메뉴 건너뛰기




Volumn 20, Issue 5-6, 2009, Pages 236-239

The current understanding of motor neuron disease

Author keywords

Amyotrophic lateral sclerosis; Dynein; Motor neuron disease; Protein aggregation; Superoxide dismutase

Indexed keywords

CHAPERONE; COPPER ZINC SUPEROXIDE DISMUTASE; HEAT SHOCK PROTEIN 70; MUTANT PROTEIN; RILUZOLE; SINGLE STRANDED RNA; SMALL INTERFERING RNA;

EID: 69649095389     PISSN: 09537112     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cacc.2009.07.009     Document Type: Article
Times cited : (3)

References (15)
  • 1
    • 69649102600 scopus 로고    scopus 로고
    • MND Association
    • MND Association, .
  • 2
    • 0033599646 scopus 로고    scopus 로고
    • Science, medicine and the future: motor neuron disease
    • Shaw P.J. Science, medicine and the future: motor neuron disease. BMJ 318 (1999) 1118-1121
    • (1999) BMJ , vol.318 , pp. 1118-1121
    • Shaw, P.J.1
  • 3
    • 0035139109 scopus 로고    scopus 로고
    • Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases
    • Sherman M.Y., and Goldberg A.L. Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases. Neuron 29 (2001) 15-32
    • (2001) Neuron , vol.29 , pp. 15-32
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 4
    • 53049109088 scopus 로고    scopus 로고
    • Complete loss of post-translational modification triggers fibrillar aggregation of SOD1 in fALS
    • Furukawa, Kaneko, Yamanaka, O'Halloran, and Nukina. Complete loss of post-translational modification triggers fibrillar aggregation of SOD1 in fALS. J Biol Chem 283 35 (2008) 24167-24176
    • (2008) J Biol Chem , vol.283 , Issue.35 , pp. 24167-24176
    • Furukawa1    Kaneko2    Yamanaka3    O'Halloran, Nukina,4
  • 5
    • 46749107070 scopus 로고    scopus 로고
    • The ER-Golgi pathway is a target for translocation and aggregation of mutant superoxide dismutase linked to ALS
    • Urushitani M., Abou Ezzi S., Matsuo A., Tooyama I., and Julien J.P. The ER-Golgi pathway is a target for translocation and aggregation of mutant superoxide dismutase linked to ALS. FASEB J 22 7 (2008) 2476-2487
    • (2008) FASEB J , vol.22 , Issue.7 , pp. 2476-2487
    • Urushitani, M.1    Abou Ezzi, S.2    Matsuo, A.3    Tooyama, I.4    Julien, J.P.5
  • 6
    • 38449116842 scopus 로고    scopus 로고
    • Superoxide dismutase 1 mutants related to amyotrophic lateral sclerosis induce endoplasmic stress in neuro2a cells
    • Oh Y.K., Shin K.S., Yuan J.Y., and Kang S.J. Superoxide dismutase 1 mutants related to amyotrophic lateral sclerosis induce endoplasmic stress in neuro2a cells. J Neurochem 4 (2008) 993-1005
    • (2008) J Neurochem , vol.4 , pp. 993-1005
    • Oh, Y.K.1    Shin, K.S.2    Yuan, J.Y.3    Kang, S.J.4
  • 7
    • 50849083264 scopus 로고    scopus 로고
    • Retrograde axonal transport and motor neuron disease
    • Ström, Gal, Shi, Kasarskis, Hayward, and Zhu. Retrograde axonal transport and motor neuron disease. J Neurochem 106 (2008) 405-505
    • (2008) J Neurochem , vol.106 , pp. 405-505
    • Ström1    Gal2    Shi3    Kasarskis4    Hayward5    Zhu6
  • 8
    • 52949094629 scopus 로고    scopus 로고
    • Novel mutations in TARDBP (TDP-43) in patients with familial amyotrophic lateral sclerosis
    • Rutherford N.J., Zhang Y.J., Baker M., Gass J.M., Finch N.A., Xu Y.F., et al. Novel mutations in TARDBP (TDP-43) in patients with familial amyotrophic lateral sclerosis. PLoS Genet 4 9 (2008) e1000193
    • (2008) PLoS Genet , vol.4 , Issue.9
    • Rutherford, N.J.1    Zhang, Y.J.2    Baker, M.3    Gass, J.M.4    Finch, N.A.5    Xu, Y.F.6
  • 9
    • 38449097283 scopus 로고    scopus 로고
    • The G59S mutation in p150glued causes dysfunction of dynactin in mice
    • Lai C., Lin X., Chandran J., Shim H., Yang W.J., and Cai H.B. The G59S mutation in p150glued causes dysfunction of dynactin in mice. J Neurosci 27 51 (2007) 13982-13990
    • (2007) J Neurosci , vol.27 , Issue.51 , pp. 13982-13990
    • Lai, C.1    Lin, X.2    Chandran, J.3    Shim, H.4    Yang, W.J.5    Cai, H.B.6
  • 10
    • 34948859426 scopus 로고    scopus 로고
    • Aging attenuates dynactin-dynein interaction: down-regulation of dynein causes accumulation of endogenous tau and amyloid precursor protein in human neuroblastoma cells
    • Kimura N., Imamura O., Ono F., and Terao K. Aging attenuates dynactin-dynein interaction: down-regulation of dynein causes accumulation of endogenous tau and amyloid precursor protein in human neuroblastoma cells. J Neurosci Res 85 (2007) 2909-2916
    • (2007) J Neurosci Res , vol.85 , pp. 2909-2916
    • Kimura, N.1    Imamura, O.2    Ono, F.3    Terao, K.4
  • 12
    • 47049099443 scopus 로고    scopus 로고
    • Therapeutic gene silencing delivered by a chemically modified small interfering RNA against mutant SOD1 slows amyotrophic lateral sclerosis progression
    • Wang H.Y., Ghosh A., Baigude H., Yang C.S., Qiu L.H., Xia X.G., et al. Therapeutic gene silencing delivered by a chemically modified small interfering RNA against mutant SOD1 slows amyotrophic lateral sclerosis progression. J Biol Chem 283 23 (2008) 15845-15852
    • (2008) J Biol Chem , vol.283 , Issue.23 , pp. 15845-15852
    • Wang, H.Y.1    Ghosh, A.2    Baigude, H.3    Yang, C.S.4    Qiu, L.H.5    Xia, X.G.6
  • 13
    • 1942486792 scopus 로고    scopus 로고
    • Treatment with arimoclomol, a coinducer of heat shock proteins, delays disease progression in ALS mice
    • Kieran D., Kalmar B., Dick J.R.T., Riddoch-Contreras J., Burnstock G., and Greensmith L. Treatment with arimoclomol, a coinducer of heat shock proteins, delays disease progression in ALS mice. Nat Med 10 (2004) 402-405
    • (2004) Nat Med , vol.10 , pp. 402-405
    • Kieran, D.1    Kalmar, B.2    Dick, J.R.T.3    Riddoch-Contreras, J.4    Burnstock, G.5    Greensmith, L.6
  • 14
    • 34547893834 scopus 로고    scopus 로고
    • Heat-shock protein 105 interacts with and suppresses aggregation of mutant Cu/Zn Superoxide dismutase: clues to a possible strategy for treating ALS
    • Yamashita H., Kawamata J., Okawa K., Kanki R., Nakamizo T., Hatayama T., et al. Heat-shock protein 105 interacts with and suppresses aggregation of mutant Cu/Zn Superoxide dismutase: clues to a possible strategy for treating ALS. J Neurochem 102 (2007) 1497-1505
    • (2007) J Neurochem , vol.102 , pp. 1497-1505
    • Yamashita, H.1    Kawamata, J.2    Okawa, K.3    Kanki, R.4    Nakamizo, T.5    Hatayama, T.6
  • 15
    • 33644551565 scopus 로고    scopus 로고
    • A motor neuron disease-associated mutation in p150glued perturbs dynactin function and induces protein aggregation
    • Levy J.R., Sumner C.J., Caviston J.P., Tokito M.K., Ranganathan S., Ligon L.A., et al. A motor neuron disease-associated mutation in p150glued perturbs dynactin function and induces protein aggregation. J Cell Biol 172 (2006) 733-745
    • (2006) J Cell Biol , vol.172 , pp. 733-745
    • Levy, J.R.1    Sumner, C.J.2    Caviston, J.P.3    Tokito, M.K.4    Ranganathan, S.5    Ligon, L.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.