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Volumn 72, Issue 7, 2013, Pages 646-661

Immunodetection of disease-associated conformers of mutant Cu/Zn superoxide dismutase 1 selectively expressed in degenerating neurons in amyotrophic lateral sclerosis

Author keywords

Amyotrophic lateral sclerosis; Conformational specific anti SOD1 antibody; Microglia; Motoneuron; Superoxide dismutase

Indexed keywords

AJ10 ANTIBODY; CELL PROTEIN; COPPER ZINC SUPEROXIDE DISMUTASE; ENHANCED GREEN FLUORESCENT PROTEIN; POLYCLONAL ANTIBODY; PURINERGIC P2X4 RECEPTOR; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 84879944791     PISSN: 00223069     EISSN: 15546578     Source Type: Journal    
DOI: 10.1097/NEN.0b013e318297fd10     Document Type: Article
Times cited : (19)

References (72)
  • 1
    • 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: 1047Y51
    • (1993) Science , vol.261
    • Deng, H.X.1    Hentati, A.2    Tainer, J.A.3
  • 4
    • 42249102078 scopus 로고    scopus 로고
    • Transgenics, toxicity and therapeutics in rodent models of mutant SOD1-mediated familial ALS
    • Turner BJ, Talbot K. Transgenics, toxicity and therapeutics in rodent models of mutant SOD1-mediated familial ALS. Prog Neurobiol 2008; 85:94-134
    • (2008) Prog Neurobiol , vol.85 , pp. 94-134
    • Turner, B.J.1    Talbot, K.2
  • 5
    • 0035516124 scopus 로고    scopus 로고
    • From Charcot to Lou Gehrig: Deciphering selective motor neuron death in ALS
    • DOI 10.1038/35097565
    • Cleveland DW, Rothstein JD. From Charcot to Lou Gehrig: Deciphering selective motor neuron death in ALS. Nat Rev Neurosci 2001;2:806-19 (Pubitemid 33674062)
    • (2001) Nature Reviews Neuroscience , vol.2 , Issue.11 , pp. 806-819
    • Cleveland, D.W.1    Rothstein, J.D.2
  • 6
    • 33846678063 scopus 로고    scopus 로고
    • How do ALS-associated mutations in superoxide dismutase 1 promote aggregation of the protein?
    • DOI 10.1016/j.tibs.2006.12.005, PII S0968000406003331
    • Shaw BF, Valentine JS. How do ALS-associated mutations in superoxide dismutase 1 promote aggregation of the protein? Trends Biochem Sci 2007;32:78-85 (Pubitemid 46199198)
    • (2007) Trends in Biochemical Sciences , vol.32 , Issue.2 , pp. 78-85
    • Shaw, B.F.1    Valentine, J.S.2
  • 8
    • 77954757268 scopus 로고    scopus 로고
    • Exposure of hydrophobic surfaces initiates aggregation of diverse ALS-causing superoxide dismutase-1 mutants
    • Munch C, Bertolotti A. Exposure of hydrophobic surfaces initiates aggregation of diverse ALS-causing superoxide dismutase-1 mutants. J Mol Biol 2010;399:512-25
    • (2010) J Mol Biol , vol.399 , pp. 512-525
    • Munch, C.1    Bertolotti, A.2
  • 9
    • 68749083546 scopus 로고    scopus 로고
    • Variation in aggregation propensities among ALS-associated variants of SOD1: Correlation to human disease
    • Prudencio M, Hart PJ, Borchelt D, et al. Variation in aggregation propensities among ALS-associated variants of SOD1: Correlation to human disease. Hum Mol Genet 2009;18:3217-26
    • (2009) Hum Mol Genet , vol.18 , pp. 3217-3226
    • Prudencio, M.1    Hart, P.J.2    Borchelt, D.3
  • 11
    • 0015935503 scopus 로고
    • On the stability of bovine superoxide dismutase. The effects of metals
    • Forman HJ, Fridovich I. On the stability of bovine superoxide dismutase. The effects of metals. J Biol Chem 1973;248:2645-49
    • (1973) J Biol Chem , vol.248 , pp. 2645-2649
    • Forman, H.J.1    Fridovich, I.2
  • 12
    • 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, et al. Superoxide dismutase is an abundant component in cell bodies, dendrites, and axons of motor neurons and in a subset of other neurons. Proc Natl Acad Sci USA 1995;92:954-58
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 954-958
    • Pardo, C.A.1    Xu, Z.2    Borchelt, D.R.3
  • 13
    • 0015694842 scopus 로고
    • Mitochondrial superoxide dismutase. Site of synthesis and intramitochondrial localization
    • Weisiger RA, Fridovich I. Mitochondrial superoxide dismutase. Site of synthesis and intramitochondrial localization. J Biol Chem 1973;248: 4793Y96
    • (1973) J Biol Chem , vol.248
    • Weisiger, R.A.1    Fridovich, I.2
  • 15
    • 77955352066 scopus 로고    scopus 로고
    • Novel antibodies reveal inclusions containing non-native SOD1 in sporadic ALS patients
    • Forsberg K, Jonsson PA, Andersen PM, et al. Novel antibodies reveal inclusions containing non-native SOD1 in sporadic ALS patients. PLoS One 2010;5(7):e11552
    • (2010) PLoS One , vol.5 , Issue.7
    • Forsberg, K.1    Jonsson, P.A.2    Andersen, P.M.3
  • 16
    • 77953028624 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis is a non-amyloid disease in which extensive misfolding of SOD1 is unique to the familial form
    • Kerman A, Liu HN, Croul S, et al. Amyotrophic lateral sclerosis is a non-amyloid disease in which extensive misfolding of SOD1 is unique to the familial form. Acta Neuropathol 2010;119:335-44
    • (2010) Acta Neuropathol , vol.119 , pp. 335-344
    • Kerman, A.1    Liu, H.N.2    Croul, S.3
  • 19
    • 37349068139 scopus 로고    scopus 로고
    • 4 purinergic receptor-like immunoreactivity is selectively associated with degenerating neurons in transgenic rodent models of amyotrophic lateral sclerosis
    • DOI 10.1002/cne.21527
    • Casanovas A, Hernandez S, Tarabal O, et al. Strong P2X4 purinergic receptorYlike immunoreactivity is selectively associated with degenerating neurons in transgenic rodent models of amyotrophic lateral sclerosis. J Comp Neurol 2008;506:75-92 (Pubitemid 350293491)
    • (2008) Journal of Comparative Neurology , vol.506 , Issue.1 , pp. 75-92
    • Casanovas, A.1    Hernandez, S.2    Tarabal, O.3    Rossello, J.4    Esquerda, J.E.5
  • 20
    • 75949096699 scopus 로고    scopus 로고
    • Neurotoxic species of misfolded SOD1G93A recognized by antibodies against the P2X4 subunit of the ATP receptor accumulate in damaged neurons of transgenic animal models of amyotrophic lateral sclerosis
    • Herna?ndez S, Casanovas A, Piedrafita L, et al. Neurotoxic species of misfolded SOD1G93A recognized by antibodies against the P2X4 subunit of the ATP receptor accumulate in damaged neurons of transgenic animal models of amyotrophic lateral sclerosis. J Neuropathol Exp Neurol 2010;69:176-87
    • (2010) J Neuropathol Exp Neurol , vol.69 , pp. 176-187
    • Hernandez, S.1    Casanovas, A.2    Piedrafita, L.3
  • 22
    • 0033169068 scopus 로고    scopus 로고
    • Differential distribution of intracellular glutamate receptors in dendrites
    • Rubio ME, Wenthold RJ. Differential distribution of intracellular glutamate receptors in dendrites. J Neurosci 1999;19:5549-62 (Pubitemid 29300218)
    • (1999) Journal of Neuroscience , vol.19 , Issue.13 , pp. 5549-5562
    • Rubio, M.E.1    Wenthold, R.J.2
  • 23
    • 23844445670 scopus 로고    scopus 로고
    • Immunocytochemistry on ultrathin cryosections
    • Spector DL, Goldman RD, Leonwand LA, eds Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Tokuyasu KT. Immunocytochemistry on ultrathin cryosections. In: Spector DL, Goldman RD, Leonwand LA, eds. Cells: A Laboratory Manual. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press, 1997:1311Y27
    • (1997) Cells: A Laboratory Manual
    • Tokuyasu, K.T.1
  • 24
    • 38449099776 scopus 로고    scopus 로고
    • Cryosectioning and immunolabeling
    • Slot JW, Geuze HJ. Cryosectioning and immunolabeling. Nat Protoc 2007;2:2480-91
    • (2007) Nat Protoc , vol.2 , pp. 2480-2491
    • Slot, J.W.1    Geuze, H.J.2
  • 25
    • 80052303432 scopus 로고    scopus 로고
    • A comprehensive assessment of the SOD1G93A low-copy transgenic mouse, which models human amyotrophic lateral sclerosis
    • Acevedo-Arozena A, Kalmar B, Essa S, et al. A comprehensive assessment of the SOD1G93A low-copy transgenic mouse, which models human amyotrophic lateral sclerosis. Dis Model Mech 2011;4: 686Y700
    • (2011) Dis Model Mech , vol.4
    • Acevedo-Arozena, A.1    Kalmar, B.2    Essa, S.3
  • 26
    • 79958135335 scopus 로고    scopus 로고
    • Glial nuclear aggregates of superoxide dismutase-1 are regularly present in patients with amyotrophic lateral sclerosis
    • Forsberg K, Andersen PM, Marklund SL, et al. Glial nuclear aggregates of superoxide dismutase-1 are regularly present in patients with amyotrophic lateral sclerosis. Acta Neuropathol 2011;121:623-34
    • (2011) Acta Neuropathol , vol.121 , pp. 623-634
    • Forsberg, K.1    Andersen, P.M.2    Marklund, S.L.3
  • 28
    • 0034662807 scopus 로고    scopus 로고
    • Aggregates of mutant protein appear progressively in dendrites, in periaxonal processes of oligodendrocytes, and in neuronal and astrocytic perikarya of mice expressing the SOD1(G93A) mutation of familial amyotrophic lateral sclerosis
    • Stieber A, Gonatas JO, Gonatas NK. Aggregates of mutant protein appear progressively in dendrites, in periaxonal processes of oligodendrocytes, and in neuronal and astrocytic perikarya of mice expressing the SOD1(G93A) mutation of familial amyotrophic lateral sclerosis. J Neurol Sci 2000;177:114-23
    • (2000) J Neurol Sci , vol.177 , pp. 114-123
    • Stieber, A.1    Gonatas, J.O.2    Gonatas, N.K.3
  • 29
    • 73949128974 scopus 로고    scopus 로고
    • Activation of innate and humoral immunity in the peripheral nervous system of ALS transgenic mice
    • Chiu IM, Phatnani H, Kuligowski M, et al. Activation of innate and humoral immunity in the peripheral nervous system of ALS transgenic mice. Proc Natl Acad Sci USA 2009;106:20960-65
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 20960-20965
    • Chiu, I.M.1    Phatnani, H.2    Kuligowski, M.3
  • 30
    • 29444443348 scopus 로고    scopus 로고
    • Chromogranin-mediated secretion of mutant superoxide dismutase proteins linked to amyotrophic lateral sclerosis
    • DOI 10.1038/nn1603
    • Urushitani M, Sik A, Sakurai T, et al. Chromogranin-mediated secretion of mutant superoxide dismutase proteins linked to amyotrophic lateral sclerosis. Nat Neurosci 2006;9:108-18 (Pubitemid 43011916)
    • (2006) Nature Neuroscience , vol.9 , Issue.1 , pp. 108-118
    • Urushitani, M.1    Sik, A.2    Sakurai, T.3    Nukina, N.4    Takahashi, R.5    Julien, J.-P.6
  • 31
    • 84862854446 scopus 로고    scopus 로고
    • Targeting of monomer/misfolded SOD1 as a therapeutic strategy for amyotrophic lateral sclerosis
    • Liu HN, Tjostheim S, Dasilva K, et al. Targeting of monomer/misfolded SOD1 as a therapeutic strategy for amyotrophic lateral sclerosis. J Neurosci 2012;32:8791-99
    • (2012) J Neurosci , vol.32 , pp. 8791-8799
    • Liu, H.N.1    Tjostheim, S.2    Dasilva, K.3
  • 32
    • 73049098692 scopus 로고    scopus 로고
    • A systematic study of brainstem motor nuclei in a mouse model of ALS, the effects of lithium
    • Ferrucci M, Spalloni A, Bartalucci A, et al. A systematic study of brainstem motor nuclei in a mouse model of ALS, the effects of lithium. Neurobiol Dis 2010;37:370-83
    • (2010) Neurobiol Dis , vol.37 , pp. 370-383
    • Ferrucci, M.1    Spalloni, A.2    Bartalucci, A.3
  • 34
    • 0023829664 scopus 로고
    • Ultrastructural study of chromatolytic neurons in an adult-onset sporadic case of amyotrophic lateral sclerosis
    • Kusaka H, Imai T, Hashimoto S, et al. Ultrastructural study of chromatolytic neurons in an adult-onset sporadic case of amyotrophic lateral sclerosis. Acta Neuropathol 1988;75:523-28 (Pubitemid 18075433)
    • (1988) Acta Neuropathologica , vol.75 , Issue.5 , pp. 523-528
    • Kusaka, H.1    Imai, T.2    Hashimoto, S.3    Yamamoto, T.4    Maya, K.5    Yamasaki, M.6
  • 35
    • 79952754297 scopus 로고    scopus 로고
    • Corticospinal motor neurons and related subcerebral projection neurons undergo early and specific neurodegeneration in hSOD1G93A transgenic ALS mice
    • Ozdinler PH, Benn S, Yamamoto TH, et al. Corticospinal motor neurons and related subcerebral projection neurons undergo early and specific neurodegeneration in hSOD1G93A transgenic ALS mice. J Neurosci 2011;31:4166-77
    • (2011) J Neurosci , vol.31 , pp. 4166-4177
    • Ozdinler, P.H.1    Benn, S.2    Yamamoto, T.H.3
  • 36
    • 57749100302 scopus 로고    scopus 로고
    • Initiation and elongation in fibrillation of ALS-linked superoxide dismutase
    • Chattopadhyay M, Durazo A, Sohn SH, et al. Initiation and elongation in fibrillation of ALS-linked superoxide dismutase. Proc Natl Acad Sci USA 2008;105:18663-68
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 18663-18668
    • Chattopadhyay, M.1    Durazo, A.2    Sohn, S.H.3
  • 37
    • 84868142104 scopus 로고    scopus 로고
    • Fibrillation precursor of superoxide dismutase 1 revealed by gradual tuning of the protein-folding equilibrium
    • Lang L, Kurnik M, Danielsson J, et al. Fibrillation precursor of superoxide dismutase 1 revealed by gradual tuning of the protein-folding equilibrium. Proc Natl Acad Sci USA 2012;109:17868-73
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 17868-17873
    • Lang, L.1    Kurnik, M.2    Danielsson, J.3
  • 38
    • 77955649302 scopus 로고    scopus 로고
    • Mutant superoxide dismutase 1Yinduced IL-1beta accelerates ALS pathogenesis
    • Meissner F, Molawi K, Zychlinsky A. Mutant superoxide dismutase 1Yinduced IL-1beta accelerates ALS pathogenesis. Proc Natl Acad Sci USA 2010;107:13046-50
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 13046-13050
    • Meissner, F.1    Molawi, K.2    Zychlinsky, A.3
  • 39
    • 0036076642 scopus 로고    scopus 로고
    • Fibrillar inclusions and motor neuron degeneration in transgenic mice expressing superoxide dismutase 1 with a disrupted copper-binding site
    • Wang J, Xu G, Gonzales V, et al. Fibrillar inclusions and motor neuron degeneration in transgenic mice expressing superoxide dismutase 1 with a disrupted copper-binding site. Neurobiol Dis 2002;10: 128Y38
    • (2002) Neurobiol Dis , vol.10
    • Wang, J.1    Xu, G.2    Gonzales, V.3
  • 42
    • 84859454704 scopus 로고    scopus 로고
    • An overoxidized form of superoxide dismutase found in sporadic amyotrophic lateral sclerosis with bulbar onset shares a toxic mechanism with mutant SOD1
    • Guareschi S, Cova E, Cereda C, et al. An overoxidized form of superoxide dismutase found in sporadic amyotrophic lateral sclerosis with bulbar onset shares a toxic mechanism with mutant SOD1. Proc Natl Acad Sci USA 2012;109:5074-79
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 5074-5079
    • Guareschi, S.1    Cova, E.2    Cereda, C.3
  • 43
    • 77958519939 scopus 로고    scopus 로고
    • Wild-type and mutant SOD1 share an aberrant conformation and a common pathogenic pathway in ALS
    • Bosco DA, Morfini G, Karabacak NM, et al. Wild-type and mutant SOD1 share an aberrant conformation and a common pathogenic pathway in ALS. Nat Neurosci 2010;13:1396-403
    • (2010) Nat Neurosci , vol.13 , pp. 1396-1403
    • Bosco, D.A.1    Morfini, G.2    Karabacak, N.M.3
  • 44
    • 84859452121 scopus 로고    scopus 로고
    • Localization of a toxic form of superoxide dismutase 1 protein to pathologically affected tissues in familial ALS
    • Brotherton TE, Li Y, Cooper D, et al. Localization of a toxic form of superoxide dismutase 1 protein to pathologically affected tissues in familial ALS. Proc Natl Acad Sci USA 2012;109:5505-10
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 5505-5510
    • Brotherton, T.E.1    Li, Y.2    Cooper, D.3
  • 45
    • 69249121554 scopus 로고    scopus 로고
    • Lack of evidence of monomer/misfolded superoxide dismutase-1 in sporadic amyotrophic lateral sclerosis
    • Liu HN, Sanelli T, Horne P, et al. Lack of evidence of monomer/misfolded superoxide dismutase-1 in sporadic amyotrophic lateral sclerosis. Ann Neurol 2009;66:75-80
    • (2009) Ann Neurol , vol.66 , pp. 75-80
    • Liu, H.N.1    Sanelli, T.2    Horne, P.3
  • 46
    • 0031723557 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis associated with genetic abnormalities in the gene encoding Cu/Zn superoxide dismutase: Molecular pathology of five new cases, and comparison with previous reports and 73 sporadic cases of ALS
    • Ince PG, Tomkins J, Slade JY, et al. Amyotrophic lateral sclerosis associated with genetic abnormalities in the gene encoding Cu/Zn superoxide dismutase: Molecular pathology of five new cases, and comparison with previous reports and 73 sporadic cases of ALS. J Neuropathol Exp Neurol 1998;57:895-904 (Pubitemid 28478000)
    • (1998) Journal of Neuropathology and Experimental Neurology , vol.57 , Issue.10 , pp. 895-904
    • Ince, P.G.1    Tomkins, J.2    Slade, J.Y.3    Thatcher, N.M.4    Shaw, P.J.5
  • 48
    • 3943102116 scopus 로고    scopus 로고
    • Unraveling the mechanisms involved in motor neuron degeneration in ALS
    • DOI 10.1146/annurev.neuro.27.070203.144244
    • Bruijn LI, Miller TM, Cleveland DW. Unraveling the mechanisms involved in motor neuron degeneration in ALS. Annu Rev Neurosci 2004; 27:723-49 (Pubitemid 39050419)
    • (2004) Annual Review of Neuroscience , vol.27 , pp. 723-749
    • Bruijn, L.I.1    Miller, T.M.2    Cleveland, D.W.3
  • 49
    • 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 2006;10:131-38
    • (2006) Curr Opin Chem Biol , vol.10 , pp. 131-138
    • Hart, P.J.1
  • 50
    • 74049164709 scopus 로고    scopus 로고
    • Non-cell autonomous toxicity in neurodegenerative disorders: ALS and beyond
    • Ilieva H, PolymenidouM, Cleveland DW. Non-cell autonomous toxicity in neurodegenerative disorders: ALS and beyond. J Cell Biol 2009;187: 761Y72
    • (2009) J Cell Biol , vol.187
    • Ilieva, H.1    Polymenidoum Cleveland, D.W.2
  • 51
    • 84861596118 scopus 로고    scopus 로고
    • Misfolded SOD1 and ALS: Zeroing in on mitochondria
    • Pickles S, Vande Velde C. Misfolded SOD1 and ALS: Zeroing in on mitochondria. Amyotroph Lateral Scler 2012;13:333-40
    • (2012) Amyotroph Lateral Scler , vol.13 , pp. 333-340
    • Pickles, S.1    Vande Velde, C.2
  • 52
    • 77955961922 scopus 로고    scopus 로고
    • Misfolded mutant SOD1 directly inhibits VDAC1 conductance in a mouse model of inherited ALS
    • Israelson A, Arbel N, Da Cruz S, et al. Misfolded mutant SOD1 directly inhibits VDAC1 conductance in a mouse model of inherited ALS. Neuron 2010;67:575-87
    • (2010) Neuron , vol.67 , pp. 575-587
    • Israelson, A.1    Arbel, N.2    Da Cruz, S.3
  • 54
    • 0032125587 scopus 로고    scopus 로고
    • Relationship of microglial and astrocytic activation to disease onset and progression in a transgenic model of familial ALS
    • DOI 10.1002/(SICI)1098-1136(199807)23:3 <249::AID-GLIA7>3.0.CO;2-#
    • Hall ED, Oostveen JA, Gurney ME. Relationship of microglial and astrocytic activation to disease onset and progression in a transgenic model of familial ALS. Glia 1998;23:249-56 (Pubitemid 28259722)
    • (1998) GLIA , vol.23 , Issue.3 , pp. 249-256
    • Hall, E.D.1    Oostveen, J.A.2    Gurney, M.E.3
  • 55
    • 0036787810 scopus 로고    scopus 로고
    • Inflammatory processes in amyotrophic lateral sclerosis
    • McGeer PL, McGeer EG. Inflammatory processes in amyotrophic lateral sclerosis. Muscle Nerve 2002;26:459-70
    • (2002) Muscle Nerve , vol.26 , pp. 459-470
    • McGeer, P.L.1    McGeer, E.G.2
  • 56
    • 37249011467 scopus 로고    scopus 로고
    • MyD88-deficient bone marrow cells accelerate onset and reduce survival in a mouse model of amyotrophic lateral sclerosis
    • DOI 10.1083/jcb.200705046
    • Kang J, Rivest S. MyD88-deficient bone marrow cells accelerate onset and reduce survival in a mouse model of amyotrophic lateral sclerosis. J Cell Biol 2007;179:1219-30 (Pubitemid 350277740)
    • (2007) Journal of Cell Biology , vol.179 , Issue.6 , pp. 1219-1230
    • Kang, J.1    Rivest, S.2
  • 57
    • 73149105494 scopus 로고    scopus 로고
    • Extracellular mutant SOD1 induces microglial-mediated motoneuron injury
    • Zhao W, Beers DR, Henkel JS, et al. Extracellular mutant SOD1 induces microglial-mediated motoneuron injury. Glia 2010;58:231-43
    • (2010) Glia , vol.58 , pp. 231-243
    • Zhao, W.1    Beers, D.R.2    Henkel, J.S.3
  • 58
    • 56649100689 scopus 로고    scopus 로고
    • T lymphocytes potentiate endogenous neuroprotective inflammation in a mouse model of ALS
    • Chiu IM, Chen A, Zheng Y, et al. T lymphocytes potentiate endogenous neuroprotective inflammation in a mouse model of ALS. Proc Natl Acad Sci USA 2008;105:17913-18
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 17913-17918
    • Chiu, I.M.1    Chen, A.2    Zheng, Y.3
  • 61
    • 0027946294 scopus 로고
    • Development of central nervous system pathology in a murine transgenic model of human amyotrophic lateral sclerosis
    • Dal Canto MC, Gurney ME. Development of central nervous system pathology in a murine transgenic model of human amyotrophic lateral sclerosis. Am J Pathol 1994;145:1271-79 (Pubitemid 24378480)
    • (1994) American Journal of Pathology , vol.145 , Issue.6 , pp. 1271-1279
    • Dal Canto, M.C.1    Gurney, M.E.2
  • 62
    • 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. Neurosci 1998;18:3241-50 (Pubitemid 28186017)
    • (1998) Journal of Neuroscience , vol.18 , Issue.9 , pp. 3241-3250
    • Kong, J.1    Xu, Z.2
  • 63
    • 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, et al. An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria. Neuron 1995;14: 1105Y16
    • (1995) Neuron , vol.14
    • Wong, P.C.1    Pardo, C.A.2    Borchelt, D.R.3
  • 65
    • 77955934441 scopus 로고    scopus 로고
    • ALS-linked mutant SOD1 damages mitochondria by promoting conformational changes in Bcl-2
    • Pedrini S, Sau D, Guareschi S, et al. ALS-linked mutant SOD1 damages mitochondria by promoting conformational changes in Bcl-2. Hum Mol Genet 2010;19:2974-86
    • (2010) Hum Mol Genet , vol.19 , pp. 2974-2986
    • Pedrini, S.1    Sau, D.2    Guareschi, S.3
  • 66
    • 0035886428 scopus 로고    scopus 로고
    • Early vacuolization and mitochondrial damage in motor neurons of FALS mice are not associated with apoptosis or with changes in cytochrome oxidase histochemical reactivity
    • DOI 10.1016/S0022-510X(01)00627-X, PII S0022510X0100627X
    • Bendotti C, Calvaresi N, Chiveri L, et al. Early vacuolization and mitochondrial damage in motor neurons of FALS mice are not associated with apoptosis or with changes in cytochrome oxidase histochemical reactivity. J Neurol Sci 2001;191:25-33 (Pubitemid 33035892)
    • (2001) Journal of the Neurological Sciences , vol.191 , Issue.1-2 , pp. 25-33
    • Bendotti, C.1    Calvaresi, N.2    Chiveri, L.3    Prelle, A.4    Moggio, M.5    Braga, M.6    Silani, V.7    De Biasi, S.8
  • 67
    • 0037088793 scopus 로고    scopus 로고
    • Mutant Cu, Zn superoxide dismutase that causes motoneuron degeneration is present in mitochondria in the CNS
    • Higgins CM, Jung C, Ding H, et al. Mutant Cu, Zn superoxide dismutase that causes motoneuron degeneration is present in mitochondria in the CNS. J Neurosci 2002;22:RC215
    • (2002) J Neurosci , vol.22
    • Higgins, C.M.1    Jung, C.2    Ding, H.3
  • 68
    • 0034821922 scopus 로고    scopus 로고
    • CuZn superoxide dismutase (SOD1) accumulates in vacuolated mitochondria in transgenic mice expressing amyotrophic lateral sclerosis-linked SOD1 mutations
    • Jaarsma D, Rognoni F, van Duijn W, et al. CuZn superoxide dismutase (SOD1) accumulates in vacuolated mitochondria in transgenic mice expressing amyotrophic lateral sclerosis-linked SOD1 mutations. Acta Neuropathol 2001;102:293-305 (Pubitemid 32894698)
    • (2001) Acta Neuropathologica , vol.102 , Issue.4 , pp. 293-305
    • Jaarsma, D.1    Rognoni, F.2    Van Duijn, W.3    Verspaget, H.W.4    Haasdijk, E.D.5    Holstege, J.C.6
  • 69
    • 33645798615 scopus 로고    scopus 로고
    • Spinal cord endoplasmic reticulum stress associated with a microsomal accumulation of mutant superoxide dismutase-1 in an ALS model
    • Kikuchi H, Almer G, Yamashita S, et al. Spinal cord endoplasmic reticulum stress associated with a microsomal accumulation of mutant superoxide dismutase-1 in an ALS model. Proc Natl Acad Sci USA 2006; 103:6025-30
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 6025-6030
    • Kikuchi, H.1    Almer, G.2    Yamashita, S.3
  • 70
    • 46749107070 scopus 로고    scopus 로고
    • The endoplasmic reticulum-Golgi pathway is a target for translocation and aggregation of mutant superoxide dismutase linked to ALS
    • DOI 10.1096/fj.07-092783
    • Urushitani M, Ezzi SA, Matsuo A, et al. The endoplasmic reticulum-Golgi pathway is a target for translocation and aggregation of mutant superoxide dismutase linked to ALS. FASEB J 2008;22:2476-87 (Pubitemid 351948665)
    • (2008) FASEB Journal , vol.22 , Issue.7 , pp. 2476-2487
    • Urushitani, M.1    Ezzi, S.A.2    Matsuo, A.3    Tooyama, I.4    Julien, J.-P.5
  • 71
    • 80155157847 scopus 로고    scopus 로고
    • The seeds of neurodegeneration: Prion-like spreading in ALS
    • Polymenidou M, Cleveland DW. The seeds of neurodegeneration: Prion-like spreading in ALS. Cell 2011;147:498-508
    • (2011) Cell , vol.147 , pp. 498-508
    • Polymenidou, M.1    Cleveland, D.W.2
  • 72
    • 77957946030 scopus 로고    scopus 로고
    • Induction of protective immunity by vaccination with wild-type apo superoxide dismutase 1 in mutant SOD1 transgenic mice
    • Takeuchi S, Fujiwara N, Ido A, et al. Induction of protective immunity by vaccination with wild-type apo superoxide dismutase 1 in mutant SOD1 transgenic mice. J Neuropathol Exp Neurol 2010;69:1044-56
    • (2010) J Neuropathol Exp Neurol , vol.69 , pp. 1044-1056
    • Takeuchi, S.1    Fujiwara, N.2    Ido, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.