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Volumn 95, Issue 3, 1997, Pages 167-172

Absence of the mutant SOD1 in familial amyotrophic lateral sclerosis (FALS) with two base pair deletion in the SOD1 gene

Author keywords

activity staining; diethyl dithiocarbamate (DDC); familial amyotrophic lateral sclerosis (FALS); single strand conformational polymorphism (SSCP); western blot analysis

Indexed keywords

COPPER; MESSENGER RNA; SUPEROXIDE DISMUTASE;

EID: 0030941967     PISSN: 00016314     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1600-0404.1997.tb00090.x     Document Type: Article
Times cited : (15)

References (25)
  • 1
    • 0027401203 scopus 로고
    • Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis
    • ROSEN DR, SIDDIQUE T, PATTERSON D et al. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 1993: 362: 59-62.
    • (1993) Nature , vol.362 , pp. 59-62
    • Rosen, D.R.1    Siddique, T.2    Patterson, D.3
  • 2
    • 0027426169 scopus 로고
    • Amyotrophic lateral sclerosis and structural defects in Cu, Zn superoxide dismutase
    • DENG HX, HENTATI A, TAINER JA et al. Amyotrophic lateral sclerosis and structural defects in Cu, Zn superoxide dismutase. Science 1993: 261: 1047-51.
    • (1993) Science , vol.261 , pp. 1047-1051
    • Deng, H.X.1    Hentati, A.2    Tainer, J.A.3
  • 3
    • 0027952571 scopus 로고
    • Cu/Zn superoxide dismutase activity in familial and sporadic amyotrophic lateral sclerosis
    • ROBBERECHT W, SAPP P, VIAENE MK et al. Cu/Zn superoxide dismutase activity in familial and sporadic amyotrophic lateral sclerosis. J Neurochem 1994: 62: 384-7.
    • (1994) J Neurochem , vol.62 , pp. 384-387
    • Robberecht, W.1    Sapp, P.2    Viaene, M.K.3
  • 4
    • 0028067985 scopus 로고
    • A two basepair deletion in the SOD1 gene causes familial amyotrophic lateral sclerosis
    • PRAMATAROVA A, GOTO J, NANBA E et al. A two basepair deletion in the SOD1 gene causes familial amyotrophic lateral sclerosis. Hum Mol Genet 1994: 3: 2061-2.
    • (1994) Hum Mol Genet , vol.3 , pp. 2061-2062
    • Pramatarova, A.1    Goto, J.2    Nanba, E.3
  • 6
    • 0028960506 scopus 로고
    • Amyotrophic lateral sclerosis: Recent insights from genetics and transgenic mice
    • BROWN RH JR. Amyotrophic lateral sclerosis: recent insights from genetics and transgenic mice. Cell 1995: 80: 687-92.
    • (1995) Cell , vol.80 , pp. 687-692
    • Brown Jr., R.H.1
  • 7
    • 0028813380 scopus 로고
    • Superoxide dismutase 1 subunits with mutations linked to familial amyotrophic lateral sclerosis do not affect wild-type subunit function
    • BORCHELT DR, GUARNIERI M, WONG PC et al. Superoxide dismutase 1 subunits with mutations linked to familial amyotrophic lateral sclerosis do not affect wild-type subunit function. J Biol Chem 1995: 270: 3234-8.
    • (1995) J Biol Chem , vol.270 , pp. 3234-3238
    • Borchelt, D.R.1    Guarnieri, M.2    Wong, P.C.3
  • 8
    • 0028933344 scopus 로고
    • Neuropathological changes in two lines of mice carrying a transgene for mutant human Cu, Zn SOD. and in mice overexpressing wild type human SOD: A model of familial amyotrophic lateral sclerosis (FALS)
    • DAL CANTO MC, GURNEY ME. Neuropathological changes in two lines of mice carrying a transgene for mutant human Cu, Zn SOD. and in mice overexpressing wild type human SOD: a model of familial amyotrophic lateral sclerosis (FALS). Brain Res 1995: 676: 25-40.
    • (1995) Brain Res , vol.676 , pp. 25-40
    • Dal Canto, M.C.1    Gurney, M.E.2
  • 9
    • 0028284779 scopus 로고
    • Motor neuron degeneration in mice that express a human Cu, Zn superoxide dismutase mutation
    • GURNEY ME, PU H, CHIU AY et al. Motor neuron degeneration in mice that express a human Cu, Zn superoxide dismutase mutation. Science 1994: 264: 1772-5.
    • (1994) Science , vol.264 , pp. 1772-1775
    • Gurney, M.E.1    Pu, H.2    Chiu, A.Y.3
  • 10
    • 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 USA 1995: 92: 689-93.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 689-693
    • Ripps, M.E.1    Huntley, G.W.2    Hof, P.R.3    Morrison, J.H.4    Gordon, J.W.5
  • 11
    • 0028221169 scopus 로고
    • Down-regulation of copper/ zinc superoxide dismutase causes apoptotic death in PC12 neuronal cells
    • TROY CM, SHELANSKI ML. Down-regulation of copper/ zinc superoxide dismutase causes apoptotic death in PC12 neuronal cells. Proc Natl Acad Sci USA 1994: 91: 6384-7.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 6384-6387
    • Troy, C.M.1    Shelanski, M.L.2
  • 13
    • 0029020394 scopus 로고
    • Abnormality of Cu/Zn superoxide dismutase (SOD1) activity in Japanese familial amyotrophic lateral sclerosis with two base pair deletion in the SOD1 gene
    • NAKASHIMA K, WATANABE Y, KUNO N, NANBA E, TAKAHASHI K. Abnormality of Cu/Zn superoxide dismutase (SOD1) activity in Japanese familial amyotrophic lateral sclerosis with two base pair deletion in the SOD1 gene. Neurology 1995: 45: 1019-20.
    • (1995) Neurology , vol.45 , pp. 1019-1020
    • Nakashima, K.1    Watanabe, Y.2    Kuno, N.3    Nanba, E.4    Takahashi, K.5
  • 14
    • 0015419721 scopus 로고
    • Hereditary amyotrophic lateral sclerosis: Histochemical and electron microscopic study of hyaline inclusions in motor neurons
    • TAKAHASHI K, NAKAMURA H, OKADA E. Hereditary amyotrophic lateral sclerosis: histochemical and electron microscopic study of hyaline inclusions in motor neurons. Arch Neurol 1972: 27: 292-9.
    • (1972) Arch Neurol , vol.27 , pp. 292-299
    • Takahashi, K.1    Nakamura, H.2    Okada, E.3
  • 15
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • BRADFORD MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976: 72: 248-54.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 16
    • 0015153416 scopus 로고
    • Superoxide dismutase: Improved assays and assay applicable to acrylamide gels
    • BEAUCHAMP C, FRIDOVICH I. Superoxide dismutase: improved assays and assay applicable to acrylamide gels. Anal Biochem 1971: 44: 276-87.
    • (1971) Anal Biochem , vol.44 , pp. 276-287
    • Beauchamp, C.1    Fridovich, I.2
  • 18
    • 0021921322 scopus 로고
    • Architecture and anatomy of the chromosomal locus in human chromosome 21 encoding the Cu/Zn superoxide dismutase
    • LEVANON D, LIEMAN-HURWITZ J, DAFNI N et al. Architecture and anatomy of the chromosomal locus in human chromosome 21 encoding the Cu/Zn superoxide dismutase. EMBO J 1985: 4: 77-84.
    • (1985) EMBO J , vol.4 , pp. 77-84
    • Levanon, D.1    Lieman-Hurwitz, J.2    Dafni, N.3
  • 19
    • 0029048164 scopus 로고
    • Characterization of mutants of the vitamin D-binding protein/group-specific component: Molecular evolution of GC*1A2 and GC*1A3, common in some Asian populations
    • YUASA I, KOFLER A, BRAUN A et al. Characterization of mutants of the vitamin D-binding protein/group-specific component: molecular evolution of GC*1A2 and GC*1A3, common in some Asian populations. Hum Genet 1995: 95: 507-12.
    • (1995) Hum Genet , vol.95 , pp. 507-512
    • Yuasa, I.1    Kofler, A.2    Braun, A.3
  • 20
    • 0029077167 scopus 로고
    • Alterations in superoxide dismutase and catalase in Fusarium oxysporum during starvation-induced differentiation
    • KONO Y, YAMAMOTO H, TAKEUCHI M, KOMADA H. Alterations in superoxide dismutase and catalase in Fusarium oxysporum during starvation-induced differentiation. Biochem Biophys Acta 1995: 1268: 35-40.
    • (1995) Biochem Biophys Acta , vol.1268 , pp. 35-40
    • Kono, Y.1    Yamamoto, H.2    Takeuchi, M.3    Komada, H.4
  • 21
    • 0028081018 scopus 로고
    • Intense oxidative DNA damage promoted by L-DOPA and its metabolites implications for neurodegenerative disease
    • SPENCER JPE, JENNER A, ARUOMA OI et al. Intense oxidative DNA damage promoted by L-DOPA and its metabolites implications for neurodegenerative disease. FEBS Lett 1994: 353: 246-50.
    • (1994) FEBS Lett , vol.353 , pp. 246-250
    • Spencer, J.P.E.1    Jenner, A.2    Aruoma, O.I.3
  • 22
    • 0017294656 scopus 로고
    • In vivo inhibition of superoxide dismutase in mice by diethyldithiocarbamate
    • HEIKKILA RE, CABBAT FS, COHEN G. In vivo inhibition of superoxide dismutase in mice by diethyldithiocarbamate. J Biol Chem 1976: 251: 2182-5.
    • (1976) J Biol Chem , vol.251 , pp. 2182-2185
    • Heikkila, R.E.1    Cabbat, F.S.2    Cohen, G.3
  • 23
    • 0026754574 scopus 로고
    • Reactive oxigen species and the central nervous system
    • HALLIWELL B. Reactive oxigen species and the central nervous system. J Neurochem 1992: 59: 1609-23.
    • (1992) J Neurochem , vol.59 , pp. 1609-1623
    • Halliwell, B.1
  • 24
    • 0028940012 scopus 로고
    • Strand scission in DNA induced by L-DOPA in the presence of Cu(II)
    • HAUSAIN S, HADI SM. Strand scission in DNA induced by L-DOPA in the presence of Cu(II). FEBS Lett 1995: 364: 75-8.
    • (1995) FEBS Lett , vol.364 , pp. 75-78
    • Hausain, S.1    Hadi, S.M.2
  • 25
    • 0021984002 scopus 로고
    • Superoxide dismutase isoenzymes in normal brains and in brains from patients with dementia of Alzheimer type
    • MARKUJND SL, ADOLFSSON R, GOTTFRIES CG, WINBLAD B. Superoxide dismutase isoenzymes in normal brains and in brains from patients with dementia of Alzheimer type. J Neurol Sci 1985: 67: 319-25.
    • (1985) J Neurol Sci , vol.67 , pp. 319-325
    • Markujnd, S.L.1    Adolfsson, R.2    Gottfries, C.G.3    Winblad, B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.