메뉴 건너뛰기




Volumn 134, Issue 1, 2017, Pages 97-111

Misfolded SOD1 is not a primary component of sporadic ALS

Author keywords

Amyotrophic lateral sclerosis (ALS); Human patients; Misfolding; Neurodegeneration; Neuropathology; Sporadic (SALS); Superoxide dismutase (SOD1)

Indexed keywords

ALANINE; COPPER ZINC SUPEROXIDE DISMUTASE; TISSUE EXTRACT; VALINE; SOD1 PROTEIN, HUMAN;

EID: 85014027713     PISSN: 00016322     EISSN: 14320533     Source Type: Journal    
DOI: 10.1007/s00401-017-1688-8     Document Type: Article
Times cited : (69)

References (73)
  • 1
    • 33750716074 scopus 로고    scopus 로고
    • TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • COI: 1:CAS:528:DC%2BD28Xht1SmsbbJ, PID: 17084815
    • Arai T, Hasegawa M, Akiyama H, Ikeda K, Nonaka T, Mori H, Mann D, Tsuchiya K, Yoshida M, Hashizume Y et al (2006) TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Biochem Biophys Res Commun 351:602–611
    • (2006) Biochem Biophys Res Commun , vol.351 , pp. 602-611
    • Arai, T.1    Hasegawa, M.2    Akiyama, H.3    Ikeda, K.4    Nonaka, T.5    Mori, H.6    Mann, D.7    Tsuchiya, K.8    Yoshida, M.9    Hashizume, Y.10
  • 2
    • 77955843240 scopus 로고    scopus 로고
    • Wild-type human SOD1 overexpression does not accelerate motor neuron disease in mice expressing murine Sod1 G86R
    • COI: 1:CAS:528:DC%2BC3cXhtVGrt73M, PID: 20573565
    • Audet JN, Gowing G, Julien JP (2010) Wild-type human SOD1 overexpression does not accelerate motor neuron disease in mice expressing murine Sod1 G86R. Neurobiol Dis 40:245–250. doi:10.1016/j.nbd.2010.05.031
    • (2010) Neurobiol Dis , vol.40 , pp. 245-250
    • Audet, J.N.1    Gowing, G.2    Julien, J.P.3
  • 3
    • 84921935837 scopus 로고    scopus 로고
    • Experimental transmissibility of mutant SOD1 motor neuron disease
    • COI: 1:CAS:528:DC%2BC2cXhs1KgtLzM, PID: 25262000
    • Ayers JI, Fromholt S, Koch M, DeBosier A, McMahon B, Xu G, Borchelt DR (2014) Experimental transmissibility of mutant SOD1 motor neuron disease. Acta Neuropathol 128:791–803. doi:10.1007/s00401-014-1342-7
    • (2014) Acta Neuropathol , vol.128 , pp. 791-803
    • Ayers, J.I.1    Fromholt, S.2    Koch, M.3    DeBosier, A.4    McMahon, B.5    Xu, G.6    Borchelt, D.R.7
  • 4
    • 84905978174 scopus 로고    scopus 로고
    • Conformational specificity of the C4F6 SOD1 antibody; low frequency of reactivity in sporadic ALS cases
    • PID: 24887207
    • Ayers JI, Xu G, Pletnikova O, Troncoso JC, Hart PJ, Borchelt DR (2014) Conformational specificity of the C4F6 SOD1 antibody; low frequency of reactivity in sporadic ALS cases. Acta Neuropathol Commun 2:55. doi:10.1186/2051-5960-2-55
    • (2014) Acta Neuropathol Commun , vol.2 , pp. 55
    • Ayers, J.I.1    Xu, G.2    Pletnikova, O.3    Troncoso, J.C.4    Hart, P.J.5    Borchelt, D.R.6
  • 5
    • 84878389217 scopus 로고    scopus 로고
    • Mutant copper-zinc superoxide dismutase (SOD1) induces protein secretion pathway alterations and exosome release in astrocytes: implications for disease spreading and motor neuron pathology in amyotrophic lateral sclerosis
    • COI: 1:CAS:528:DC%2BC3sXosFyltrs%3D, PID: 23592792
    • Basso M, Pozzi S, Tortarolo M, Fiordaliso F, Bisighini C, Pasetto L, Spaltro G, Lidonnici D, Gensano F, Battaglia E et al (2013) Mutant copper-zinc superoxide dismutase (SOD1) induces protein secretion pathway alterations and exosome release in astrocytes: implications for disease spreading and motor neuron pathology in amyotrophic lateral sclerosis. J Biol Chem 288:15699–15711. doi:10.1074/jbc.M112.425066
    • (2013) J Biol Chem , vol.288 , pp. 15699-15711
    • Basso, M.1    Pozzi, S.2    Tortarolo, M.3    Fiordaliso, F.4    Bisighini, C.5    Pasetto, L.6    Spaltro, G.7    Lidonnici, D.8    Gensano, F.9    Battaglia, E.10
  • 7
    • 84859452121 scopus 로고    scopus 로고
    • Localization of a toxic form of superoxide dismutase 1 protein to pathologically affected tissues in familial ALS
    • COI: 1:CAS:528:DC%2BC38XlslOjtro%3D, PID: 22431618
    • Brotherton TE, Li Y, Cooper D, Gearing M, Julien JP, Rothstein JD, Boylan K, Glass JD (2012) Localization of a toxic form of superoxide dismutase 1 protein to pathologically affected tissues in familial ALS. Proc Natl Acad Sci U S A 109:5505–5510. doi:10.1073/pnas.1115009109
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 5505-5510
    • Brotherton, T.E.1    Li, Y.2    Cooper, D.3    Gearing, M.4    Julien, J.P.5    Rothstein, J.D.6    Boylan, K.7    Glass, J.D.8
  • 10
    • 0032937953 scopus 로고    scopus 로고
    • Corpora-amylacea and the family of polyglucosan diseases
    • COI: 1:CAS:528:DyaK1MXisV2itbc%3D, PID: 10209236
    • Cavanagh JB (1999) Corpora-amylacea and the family of polyglucosan diseases. Brain Res Brain Res Rev 29:265–295
    • (1999) Brain Res Brain Res Rev , vol.29 , pp. 265-295
    • Cavanagh, J.B.1
  • 11
    • 84885410476 scopus 로고    scopus 로고
    • Altered intracellular localization of SOD1 in leukocytes from patients with sporadic amyotrophic lateral sclerosis
    • COI: 1:CAS:528:DC%2BC3sXhs1GjsrvN, PID: 24155874
    • Cereda C, Leoni E, Milani P, Pansarasa O, Mazzini G, Guareschi S, Alvisi E, Ghiroldi A, Diamanti L, Bernuzzi S et al (2013) Altered intracellular localization of SOD1 in leukocytes from patients with sporadic amyotrophic lateral sclerosis. PLoS One 8:e75916. doi:10.1371/journal.pone.0075916
    • (2013) PLoS One , vol.8
    • Cereda, C.1    Leoni, E.2    Milani, P.3    Pansarasa, O.4    Mazzini, G.5    Guareschi, S.6    Alvisi, E.7    Ghiroldi, A.8    Diamanti, L.9    Bernuzzi, S.10
  • 12
    • 84950327128 scopus 로고    scopus 로고
    • The disulfide bond, but not zinc or dimerization, controls initiation and seeded growth in amyotrophic lateral sclerosis-linked Cu, Zn superoxide dismutase (SOD1) fibrillation
    • COI: 1:CAS:528:DC%2BC2MXitVGhtrrO, PID: 26511321
    • Chattopadhyay M, Nwadibia E, Strong CD, Gralla EB, Valentine JS, Whitelegge JP (2015) The disulfide bond, but not zinc or dimerization, controls initiation and seeded growth in amyotrophic lateral sclerosis-linked Cu, Zn superoxide dismutase (SOD1) fibrillation. J Biol Chem 290:30624–30636. doi:10.1074/jbc.M115.666503
    • (2015) J Biol Chem , vol.290 , pp. 30624-30636
    • Chattopadhyay, M.1    Nwadibia, E.2    Strong, C.D.3    Gralla, E.B.4    Valentine, J.S.5    Whitelegge, J.P.6
  • 14
    • 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)
    • COI: 1:CAS:528:DyaK2MXks1Khtrk%3D, PID: 7796176
    • Dal Canto MC, Gurney ME (1995) Neuropathological changes in two lines of mice carrying a transgene for mutant human Cu, Zn SOD, and in mice overexpressing wild type human SOD: a model of familial amyotrophic lateral sclerosis (FALS). Brain Res 676:25–40
    • (1995) Brain Res , vol.676 , pp. 25-40
    • Dal Canto, M.C.1    Gurney, M.E.2
  • 15
    • 33646466296 scopus 로고    scopus 로고
    • Conversion to the amyotrophic lateral sclerosis phenotype is associated with intermolecular linked insoluble aggregates of SOD1 in mitochondria
    • COI: 1:CAS:528:DC%2BD28XkslCktLg%3D, PID: 16636275
    • Deng HX, Shi Y, Furukawa Y, Zhai H, Fu R, Liu E, Gorrie GH, Khan MS, Hung WY, Bigio EH et al (2006) Conversion to the amyotrophic lateral sclerosis phenotype is associated with intermolecular linked insoluble aggregates of SOD1 in mitochondria. Proc Natl Acad Sci U S A 103:7142–7147. doi:10.1073/pnas.0602046103
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 7142-7147
    • Deng, H.X.1    Shi, Y.2    Furukawa, Y.3    Zhai, H.4    Fu, R.5    Liu, E.6    Gorrie, G.H.7    Khan, M.S.8    Hung, W.Y.9    Bigio, E.H.10
  • 16
    • 34250177650 scopus 로고    scopus 로고
    • Wild-type superoxide dismutase acquires binding and toxic properties of ALS-linked mutant forms through oxidation
    • PID: 17394546
    • Ezzi SA, Urushitani M, Julien JP (2007) Wild-type superoxide dismutase acquires binding and toxic properties of ALS-linked mutant forms through oxidation. J Neurochem 102:170–178. doi:10.1111/j.1471-4159.2007.04531.x
    • (2007) J Neurochem , vol.102 , pp. 170-178
    • Ezzi, S.A.1    Urushitani, M.2    Julien, J.P.3
  • 18
    • 79958135335 scopus 로고    scopus 로고
    • Glial nuclear aggregates of superoxide dismutase-1 are regularly present in patients with amyotrophic lateral sclerosis
    • COI: 1:CAS:528:DC%2BC3MXlsVKqt7k%3D, PID: 21287393
    • Forsberg K, Andersen PM, Marklund SL, Brannstrom T (2011) Glial nuclear aggregates of superoxide dismutase-1 are regularly present in patients with amyotrophic lateral sclerosis. Acta Neuropathol 121:623–634. doi:10.1007/s00401-011-0805-3
    • (2011) Acta Neuropathol , vol.121 , pp. 623-634
    • Forsberg, K.1    Andersen, P.M.2    Marklund, S.L.3    Brannstrom, T.4
  • 21
    • 35448956015 scopus 로고    scopus 로고
    • Evidence for secretion of Cu, Zn superoxide dismutase via exosomes from a cell model of amyotrophic lateral sclerosis
    • COI: 1:CAS:528:DC%2BD2sXht1Kjs73O, PID: 17942226
    • Gomes C, Keller S, Altevogt P, Costa J (2007) Evidence for secretion of Cu, Zn superoxide dismutase via exosomes from a cell model of amyotrophic lateral sclerosis. Neurosci Lett 428:43–46. doi:10.1016/j.neulet.2007.09.024
    • (2007) Neurosci Lett , vol.428 , pp. 43-46
    • Gomes, C.1    Keller, S.2    Altevogt, P.3    Costa, J.4
  • 22
    • 84920768238 scopus 로고    scopus 로고
    • Exosome-dependent and independent mechanisms are involved in prion-like transmission of propagated Cu/Zn superoxide dismutase misfolding
    • COI: 1:CAS:528:DC%2BC2MXisFaqsLg%3D, PID: 25551548
    • Grad LI, Pokrishevsky E, Silverman JM, Cashman NR (2014) Exosome-dependent and independent mechanisms are involved in prion-like transmission of propagated Cu/Zn superoxide dismutase misfolding. Prion 8:331–335. doi:10.4161/19336896.2014.983398
    • (2014) Prion , vol.8 , pp. 331-335
    • Grad, L.I.1    Pokrishevsky, E.2    Silverman, J.M.3    Cashman, N.R.4
  • 25
    • 77951924183 scopus 로고    scopus 로고
    • Intracerebroventricular infusion of monoclonal antibody or its derived Fab fragment against misfolded forms of SOD1 mutant delays mortality in a mouse model of ALS
    • COI: 1:CAS:528:DC%2BC3cXnt1GnsLk%3D, PID: 20345765
    • Gros-Louis F, Soucy G, Lariviere R, Julien JP (2010) Intracerebroventricular infusion of monoclonal antibody or its derived Fab fragment against misfolded forms of SOD1 mutant delays mortality in a mouse model of ALS. J Neurochem 113:1188–1199. doi:10.1111/j.1471-4159.2010.06683.x
    • (2010) J Neurochem , vol.113 , pp. 1188-1199
    • Gros-Louis, F.1    Soucy, G.2    Lariviere, R.3    Julien, J.P.4
  • 27
    • 84859454704 scopus 로고    scopus 로고
    • An over-oxidized form of superoxide dismutase found in sporadic amyotrophic lateral sclerosis with bulbar onset shares a toxic mechanism with mutant SOD1
    • COI: 1:CAS:528:DC%2BC38Xlt1Sisr4%3D, PID: 22416121
    • Guareschi S, Cova E, Cereda C, Ceroni M, Donetti E, Bosco DA, Trotti D, Pasinelli P (2012) An over-oxidized form of superoxide dismutase found in sporadic amyotrophic lateral sclerosis with bulbar onset shares a toxic mechanism with mutant SOD1. Proc Natl Acad Sci U S A 109:5074–5079. doi:10.1073/pnas.1115402109
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 5074-5079
    • Guareschi, S.1    Cova, E.2    Cereda, C.3    Ceroni, M.4    Donetti, E.5    Bosco, D.A.6    Trotti, D.7    Pasinelli, P.8
  • 31
    • 0037022339 scopus 로고    scopus 로고
    • Focal loss of the glutamate transporter EAAT2 in a transgenic rat model of SOD1 mutant-mediated amyotrophic lateral sclerosis (ALS)
    • COI: 1:CAS:528:DC%2BD38Xht1Clt78%3D, PID: 11818550
    • Howland DS, Liu J, She Y, Goad B, Maragakis NJ, Kim B, Erickson J, Kulik J, DeVito L, Psaltis G et al (2002) Focal loss of the glutamate transporter EAAT2 in a transgenic rat model of SOD1 mutant-mediated amyotrophic lateral sclerosis (ALS). Proc Natl Acad Sci U S A 99:1604–1609. doi:10.1073/pnas.032539299
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 1604-1609
    • Howland, D.S.1    Liu, J.2    She, Y.3    Goad, B.4    Maragakis, N.J.5    Kim, B.6    Erickson, J.7    Kulik, J.8    DeVito, L.9    Psaltis, G.10
  • 32
    • 82355170711 scopus 로고    scopus 로고
    • Molecular pathology and genetic advances in amyotrophic lateral sclerosis: an emerging molecular pathway and the significance of glial pathology
    • COI: 1:CAS:528:DC%2BC3MXhsFCms7%2FP, PID: 22105541
    • Ince PG, Highley JR, Kirby J, Wharton SB, Takahashi H, Strong MJ, Shaw PJ (2011) Molecular pathology and genetic advances in amyotrophic lateral sclerosis: an emerging molecular pathway and the significance of glial pathology. Acta Neuropathol 122:657–671. doi:10.1007/s00401-011-0913-0
    • (2011) Acta Neuropathol , vol.122 , pp. 657-671
    • Ince, P.G.1    Highley, J.R.2    Kirby, J.3    Wharton, S.B.4    Takahashi, H.5    Strong, M.J.6    Shaw, P.J.7
  • 33
    • 77955961922 scopus 로고    scopus 로고
    • Misfolded mutant SOD1 directly inhibits VDAC1 conductance in a mouse model of inherited ALS
    • COI: 1:CAS:528:DC%2BC3cXhtV2gtb3L, PID: 20797535
    • Israelson A, Arbel N, Da Cruz S, Ilieva H, Yamanaka K, Shoshan-Barmatz V, Cleveland DW (2010) Misfolded mutant SOD1 directly inhibits VDAC1 conductance in a mouse model of inherited ALS. Neuron 67:575–587. doi:10.1016/j.neuron.2010.07.019
    • (2010) Neuron , vol.67 , pp. 575-587
    • Israelson, A.1    Arbel, N.2    Da Cruz, S.3    Ilieva, H.4    Yamanaka, K.5    Shoshan-Barmatz, V.6    Cleveland, D.W.7
  • 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
    • COI: 1:CAS:528:DC%2BD3cXoslSms74%3D, PID: 11114261
    • Jaarsma D, Haasdijk ED, Grashorn JA, Hawkins R, van Duijn W, Verspaget HW, London J, Holstege JC (2000) 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. Neurobiol Dis 7:623–643
    • (2000) Neurobiol Dis , vol.7 , pp. 623-643
    • Jaarsma, D.1    Haasdijk, E.D.2    Grashorn, J.A.3    Hawkins, R.4    van Duijn, W.5    Verspaget, H.W.6    London, J.7    Holstege, J.C.8
  • 36
    • 33845361242 scopus 로고    scopus 로고
    • Motor neuron disease in mice expressing the wild type-like D90A mutant superoxide dismutase-1
    • COI: 1:CAS:528:DC%2BD2sXkt1Chsg%3D%3D, PID: 17146286
    • Jonsson PA, Graffmo KS, Brannstrom T, Nilsson P, Andersen PM, Marklund SL (2006) Motor neuron disease in mice expressing the wild type-like D90A mutant superoxide dismutase-1. J Neuropathol Exp Neurol 65:1126–1136. doi:10.1097/01.jnen.0000248545.36046.3c
    • (2006) J Neuropathol Exp Neurol , vol.65 , pp. 1126-1136
    • Jonsson, P.A.1    Graffmo, K.S.2    Brannstrom, T.3    Nilsson, P.4    Andersen, P.M.5    Marklund, S.L.6
  • 37
    • 66049156169 scopus 로고    scopus 로고
    • Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALS
    • COI: 1:CAS:528:DC%2BD1MXmt1ams7Y%3D, PID: 19416874
    • Karch CM, Prudencio M, Winkler DD, Hart PJ, Borchelt DR (2009) Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALS. Proc Natl Acad Sci U S A 106:7774–7779. doi:10.1073/pnas.0902505106
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 7774-7779
    • Karch, C.M.1    Prudencio, M.2    Winkler, D.D.3    Hart, P.J.4    Borchelt, D.R.5
  • 38
    • 31344462620 scopus 로고    scopus 로고
    • Age-related neuropathology, cognitive decline, and Alzheimer’s disease
    • COI: 1:CAS:528:DC%2BD28Xis1yis7Y%3D, PID: 16084778
    • Keller JN (2006) Age-related neuropathology, cognitive decline, and Alzheimer’s disease. Ageing Res Rev 5:1–13. doi:10.1016/j.arr.2005.06.002
    • (2006) Ageing Res Rev , vol.5 , pp. 1-13
    • Keller, J.N.1
  • 39
    • 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
    • PID: 20111867
    • Kerman A, Liu HN, Croul S, Bilbao J, Rogaeva E, Zinman L, Robertson J, Chakrabartty A (2010) Amyotrophic lateral sclerosis is a non-amyloid disease in which extensive misfolding of SOD1 is unique to the familial form. Acta Neuropathol 119:335–344. doi:10.1007/s00401-010-0646-5
    • (2010) Acta Neuropathol , vol.119 , pp. 335-344
    • Kerman, A.1    Liu, H.N.2    Croul, S.3    Bilbao, J.4    Rogaeva, E.5    Zinman, L.6    Robertson, J.7    Chakrabartty, A.8
  • 40
    • 69249121554 scopus 로고    scopus 로고
    • Lack of evidence of monomer/misfolded superoxide dismutase-1 in sporadic amyotrophic lateral sclerosis
    • COI: 1:CAS:528:DC%2BD1MXhtFWju7fI, PID: 19670443
    • Liu HN, Sanelli T, Horne P, Pioro EP, Strong MJ, Rogaeva E, Bilbao J, Zinman L, Robertson J (2009) Lack of evidence of monomer/misfolded superoxide dismutase-1 in sporadic amyotrophic lateral sclerosis. Ann Neurol 66:75–80. doi:10.1002/ana.21704
    • (2009) Ann Neurol , vol.66 , pp. 75-80
    • Liu, H.N.1    Sanelli, T.2    Horne, P.3    Pioro, E.P.4    Strong, M.J.5    Rogaeva, E.6    Bilbao, J.7    Zinman, L.8    Robertson, J.9
  • 42
    • 34249946466 scopus 로고    scopus 로고
    • Pathological TDP-43 distinguishes sporadic amyotrophic lateral sclerosis from amyotrophic lateral sclerosis with SOD1 mutations
    • COI: 1:CAS:528:DC%2BD2sXnsFKmtbc%3D, PID: 17469116
    • Mackenzie IR, Bigio EH, Ince PG, Geser F, Neumann M, Cairns NJ, Kwong LK, Forman MS, Ravits J, Stewart H et al (2007) Pathological TDP-43 distinguishes sporadic amyotrophic lateral sclerosis from amyotrophic lateral sclerosis with SOD1 mutations. Ann Neurol 61:427–434. doi:10.1002/ana.21147
    • (2007) Ann Neurol , vol.61 , pp. 427-434
    • Mackenzie, I.R.1    Bigio, E.H.2    Ince, P.G.3    Geser, F.4    Neumann, M.5    Cairns, N.J.6    Kwong, L.K.7    Forman, M.S.8    Ravits, J.9    Stewart, H.10
  • 43
    • 70449698510 scopus 로고    scopus 로고
    • TDP-43 is consistently co-localized with ubiquitinated inclusions in sporadic and Guam amyotrophic lateral sclerosis but not in familial amyotrophic lateral sclerosis with and without SOD1 mutations
    • Maekawa S, Leigh PN, King A, Jones E, Steele JC, Bodi I, Shaw CE, Hortobagyi T, Al-Sarraj S (2009) TDP-43 is consistently co-localized with ubiquitinated inclusions in sporadic and Guam amyotrophic lateral sclerosis but not in familial amyotrophic lateral sclerosis with and without SOD1 mutations. Neuropathol Off J Jpn Soc Neuropathol 29:672–683. doi:10.1111/j.1440-1789.2009.01029.x
    • (2009) Neuropathol Off J Jpn Soc Neuropathol , vol.29 , pp. 672-683
    • Maekawa, S.1    Leigh, P.N.2    King, A.3    Jones, E.4    Steele, J.C.5    Bodi, I.6    Shaw, C.E.7    Hortobagyi, T.8    Al-Sarraj, S.9
  • 44
    • 84876466100 scopus 로고    scopus 로고
    • An antisense oligonucleotide against SOD1 delivered intrathecally for patients with SOD1 familial amyotrophic lateral sclerosis: a phase 1, randomised, first-in-man study
    • COI: 1:CAS:528:DC%2BC3sXltVynsrY%3D, PID: 23541756
    • Miller TM, Pestronk A, David W, Rothstein J, Simpson E, Appel SH, Andres PL, Mahoney K, Allred P, Alexander K et al (2013) An antisense oligonucleotide against SOD1 delivered intrathecally for patients with SOD1 familial amyotrophic lateral sclerosis: a phase 1, randomised, first-in-man study. Lancet Neurol 12:435–442. doi:10.1016/S1474-4422(13)70061-9
    • (2013) Lancet Neurol , vol.12 , pp. 435-442
    • Miller, T.M.1    Pestronk, A.2    David, W.3    Rothstein, J.4    Simpson, E.5    Appel, S.H.6    Andres, P.L.7    Mahoney, K.8    Allred, P.9    Alexander, K.10
  • 45
    • 79952743365 scopus 로고    scopus 로고
    • Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells
    • COI: 1:CAS:528:DC%2BC3MXivFGqur8%3D, PID: 21321227
    • Munch C, O’Brien J, Bertolotti A (2011) Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells. Proc Natl Acad Sci U S A 108:3548–3553. doi:10.1073/pnas.1017275108
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 3548-3553
    • Munch, C.1    O’Brien, J.2    Bertolotti, A.3
  • 47
    • 63449092530 scopus 로고    scopus 로고
    • Loss of metal ions, disulfide reduction and mutations related to familial ALS promote formation of amyloid-like aggregates from superoxide dismutase
    • PID: 19325915
    • Oztug Durer ZA, Cohlberg JA, Dinh P, Padua S, Ehrenclou K, Downes S, Tan JK, Nakano Y, Bowman CJ, Hoskins JL et al (2009) Loss of metal ions, disulfide reduction and mutations related to familial ALS promote formation of amyloid-like aggregates from superoxide dismutase. PLoS One 4:e5004. doi:10.1371/journal.pone.0005004
    • (2009) PLoS One , vol.4
    • Oztug Durer, Z.A.1    Cohlberg, J.A.2    Dinh, P.3    Padua, S.4    Ehrenclou, K.5    Downes, S.6    Tan, J.K.7    Nakano, Y.8    Bowman, C.J.9    Hoskins, J.L.10
  • 48
    • 84874914445 scopus 로고    scopus 로고
    • Enhancing mitochondrial calcium buffering capacity reduces aggregation of misfolded SOD1 and motor neuron cell death without extending survival in mouse models of inherited amyotrophic lateral sclerosis
    • COI: 1:CAS:528:DC%2BC3sXhtlOjs73J, PID: 23486940
    • Parone PA, Da Cruz S, Han JS, McAlonis-Downes M, Vetto AP, Lee SK, Tseng E, Cleveland DW (2013) Enhancing mitochondrial calcium buffering capacity reduces aggregation of misfolded SOD1 and motor neuron cell death without extending survival in mouse models of inherited amyotrophic lateral sclerosis. J Neurosci 33:4657–4671. doi:10.1523/JNEUROSCI.1119-12.2013
    • (2013) J Neurosci , vol.33 , pp. 4657-4671
    • Parone, P.A.1    Da Cruz, S.2    Han, J.S.3    McAlonis-Downes, M.4    Vetto, A.P.5    Lee, S.K.6    Tseng, E.7    Cleveland, D.W.8
  • 51
    • 84861596118 scopus 로고    scopus 로고
    • Misfolded SOD1 and ALS: zeroing in on mitochondria
    • COI: 1:CAS:528:DC%2BC38XnslKitrs%3D
    • Pickles S, Vande Velde C (2012) Misfolded SOD1 and ALS: zeroing in on mitochondria. Amyotroph Later Scler 13:333–340. doi:10.3109/17482968.2012.648645
    • (2012) Amyotroph Later Scler , vol.13 , pp. 333-340
    • Pickles, S.1    Vande Velde, C.2
  • 53
    • 84859512071 scopus 로고    scopus 로고
    • Aberrant localization of FUS and TDP43 is associated with misfolding of SOD1 in amyotrophic lateral sclerosis
    • COI: 1:CAS:528:DC%2BC38XlvV2jsr8%3D, PID: 22493728
    • Pokrishevsky E, Grad LI, Yousefi M, Wang J, Mackenzie IR, Cashman NR (2012) Aberrant localization of FUS and TDP43 is associated with misfolding of SOD1 in amyotrophic lateral sclerosis. PLoS One 7:e35050. doi:10.1371/journal.pone.0035050
    • (2012) PLoS One , vol.7
    • Pokrishevsky, E.1    Grad, L.I.2    Yousefi, M.3    Wang, J.4    Mackenzie, I.R.5    Cashman, N.R.6
  • 54
    • 78649473387 scopus 로고    scopus 로고
    • An examination of wild-type SOD1 in modulating the toxicity and aggregation of ALS-associated mutant SOD1
    • COI: 1:CAS:528:DC%2BC3cXhsVyhsr3M, PID: 20871097
    • Prudencio M, Durazo A, Whitelegge JP, Borchelt DR (2010) An examination of wild-type SOD1 in modulating the toxicity and aggregation of ALS-associated mutant SOD1. Hum Mol Genet 19:4774–4789. doi:10.1093/hmg/ddq408
    • (2010) Hum Mol Genet , vol.19 , pp. 4774-4789
    • Prudencio, M.1    Durazo, A.2    Whitelegge, J.P.3    Borchelt, D.R.4
  • 55
    • 2442624720 scopus 로고    scopus 로고
    • Monomeric Cu, Zn-superoxide dismutase is a common misfolding intermediate in the oxidation models of sporadic and familial amyotrophic lateral sclerosis
    • COI: 1:CAS:528:DC%2BD2cXivVKgt78%3D, PID: 14734542
    • Rakhit R, Crow JP, Lepock JR, Kondejewski LH, Cashman NR, Chakrabartty A (2004) Monomeric Cu, Zn-superoxide dismutase is a common misfolding intermediate in the oxidation models of sporadic and familial amyotrophic lateral sclerosis. J Biol Chem 279:15499–15504. doi:10.1074/jbc.M313295200
    • (2004) J Biol Chem , vol.279 , pp. 15499-15504
    • Rakhit, R.1    Crow, J.P.2    Lepock, J.R.3    Kondejewski, L.H.4    Cashman, N.R.5    Chakrabartty, A.6
  • 57
    • 84895508213 scopus 로고    scopus 로고
    • Necroptosis drives motor neuron death in models of both sporadic and familial ALS
    • COI: 1:CAS:528:DC%2BC2cXitVyrtb0%3D, PID: 24508385
    • Re DB, Le Verche V, Yu C, Amoroso MW, Politi KA, Phani S, Ikiz B, Hoffmann L, Koolen M, Nagata T et al (2014) Necroptosis drives motor neuron death in models of both sporadic and familial ALS. Neuron 81:1001–1008. doi:10.1016/j.neuron.2014.01.011
    • (2014) Neuron , vol.81 , pp. 1001-1008
    • Re, D.B.1    Le Verche, V.2    Yu, C.3    Amoroso, M.W.4    Politi, K.A.5    Phani, S.6    Ikiz, B.7    Hoffmann, L.8    Koolen, M.9    Nagata, T.10
  • 58
    • 34249313704 scopus 로고    scopus 로고
    • Lack of TDP-43 abnormalities in mutant SOD1 transgenic mice shows disparity with ALS
    • COI: 1:CAS:528:DC%2BD2sXmtVKjurg%3D, PID: 17543992
    • Robertson J, Sanelli T, Xiao S, Yang W, Horne P, Hammond R, Pioro EP, Strong MJ (2007) Lack of TDP-43 abnormalities in mutant SOD1 transgenic mice shows disparity with ALS. Neurosci Lett 420:128–132. doi:10.1016/j.neulet.2007.03.066
    • (2007) Neurosci Lett , vol.420 , pp. 128-132
    • Robertson, J.1    Sanelli, T.2    Xiao, S.3    Yang, W.4    Horne, P.5    Hammond, R.6    Pioro, E.P.7    Strong, M.J.8
  • 60
    • 84884765656 scopus 로고    scopus 로고
    • Neuroprotection through excitability and mTOR required in ALS motoneurons to delay disease and extend survival
    • COI: 1:CAS:528:DC%2BC3sXhsFGru7nK, PID: 24094105
    • Saxena S, Roselli F, Singh K, Leptien K, Julien JP, Gros-Louis F, Caroni P (2013) Neuroprotection through excitability and mTOR required in ALS motoneurons to delay disease and extend survival. Neuron 80:80–96. doi:10.1016/j.neuron.2013.07.027
    • (2013) Neuron , vol.80 , pp. 80-96
    • Saxena, S.1    Roselli, F.2    Singh, K.3    Leptien, K.4    Julien, J.P.5    Gros-Louis, F.6    Caroni, P.7
  • 62
    • 84893565750 scopus 로고    scopus 로고
    • Astroglial heme oxygenase-1 and the origin of corpora amylacea in aging and degenerating neural tissues
    • COI: 1:CAS:528:DC%2BC2cXktVWhu70%3D, PID: 24440642
    • Song W, Zukor H, Liberman A, Kaduri S, Arvanitakis Z, Bennett DA, Schipper HM (2014) Astroglial heme oxygenase-1 and the origin of corpora amylacea in aging and degenerating neural tissues. Exp Neurol 254:78–89. doi:10.1016/j.expneurol.2014.01.006
    • (2014) Exp Neurol , vol.254 , pp. 78-89
    • Song, W.1    Zukor, H.2    Liberman, A.3    Kaduri, S.4    Arvanitakis, Z.5    Bennett, D.A.6    Schipper, H.M.7
  • 63
    • 0037795635 scopus 로고    scopus 로고
    • Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis show enhanced formation of aggregates in vitro
    • COI: 1:CAS:528:DC%2BD3sXkslOntbw%3D, PID: 12773627
    • Stathopulos PB, Rumfeldt JA, Scholz GA, Irani RA, Frey HE, Hallewell RA, Lepock JR, Meiering EM (2003) Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis show enhanced formation of aggregates in vitro. Proc Natl Acad Sci U S A 100:7021–7026. doi:10.1073/pnas.1237797100
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 7021-7026
    • Stathopulos, P.B.1    Rumfeldt, J.A.2    Scholz, G.A.3    Irani, R.A.4    Frey, H.E.5    Hallewell, R.A.6    Lepock, J.R.7    Meiering, E.M.8
  • 64
    • 34247606414 scopus 로고    scopus 로고
    • TDP-43 immunoreactivity in neuronal inclusions in familial amyotrophic lateral sclerosis with or without SOD1 gene mutation
    • COI: 1:CAS:528:DC%2BD2sXks1ygt7k%3D, PID: 17333220
    • Tan CF, Eguchi H, Tagawa A, Onodera O, Iwasaki T, Tsujino A, Nishizawa M, Kakita A, Takahashi H (2007) TDP-43 immunoreactivity in neuronal inclusions in familial amyotrophic lateral sclerosis with or without SOD1 gene mutation. Acta Neuropathol 113:535–542. doi:10.1007/s00401-007-0206-9
    • (2007) Acta Neuropathol , vol.113 , pp. 535-542
    • Tan, C.F.1    Eguchi, H.2    Tagawa, A.3    Onodera, O.4    Iwasaki, T.5    Tsujino, A.6    Nishizawa, M.7    Kakita, A.8    Takahashi, H.9
  • 65
    • 12144249923 scopus 로고    scopus 로고
    • Impaired extracellular secretion of mutant superoxide dismutase 1 associates with neurotoxicity in familial amyotrophic lateral sclerosis
    • COI: 1:CAS:528:DC%2BD2MXhtVWku7s%3D, PID: 15634772
    • Turner BJ, Atkin JD, Farg MA, Zang DW, Rembach A, Lopes EC, Patch JD, Hill AF, Cheema SS (2005) Impaired extracellular secretion of mutant superoxide dismutase 1 associates with neurotoxicity in familial amyotrophic lateral sclerosis. J Neurosci 25:108–117. doi:10.1523/JNEUROSCI.4253-04.2005
    • (2005) J Neurosci , vol.25 , pp. 108-117
    • Turner, B.J.1    Atkin, J.D.2    Farg, M.A.3    Zang, D.W.4    Rembach, A.5    Lopes, E.C.6    Patch, J.D.7    Hill, A.F.8    Cheema, S.S.9
  • 66
    • 33847787621 scopus 로고    scopus 로고
    • Therapeutic effects of immunization with mutant superoxide dismutase in mice models of amyotrophic lateral sclerosis
    • COI: 1:CAS:528:DC%2BD2sXisVSgt7w%3D, PID: 17277077
    • Urushitani M, Ezzi SA, Julien JP (2007) Therapeutic effects of immunization with mutant superoxide dismutase in mice models of amyotrophic lateral sclerosis. Proc Natl Acad Sci U S A 104:2495–2500. doi:10.1073/pnas.0606201104
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 2495-2500
    • Urushitani, M.1    Ezzi, S.A.2    Julien, J.P.3
  • 67
    • 0037388067 scopus 로고    scopus 로고
    • Misfolded CuZnSOD and amyotrophic lateral sclerosis
    • COI: 1:CAS:528:DC%2BD3sXivFSqs7w%3D, PID: 12655070
    • Valentine JS, Hart PJ (2003) Misfolded CuZnSOD and amyotrophic lateral sclerosis. Proc Natl Acad Sci U S A 100:3617–3622. doi:10.1073/pnas.0730423100
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 3617-3622
    • Valentine, J.S.1    Hart, P.J.2
  • 68
    • 41649086378 scopus 로고    scopus 로고
    • Selective association of misfolded ALS-linked mutant SOD1 with the cytoplasmic face of mitochondria
    • PID: 18296640
    • Vande Velde C, Miller TM, Cashman NR, Cleveland DW (2008) Selective association of misfolded ALS-linked mutant SOD1 with the cytoplasmic face of mitochondria. Proc Natl Acad Sci U S A 105:4022–4027. doi:10.1073/pnas.0712209105
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 4022-4027
    • Vande Velde, C.1    Miller, T.M.2    Cashman, N.R.3    Cleveland, D.W.4
  • 69
    • 0036199623 scopus 로고    scopus 로고
    • High molecular weight complexes of mutant superoxide dismutase 1: age-dependent and tissue-specific accumulation
    • COI: 1:CAS:528:DC%2BD38XhvVSksrw%3D, PID: 11895367
    • Wang J, Xu G, Borchelt DR (2002) High molecular weight complexes of mutant superoxide dismutase 1: age-dependent and tissue-specific accumulation. Neurobiol Dis 9:139–148. doi:10.1006/nbdi.2001.0471
    • (2002) Neurobiol Dis , vol.9 , pp. 139-148
    • Wang, J.1    Xu, G.2    Borchelt, D.R.3
  • 70
    • 0036076642 scopus 로고    scopus 로고
    • Fibrillar inclusions and motor neuron degeneration in transgenic mice expressing superoxide dismutase 1 with a disrupted copper-binding site
    • COI: 1:CAS:528:DC%2BD38XltFyrtb8%3D, PID: 12127151
    • Wang J, Xu G, Gonzales V, Coonfield M, Fromholt D, Copeland NG, Jenkins NA, Borchelt DR (2002) Fibrillar inclusions and motor neuron degeneration in transgenic mice expressing superoxide dismutase 1 with a disrupted copper-binding site. Neurobiol Dis 10:128–138
    • (2002) Neurobiol Dis , vol.10 , pp. 128-138
    • Wang, J.1    Xu, G.2    Gonzales, V.3    Coonfield, M.4    Fromholt, D.5    Copeland, N.G.6    Jenkins, N.A.7    Borchelt, D.R.8
  • 71
    • 64549124726 scopus 로고    scopus 로고
    • Wild-type SOD1 overexpression accelerates disease onset of a G85R SOD1 mouse
    • COI: 1:CAS:528:DC%2BD1MXksVeitbg%3D, PID: 19233858
    • Wang L, Deng HX, Grisotti G, Zhai H, Siddique T, Roos RP (2009) Wild-type SOD1 overexpression accelerates disease onset of a G85R SOD1 mouse. Hum Mol Genet 18:1642–1651. doi:10.1093/hmg/ddp085
    • (2009) Hum Mol Genet , vol.18 , pp. 1642-1651
    • Wang, L.1    Deng, H.X.2    Grisotti, G.3    Zhai, H.4    Siddique, T.5    Roos, R.P.6
  • 72
    • 84922477400 scopus 로고    scopus 로고
    • Direct and indirect mechanisms for wild-type SOD1 to enhance the toxicity of mutant SOD1 in bigenic transgenic mice
    • COI: 1:CAS:528:DC%2BC2MXhsVylsb%2FE, PID: 25305079
    • Xu G, Ayers JI, Roberts BL, Brown H, Fromholt S, Green C, Borchelt DR (2015) Direct and indirect mechanisms for wild-type SOD1 to enhance the toxicity of mutant SOD1 in bigenic transgenic mice. Hum Mol Genet 24:1019–1035. doi:10.1093/hmg/ddu517
    • (2015) Hum Mol Genet , vol.24 , pp. 1019-1035
    • Xu, G.1    Ayers, J.I.2    Roberts, B.L.3    Brown, H.4    Fromholt, S.5    Green, C.6    Borchelt, D.R.7
  • 73
    • 84874754257 scopus 로고    scopus 로고
    • Composition of soluble misfolded superoxide dismutase-1 in murine models of amyotrophic lateral sclerosis
    • Zetterstrom P, Graffmo KS, Andersen PM, Brannstrom T, Marklund SL (2013) Composition of soluble misfolded superoxide dismutase-1 in murine models of amyotrophic lateral sclerosis. Neuromol Med 15:147–158. doi:10.1007/s12017-012-8204-z
    • (2013) Neuromol Med , vol.15 , pp. 147-158
    • Zetterstrom, P.1    Graffmo, K.S.2    Andersen, P.M.3    Brannstrom, T.4    Marklund, S.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.