuropathies
    • Bradley, W. G. Double-blind controlled trial of purified brain gangliosides in amyotrophic lateral sclerosis and experience with peripheral neuropathies. Adv. Exp. Med. Biol. 174, 565-573 (1984).
    • (1984) Adv. Exp. Med. Biol. , vol.174 , pp. 565-573
    • Bradley, W.G.1
  • 137
    • 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. 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).
    • (2000) Brain Res , vol.879 , pp. 183-187
    • Prudlo, J.1
  • 138
    • 0030006282 scopus 로고    scopus 로고
    • A clinical trial of verapamil in amyotrophic lateral sclerosis
    • Miller, R. G. et al. A clinical trial of verapamil in amyotrophic lateral sclerosis. Muscle Wen/e 19, 511-515 (1996).
    • (1996) Muscle Wen/E , vol.19 , pp. 511-515
    • Miller, R.G.1
  • 139
    • 0029923440 scopus 로고    scopus 로고
    • Controlled trial of nimodipine in amyotrophic lateral sclerosis
    • Miller, R. G. et al. Controlled trial of nimodipine in amyotrophic lateral sclerosis. Weuromuscul. Disord. 6, 101-104 (1996).
    • (1996) Weuromuscul. Disord. , vol.6 , pp. 101-104
    • Miller, R.G.1
  • 140
    • 0347233783 scopus 로고    scopus 로고
    • Naaladase inhibition increases survival and delays clinical symptoms in SOD transgenic model of ALS
    • Slusher, B. S. et al. Naaladase inhibition increases survival and delays clinical symptoms in SOD transgenic model of ALS. Soc. Weurosci. Abstr. 26, 43.10 (2000).
    • (2000) Soc. Weurosci. Abstr. , vol.26 , Issue.43 , pp. 10
    • Slusher, B.S.1
  • 141
    • 84884526436 scopus 로고    scopus 로고
    • EAAT2 overexpression plays a neuroprotective role in the SOD1 G93A model of amyotrophic lateral sclerosis
    • (in the press)
    • Sutherland, M. L., Martinowich, K. & Rothstein, J. D. EAAT2 overexpression plays a neuroprotective role in the SOD1 G93A model of amyotrophic lateral sclerosis. Soc. Weurosci. Abstr. 27, (in the press).
    • Soc. Weurosci. Abstr , vol.27
    • Sutherland, M.L.1    Martinowich, K.2    Rothstein, J.D.3
  • 142
    • 0023913736 scopus 로고
    • Pilot trial of branched-chain amino acids in amyotrophic lateral sclerosis
    • Plaitakis, A., Smith, J., Mandeli, J. & Yahr, M. D. Pilot trial of branched-chain amino acids in amyotrophic lateral sclerosis. Lancet 1, 1015-1018 (1988).
    • (1988) Lancet , vol.1 , pp. 1015-1018
    • Plaitakis, A.1    Smith, J.2    Mandeli, J.3    Yahr, M.D.4
  • 143
    • 0033587480 scopus 로고    scopus 로고
    • Intramuscular grafts of myoblasts genetically modified to secrete glial cell line-derived neurotrophic factor prevent motoneuron loss and disease progression in a mouse model of familial amyotrophic lateral sclerosis
    • Mohajeri, M. H., Figlewicz, D. A. & Bohn, M. C. Intramuscular grafts of myoblasts genetically modified to secrete glial cell line-derived neurotrophic factor prevent motoneuron loss and disease progression in a mouse model of familial amyotrophic lateral sclerosis. Hum. Gene Tier. 10, 1853-1866 (1999).
    • (1999) Hum. Gene Tier. , vol.10 , pp. 1853-1866
    • Mohajeri, M.H.1    Figlewicz, D.A.2    Bohn, M.C.3
  • 144
    • 84984762646 scopus 로고    scopus 로고
    • Intracisternal injection of bone morphogenic protein-7 at time of disease onset did not alter disease course in a transgenic mouse model of amyotrophic lateral sclerosis
    • Dreibelbis, J. E., Cudkowicz, M. E., Pastuszak, K. A., Smith, E. R. & Brown, R. H. Jr. Intracisternal injection of bone morphogenic protein-7 at time of disease onset did not alter disease course in a transgenic mouse model of amyotrophic lateral sclerosis. Soc. Weurosci.Abstr. 26, 865-4 (2000).
    • (2000) Soc. Weurosci.Abstr. , vol.26 , pp. 865-874
    • Dreibelbis, J.E.1    Cudkowicz, M.E.2    Pastuszak, K.A.3    Smith, E.R.4    Brown, R.H.5
  • 145
    • 0035444173 scopus 로고    scopus 로고
    • Protective effects of cardiotrophin-1 adenoviral gene transfer on neuromuscular degeneration in transgenic ALS mice
    • Bordet, T. et al. Protective effects of cardiotrophin-1 adenoviral gene transfer on neuromuscular degeneration in transgenic ALS mice. Hum. Mol. Genet. 10, 1925-1933 (2001).
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1925-1933
    • Bordet, T.1
  • 146
    • 0345972723 scopus 로고    scopus 로고
    • Hepatocyte growth factor gene transfer improves life span, motor function and motorneuronal death in an ALS transgenic mouse model
    • (in the press)
    • Sun, W. & Funakoshi, H. N. T. Hepatocyte growth factor gene transfer improves life span, motor function and motorneuronal death in an ALS transgenic mouse model. Soc. Weurosci. Abstr. 27, (in the press).
    • Soc. Weurosci. Abstr , vol.27
    • Sun, W.1    Funakoshi, H.2
  • 147
    • 0026729250 scopus 로고
    • Intrathecal thyrotropin-releasing hormone does not alter the progressive course of ALS: Experience with an intrathecal drug delivery system
    • Munsat, T. L. et al. Intrathecal thyrotropin-releasing hormone does not alter the progressive course of ALS: experience with an intrathecal drug delivery system. Weurology 42, 1049-1053 (1992).
    • (1992) Weurology , vol.42 , pp. 1049-1053
    • Munsat, T.L.1
  • 148
    • 0023142099 scopus 로고
    • Intravenous thyrotropin- releasing hormone in patients with amyotrophic lateral sclerosis. Dose-response and randomized concurrent placebo-controlled pilot studies
    • Brooks, B. R., Sufit, R. L., Montgomery, G. K., Beaulieu, D. A. & Erickson, L. M. Intravenous thyrotropin- releasing hormone in patients with amyotrophic lateral sclerosis. Dose-response and randomized concurrent placebo-controlled pilot studies. Weurol. Clin. 5, 143-158 (1987).
    • (1987) Weurol. Clin. , vol.5 , pp. 143-158
    • Brooks, B.R.1    Sufit, R.L.2    Montgomery, G.K.3    Beaulieu, D.A.4    Erickson, L.M.5
  • 149
    • 0022636979 scopus 로고
    • A double-blind, placebo-controlled trial of TRH in amyotrophic lateral sclerosis
    • Caroscio, J. T. et al. A double-blind, placebo-controlled trial of TRH in amyotrophic lateral sclerosis. Weurology 36, 141-145 (1986).
    • (1986) Weurology , vol.36 , pp. 141-145
    • Caroscio, J.T.1
  • 150
    • 0033583834 scopus 로고    scopus 로고
    • Genistein is neuroprotective in murine models of familial amyotrophic lateral sclerosis and stroke
    • Trieu, V N. & Uckun, F. M. Genistein is neuroprotective in murine models of familial amyotrophic lateral sclerosis and stroke. Biochem. Biophys. Res. Commun. 258, 685-688 (1999).
    • (1999) Biochem. Biophys. Res. Commun. , vol.258 , pp. 685-688
    • Trieu, V.N.1    Uckun, F.M.2
  • 151
    • 0022518578 scopus 로고
    • Trial of octacosanol in amyotrophic lateral sclerosis
    • Norris, F. H., Denys, E. H. & Fallat, R. J. Trial of octacosanol in amyotrophic lateral sclerosis. Weurology 36, 1263-1264 (1986).
    • (1986) Weurology , vol.36 , pp. 1263-1264
    • Norris, F.H.1    Denys, E.H.2    Fallat, R.J.3
  • 153
    • 0018321151 scopus 로고
    • Transfer factor is ineffective in amyotrophic lateral sclerosis
    • Olarte, M. R., Gersten, J. C., Zabriskie, J. & Rowland, L. P. Transfer factor is ineffective in amyotrophic lateral sclerosis. Ann. Weurol. 5, 385-388 (1979).
    • (1979) Ann. Weurol. , vol.5 , pp. 385-388
    • Olarte, M.R.1    Gersten, J.C.2    Zabriskie, J.3    Rowland, L.P.4
  • 154
    • 0018075269 scopus 로고
    • Therapeutic trial of tilorone in ALS: Lack of benefit in a double-blind, placebo-controlled study
    • Olson, W. H., Simons, J. A. & Halaas, G. W. Therapeutic trial of tilorone in ALS: lack of benefit in a double-blind, placebo-controlled study. Weurology 28, 1293-1295 (1978).
    • (1978) Weurology , vol.28 , pp. 1293-1295
    • Olson, W.H.1    Simons, J.A.2    Halaas, G.W.3
  • 155
    • 0015128099 scopus 로고
    • The use of isoprinosine in patients with amyotrophic lateral sclerosis
    • Fareed, G. C. & Tyler, H. R. The use of isoprinosine in patients with amyotrophic lateral sclerosis. Weurology 21, 937-940 (1971).
    • (1971) Weurology , vol.21 , pp. 937-940
    • Fareed, G.C.1    Tyler, H.R.2
  • 156
    • 0034717016 scopus 로고    scopus 로고
    • Human umbilical cord blood effect on sod mice (Amyotrophic lateral sclerosis)
    • Ende, N., Weinstein, F, Chen, R. & Ende, M. Human umbilical cord blood effect on sod mice (amyotrophic lateral sclerosis). Life Sci. 67, 53-59 (2000).
    • (2000) Life Sci , vol.67 , pp. 53-59
    • Ende, N.1    Weinstein, F.2    Chen, R.3    Ende, M.4
  • 157
    • 0141613347 scopus 로고    scopus 로고
    • Transplanted neural stem cells are capable of engraftment and diffrentiation in transgenic mutant SOD1 mice
    • Maragakis, N. J. et al. Transplanted neural stem cells are capable of engraftment and diffrentiation in transgenic mutant SOD1 mice. Soc. Weurosci.Abstr. 26, 668.3 (2000).
    • (2000) Soc. Weurosci.Abstr. , vol.26 , Issue.668 , pp. 3
    • Maragakis, N.J.1


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