메뉴 건너뛰기




Volumn 314, Issue 1-2, 2012, Pages 92-96

Misfolded SOD1 forms high-density molecular complexes with synaptic molecules in mutant SOD1-linked familial amyotrophic lateral sclerosis cases

Author keywords

Amyotrophic lateral schlerosis; L126S mutation; SOD1; Synapse

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE; GLUTAMATE RECEPTOR; GLUTAMATE RECEPTOR GLUR2; GLUTAMATE RECEPTOR GLUR3; KAP3 PROTEIN; KINESIN 2; MISFOLDED SUPEROXIDE DISMUTASE 1; MUTANT PROTEIN; POSTSYNAPTIC DENSITY PROTEIN 95; SYNAPTOPHYSIN; SYNAPTOSOMAL ASSOCIATED PROTEIN 25; UNCLASSIFIED DRUG;

EID: 84857059828     PISSN: 0022510X     EISSN: 18785883     Source Type: Journal    
DOI: 10.1016/j.jns.2011.10.017     Document Type: Article
Times cited : (5)

References (15)
  • 1
    • 33749056809 scopus 로고    scopus 로고
    • ALS: A disease of motor neurons and their nonneuronal neighbors
    • S. Boillee, C. Vande Velde, and D.W. Cleveland ALS: a disease of motor neurons and their nonneuronal neighbors Neuron 52 2006 39 59
    • (2006) Neuron , vol.52 , pp. 39-59
    • Boillee, S.1    Vande Velde, C.2    Cleveland, D.W.3
  • 2
    • 33747605320 scopus 로고    scopus 로고
    • Molecular biology of amyotrophic lateral sclerosis: Insights from genetics
    • P. Pasinelli, and R.H. Brown Molecular biology of amyotrophic lateral sclerosis: insights from genetics Nat Rev Neurosci 7 2006 710 723
    • (2006) Nat Rev Neurosci , vol.7 , pp. 710-723
    • Pasinelli, P.1    Brown, R.H.2
  • 3
    • 33846678063 scopus 로고    scopus 로고
    • How do ALS-associated mutations in superoxide dismutase 1 promote aggregation of the protein?
    • B.F. Shaw, and J.S. Valentine How do ALS-associated mutations in superoxide dismutase 1 promote aggregation of the protein? Trends Biochem Sci 32 2007 78 85
    • (2007) Trends Biochem Sci , vol.32 , pp. 78-85
    • Shaw, B.F.1    Valentine, J.S.2
  • 4
    • 33751003518 scopus 로고    scopus 로고
    • Oxidative stress in ALS: A mechanism of neurodegeneration and a therapeutic target
    • S.C. Barber, R.J. Mead, and P.J. Shaw Oxidative stress in ALS: a mechanism of neurodegeneration and a therapeutic target Biochim Biophys Acta 1762 2006 1051 1067
    • (2006) Biochim Biophys Acta , vol.1762 , pp. 1051-1067
    • Barber, S.C.1    Mead, R.J.2    Shaw, P.J.3
  • 5
    • 60549104791 scopus 로고    scopus 로고
    • Mutant SOD1 impairs axonal transport of choline acetyltransferase and acetylcholine release by sequestering KAP3
    • M. Tateno, S. Kato, T. Sakurai, N. Nukina, R. Takahashi, and T. Araki Mutant SOD1 impairs axonal transport of choline acetyltransferase and acetylcholine release by sequestering KAP3 Hum Mol Genet 18 2009 942 955
    • (2009) Hum Mol Genet , vol.18 , pp. 942-955
    • Tateno, M.1    Kato, S.2    Sakurai, T.3    Nukina, N.4    Takahashi, R.5    Araki, T.6
  • 6
    • 14844331501 scopus 로고    scopus 로고
    • Molecular motors and mechanisms of directional transport in neurons
    • N. Hirokawa, and R. Takemura Molecular motors and mechanisms of directional transport in neurons Nat Rev Neurosci 6 2005 201 214
    • (2005) Nat Rev Neurosci , vol.6 , pp. 201-214
    • Hirokawa, N.1    Takemura, R.2
  • 7
    • 5444222849 scopus 로고    scopus 로고
    • Calcium-permeable AMPA receptors promote misfolding of mutant SOD1 protein and development of amyotrophic lateral sclerosis in a transgenic mouse model
    • M. Tateno, H. Sadakata, M. Tanaka, S. Itohara, R.M. Shin, and M. Miura Calcium-permeable AMPA receptors promote misfolding of mutant SOD1 protein and development of amyotrophic lateral sclerosis in a transgenic mouse model Hum Mol Genet 13 2004 2183 2196
    • (2004) Hum Mol Genet , vol.13 , pp. 2183-2196
    • Tateno, M.1    Sadakata, H.2    Tanaka, M.3    Itohara, S.4    Shin, R.M.5    Miura, M.6
  • 8
    • 0032731637 scopus 로고    scopus 로고
    • ALS-linked Cu/Zn-SOD mutation increases vulnerability of motor neurons to excitotoxicity by a mechanism involving increased oxidative stress and perturbed calcium homeostasis
    • I.I. Kruman, W.A. Pedersen, J.E. Springer, and M.P. Mattson ALS-linked Cu/Zn-SOD mutation increases vulnerability of motor neurons to excitotoxicity by a mechanism involving increased oxidative stress and perturbed calcium homeostasis Exp Neurol 160 1999 28 39
    • (1999) Exp Neurol , vol.160 , pp. 28-39
    • Kruman, I.I.1    Pedersen, W.A.2    Springer, J.E.3    Mattson, M.P.4
  • 9
    • 0031931578 scopus 로고    scopus 로고
    • Riluzole preserves motor function in a transgenic model of familial amyotrophic lateral sclerosis
    • M.E. Gurney, T.J. Fleck, C.S. Himes, and E.D. Hall Riluzole preserves motor function in a transgenic model of familial amyotrophic lateral sclerosis Neurology 50 1998 62 66
    • (1998) Neurology , vol.50 , pp. 62-66
    • Gurney, M.E.1    Fleck, T.J.2    Himes, C.S.3    Hall, E.D.4
  • 10
    • 0029030610 scopus 로고
    • Selective loss of glial glutamate transporter GLT-1 in amyotrophic lateral sclerosis
    • J.D. Rothstein, M. Van Kammen, A.I. Levey, L.J. Martin, and R.W. Kuncl Selective loss of glial glutamate transporter GLT-1 in amyotrophic lateral sclerosis Ann Neurol 38 1995 73 84
    • (1995) Ann Neurol , vol.38 , pp. 73-84
    • Rothstein, J.D.1    Van Kammen, M.2    Levey, A.I.3    Martin, L.J.4    Kuncl, R.W.5
  • 11
    • 0034031598 scopus 로고    scopus 로고
    • Molecular factors underlying selective vulnerability of motor neurons to neurodegeneration in amyotrophic lateral sclerosis
    • P.J. Shaw, and C.J. Eggett Molecular factors underlying selective vulnerability of motor neurons to neurodegeneration in amyotrophic lateral sclerosis J Neurol 247 Suppl. 1 2000 I17 I27
    • (2000) J Neurol , vol.247 , Issue.SUPPL. 1
    • Shaw, P.J.1    Eggett, C.J.2
  • 12
    • 0037986558 scopus 로고    scopus 로고
    • The AMPA receptor antagonist NBQX prolongs survival in a transgenic mouse model of amyotrophic lateral sclerosis
    • P. Van Damme, M. Leyssen, G. Callewaert, W. Robberecht, and L. Van Den Bosch The AMPA receptor antagonist NBQX prolongs survival in a transgenic mouse model of amyotrophic lateral sclerosis Neurosci Lett 343 2003 81 84
    • (2003) Neurosci Lett , vol.343 , pp. 81-84
    • Van Damme, P.1    Leyssen, M.2    Callewaert, G.3    Robberecht, W.4    Van Den Bosch, L.5
  • 13
    • 33344469934 scopus 로고    scopus 로고
    • Kinesin-2 differentially regulates the anterograde axonal transports of acetylcholinesterase and choline acetyltransferase in Drosophila
    • R. Baqri, R. Charan, K. Schimmelpfeng, S. Chavan, and K. Ray Kinesin-2 differentially regulates the anterograde axonal transports of acetylcholinesterase and choline acetyltransferase in Drosophila J Neurobiol 66 2006 378 392
    • (2006) J Neurobiol , vol.66 , pp. 378-392
    • Baqri, R.1    Charan, R.2    Schimmelpfeng, K.3    Chavan, S.4    Ray, K.5
  • 14
    • 0033230363 scopus 로고    scopus 로고
    • Kinesin-II is required for axonal transport of choline acetyltransferase in Drosophila
    • K. Ray, S.E. Perez, Z. Yang, J. Xu, B.W. Ritchings, and H. Steller Kinesin-II is required for axonal transport of choline acetyltransferase in Drosophila J Cell Biol 147 1999 507 518
    • (1999) J Cell Biol , vol.147 , pp. 507-518
    • Ray, K.1    Perez, S.E.2    Yang, Z.3    Xu, J.4    Ritchings, B.W.5    Steller, H.6
  • 15
    • 77953609956 scopus 로고    scopus 로고
    • Alterations in subcellular localization of TDP-43 immunoreactivity in the anterior horns in sporadic amyotrophic lateral sclerosis
    • S. Sasaki, T. Takeda, N. Shibata, and M. Kobayashi Alterations in subcellular localization of TDP-43 immunoreactivity in the anterior horns in sporadic amyotrophic lateral sclerosis Neurosci Lett 478 2010 72 76
    • (2010) Neurosci Lett , vol.478 , pp. 72-76
    • Sasaki, S.1    Takeda, T.2    Shibata, N.3    Kobayashi, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.