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Volumn 234, Issue 10, 2009, Pages 1140-1154

Immature copper-zinc superoxide dismutase and familial amyotrophic lateral sclerosis

Author keywords

Amyloid; Amyotrophic lateral sclerosis; Motor neuron disease; Protein aggregation; Protein misfolding; Protofibrils; SOD1; Superoxide dismutase

Indexed keywords

CHAPERONE; COPPER; COPPER ZINC SUPEROXIDE DISMUTASE; POLYPEPTIDE; PROTEIN; AMYLOID; DISULFIDE; SUPEROXIDE DISMUTASE;

EID: 70349759885     PISSN: 15353702     EISSN: 15353699     Source Type: Journal    
DOI: 10.3181/0903-MR-104     Document Type: Short Survey
Times cited : (76)

References (138)
  • 1
    • 0000280462 scopus 로고
    • Deux cas d'atrophie musculaire progressive avec lesions de la substance grise et de faisceaux anterolateraux de la moelle epiniere
    • Charcot JM, A J. Deux cas d'atrophie musculaire progressive avec lesions de la substance grise et de faisceaux anterolateraux de la moelle epiniere. Arch Physiol Norm Pathol 1:354-367, 1869.
    • (1869) Arch Physiol Norm Pathol , vol.1 , pp. 354-367
    • Charcot, J.M.1    Deux, A.J.2
  • 2
    • 0022443737 scopus 로고
    • Familial adult motor neuron disease: Amyotrophic lateral sclerosis
    • Mulder DW, Kurland LT, Offord KP, Beard CM. Familial adult motor neuron disease: amyotrophic lateral sclerosis. Neurology 36:511-517, 1986. (Pubitemid 16070005)
    • (1986) Neurology , vol.36 , Issue.4 , pp. 511-517
    • Mulder, D.W.1    Kurland, L.T.2    Offord, K.P.3    Beard, M.4
  • 3
    • 3943102116 scopus 로고    scopus 로고
    • Unraveling the mechanisms involved in motor neuron degeneration in ALS
    • Bruijn LI, Miller TM, Cleveland DW. Unraveling the mechanisms involved in motor neuron degeneration in ALS. Annu Rev Neurosci 27:723-749, 2004.
    • (2004) Annu Rev Neurosci , vol.27 , pp. 723-749
    • Bruijn, L.I.1    Miller, T.M.2    Cleveland, D.W.3
  • 4
    • 22244479388 scopus 로고    scopus 로고
    • Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis
    • DOI 10.1146/annurev.biochem.72.121801.161647
    • Valentine JS, Doucette PA, Zittin Potter S. Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis. Annu Rev Biochem 74:563-593, 2005. (Pubitemid 40995518)
    • (2005) Annual Review of Biochemistry , vol.74 , pp. 563-593
    • Valentine, J.S.1    Doucette, P.A.2    Potter, S.Z.3
  • 7
    • 33645225597 scopus 로고    scopus 로고
    • Pathogenic superoxide dismutase structure, folding, aggregation and turnover
    • Hart PJ. Pathogenic superoxide dismutase structure, folding, aggregation and turnover. Curr Opin Chem Biol 10:131-138, 2006.
    • (2006) Curr Opin Chem Biol , vol.10 , pp. 131-138
    • Hart, P.J.1
  • 8
    • 70349940117 scopus 로고    scopus 로고
    • Copper-zinc superoxide dismutase, its copper chaperone, and familial amyotrophic lateral sclerosis
    • Dobson CM, Kelly JW, Ramirez-Alvarado M, Eds. Hoboken, NJ: John Wiley & Sons, Inc.
    • Winkler DD, Prudencio M, Karch C, Borchelt DR, Hart PJ. Copper-zinc superoxide dismutase, its copper chaperone, and familial amyotrophic lateral sclerosis. In: Dobson CM, Kelly JW, Ramirez-Alvarado M, Eds. Protein Misfolding Diseases: Current and Emerging Prinicples. Hoboken, NJ: John Wiley & Sons, Inc., 2009.
    • (2009) Protein Misfolding Diseases: Current and Emerging Prinicples
    • Winkler, D.D.1    Prudencio, M.2    Karch, C.3    Borchelt, D.R.4    Hart, P.J.5
  • 9
    • 0024308039 scopus 로고
    • Superoxide dismutases. An adaptation to a paramagnetic gas
    • Fridovich I. Superoxide dismutases. An adaptation to a paramagnetic gas. J Biol Chem 264:7761-7764, 1989. (Pubitemid 19137245)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.14 , pp. 7761-7764
    • Fridovich, I.1
  • 10
    • 0035851122 scopus 로고    scopus 로고
    • A fraction of yeast Cu,Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria. a physiological role for SOD1 in guarding against mitochondrial oxidative damage
    • Sturtz LA, Diekert K, Jensen LT, Lill R, Culotta VC. A fraction of yeast Cu,Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria. A physiological role for SOD1 in guarding against mitochondrial oxidative damage. J Biol Chem 276:38084-38089, 2001. (Pubitemid 37384061)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.41 , pp. 38084-38089
    • Sturtz, L.A.1    Diekert, K.2    Jensen, L.T.3    Lill, R.4    Culotta, V.C.5
  • 11
    • 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
    • Pardo CA, Xu Z, Borchelt DR, Price DL, Sisodia SS, Cleveland DW. 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 U S A 92:954-958, 1995.
    • (1995) Proc Natl Acad Sci U S A , 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
  • 12
    • 0021745377 scopus 로고
    • Extracellular superoxide dismutase in human tissues and human cell lines
    • Marklund SL. Extracellular superoxide dismutase in human tissues and human cell lines. J Clin Invest 74:1398-1403, 1984. (Pubitemid 15206836)
    • (1984) Journal of Clinical Investigation , vol.74 , Issue.4 , pp. 1398-1403
    • Marklund, S.L.1
  • 14
    • 26444542945 scopus 로고    scopus 로고
    • Somatodendritic accumulation of misfolded SOD1-L126Z in motor neurons mediates degeneration: alphaB-crystallin modulates aggregation
    • DOI 10.1093/hmg/ddi236
    • Wang J, Xu G, Li H, Gonzales V, Fromholt D, Karch C, Copeland NG, Jenkins NA, Borchelt DR. Somatodendritic accumulation of misfolded SOD1-L126Z in motor neurons mediates degeneration: alphaB-crystallin modulates aggregation. Hum Mol Genet 14:2335-2347, 2005. (Pubitemid 41417996)
    • (2005) Human Molecular Genetics , vol.14 , Issue.16 , pp. 2335-2347
    • Wang, J.1    Xu, G.2    Li, H.3    Gonzales, V.4    Fromholt, D.5    Karch, C.6    Copeland, N.G.7    Jenkins, N.A.8    Borchelt, D.R.9
  • 17
    • 0021768595 scopus 로고
    • Human Cu/Zn superoxide dismutase gene: Molecular characterization of its two mRNA species
    • Sherman L, Levanon D, Lieman-Hurwitz J, Dafni N, Groner Y. Human Cu/Zn superoxide dismutase gene: molecular characterization of its two mRNA species. Nucleic Acids Res 12:9349-9365, 1984.
    • (1984) Nucleic Acids Res , vol.12 , pp. 9349-9365
    • Sherman, L.1    Levanon, D.2    Lieman-Hurwitz, J.3    Dafni, N.4    Groner, Y.5
  • 18
    • 33645108336 scopus 로고    scopus 로고
    • Mapping superoxide dismutase 1 domains of non-native interaction: Roles of intra- And intermolecular disulfide bonding in aggregation
    • Wang J, Xu G, Borchelt DR. Mapping superoxide dismutase 1 domains of non-native interaction: roles of intra- and intermolecular disulfide bonding in aggregation. J Neurochem 96:1277-1288, 2006.
    • (2006) J Neurochem , vol.96 , pp. 1277-1288
    • Wang, J.1    Xu, G.2    Borchelt, D.R.3
  • 19
    • 0028888945 scopus 로고
    • Transgenic mice expressing an altered murine superoxide dismutase gene provide an animal model of amyotrophic lateral sclerosis
    • Ripps ME, Huntley GW, Hof PR, Morrison JH, Gordon JW. Transgenic mice expressing an altered murine superoxide dismutase gene provide an animal model of amyotrophic lateral sclerosis. Proc Natl Acad Sci U S A 92:689-693, 1995.
    • (1995) Proc Natl Acad Sci U S A , 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
  • 22
    • 0029053881 scopus 로고
    • An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria
    • Wong PC, Pardo CA, Borchelt DR, Lee MK, Copeland NG, Jenkins NA, Sisodia SS, Cleveland DW, Price DL. An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria. Neuron 14:1105-1116, 1995.
    • (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
  • 25
    • 0347358915 scopus 로고    scopus 로고
    • Minute quantities of misfolded mutant superoxide dismutase-1 cause amyotrophic lateral sclerosis
    • DOI 10.1093/brain/awh005
    • Jonsson PA, Ernhill K, Andersen PM, Bergemalm D, Brannstrom T, Gredal O, Nilsson P, Marklund SL. Minute quantities of misfolded mutant superoxide dismutase-1 cause amyotrophic lateral sclerosis. Brain 127:73-88, 2004. (Pubitemid 38055347)
    • (2004) Brain , vol.127 , Issue.1 , pp. 73-88
    • Jonsson, P.A.1    Ernhill, K.2    Andersen, P.M.3    Bergemalm, D.4    Brannstrom, T.5    Gredal, O.6    Nilsson, P.7    Marklund, S.L.8
  • 27
    • 0035575761 scopus 로고    scopus 로고
    • Rats expressing human cytosolic copper-zinc superoxide dismutase transgenes with amyotrophic lateral sclerosis: Associated mutations develop motor neuron disease
    • Nagai M, Aoki M, Miyoshi I, Kato M, Pasinelli P, Kasai N, Brown RH Jr, Itoyama Y. Rats expressing human cytosolic copper-zinc superoxide dismutase transgenes with amyotrophic lateral sclerosis: associated mutations develop motor neuron disease. J Neurosci 21:9246-9254, 2001. (Pubitemid 33096868)
    • (2001) Journal of Neuroscience , vol.21 , Issue.23 , pp. 9246-9254
    • Nagai, M.1    Aoki, M.2    Miyoshi, I.3    Kato, M.4    Pasinelli, P.5    Kasai, N.6    Brown Jr., R.H.7    Itoyama, Y.8
  • 28
  • 29
    • 32044475396 scopus 로고    scopus 로고
    • Variable metallation of human superoxide dismutase: Atomic resolution crystal structures of Cu-Zn, Zn-Zn and as-isolated wild-type enzymes
    • Strange RW, Antonyuk SV, Hough MA, Doucette PA, Valentine JS, Hasnain SS. Variable metallation of human superoxide dismutase: atomic resolution crystal structures of Cu-Zn, Zn-Zn and as-isolated wild-type enzymes. J Mol Biol 356:1152-1162, 2006.
    • (2006) J Mol Biol , vol.356 , pp. 1152-1162
    • Strange, R.W.1    Antonyuk, S.V.2    Hough, M.A.3    Doucette, P.A.4    Valentine, J.S.5    Hasnain, S.S.6
  • 31
    • 0037388067 scopus 로고    scopus 로고
    • Misfolded CuZnSOD and amyotrophic lateral sclerosis
    • Valentine JS, Hart PJ. Misfolded CuZnSOD and amyotrophic lateral sclerosis. Proc Natl Acad Sci U S A 100:3617-3622, 2003.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 3617-3622
    • Valentine, J.S.1    Hart, P.J.2
  • 33
    • 0031911637 scopus 로고    scopus 로고
    • Subunit asymmetry in the three-dimensional structure of a human CuZnSOD mutant found in familial amyotrophic lateral sclerosis
    • Hart PJ, Liu H, Pellegrini M, Nersissian AM, Gralla EB, Valentine JS, Eisenberg D. Subunit asymmetry in the three-dimensional structure of a human CuZnSOD mutant found in familial amyotrophic lateral sclerosis. Protein Sci 7:545-555, 1998. (Pubitemid 28130875)
    • (1998) Protein Science , vol.7 , Issue.3 , pp. 545-555
    • Hart, P.J.1    Liu, H.2    Pellegrini, M.3    Nersissian, A.M.4    Gralla, E.B.5    Valentine, J.S.6    Eisenberg, D.7
  • 34
    • 34548513550 scopus 로고    scopus 로고
    • Metalation of the amyotrophic lateral sclerosis mutant glycine 37 to arginine superoxide dismutase (SOD1) apoprotein restores its structural and dynamical properties in solution to those of metalated wild-type SOD1
    • DOI 10.1021/bi700620r
    • Banci L, Bertini I, D'Amelio N, Libralesso E, Turano P, Valentine JS. Metalation of the amyotrophic lateral sclerosis mutant glycine 37 to arginine superoxide dismutase (SOD1) apoprotein restores its structural and dynamical properties in solution to those of metalated wild-type SOD1. Biochemistry 46:9953-9962, 2007. (Pubitemid 47378585)
    • (2007) Biochemistry , vol.46 , Issue.35 , pp. 9953-9962
    • Banci, L.1    Bertini, I.2    D'Amelio, N.3    Libralesso, E.4    Turano, P.5    Valentine, J.S.6
  • 36
    • 0344839082 scopus 로고    scopus 로고
    • Dynamic properties of the G93A mutant of copper-zinc superoxide dismutase as detected by NMR spectroscopy: Implications for the pathology of familial amyotrophic lateral sclerosis
    • Shipp EL, Cantini F, Bertini I, Valentine JS, Banci L. Dynamic properties of the G93A mutant of copper-zinc superoxide dismutase as detected by NMR spectroscopy: implications for the pathology of familial amyotrophic lateral sclerosis. Biochemistry 42:1890-1899, 2003.
    • (2003) Biochemistry , vol.42 , pp. 1890-1899
    • Shipp, E.L.1    Cantini, F.2    Bertini, I.3    Valentine, J.S.4    Banci, L.5
  • 44
    • 0037013224 scopus 로고    scopus 로고
    • Familial amyotrophic lateral sclerosis-associated mutations decrease the thermal stability of distinctly metallated species of human copper/zinc superoxide dismutase
    • DOI 10.1074/jbc.M112088200
    • Rodriguez JA, Valentine JS, Eggers DK, Roe JA, Tiwari A, Brown RH Jr, Hayward LJ. Familial ALS-associated mutations decrease the thermal stability of distinctly metallated species of human copper-zinc superoxide dismutase. J Biol Chem 277:15932-15937, 2002. (Pubitemid 34967874)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.18 , pp. 15932-15937
    • Rodriguez, J.A.1    Valentine, J.S.2    Eggers, D.K.3    Roe, J.A.4    Tiwari, A.5    Brown Jr., R.H.6    Hayward, L.J.7
  • 46
    • 0015935503 scopus 로고
    • On the stability of bovine superoxide dismutase. the effects of metals. Histidine at the active site of superoxide dismutase
    • Forman HJ, Fridovich I. On the stability of bovine superoxide dismutase. The effects of metals. Histidine at the active site of superoxide dismutase. J Biol Chem 248:2645-2649, 1973.
    • (1973) J Biol Chem , vol.248 , pp. 2645-2649
    • Forman, H.J.1    Fridovich, I.2
  • 47
    • 0015502085 scopus 로고
    • Subunit structure of human superoxide dismutase
    • Hartz JW, Deutsch HF. Subunit structure of human superoxide dismutase. J Biol Chem 247:7043-7050, 1972.
    • (1972) J Biol Chem , vol.247 , pp. 7043-7050
    • Hartz, J.W.1    Deutsch, H.F.2
  • 48
    • 11144227941 scopus 로고    scopus 로고
    • Dissociation of human copper-zinc superoxide dismutase dimers using chaotrope and reductant: Insights into the molecular basis for dimer stability
    • DOI 10.1074/jbc.M409744200
    • Doucette PA, Whitson LJ, Cao X, Schirf V, Demeler B, Valentine JS, Hansen JC, Hart PJ. Dissociation of human copper-zinc superoxide dismutase dimers using chaotrope and reductant. Insights into the molecular basis for dimer stability. J Biol Chem 279:54558-54566, 2004. (Pubitemid 40053198)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.52 , pp. 54558-54566
    • Doucette, P.A.1    Whitson, L.J.2    Cao, X.3    Schirf, V.4    Demeler, B.5    Valentine, J.S.6    Hansen, J.C.7    Hart, P.J.8
  • 50
    • 9144261759 scopus 로고    scopus 로고
    • The unusually stable quaternary structure of human Cu,Zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide status
    • DOI 10.1074/jbc.M406021200
    • Arnesano F, Banci L, Bertini I, Martinelli M, Furukawa Y, O'Halloran TV. The unusually stable quaternary structure of human Cu,Zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide status. J Biol Chem 279:47998-48003, 2004. (Pubitemid 39540952)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.46 , pp. 47998-48003
    • Arnesano, F.1    Banci, L.2    Bertini, I.3    Martinelli, M.4    Furukawa, Y.5    O'Halloran, T.V.6
  • 51
    • 33644853318 scopus 로고    scopus 로고
    • Human SOD1 before harboring the catalytic metal: Solution structure of copper-depleted, disulfide-reduced form
    • DOI 10.1074/jbc.M506497200
    • Banci L, Bertini I, Cantini F, D'Amelio N, Gaggelli E. Human SOD1 before harboring the catalytic metal: solution structure of copper-depleted, disulfide-reduced form. J Biol Chem 281:2333-2337, 2006. (Pubitemid 43845824)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.4 , pp. 2333-2337
    • Banci, L.1    Bertini, I.2    Cantini, F.3    D'Amelio, N.4    Gaggelli, E.5
  • 53
    • 0036407227 scopus 로고    scopus 로고
    • Peptide aggregation in neurodegenerative disease
    • Murphy RM. Peptide aggregation in neurodegenerative disease. Annu Rev Biomed Eng 4:155-174, 2002.
    • (2002) Annu Rev Biomed Eng , vol.4 , pp. 155-174
    • Murphy, R.M.1
  • 54
    • 2142761528 scopus 로고    scopus 로고
    • An Intersubunit Disulfide Bond Prevents in Vitro Aggregation of a Superoxide Dismutase-1 Mutant Linked to Familial Amytrophic Lateral Sclerosis
    • DOI 10.1021/bi030246r
    • Ray SS, Nowak RJ, Strokovich K, Brown RH Jr., Walz T, Lansbury PT Jr. An intersubunit disulfide bond prevents in vitro aggregation of a superoxide dismutase-1 mutant linked to familial amytrophic lateral sclerosis. Biochemistry 43:4899-4905, 2004. (Pubitemid 38544443)
    • (2004) Biochemistry , vol.43 , Issue.17 , pp. 4899-4905
    • Ray, S.S.1    Nowak, R.J.2    Strokovich, K.3    Brown Jr., R.H.4    Walz, T.5    Lansbury Jr., P.T.6
  • 55
    • 46649096661 scopus 로고    scopus 로고
    • A limited role for disulfide cross-linking in the aggregation of mutant SOD1 linked to familial amyotrophic lateral sclerosis
    • Karch CM, Borchelt DR. A limited role for disulfide cross-linking in the aggregation of mutant SOD1 linked to familial amyotrophic lateral sclerosis. J Biol Chem 283:13528-13537, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 13528-13537
    • Karch, C.M.1    Borchelt, D.R.2
  • 57
    • 0034869733 scopus 로고    scopus 로고
    • Copper chaperone for superoxide dismutase co-aggregates with superoxide dismutase 1 (SOD1) in neuronal Lewy body-like hyaline inclusions: An immunohistochemical study on familial amyotrophic lateral sclerosis with SOD1 gene mutation
    • Kato S, Sumi-Akamaru H, Fujimura H, Sakoda S, Kato M, Hirano A, Takikawa M, Ohama E. Copper chaperone for superoxide dismutase co-aggregates with superoxide dismutase 1 (SOD1) in neuronal Lewy body-like hyaline inclusions: an immunohistochemical study on familial amyotrophic lateral sclerosis with SOD1 gene mutation. Acta Neuropathol (Berl) 102:233-238, 2001. (Pubitemid 32816143)
    • (2001) Acta Neuropathologica , vol.102 , Issue.3 , pp. 233-238
    • Kato, S.1    Sumi-Akamaru, H.2    Fujimura, H.3    Sakoda, S.4    Kato, M.5    Hirano, A.6    Takikawa, M.7    Ohama, E.8
  • 58
    • 4744373180 scopus 로고    scopus 로고
    • Familial amyotrophic lateral sclerosis with His46Arg mutation in Cu/Zn superoxide dismutase presenting characteristic clinical features and Lewy body-like hyaline inclusions
    • DOI 10.1016/j.jns.2004.06.008, PII S0022510X0400200X
    • Ohi T, Nabeshima K, Kato S, Yazawa S, Takechi S. Familial amyotrophic lateral sclerosis with His46Arg mutation in Cu/Zn superoxide dismutase presenting characteristic clinical features and Lewy body-like hyaline inclusions. J Neurol Sci 225:19-25, 2004. (Pubitemid 39311705)
    • (2004) Journal of the Neurological Sciences , vol.225 , Issue.1-2 , pp. 19-25
    • Ohi, T.1    Nabeshima, K.2    Kato, S.3    Yazawa, S.4    Takechi, S.5
  • 61
    • 0029840428 scopus 로고    scopus 로고
    • Familial amyotrophic lateral sclerosis with a two base pair deletion in superoxide dismutase 1 gene: Multisystem degeneration with intracytoplasmic hyaline inclusions in astrocytes
    • Kato S, Shimoda M, Watanabe Y, Nakashima K, Takahashi K, Ohama E. Familial amyotrophic lateral sclerosis with a two base pair deletion in superoxide dismutase 1 gene: Multisystem degeneration with intracytoplasmic hyaline inclusioins in astrocytes. J Neuropathol Exp Neurol 55:1089-1101, 1996. (Pubitemid 26338021)
    • (1996) Journal of Neuropathology and Experimental Neurology , vol.55 , Issue.10 , pp. 1089-1101
    • Kato, S.1    Shimoda, M.2    Watanabe, Y.3    Nakashima, K.4    Takahashi, K.5    Ohama, E.6
  • 63
    • 0029792449 scopus 로고    scopus 로고
    • Familial amyotrophic lateral sclerosis with a mutation in exon 4 of the Cu/Zn superoxide dismutase gene: Pathological and immunocytochemical changes
    • DOI 10.1007/s004010050535
    • Ince PG. Familial amyotrophic lateral sclerosis with a mutation in exon 4 of the Cu/Zn superoxide dismutase gene: pathological and immunocytochemical changes. Acta Neuropathol 92:395-403, 1996. (Pubitemid 26317107)
    • (1996) Acta Neuropathologica , vol.92 , Issue.4 , pp. 395-403
    • Ince, P.G.1    Shaw, P.J.2    Slade, J.Y.3    Jones, C.4    Hudgson, P.5
  • 65
    • 0030838263 scopus 로고    scopus 로고
    • A clinicopathological study of a patient with familial amyotrophic lateral sclerosis associated with a two base pair deletion in the copper/zinc superoxide dismutase (SOD1) gene
    • DOI 10.1007/s004010050758
    • Kadekawa J, Fujimura H, Ogawa Y, Hattori N, Kaido M, Nishimura T, Yoshikawa H, Shirahata N, Sakoda S, Yanagihara T. A clinicopathological study of a patient with familial amyotrophic lateral sclerosis associated with a two base pair deletion in the copper/zinc superoxide dismutase (SOD1) gene. Acta Neuropathol 94:617-622, 1997. (Pubitemid 27511185)
    • (1997) Acta Neuropathologica , vol.94 , Issue.6 , pp. 617-622
    • Kadekawa, J.1    Fujimura, H.2    Ogawa, Y.3    Hattori, N.4    Kaido, M.5    Nishimura, T.6    Yoshikawa, H.7    Shirahata, N.8    Sakoda, S.9    Yanagihara, T.10
  • 68
    • 33745821631 scopus 로고    scopus 로고
    • Posttranslational modifications in Cu,Zn-superoxide dismutase and mutations associated with amyptrophic lateral sclerosis
    • DOI 10.1089/ars.2006.8.847
    • Furukawa Y, O'Halloran TV. Posttranslational modifications in Cu,Zn-superoxide dismutase and mutations associated with amyotrophic lateral sclerosis. Antioxid Redox Signal 8:847-867, 2006. (Pubitemid 44036502)
    • (2006) Antioxidants and Redox Signaling , vol.8 , Issue.5-6 , pp. 847-867
    • Furukawa, Y.1    O'Halloran, T.V.2
  • 69
    • 38149115471 scopus 로고    scopus 로고
    • Cysteine 111 affects aggregation and cytotoxicity of mutant Cu,Zn-superoxide dismutase associated with familial amyotrophic lateral sclerosis
    • Cozzolino M, Amori I, Pesaresi MG, Ferri A, Nencini M, Carrì MT. Cysteine 111 affects aggregation and cytotoxicity of mutant Cu,Zn-superoxide dismutase associated with familial amyotrophic lateral sclerosis. J Biol Chem 283:866-874, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 866-874
    • Cozzolino, M.1    Amori, I.2    Pesaresi, M.G.3    Ferri, A.4    Nencini, M.5    Carrì, M.T.6
  • 70
    • 31544467869 scopus 로고    scopus 로고
    • Disulphide-reduced superoxide dismutase-1 in CNS of transgenic amyotrophic lateral sclerosis models
    • DOI 10.1093/brain/awh704
    • Jonsson PA, Karin SG, Peter MA, Thomas Bnm, Mikael L, Mikael O. Disulphide-reduced superoxide dismutase-1 in CNS of transgenic amyotrophic lateral sclerosis models. Brain 129:451-464, 2006. (Pubitemid 43164368)
    • (2006) Brain , vol.129 , Issue.2 , pp. 451-464
    • Jonsson, P.A.1    Graffmo, K.S.2    Andersen, P.M.3    Brannstrom, T.4    Lindberg, M.5    Oliveberg, M.6    Marklund, S.L.7
  • 74
    • 0037022563 scopus 로고    scopus 로고
    • Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation
    • Richardson JS, Richardson DC. Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc Natl Acad Sci U S A 99:2754-2759, 2002.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 2754-2759
    • Richardson, J.S.1    Richardson, D.C.2
  • 75
    • 0037130174 scopus 로고    scopus 로고
    • Neurodegenerative disease: Amyloid pores from pathogenic mutations
    • Lashuel HA, Hartley D, Petre BM, Walz T, Lansbury PT Jr. Neurodegenerative disease: amyloid pores from pathogenic mutations. Nature 418:291, 2002. (Pubitemid 34790672)
    • (2002) Nature , vol.418 , Issue.6895 , pp. 291
    • Lashuel, H.A.1    Hartley, D.2    Petre, B.M.3    Walz, T.4    Lansbury Jr., P.T.5
  • 76
    • 43049132896 scopus 로고    scopus 로고
    • Heterodimer formation of wild-type and amyotrophic lateral sclerosis-causing mutant Cu/Zn-superoxide dismutase induces toxicity independent of protein aggregation
    • DOI 10.1093/hmg/ddn025
    • Witan H, Kern A, Koziollek-Drechsler I, Wade R, Behl C, Clement AM. Heterodimer formation of wild-type and amyotrophic lateral sclerosis-causing mutant Cu/Zn-superoxide dismutase induces toxicity independent of protein aggregation. Hum Mol Genet 17:1373-1385, 2008. (Pubitemid 351627334)
    • (2008) Human Molecular Genetics , vol.17 , Issue.10 , pp. 1373-1385
    • Witan, H.1    Kern, A.2    Koziollek-Drechsler, I.3    Wade, R.4    Behl, C.5    Clement, A.M.6
  • 77
    • 26444471905 scopus 로고    scopus 로고
    • Structural properties and neuronal toxicity of amyotrophic lateral sclerosis-associated Cu/Zn superoxide dismutase 1 aggregates
    • DOI 10.1083/jcb.200504050
    • Matsumoto G, Stojanovic A, Holmberg CI, Kim S, Morimoto RI. Structural properties and neuronal toxicity of amyotrophic lateral sclerosis-associated Cu/Zn superoxide dismutase 1 aggregates. J Cell Biol 171:75-85, 2005. (Pubitemid 41434603)
    • (2005) Journal of Cell Biology , vol.171 , Issue.1 , pp. 75-85
    • Matsumoto, G.1    Stojanovic, A.2    Holmberg, C.I.3    Kim, S.4    Morimoto, R.I.5
  • 78
    • 1842782787 scopus 로고    scopus 로고
    • Oxygen and the copper chaperone CCS regulate posttranslational activation of Cu,Zn superoxide dismutase
    • Brown NM, Torres AS, Doan PE, O'Halloran TV. Oxygen and the copper chaperone CCS regulate posttranslational activation of Cu,Zn superoxide dismutase. Proc Natl Acad Sci U S A 101:5518-5523, 2004.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 5518-5523
    • Brown, N.M.1    Torres, A.S.2    Doan, P.E.3    O'Halloran, T.V.4
  • 82
    • 35448929548 scopus 로고    scopus 로고
    • A multinuclear copper(I) cluster forms the dimerization interface in copper-loaded human copper chaperone for superoxide dismutase
    • Stasser JP, Siluvai GS, Barry AN, Blackburn NJ. A multinuclear copper(I) cluster forms the dimerization interface in copper-loaded human copper chaperone for superoxide dismutase. Biochemistry 46:11845-11856, 2007.
    • (2007) Biochemistry , vol.46 , pp. 11845-11856
    • Stasser, J.P.1    Siluvai, G.S.2    Barry, A.N.3    Blackburn, N.J.4
  • 83
    • 0034878525 scopus 로고    scopus 로고
    • Heterodimeric structure of superoxide dismutase in complex with its metallochaperone
    • DOI 10.1038/nsb0901-751
    • Lamb AL, Torres AS, O'Halloran TV, Rosenzweig AC. Heterodimeric structure of superoxide dismutase in complex with its metallochaperone. Nat Struct Biol 8:751-755, 2001. (Pubitemid 32803590)
    • (2001) Nature Structural Biology , vol.8 , Issue.9 , pp. 751-755
    • Lamb, A.L.1    Torres, A.S.2    O'Halloran, T.V.3    Rosenzweig, A.C.4
  • 84
    • 53049109088 scopus 로고    scopus 로고
    • Complete loss of post-translational modifications triggers fibrillar aggregation of SOD1 in the familial form of amyotrophic lateral sclerosis
    • Furukawa Y, Kaneko K, Yamanaka K, O'Halloran TV, Nukina N. Complete loss of post-translational modifications triggers fibrillar aggregation of SOD1 in the familial form of amyotrophic lateral sclerosis. J Biol Chem 283:24167-24176, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 24167-24176
    • Furukawa, Y.1    Kaneko, K.2    Yamanaka, K.3    O'Halloran, T.V.4    Nukina, N.5
  • 88
    • 44849139852 scopus 로고    scopus 로고
    • Biological effects of CCS in the absence of SOD1 enzyme activation: Implications for disease in a mouse model for ALS
    • DOI 10.1093/hmg/ddn063
    • Proescher JB, Son M, Elliott JL, Culotta VC. Biological effects of CCS in the absence of SOD1 enzyme activation: implications for disease in a mouse model for ALS. Hum Mol Genet 17:1728-1737, 2008. (Pubitemid 351791499)
    • (2008) Human Molecular Genetics , vol.17 , Issue.12 , pp. 1728-1737
    • Proescher, J.B.1    Son, M.2    Elliott, J.L.3    Culotta, V.C.4
  • 90
    • 0032101171 scopus 로고    scopus 로고
    • Simple and defined method to detect the SOD-1 mutants from patients with familial amyotrophic lateral sclerosis by mass spectrometry
    • DOI 10.1016/S0165-0270(98)00012-0, PII S0165027098000120
    • Nakanishi T, Kishikawa M, Miyazaki A, Shimizu A, Ogawa Y, Sakoda S, Ohi T, Shoji H. Simple and defined method to detect the SOD-1 mutants from patients with familial amyotrophic lateral sclerosis by mass spectrometry. J Neurosci Methods 81:41-44, 1998. (Pubitemid 28293717)
    • (1998) Journal of Neuroscience Methods , vol.81 , Issue.1-2 , pp. 41-44
    • Nakanishi, T.1    Kishikawa, M.2    Miyazaki, A.3    Shimizu, A.4    Ogawa, Y.5    Sakoda, S.6    Ohi, T.7    Shoji, H.8
  • 91
    • 0030900245 scopus 로고    scopus 로고
    • A familial amyotrophic lateral sclerosis-associated A4V Cu, Zn- Superoxide dismutase mutant has a lower Km for hydrogen peroxide. Correlation between clinical severity and the Km value
    • Yim HS, Kang JH, Chock PB, Stadtman ER, Yim MB. A familial amyotrophic lateral sclerosis-associated A4V Cu, Zn- superoxide dismutase mutant has a lower Km for hydrogen peroxide. Correlation between clinical severity and the Km value. J Biol Chem 272:8861-8863, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 8861-8863
    • Yim, H.S.1    Kang, J.H.2    Chock, P.B.3    Stadtman, E.R.4    Yim, M.B.5
  • 93
    • 0035036119 scopus 로고    scopus 로고
    • Superoxide dismutase gene mutations in Italian patients with familial and sporadic amyotrophic lateral sclerosis: Identification of three novel missense mutations
    • DOI 10.1016/S0960-8966(00)00215-7, PII S0960896600002157
    • Gellera C, Castellotti B, Riggio MC, Silani V, Morandi L, Testa D, Casali C, Taroni F, Di Donato S, Zeviani M, Mariotti C. Superoxide dismutase gene mutations in Italian patients with familial and sporadic amyotrophic lateral sclerosis: Identification of three novel missense mutations. Neuromuscul Disord 11:404-410, 2001. (Pubitemid 32448085)
    • (2001) Neuromuscular Disorders , vol.11 , Issue.4 , pp. 404-410
    • Gellera, C.1    Castellotti, B.2    Riggio, M.C.3    Silani, V.4    Morandi, L.5    Testa, D.6    Casali, C.7    Taroni, F.8    Di Donato, S.9    Zeviani, M.10    Mariotti, C.11
  • 94
    • 0032749585 scopus 로고    scopus 로고
    • A novel mutation (Cys6Gly) in the Cu/Zn superoxide dismutase gene associated with rapidly progressive familial amyotrophic lateral sclerosis
    • DOI 10.1016/S0304-3940(99)00803-4, PII S0304394099008034
    • Kohno S, Takahashi Y, Miyajima H, Serizawa M, Mizoguchi K. A novel mutation (Cys6Gly) in the Cu/Zn superoxide dismutase gene associated with rapidly progressive familial amyotrophic lateral sclerosis. Neurosci Lett 276:135-137, 1999. (Pubitemid 29525508)
    • (1999) Neuroscience Letters , vol.276 , Issue.2 , pp. 135-137
    • Kohno, S.1    Takahashi, Y.2    Miyajima, H.3    Serizawa, M.4    Mizoguchi, K.5
  • 95
    • 0030052392 scopus 로고    scopus 로고
    • A novel two-base mutation in the Cu/Zn superoxide dismutase gene associated with familial amyotrophic lateral sclerosis in Japan
    • DOI 10.1016/0304-3940(96)12378-8
    • Morita M, Aoki M, Abe K, Hasegawa T, Sakuma R, Onodera Y, Ichikawa N, Nishizawa M, Itoyama Y. A novel two-base mutation in the Cu/Zn superoxide dismutase gene associated with familial amyotrophic lateral sclerosis in Japan. Neurosci Lett 205:79-82, 1996. (Pubitemid 26071319)
    • (1996) Neuroscience Letters , vol.205 , Issue.2 , pp. 79-82
    • Morita, M.1    Aoki, M.2    Abe, K.3    Hasegawa, T.4    Sakuma, R.5    Onodera, Y.6    Ichikawa, N.7    Nishizawa, M.8    Itoyama, Y.9
  • 96
    • 0035136084 scopus 로고    scopus 로고
    • Compound heterozygous D90A and D96N SOD1 mutations in a recessive amyotrophic lateral sclerosis family
    • DOI 10.1002/1531-8249(20010201)49:2<267::AID-ANA51>3.0.CO;2-D
    • Hand CK, Mayeux-Portas V, Khoris J, Briolotti V, Clavelou P, Camu W, Rouleau GA. Compound heterozygous D90A and D96N SOD1 mutations in a recessive amyotrophic lateral sclerosis family. Ann Neurol 49:267-271, 2001. (Pubitemid 32158007)
    • (2001) Annals of Neurology , vol.49 , Issue.2 , pp. 267-271
    • Hand, C.K.1    Mayeux-Portas, V.2    Khoris, J.3    Briolotti, V.4    Clavelou, P.5    Camu, W.6    Rouleau, G.A.7
  • 99
    • 0029810307 scopus 로고    scopus 로고
    • Genetics of amyotrophic lateral sclerosis
    • Siddique T, Deng HX. Genetics of amyotrophic lateral sclerosis. Hum Mol Genet 5(Spec No):1465-1470, 1996.
    • (1996) Hum Mol Genet , vol.5 , Issue.SPEC. NO. , pp. 1465-1470
    • Siddique, T.1    Deng, H.X.2
  • 100
    • 0037437678 scopus 로고    scopus 로고
    • A novel SOD1 gene mutation in a Korean family with amyotrophic lateral sclerosis
    • DOI 10.1016/S0022-510X(02)00338-6, PII S0022510X02003386
    • Kim NH, Kim HJ, Kim M, Lee KW. A novel SOD1 gene mutation in a Korean family with amyotrophic lateral sclerosis. J Neurol Sci 206:65-69, 2003. (Pubitemid 35448080)
    • (2003) Journal of the Neurological Sciences , vol.206 , Issue.1 , pp. 65-69
    • Kim, N.-H.1    Kim, H.-J.2    Kim, M.3    Lee, K.-W.4
  • 101
    • 0029036463 scopus 로고
    • An improved protocol for the analysis of SOD1 gene mutations, and a new mutation in exon 4
    • Yulug IG, Katsanis N, de Belleroche J, Collinge J, Fisher EM. An improved protocol for the analysis of SOD1 gene mutations, and a new mutation in exon 4. Hum Mol Genet 4:1101-1104, 1995.
    • (1995) Hum Mol Genet , vol.4 , pp. 1101-1104
    • Yulug, I.G.1    Katsanis, N.2    De Belleroche, J.3    Collinge, J.4    Fisher, E.M.5
  • 103
    • 0027944708 scopus 로고
    • Identification of a novel exon 4 SOD1 mutation in a sporadic amyotrophic lateral sclerosis patient
    • DOI 10.1006/mcpr.1994.1046
    • Jones CT, Shaw PJ, Chari G, Brock DJ. Identification of a novel exon 4 SOD1 mutation in a sporadic amyotrophic lateral sclerosis patient. Mol Cell Probes 8:329-330, 1994. (Pubitemid 24324606)
    • (1994) Molecular and Cellular Probes , vol.8 , Issue.4 , pp. 329-330
    • Jones, C.T.1    Shaw, P.J.2    Chari, G.3    Brock, D.J.H.4
  • 106
    • 0029400840 scopus 로고
    • Variable clinical symptoms in familial amyotrophic lateral sclerosis with a novel point mutation in the Cu/Zn superoxide dismutase gene
    • Ikeda M, Abe K, Aoki M, Sahara M, Watanabe M, Shoji M, St George-Hyslop PH, Hirai S, Itoyama Y. Variable clinical symptoms in familial amyotrophic lateral sclerosis with a novel point mutation in the Cu/Zn superoxide dismutase gene. Neurology 45:2038-2042, 1995.
    • (1995) Neurology , vol.45 , pp. 2038-2042
    • Ikeda, M.1    Abe, K.2    Aoki, M.3    Sahara, M.4    Watanabe, M.5    Shoji, M.6    St George-Hyslop, P.H.7    Hirai, S.8    Itoyama, Y.9
  • 107
    • 0030749160 scopus 로고    scopus 로고
    • Phenotypic heterogeneity in motor neuron disease patients with CuZn-superoxide dismutase mutations in Scandinavia
    • DOI 10.1093/brain/120.10.1723
    • Andersen PM, Nilsson P, Keranen ML, Forsgren L, Hagglund J, Karlsborg M, Ronnevi LO, Gredal O, Marklund SL. Phenotypic heterogeneity in motor neuron disease patients with CuZn-superoxide dismutase mutations in Scandinavia. Brain 120(Pt 10):1723-1737, 1997. (Pubitemid 27443049)
    • (1997) Brain , vol.120 , Issue.10 , pp. 1723-1737
    • Andersen, P.M.1    Nilsson, P.2    Keranen, M.-L.3    Forsgren, L.4    Hagglund, J.5    Karlsborg, M.6    Ronnevi, L.-O.7    Gredal, O.8    Marklund, S.L.9
  • 109
    • 0030961866 scopus 로고    scopus 로고
    • Novel G16S (GGC-AGC) mutation in the SOD-1 gene in a patient with apparently sporadic young-onset amyotrophic lateral sclerosis
    • DOI 10.1002/(SICI)1098-1004(1997)9:4<356::AID-HUMU9>3.0.CO;2-3
    • Kawamata J, Shimohama S, Takano S, Harada K, Ueda K, Kimura J. Novel G16S (GGC-AGC) mutation in the SOD-1 gene in a patient with apparently sporadic young-onset amyotrophic lateral sclerosis. Hum Mutat 9:356-358, 1997. (Pubitemid 27157655)
    • (1997) Human Mutation , vol.9 , Issue.4 , pp. 356-358
    • Kawamata, J.1    Shimohama, S.2    Takano, S.3    Harada, K.4    Ueda, K.5    Kimura, J.6
  • 110
    • 0030945491 scopus 로고    scopus 로고
    • Clinical and functional investigation of 10 missense mutations and a novel frameshift insertion mutation of the gene for copper-zinc superoxide dismutase in UK families with amyotrophic lateral sclerosis
    • Orrell RW, Habgood JJ, Gardiner I, King AW, Bowe FA, Hallewell RA, Marklund SL, Greenwood J, Lane RJ, deBelleroche J. Clinical and functional investigation of 10 missense mutations and a novel frameshift insertion mutation of the gene for copper-zinc superoxide dismutase in UK families with amyotrophic lateral sclerosis. Neurology 48:746-751, 1997.
    • (1997) Neurology , vol.48 , pp. 746-751
    • Orrell, R.W.1    Habgood, J.J.2    Gardiner, I.3    King, A.W.4    Bowe, F.A.5    Hallewell, R.A.6    Marklund, S.L.7    Greenwood, J.8    Lane, R.J.9    DeBelleroche, J.10
  • 111
    • 33847334695 scopus 로고    scopus 로고
    • Identification of a novel D109Y mutation in Cu/Zn superoxide dismutase (sod1) gene associated with amyotrophic lateral sclerosis
    • DOI 10.1016/j.jns.2006.12.009, PII S0022510X06005648
    • Naini A, Mehrazin M, Lu J, Gordon P, Mitsumoto H. Identification of a novel D109Y mutation in Cu/Zn superoxide dismutase (sod1) gene associated with amyotrophic lateral sclerosis. J Neurol Sci 254:17-21, 2007. (Pubitemid 46330402)
    • (2007) Journal of the Neurological Sciences , vol.254 , Issue.1-2 , pp. 17-21
    • Naini, A.1    Mehrazin, M.2    Lu, J.3    Gordon, P.4    Mitsumoto, H.5
  • 112
    • 0028273306 scopus 로고
    • Identification of a novel SOD1 mutation in an apparently sporadic amyotrophic lateral sclerosis patient and the detection of lle113Thr in three others
    • Jones CT, Swingler RJ, Brock DJ. Identification of a novel SOD1 mutation in an apparently sporadic amyotrophic lateral sclerosis patient and the detection of Ile113Thr in three others. Hum Mol Genet 3:649-650, 1994. (Pubitemid 24122183)
    • (1994) Human Molecular Genetics , vol.3 , Issue.4 , pp. 649-650
    • Jones, C.T.1    Swingler, R.J.2    Brock, D.J.H.3
  • 117
    • 0028601342 scopus 로고
    • Autosomal dominant amyotrophic lateral sclerosis: A novel mutation in the Cu/Zn superoxide dismutase-1 gene
    • Kostrzewa M, Burck-Lehmann U, Muller U. Autosomal dominant amyotrophic lateral sclerosis: a novel mutation in the Cu/Zn superoxide dismutase-1 gene. Hum Mol Genet 3:2261-2262, 1994.
    • (1994) Hum Mol Genet , vol.3 , pp. 2261-2262
    • Kostrzewa, M.1    Burck-Lehmann, U.2    Muller, U.3
  • 118
    • 31544466502 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis associated with mutations in the CuZn superoxide dismutase gene
    • Andersen PM. Amyotrophic lateral sclerosis associated with mutations in the CuZn superoxide dismutase gene. Curr Neurol Neurosci Rep 6:37-46, 2006. (Pubitemid 43154251)
    • (2006) Current Neurology and Neuroscience Reports , vol.6 , Issue.1 , pp. 37-46
    • Andersen, P.M.1
  • 120
    • 0030780350 scopus 로고    scopus 로고
    • Copper/zinc superoxide dismutase 1 and sporadic amyotrophic lateral sclerosis: Analysis of 155 cases and identification of a novel insertion mutation
    • DOI 10.1002/ana.410420518
    • Jackson M, Al-Chalabi A, Enayat ZE, Chioza B, Leigh PN, Morrison KE. Copper/zinc superoxide dismutase 1 and sporadic amyotrophic lateral sclerosis: analysis of 155 cases and identification of a novel insertion mutation. Ann Neurol 42:803-807, 1997. (Pubitemid 27481554)
    • (1997) Annals of Neurology , vol.42 , Issue.5 , pp. 803-807
    • Jackson, M.1    Al-Chalabi, A.2    Enayat, Z.E.3    Chioza, B.4    Leigh, P.N.5    Morrison, K.E.6
  • 125
    • 16944364061 scopus 로고    scopus 로고
    • A novel missense point mutation (S134N) of the Cu/Zn superoxide dismutase gene in a patient with familal motor neuron disease
    • DOI 10.1002/(SICI)1098-1004(1997)9:1<69::AID-HUMU14>3.0.CO;2-N
    • Watanabe M, Aoki M, Abe K, Shoji M, Iizuka T, Ikeda Y, Hirai S, Kurokawa K, Kato T, Sasaki H, Itoyama Y. A novel missense point mutation (S134N) of the Cu/Zn superoxide dismutase gene in a patient with familial motor neuron disease. Hum Mutat 9:69-71, 1997. (Pubitemid 27024037)
    • (1997) Human Mutation , vol.9 , Issue.1 , pp. 69-71
    • Watanabe, M.1    Aoki, M.2    Abe, K.3    Shoji, M.4    Iizuka, T.5    Ikeda, Y.6    Hirai, S.7    Kurokawa, K.8    Kato, T.9    Sasaki, H.10    Itoyama, Y.11
  • 126
    • 1642569552 scopus 로고    scopus 로고
    • A novel exon 5 mutation (N139H) in the SOD1 gene in a Spanish family associated with incomplete penetrance
    • DOI 10.1016/j.jns.2003.10.018, PII S0022510X03003319
    • Nogales-Gadea G, Garcia-Arumi E, Andreu AL, Cervera C, Gamez J. A novel exon 5 mutation (N139H) in the SOD1 gene in a Spanish family associated with incomplete penetrance. J Neurol Sci 219:1-6, 2004. (Pubitemid 38405990)
    • (2004) Journal of the Neurological Sciences , vol.219 , Issue.1-2 , pp. 1-6
    • Nogales-Gadea, G.1    Garcia-Arumi, E.2    Andreu, A.L.3    Cervera, C.4    Gamez, J.5
  • 131
    • 0029005002 scopus 로고
    • Variance of age at onset in a Japanese family with amyotrophic lateral sclerosis associated with a novel Cu/Zn superoxide dismutase mutation
    • Aoki M, Abe K, Houi K, Ogasawara M, Matsubara Y, Kobayashi T. Variance of age at onset in a Japanese family with amyotrophic lateral sclerosis associated with a novel Cu/Zn superoxide dismutase mutation. Ann Neurol 37:676-679, 1995.
    • (1995) Ann Neurol , vol.37 , pp. 676-679
    • Aoki, M.1    Abe, K.2    Houi, K.3    Ogasawara, M.4    Matsubara, Y.5    Kobayashi, T.6
  • 132
    • 34347354304 scopus 로고    scopus 로고
    • Novel SOD1 N86K mutation is associated with a severe phenotype in familial ALS
    • DOI 10.1002/mus.20756
    • Beck M, Sendtner M, Toyka KV. Novel SOD1 N86K mutation is associated with a severe phenotype in familial ALS. Muscle Nerve 36:111-114, 2007. (Pubitemid 47016170)
    • (2007) Muscle and Nerve , vol.36 , Issue.1 , pp. 111-114
    • Beck, M.1    Sendtner, M.2    Toyka, K.V.3
  • 133
    • 0031960868 scopus 로고    scopus 로고
    • Homozygosity for Asn86Ser mutation in the CuZn-superoxide dismutase gene produces a severe clinical phenotype in a juvenile onset case of familial amyotrophic lateral sclerosis [1]
    • Hayward C, Brock DJ, Minns RA, Swingler RJ. Homozygosity for Asn86Ser mutation in the CuZn-superoxide dismutase gene produces a severe clinical phenotype in a juvenile onset case of familial amyotrophic lateral sclerosis. J Med Genet 35:174, 1998. (Pubitemid 28156526)
    • (1998) Journal of Medical Genetics , vol.35 , Issue.2 , pp. 174
    • Hayward, C.1    Brock, D.J.H.2    Minns, R.A.3    Swingler, R.J.4
  • 134
    • 0029977273 scopus 로고    scopus 로고
    • Superoxide dismutase 1: Identification of a novel mutation in a case of familial amyotrophic lateral sclerosis
    • DOI 10.1007/s004390050157
    • Kostrzewa M, Damian MS, Muller U. Superoxide dismutase 1: identification of a novel mutation in a case of familial amyotrophic lateral sclerosis. Hum Genet 98:48-50, 1996. (Pubitemid 26181280)
    • (1996) Human Genetics , vol.98 , Issue.1 , pp. 48-50
    • Kostrzewa, M.1    Damian, M.S.2    Muller, U.3
  • 137
    • 22044435425 scopus 로고    scopus 로고
    • Identification of three mutations in the Cu,Zn-superoxide dismutase (Cu,Zn-SOD) gene with familial amyotrophic lateral sclerosis: Transduction of human Cu,Zn-SOD into PC12 cells by HIV-1 TAT protein basic domain
    • Chou CM, Huang CJ, Shih CM, Chen YP, Liu TP, Chen CT. Identification of three mutations in the Cu,Zn-superoxide dismutase (Cu,Zn-SOD) gene with familial amyotrophic lateral sclerosis: transduction of human Cu,Zn-SOD into PC12 cells by HIV-1 TAT protein basic domain. Ann N Y Acad Sci 1042:303-313, 2005.
    • (2005) Ann N Y Acad Sci , vol.1042 , pp. 303-313
    • Chou, C.M.1    Huang, C.J.2    Shih, C.M.3    Chen, Y.P.4    Liu, T.P.5    Chen, C.T.6
  • 138
    • 0028123297 scopus 로고
    • Identification of a new missense point mutation in exon 4 of the Cu/Zn superoxide dismutase (SOD-1) gene in a family with amyotrophic lateral sclerosis
    • Elshafey A, Lanyon WG, Connor JM. Identification of a new missense point mutation in exon 4 of the Cu/Zn superoxide dismutase (SOD-1) gene in a family with amyotrophic lateral sclerosis. Hum Mol Genet 3:363-364, 1994. (Pubitemid 124000462)
    • (1994) Human Molecular Genetics , vol.3 , Issue.2 , pp. 363-364
    • Elshafey, A.1    Lanyon, W.G.2    Connor, J.M.3


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