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Volumn 16, Issue 18, 2010, Pages 2053-2073

Current nervous system related drug targets for the treatment of amyotrophic lateral sclerosis

Author keywords

Als; Amyotrophic lateral sclerosis; Drug targets; Heat shock; Neurodegeneration; Tdp 43

Indexed keywords

AMIODARONE; BENZOTHIAZOLE DERIVATIVE; BENZOXAZOLE DERIVATIVE; CENTRAL NERVOUS SYSTEM AGENTS; EXCITATORY AMINO ACID TRANSPORTER 2; FLUSPIRILENE; FUSED IN SARCOMA PROTEIN; GLUTAMIC ACID; HEAT SHOCK PROTEIN 27; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; KINESIN ASSOCIATED PROTEIN 3; LAMOTRIGINE; LITHIUM; LOPERAMIDE; MINOCYCLINE; NIGULDIPINE; NUCLEIC ACID BINDING PROTEIN; PIMOZIDE; PROTEASOME; RILUZOLE; RNA HELICASE; SENATAXIN; TAR DNA BINDING PROTEIN; TRANSLOCATION IN LIPOSARCOMA PROTEIN; TRIFLUOPERAZINE; UBIQUITIN; UNCLASSIFIED DRUG; UNINDEXED DRUG; VALPROIC ACID; VAMP ASSOCIATED PROTEIN B; COPPER ZINC SUPEROXIDE DISMUTASE; DNA BINDING PROTEIN; PROTEIN TDP-43; SUPEROXIDE DISMUTASE;

EID: 77953488668     PISSN: 13816128     EISSN: None     Source Type: Journal    
DOI: 10.2174/138161210791293024     Document Type: Article
Times cited : (8)

References (332)
  • 3
    • 0036290110 scopus 로고    scopus 로고
    • Cost effectiveness of treatments for amyotro-phic lateral sclerosis: A review of the literature
    • Ginsberg G, Lowe S. Cost effectiveness of treatments for amyotro-phic lateral sclerosis: a review of the literature. Pharmacoe-conomics 2002; 20: 367-87.
    • (2002) Pharmacoe-Conomics , vol.20 , pp. 367-387
    • Ginsberg, G.1    Lowe, S.2
  • 4
    • 0032843510 scopus 로고    scopus 로고
    • Cost effectiveness of riluzole in amyotrophic lateral sclerosis. Italian Cooperative Group for the Study of Meta-Analysis and the Osservatorio SIFO sui Farmaci
    • Messori A, Trippoli S, Becagli P, Zaccara G. Cost effectiveness of riluzole in amyotrophic lateral sclerosis. Italian Cooperative Group for the Study of Meta-Analysis and the Osservatorio SIFO sui Farmaci. Pharmacoeconomics 1999; 16: 153-63.
    • (1999) Pharmacoeconomics , vol.16 , pp. 153-163
    • Messori, A.1    Trippoli, S.2    Becagli, P.3    Zaccara, G.4
  • 5
    • 8844281519 scopus 로고    scopus 로고
    • The tolerability of riluzole in the treatment of patients with amyotrophic lateral sclerosis
    • Bensimon G, Doble A. The tolerability of riluzole in the treatment of patients with amyotrophic lateral sclerosis. Expert Opin Drug Saf 2004; 3: 525-34.
    • (2004) Expert Opin Drug Saf , vol.3 , pp. 525-534
    • Bensimon, G.1    Doble, A.2
  • 7
    • 65549128133 scopus 로고    scopus 로고
    • Muscle mitochondrial uncoupling dismantles neuromuscular junction and triggers distal degeneration of motor neurons
    • Dupuis L, Gonzalez de Aguilar JL, Echaniz-Laguna A, Eschbach J, Rene F, Oudart H, et al. Muscle mitochondrial uncoupling dismantles neuromuscular junction and triggers distal degeneration of motor neurons. PLoS One 2009; 4: e5390.
    • (2009) PLoS One , vol.4
    • Dupuis, L.1    Gonzalez de Aguilar, J.L.2    Echaniz-Laguna, A.3    Eschbach, J.4    Rene, F.5    Oudart, H.6
  • 8
  • 9
    • 65949094823 scopus 로고    scopus 로고
    • Neuromuscular junction destruction during amyotrophic lateral sclerosis: Insights from transgenic models
    • Dupuis L, Loeffler JP. Neuromuscular junction destruction during amyotrophic lateral sclerosis: insights from transgenic models. Curr Opin Pharmacol 2009; 9: 341-6.
    • (2009) Curr Opin Pharmacol , vol.9 , pp. 341-346
    • Dupuis, L.1    Loeffler, J.P.2
  • 10
    • 18044366164 scopus 로고    scopus 로고
    • The metabolic hypothesis in amyotrophic lateral sclerosis: Insights from mutant Cu/Zn-superoxide dismutase mice
    • Gonzalez de Aguilar JL, Dupuis L, Oudart H, Loeffler JP. The metabolic hypothesis in amyotrophic lateral sclerosis: insights from mutant Cu/Zn-superoxide dismutase mice. Biomed Pharmacother 2005; 59: 190-6.
    • (2005) Biomed Pharmacother , vol.59 , pp. 190-196
    • Gonzalez de Aguilar, J.L.1    Dupuis, L.2    Oudart, H.3    Loeffler, J.P.4
  • 13
    • 26244454729 scopus 로고    scopus 로고
    • Skeletal muscle in amyotrophic lateral sclerosis: Emerging concepts and therapeutic implications
    • Abmayr S, Weydt P. Skeletal muscle in amyotrophic lateral sclerosis: emerging concepts and therapeutic implications. Phys Med Rehabil Clin N Am 2005; 16: 1091-7, xi-xii.
    • (2005) Phys Med Rehabil Clin N Am , vol.16
    • Abmayr, S.1    Weydt, P.2
  • 14
    • 71549164101 scopus 로고    scopus 로고
    • Oxidative stress sensitivity in ALS muscle cells
    • Dupuis L. Oxidative stress sensitivity in ALS muscle cells. Exp Neurol 2009; 220: 219-23.
    • (2009) Exp Neurol , vol.220 , pp. 219-223
    • Dupuis, L.1
  • 16
    • 77953078946 scopus 로고    scopus 로고
    • Counteracting muscle wasting in aging and neuromuscular diseases: The critical role of IGF-1
    • Scicchitano BM, Rizzuto E, Musaro A. Counteracting muscle wasting in aging and neuromuscular diseases: the critical role of IGF-1. Aging (Albany NY) 2009; 1: 451-7.
    • (2009) Aging (Albany NY) , vol.1 , pp. 451-457
    • Scicchitano, B.M.1    Rizzuto, E.2    Musaro, A.3
  • 17
    • 35348853257 scopus 로고    scopus 로고
    • TDP-43 proteinopathy in frontotemporal lobar degeneration and amyotrophic lateral sclerosis: Protein misfolding diseases without amyloidosis
    • Neumann M, Kwong LK, Sampathu DM, Trojanowski JQ, Lee VM. TDP-43 proteinopathy in frontotemporal lobar degeneration and amyotrophic lateral sclerosis: protein misfolding diseases without amyloidosis. Arch Neurol 2007; 64: 1388-94.
    • (2007) Arch Neurol , vol.64 , pp. 1388-1394
    • Neumann, M.1    Kwong, L.K.2    Sampathu, D.M.3    Trojanowski, J.Q.4    Lee, V.M.5
  • 18
    • 49249118746 scopus 로고    scopus 로고
    • TDP-43 is a culprit in human neurodegeneration, and not just an innocent bystander
    • Banks GT, Kuta A, Isaacs AM, Fisher EM. TDP-43 is a culprit in human neurodegeneration, and not just an innocent bystander. Mamm Genome 2008; 19: 299-305.
    • (2008) Mamm Genome , vol.19 , pp. 299-305
    • Banks, G.T.1    Kuta, A.2    Isaacs, A.M.3    Fisher, E.M.4
  • 19
    • 34447103093 scopus 로고    scopus 로고
    • TDP-43 proteinopathy: The neuropathology underlying major forms of sporadic and familial frontotemporal lobar degeneration and motor neuron disease
    • Kwong LK, Neumann M, Sampathu DM, Lee VM, Trojanowski JQ. TDP-43 proteinopathy: the neuropathology underlying major forms of sporadic and familial frontotemporal lobar degeneration and motor neuron disease. Acta Neuropathol 2007; 114: 63-70.
    • (2007) Acta Neuropathol , vol.114 , pp. 63-70
    • Kwong, L.K.1    Neumann, M.2    Sampathu, D.M.3    Lee, V.M.4    Trojanowski, J.Q.5
  • 20
    • 62149141328 scopus 로고    scopus 로고
    • Rethinking ALS: The FUS about TDP-43
    • Lagier-Tourenne C, Cleveland DW. Rethinking ALS: the FUS about TDP-43. Cell 2009; 136: 1001-4.
    • (2009) Cell , vol.136 , pp. 1001-1004
    • Lagier-Tourenne, C.1    Cleveland, D.W.2
  • 22
    • 77649252528 scopus 로고    scopus 로고
    • Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis
    • Pesiridis GS, Lee VM, Trojanowski JQ. Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis. Hum Mol Genet 2009; 18: R156-62.
    • (2009) Hum Mol Genet , vol.18
    • Pesiridis, G.S.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 23
    • 63949083624 scopus 로고    scopus 로고
    • Mimicking aspects of frontotemporal lobar degeneration and Lou Gehrig's disease in rats via TDP-43 overexpression
    • Tatom JB, Wang DB, Dayton RD, Skalli O, Hutton ML, Dickson DW, et al. Mimicking aspects of frontotemporal lobar degeneration and Lou Gehrig's disease in rats via TDP-43 overexpression. Mol Ther 2009; 17: 607-13.
    • (2009) Mol Ther , vol.17 , pp. 607-613
    • Tatom, J.B.1    Wang, D.B.2    Dayton, R.D.3    Skalli, O.4    Hutton, M.L.5    Dickson, D.W.6
  • 24
    • 67349271683 scopus 로고    scopus 로고
    • Depletion of TDP-43 affects Drosophila motoneurons terminal synapsis and locomotive behavior
    • Feiguin F, Godena VK, Romano G, D'Ambrogio A, Klima R, Baralle FE. Depletion of TDP-43 affects Drosophila motoneurons terminal synapsis and locomotive behavior. FEBS Lett 2009; 583: 1586-92.
    • (2009) FEBS Lett , vol.583 , pp. 1586-1592
    • Feiguin, F.1    Godena, V.K.2    Romano, G.3    D'Ambrogio, A.4    Klima, R.5    Baralle, F.E.6
  • 25
    • 17144426507 scopus 로고    scopus 로고
    • Human, Drosophila, and C.elegans TDP43: Nucleic acid binding properties and splicing regulatory function
    • Ayala YM, Pantano S, D'Ambrogio A, Buratti E, Brindisi A, Marchetti C, et al. Human, Drosophila, and C.elegans TDP43: nucleic acid binding properties and splicing regulatory function. J Mol Biol 2005; 348: 575-88.
    • (2005) J Mol Biol , vol.348 , pp. 575-588
    • Ayala, Y.M.1    Pantano, S.2    D'Ambrogio, A.3    Buratti, E.4    Brindisi, A.5    Marchetti, C.6
  • 26
    • 59549094064 scopus 로고    scopus 로고
    • Structural determinants of the cellular localization and shuttling of TDP-43
    • Ayala YM, Zago P, D'Ambrogio A, Xu YF, Petrucelli L, Buratti E, et al. Structural determinants of the cellular localization and shuttling of TDP-43. J Cell Sci 2008; 121: 3778-85.
    • (2008) J Cell Sci , vol.121 , pp. 3778-3785
    • Ayala, Y.M.1    Zago, P.2    D'Ambrogio, A.3    Xu, Y.F.4    Petrucelli, L.5    Buratti, E.6
  • 27
    • 0035965309 scopus 로고    scopus 로고
    • Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9
    • Buratti E, Baralle FE. Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9. J Biol Chem 2001; 276: 36337-43.
    • (2001) J Biol Chem , vol.276 , pp. 36337-36343
    • Buratti, E.1    Baralle, F.E.2
  • 28
    • 0035794665 scopus 로고    scopus 로고
    • Nuclear factor TDP-43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping
    • Buratti E, Dork T, Zuccato E, Pagani F, Romano M, Baralle FE. Nuclear factor TDP-43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping. EMBO J 2001; 20: 1774-84.
    • (2001) EMBO J , vol.20 , pp. 1774-1784
    • Buratti, E.1    Dork, T.2    Zuccato, E.3    Pagani, F.4    Romano, M.5    Baralle, F.E.6
  • 29
    • 70350454798 scopus 로고    scopus 로고
    • Rapamycin rescues TDP-43 mislocalization and the associated low molecular mass neurofilament instability
    • Caccamo A, Majumder S, Deng JJ, Bai Y, Thornton FB, Oddo S. Rapamycin rescues TDP-43 mislocalization and the associated low molecular mass neurofilament instability. J Biol Chem 2009; 284: 27416-24.
    • (2009) J Biol Chem , vol.284 , pp. 27416-27424
    • Caccamo, A.1    Majumder, S.2    Deng, J.J.3    Bai, Y.4    Thornton, F.B.5    Oddo, S.6
  • 30
    • 11344275763 scopus 로고    scopus 로고
    • A T3 allele in the CFTR gene exacerbates exon 9 skipping in vas deferens and epididymal cell lines and is associated with Congenital Bilateral Absence of Vas Deferens (CBAVD)
    • Disset A, Michot C, Harris A, Buratti E, Claustres M, Tuffery-Giraud S. A T3 allele in the CFTR gene exacerbates exon 9 skipping in vas deferens and epididymal cell lines and is associated with Congenital Bilateral Absence of Vas Deferens (CBAVD). Hum Mutat 2005; 25: 72-81.
    • (2005) Hum Mutat , vol.25 , pp. 72-81
    • Disset, A.1    Michot, C.2    Harris, A.3    Buratti, E.4    Claustres, M.5    Tuffery-Giraud, S.6
  • 31
    • 64549100193 scopus 로고    scopus 로고
    • Structural insights into TDP-43 in nucleic-acid binding and domain interactions
    • Kuo PH, Doudeva LG, Wang YT, Shen CK, Yuan HS. Structural insights into TDP-43 in nucleic-acid binding and domain interactions. Nucleic Acids Res 2009; 37: 1799-808.
    • (2009) Nucleic Acids Res , vol.37 , pp. 1799-1808
    • Kuo, P.H.1    Doudeva, L.G.2    Wang, Y.T.3    Shen, C.K.4    Yuan, H.S.5
  • 32
    • 27744554553 scopus 로고    scopus 로고
    • Depletion of TDP 43 overrides the need for exonic and intronic splicing enhancers in the human apoA-II gene
    • Mercado PA, Ayala YM, Romano M, Buratti E, Baralle FE. Depletion of TDP 43 overrides the need for exonic and intronic splicing enhancers in the human apoA-II gene. Nucleic Acids Res 2005; 33: 6000-10.
    • (2005) Nucleic Acids Res , vol.33 , pp. 6000-6010
    • Mercado, P.A.1    Ayala, Y.M.2    Romano, M.3    Buratti, E.4    Baralle, F.E.5
  • 33
    • 34249313704 scopus 로고    scopus 로고
    • Lack of TDP-43 abnormalities in mutant SOD1 transgenic mice shows disparity with ALS
    • Robertson J, Sanelli T, Xiao S, Yang W, Horne P, Hammond R, et al. Lack of TDP-43 abnormalities in mutant SOD1 transgenic mice shows disparity with ALS. Neurosci Lett 2007; 420: 128-32.
    • (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
  • 34
    • 65149101697 scopus 로고    scopus 로고
    • Mislocalization of TDP-43 in the G93A mutant SOD1 transgenic mouse model of ALS
    • Shan X, Vocadlo D, Krieger C. Mislocalization of TDP-43 in the G93A mutant SOD1 transgenic mouse model of ALS. Neurosci Lett 2009; 458: 70-4.
    • (2009) Neurosci Lett , vol.458 , pp. 70-74
    • Shan, X.1    Vocadlo, D.2    Krieger, C.3
  • 35
    • 68349125007 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis, frontotemporal dementia and beyond: The TDP-43 diseases
    • Geser F, Martinez-Lage M, Kwong LK, Lee VM, Trojanowski JQ. Amyotrophic lateral sclerosis, frontotemporal dementia and beyond: the TDP-43 diseases. J Neurol 2009; 256: 1205-14.
    • (2009) J Neurol , vol.256 , pp. 1205-1214
    • Geser, F.1    Martinez-Lage, M.2    Kwong, L.K.3    Lee, V.M.4    Trojanowski, J.Q.5
  • 36
    • 34249946466 scopus 로고    scopus 로고
    • Pathological TDP-43 distinguishes sporadic amyotrophic lateral sclerosis from amyotrophic lateral sclerosis with SOD1 mutations
    • Mackenzie IR, Bigio EH, Ince PG, Geser F, Neumann M, Cairns NJ, et al. Pathological TDP-43 distinguishes sporadic amyotrophic lateral sclerosis from amyotrophic lateral sclerosis with SOD1 mutations. Ann Neurol 2007; 61: 427-34.
    • (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
  • 38
    • 61349162349 scopus 로고    scopus 로고
    • Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6
    • Vance C, Rogelj B, Hortobagyi T, De Vos KJ, Nishimura AL, Sreedharan J, et al. Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6. Science 2009; 323: 1208-11.
    • (2009) Science , vol.323 , pp. 1208-1211
    • Vance, C.1    Rogelj, B.2    Hortobagyi, T.3    de Vos, K.J.4    Nishimura, A.L.5    Sreedharan, J.6
  • 40
    • 70350156915 scopus 로고    scopus 로고
    • Analysis of FUS gene mutation in familial amyotrophic lateral sclerosis within an Italian cohort
    • Ticozzi N, Silani V, LeClerc AL, Keagle P, Gellera C, Ratti A, et al. Analysis of FUS gene mutation in familial amyotrophic lateral sclerosis within an Italian cohort. Neurology 2009; 73: 1180-5.
    • (2009) Neurology , vol.73 , pp. 1180-1185
    • Ticozzi, N.1    Silani, V.2    Leclerc, A.L.3    Keagle, P.4    Gellera, C.5    Ratti, A.6
  • 42
    • 33747605320 scopus 로고    scopus 로고
    • Molecular biology of amyotrophic lateral sclerosis: Insights from genetics
    • Pasinelli P, Brown RH. Molecular biology of amyotrophic lateral sclerosis: insights from genetics. Nat Rev Neurosci 2006; 7: 710-23.
    • (2006) Nat Rev Neurosci , vol.7 , pp. 710-723
    • Pasinelli, P.1    Brown, R.H.2
  • 43
    • 33845615472 scopus 로고    scopus 로고
    • In cis autosomal dominant mutation of Senataxin associated with tremor/ataxia syndrome
    • Bassuk AG, Chen YZ, Batish SD, Nagan N, Opal P, Chance PF, et al. In cis autosomal dominant mutation of Senataxin associated with tremor/ataxia syndrome. Neurogenetics 2007; 8: 45-9.
    • (2007) Neurogenetics , vol.8 , pp. 45-49
    • Bassuk, A.G.1    Chen, Y.Z.2    Batish, S.D.3    Nagan, N.4    Opal, P.5    Chance, P.F.6
  • 44
    • 62549146705 scopus 로고    scopus 로고
    • A novel mutation in the senataxin gene identified in a Chinese patient with sporadic amyotrophic lateral sclerosis
    • Zhao ZH, Chen WZ, Wu ZY, Wang N, Zhao GX, Chen WJ, et al. A novel mutation in the senataxin gene identified in a Chinese patient with sporadic amyotrophic lateral sclerosis. Amyotroph Lateral Scler 2009; 10: 118-22.
    • (2009) Amyotroph Lateral Scler , vol.10 , pp. 118-122
    • Zhao, Z.H.1    Chen, W.Z.2    Wu, Z.Y.3    Wang, N.4    Zhao, G.X.5    Chen, W.J.6
  • 46
    • 0034666282 scopus 로고    scopus 로고
    • Neurofilaments are transported rapidly but intermittently in axons: Implications for slow axonal transport
    • Roy S, Coffee P, Smith G, Liem RK, Brady ST, Black MM. Neurofilaments are transported rapidly but intermittently in axons: implications for slow axonal transport. J Neurosci 2000; 20: 6849-61.
    • (2000) J Neurosci , vol.20 , pp. 6849-6861
    • Roy, S.1    Coffee, P.2    Smith, G.3    Liem, R.K.4    Brady, S.T.5    Black, M.M.6
  • 47
    • 0033776708 scopus 로고    scopus 로고
    • Rapid movement of axonal neurofilaments interrupted by prolonged pauses
    • Wang L, Ho CL, Sun D, Liem RK, Brown A. Rapid movement of axonal neurofilaments interrupted by prolonged pauses. Nat Cell Biol 2000; 2: 137-41.
    • (2000) Nat Cell Biol , vol.2 , pp. 137-141
    • Wang, L.1    Ho, C.L.2    Sun, D.3    Liem, R.K.4    Brown, A.5
  • 48
    • 60849093466 scopus 로고    scopus 로고
    • Current hypotheses for the underlying biology of amyotrophic lateral sclerosis
    • Rothstein JD. Current hypotheses for the underlying biology of amyotrophic lateral sclerosis. Ann Neurol 2009; 65 (Suppl 1): S3-9.
    • (2009) Ann Neurol , vol.65 , Issue.SUPPL. 1
    • Rothstein, J.D.1
  • 49
    • 27644591304 scopus 로고    scopus 로고
    • Axon degeneration mechanisms: Commonality amid diversity
    • Coleman M. Axon degeneration mechanisms: commonality amid diversity. Nat Rev Neurosci 2005; 6: 889-98.
    • (2005) Nat Rev Neurosci , vol.6 , pp. 889-898
    • Coleman, M.1
  • 50
    • 0027410516 scopus 로고
    • Increased expression of neurofilament subunit NF-L produces morphological alterations that resemble the pathology of human motor neuron disease
    • Xu Z, Cork LC, Griffin JW, Cleveland DW. Increased expression of neurofilament subunit NF-L produces morphological alterations that resemble the pathology of human motor neuron disease. Cell 1993; 73: 23-33.
    • (1993) Cell , vol.73 , pp. 23-33
    • Xu, Z.1    Cork, L.C.2    Griffin, J.W.3    Cleveland, D.W.4
  • 51
    • 0038632271 scopus 로고    scopus 로고
    • Defective neurofilament transport in mouse models of amyotrophic lateral sclerosis: A review
    • Rao MV, Nixon RA. Defective neurofilament transport in mouse models of amyotrophic lateral sclerosis: a review. Neurochem Res 2003; 28: 1041-7.
    • (2003) Neurochem Res , vol.28 , pp. 1041-1047
    • Rao, M.V.1    Nixon, R.A.2
  • 52
    • 23844448652 scopus 로고    scopus 로고
    • Loss of ALS2 function is insufficient to trigger motor neuron degeneration in knock-out mice but predisposes neurons to oxidative stress
    • Cai H, Lin X, Xie C, Laird FM, Lai C, Wen H, et al. Loss of ALS2 function is insufficient to trigger motor neuron degeneration in knock-out mice but predisposes neurons to oxidative stress. J Neurosci 2005; 25: 7567-74.
    • (2005) J Neurosci , vol.25 , pp. 7567-7574
    • Cai, H.1    Lin, X.2    Xie, C.3    Laird, F.M.4    Lai, C.5    Wen, H.6
  • 53
    • 31144448704 scopus 로고    scopus 로고
    • Mice deficient in the Rab5 guanine nucleotide exchange factor ALS2/alsin exhibit age-dependent neurological deficits and altered endosome trafficking
    • Hadano S, Benn SC, Kakuta S, Otomo A, Sudo K, Kunita R, et al. Mice deficient in the Rab5 guanine nucleotide exchange factor ALS2/alsin exhibit age-dependent neurological deficits and altered endosome trafficking. Hum Mol Genet 2006; 15: 233-50.
    • (2006) Hum Mol Genet , vol.15 , pp. 233-250
    • Hadano, S.1    Benn, S.C.2    Kakuta, S.3    Otomo, A.4    Sudo, K.5    Kunita, R.6
  • 56
    • 67049155508 scopus 로고    scopus 로고
    • Reduced expression of the Kinesin-Associated Protein 3 (KIFAP3) gene increases survival in sporadic amyotrophic lateral sclerosis
    • Landers JE, Melki J, Meininger V, Glass JD, van den Berg LH, van Es MA, et al. Reduced expression of the Kinesin-Associated Protein 3 (KIFAP3) gene increases survival in sporadic amyotrophic lateral sclerosis. Proc Natl Acad Sci USA 2009; 106: 9004-9.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 9004-9009
    • Landers, J.E.1    Melki, J.2    Meininger, V.3    Glass, J.D.4    van den Berg, L.H.5    van Es, M.A.6
  • 57
    • 0033754604 scopus 로고    scopus 로고
    • Stirring up development with the heterotrimeric kinesin KIF3
    • Hirokawa N. Stirring up development with the heterotrimeric kinesin KIF3. Traffic 2000; 1: 29-34.
    • (2000) Traffic , vol.1 , pp. 29-34
    • Hirokawa, N.1
  • 58
    • 0033826065 scopus 로고    scopus 로고
    • Differential screening of mutated SOD1 transgenic mice reveals early up-regulation of a fast axonal transport component in spinal cord motor neurons
    • Dupuis L, de Tapia M, Rene F, Lutz-Bucher B, Gordon JW, Mercken L, et al. Differential screening of mutated SOD1 transgenic mice reveals early up-regulation of a fast axonal transport component in spinal cord motor neurons. Neurobiol Dis 2000; 7: 274-85.
    • (2000) Neurobiol Dis , vol.7 , pp. 274-285
    • Dupuis, L.1    de Tapia, M.2    Rene, F.3    Lutz-Bucher, B.4    Gordon, J.W.5    Mercken, L.6
  • 60
    • 60549104791 scopus 로고    scopus 로고
    • Mutant SOD1 impairs axonal transport of choline acetyltransferase and acetylcholine release by sequestering KAP3
    • Tateno M, Kato S, Sakurai T, Nukina N, Takahashi R, Araki T. Mutant SOD1 impairs axonal transport of choline acetyltransferase and acetylcholine release by sequestering KAP3. Hum Mol Genet 2009; 18: 942-55.
    • (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
  • 61
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl FU. Molecular chaperones in cellular protein folding. Nature 1996; 381: 571-9.
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 62
    • 0030041936 scopus 로고    scopus 로고
    • Heat shock proteins increase resistance to apoptosis
    • Samali A, Cotter TG. Heat shock proteins increase resistance to apoptosis. Exp Cell Res 1996; 223: 163-70.
    • (1996) Exp Cell Res , vol.223 , pp. 163-170
    • Samali, A.1    Cotter, T.G.2
  • 63
    • 0034253533 scopus 로고    scopus 로고
    • Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome
    • Beere HM, Wolf BB, Cain K, Mosser DD, Mahboubi A, Kuwana T, et al. Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome. Nat Cell Biol 2000; 2: 469-75.
    • (2000) Nat Cell Biol , vol.2 , pp. 469-475
    • Beere, H.M.1    Wolf, B.B.2    Cain, K.3    Mosser, D.D.4    Mahboubi, A.5    Kuwana, T.6
  • 64
    • 84925565291 scopus 로고    scopus 로고
    • The Role of Heat Shock Proteins during Neurodegeneration in Alzheimer's, Parkinson's and Huntington's Disease
    • NCBI 2010
    • Wyttenbach A, Arrigo AP. The Role of Heat Shock Proteins during Neurodegeneration in Alzheimer's, Parkinson's and Huntington's Disease. In Madame Curie Bioscience Database; NCBI 2010.
    • Madame Curie Bioscience Database
    • Wyttenbach, A.1    Arrigo, A.P.2
  • 65
    • 0032535245 scopus 로고    scopus 로고
    • Regulation of the heat shock transcriptional response: Cross talk between a family of heat shock factors, molecular chaperones, and negative regulators
    • Morimoto RI. Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators. Genes Dev 1998; 12: 3788-96.
    • (1998) Genes Dev , vol.12 , pp. 3788-3796
    • Morimoto, R.I.1
  • 66
    • 17744372861 scopus 로고    scopus 로고
    • Roles of the heat shock transcription factors in regulation of the heat shock response and beyond
    • Pirkkala L, Nykanen P, Sistonen L. Roles of the heat shock transcription factors in regulation of the heat shock response and beyond. FASEB J 2001; 15: 1118-31.
    • (2001) FASEB J , vol.15 , pp. 1118-1131
    • Pirkkala, L.1    Nykanen, P.2    Sistonen, L.3
  • 67
    • 59249106080 scopus 로고    scopus 로고
    • Integrating the stress response: Lessons for neurodegenerative diseases from C. elegans
    • Prahlad V, Morimoto RI. Integrating the stress response: lessons for neurodegenerative diseases from C. elegans. Trends Cell Biol 2009; 19: 52-61.
    • (2009) Trends Cell Biol , vol.19 , pp. 52-61
    • Prahlad, V.1    Morimoto, R.I.2
  • 68
    • 0037707633 scopus 로고    scopus 로고
    • High threshold for induction of the stress response in motor neurons is associated with failure to activate HSF1
    • Batulan Z, Shinder GA, Minotti S, He BP, Doroudchi MM, Nalbantoglu J, et al. High threshold for induction of the stress response in motor neurons is associated with failure to activate HSF1. J Neurosci 2003; 23: 5789-98.
    • (2003) J Neurosci , vol.23 , pp. 5789-5798
    • Batulan, Z.1    Shinder, G.A.2    Minotti, S.3    He, B.P.4    Doroudchi, M.M.5    Nalbantoglu, J.6
  • 69
    • 33749989045 scopus 로고    scopus 로고
    • Induction of multiple heat shock proteins and neuroprotection in a primary culture model of familial amyotrophic lateral sclerosis
    • Batulan Z, Taylor DM, Aarons RJ, Minotti S, Doroudchi MM, Nalbantoglu J, et al. Induction of multiple heat shock proteins and neuroprotection in a primary culture model of familial amyotrophic lateral sclerosis. Neurobiol Dis 2006; 24: 213-25.
    • (2006) Neurobiol Dis , vol.24 , pp. 213-225
    • Batulan, Z.1    Taylor, D.M.2    Aarons, R.J.3    Minotti, S.4    Doroudchi, M.M.5    Nalbantoglu, J.6
  • 70
    • 0026291437 scopus 로고
    • Expression of heat shock genes (hsp70) in the mammalian nervous system
    • Brown IR. Expression of heat shock genes (hsp70) in the mammalian nervous system. Results Probl Cell Differ 1991; 17: 217-29.
    • (1991) Results Probl Cell Differ , vol.17 , pp. 217-229
    • Brown, I.R.1
  • 71
    • 36849005504 scopus 로고    scopus 로고
    • Exogenous delivery of heat shock protein 70 increases lifespan in a mouse model of amyotrophic lateral sclerosis
    • Gifondorwa DJ, Robinson MB, Hayes CD, Taylor AR, Prevette DM, Oppenheim RW, et al. Exogenous delivery of heat shock protein 70 increases lifespan in a mouse model of amyotrophic lateral sclerosis. J Neurosci 2007; 27: 13173-80.
    • (2007) J Neurosci , vol.27 , pp. 13173-13180
    • Gifondorwa, D.J.1    Robinson, M.B.2    Hayes, C.D.3    Taylor, A.R.4    Prevette, D.M.5    Oppenheim, R.W.6
  • 72
    • 63449114950 scopus 로고    scopus 로고
    • Activation of the heat shock response in a primary cellular model of motoneuron neurodegeneration-evidence for neuroprotective and neurotoxic effects
    • Kalmar B, Greensmith L. Activation of the heat shock response in a primary cellular model of motoneuron neurodegeneration-evidence for neuroprotective and neurotoxic effects. Cell Mol Biol Lett 2009; 14: 319-35.
    • (2009) Cell Mol Biol Lett , vol.14 , pp. 319-335
    • Kalmar, B.1    Greensmith, L.2
  • 73
    • 53149114499 scopus 로고    scopus 로고
    • Late stage treatment with arimoclomol delays disease progression and prevents protein aggregation in the SOD1 mouse model of ALS
    • Kalmar B, Novoselov S, Gray A, Cheetham ME, Margulis B, Greensmith L. Late stage treatment with arimoclomol delays disease progression and prevents protein aggregation in the SOD1 mouse model of ALS. J Neurochem 2008; 107: 339-50.
    • (2008) J Neurochem , vol.107 , pp. 339-350
    • Kalmar, B.1    Novoselov, S.2    Gray, A.3    Cheetham, M.E.4    Margulis, B.5    Greensmith, L.6
  • 74
    • 0037173038 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis: A proposed mechanism
    • Okado-Matsumoto A, Fridovich I. Amyotrophic lateral sclerosis: a proposed mechanism. Proc Natl Acad Sci USA 2002; 99: 9010-4.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 9010-9014
    • Okado-Matsumoto, A.1    Fridovich, I.2
  • 75
    • 3042817421 scopus 로고    scopus 로고
    • CHIP promotes proteasomal degradation of familial ALS-linked mutant SOD1 by ubiquitinating Hsp/Hsc70
    • Urushitani M, Kurisu J, Tateno M, Hatakeyama S, Nakayama K, Kato S, et al. CHIP promotes proteasomal degradation of familial ALS-linked mutant SOD1 by ubiquitinating Hsp/Hsc70. J Neurochem 2004; 90: 231-44.
    • (2004) J Neurochem , vol.90 , pp. 231-244
    • Urushitani, M.1    Kurisu, J.2    Tateno, M.3    Hatakeyama, S.4    Nakayama, K.5    Kato, S.6
  • 76
    • 56149106877 scopus 로고    scopus 로고
    • Hsp60 expression, new locations, functions and perspectives for cancer diagnosis and therapy
    • Cappello F, de Macario EC, Marasa L, Zummo G, Macario AJ. Hsp60 expression, new locations, functions and perspectives for cancer diagnosis and therapy. Cancer Biol Ther 2008; 7: 801-9.
    • (2008) Cancer Biol Ther , vol.7 , pp. 801-809
    • Cappello, F.1    de Macario, E.C.2    Marasa, L.3    Zummo, G.4    Macario, A.J.5
  • 77
    • 0030225159 scopus 로고    scopus 로고
    • Exogenous heat shock cognate protein Hsc 70 prevents axotomy-induced death of spinal sensory neurons
    • Houenou LJ, Li L, Lei M, Kent CR, Tytell M. Exogenous heat shock cognate protein Hsc 70 prevents axotomy-induced death of spinal sensory neurons. Cell Stress Chaperones 1996; 1: 161-6.
    • (1996) Cell Stress Chaperones , vol.1 , pp. 161-166
    • Houenou, L.J.1    Li, L.2    Lei, M.3    Kent, C.R.4    Tytell, M.5
  • 78
    • 38149065825 scopus 로고    scopus 로고
    • Exogenous Hsc70, but not thermal preconditioning, confers protection to motoneurons subjected to oxidative stress
    • Robinson MB, Taylor AR, Gifondorwa DJ, Tytell M, Milligan CE. Exogenous Hsc70, but not thermal preconditioning, confers protection to motoneurons subjected to oxidative stress. Dev Neurobiol 2008; 68: 1-17.
    • (2008) Dev Neurobiol , vol.68 , pp. 1-17
    • Robinson, M.B.1    Taylor, A.R.2    Gifondorwa, D.J.3    Tytell, M.4    Milligan, C.E.5
  • 80
    • 1242269219 scopus 로고    scopus 로고
    • Mechanisms for regulation of Hsp70 function by Hsp40
    • Fan CY, Lee S, Cyr DM. Mechanisms for regulation of Hsp70 function by Hsp40. Cell Stress Chaperones 2003; 8: 309-16.
    • (2003) Cell Stress Chaperones , vol.8 , pp. 309-316
    • Fan, C.Y.1    Lee, S.2    Cyr, D.M.3
  • 81
    • 0036142488 scopus 로고    scopus 로고
    • Synergistic induction of HSP40 and HSC70 in the mouse hippocampal neurons after cerebral ischemia and ischemic tolerance in gerbil hippocampus
    • Tanaka S, Kitagawa K, Ohtsuki T, Yagita Y, Takasawa K, Hori M, et al. Synergistic induction of HSP40 and HSC70 in the mouse hippocampal neurons after cerebral ischemia and ischemic tolerance in gerbil hippocampus. J Neurosci Res 2002; 67: 37-47.
    • (2002) J Neurosci Res , vol.67 , pp. 37-47
    • Tanaka, S.1    Kitagawa, K.2    Ohtsuki, T.3    Yagita, Y.4    Takasawa, K.5    Hori, M.6
  • 82
    • 0031945665 scopus 로고    scopus 로고
    • Structure, function and evolution of DnaJ: Conservation and adaptation of chaperone function
    • Cheetham ME, Caplan AJ. Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function. Cell Stress Chaperones 1998; 3: 28-36.
    • (1998) Cell Stress Chaperones , vol.3 , pp. 28-36
    • Cheetham, M.E.1    Caplan, A.J.2
  • 83
    • 0028940309 scopus 로고
    • Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo
    • Jakob U, Lilie H, Meyer I, Buchner J. Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo. J Biol Chem 1995; 270: 7288-94.
    • (1995) J Biol Chem , vol.270 , pp. 7288-7294
    • Jakob, U.1    Lilie, H.2    Meyer, I.3    Buchner, J.4
  • 84
    • 0027439595 scopus 로고
    • Identification of a 60-kilodalton stress-related protein, p60, which interacts with hsp90 and hsp70
    • Smith DF, Sullivan WP, Marion TN, Zaitsu K, Madden B, McCormick DJ, et al. Identification of a 60-kilodalton stress-related protein, p60, which interacts with hsp90 and hsp70. Mol Cell Biol 1993; 13: 869-76.
    • (1993) Mol Cell Biol , vol.13 , pp. 869-876
    • Smith, D.F.1    Sullivan, W.P.2    Marion, T.N.3    Zaitsu, K.4    Madden, B.5    McCormick, D.J.6
  • 85
    • 0036566675 scopus 로고    scopus 로고
    • Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin
    • Wyttenbach A, Sauvageot O, Carmichael J, Diaz-Latoud C, Arrigo AP, Rubinsztein DC. Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin. Hum Mol Genet 2002; 11: 1137-51.
    • (2002) Hum Mol Genet , vol.11 , pp. 1137-1151
    • Wyttenbach, A.1    Sauvageot, O.2    Carmichael, J.3    Diaz-Latoud, C.4    Arrigo, A.P.5    Rubinsztein, D.C.6
  • 86
    • 1642356755 scopus 로고    scopus 로고
    • HSP27 but not HSP70 has a potent protective effect against alpha-synuclein-induced cell death in mammalian neuronal cells
    • Zourlidou A, Payne Smith MD, Latchman DS. HSP27 but not HSP70 has a potent protective effect against alpha-synuclein-induced cell death in mammalian neuronal cells. J Neurochem 2004; 88: 1439-48.
    • (2004) J Neurochem , vol.88 , pp. 1439-1448
    • Zourlidou, A.1    Payne Smith, M.D.2    Latchman, D.S.3
  • 87
    • 0037179756 scopus 로고    scopus 로고
    • Hsp27 upregulation and phosphorylation is required for injured sensory and motor neuron survival
    • Benn SC, Perrelet D, Kato AC, Scholz J, Decosterd I, Mannion RJ, et al. Hsp27 upregulation and phosphorylation is required for injured sensory and motor neuron survival. Neuron 2002; 36: 45-56.
    • (2002) Neuron , vol.36 , pp. 45-56
    • Benn, S.C.1    Perrelet, D.2    Kato, A.C.3    Scholz, J.4    Decosterd, I.5    Mannion, R.J.6
  • 88
    • 0346665904 scopus 로고    scopus 로고
    • Heat shock protein 27 delivered via a herpes simplex virus vector can protect neurons of the hippocampus against kainic-acid-induced cell loss
    • Kalwy SA, Akbar MT, Coffin RS, de Belleroche J, Latchman DS. Heat shock protein 27 delivered via a herpes simplex virus vector can protect neurons of the hippocampus against kainic-acid-induced cell loss. Brain Res Mol Brain Res 2003; 111: 91-103.
    • (2003) Brain Res Mol Brain Res , vol.111 , pp. 91-103
    • Kalwy, S.A.1    Akbar, M.T.2    Coffin, R.S.3    de Belleroche, J.4    Latchman, D.S.5
  • 92
    • 0034724792 scopus 로고    scopus 로고
    • Benign focal ischemic preconditioning induces neuronal Hsp70 and prolonged astrogliosis with expression of Hsp27
    • Currie RW, Ellison JA, White RF, Feuerstein GZ, Wang X, Barone FC. Benign focal ischemic preconditioning induces neuronal Hsp70 and prolonged astrogliosis with expression of Hsp27. Brain Res 2000; 863: 169-81.
    • (2000) Brain Res , vol.863 , pp. 169-181
    • Currie, R.W.1    Ellison, J.A.2    White, R.F.3    Feuerstein, G.Z.4    Wang, X.5    Barone, F.C.6
  • 93
    • 0031657749 scopus 로고    scopus 로고
    • Ischemic preconditioning and brain tolerance: Temporal histological and functional outcomes, protein synthesis requirement, and interleukin-1 receptor antagonist and early gene expression
    • discussion 1950-1
    • Barone FC, White RF, Spera PA, Ellison J, Currie RW, Wang X, et al. Ischemic preconditioning and brain tolerance: temporal histological and functional outcomes, protein synthesis requirement, and interleukin-1 receptor antagonist and early gene expression. Stroke 1998; 29: 1937-50; discussion 1950-1.
    • (1998) Stroke , vol.29 , pp. 1937-1950
    • Barone, F.C.1    White, R.F.2    Spera, P.A.3    Ellison, J.4    Currie, R.W.5    Wang, X.6
  • 94
    • 0037426594 scopus 로고    scopus 로고
    • Changes in heat shock protein 27 phosphorylation and immunocontent in response to preconditioning to oxygen and glucose deprivation in organotypic hippocampal cultures
    • Valentim LM, Rodnight R, Geyer AB, Horn AP, Tavares A, Cimarosti H, et al. Changes in heat shock protein 27 phosphorylation and immunocontent in response to preconditioning to oxygen and glucose deprivation in organotypic hippocampal cultures. Neuroscience 2003; 118: 379-86.
    • (2003) Neuroscience , vol.118 , pp. 379-386
    • Valentim, L.M.1    Rodnight, R.2    Geyer, A.B.3    Horn, A.P.4    Tavares, A.5    Cimarosti, H.6
  • 95
    • 0032825969 scopus 로고    scopus 로고
    • Ischaemic pre-conditioning in organotypic hippocampal slice cultures is inversely correlated to the induction of the 72 kDa heat shock protein (HSP72)
    • Pringle AK, Thomas SJ, Signorelli F, Iannotti F. Ischaemic pre-conditioning in organotypic hippocampal slice cultures is inversely correlated to the induction of the 72 kDa heat shock protein (HSP72). Brain Res 1999; 845: 152-64.
    • (1999) Brain Res , vol.845 , pp. 152-164
    • Pringle, A.K.1    Thomas, S.J.2    Signorelli, F.3    Iannotti, F.4
  • 96
    • 34548239171 scopus 로고    scopus 로고
    • Genetic variant in the HSPB1 promoter region impairs the HSP27 stress response
    • Dierick I, Irobi J, Janssens S, Theuns J, Lemmens R, Jacobs A, et al. Genetic variant in the HSPB1 promoter region impairs the HSP27 stress response. Hum Mutat 2007; 28: 830.
    • (2007) Hum Mutat , vol.28 , pp. 830
    • Dierick, I.1    Irobi, J.2    Janssens, S.3    Theuns, J.4    Lemmens, R.5    Jacobs, A.6
  • 98
    • 17044403380 scopus 로고    scopus 로고
    • Hsp27 and Hsp70 administered in combination have a potent protective effect against FALS-associated SOD1-mutant-induced cell death in mammalian neuronal cells
    • Patel YJ, Payne Smith MD, de Belleroche J, Latchman DS. Hsp27 and Hsp70 administered in combination have a potent protective effect against FALS-associated SOD1-mutant-induced cell death in mammalian neuronal cells. Brain Res Mol Brain Res 2005; 134: 256-74.
    • (2005) Brain Res Mol Brain Res , vol.134 , pp. 256-274
    • Patel, Y.J.1    Payne Smith, M.D.2    de Belleroche, J.3    Latchman, D.S.4
  • 99
    • 33750089740 scopus 로고    scopus 로고
    • Degradation of amyotrophic lateral sclerosis-linked mutant Cu,Zn-superoxide dismutase proteins by macroautophagy and the proteasome
    • Kabuta T, Suzuki Y, Wada K. Degradation of amyotrophic lateral sclerosis-linked mutant Cu,Zn-superoxide dismutase proteins by macroautophagy and the proteasome. J Biol Chem 2006; 281: 30524-33.
    • (2006) J Biol Chem , vol.281 , pp. 30524-30533
    • Kabuta, T.1    Suzuki, Y.2    Wada, K.3
  • 100
    • 6344275803 scopus 로고    scopus 로고
    • Activation of chaperone-mediated autophagy during oxidative stress
    • Kiffin R, Christian C, Knecht E, Cuervo AM. Activation of chaperone-mediated autophagy during oxidative stress. Mol Biol Cell 2004; 15: 4829-40.
    • (2004) Mol Biol Cell , vol.15 , pp. 4829-4840
    • Kiffin, R.1    Christian, C.2    Knecht, E.3    Cuervo, A.M.4
  • 101
    • 0036591852 scopus 로고    scopus 로고
    • Formation of hydrogen peroxide and hydroxyl radicals from A(beta) and alpha-synuclein as a possible mechanism of cell death in Alzheimer's disease and Parkinson's disease
    • Tabner BJ, Turnbull S, El-Agnaf OM, Allsop D. Formation of hydrogen peroxide and hydroxyl radicals from A(beta) and alpha-synuclein as a possible mechanism of cell death in Alzheimer's disease and Parkinson's disease. Free Radic Biol Med 2002; 32: 1076-83.
    • (2002) Free Radic Biol Med , vol.32 , pp. 1076-1083
    • Tabner, B.J.1    Turnbull, S.2    El-Agnaf, O.M.3    Allsop, D.4
  • 103
    • 0034682748 scopus 로고    scopus 로고
    • Heat shock protein 70 inhibits apoptosis downstream of cytochrome c release and upstream of caspase-3 activation
    • Li CY, Lee JS, Ko YG, Kim JI, Seo JS. Heat shock protein 70 inhibits apoptosis downstream of cytochrome c release and upstream of caspase-3 activation. J Biol Chem 2000; 275: 25665-71.
    • (2000) J Biol Chem , vol.275 , pp. 25665-25671
    • Li, C.Y.1    Lee, J.S.2    Ko, Y.G.3    Kim, J.I.4    Seo, J.S.5
  • 104
    • 0034664030 scopus 로고    scopus 로고
    • Negative regulation of cytochrome c-mediated oligomerization of Apaf-1 and activation of procaspase-9 by heat shock protein 90
    • Pandey P, Saleh A, Nakazawa A, Kumar S, Srinivasula SM, Kumar V, et al. Negative regulation of cytochrome c-mediated oligomerization of Apaf-1 and activation of procaspase-9 by heat shock protein 90. EMBO J 2000; 19: 4310-22.
    • (2000) EMBO J , vol.19 , pp. 4310-4322
    • Pandey, P.1    Saleh, A.2    Nakazawa, A.3    Kumar, S.4    Srinivasula, S.M.5    Kumar, V.6
  • 105
    • 0034512869 scopus 로고    scopus 로고
    • The interaction of HSP27 with Daxx identifies a potential regulatory role of HSP27 in Fas-induced apoptosis
    • Charette SJ, Landry J. The interaction of HSP27 with Daxx identifies a potential regulatory role of HSP27 in Fas-induced apoptosis. Ann N Y Acad Sci 2000; 926: 126-31.
    • (2000) Ann N Y Acad Sci , vol.926 , pp. 126-131
    • Charette, S.J.1    Landry, J.2
  • 106
    • 4344674075 scopus 로고    scopus 로고
    • Role of heat shock proteins during polyglutamine neurodegeneration: Mechanisms and hypothesis
    • Wyttenbach A. Role of heat shock proteins during polyglutamine neurodegeneration: mechanisms and hypothesis. J Mol Neurosci 2004; 23: 69-96.
    • (2004) J Mol Neurosci , vol.23 , pp. 69-96
    • Wyttenbach, A.1
  • 107
    • 25844466597 scopus 로고    scopus 로고
    • Heat shock response modulators as therapeutic tools for diseases of protein conformation
    • Westerheide SD, Morimoto RI. Heat shock response modulators as therapeutic tools for diseases of protein conformation. J Biol Chem 2005; 280: 33097-100.
    • (2005) J Biol Chem , vol.280 , pp. 33097-33100
    • Westerheide, S.D.1    Morimoto, R.I.2
  • 108
    • 0344507132 scopus 로고    scopus 로고
    • Up-regulation of protein chaperones preserves viability of cells expressing toxic Cu/Zn-superoxide dismutase mutants associated with amyotrophic lateral sclerosis
    • Bruening W, Roy J, Giasson B, Figlewicz DA, Mushynski WE, Durham HD. Up-regulation of protein chaperones preserves viability of cells expressing toxic Cu/Zn-superoxide dismutase mutants associated with amyotrophic lateral sclerosis. J Neurochem 1999; 72: 693-9.
    • (1999) J Neurochem , vol.72 , pp. 693-699
    • Bruening, W.1    Roy, J.2    Giasson, B.3    Figlewicz, D.A.4    Mushynski, W.E.5    Durham, H.D.6
  • 110
    • 0032146775 scopus 로고    scopus 로고
    • Increased production of amyloid precursor protein provides a substrate for caspase-3 in dying motoneurons
    • Barnes NY, Li L, Yoshikawa K, Schwartz LM, Oppenheim RW, Milligan CE. Increased production of amyloid precursor protein provides a substrate for caspase-3 in dying motoneurons. J Neurosci 1998; 18: 5869-80.
    • (1998) J Neurosci , vol.18 , pp. 5869-5880
    • Barnes, N.Y.1    Li, L.2    Yoshikawa, K.3    Schwartz, L.M.4    Oppenheim, R.W.5    Milligan, C.E.6
  • 111
    • 0036318499 scopus 로고    scopus 로고
    • Upregulation of heat shock proteins rescues motoneurones from axotomy-induced cell death in neonatal rats
    • Kalmar B, Burnstock G, Vrbova G, Urbanics R, Csermely P, Greensmith L. Upregulation of heat shock proteins rescues motoneurones from axotomy-induced cell death in neonatal rats. Exp Neurol 2002; 176: 87-97.
    • (2002) Exp Neurol , vol.176 , pp. 87-97
    • Kalmar, B.1    Burnstock, G.2    Vrbova, G.3    Urbanics, R.4    Csermely, P.5    Greensmith, L.6
  • 112
    • 0031758859 scopus 로고    scopus 로고
    • Involvement of specific caspases in motoneuron cell death in vivo and in vitro following trophic factor deprivation
    • Li L, Prevette D, Oppenheim RW, Milligan CE. Involvement of specific caspases in motoneuron cell death in vivo and in vitro following trophic factor deprivation. Mol Cell Neurosci 1998; 12: 157-67.
    • (1998) Mol Cell Neurosci , vol.12 , pp. 157-167
    • Li, L.1    Prevette, D.2    Oppenheim, R.W.3    Milligan, C.E.4
  • 113
    • 0029092507 scopus 로고
    • Peptide inhibitors of the ICE protease family arrest programmed cell death of motoneurons in vivo and in vitro
    • Milligan CE, Prevette D, Yaginuma H, Homma S, Cardwell C, Fritz LC, et al. Peptide inhibitors of the ICE protease family arrest programmed cell death of motoneurons in vivo and in vitro. Neuron 1995; 15: 385-93.
    • (1995) Neuron , vol.15 , pp. 385-393
    • Milligan, C.E.1    Prevette, D.2    Yaginuma, H.3    Homma, S.4    Cardwell, C.5    Fritz, L.C.6
  • 114
    • 0031148590 scopus 로고    scopus 로고
    • Differential effects of axotomy on the in vivo synthesis of the stress-inducible and constitutive 70-kDa heat-shock proteins in rat dorsal root ganglia
    • Tedeschi B, Ciavarra RP. Differential effects of axotomy on the in vivo synthesis of the stress-inducible and constitutive 70-kDa heat-shock proteins in rat dorsal root ganglia. Brain Res Mol Brain Res 1997; 45: 199-206.
    • (1997) Brain Res Mol Brain Res , vol.45 , pp. 199-206
    • Tedeschi, B.1    Ciavarra, R.P.2
  • 115
    • 0035664213 scopus 로고    scopus 로고
    • Histological evidence of protein aggregation in mutant SOD1 transgenic mice and in amyotrophic lateral sclerosis neural tissues
    • Watanabe M, Dykes-Hoberg M, Culotta VC, Price DL, Wong PC, Rothstein JD. Histological evidence of protein aggregation in mutant SOD1 transgenic mice and in amyotrophic lateral sclerosis neural tissues. Neurobiol Dis 2001; 8: 933-41.
    • (2001) Neurobiol Dis , vol.8 , pp. 933-941
    • Watanabe, M.1    Dykes-Hoberg, M.2    Culotta, V.C.3    Price, D.L.4    Wong, P.C.5    Rothstein, J.D.6
  • 116
  • 117
    • 0034113617 scopus 로고    scopus 로고
    • HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokine
    • Asea A, Kraeft SK, Kurt-Jones EA, Stevenson MA, Chen LB, Finberg RW, et al. HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokine. Nat Med 2000; 6: 435-42.
    • (2000) Nat Med , vol.6 , pp. 435-442
    • Asea, A.1    Kraeft, S.K.2    Kurt-Jones, E.A.3    Stevenson, M.A.4    Chen, L.B.5    Finberg, R.W.6
  • 118
    • 0033120990 scopus 로고    scopus 로고
    • Cutting edge: Receptor-mediated endocytosis of heat shock proteins by professional antigen-presenting cells
    • Arnold-Schild D, Hanau D, Spehner D, Schmid C, Rammensee HG, de la Salle H, et al. Cutting edge: receptor-mediated endocytosis of heat shock proteins by professional antigen-presenting cells. J Immunol 1999; 162: 3757-60.
    • (1999) J Immunol , vol.162 , pp. 3757-3760
    • Arnold-Schild, D.1    Hanau, D.2    Spehner, D.3    Schmid, C.4    Rammensee, H.G.5    de la Salle, H.6
  • 119
    • 20244367890 scopus 로고    scopus 로고
    • Bimoclomol: A nontoxic, hydroxylamine derivative with stress protein-inducing activity and cytoprotective effects
    • Vigh L, Literati PN, Horvath I, Torok Z, Balogh G, Glatz A, et al. Bimoclomol: a nontoxic, hydroxylamine derivative with stress protein-inducing activity and cytoprotective effects. Nat Med 1997; 3: 1150-4.
    • (1997) Nat Med , vol.3 , pp. 1150-1154
    • Vigh, L.1    Literati, P.N.2    Horvath, I.3    Torok, Z.4    Balogh, G.5    Glatz, A.6
  • 120
    • 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 JR, Riddoch-Contreras J, Burnstock G, Greensmith L. Treatment with arimoclomol, a coinducer of heat shock proteins, delays disease progression in ALS mice. Nat Med 2004; 10: 402-5.
    • (2004) Nat Med , vol.10 , pp. 402-405
    • Kieran, D.1    Kalmar, B.2    Dick, J.R.3    Riddoch-Contreras, J.4    Burnstock, G.5    Greensmith, L.6
  • 121
    • 65149106747 scopus 로고    scopus 로고
    • Chloro-oxime derivatives as novel small molecule chaperone amplifiers
    • Zhou Y, Vu K, Chen Y, Pham J, Brady T, Liu G, et al. Chloro-oxime derivatives as novel small molecule chaperone amplifiers. Bioorg Med Chem Lett 2009; 19: 3128-35.
    • (2009) Bioorg Med Chem Lett , vol.19 , pp. 3128-3135
    • Zhou, Y.1    Vu, K.2    Chen, Y.3    Pham, J.4    Brady, T.5    Liu, G.6
  • 122
    • 3242671372 scopus 로고    scopus 로고
    • A field guide to ubiquitylation
    • Fang S, Weissman AM. A field guide to ubiquitylation. Cell Mol Life Sci 2004; 61: 1546-61.
    • (2004) Cell Mol Life Sci , vol.61 , pp. 1546-1561
    • Fang, S.1    Weissman, A.M.2
  • 124
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart CM. Mechanisms underlying ubiquitination. Annu Rev Biochem 2001; 70: 503-33.
    • (2001) Annu Rev Biochem , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 125
    • 0035292759 scopus 로고    scopus 로고
    • Themes and variations on ubiquitylation
    • Weissman AM. Themes and variations on ubiquitylation. Nat Rev Mol Cell Biol 2001; 2: 169-78.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 169-178
    • Weissman, A.M.1
  • 126
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman MH, Ciechanover A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol Rev 2002; 82: 373-428.
    • (2002) Physiol Rev , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 127
    • 44649101850 scopus 로고    scopus 로고
    • Atypical ubiquitin chains: New molecular signals. 'protein modifications: Beyond the usual suspects' review series
    • Ikeda F, Dikic I. Atypical ubiquitin chains: new molecular signals. 'protein modifications: beyond the usual suspects' review series. EMBO Rep 2008; 9: 536-42.
    • (2008) EMBO Rep , vol.9 , pp. 536-542
    • Ikeda, F.1    Dikic, I.2
  • 128
    • 34547130325 scopus 로고    scopus 로고
    • Certain pairs of ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s) synthesize nondegradable forked ubiquitin chains containing all possible isopeptide linkages
    • Kim HT, Kim KP, Lledias F, Kisselev AF, Scaglione KM, Skowyra D, et al. Certain pairs of ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s) synthesize nondegradable forked ubiquitin chains containing all possible isopeptide linkages. J Biol Chem 2007; 282: 17375-86.
    • (2007) J Biol Chem , vol.282 , pp. 17375-17386
    • Kim, H.T.1    Kim, K.P.2    Lledias, F.3    Kisselev, A.F.4    Scaglione, K.M.5    Skowyra, D.6
  • 129
    • 23144449208 scopus 로고    scopus 로고
    • Ubiquitin and ubiquitin-like proteins as multifunctional signals
    • Welchman RL, Gordon C, Mayer RJ. Ubiquitin and ubiquitin-like proteins as multifunctional signals. Nat Rev Mol Cell Biol 2005; 6: 599-609.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 599-609
    • Welchman, R.L.1    Gordon, C.2    Mayer, R.J.3
  • 130
    • 65249166493 scopus 로고    scopus 로고
    • Functional roles of ubiquitin-like domain (ULD) and ubiquitin-binding domain (UBD) containing proteins
    • Grabbe C, Dikic I. Functional roles of ubiquitin-like domain (ULD) and ubiquitin-binding domain (UBD) containing proteins. Chem Rev 2009; 109: 1481-94.
    • (2009) Chem Rev , vol.109 , pp. 1481-1494
    • Grabbe, C.1    Dikic, I.2
  • 131
    • 0025999463 scopus 로고
    • Cytoskeletal pathology in motor neuron diseases
    • Leigh PN, Swash M. Cytoskeletal pathology in motor neuron diseases. Adv Neurol 1991; 56: 115-24.
    • (1991) Adv Neurol , vol.56 , pp. 115-124
    • Leigh, P.N.1    Swash, M.2
  • 132
    • 37349034999 scopus 로고    scopus 로고
    • Evidence that TDP-43 is not the major ubiquitinated target within the pathological inclusions of amyotrophic lateral sclerosis
    • Sanelli T, Xiao S, Horne P, Bilbao J, Zinman L, Robertson J. Evidence that TDP-43 is not the major ubiquitinated target within the pathological inclusions of amyotrophic lateral sclerosis. J Neuropathol Exp Neurol 2007; 66: 1147-53.
    • (2007) J Neuropathol Exp Neurol , vol.66 , pp. 1147-1153
    • Sanelli, T.1    Xiao, S.2    Horne, P.3    Bilbao, J.4    Zinman, L.5    Robertson, J.6
  • 133
    • 33749070043 scopus 로고    scopus 로고
    • Insoluble mutant SOD1 is partly oligoubiquitinated in amyotrophic lateral sclerosis mice
    • Basso M, Massignan T, Samengo G, Cheroni C, De Biasi S, Salmona M, et al. Insoluble mutant SOD1 is partly oligoubiquitinated in amyotrophic lateral sclerosis mice. J Biol Chem 2006; 281: 33325-35.
    • (2006) J Biol Chem , vol.281 , pp. 33325-33335
    • Basso, M.1    Massignan, T.2    Samengo, G.3    Cheroni, C.4    de Biasi, S.5    Salmona, M.6
  • 134
    • 0037184063 scopus 로고    scopus 로고
    • Dorfin ubiquitylates mutant SOD1 and prevents mutant SOD1-mediated neurotoxicity
    • Niwa J, Ishigaki S, Hishikawa N, Yamamoto M, Doyu M, Murata S, et al. Dorfin ubiquitylates mutant SOD1 and prevents mutant SOD1-mediated neurotoxicity. J Biol Chem 2002; 277: 36793-8.
    • (2002) J Biol Chem , vol.277 , pp. 36793-36798
    • Niwa, J.1    Ishigaki, S.2    Hishikawa, N.3    Yamamoto, M.4    Doyu, M.5    Murata, S.6
  • 135
    • 35348817955 scopus 로고    scopus 로고
    • Proteasome inhibitor, bortezomib, for myeloma and lymphoma
    • Tobinai K. Proteasome inhibitor, bortezomib, for myeloma and lymphoma. Int J Clin Oncol 2007; 12: 318-26.
    • (2007) Int J Clin Oncol , vol.12 , pp. 318-326
    • Tobinai, K.1
  • 136
    • 37349059645 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system and proteasome inhibitors in central nervous system diseases
    • Shah IM, Di Napoli M. The ubiquitin-proteasome system and proteasome inhibitors in central nervous system diseases. Cardiovasc Hematol Disord Drug Targets 2007; 7: 250-73.
    • (2007) Cardiovasc Hematol Disord Drug Targets , vol.7 , pp. 250-273
    • Shah, I.M.1    Di Napoli, M.2
  • 137
    • 4544385218 scopus 로고    scopus 로고
    • Autophagy: Many paths to the same end
    • Cuervo AM. Autophagy: many paths to the same end. Mol Cell Biochem 2004; 263: 55-72.
    • (2004) Mol Cell Biochem , vol.263 , pp. 55-72
    • Cuervo, A.M.1
  • 139
    • 34447571032 scopus 로고    scopus 로고
    • The correct way to monitor autophagy in higher eukaryotes
    • Klionsky DJ. The correct way to monitor autophagy in higher eukaryotes. Autophagy 2005; 1: 65.
    • (2005) Autophagy , vol.1 , pp. 65
    • Klionsky, D.J.1
  • 140
    • 26844531363 scopus 로고    scopus 로고
    • Maturation of autophagic vacuoles in Mammalian cells
    • Eskelinen EL. Maturation of autophagic vacuoles in Mammalian cells. Autophagy 2005; 1: 1-10.
    • (2005) Autophagy , vol.1 , pp. 1-10
    • Eskelinen, E.L.1
  • 142
    • 0033978633 scopus 로고    scopus 로고
    • Distinct classes of phosphatidylinositol 3'-kinases are involved in signaling pathways that control macroautophagy in HT-29 cells
    • Petiot A, Ogier-Denis E, Blommaart EF, Meijer AJ, Codogno P. Distinct classes of phosphatidylinositol 3'-kinases are involved in signaling pathways that control macroautophagy in HT-29 cells. J Biol Chem 2000; 275: 992-8.
    • (2000) J Biol Chem , vol.275 , pp. 992-998
    • Petiot, A.1    Ogier-Denis, E.2    Blommaart, E.F.3    Meijer, A.J.4    Codogno, P.5
  • 143
    • 27644495684 scopus 로고    scopus 로고
    • Autophagic degeneration of motor neurons in a model of slow glutamate excitotoxicity in vitro
    • Matyja E, Taraszewska A, Naganska E, Rafalowska J. Autophagic degeneration of motor neurons in a model of slow glutamate excitotoxicity in vitro. Ultrastruct Pathol 2005; 29: 331-9.
    • (2005) Ultrastruct Pathol , vol.29 , pp. 331-339
    • Matyja, E.1    Taraszewska, A.2    Naganska, E.3    Rafalowska, J.4
  • 144
    • 56349119573 scopus 로고    scopus 로고
    • Motor deficit in a Drosophila model of mucolipidosis type IV due to defective clearance of apoptotic cells
    • Venkatachalam K, Long AA, Elsaesser R, Nikolaeva D, Broadie K, Montell C. Motor deficit in a Drosophila model of mucolipidosis type IV due to defective clearance of apoptotic cells. Cell 2008; 135: 838-51.
    • (2008) Cell , vol.135 , pp. 838-851
    • Venkatachalam, K.1    Long, A.A.2    Elsaesser, R.3    Nikolaeva, D.4    Broadie, K.5    Montell, C.6
  • 146
  • 147
    • 33847787621 scopus 로고    scopus 로고
    • Therapeutic effects of immunization with mutant superoxide dismutase in mice models of amyotrophic lateral sclerosis
    • Urushitani M, Ezzi SA, Julien JP. Therapeutic effects of immunization with mutant superoxide dismutase in mice models of amyotrophic lateral sclerosis. Proc Natl Acad Sci USA 2007; 104: 2495-500.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 2495-2500
    • Urushitani, M.1    Ezzi, S.A.2    Julien, J.P.3
  • 149
    • 49749096430 scopus 로고    scopus 로고
    • Small molecule enhancers of autophagy for neurodegenerative diseases
    • Sarkar S, Rubinsztein DC. Small molecule enhancers of autophagy for neurodegenerative diseases. Mol Biosyst 2008; 4: 895-901.
    • (2008) Mol Biosyst , vol.4 , pp. 895-901
    • Sarkar, S.1    Rubinsztein, D.C.2
  • 150
    • 49249136687 scopus 로고    scopus 로고
    • Combined lithium and valproate treatment delays disease onset, reduces neurological deficits and prolongs survival in an amyotrophic lateral sclerosis mouse model
    • Feng HL, Leng Y, Ma CH, Zhang J, Ren M, Chuang DM. Combined lithium and valproate treatment delays disease onset, reduces neurological deficits and prolongs survival in an amyotrophic lateral sclerosis mouse model. Neuroscience 2008; 155: 567-72.
    • (2008) Neuroscience , vol.155 , pp. 567-572
    • Feng, H.L.1    Leng, Y.2    Ma, C.H.3    Zhang, J.4    Ren, M.5    Chuang, D.M.6
  • 151
    • 37649024076 scopus 로고    scopus 로고
    • Small molecule regulators of autophagy identified by an image-based high-throughput screen
    • Zhang L, Yu J, Pan H, Hu P, Hao Y, Cai W, et al. Small molecule regulators of autophagy identified by an image-based high-throughput screen. Proc Natl Acad Sci USA 2007; 104: 19023-8.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 19023-19028
    • Zhang, L.1    Yu, J.2    Pan, H.3    Hu, P.4    Hao, Y.5    Cai, W.6
  • 152
  • 153
    • 0034953632 scopus 로고    scopus 로고
    • Apoptosis-regulating proteins as targets for drug discovery
    • Reed JC. Apoptosis-regulating proteins as targets for drug discovery. Trends Mol Med 2001; 7: 314-9.
    • (2001) Trends Mol Med , vol.7 , pp. 314-319
    • Reed, J.C.1
  • 154
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • Thornberry NA, Lazebnik Y. Caspases: enemies within. Science 1998; 281: 1312-6.
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 155
    • 2642689658 scopus 로고    scopus 로고
    • Proteases to die for
    • Cryns V, Yuan J. Proteases to die for. Genes Dev 1998; 12: 1551-70.
    • (1998) Genes Dev , vol.12 , pp. 1551-1570
    • Cryns, V.1    Yuan, J.2
  • 156
    • 0030702084 scopus 로고    scopus 로고
    • Caspases: Intracellular signaling by proteolysis
    • Salvesen GS, Dixit VM. Caspases: intracellular signaling by proteolysis. Cell 1997; 91: 443-6.
    • (1997) Cell , vol.91 , pp. 443-446
    • Salvesen, G.S.1    Dixit, V.M.2
  • 158
    • 22144491587 scopus 로고    scopus 로고
    • Apoptosis in amyotrophic lateral sclerosis--what is the evidence?
    • Sathasivam S, Shaw PJ. Apoptosis in amyotrophic lateral sclerosis--what is the evidence? Lancet Neurol 2005; 4: 500-9.
    • (2005) Lancet Neurol , vol.4 , pp. 500-509
    • Sathasivam, S.1    Shaw, P.J.2
  • 160
    • 0036019165 scopus 로고    scopus 로고
    • Mechanisms of cell death in neurodegenerative diseases: Fashion, fiction, and facts
    • Graeber MB, Moran LB. Mechanisms of cell death in neurodegenerative diseases: fashion, fiction, and facts. Brain Pathol 2002; 12: 385-90.
    • (2002) Brain Pathol , vol.12 , pp. 385-390
    • Graeber, M.B.1    Moran, L.B.2
  • 161
    • 0032862513 scopus 로고    scopus 로고
    • Upregulation of Bax protein and increased DNA degradation in ALS spinal cord motor neurons
    • Ekegren T, Grundstrom E, Lindholm D, Aquilonius SM. Upregulation of Bax protein and increased DNA degradation in ALS spinal cord motor neurons. Acta Neurol Scand 1999; 100: 317-21.
    • (1999) Acta Neurol Scand , vol.100 , pp. 317-321
    • Ekegren, T.1    Grundstrom, E.2    Lindholm, D.3    Aquilonius, S.M.4
  • 162
    • 0032896327 scopus 로고    scopus 로고
    • Neuronal death in amyotrophic lateral sclerosis is apoptosis: Possible contribution of a programmed cell death mechanism
    • Martin LJ. Neuronal death in amyotrophic lateral sclerosis is apoptosis: possible contribution of a programmed cell death mechanism. J Neuropathol Exp Neurol 1999; 58: 459-71.
    • (1999) J Neuropathol Exp Neurol , vol.58 , pp. 459-471
    • Martin, L.J.1
  • 163
    • 0029563461 scopus 로고
    • Apoptosis in amyotrophic lateral sclerosis is not restricted to motor neurons. Bcl-2 expression is increased in unaffected post-central gyrus
    • Troost D, Aten J, Morsink F, de Jong JM. Apoptosis in amyotrophic lateral sclerosis is not restricted to motor neurons. Bcl-2 expression is increased in unaffected post-central gyrus. Neuropathol Appl Neurobiol 1995; 21: 498-504.
    • (1995) Neuropathol Appl Neurobiol , vol.21 , pp. 498-504
    • Troost, D.1    Aten, J.2    Morsink, F.3    de Jong, J.M.4
  • 164
    • 0028101227 scopus 로고
    • Apoptosis related antigen, Le(Y) and nick-end labeling are positive in spinal motor neurons in amyotrophic lateral sclerosis
    • Yoshiyama Y, Yamada T, Asanuma K, Asahi T. Apoptosis related antigen, Le(Y) and nick-end labeling are positive in spinal motor neurons in amyotrophic lateral sclerosis. Acta Neuropathol 1994; 88: 207-11.
    • (1994) Acta Neuropathol , vol.88 , pp. 207-211
    • Yoshiyama, Y.1    Yamada, T.2    Asanuma, K.3    Asahi, T.4
  • 165
    • 0033625507 scopus 로고    scopus 로고
    • Motor neuronal death in sporadic amyotrophic lateral sclerosis (ALS) is not apoptotic. A comparative study of ALS and chronic aluminium chloride neurotoxicity in New Zealand white rabbits
    • He BP, Strong MJ. Motor neuronal death in sporadic amyotrophic lateral sclerosis (ALS) is not apoptotic. A comparative study of ALS and chronic aluminium chloride neurotoxicity in New Zealand white rabbits. Neuropathol Appl Neurobiol 2000; 26: 150-60.
    • (2000) Neuropathol Appl Neurobiol , vol.26 , pp. 150-160
    • He, B.P.1    Strong, M.J.2
  • 166
    • 0027985477 scopus 로고
    • A study of apoptosis in normal and pathologic nervous tissue after in situ end-labeling of DNA strand breaks
    • Migheli A, Cavalla P, Marino S, Schiffer D. A study of apoptosis in normal and pathologic nervous tissue after in situ end-labeling of DNA strand breaks. J Neuropathol Exp Neurol 1994; 53: 606-16.
    • (1994) J Neuropathol Exp Neurol , vol.53 , pp. 606-616
    • Migheli, A.1    Cavalla, P.2    Marino, S.3    Schiffer, D.4
  • 167
    • 85047699103 scopus 로고    scopus 로고
    • Is motoneuronal cell death in amyotrophic lateral sclerosis apoptosis?
    • Yamazaki M, Esumi E, Nakano I. Is motoneuronal cell death in amyotrophic lateral sclerosis apoptosis? Neuropathology 2005; 25: 381-7.
    • (2005) Neuropathology , vol.25 , pp. 381-387
    • Yamazaki, M.1    Esumi, E.2    Nakano, I.3
  • 169
    • 0034864628 scopus 로고    scopus 로고
    • Apoptosis in amyotrophic lateral sclerosis: A review of the evidence
    • Sathasivam S, Ince PG, Shaw PJ. Apoptosis in amyotrophic lateral sclerosis: a review of the evidence. Neuropathol Appl Neurobiol 2001; 27: 257-74.
    • (2001) Neuropathol Appl Neurobiol , vol.27 , pp. 257-274
    • Sathasivam, S.1    Ince, P.G.2    Shaw, P.J.3
  • 170
    • 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
  • 171
    • 0034647003 scopus 로고    scopus 로고
    • Functional role of caspase-1 and caspase-3 in an ALS transgenic mouse model
    • Li M, Ona VO, Guegan C, Chen M, Jackson-Lewis V, Andrews LJ, et al. Functional role of caspase-1 and caspase-3 in an ALS transgenic mouse model. Science 2000; 288: 335-9.
    • (2000) Science , vol.288 , pp. 335-339
    • Li, M.1    Ona, V.O.2    Guegan, C.3    Chen, M.4    Jackson-Lewis, V.5    Andrews, L.J.6
  • 172
    • 10744223086 scopus 로고    scopus 로고
    • The crucial role of caspase-9 in the disease progression of a transgenic ALS mouse model
    • Inoue H, Tsukita K, Iwasato T, Suzuki Y, Tomioka M, Tateno M, et al. The crucial role of caspase-9 in the disease progression of a transgenic ALS mouse model. EMBO J 2003; 22: 6665-74.
    • (2003) EMBO J , vol.22 , pp. 6665-6674
    • Inoue, H.1    Tsukita, K.2    Iwasato, T.3    Suzuki, Y.4    Tomioka, M.5    Tateno, M.6
  • 173
    • 0034771172 scopus 로고    scopus 로고
    • Apoptosis signals in sporadic amyotrophic lateral sclerosis: An immunocytochemical study
    • Embacher N, Kaufmann WA, Beer R, Maier H, Jellinger KA, Poewe W, et al. Apoptosis signals in sporadic amyotrophic lateral sclerosis: an immunocytochemical study. Acta Neuropathol 2001; 102: 426-34.
    • (2001) Acta Neuropathol , vol.102 , pp. 426-434
    • Embacher, N.1    Kaufmann, W.A.2    Beer, R.3    Maier, H.4    Jellinger, K.A.5    Poewe, W.6
  • 174
    • 60549089207 scopus 로고    scopus 로고
    • APP binds DR6 to trigger axon pruning and neuron death via distinct caspases
    • Nikolaev A, McLaughlin T, O'Leary DD, Tessier-Lavigne M. APP binds DR6 to trigger axon pruning and neuron death via distinct caspases. Nature 2009; 457: 981-9.
    • (2009) Nature , vol.457 , pp. 981-989
    • Nikolaev, A.1    McLaughlin, T.2    O'Leary, D.D.3    Tessier-Lavigne, M.4
  • 175
    • 2442715084 scopus 로고    scopus 로고
    • Placebo-controlled phase I/II studies of minocycline in amyotrophic lateral sclerosis
    • Gordon PH, Moore DH, Gelinas DF, Qualls C, Meister ME, Werner J, et al. Placebo-controlled phase I/II studies of minocycline in amyotrophic lateral sclerosis. Neurology 2004; 62: 1845-7.
    • (2004) Neurology , vol.62 , pp. 1845-1847
    • Gordon, P.H.1    Moore, D.H.2    Gelinas, D.F.3    Qualls, C.4    Meister, M.E.5    Werner, J.6
  • 177
    • 36749049874 scopus 로고    scopus 로고
    • Glutamate excitotoxicity and therapeutic targets for amyotrophic lateral sclerosis
    • Corona JC, Tovar-y-Romo LB, Tapia R. Glutamate excitotoxicity and therapeutic targets for amyotrophic lateral sclerosis. Expert Opin Ther Targets 2007; 11: 1415-28.
    • (2007) Expert Opin Ther Targets , vol.11 , pp. 1415-1428
    • Corona, J.C.1    Tovar-y-Romo, L.B.2    Tapia, R.3
  • 179
    • 0029067210 scopus 로고
    • CSF and plasma amino acid levels in motor neuron disease: Elevation of CSF glutamate in a subset of patients
    • Shaw PJ, Forrest V, Ince PG, Richardson JP, Wastell HJ. CSF and plasma amino acid levels in motor neuron disease: elevation of CSF glutamate in a subset of patients. Neurodegeneration 1995; 4: 209-16.
    • (1995) Neurodegeneration , vol.4 , pp. 209-216
    • Shaw, P.J.1    Forrest, V.2    Ince, P.G.3    Richardson, J.P.4    Wastell, H.J.5
  • 180
    • 0033551415 scopus 로고    scopus 로고
    • 1H-MRS evidence of neurodegeneration and excess glutamate + glutamine in ALS medulla
    • Pioro EP, Majors AW, Mitsumoto H, Nelson DR, Ng TC. 1H-MRS evidence of neurodegeneration and excess glutamate + glutamine in ALS medulla. Neurology 1999; 53: 71-9.
    • (1999) Neurology , vol.53 , pp. 71-79
    • Pioro, E.P.1    Majors, A.W.2    Mitsumoto, H.3    Nelson, D.R.4    Ng, T.C.5
  • 181
    • 0025337382 scopus 로고
    • Amyotrophic lateral sclerosis: Amino acid levels in plasma and cerebrospinal fluid
    • Perry TL, Krieger C, Hansen S, Eisen A. Amyotrophic lateral sclerosis: amino acid levels in plasma and cerebrospinal fluid. Ann Neurol 1990; 28: 12-7.
    • (1990) Ann Neurol , vol.28 , pp. 12-17
    • Perry, T.L.1    Krieger, C.2    Hansen, S.3    Eisen, A.4
  • 182
    • 0034099564 scopus 로고    scopus 로고
    • Elevated cortical extracellular fluid glutamate in transgenic mice expressing human mutant (G93A) Cu/Zn superoxide dismutase
    • Alexander GM, Deitch JS, Seeburger JL, Del Valle L, Heiman-Patterson TD. Elevated cortical extracellular fluid glutamate in transgenic mice expressing human mutant (G93A) Cu/Zn superoxide dismutase. J Neurochem 2000; 74: 1666-73.
    • (2000) J Neurochem , vol.74 , pp. 1666-1673
    • Alexander, G.M.1    Deitch, J.S.2    Seeburger, J.L.3    Del Valle, L.4    Heiman-Patterson, T.D.5
  • 183
    • 0026597010 scopus 로고
    • Decreased glutamate transport by the brain and spinal cord in amyotrophic lateral sclerosis
    • Rothstein JD, Martin LJ, Kuncl RW. Decreased glutamate transport by the brain and spinal cord in amyotrophic lateral sclerosis. N Engl J Med 1992; 326: 1464-8.
    • (1992) N Engl J Med , vol.326 , pp. 1464-1468
    • Rothstein, J.D.1    Martin, L.J.2    Kuncl, R.W.3
  • 184
    • 0028168346 scopus 로고
    • Ince PG. [3H]D-aspartate binding sites in the normal human spinal cord and changes in motor neuron disease: A quantitative autoradiographic study
    • Shaw PJ, Chinnery RM, Ince PG. [3H]D-aspartate binding sites in the normal human spinal cord and changes in motor neuron disease: a quantitative autoradiographic study. Brain Res 1994; 655: 195-201.
    • (1994) Brain Res , vol.655 , pp. 195-201
    • Shaw, P.J.1    Chinnery, R.M.2
  • 185
    • 0029030610 scopus 로고
    • Selective loss of glial glutamate transporter GLT-1 in amyotrophic lateral sclerosis
    • Rothstein JD, Van Kammen M, Levey AI, Martin LJ, Kuncl RW. Selective loss of glial glutamate transporter GLT-1 in amyotrophic lateral sclerosis. Ann Neurol 1995; 38: 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
  • 186
    • 0033938202 scopus 로고    scopus 로고
    • Excitatory amino acid transporter 1 and 2 immunoreactivity in the spinal cord in amyotrophic lateral sclerosis
    • Sasaki S, Komori T, Iwata M. Excitatory amino acid transporter 1 and 2 immunoreactivity in the spinal cord in amyotrophic lateral sclerosis. Acta Neuropathol 2000; 100: 138-44.
    • (2000) Acta Neuropathol , vol.100 , pp. 138-144
    • Sasaki, S.1    Komori, T.2    Iwata, M.3
  • 187
    • 0031879593 scopus 로고    scopus 로고
    • The expression of the glial glutamate transporter protein EAAT2 in motor neuron disease: An immunohistochemical study
    • Fray AE, Ince PG, Banner SJ, Milton ID, Usher PA, Cookson MR, et al. The expression of the glial glutamate transporter protein EAAT2 in motor neuron disease: an immunohistochemical study. Eur J Neurosci 1998; 10: 2481-9.
    • (1998) Eur J Neurosci , vol.10 , pp. 2481-2489
    • Fray, A.E.1    Ince, P.G.2    Banner, S.J.3    Milton, I.D.4    Usher, P.A.5    Cookson, M.R.6
  • 188
    • 0035189072 scopus 로고    scopus 로고
    • Transgenic SOD1 G93A mice develop reduced GLT-1 in spinal cord without alterations in cerebrospinal fluid glutamate levels
    • Bendotti C, Tortarolo M, Suchak SK, Calvaresi N, Carvelli L, Bastone A, et al. Transgenic SOD1 G93A mice develop reduced GLT-1 in spinal cord without alterations in cerebrospinal fluid glutamate levels. J Neurochem 2001; 79: 737-46.
    • (2001) J Neurochem , vol.79 , pp. 737-746
    • Bendotti, C.1    Tortarolo, M.2    Suchak, S.K.3    Calvaresi, N.4    Carvelli, L.5    Bastone, A.6
  • 189
    • 0031051485 scopus 로고    scopus 로고
    • ALS-linked SOD1 mutant G85R mediates damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions
    • Bruijn LI, Becher MW, Lee MK, Anderson KL, Jenkins NA, Copeland NG, et al. ALS-linked SOD1 mutant G85R mediates damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions. Neuron 1997; 18: 327-38.
    • (1997) Neuron , vol.18 , pp. 327-338
    • Bruijn, L.I.1    Becher, M.W.2    Lee, M.K.3    Anderson, K.L.4    Jenkins, N.A.5    Copeland, N.G.6
  • 190
    • 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)
    • Howland DS, Liu J, She Y, Goad B, Maragakis NJ, Kim B, et al. Focal loss of the glutamate transporter EAAT2 in a transgenic rat model of SOD1 mutant-mediated amyotrophic lateral sclerosis (ALS). Proc Natl Acad Sci USA 2002; 99: 1604-9.
    • (2002) Proc Natl Acad Sci USA , 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
  • 191
    • 0035947131 scopus 로고    scopus 로고
    • EAAT1 and EAAT2 immunoreactivity in transgenic mice with a G93A mutant SOD1 gene
    • Sasaki S, Warita H, Abe K, Komori T, Iwata M. EAAT1 and EAAT2 immunoreactivity in transgenic mice with a G93A mutant SOD1 gene. Neuroreport 2001; 12: 1359-62.
    • (2001) Neuroreport , vol.12 , pp. 1359-1362
    • Sasaki, S.1    Warita, H.2    Abe, K.3    Komori, T.4    Iwata, M.5
  • 192
    • 0037081303 scopus 로고    scopus 로고
    • GLT-1 glutamate transporter levels are unchanged in mice expressing G93A human mutant SOD1
    • Deitch JS, Alexander GM, Del Valle L, Heiman-Patterson TD. GLT-1 glutamate transporter levels are unchanged in mice expressing G93A human mutant SOD1. J Neurol Sci 2002; 193: 117-26.
    • (2002) J Neurol Sci , vol.193 , pp. 117-126
    • Deitch, J.S.1    Alexander, G.M.2    Del Valle, L.3    Heiman-Patterson, T.D.4
  • 193
    • 0141618315 scopus 로고    scopus 로고
    • Increased expression of the glial glutamate transporter EAAT2 modulates excitotoxicity and delays the onset but not the outcome of ALS in mice
    • Guo H, Lai L, Butchbach ME, Stockinger MP, Shan X, Bishop GA, et al. Increased expression of the glial glutamate transporter EAAT2 modulates excitotoxicity and delays the onset but not the outcome of ALS in mice. Hum Mol Genet 2003; 12: 2519-32.
    • (2003) Hum Mol Genet , vol.12 , pp. 2519-2532
    • Guo, H.1    Lai, L.2    Butchbach, M.E.3    Stockinger, M.P.4    Shan, X.5    Bishop, G.A.6
  • 194
    • 19944428649 scopus 로고    scopus 로고
    • Beta-lactam antibiotics offer neuroprotection by increasing glutamate transporter expression
    • Rothstein JD, Patel S, Regan MR, Haenggeli C, Huang YH, Bergles DE, et al. Beta-lactam antibiotics offer neuroprotection by increasing glutamate transporter expression. Nature 2005; 433: 73-7.
    • (2005) Nature , vol.433 , pp. 73-77
    • Rothstein, J.D.1    Patel, S.2    Regan, M.R.3    Haenggeli, C.4    Huang, Y.H.5    Bergles, D.E.6
  • 195
    • 0030050727 scopus 로고    scopus 로고
    • Benefit of vitamin E, riluzole, and gabapentin in a transgenic model of familial amyotrophic lateral sclerosis
    • Gurney ME, Cutting FB, Zhai P, Doble A, Taylor CP, Andrus PK, et al. Benefit of vitamin E, riluzole, and gabapentin in a transgenic model of familial amyotrophic lateral sclerosis. Ann Neurol 1996; 39: 147-57.
    • (1996) Ann Neurol , vol.39 , pp. 147-157
    • Gurney, M.E.1    Cutting, F.B.2    Zhai, P.3    Doble, A.4    Taylor, C.P.5    Andrus, P.K.6
  • 196
    • 0028097839 scopus 로고
    • A controlled trial of riluzole in amyotrophic lateral sclerosis. ALS/Riluzole Study Group
    • Bensimon G, Lacomblez L, Meininger V. A controlled trial of riluzole in amyotrophic lateral sclerosis. ALS/Riluzole Study Group. N Engl J Med 1994; 330: 585-91.
    • (1994) N Engl J Med , vol.330 , pp. 585-591
    • Bensimon, G.1    Lacomblez, L.2    Meininger, V.3
  • 197
    • 0029977337 scopus 로고    scopus 로고
    • Dose-ranging study of riluzole in amyotrophic lateral sclerosis. Amyotrophic Lateral Sclerosis/Riluzole Study Group II
    • Lacomblez L, Bensimon G, Leigh PN, Guillet P, Meininger V. Dose-ranging study of riluzole in amyotrophic lateral sclerosis. Amyotrophic Lateral Sclerosis/Riluzole Study Group II. Lancet 1996; 347: 1425-31.
    • (1996) Lancet , vol.347 , pp. 1425-1431
    • Lacomblez, L.1    Bensimon, G.2    Leigh, P.N.3    Guillet, P.4    Meininger, V.5
  • 198
    • 0034004476 scopus 로고    scopus 로고
    • AMPA exposures induce mitochondrial Ca(2+) overload and ROS generation in spinal motor neurons in vitro
    • Carriedo SG, Sensi SL, Yin HZ, Weiss JH. AMPA exposures induce mitochondrial Ca(2+) overload and ROS generation in spinal motor neurons in vitro. J Neurosci 2000; 20: 240-50.
    • (2000) J Neurosci , vol.20 , pp. 240-250
    • Carriedo, S.G.1    Sensi, S.L.2    Yin, H.Z.3    Weiss, J.H.4
  • 200
    • 0036239183 scopus 로고    scopus 로고
    • An alpha-mercaptoacrylic acid derivative (PD150606) inhibits selective motor neuron death via inhibition of kainate-induced Ca2+ influx and not via calpain inhibition
    • Van den Bosch L, Van Damme P, Vleminckx V, Van Houtte E, Lemmens G, Missiaen L, et al. An alpha-mercaptoacrylic acid derivative (PD150606) inhibits selective motor neuron death via inhibition of kainate-induced Ca2+ influx and not via calpain inhibition. Neuropharmacology 2002; 42: 706-13.
    • (2002) Neuropharmacology , vol.42 , pp. 706-713
    • Van den Bosch, L.1    van Damme, P.2    Vleminckx, V.3    van Houtte, E.4    Lemmens, G.5    Missiaen, L.6
  • 201
  • 202
    • 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
    • Tateno M, Sadakata H, Tanaka M, Itohara S, Shin RM, Miura M, et al. Calcium-permeable AMPA receptors promote misfolding of mutant SOD1 protein and development of amyotrophic lateral sclerosis in a transgenic mouse model. Hum Mol Genet 2004; 13: 2183-96.
    • (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
  • 203
    • 0032752054 scopus 로고    scopus 로고
    • Reduction of GluR2 RNA editing, a molecular change that increases calcium influx through AMPA receptors, selective in the spinal ventral gray of patients with amyotrophic lateral sclerosis
    • Takuma H, Kwak S, Yoshizawa T, Kanazawa I. Reduction of GluR2 RNA editing, a molecular change that increases calcium influx through AMPA receptors, selective in the spinal ventral gray of patients with amyotrophic lateral sclerosis. Ann Neurol 1999; 46: 806-15.
    • (1999) Ann Neurol , vol.46 , pp. 806-815
    • Takuma, H.1    Kwak, S.2    Yoshizawa, T.3    Kanazawa, I.4
  • 205
    • 0035958752 scopus 로고    scopus 로고
    • Immunohistochemical localization of group I and II metabotropic glutamate receptors in control and amyotrophic lateral sclerosis human spinal cord: Upregulation in reactive astrocytes
    • Aronica E, Catania MV, Geurts J, Yankaya B, Troost D. Immunohistochemical localization of group I and II metabotropic glutamate receptors in control and amyotrophic lateral sclerosis human spinal cord: upregulation in reactive astrocytes. Neuroscience 2001; 105: 509-20.
    • (2001) Neuroscience , vol.105 , pp. 509-520
    • Aronica, E.1    Catania, M.V.2    Geurts, J.3    Yankaya, B.4    Troost, D.5
  • 206
    • 0033976804 scopus 로고    scopus 로고
    • Neuroprotection by metabotropic glutamate receptor agonists on kainate-induced degeneration of motor neurons in spinal cord slices from adult rat
    • Pizzi M, Benarese M, Boroni F, Goffi F, Valerio A, Spano PF. Neuroprotection by metabotropic glutamate receptor agonists on kainate-induced degeneration of motor neurons in spinal cord slices from adult rat. Neuropharmacology 2000; 39: 903-10.
    • (2000) Neuropharmacology , vol.39 , pp. 903-910
    • Pizzi, M.1    Benarese, M.2    Boroni, F.3    Goffi, F.4    Valerio, A.5    Spano, P.F.6
  • 207
    • 0032557929 scopus 로고    scopus 로고
    • Activation of metabotropic glutamate receptors delays apoptosis of chick embryonic motor neurons in vitro
    • Anneser JM, Horstmann S, Weydt P, Borasio GD. Activation of metabotropic glutamate receptors delays apoptosis of chick embryonic motor neurons in vitro. Neuroreport 1998; 9: 2039-43.
    • (1998) Neuroreport , vol.9 , pp. 2039-2043
    • Anneser, J.M.1    Horstmann, S.2    Weydt, P.3    Borasio, G.D.4
  • 210
    • 1842714301 scopus 로고    scopus 로고
    • Neuroinflammation, COX-2, and ALS-a dual role
    • Consilvio C, Vincent AM, Feldman EL. Neuroinflammation, COX-2, and ALS-a dual role? Exp Neurol 2004; 187: 1-10.
    • (2004) Exp Neurol , vol.187 , pp. 1-10
    • Consilvio, C.1    Vincent, A.M.2    Feldman, E.L.3
  • 211
    • 0344838679 scopus 로고    scopus 로고
    • Neuro-inflammation as a therapeutic target in amyotrophic lateral sclerosis
    • Weydt P, Weiss MD, Moller T, Carter GT. Neuro-inflammation as a therapeutic target in amyotrophic lateral sclerosis. Curr Opin Investig Drugs 2002; 3: 1720-4.
    • (2002) Curr Opin Investig Drugs , vol.3 , pp. 1720-1724
    • Weydt, P.1    Weiss, M.D.2    Moller, T.3    Carter, G.T.4
  • 212
    • 0035132167 scopus 로고    scopus 로고
    • Increased expression of the pro-inflammatory enzyme cyclooxygenase-2 in amyotrophic lateral sclerosis
    • Almer G, Guegan C, Teismann P, Naini A, Rosoklija G, Hays AP, et al. Increased expression of the pro-inflammatory enzyme cyclooxygenase-2 in amyotrophic lateral sclerosis. Ann Neurol 2001; 49: 176-85.
    • (2001) Ann Neurol , vol.49 , pp. 176-185
    • Almer, G.1    Guegan, C.2    Teismann, P.3    Naini, A.4    Rosoklija, G.5    Hays, A.P.6
  • 213
    • 0141816705 scopus 로고    scopus 로고
    • Expression and localization of cyclooxygenase-1 and -2 in human sporadic amyotrophic lateral sclerosis
    • Maihofner C, Probst-Cousin S, Bergmann M, Neuhuber W, Neundorfer B, Heuss D. Expression and localization of cyclooxygenase-1 and -2 in human sporadic amyotrophic lateral sclerosis. Eur J Neurosci 2003; 18: 1527-34.
    • (2003) Eur J Neurosci , vol.18 , pp. 1527-1534
    • Maihofner, C.1    Probst-Cousin, S.2    Bergmann, M.3    Neuhuber, W.4    Neundorfer, B.5    Heuss, D.6
  • 214
    • 0037161253 scopus 로고    scopus 로고
    • Increased levels of the pro-inflammatory prostaglandin PGE2 in CSF from ALS patients
    • Almer G, Teismann P, Stevic Z, Halaschek-Wiener J, Deecke L, Kostic V, et al. Increased levels of the pro-inflammatory prostaglandin PGE2 in CSF from ALS patients. Neurology 2002; 58: 1277-9.
    • (2002) Neurology , vol.58 , pp. 1277-1279
    • Almer, G.1    Teismann, P.2    Stevic, Z.3    Halaschek-Wiener, J.4    Deecke, L.5    Kostic, V.6
  • 216
    • 0032887341 scopus 로고    scopus 로고
    • Potentiation of excitotoxicity in transgenic mice overexpressing neuronal cyclooxygenase-2
    • Kelley KA, Ho L, Winger D, Freire-Moar J, Borelli CB, Aisen PS, et al. Potentiation of excitotoxicity in transgenic mice overexpressing neuronal cyclooxygenase-2. Am J Pathol 1999; 155: 995-1004.
    • (1999) Am J Pathol , vol.155 , pp. 995-1004
    • Kelley, K.A.1    Ho, L.2    Winger, D.3    Freire-Moar, J.4    Borelli, C.B.5    Aisen, P.S.6
  • 217
    • 0035970036 scopus 로고    scopus 로고
    • Reduced susceptibility to ischemic brain injury and N-methyl-D-aspartate-mediated neurotoxicity in cyclooxygenase-2-deficient mice
    • Iadecola C, Niwa K, Nogawa S, Zhao X, Nagayama M, Araki E, et al. Reduced susceptibility to ischemic brain injury and N-methyl-D-aspartate-mediated neurotoxicity in cyclooxygenase-2-deficient mice. Proc Natl Acad Sci USA 2001; 98: 1294-9.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 1294-1299
    • Iadecola, C.1    Niwa, K.2    Nogawa, S.3    Zhao, X.4    Nagayama, M.5    Araki, E.6
  • 218
    • 54849418885 scopus 로고    scopus 로고
    • The prostaglandin E2 EP2 receptor accelerates disease progression and inflammation in a model of amyotrophic lateral sclerosis
    • Liang X, Wang Q, Shi J, Lokteva L, Breyer RM, Montine TJ, et al. The prostaglandin E2 EP2 receptor accelerates disease progression and inflammation in a model of amyotrophic lateral sclerosis. Ann Neurol 2008; 64: 304-14.
    • (2008) Ann Neurol , vol.64 , pp. 304-314
    • Liang, X.1    Wang, Q.2    Shi, J.3    Lokteva, L.4    Breyer, R.M.5    Montine, T.J.6
  • 219
    • 0036895241 scopus 로고    scopus 로고
    • Cyclooxygenase 2 inhibition protects motor neurons and prolongs survival in a transgenic mouse model of ALS
    • Drachman DB, Frank K, Dykes-Hoberg M, Teismann P, Almer G, Przedborski S, et al. Cyclooxygenase 2 inhibition protects motor neurons and prolongs survival in a transgenic mouse model of ALS. Ann Neurol 2002; 52: 771-8.
    • (2002) Ann Neurol , vol.52 , pp. 771-778
    • Drachman, D.B.1    Frank, K.2    Dykes-Hoberg, M.3    Teismann, P.4    Almer, G.5    Przedborski, S.6
  • 223
    • 41149088328 scopus 로고    scopus 로고
    • T cells in amyotrophic lateral sclerosis
    • Holmoy T. T cells in amyotrophic lateral sclerosis. Eur J Neurol 2008; 15: 360-6.
    • (2008) Eur J Neurol , vol.15 , pp. 360-366
    • Holmoy, T.1
  • 226
    • 33744968445 scopus 로고    scopus 로고
    • Breaking ignorance: The case of the brain
    • Wekerle H. Breaking ignorance: the case of the brain. Curr Top Microbiol Immunol 2006; 305: 25-50.
    • (2006) Curr Top Microbiol Immunol , vol.305 , pp. 25-50
    • Wekerle, H.1
  • 227
    • 0024955336 scopus 로고
    • Lymphocytic infiltration in the spinal cord of patients with amyotrophic lateral sclerosis
    • Troost D, van den Oord JJ, de Jong JM, Swaab DF. Lymphocytic infiltration in the spinal cord of patients with amyotrophic lateral sclerosis. Clin Neuropathol 1989; 8: 289-94.
    • (1989) Clin Neuropathol , vol.8 , pp. 289-294
    • Troost, D.1    van den Oord, J.J.2    de Jong, J.M.3    Swaab, D.F.4
  • 228
    • 0025185079 scopus 로고
    • Immunohisto-chemical characterization of the inflammatory infiltrate in amyotrophic lateral sclerosis
    • Troost D, Van den Oord JJ, Vianney de Jong JM. Immunohisto-chemical characterization of the inflammatory infiltrate in amyotrophic lateral sclerosis. Neuropathol Appl Neurobiol 1990; 16: 401-10.
    • (1990) Neuropathol Appl Neurobiol , vol.16 , pp. 401-410
    • Troost, D.1    Van den Oord, J.J.2    Vianney de Jong, J.M.3
  • 229
    • 0026605961 scopus 로고
    • Immunologic reactions in amyotrophic lateral sclerosis brain and spinal cord tissue
    • Kawamata T, Akiyama H, Yamada T, McGeer PL. Immunologic reactions in amyotrophic lateral sclerosis brain and spinal cord tissue. Am J Pathol 1992; 140: 691-707.
    • (1992) Am J Pathol , vol.140 , pp. 691-707
    • Kawamata, T.1    Akiyama, H.2    Yamada, T.3    McGeer, P.L.4
  • 230
    • 0027473452 scopus 로고
    • Lymphocytic infiltrates in the spinal cord in amyotrophic lateral sclerosis
    • Engelhardt JI, Tajti J, Appel SH. Lymphocytic infiltrates in the spinal cord in amyotrophic lateral sclerosis. Arch Neurol 1993; 50: 30-6.
    • (1993) Arch Neurol , vol.50 , pp. 30-36
    • Engelhardt, J.I.1    Tajti, J.2    Appel, S.H.3
  • 231
    • 0344490328 scopus 로고    scopus 로고
    • Therapeutic vaccine for acute and chronic motor neuron diseases: Implications for amyotrophic lateral sclerosis
    • Angelov DN, Waibel S, Guntinas-Lichius O, Lenzen M, Neiss WF, Tomov TL, et al. Therapeutic vaccine for acute and chronic motor neuron diseases: implications for amyotrophic lateral sclerosis. Proc Natl Acad Sci USA 2003; 100: 4790-5.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 4790-4795
    • Angelov, D.N.1    Waibel, S.2    Guntinas-Lichius, O.3    Lenzen, M.4    Neiss, W.F.5    Tomov, T.L.6
  • 232
    • 55749110043 scopus 로고    scopus 로고
    • CD4+ T cells support glial neuroprotection, slow disease progression, and modify glial morphology in an animal model of inherited ALS
    • Beers DR, Henkel JS, Zhao W, Wang J, Appel SH. CD4+ T cells support glial neuroprotection, slow disease progression, and modify glial morphology in an animal model of inherited ALS. Proc Natl Acad Sci USA 2008; 105: 15558-63.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 15558-15563
    • Beers, D.R.1    Henkel, J.S.2    Zhao, W.3    Wang, J.4    Appel, S.H.5
  • 233
    • 12344300485 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor supports facial motoneuron survival after facial nerve transection in immunodeficient mice
    • Serpe CJ, Byram SC, Sanders VM, Jones KJ. Brain-derived neurotrophic factor supports facial motoneuron survival after facial nerve transection in immunodeficient mice. Brain Behav Immun 2005; 19: 173-80.
    • (2005) Brain Behav Immun , vol.19 , pp. 173-180
    • Serpe, C.J.1    Byram, S.C.2    Sanders, V.M.3    Jones, K.J.4
  • 235
    • 5144227225 scopus 로고    scopus 로고
    • Dual effect of CD4+CD25+ regulatory T cells in neurodegeneration: A dialogue with microglia
    • Kipnis J, Avidan H, Caspi RR, Schwartz M. Dual effect of CD4+CD25+ regulatory T cells in neurodegeneration: a dialogue with microglia. Proc Natl Acad Sci USA 2004; 101 (Suppl 2): 14663-9.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.SUPPL. 2 , pp. 14663-14669
    • Kipnis, J.1    Avidan, H.2    Caspi, R.R.3    Schwartz, M.4
  • 236
    • 34848885871 scopus 로고    scopus 로고
    • Mechanism of action of glatiramer acetate in treatment of multiple sclerosis
    • Weber MS, Hohlfeld R, Zamvil SS. Mechanism of action of glatiramer acetate in treatment of multiple sclerosis. Neurotherapeutics 2007; 4: 647-53.
    • (2007) Neurotherapeutics , vol.4 , pp. 647-653
    • Weber, M.S.1    Hohlfeld, R.2    Zamvil, S.S.3
  • 238
    • 33947216452 scopus 로고    scopus 로고
    • Therapeutic immunization with a glatiramer acetate derivative does not alter survival in G93A and G37R SOD1 mouse models of familial ALS
    • Haenggeli C, Julien JP, Mosley RL, Perez N, Dhar A, Gendelman HE, et al. Therapeutic immunization with a glatiramer acetate derivative does not alter survival in G93A and G37R SOD1 mouse models of familial ALS. Neurobiol Dis 2007; 26: 146-52.
    • (2007) Neurobiol Dis , vol.26 , pp. 146-152
    • Haenggeli, C.1    Julien, J.P.2    Mosley, R.L.3    Perez, N.4    Dhar, A.5    Gendelman, H.E.6
  • 241
    • 0036708987 scopus 로고    scopus 로고
    • Myelin specific Th1 cells are necessary for post-traumatic protective autoimmunity
    • Kipnis J, Mizrahi T, Yoles E, Ben-Nun A, Schwartz M. Myelin specific Th1 cells are necessary for post-traumatic protective autoimmunity. J Neuroimmunol 2002; 130: 78-85.
    • (2002) J Neuroimmunol , vol.130 , pp. 78-85
    • Kipnis, J.1    Mizrahi, T.2    Yoles, E.3    Ben-Nun, A.4    Schwartz, M.5
  • 242
    • 34249902026 scopus 로고    scopus 로고
    • Statins, neuromuscular degenerative disease and an amyotrophic lateral sclerosis-like syndrome: An analysis of individual case safety reports from vigibase
    • Edwards IR, Star K, Kiuru A. Statins, neuromuscular degenerative disease and an amyotrophic lateral sclerosis-like syndrome: an analysis of individual case safety reports from vigibase. Drug Saf 2007; 30: 515-25.
    • (2007) Drug Saf , vol.30 , pp. 515-525
    • Edwards, I.R.1    Star, K.2    Kiuru, A.3
  • 243
    • 38549113445 scopus 로고    scopus 로고
    • Statins, regulatory T cells and amyotrophic lateral sclerosis
    • author reply 181-3
    • Goldstein MR, Mascitelli L, Pezzetta F. Statins, regulatory T cells and amyotrophic lateral sclerosis. Drug Saf 2008; 31: 181; author reply 181-3.
    • (2008) Drug Saf , vol.31 , pp. 181
    • Goldstein, M.R.1    Mascitelli, L.2    Pezzetta, F.3
  • 244
    • 33750998792 scopus 로고    scopus 로고
    • Innate immunity in amyotrophic lateral sclerosis
    • Moisse K, Strong MJ. Innate immunity in amyotrophic lateral sclerosis. Biochim Biophys Acta 2006; 1762: 1083-93.
    • (2006) Biochim Biophys Acta , vol.1762 , pp. 1083-1093
    • Moisse, K.1    Strong, M.J.2
  • 246
    • 35148846456 scopus 로고    scopus 로고
    • RANTES levels are elevated in serum and cerebrospinal fluid in patients with amyotrophic lateral sclerosis
    • Rentzos M, Nikolaou C, Rombos A, Boufidou F, Zoga M, Dimitrakopoulos A, et al. RANTES levels are elevated in serum and cerebrospinal fluid in patients with amyotrophic lateral sclerosis. Amyotroph Lateral Scler 2007; 8: 283-7.
    • (2007) Amyotroph Lateral Scler , vol.8 , pp. 283-287
    • Rentzos, M.1    Nikolaou, C.2    Rombos, A.3    Boufidou, F.4    Zoga, M.5    Dimitrakopoulos, A.6
  • 247
    • 0035873076 scopus 로고    scopus 로고
    • Neuron-specific expression of mutant superoxide dismutase 1 in transgenic mice does not lead to motor impairment
    • Pramatarova A, Laganiere J, Roussel J, Brisebois K, Rouleau GA. Neuron-specific expression of mutant superoxide dismutase 1 in transgenic mice does not lead to motor impairment. J Neurosci 2001; 21: 3369-74.
    • (2001) J Neurosci , vol.21 , pp. 3369-3374
    • Pramatarova, A.1    Laganiere, J.2    Roussel, J.3    Brisebois, K.4    Rouleau, G.A.5
  • 248
    • 70349265930 scopus 로고    scopus 로고
    • Intra-bone marrow-bone marrow transplantation slows disease progression and prolongs survival in G93A mutant SOD1 transgenic mice, an animal model mouse for amyotrophic lateral sclerosis
    • Ohnishi S, Ito H, Suzuki Y, Adachi Y, Wate R, Zhang J, et al. Intra-bone marrow-bone marrow transplantation slows disease progression and prolongs survival in G93A mutant SOD1 transgenic mice, an animal model mouse for amyotrophic lateral sclerosis. Brain Res 2009; 1296: 216-24.
    • (2009) Brain Res , vol.1296 , pp. 216-224
    • Ohnishi, S.1    Ito, H.2    Suzuki, Y.3    Adachi, Y.4    Wate, R.5    Zhang, J.6
  • 249
    • 33750478657 scopus 로고    scopus 로고
    • Wild-type microglia extend survival in PU.1 knockout mice with familial amyotrophic lateral sclerosis
    • Beers DR, Henkel JS, Xiao Q, Zhao W, Wang J, Yen AA, et al. Wild-type microglia extend survival in PU.1 knockout mice with familial amyotrophic lateral sclerosis. Proc Natl Acad Sci USA 2006; 103: 16021-6.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 16021-16026
    • Beers, D.R.1    Henkel, J.S.2    Xiao, Q.3    Zhao, W.4    Wang, J.5    Yen, A.A.6
  • 250
    • 67949100439 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha and interferon gamma cooperatively induce oxidative stress and motoneuron death in rat spinal cord embryonic explants
    • Mir M, Asensio VJ, Tolosa L, Gou-Fabregas M, Soler RM, Llado J, et al. Tumor necrosis factor alpha and interferon gamma cooperatively induce oxidative stress and motoneuron death in rat spinal cord embryonic explants. Neuroscience 2009; 162: 959-71.
    • (2009) Neuroscience , vol.162 , pp. 959-971
    • Mir, M.1    Asensio, V.J.2    Tolosa, L.3    Gou-Fabregas, M.4    Soler, R.M.5    Llado, J.6
  • 251
    • 55049120934 scopus 로고    scopus 로고
    • Ablation of proliferating microglia does not affect motor neuron degeneration in amyotrophic lateral sclerosis caused by mutant superoxide dismutase
    • Gowing G, Philips T, Van Wijmeersch B, Audet JN, Dewil M, Van Den Bosch L, et al. Ablation of proliferating microglia does not affect motor neuron degeneration in amyotrophic lateral sclerosis caused by mutant superoxide dismutase. J Neurosci 2008; 28: 10234-44.
    • (2008) J Neurosci , vol.28 , pp. 10234-10244
    • Gowing, G.1    Philips, T.2    van Wijmeersch, B.3    Audet, J.N.4    Dewil, M.5    Van Den Bosch, L.6
  • 252
    • 0037067009 scopus 로고    scopus 로고
    • Minocycline delays disease onset and mortality in a transgenic model of ALS
    • Van Den Bosch L, Tilkin P, Lemmens G, Robberecht W. Minocycline delays disease onset and mortality in a transgenic model of ALS. Neuroreport 2002; 13: 1067-70.
    • (2002) Neuroreport , vol.13 , pp. 1067-1070
    • Van Den Bosch, L.1    Tilkin, P.2    Lemmens, G.3    Robberecht, W.4
  • 253
    • 0036406903 scopus 로고    scopus 로고
    • Minocycline slows disease progression in a mouse model of amyotrophic lateral sclerosis
    • Kriz J, Nguyen MD, Julien JP. Minocycline slows disease progression in a mouse model of amyotrophic lateral sclerosis. Neurobiol Dis 2002; 10: 268-78.
    • (2002) Neurobiol Dis , vol.10 , pp. 268-278
    • Kriz, J.1    Nguyen, M.D.2    Julien, J.P.3
  • 254
    • 36148960127 scopus 로고    scopus 로고
    • Efficacy of minocycline in patients with amyotrophic lateral sclerosis: A phase III randomised trial
    • Gordon PH, Moore DH, Miller RG, Florence JM, Verheijde JL, Doorish C, et al. Efficacy of minocycline in patients with amyotrophic lateral sclerosis: a phase III randomised trial. Lancet Neurol 2007; 6: 1045-53.
    • (2007) Lancet Neurol , vol.6 , pp. 1045-1053
    • Gordon, P.H.1    Moore, D.H.2    Miller, R.G.3    Florence, J.M.4    Verheijde, J.L.5    Doorish, C.6
  • 255
    • 22144454595 scopus 로고    scopus 로고
    • Minocycline attenuates T cell and microglia activity to impair cytokine production in T cell-microglia interaction
    • Giuliani F, Hader W, Yong VW. Minocycline attenuates T cell and microglia activity to impair cytokine production in T cell-microglia interaction. J Leukoc Biol 2005; 78: 135-43.
    • (2005) J Leukoc Biol , vol.78 , pp. 135-143
    • Giuliani, F.1    Hader, W.2    Yong, V.W.3
  • 257
    • 33846794822 scopus 로고    scopus 로고
    • The NOX family of ROS-generating NADPH oxidases: Physiology and pathophysiology
    • Bedard K, Krause KH. The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology. Physiol Rev 2007; 87: 245-313.
    • (2007) Physiol Rev , vol.87 , pp. 245-313
    • Bedard, K.1    Krause, K.H.2
  • 258
    • 33747047814 scopus 로고    scopus 로고
    • The inflammatory NADPH oxidase enzyme modulates motor neuron degeneration in amyotrophic lateral sclerosis mice
    • Wu DC, Re DB, Nagai M, Ischiropoulos H, Przedborski S. The inflammatory NADPH oxidase enzyme modulates motor neuron degeneration in amyotrophic lateral sclerosis mice. Proc Natl Acad Sci USA 2006; 103: 12132-7.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 12132-12137
    • Wu, D.C.1    Re, D.B.2    Nagai, M.3    Ischiropoulos, H.4    Przedborski, S.5
  • 260
    • 38849182472 scopus 로고    scopus 로고
    • SOD1 mutations disrupt redox-sensitive Rac regulation of NADPH oxidase in a familial ALS model
    • Harraz MM, Marden JJ, Zhou W, Zhang Y, Williams A, Sharov VS, et al. SOD1 mutations disrupt redox-sensitive Rac regulation of NADPH oxidase in a familial ALS model. J Clin Invest 2008; 118: 659-70.
    • (2008) J Clin Invest , vol.118 , pp. 659-670
    • Harraz, M.M.1    Marden, J.J.2    Zhou, W.3    Zhang, Y.4    Williams, A.5    Sharov, V.S.6
  • 261
    • 38849143389 scopus 로고    scopus 로고
    • Revisiting oxidative damage in ALS: Microglia, Nox, and mutant SOD1
    • Boillee S, Cleveland DW. Revisiting oxidative damage in ALS: microglia, Nox, and mutant SOD1. J Clin Invest 2008; 118: 474-8.
    • (2008) J Clin Invest , vol.118 , pp. 474-478
    • Boillee, S.1    Cleveland, D.W.2
  • 262
  • 263
    • 52949103699 scopus 로고    scopus 로고
    • The endocannabinoid system in amyotrophic lateral sclerosis
    • Bilsland LG, Greensmith L. The endocannabinoid system in amyotrophic lateral sclerosis. Curr Pharm Des 2008; 14: 2306-16.
    • (2008) Curr Pharm Des , vol.14 , pp. 2306-2316
    • Bilsland, L.G.1    Greensmith, L.2
  • 264
    • 24644450190 scopus 로고    scopus 로고
    • Cannabinoid receptors and their role in neuroprotection
    • van der Stelt M, Di Marzo V. Cannabinoid receptors and their role in neuroprotection. Neuromolecular Med 2005; 7: 37-50.
    • (2005) Neuromolecular Med , vol.7 , pp. 37-50
    • van der Stelt, M.1    Di Marzo, V.2
  • 265
    • 0038684167 scopus 로고    scopus 로고
    • Induction of CB2 receptor expression in the rat spinal cord of neuropathic but not inflammatory chronic pain models
    • Zhang J, Hoffert C, Vu HK, Groblewski T, Ahmad S, O'Donnell D. Induction of CB2 receptor expression in the rat spinal cord of neuropathic but not inflammatory chronic pain models. Eur J Neurosci 2003; 17: 2750-4.
    • (2003) Eur J Neurosci , vol.17 , pp. 2750-2754
    • Zhang, J.1    Hoffert, C.2    Vu, H.K.3    Groblewski, T.4    Ahmad, S.5    O'Donnell, D.6
  • 266
    • 0037440415 scopus 로고    scopus 로고
    • Cannabinoids ablate release of TNFalpha in rat microglial cells stimulated with lypopolysaccharide
    • Facchinetti F, Del Giudice E, Furegato S, Passarotto M, Leon A. Cannabinoids ablate release of TNFalpha in rat microglial cells stimulated with lypopolysaccharide. Glia 2003; 41: 161-8.
    • (2003) Glia , vol.41 , pp. 161-168
    • Facchinetti, F.1    Del Giudice, E.2    Furegato, S.3    Passarotto, M.4    Leon, A.5
  • 267
    • 0033986604 scopus 로고    scopus 로고
    • Cannabinoids inhibit LPS-inducible cytokine mRNA expression in rat microglial cells
    • Puffenbarger RA, Boothe AC, Cabral GA. Cannabinoids inhibit LPS-inducible cytokine mRNA expression in rat microglial cells. Glia 2000; 29: 58-69.
    • (2000) Glia , vol.29 , pp. 58-69
    • Puffenbarger, R.A.1    Boothe, A.C.2    Cabral, G.A.3
  • 268
    • 0038678773 scopus 로고    scopus 로고
    • Reduction of human monocytic cell neurotoxicity and cytokine secretion by ligands of the cannabinoid-type CB2 receptor
    • Klegeris A, Bissonnette CJ, McGeer PL. Reduction of human monocytic cell neurotoxicity and cytokine secretion by ligands of the cannabinoid-type CB2 receptor. Br J Pharmacol 2003; 139: 775-86.
    • (2003) Br J Pharmacol , vol.139 , pp. 775-786
    • Klegeris, A.1    Bissonnette, C.J.2    McGeer, P.L.3
  • 269
    • 33947278309 scopus 로고    scopus 로고
    • The CB2 cannabinoid agonist AM-1241 prolongs survival in a transgenic mouse model of amyotrophic lateral sclerosis when initiated at symptom onset
    • Shoemaker JL, Seely KA, Reed RL, Crow JP, Prather PL. The CB2 cannabinoid agonist AM-1241 prolongs survival in a transgenic mouse model of amyotrophic lateral sclerosis when initiated at symptom onset. J Neurochem 2007; 101: 87-98.
    • (2007) J Neurochem , vol.101 , pp. 87-98
    • Shoemaker, J.L.1    Seely, K.A.2    Reed, R.L.3    Crow, J.P.4    Prather, P.L.5
  • 270
    • 33845683331 scopus 로고    scopus 로고
    • Increasing cannabinoid levels by pharmacological and genetic manipulation delay disease progression in SOD1 mice
    • Bilsland LG, Dick JR, Pryce G, Petrosino S, Di Marzo V, Baker D, et al. Increasing cannabinoid levels by pharmacological and genetic manipulation delay disease progression in SOD1 mice. FASEB J 2006; 20: 1003-5.
    • (2006) FASEB J , vol.20 , pp. 1003-1005
    • Bilsland, L.G.1    Dick, J.R.2    Pryce, G.3    Petrosino, S.4    Di Marzo, V.5    Baker, D.6
  • 272
    • 39049161976 scopus 로고    scopus 로고
    • Altered presymptomatic AMPA and cannabinoid receptor trafficking in motor neurons of ALS model mice: Implications for excitotoxicity
    • Zhao P, Ignacio S, Beattie EC, Abood ME. Altered presymptomatic AMPA and cannabinoid receptor trafficking in motor neurons of ALS model mice: implications for excitotoxicity. Eur J Neurosci 2008; 27: 572-9.
    • (2008) Eur J Neurosci , vol.27 , pp. 572-579
    • Zhao, P.1    Ignacio, S.2    Beattie, E.C.3    Abood, M.E.4
  • 275
    • 0034763566 scopus 로고    scopus 로고
    • Parvalbumin overexpression alters immune-mediated increases in intracellular calcium, and delays disease onset in a transgenic model of familial amyotrophic lateral sclerosis
    • Beers DR, Ho BK, Siklos L, Alexianu ME, Mosier DR, Mohamed AH, et al. Parvalbumin overexpression alters immune-mediated increases in intracellular calcium, and delays disease onset in a transgenic model of familial amyotrophic lateral sclerosis. J Neurochem 2001; 79: 499-509.
    • (2001) J Neurochem , vol.79 , pp. 499-509
    • Beers, D.R.1    Ho, B.K.2    Siklos, L.3    Alexianu, M.E.4    Mosier, D.R.5    Mohamed, A.H.6
  • 276
    • 0035404366 scopus 로고    scopus 로고
    • Marijuana in the management of amyotrophic lateral sclerosis
    • Carter GT, Rosen BS. Marijuana in the management of amyotrophic lateral sclerosis. Am J Hosp Palliat Care 2001; 18: 264-70.
    • (2001) Am J Hosp Palliat Care , vol.18 , pp. 264-270
    • Carter, G.T.1    Rosen, B.S.2
  • 278
    • 0028827252 scopus 로고
    • Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase
    • Li Y, Huang TT, Carlson EJ, Melov S, Ursell PC, Olson JL, et al. Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase. Nat Genet 1995; 11: 376-81.
    • (1995) Nat Genet , vol.11 , pp. 376-381
    • Li, Y.1    Huang, T.T.2    Carlson, E.J.3    Melov, S.4    Ursell, P.C.5    Olson, J.L.6
  • 279
    • 13844253808 scopus 로고    scopus 로고
    • Selective neuronal vulnerability and inadequate stress response in superoxide dismutase mutant mice
    • Lynn S, Huang EJ, Elchuri S, Naeemuddin M, Nishinaka Y, Yodoi J, et al. Selective neuronal vulnerability and inadequate stress response in superoxide dismutase mutant mice. Free Radic Biol Med 2005; 38: 817-28.
    • (2005) Free Radic Biol Med , vol.38 , pp. 817-828
    • Lynn, S.1    Huang, E.J.2    Elchuri, S.3    Naeemuddin, M.4    Nishinaka, Y.5    Yodoi, J.6
  • 280
    • 33646588683 scopus 로고    scopus 로고
    • Absence of CuZn superoxide dismutase leads to elevated oxidative stress and acceleration of age-dependent skeletal muscle atrophy
    • Muller FL, Song W, Liu Y, Chaudhuri A, Pieke-Dahl S, Strong R, et al. Absence of CuZn superoxide dismutase leads to elevated oxidative stress and acceleration of age-dependent skeletal muscle atrophy. Free Radic Biol Med 2006; 40: 1993-2004.
    • (2006) Free Radic Biol Med , vol.40 , pp. 1993-2004
    • Muller, F.L.1    Song, W.2    Liu, Y.3    Chaudhuri, A.4    Pieke-Dahl, S.5    Strong, R.6
  • 281
    • 37849007550 scopus 로고    scopus 로고
    • Oxidized/misfolded superoxide dismutase-1: The cause of all amyotrophic lateral sclerosis?
    • Kabashi E, Valdmanis PN, Dion P, Rouleau GA. Oxidized/misfolded superoxide dismutase-1: the cause of all amyotrophic lateral sclerosis? Ann Neurol 2007; 62: 553-9.
    • (2007) Ann Neurol , vol.62 , pp. 553-559
    • Kabashi, E.1    Valdmanis, P.N.2    Dion, P.3    Rouleau, G.A.4
  • 283
    • 33846678063 scopus 로고    scopus 로고
    • How do ALS-associated mutations in superoxide dismutase 1 promote aggregation of the protein?
    • 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.
    • (2007) Trends Biochem Sci , vol.32 , pp. 78-85
    • Shaw, B.F.1    Valentine, J.S.2
  • 284
    • 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, Coonfield M, Fromholt D, Copeland NG, 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: 128-38.
    • (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
  • 285
    • 0036199623 scopus 로고    scopus 로고
    • High molecular weight complexes of mutant superoxide dismutase 1: Age-dependent and tissue-specific accumulation
    • Wang J, Xu G, Borchelt DR. High molecular weight complexes of mutant superoxide dismutase 1: age-dependent and tissue-specific accumulation. Neurobiol Dis 2002; 9: 139-48.
    • (2002) Neurobiol Dis , vol.9 , pp. 139-148
    • Wang, J.1    Xu, G.2    Borchelt, D.R.3
  • 286
    • 33751212177 scopus 로고    scopus 로고
    • Structure, folding, and misfolding of Cu,Zn superoxide dismutase in amyotrophic lateral sclerosis
    • Rakhit R, Chakrabartty A. Structure, folding, and misfolding of Cu,Zn superoxide dismutase in amyotrophic lateral sclerosis. Biochim Biophys Acta 2006; 1762: 1025-37.
    • (2006) Biochim Biophys Acta , vol.1762 , pp. 1025-1037
    • Rakhit, R.1    Chakrabartty, A.2
  • 287
    • 0347155578 scopus 로고    scopus 로고
    • Oxidation-induced misfolding and aggregation of superoxide dismutase and its implications for amyotrophic lateral sclerosis
    • Rakhit R, Cunningham P, Furtos-Matei A, Dahan S, Qi XF, Crow JP, et al. Oxidation-induced misfolding and aggregation of superoxide dismutase and its implications for amyotrophic lateral sclerosis. J Biol Chem 2002; 277: 47551-6.
    • (2002) J Biol Chem , vol.277 , pp. 47551-47556
    • Rakhit, R.1    Cunningham, P.2    Furtos-Matei, A.3    Dahan, S.4    Qi, X.F.5    Crow, J.P.6
  • 288
    • 18144398928 scopus 로고    scopus 로고
    • Protein nitration in a mouse model of familial amyotrophic lateral sclerosis: Possible multifunctional role in the pathogenesis
    • Casoni F, Basso M, Massignan T, Gianazza E, Cheroni C, Salmona M, et al. Protein nitration in a mouse model of familial amyotrophic lateral sclerosis: possible multifunctional role in the pathogenesis. J Biol Chem 2005; 280: 16295-304.
    • (2005) J Biol Chem , vol.280 , pp. 16295-16304
    • Casoni, F.1    Basso, M.2    Massignan, T.3    Gianazza, E.4    Cheroni, C.5    Salmona, M.6
  • 289
    • 33947323759 scopus 로고    scopus 로고
    • Lost in translation: Treatment trials in the SOD1 mouse and in human ALS
    • Benatar M. Lost in translation: treatment trials in the SOD1 mouse and in human ALS. Neurobiol Dis 2007; 26: 1-13.
    • (2007) Neurobiol Dis , vol.26 , pp. 1-13
    • Benatar, M.1
  • 291
    • 33749056809 scopus 로고    scopus 로고
    • ALS: A disease of motor neurons and their nonneuronal neighbors
    • Boillee S, Vande Velde C, Cleveland DW. ALS: a disease of motor neurons and their nonneuronal neighbors. Neuron 2006; 52: 39-59.
    • (2006) Neuron , vol.52 , pp. 39-59
    • Boillee, S.1    Vande Velde, C.2    Cleveland, D.W.3
  • 292
    • 0037096354 scopus 로고    scopus 로고
    • Accumulation of SOD1 mutants in postnatal motoneurons does not cause motoneuron pathology or motoneuron disease
    • Lino MM, Schneider C, Caroni P. Accumulation of SOD1 mutants in postnatal motoneurons does not cause motoneuron pathology or motoneuron disease. J Neurosci 2002; 22: 4825-32.
    • (2002) J Neurosci , vol.22 , pp. 4825-4832
    • Lino, M.M.1    Schneider, C.2    Caroni, P.3
  • 293
    • 39849103473 scopus 로고    scopus 로고
    • Neuron-specific expression of mutant superoxide dismutase is sufficient to induce amyotrophic lateral sclerosis in transgenic mice
    • Jaarsma D, Teuling E, Haasdijk ED, De Zeeuw CI, Hoogenraad CC. Neuron-specific expression of mutant superoxide dismutase is sufficient to induce amyotrophic lateral sclerosis in transgenic mice. J Neurosci 2008; 28: 2075-88.
    • (2008) J Neurosci , vol.28 , pp. 2075-2088
    • Jaarsma, D.1    Teuling, E.2    Haasdijk, E.D.3    de Zeeuw, C.I.4    Hoogenraad, C.C.5
  • 294
    • 20244381261 scopus 로고    scopus 로고
    • Silencing mutant SOD1 using RNAi protects against neurodegeneration and extends survival in an ALS model
    • Ralph GS, Radcliffe PA, Day DM, Carthy JM, Leroux MA, Lee DC, et al. Silencing mutant SOD1 using RNAi protects against neurodegeneration and extends survival in an ALS model. Nat Med 2005; 11: 429-33.
    • (2005) Nat Med , vol.11 , pp. 429-433
    • Ralph, G.S.1    Radcliffe, P.A.2    Day, D.M.3    Carthy, J.M.4    Leroux, M.A.5    Lee, D.C.6
  • 296
    • 0141642203 scopus 로고    scopus 로고
    • Wild-type nonneuronal cells extend survival of SOD1 mutant motor neurons in ALS mice
    • Clement AM, Nguyen MD, Roberts EA, Garcia ML, Boillee S, Rule M, et al. Wild-type nonneuronal cells extend survival of SOD1 mutant motor neurons in ALS mice. Science 2003; 302: 113-7.
    • (2003) Science , vol.302 , pp. 113-117
    • Clement, A.M.1    Nguyen, M.D.2    Roberts, E.A.3    Garcia, M.L.4    Boillee, S.5    Rule, M.6
  • 297
    • 61349134134 scopus 로고    scopus 로고
    • Retrogradely transported siRNA silences human mutant SOD1 in spinal cord motor neurons
    • Rizvanov AA, Mukhamedyarov MA, Palotas A, Islamov RR. Retrogradely transported siRNA silences human mutant SOD1 in spinal cord motor neurons. Exp Brain Res 2009; 195: 1-4.
    • (2009) Exp Brain Res , vol.195 , pp. 1-4
    • Rizvanov, A.A.1    Mukhamedyarov, M.A.2    Palotas, A.3    Islamov, R.R.4
  • 298
    • 33747201641 scopus 로고    scopus 로고
    • Allele-specific RNAi selectively silences mutant SOD1 and achieves significant therapeutic benefit in vivo
    • Xia X, Zhou H, Huang Y, Xu Z. Allele-specific RNAi selectively silences mutant SOD1 and achieves significant therapeutic benefit in vivo. Neurobiol Dis 2006; 23: 578-86.
    • (2006) Neurobiol Dis , vol.23 , pp. 578-586
    • Xia, X.1    Zhou, H.2    Huang, Y.3    Xu, Z.4
  • 299
    • 0033605612 scopus 로고    scopus 로고
    • Decreased accumulation of endogenous brain-derived neurotrophic factor against constricting sciatic nerve ligatures in streptozotocin-diabetic and galactose-fed rats
    • Mizisin AP, DiStefano PS, Liu X, Garrett DN, Tonra JR. Decreased accumulation of endogenous brain-derived neurotrophic factor against constricting sciatic nerve ligatures in streptozotocin-diabetic and galactose-fed rats. Neurosci Lett 1999; 263: 149-52.
    • (1999) Neurosci Lett , vol.263 , pp. 149-152
    • Mizisin, A.P.1    Distefano, P.S.2    Liu, X.3    Garrett, D.N.4    Tonra, J.R.5
  • 301
    • 0028854836 scopus 로고
    • In vivo neurotrophic effects of GDNF on neonatal and adult facial motor neurons
    • Yan Q, Matheson C, Lopez OT. In vivo neurotrophic effects of GDNF on neonatal and adult facial motor neurons. Nature 1995; 373: 341-4.
    • (1995) Nature , vol.373 , pp. 341-344
    • Yan, Q.1    Matheson, C.2    Lopez, O.T.3
  • 302
    • 0034608712 scopus 로고    scopus 로고
    • GDNF but not BDNF is increased in cerebrospinal fluid in amyotrophic lateral sclerosis
    • Grundstrom E, Lindholm D, Johansson A, Blennow K, Askmark H. GDNF but not BDNF is increased in cerebrospinal fluid in amyotrophic lateral sclerosis. Neuroreport 2000; 11: 1781-3.
    • (2000) Neuroreport , vol.11 , pp. 1781-1783
    • Grundstrom, E.1    Lindholm, D.2    Johansson, A.3    Blennow, K.4    Askmark, H.5
  • 303
    • 2942695980 scopus 로고    scopus 로고
    • IGF-I prevents glutamate-induced motor neuron programmed cell death
    • Vincent AM, Mobley BC, Hiller A, Feldman EL. IGF-I prevents glutamate-induced motor neuron programmed cell death. Neurobiol Dis 2004; 16: 407-16.
    • (2004) Neurobiol Dis , vol.16 , pp. 407-416
    • Vincent, A.M.1    Mobley, B.C.2    Hiller, A.3    Feldman, E.L.4
  • 304
    • 0032924286 scopus 로고    scopus 로고
    • Insulin-like growth factor-I and central nervous system development
    • Anlar B, Sullivan KA, Feldman EL. Insulin-like growth factor-I and central nervous system development. Horm Metab Res 1999; 31: 120-5.
    • (1999) Horm Metab Res , vol.31 , pp. 120-125
    • Anlar, B.1    Sullivan, K.A.2    Feldman, E.L.3
  • 305
    • 0031895401 scopus 로고    scopus 로고
    • The peripheral insulin-like growth factor system in amyotrophic lateral sclerosis and in multiple sclerosis
    • Torres-Aleman I, Barrios V, Berciano J. The peripheral insulin-like growth factor system in amyotrophic lateral sclerosis and in multiple sclerosis. Neurology 1998; 50: 772-6.
    • (1998) Neurology , vol.50 , pp. 772-776
    • Torres-Aleman, I.1    Barrios, V.2    Berciano, J.3
  • 306
    • 35848932533 scopus 로고    scopus 로고
    • Circulating insulin-like growth factors and related binding proteins are selectively altered in amyotrophic lateral sclerosis and multiple sclerosis
    • Hosback S, Hardiman O, Nolan CM, Doyle MA, Gorman G, Lynch C, et al. Circulating insulin-like growth factors and related binding proteins are selectively altered in amyotrophic lateral sclerosis and multiple sclerosis. Growth Horm IGF Res 2007; 17: 472-9.
    • (2007) Growth Horm IGF Res , vol.17 , pp. 472-479
    • Hosback, S.1    Hardiman, O.2    Nolan, C.M.3    Doyle, M.A.4    Gorman, G.5    Lynch, C.6
  • 307
    • 6844266272 scopus 로고    scopus 로고
    • Effect of recombinant human insulin-like growth factor-I on progression of ALS. A placebo-controlled study. The North America ALS/IGF-I Study Group
    • Lai EC, Felice KJ, Festoff BW, Gawel MJ, Gelinas DF, Kratz R, et al. Effect of recombinant human insulin-like growth factor-I on progression of ALS. A placebo-controlled study. The North America ALS/IGF-I Study Group. Neurology 1997; 49: 1621-30.
    • (1997) Neurology , vol.49 , pp. 1621-1630
    • Lai, E.C.1    Felice, K.J.2    Festoff, B.W.3    Gawel, M.J.4    Gelinas, D.F.5    Kratz, R.6
  • 308
    • 0031722582 scopus 로고    scopus 로고
    • A placebo-controlled trial of insulin-like growth factor-I in amyotrophic lateral sclerosis. European ALS/IGF-I Study Group
    • Borasio GD, Robberecht W, Leigh PN, Emile J, Guiloff RJ, Jerusalem F, et al. A placebo-controlled trial of insulin-like growth factor-I in amyotrophic lateral sclerosis. European ALS/IGF-I Study Group. Neurology 1998; 51: 583-6.
    • (1998) Neurology , vol.51 , pp. 583-586
    • Borasio, G.D.1    Robberecht, W.2    Leigh, P.N.3    Emile, J.4    Guiloff, R.J.5    Jerusalem, F.6
  • 309
    • 70350146791 scopus 로고    scopus 로고
    • Subcutaneous IGF-1 is not beneficial in 2-year ALS trial
    • author reply 1247-8
    • Howe CL, Bergstrom RA, Horazdovsky BF. Subcutaneous IGF-1 is not beneficial in 2-year ALS trial. Neurology 2009; 73: 1247; author reply 1247-8.
    • (2009) Neurology , vol.73 , pp. 1247
    • Howe, C.L.1    Bergstrom, R.A.2    Horazdovsky, B.F.3
  • 310
    • 36849090838 scopus 로고    scopus 로고
    • VEGF in biological control
    • Breen EC. VEGF in biological control. J Cell Biochem 2007; 102: 1358-67.
    • (2007) J Cell Biochem , vol.102 , pp. 1358-1367
    • Breen, E.C.1
  • 311
    • 0034978562 scopus 로고    scopus 로고
    • Deletion of the hypoxia-response element in the vascular endothelial growth factor promoter causes motor neuron degeneration
    • Oosthuyse B, Moons L, Storkebaum E, Beck H, Nuyens D, Brusselmans K, et al. Deletion of the hypoxia-response element in the vascular endothelial growth factor promoter causes motor neuron degeneration. Nat Genet 2001; 28: 131-8.
    • (2001) Nat Genet , vol.28 , pp. 131-138
    • Oosthuyse, B.1    Moons, L.2    Storkebaum, E.3    Beck, H.4    Nuyens, D.5    Brusselmans, K.6
  • 312
    • 4844227301 scopus 로고    scopus 로고
    • Vascular endothelial growth factor prolongs survival in a transgenic mouse model of ALS
    • Zheng C, Nennesmo I, Fadeel B, Henter JI. Vascular endothelial growth factor prolongs survival in a transgenic mouse model of ALS. Ann Neurol 2004; 56: 564-7.
    • (2004) Ann Neurol , vol.56 , pp. 564-567
    • Zheng, C.1    Nennesmo, I.2    Fadeel, B.3    Henter, J.I.4
  • 313
    • 42549127816 scopus 로고    scopus 로고
    • Vascular endothelial growth factor protects spinal cord motoneurons against glutamate-induced excitotoxicity via phosphatidylinositol 3-kinase
    • Tolosa L, Mir M, Asensio VJ, Olmos G, Llado J. Vascular endothelial growth factor protects spinal cord motoneurons against glutamate-induced excitotoxicity via phosphatidylinositol 3-kinase. J Neurochem 2008; 105: 1080-90.
    • (2008) J Neurochem , vol.105 , pp. 1080-1090
    • Tolosa, L.1    Mir, M.2    Asensio, V.J.3    Olmos, G.4    Llado, J.5
  • 314
    • 67651206063 scopus 로고    scopus 로고
    • Stem cells: Comprehensive treatments for amyotrophic lateral sclerosis in conjunction with growth factor delivery
    • Lunn JS, Hefferan MP, Marsala M, Feldman EL. Stem cells: comprehensive treatments for amyotrophic lateral sclerosis in conjunction with growth factor delivery. Growth Factors 2009; 27: 133-40.
    • (2009) Growth Factors , vol.27 , pp. 133-140
    • Lunn, J.S.1    Hefferan, M.P.2    Marsala, M.3    Feldman, E.L.4
  • 318
    • 33744820872 scopus 로고    scopus 로고
    • Reticulons as markers of neurological diseases: Focus on amyotrophic lateral sclerosis
    • Fergani A, Dupuis L, Jokic N, Larmet Y, de Tapia M, Rene F, et al. Reticulons as markers of neurological diseases: focus on amyotrophic lateral sclerosis. Neurodegener Dis 2005; 2: 185-94.
    • (2005) Neurodegener Dis , vol.2 , pp. 185-194
    • Fergani, A.1    Dupuis, L.2    Jokic, N.3    Larmet, Y.4    de Tapia, M.5    Rene, F.6
  • 321
    • 49549113645 scopus 로고    scopus 로고
    • Nogo-A and Nogo-66 receptor in amyotrophic lateral sclerosis
    • Teng FY, Tang BL. Nogo-A and Nogo-66 receptor in amyotrophic lateral sclerosis. J Cell Mol Med 2008; 12: 1199-204.
    • (2008) J Cell Mol Med , vol.12 , pp. 1199-1204
    • Teng, F.Y.1    Tang, B.L.2
  • 322
    • 33750527780 scopus 로고    scopus 로고
    • The neurite outgrowth inhibitor Nogo-A promotes denervation in an amyotrophic lateral sclerosis model
    • Jokic N, Gonzalez de Aguilar JL, Dimou L, Lin S, Fergani A, Ruegg MA, et al. The neurite outgrowth inhibitor Nogo-A promotes denervation in an amyotrophic lateral sclerosis model. EMBO Rep 2006; 7: 1162-7.
    • (2006) EMBO Rep , vol.7 , pp. 1162-1167
    • Jokic, N.1    Gonzalez de Aguilar, J.L.2    Dimou, L.3    Lin, S.4    Fergani, A.5    Ruegg, M.A.6
  • 323
    • 70449377144 scopus 로고    scopus 로고
    • Reticulon-4A (Nogo-A) redistributes protein disulfide isomerase to protect mice from SOD1-dependent amyotrophic lateral sclerosis
    • Yang YS, Harel NY, Strittmatter SM. Reticulon-4A (Nogo-A) redistributes protein disulfide isomerase to protect mice from SOD1-dependent amyotrophic lateral sclerosis. J Neurosci 2009; 29: 13850-9.
    • (2009) J Neurosci , vol.29 , pp. 13850-13859
    • Yang, Y.S.1    Harel, N.Y.2    Strittmatter, S.M.3
  • 324
    • 0038076000 scopus 로고    scopus 로고
    • Systemic deletion of the myelin-associated outgrowth inhibitor Nogo-A improves regenerative and plastic responses after spinal cord injury
    • Simonen M, Pedersen V, Weinmann O, Schnell L, Buss A, Ledermann B, et al. Systemic deletion of the myelin-associated outgrowth inhibitor Nogo-A improves regenerative and plastic responses after spinal cord injury. Neuron 2003; 38: 201-11.
    • (2003) Neuron , vol.38 , pp. 201-211
    • Simonen, M.1    Pedersen, V.2    Weinmann, O.3    Schnell, L.4    Buss, A.5    Ledermann, B.6
  • 326
    • 34547123812 scopus 로고    scopus 로고
    • Identification and characterization of cholest-4-en-3-one, oxime (TRO19622), a novel drug candidate for amyotrophic lateral sclerosis
    • Bordet T, Buisson B, Michaud M, Drouot C, Galea P, Delaage P, et al. Identification and characterization of cholest-4-en-3-one, oxime (TRO19622), a novel drug candidate for amyotrophic lateral sclerosis. J Pharmacol Exp Ther 2007; 322: 709-20.
    • (2007) J Pharmacol Exp Ther , vol.322 , pp. 709-720
    • Bordet, T.1    Buisson, B.2    Michaud, M.3    Drouot, C.4    Galea, P.5    Delaage, P.6
  • 327
    • 70449339417 scopus 로고    scopus 로고
    • The antiapoptotic activity of melatonin in neurodegenerative diseases
    • Wang X. The antiapoptotic activity of melatonin in neurodegenerative diseases. CNS Neurosci Ther 2009; 15: 345-57.
    • (2009) CNS Neurosci Ther , vol.15 , pp. 345-357
    • Wang, X.1
  • 329
    • 0036482282 scopus 로고    scopus 로고
    • Chemical and physical properties and potential mechanisms: Melatonin as a broad spectrum antioxidant and free radical scavenger
    • Tan DX, Reiter RJ, Manchester LC, Yan MT, El-Sawi M, Sainz RM, et al. Chemical and physical properties and potential mechanisms: melatonin as a broad spectrum antioxidant and free radical scavenger. Curr Top Med Chem 2002; 2: 181-97.
    • (2002) Curr Top Med Chem , vol.2 , pp. 181-197
    • Tan, D.X.1    Reiter, R.J.2    Manchester, L.C.3    Yan, M.T.4    El-Sawi, M.5    Sainz, R.M.6
  • 330
    • 0033451946 scopus 로고    scopus 로고
    • Melatonin as a pharmacological agent against neuronal loss in experimental models of Huntington's disease, Alzheimer's disease and parkinsonism
    • Reiter RJ, Cabrera J, Sainz RM, Mayo JC, Manchester LC, Tan DX. Melatonin as a pharmacological agent against neuronal loss in experimental models of Huntington's disease, Alzheimer's disease and parkinsonism. Ann N Y Acad Sci 1999; 890: 471-85.
    • (1999) Ann N Y Acad Sci , vol.890 , pp. 471-485
    • Reiter, R.J.1    Cabrera, J.2    Sainz, R.M.3    Mayo, J.C.4    Manchester, L.C.5    Tan, D.X.6
  • 331
    • 65549160834 scopus 로고    scopus 로고
    • Methazolamide and melatonin inhibit mitochondrial cytochrome C release and are neuroprotective in experimental models of ischemic injury
    • Wang X, Figueroa BE, Stavrovskaya IG, Zhang Y, Sirianni AC, Zhu S, et al. Methazolamide and melatonin inhibit mitochondrial cytochrome C release and are neuroprotective in experimental models of ischemic injury. Stroke 2009; 40: 1877-85.
    • (2009) Stroke , vol.40 , pp. 1877-1885
    • Wang, X.1    Figueroa, B.E.2    Stavrovskaya, I.G.3    Zhang, Y.4    Sirianni, A.C.5    Zhu, S.6
  • 332
    • 3142713361 scopus 로고    scopus 로고
    • Direct inhibition of the mitochondrial permeability transition pore: A possible mechanism responsible for anti-apoptotic effects of melatonin
    • Andrabi SA, Sayeed I, Siemen D, Wolf G, Horn TF. Direct inhibition of the mitochondrial permeability transition pore: a possible mechanism responsible for anti-apoptotic effects of melatonin. FASEB J 2004; 18: 869-71.
    • (2004) FASEB J , vol.18 , pp. 869-871
    • Andrabi, S.A.1    Sayeed, I.2    Siemen, D.3    Wolf, G.4    Horn, T.F.5


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