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Volumn 389, Issue 1-2, 2014, Pages 277-291

A mitochondrial basis for Huntington's disease: Therapeutic prospects

Author keywords

Dynamin related protein 1; Mitochondria as a therapeutic target; Mitochondrial biogenesis; Mitochondrial ETC complex activity; Mitofusin 1 2; Mutant Huntingtin

Indexed keywords

ACETYLSALICYLIC ACID; AMANTADINE; CALCIUM ION; CLONAZEPAM; CLOZAPINE; CREATINE; DIAZEPAM; DICHLOROACETIC ACID; DIMEBON; DOPA; DOPAMINE; ETIRACETAM; FAS LIGAND; GABAPENTIN; GLUTAMIC ACID; HALOPERIDOL; HUNTINGTIN; LACTAM; LAMOTRIGINE; LITHIUM; MELATONIN; MEMANTINE; MINOCYCLINE; RAPAMYCIN; TETRABENAZINE; THIOCTIC ACID; TREHALOSE; TUMOR NECROSIS FACTOR ALPHA; UBIDECARENONE;

EID: 84896549657     PISSN: 03008177     EISSN: 15734919     Source Type: Journal    
DOI: 10.1007/s11010-013-1951-9     Document Type: Review
Times cited : (16)

References (193)
  • 1
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • The Huntington's disease collaborative research group
    • The Huntington's disease collaborative research group (1993) A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell 72:971-983
    • (1993) Cell , vol.72 , pp. 971-983
  • 3
    • 0027327418 scopus 로고
    • Trinucleotide repeat elongation in the Huntingtin gene in Huntington disease patients from 71 Danish families
    • Nørremølle A, Riess O, Epplen JT, Fenger K, Hasholt L, Sørensen SA (1993) Trinucleotide repeat elongation in the Huntingtin gene in Huntington disease patients from 71 Danish families. Hum Mol Genet 2:1475-1476
    • (1993) Hum Mol Genet , vol.2 , pp. 1475-1476
    • Nørremølle, A.1    Riess, O.2    Epplen, J.T.3    Fenger, K.4    Hasholt, L.5    Sørensen, S.A.6
  • 4
    • 0027745692 scopus 로고
    • Mitotic stability and meiotic variability of the (CAG)(n) repeat in the Huntington disease gene
    • Zühlke C, Riess O, Bockel B, Lange H, Thies U (1993) Mitotic stability and meiotic variability of the (CAG)n repeat in the Huntington disease gene. Hum Mol Genet 2:2063-2067 (Pubitemid 24003399)
    • (1993) Human Molecular Genetics , vol.2 , Issue.12 , pp. 2063-2067
    • Zuhlke, C.1    Riess, O.2    Bockel, B.3    Lange, H.4    Thies, U.5
  • 5
    • 0029034511 scopus 로고
    • Widespread expression of Huntington's disease gene (IT15) protein product
    • Sharp AH, Love SJ, Schilling G et al (1995) Widespread expression of Huntington's disease gene (IT15) protein product. Neuron 14:1065-1074
    • (1995) Neuron , vol.14 , pp. 1065-1074
    • Sharp, A.H.1    Love, S.J.2    Schilling, G.3
  • 6
    • 0029055717 scopus 로고
    • Targeted disruption of the Huntington's disease gene results in embryonic lethality and behavioral and morphological changes in heterozygotes
    • Nasir J, Floresco SB, O'Kusky JR et al (1995) Targeted disruption of the Huntington's disease gene results in embryonic lethality and behavioral and morphological changes in heterozygotes. Cell 81:811-823
    • (1995) Cell , vol.81 , pp. 811-823
    • Nasir, J.1    Floresco, S.B.2    O'Kusky, J.R.3
  • 9
    • 0037408279 scopus 로고    scopus 로고
    • Transcriptional abnormalities in Huntington disease
    • DOI 10.1016/S0168-9525(03)00074-X
    • Sugars KL, Rubinsztein DC (2003) Transcriptional abnormalities in Huntington disease. Trends Genet 19:233-238 (Pubitemid 36511427)
    • (2003) Trends in Genetics , vol.19 , Issue.5 , pp. 233-238
    • Sugars, K.L.1    Rubinsztein, D.C.2
  • 10
    • 84872183040 scopus 로고    scopus 로고
    • Mutant Huntingtin affects endocytosis in striatal cells by altering the binding of AP-2 to membranes
    • Borgonovo JE, Troncoso M, Lucas JJ, Sosa MA (2013) Mutant Huntingtin affects endocytosis in striatal cells by altering the binding of AP-2 to membranes. Exp Neurol 241:75-83
    • (2013) Exp Neurol , vol.241 , pp. 75-83
    • Borgonovo, J.E.1    Troncoso, M.2    Lucas, J.J.3    Sosa, M.A.4
  • 11
    • 33845357970 scopus 로고    scopus 로고
    • Mutant huntingtin inhibits clathrin-independent endocytosis and causes accumulation of cholesterol in vitro and in vivo
    • DOI 10.1093/hmg/ddl434
    • Trushina E, Singh RD, Dyer RB, Cao S, Shah VH, Parton RG, Pagano RE, McMurray CT (2006) Mutant Huntingtin inhibits clathrin-independent endocytosis and causes accumulation of cholesterol in vitro and in vivo. Hum Mol Genet 15:3578-3591 (Pubitemid 44884124)
    • (2006) Human Molecular Genetics , vol.15 , Issue.24 , pp. 3578-3591
    • Trushina, E.1    Singh, R.D.2    Dyer, R.B.3    Cao, S.4    Shah, V.H.5    Parton, R.G.6    Pagano, R.E.7    McMurray, C.T.8
  • 12
    • 38049053467 scopus 로고    scopus 로고
    • A stress sensitive ER membrane-association domain in Huntingtin protein defines a potential role for Huntingtin in the regulation of autophagy
    • Atwal RS, Truant R (2008) A stress sensitive ER membrane-association domain in Huntingtin protein defines a potential role for Huntingtin in the regulation of autophagy. Autophagy 4:91-93
    • (2008) Autophagy , vol.4 , pp. 91-93
    • Atwal, R.S.1    Truant, R.2
  • 15
    • 1542330658 scopus 로고    scopus 로고
    • Inhibition of mitochondrial complex II alters striatal expression of genes involved in glutamatergic and dopaminergic signaling: Possible implications for Huntington's disease
    • DOI 10.1016/j.nbd.2003.11.021, PII S0969996103002602
    • Napolitano M, Centonze D, Gubellini P, Rossi S, Spiezia S, Bernardi G, Gulino A, Calabresi P (2004) Inhibition of mitochondrial complex II alters striatal expression of genes involved in glutamatergic and dopaminergic signaling: possible implications for Huntington's disease. Neurobiol Dis 15:407-414 (Pubitemid 38296771)
    • (2004) Neurobiology of Disease , vol.15 , Issue.2 , pp. 407-414
    • Napolitano, M.1    Centonze, D.2    Gubellini, P.3    Rossi, S.4    Spiezia, S.5    Bernardi, G.6    Gulino, A.7    Calabresi, P.8
  • 16
    • 67650248280 scopus 로고    scopus 로고
    • Striatal dopamine level contributes to hydroxyl radical generation and subsequent neurodegeneration in the striatum in 3-nitropropionic acid-induced Huntington's disease in rats
    • Pandey M, Borah A, Varghese M, Barman PK, Mohanakumar KP, Usha R (2009) Striatal dopamine level contributes to hydroxyl radical generation and subsequent neurodegeneration in the striatum in 3-nitropropionic acid-induced Huntington's disease in rats. Neurochem Int 55:431-437
    • (2009) Neurochem Int , vol.55 , pp. 431-437
    • Pandey, M.1    Borah, A.2    Varghese, M.3    Barman, P.K.4    Mohanakumar, K.P.5    Usha, R.6
  • 17
    • 0035783462 scopus 로고    scopus 로고
    • Resistance to NMDA toxicity correlates with appearance of nuclear inclusions, behavioural deficits and changes in calcium homeostasis in mice transgenic for exon 1 of the huntington gene
    • DOI 10.1046/j.0953-816X.2001.01767.x
    • Hansson O, Guatteo E, Mercuri NB, Bernardi G, Li XJ, Castilho RF, Brundin P (2001) Resistance to NMDA toxicity correlates with appearance of nuclear inclusions, behavioural deficits and changes in calcium homeostasis in mice transgenic for exon 1 of the Huntington gene. Eur J Neurosci 14:1492-1504 (Pubitemid 35463716)
    • (2001) European Journal of Neuroscience , vol.14 , Issue.9 , pp. 1492-1504
    • Hansson, O.1    Guatteo, E.2    Mercuri, N.B.3    Bernardi, G.4    Li, X.-J.5    Castilho, R.F.6    Brundin, P.7
  • 20
    • 0034628981 scopus 로고    scopus 로고
    • 3-Nitropropionic acid induced in vivo protein oxidation in striatal and cortical synaptosomes: Insights into Huntington's disease
    • DOI 10.1016/S0006-8993(00)01948-X, PII S000689930001948X
    • La Fontaine MA, Geddes JW, Banks A, Butterfield DA (2000) 3-Nitropropionic acid-induced in vivo protein oxidation in striatal and cortical synaptosomes: insights into Huntington's disease. Brain Res 858:356-362 (Pubitemid 30119997)
    • (2000) Brain Research , vol.858 , Issue.2 , pp. 356-362
    • La, F.M.A.1    Geddes, J.W.2    Banks, A.3    Butterfield, D.A.4
  • 23
    • 33748591092 scopus 로고    scopus 로고
    • Oxidative stress in skin fibroblasts cultures of patients with Huntington's disease
    • del Hoyo P, Redondo AG, de Bustos F et al (2006) Oxidative stress in skin fibroblasts cultures of patients with Huntington's disease. Neurochem Res 31:1103-1109
    • (2006) Neurochem Res , vol.31 , pp. 1103-1109
    • Del Hoyo, P.1    Redondo, A.G.2    De Bustos, F.3
  • 27
    • 37349084923 scopus 로고    scopus 로고
    • +-linked State 3 respiration and complex-I activity are compromised in the cerebral cortex of 3-nitropropionic acid-induced rat model of Huntington's disease
    • DOI 10.1111/j.1471-4159.2007.04996.x
    • Pandey M, Varghese M, Sindhu KM, Sreetama S, Navneet AK, Mohanakumar KP, Usha R (2008) Mitochondrial NAD+-linked State 3 respiration and complex-I activity are compromised in the cerebral cortex of 3-nitropropionic acid-induced rat model of Huntington's disease. J Neurochem 104:420-434 (Pubitemid 350293876)
    • (2008) Journal of Neurochemistry , vol.104 , Issue.2 , pp. 420-434
    • Pandey, M.1    Varghese, M.2    Sindhu, K.M.3    Sreetama, S.4    Navneet, A.K.5    Mohanakumar, K.P.6    Usha, R.7
  • 28
    • 67649856863 scopus 로고    scopus 로고
    • Distinct conformations of in vitro and in vivo amyloids of Huntingtin-exon1 show different cytotoxicity
    • Nekooki-Machida Y, Kurosawa M, Nukina N, Ito K, Oda T, Tanaka M (2009) Distinct conformations of in vitro and in vivo amyloids of Huntingtin-exon1 show different cytotoxicity. Proc Natl Acad Sci USA 106:9679-9684
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 9679-9684
    • Nekooki-Machida, Y.1    Kurosawa, M.2    Nukina, N.3    Ito, K.4    Oda, T.5    Tanaka, M.6
  • 30
    • 0036850529 scopus 로고    scopus 로고
    • Aggregated polyglutamine peptides delivered to nuclei are toxic to mammalian cells
    • Yang W, Dunlap JR, Andrews RB, Wetzel R (2002) Aggregated polyglutamine peptides delivered to nuclei are toxic to mammalian cells. Hum Mol Genet 11:2905-2917
    • (2002) Hum Mol Genet , vol.11 , pp. 2905-2917
    • Yang, W.1    Dunlap, J.R.2    Andrews, R.B.3    Wetzel, R.4
  • 31
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • DOI 10.1038/nature02998
    • Arrasate M, Mitra S, Schweitzer ES, Segal MR, Finkbeiner S (2004) Inclusion body formation reduces levels of mutant Huntingtin and the risk of neuronal death. Nature 431:805-810 (Pubitemid 39434070)
    • (2004) Nature , vol.431 , Issue.7010 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 32
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DOI 10.1126/science.277.5334.1990
    • DiFiglia M, Sapp E, Chase KO, Davies SW, Bates GP, Vonsattel JP, Aronin N (1997) Aggregation of Huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 277:1990-1993 (Pubitemid 27449140)
    • (1997) Science , vol.277 , Issue.5334 , pp. 1990-1993
    • DiFiglia, M.1    Sapp, E.2    Chase, K.O.3    Davies, S.W.4    Bates, G.P.5    Vonsattel, J.P.6    Aronin, N.7
  • 33
    • 79952443408 scopus 로고    scopus 로고
    • Mutant Huntingtin binds the mitochondrial fission GTPase dynamin-related protein-1 and increases its enzymatic activity
    • Song W, Chen J, Petrilli A (2011) Mutant Huntingtin binds the mitochondrial fission GTPase dynamin-related protein-1 and increases its enzymatic activity. Nat Med 17:377-382
    • (2011) Nat Med , vol.17 , pp. 377-382
    • Song, W.1    Chen, J.2    Petrilli, A.3
  • 34
    • 79952585486 scopus 로고    scopus 로고
    • Abnormal mitochondrial dynamics, mitochondrial loss and mutant Huntingtin oligomers in Huntington's disease: Implications for selective neuronal damage
    • Shirendeb U, Reddy AP, Manczak M, Calkins MJ, Mao P, Tagle DA, Reddy PH (2011) Abnormal mitochondrial dynamics, mitochondrial loss and mutant Huntingtin oligomers in Huntington's disease: implications for selective neuronal damage. Hum Mol Genet 20:1438-1455
    • (2011) Hum Mol Genet , vol.20 , pp. 1438-1455
    • Shirendeb, U.1    Reddy, A.P.2    Manczak, M.3    Calkins, M.J.4    Mao, P.5    Tagle, D.A.6    Reddy, P.H.7
  • 35
  • 36
    • 84855395163 scopus 로고    scopus 로고
    • Mutant Huntingtin's interaction with mitochondrial protein Drp1 impairs mitochondrial biogenesis and causes defective axonal transport and synaptic degeneration in Huntington's disease
    • Shirendeb UP, Calkins MJ, Manczak M, Anekonda V, Dufour B, McBride JL, Mao P, Reddy PH (2012) Mutant Huntingtin's interaction with mitochondrial protein Drp1 impairs mitochondrial biogenesis and causes defective axonal transport and synaptic degeneration in Huntington's disease. Hum Mol Genet 21:406-420
    • (2012) Hum Mol Genet , vol.21 , pp. 406-420
    • Shirendeb, U.P.1    Calkins, M.J.2    Manczak, M.3    Anekonda, V.4    Dufour, B.5    McBride, J.L.6    Mao, P.7    Reddy, P.H.8
  • 40
  • 41
    • 29144468251 scopus 로고    scopus 로고
    • 3-Nitropropionic acid: A mitochondrial toxin to uncover physiopathological mechanisms underlying striatal degeneration in Huntington's disease
    • DOI 10.1111/j.1471-4159.2005.03515.x
    • Brouillet E, Jacquard C, Bizat N, Blum D (2005) 3-Nitropropionic acid: a mitochondrial toxin to uncover physiopathological mechanisms underlying striatal degeneration in Huntington's disease. J Neurochem 95:1521-1540 (Pubitemid 41804051)
    • (2005) Journal of Neurochemistry , vol.95 , Issue.6 , pp. 1521-1540
    • Brouillet, E.1    Jacquard, C.2    Bizat, N.3    Blum, D.4
  • 43
    • 0026357457 scopus 로고
    • 3-Nitropropionic acid-exogenous animal neurotoxin and possible human striatal toxin
    • Ludolph AC, He F, Spencer PS, Hammerstad J, Sabri M (1991) 3-Nitropropionic acid-exogenous animal neurotoxin and possible human striatal toxin. Can J Neurol Sci 18:492-498
    • (1991) Can J Neurol Sci , vol.18 , pp. 492-498
    • Ludolph, A.C.1    He, F.2    Spencer, P.S.3    Hammerstad, J.4    Sabri, M.5
  • 45
    • 0035336658 scopus 로고    scopus 로고
    • Altered proteasomal function due to the expression of polyglutamine-expanded truncated N-terminal huntingtin induces apoptosis by caspase activation through mitochondrial cytochrome c release
    • Jana NR, Zemskov EA, Wang Gh, Nukina N (2001) Altered proteasomal function due to the expression of polyglutamine-expanded truncated N-terminal Huntingtin induces apoptosis by caspase activation through mitochondrial cytochrome c release. Hum Mol Genet 10:1049-1059 (Pubitemid 32447782)
    • (2001) Human Molecular Genetics , vol.10 , Issue.10 , pp. 1049-1059
    • Jana, N.R.1    Zemskov, E.A.2    Wang, G.-H.3    Nukina, N.4
  • 46
    • 34447309764 scopus 로고    scopus 로고
    • Extended polyglutamine repeats trigger a feedback loop involving the mitochondrial complex III, the proteasome and huntingtin aggregates
    • DOI 10.1093/hmg/ddm023
    • Fukui H, Moraes CT (2007) Extended polyglutamine repeats trigger a feedback loop involving the mitochondrial complex III, the proteasome and Huntingtin aggregates. Hum Mol Genet 16:783-797 (Pubitemid 47061625)
    • (2007) Human Molecular Genetics , vol.16 , Issue.7 , pp. 783-797
    • Fukui, H.1    Moraes, C.T.2
  • 47
    • 0033520166 scopus 로고    scopus 로고
    • Oxidative damage to mitochondrial DNA in Huntington's disease parietal cortex
    • Polidori MC, Mecocci P, Browne SE, Senin U, Beal MF (1999) Oxidative damage to mitochondrial DNA in Huntington's disease parietal cortex. Neurosci Lett 272:53-56
    • (1999) Neurosci Lett , vol.272 , pp. 53-56
    • Polidori, M.C.1    Mecocci, P.2    Browne, S.E.3    Senin, U.4    Beal, M.F.5
  • 48
    • 0027082367 scopus 로고
    • Allocortical involvement in Huntington's disease
    • Braak H, Braak E (1992) Allocortical involvement in Huntington's disease. Neuropathol Appl Neurobiol 18:539-547 (Pubitemid 23010156)
    • (1992) Neuropathology and Applied Neurobiology , vol.18 , Issue.6 , pp. 539-547
    • Braak, H.1    BRaak, E.2
  • 49
    • 0033803048 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor gamma coactivator-1 promotes cardiac mitochondrial biogenesis
    • Lehman JJ, Barger PM, Kovacs A, Saffitz JE, Medeiros DM, Kelly DP (2000) Peroxisome proliferator-activated receptor gamma coactivator-1 promotes cardiac mitochondrial biogenesis. J Clin Invest 106:847-856
    • (2000) J Clin Invest , vol.106 , pp. 847-856
    • Lehman, J.J.1    Barger, P.M.2    Kovacs, A.3    Saffitz, J.E.4    Medeiros, D.M.5    Kelly, D.P.6
  • 51
    • 33749042331 scopus 로고    scopus 로고
    • Transcriptional Repression of PGC-1alpha by Mutant Huntingtin Leads to Mitochondrial Dysfunction and Neurodegeneration
    • DOI 10.1016/j.cell.2006.09.015, PII S0092867406012050
    • Cui L, Jeong H, Borovecki F, Parkhurst CN, Tanese N, Krainc D (2006) Transcriptional repression of PGC-1alpha by mutant Huntingtin leads to mitochondrial dysfunction and neurodegeneration. Cell 127:59-69 (Pubitemid 44466642)
    • (2006) Cell , vol.127 , Issue.1 , pp. 59-69
    • Cui, L.1    Jeong, H.2    Borovecki, F.3    Parkhurst, C.N.4    Tanese, N.5    Krainc, D.6
  • 52
    • 67650061723 scopus 로고    scopus 로고
    • Impaired PGC-1a function in muscle in Huntington's disease
    • Chaturvedi RK, Adhihetty P, Shukla S et al (2009) Impaired PGC-1a function in muscle in Huntington's disease. Hum Mol Genet 18:3048-3065
    • (2009) Hum Mol Genet , vol.18 , pp. 3048-3065
    • Chaturvedi, R.K.1    Adhihetty, P.2    Shukla, S.3
  • 54
    • 37249083913 scopus 로고    scopus 로고
    • Mitochondrial sensitivity and altered calcium handling underlie enhanced NMDA-induced apoptosis in YAC128 model of Huntington's disease
    • DOI 10.1523/JNEUROSCI.3455-07.2007
    • Fernandes HB, Baimbridge KG, Church J, Hayden MR, Raymond LA (2007) Mitochondrial sensitivity and altered calcium handling underlie enhanced NMDA-induced apoptosis in YAC128 model of Huntington's disease. J Neurosci 27:13614-13623 (Pubitemid 350278271)
    • (2007) Journal of Neuroscience , vol.27 , Issue.50 , pp. 13614-13623
    • Fernandes, H.B.1    Baimbridge, K.G.2    Church, J.3    Hayden, M.R.4    Raymond, L.A.5
  • 55
    • 14244264746 scopus 로고    scopus 로고
    • 2+-induced permeability transition in human lymphoblastoid cell mitochondria from normal and Huntington's disease individuals
    • 2+-induced permeability transition in human lymphoblastoid cell mitochondria from normal and Huntington's disease individuals. Mol Cell Biochem 269:143-152
    • (2005) Mol Cell Biochem , vol.269 , pp. 143-152
    • Panov, A.V.1    Lund, S.2    Greenamyre, J.T.3
  • 56
    • 1442274934 scopus 로고    scopus 로고
    • Mitochondrial calcium, oxidative stress and apoptosis in a neurodegenerative disease model induced by 3-nitropropionic acid
    • DOI 10.1046/j.1471-4159.2003.02250.x
    • Rosenstock TR, Carvalho AC, Jurkiewicz A, Frussa-Filho R, Smaili SS (2004) Mitochondrial calcium, oxidative stress and apoptosis in a neurodegenerative disease model induced by 3-nitropropionic acid. J Neurochem 88:1220-1228 (Pubitemid 38280690)
    • (2004) Journal of Neurochemistry , vol.88 , Issue.5 , pp. 1220-1228
    • Rosenstock, T.R.1    Carvalho, A.C.P.2    Jurkiewicz, A.3    Frussa-Filho, R.4    Smaili, S.S.5
  • 57
    • 0035166814 scopus 로고    scopus 로고
    • Dynamin-related protein Drp1 is required for mitochondrial division in mammalian cells
    • Smirnova E, Griparic L, Shurland DL, van der Bliek AM (2001) Dynamin-related protein Drp1 is required for mitochondrial division in mammalian cells. Mol Biol Cell 12:2245-2256 (Pubitemid 33051954)
    • (2001) Molecular Biology of the Cell , vol.12 , Issue.8 , pp. 2245-2256
    • Smirnova, E.1    Griparic, L.2    Shurland, D.-L.3    Van Der, B.A.M.4
  • 58
    • 57349160257 scopus 로고    scopus 로고
    • Dephosphorylation by calcineurin regulates translocation of Drp1 to mitochondria
    • Cereghetti GM, Stangherlin A, Martins de Brito O (2008) Dephosphorylation by calcineurin regulates translocation of Drp1 to mitochondria. Proc Natl Acad Sci USA 105:15803-15808
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 15803-15808
    • Cereghetti, G.M.1    Stangherlin, A.2    Martins De Brito, O.3
  • 59
    • 34848840991 scopus 로고    scopus 로고
    • Reversible phosphorylation of Drp1 by cyclic AMP-dependent protein kinase and calcineurin regulates mitochondrial fission and cell death
    • DOI 10.1038/sj.embor.7401062, PII 7401062
    • Cribbs JT, Strack S (2007) Reversible phosphorylation of Drp1 by cyclic AMP-dependent protein kinase and calcineurin regulates mitochondrial fission and cell death. EMBO Rep 8:939-944 (Pubitemid 47500477)
    • (2007) EMBO Reports , vol.8 , Issue.10 , pp. 939-944
    • Cribbs, J.T.1    Strack, S.2
  • 60
    • 1542380494 scopus 로고    scopus 로고
    • Sumo1 conjugates mitochondrial substrates and participates in mitochondrial fission
    • DOI 10.1016/S0960-9822(04)00084-3, PII S0960982204000843
    • Harder Z, Zunino R, McBride H (2004) Sumo1 conjugates mitochondrial substrates and participates in mitochondrial fission. Curr Biol 14:340-345 (Pubitemid 38300214)
    • (2004) Current Biology , vol.14 , Issue.4 , pp. 340-345
    • Harder, Z.1    Zunino, R.2    McBride, H.3
  • 61
    • 34347398050 scopus 로고    scopus 로고
    • The mitochondrial E3 ubiquitin ligase MARCH5 is required for Drp1 dependent mitochondrial division
    • DOI 10.1083/jcb.200611064
    • Karbowski M, Neutzner A, Youle RJ (2007) The mitochondrial E3 ubiquitin ligase MARCH5 is required for Drp1 dependent mitochondrial division. J Cell Biol 178:71-84 (Pubitemid 47026403)
    • (2007) Journal of Cell Biology , vol.178 , Issue.1 , pp. 71-84
    • Karbowski, M.1    Neutzner, A.2    Youle, R.J.3
  • 62
    • 76649142385 scopus 로고    scopus 로고
    • Loss of MARCH5 mitochondrial E3 ubiquitin ligase induces cellular senescence through dynamin-related protein 1 and mitofusin 1
    • Park YY, Lee S, Karbowski M, Neutzner A, Youle RJ, Cho H (2010) Loss of MARCH5 mitochondrial E3 ubiquitin ligase induces cellular senescence through dynamin-related protein 1 and mitofusin 1. J Cell Sci 123:619-626
    • (2010) J Cell Sci , vol.123 , pp. 619-626
    • Park, Y.Y.1    Lee, S.2    Karbowski, M.3    Neutzner, A.4    Youle, R.J.5    Cho, H.6
  • 63
    • 34249689057 scopus 로고    scopus 로고
    • Mitotic phosphorylation of dynamin-related GTPase Drp1 participates in mitochondrial fission
    • DOI 10.1074/jbc.M607279200
    • Taguchi N, Ishihara N, Jofuku A, Oka T, Mihara K (2007) Mitotic phosphorylation of dynamin-related GTPase Drp1 participates in mitochondrial fission. J Biol Chem 282:11521-11529 (Pubitemid 47100787)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.15 , pp. 11521-11529
    • Taguchi, N.1    Ishihara, N.2    Jofuku, A.3    Oka, T.4    Mihara, K.5
  • 64
    • 34248225298 scopus 로고    scopus 로고
    • The SUMO protease SENP5 is required to maintain mitochondrial morphology and function
    • DOI 10.1242/jcs.03418
    • Zunino R, Schauss A, Rippstein P, Andrade-Navarro M, McBride HM (2007) The SUMO protease SENP5 is required to maintain mitochondrial morphology and function. J Cell Sci 120:1178-1188 (Pubitemid 46711836)
    • (2007) Journal of Cell Science , vol.120 , Issue.7 , pp. 1178-1188
    • Zunino, R.1    Schauss, A.2    Rippstein, P.3    Andrade-Navarro, M.4    McBride, H.M.5
  • 65
    • 77955432558 scopus 로고    scopus 로고
    • S-nitrosylation of Drp1 links excessive mitochondrial fission to neuronal injury in neurodegeneration
    • Nakamura T, Cieplak P, Cho DH, Godzik A, Lipton SA (2010) S-nitrosylation of Drp1 links excessive mitochondrial fission to neuronal injury in neurodegeneration. Mitochondrion 10:573-578
    • (2010) Mitochondrion , vol.10 , pp. 573-578
    • Nakamura, T.1    Cieplak, P.2    Cho, D.H.3    Godzik, A.4    Lipton, S.A.5
  • 66
    • 58949099388 scopus 로고    scopus 로고
    • Effects of overexpression of Huntingtin proteins on mitochondrial integrity
    • Wang H, Lim PJ, Karbowski M, Monteiro MJ (2009) Effects of overexpression of Huntingtin proteins on mitochondrial integrity. Hum Mol Genet 18:737-752
    • (2009) Hum Mol Genet , vol.18 , pp. 737-752
    • Wang, H.1    Lim, P.J.2    Karbowski, M.3    Monteiro, M.J.4
  • 67
    • 78650284389 scopus 로고    scopus 로고
    • Mitochondrial fission and cristae disruption increase the response of cell models of Huntington's disease to apoptotic stimuli
    • Costa V, Giacomello M, Hudec R (2010) Mitochondrial fission and cristae disruption increase the response of cell models of Huntington's disease to apoptotic stimuli. EMBO Mol Med 2:490-503
    • (2010) EMBO Mol Med , vol.2 , pp. 490-503
    • Costa, V.1    Giacomello, M.2    Hudec, R.3
  • 68
    • 67349120572 scopus 로고    scopus 로고
    • Complex II inhibition by 3-NP causes mitochondrial fragmentation and neuronal cell death via an NMDA-and ROS-dependent pathway
    • Liot G, Bossy B, Lubitz S, Kushnareva Y, Sejbuk N, Bossy-Wetzel E (2009) Complex II inhibition by 3-NP causes mitochondrial fragmentation and neuronal cell death via an NMDA-and ROS-dependent pathway. Cell Death Differ 16:899-909
    • (2009) Cell Death Differ , vol.16 , pp. 899-909
    • Liot, G.1    Bossy, B.2    Lubitz, S.3    Kushnareva, Y.4    Sejbuk, N.5    Bossy-Wetzel, E.6
  • 69
    • 84880940047 scopus 로고    scopus 로고
    • S-Nitrosylation of dynamin-related protein 1 mediates mutant Huntingtin-induced mitochondrial fragmentation and neuronal injury in Huntington's disease
    • Haun F, Nakamura T, Shiu AD, Cho DH, Tsunemi T, Holland EA, La Spada AR, Lipton SA (2013) S-Nitrosylation of dynamin-related protein 1 mediates mutant Huntingtin-induced mitochondrial fragmentation and neuronal injury in Huntington's disease. Antioxid Redox Signal 19:1173-1184
    • (2013) Antioxid Redox Signal , vol.19 , pp. 1173-1184
    • Haun, F.1    Nakamura, T.2    Shiu, A.D.3    Cho, D.H.4    Tsunemi, T.5    Holland, E.A.6    La Spada, A.R.7    Lipton, S.A.8
  • 70
    • 70849122412 scopus 로고    scopus 로고
    • Disruption of mitochondrial DNA replication in Drosophila increases mitochondrial fast axonal transport in vivo
    • Baqri RM, Turner BA, Rheuben MB, Hammond BD, Kaguni LS, Miller KE (2009) Disruption of mitochondrial DNA replication in Drosophila increases mitochondrial fast axonal transport in vivo. PLoS One 4:e7874
    • (2009) PLoS One , vol.4
    • Baqri, R.M.1    Turner, B.A.2    Rheuben, M.B.3    Hammond, B.D.4    Kaguni, L.S.5    Miller, K.E.6
  • 71
    • 3242875557 scopus 로고    scopus 로고
    • Axonal mitochondrial transport and potential are correlated
    • DOI 10.1242/jcs.01130
    • Miller KE, Sheetz MP (2004) Axonal mitochondrial transport and potential are correlated. J Cell Sci 117:2791-2804 (Pubitemid 38997261)
    • (2004) Journal of Cell Science , vol.117 , Issue.13 , pp. 2791-2804
    • Miller, K.E.1    Sheetz, M.P.2
  • 72
    • 30544452263 scopus 로고    scopus 로고
    • The axonal transport of mitochondria
    • DOI 10.1242/jcs.02745
    • Hollenbeck PJ, Saxton WM (2005) The axonal transport of mitochondria. J Cell Sci 118:5411-5419 (Pubitemid 43079283)
    • (2005) Journal of Cell Science , vol.118 , Issue.23 , pp. 5411-5419
    • Hollenbeck, P.J.1    Saxton, W.M.2
  • 73
    • 84862870271 scopus 로고    scopus 로고
    • The axonal transport of mitochondria
    • Saxton WM, Hollenbeck PJ (2012) The axonal transport of mitochondria. J Cell Sci 125:2095-2104
    • (2012) J Cell Sci , vol.125 , pp. 2095-2104
    • Saxton, W.M.1    Hollenbeck, P.J.2
  • 75
    • 67349234086 scopus 로고    scopus 로고
    • The Miro GTPases: At the heart of the mitochondrial transport machinery
    • Reis K, Fransson A, Aspenström P (2009) The Miro GTPases: at the heart of the mitochondrial transport machinery. FEBS Lett 583:1391-1398
    • (2009) FEBS Lett , vol.583 , pp. 1391-1398
    • Reis, K.1    Fransson, A.2    Aspenström, P.3
  • 76
    • 60149097713 scopus 로고    scopus 로고
    • GTPase dependent recruitment of Grif-1 by Miro1 regulates mitochondrial trafficking in hippocampal neurons
    • MacAskill AF, Brickley K, Stephenson FA, Kittler JT (2009) GTPase dependent recruitment of Grif-1 by Miro1 regulates mitochondrial trafficking in hippocampal neurons. Mol Cell Neurosci 40:301-312
    • (2009) Mol Cell Neurosci , vol.40 , pp. 301-312
    • MacAskill, A.F.1    Brickley, K.2    Stephenson, F.A.3    Kittler, J.T.4
  • 77
    • 5444235717 scopus 로고    scopus 로고
    • Syntabulin is a microtubule-associated protein implicated in syntaxin transport in neurons
    • DOI 10.1038/ncb1169
    • Su Q, Cai Q, Gerwin C, Smith CL, Sheng ZH (2004) Syntabulin is a microtubule-associated protein implicated in syntaxin transport in neurons. Nat Cell Biol 6:941-953 (Pubitemid 39359847)
    • (2004) Nature Cell Biology , vol.6 , Issue.10 , pp. 941-953
    • Su, Q.1    Cai, Q.2    Gerwin, C.3    Smith, C.L.4    Sheng, Z.-H.5
  • 78
    • 70350444463 scopus 로고    scopus 로고
    • KIF5B motor adaptor syntabulin maintains synaptic transmission in sympathetic neurons
    • Ma H, Cai Q, Lu W, Sheng ZH, Mochida S (2009) KIF5B motor adaptor syntabulin maintains synaptic transmission in sympathetic neurons. J Neurosci 29:13019-13029
    • (2009) J Neurosci , vol.29 , pp. 13019-13029
    • Ma, H.1    Cai, Q.2    Lu, W.3    Sheng, Z.H.4    Mochida, S.5
  • 79
    • 75149115122 scopus 로고    scopus 로고
    • Control of mitochondrial transport and localization in neurons
    • MacAskill AF, Kittler JT (2010) Control of mitochondrial transport and localization in neurons. Trends Cell Biol 20:102-112
    • (2010) Trends Cell Biol , vol.20 , pp. 102-112
    • MacAskill, A.F.1    Kittler, J.T.2
  • 80
    • 0036257364 scopus 로고    scopus 로고
    • Voltage-dependent anion-selective channel (VDAC) interacts with the dynein light chain Tctex1 and the heat-shock protein PBP74
    • DOI 10.1016/S1357-2725(02)00026-2, PII S1357272502000262
    • Schwarzer C, Barnikol-Watanabe S, Thinnes FP, Hilschmann N (2002) Voltage-dependent anion-selective channel (VDAC) interacts with the dynein light chain Tctex1 and the heat-shock protein PBP74. Int J Biochem Cell Biol 34:1059-1070 (Pubitemid 34493767)
    • (2002) International Journal of Biochemistry and Cell Biology , vol.34 , Issue.9 , pp. 1059-1070
    • Schwarzer, C.1    Barnikol-Watanabe, S.2    Thinnes, F.P.3    Hilschmann, N.4
  • 81
    • 79956316194 scopus 로고    scopus 로고
    • Myelination and axonal electrical activity modulate the distribution and motility of mitochondria at CNS nodes of Ranvier
    • Ohno N, Kidd GJ, Mahad D, Kiryu-Seo S, Avishai A, Komuro H, Trapp BD (2011) Myelination and axonal electrical activity modulate the distribution and motility of mitochondria at CNS nodes of Ranvier. J Neurosci 31:7249-7258
    • (2011) J Neurosci , vol.31 , pp. 7249-7258
    • Ohno, N.1    Kidd, G.J.2    Mahad, D.3    Kiryu-Seo, S.4    Avishai, A.5    Komuro, H.6    Trapp, B.D.7
  • 82
    • 33645843025 scopus 로고    scopus 로고
    • Nitric oxide inhibits mitochondrial movement in forebrain neurons associated with disruption of mitochondrial membrane potential
    • Rintoul GL, Bennett VJ, Papaconstandinou NA, Reynolds IJ (2006) Nitric oxide inhibits mitochondrial movement in forebrain neurons associated with disruption of mitochondrial membrane potential. J Neurochem 97:800-806
    • (2006) J Neurochem , vol.97 , pp. 800-806
    • Rintoul, G.L.1    Bennett, V.J.2    Papaconstandinou, N.A.3    Reynolds, I.J.4
  • 84
    • 9644290768 scopus 로고    scopus 로고
    • Mitochondrial organization and motility probed by two-photon microscopy in cultured mouse brainstem neurons
    • DOI 10.1016/j.yexcr.2004.09.025, PII S0014482704005713
    • Müller M, Mironov SL, Ivannikov MV, Schmidt J, Richter DW (2005) Mitochondrial organization and motility probed by two-photon microscopy in cultured mouse brainstem neurons. Exp Cell Res 303:114-127 (Pubitemid 39575148)
    • (2005) Experimental Cell Research , vol.303 , Issue.1 , pp. 114-127
    • Muller, M.1    Mironov, S.L.2    Ivannikov, M.V.3    Schmidt, J.4    Richter, D.W.5
  • 85
    • 33645840444 scopus 로고    scopus 로고
    • Nitric oxide impairs mitochondrial movement in cortical neurons during hypoxia
    • Zanelli SA, Trimmer PA, Solenski NJ (2006) Nitric oxide impairs mitochondrial movement in cortical neurons during hypoxia. J Neurochem 97:724-736
    • (2006) J Neurochem , vol.97 , pp. 724-736
    • Zanelli, S.A.1    Trimmer, P.A.2    Solenski, N.J.3
  • 86
    • 77949359551 scopus 로고    scopus 로고
    • Activity-dependent regulation of mitochondrial motility by calcium and Na/K-ATPase at nodes of Ranvier of myelinated nerves
    • Zhang CL, Ho PL, Kintner DB, Sun D, Chiu SY (2010) Activity-dependent regulation of mitochondrial motility by calcium and Na/K-ATPase at nodes of Ranvier of myelinated nerves. J Neurosci 30:3555-3566
    • (2010) J Neurosci , vol.30 , pp. 3555-3566
    • Zhang, C.L.1    Ho, P.L.2    Kintner, D.B.3    Sun, D.4    Chiu, S.Y.5
  • 87
    • 77949801029 scopus 로고    scopus 로고
    • Mitofusin 2 is necessary for transport of axonal mitochondria and interacts with the Miro/Milton complex
    • Misko A, Jiang S, Wegorzewska I, Milbrandt J, Baloh RH (2010) Mitofusin 2 is necessary for transport of axonal mitochondria and interacts with the Miro/Milton complex. J Neurosci 30:4232-4240
    • (2010) J Neurosci , vol.30 , pp. 4232-4240
    • Misko, A.1    Jiang, S.2    Wegorzewska, I.3    Milbrandt, J.4    Baloh, R.H.5
  • 88
    • 33646136884 scopus 로고    scopus 로고
    • Mutant Huntingtin aggregates impair mitochondrial movement and trafficking in cortical neurons
    • Chang DT, Rintoul GL, Pandipati S, Reynolds IJ (2006) Mutant Huntingtin aggregates impair mitochondrial movement and trafficking in cortical neurons. Neurobiol Dis 22:388-400
    • (2006) Neurobiol Dis , vol.22 , pp. 388-400
    • Chang, D.T.1    Rintoul, G.L.2    Pandipati, S.3    Reynolds, I.J.4
  • 91
    • 33645642673 scopus 로고    scopus 로고
    • Interaction of Huntingtin-associated protein-1 with kinesin light chain: Implications in intracellular trafficking in neurons
    • DOI 10.1074/jbc.M509806200
    • McGuire JR, Rong J, Li SH, Li XJ (2006) Interaction of Huntingtin-associated protein-1 with kinesin light chain: implications in intracellular trafficking in neurons. J Biol Chem 281:3552-3559 (Pubitemid 43845972)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.6 , pp. 3552-3559
    • McGuire, J.R.1    Rong, J.2    Li, S.-H.3    Li, X.-J.4
  • 92
    • 84859904873 scopus 로고    scopus 로고
    • Shaping the role of mitochondria in the pathogenesis of Huntington's disease
    • Costa V, Scorrano L (2012) Shaping the role of mitochondria in the pathogenesis of Huntington's disease. EMBO J 31:1853-1864
    • (2012) EMBO J , vol.31 , pp. 1853-1864
    • Costa, V.1    Scorrano, L.2
  • 95
    • 9144223729 scopus 로고    scopus 로고
    • Inefficient degradation of truncated polyglutamine proteins by the proteasome
    • DOI 10.1038/sj.emboj.7600426
    • Holmberg CI, Staniszewski KE, Mensah KN, Matouschek A, Morimoto RI (2004) Inefficient degradation of truncated polyglutamine proteins by the proteasome. EMBO J 23:4307-4318 (Pubitemid 39546168)
    • (2004) EMBO Journal , vol.23 , Issue.21 , pp. 4307-4318
    • Holmberg, C.I.1    Staniszewski, K.E.2    Mensah, K.N.3    Matouschek, A.4    Morimoto, R.I.5
  • 96
    • 0032475931 scopus 로고    scopus 로고
    • Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions
    • Saudou F, Finkbeiner S, Devys D, Greenberg ME (1998) Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions. Cell 95:55-66
    • (1998) Cell , vol.95 , pp. 55-66
    • Saudou, F.1    Finkbeiner, S.2    Devys, D.3    Greenberg, M.E.4
  • 97
    • 84883145851 scopus 로고    scopus 로고
    • Morphometric analysis of Huntington's disease neurodegeneration in Drosophila
    • Song W, Smith MR, Syed A (2013) Morphometric analysis of Huntington's disease neurodegeneration in Drosophila. Methods Mol Biol 1017:41-57
    • (2013) Methods Mol Biol , vol.1017 , pp. 41-57
    • Song, W.1    Smith, M.R.2    Syed, A.3
  • 98
    • 59649109467 scopus 로고    scopus 로고
    • Decreased BDNF levels are a major contributor to the embryonic phenotype of Huntingtin knockdown zebrafish
    • Diekmann H, Anichtchik O, Fleming A et al (2009) Decreased BDNF levels are a major contributor to the embryonic phenotype of Huntingtin knockdown zebrafish. J Neurosci 29:1343-1349
    • (2009) J Neurosci , vol.29 , pp. 1343-1349
    • Diekmann, H.1    Anichtchik, O.2    Fleming, A.3
  • 99
    • 84885020652 scopus 로고    scopus 로고
    • Gutathione peroxidase activity is neuroprotective in models of Huntington's disease
    • Mason RP, Casu M, Butler N (2013) Gutathione peroxidase activity is neuroprotective in models of Huntington's disease. Nat Genet 45:1249-1254
    • (2013) Nat Genet , vol.45 , pp. 1249-1254
    • Mason, R.P.1    Casu, M.2    Butler, N.3
  • 100
    • 0031056685 scopus 로고    scopus 로고
    • Instability of highly expanded CAG repeats in mice transgenic for the Huntington's disease mutation
    • DOI 10.1038/ng0297-197
    • Mangiarini L, Sathasivam K, Mahal A, Mott R, Seller M, Bates GP (1997) Instability of highly expanded CAG repeats in mice transgenic for the Huntington's disease mutation. Nat Genet 15:197-200 (Pubitemid 27061643)
    • (1997) Nature Genetics , vol.15 , Issue.2 , pp. 197-200
    • Mangiarini, L.1    Sathasivam, K.2    Mahal, A.3    Mott, R.4    Seller, M.5    Bates, G.P.6
  • 101
    • 56549089781 scopus 로고    scopus 로고
    • Mitochondrial DNA damage is a hallmark of chemically induced and the R6/2 transgenic model of Huntington's disease
    • Amst
    • Acevedo-Torres K, Berríos L, Rosario N et al (2009) Mitochondrial DNA damage is a hallmark of chemically induced and the R6/2 transgenic model of Huntington's disease. DNA Repair (Amst) 8:126-136
    • (2009) DNA Repair , vol.8 , pp. 126-136
    • Acevedo-Torres, K.1    Berríos, L.2    Rosario, N.3
  • 102
    • 0035668684 scopus 로고    scopus 로고
    • Increased oxidative damage to DNA in a transgenic mouse model of Huntington's disease
    • DOI 10.1046/j.1471-4159.2001.00689.x
    • Bogdanov MB, Andreassen OA, Dedeoglu A, Ferrante RJ, Beal MF (2001) Increased oxidative damage to DNA in a transgenic mouse model of Huntington's disease. J Neurochem 79:1246-1249 (Pubitemid 34019802)
    • (2001) Journal of Neurochemistry , vol.79 , Issue.6 , pp. 1246-1249
    • Bogdanov, M.B.1    Andreassen, O.A.2    Dedeoglu, A.3    Ferrante, R.J.4    Beal, M.F.5
  • 104
    • 29644433718 scopus 로고    scopus 로고
    • Proteasome impairment does not contribute to pathogenesis in R6/2 Huntington's disease mice: Exclusion of proteasome activator REGgamma as a therapeutic target
    • DOI 10.1093/hmg/ddi423
    • Bett JS, Goellner GM, Woodman B, Pratt G, Rechsteiner M, Bates GP (2006) Proteasome impairment does not contribute to pathogenesis in R6/2 Huntington's disease mice: exclusion of proteasome activator REG gamma as a therapeutic target. Hum Mol Genet 15:33-44 (Pubitemid 43020102)
    • (2006) Human Molecular Genetics , vol.15 , Issue.1 , pp. 33-44
    • Bett, J.S.1    Goellner, G.M.2    Woodman, B.3    Pratt, G.4    Rechsteiner, M.5    Bates, G.P.6
  • 105
    • 53349101055 scopus 로고    scopus 로고
    • Compensatory changes in the ubiquitin-proteasome system, brain-derived neurotrophic factor and mitochondrial complex II/III in YAC72 and R6/2 transgenic mice partially model Huntington's disease patients
    • Seo H, Kim W, Isacson O (2008) Compensatory changes in the ubiquitin-proteasome system, brain-derived neurotrophic factor and mitochondrial complex II/III in YAC72 and R6/2 transgenic mice partially model Huntington's disease patients. Hum Mol Genet 17:3144-3153
    • (2008) Hum Mol Genet , vol.17 , pp. 3144-3153
    • Seo, H.1    Kim, W.2    Isacson, O.3
  • 107
    • 0017090806 scopus 로고
    • Duplication of biochemical changes of Huntington's chorea by intrastriatal injections of glutamic and kainic acids
    • McGeer EG, McGeer PL (1976) Duplication of biochemical changes of Huntington's chorea by intrastriatal injections of glutamic and kainic acids. Nature 263:517-519
    • (1976) Nature , vol.263 , pp. 517-519
    • McGeer, E.G.1    McGeer, P.L.2
  • 108
    • 0017167057 scopus 로고
    • Lesion of striatal neurones with kainic acid provides a model for Huntington's chorea
    • Coyle JT, Schwarcz R (1976) Lesion of striatal neurones with kainic acid provides a model for Huntington's chorea. Nature 263:244-246
    • (1976) Nature , vol.263 , pp. 244-246
    • Coyle, J.T.1    Schwarcz, R.2
  • 109
    • 76849100874 scopus 로고    scopus 로고
    • Of mice, rats and men: Revisiting the quinolinic acid hypothesis of Huntington's disease
    • Schwarcz R, Guidetti P, Sathyasaikumar KV, Muchowski PJ (2010) Of mice, rats and men: revisiting the quinolinic acid hypothesis of Huntington's disease. Prog Neurobiol 90:230-245
    • (2010) Prog Neurobiol , vol.90 , pp. 230-245
    • Schwarcz, R.1    Guidetti, P.2    Sathyasaikumar, K.V.3    Muchowski, P.J.4
  • 110
    • 0022446150 scopus 로고
    • Replication of the neurochemical characteristics of Huntington's disease by quinolinic acid
    • Beal MF, Kowall NW, Ellison DW, Mazurek MF, Swartz KJ, Martin JB (1986) Replication of the neurochemical characteristics of Huntington's disease by quinolinic acid. Nature 321:168-171 (Pubitemid 16022019)
    • (1986) Nature , vol.321 , Issue.6066 , pp. 168-171
    • Beal, M.F.1    Kowall, N.W.2    Ellison, D.W.3
  • 111
  • 112
    • 0027396021 scopus 로고
    • Excitotoxin lesions in primates as a model for Huntington's disease: Histopathologic and neurochemical characterization
    • DOI 10.1006/exnr.1993.1006
    • Ferrante RJ, Kowall NW, Cipolloni PB, Storey E, Beal MF (1993) Excitotoxin lesions in primates as a model for Huntington's disease: histopathologic and neurochemicalcharacterization. Exp Neurol 119:46-71 (Pubitemid 23074242)
    • (1993) Experimental Neurology , vol.119 , Issue.1 , pp. 46-71
    • Ferrante, R.J.1    Kowall, N.W.2    Cipolloni, P.B.3    Storey, E.4    Beal, M.F.5
  • 113
    • 84872855026 scopus 로고    scopus 로고
    • 3-Nitropropionic acid induces autophagy by forming mitochondrial permeability transition pores rather than activating the mitochondrial fission pathway
    • Solesio ME, Saez-Atienzar S, Jordan J, Galindo MF (2013) 3-Nitropropionic acid induces autophagy by forming mitochondrial permeability transition pores rather than activating the mitochondrial fission pathway. Br J Pharmacol 168:63-75
    • (2013) Br J Pharmacol , vol.168 , pp. 63-75
    • Solesio, M.E.1    Saez-Atienzar, S.2    Jordan, J.3    Galindo, M.F.4
  • 115
    • 47149108940 scopus 로고    scopus 로고
    • Effect of dimebon on cognition, activities of daily living, behaviour, and global function in patients with mild-to-moderate Alzheimer's disease: A randomised, double-blind, placebo-controlled study
    • DOI 10.1016/S0140-6736(08)61074-0, PII S0140673608610740
    • Doody RS, Gavrilova SI, Sano M, Thomas RG, Aisen PS, Bachurin SO, Seely L, Hung D (2008) Effect of dimebon on cognition, activities of daily living, behaviour, and global function in patients with mild-to-moderate Alzheimer's disease: a randomised, double-blind, placebo-controlled study. Lancet 372:207-215 (Pubitemid 351978110)
    • (2008) The Lancet , vol.372 , Issue.9634 , pp. 207-215
    • Doody, R.S.1    Gavrilova, S.I.2    Sano, M.3    Thomas, R.G.4    Aisen, P.S.5    Bachurin, S.O.6    Seely, L.7    Hung, D.8
  • 116
    • 55349083365 scopus 로고    scopus 로고
    • Evaluation of Dimebon in cellular model of Huntington's disease
    • Wu J, Li Q, Bezprozvanny I (2008) Evaluation of Dimebon in cellular model of Huntington's disease. Mol Neurodegener 3:15
    • (2008) Mol Neurodegener , vol.3 , pp. 15
    • Wu, J.1    Li, Q.2    Bezprozvanny, I.3
  • 117
    • 77957138323 scopus 로고    scopus 로고
    • The rise and fall of Dimebon
    • Bezprozvanny I (2010) The rise and fall of Dimebon. Drug News Perspect 23:518-523
    • (2010) Drug News Perspect , vol.23 , pp. 518-523
    • Bezprozvanny, I.1
  • 119
    • 0035754146 scopus 로고    scopus 로고
    • Biochemical reactivity of melatonin with reactive oxygen and nitrogen species: A review of the evidence
    • DOI 10.1385/CBB:34:2:237
    • Reiter RJ, Tan DX, Manchester LC, Qi W (2001) Biochemical reactivity of melatonin with reactive oxygen and nitrogen species: a review of the evidence. Cell Biochem Biophys 34:237-256 (Pubitemid 33615836)
    • (2001) Cell Biochemistry and Biophysics , vol.34 , Issue.2 , pp. 237-256
    • Reiter, R.J.1    Tan, D.-X.2    Manchester, L.C.3    Qi, W.4
  • 120
    • 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 (2004) Direct inhibition of the mitochondrial permeability transition pore: a possible mechanism responsible for anti-apoptotic effects of melatonin. FASEB J 18:869-871
    • (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
  • 121
    • 0027725205 scopus 로고
    • Distribution of melatonin in mammalian tissues: The relative importance of nuclear versus cytosolic localization
    • Menendez-pelaez A, Reiter RJ (1993) Distribution of melatonin in mammalian tissues: the relative importance of nuclear versus cytosolic localization. J Pineal Res 15:59-69
    • (1993) J Pineal Res , vol.15 , pp. 59-69
    • Menendez-pelaez, A.1    Reiter, R.J.2
  • 122
    • 33746504821 scopus 로고    scopus 로고
    • Melatonin protects against hydrogen peroxide-induced cell death signaling in SH-SY5Y cultured cells: Involvement of nuclear factor kappa B, Bax and Bcl-2
    • DOI 10.1111/j.1600-079X.2006.00335.x
    • Chetsawang B, Putthaprasart C, Phansuwan-Pujito P, Govitrapong P (2006) Melatonin protects against hydrogen peroxide-induced cell death signaling in SH-SY5Y cultured cells: involvement of nuclear factor kappa B, Bax and Bcl-2. J Pineal Res 41:116-123 (Pubitemid 44141745)
    • (2006) Journal of Pineal Research , vol.41 , Issue.2 , pp. 116-123
    • Chetsawang, B.1    Putthaprasart, C.2    Phansuwan-Pujito, P.3    Govitrapong, P.4
  • 123
    • 64649097900 scopus 로고    scopus 로고
    • Melatonin reduces induction of Bax, caspase and cell death in methamphetamine-treated human neuroblastoma SH-SY5Y cultured cells
    • Wisessmith W, Phansuwan-Pujito P, Govitrapong P, Chetsawang B (2009) Melatonin reduces induction of Bax, caspase and cell death in methamphetamine-treated human neuroblastoma SH-SY5Y cultured cells. J Pineal Res 46:433-440
    • (2009) J Pineal Res , vol.46 , pp. 433-440
    • Wisessmith, W.1    Phansuwan-Pujito, P.2    Govitrapong, P.3    Chetsawang, B.4
  • 124
    • 67749124210 scopus 로고    scopus 로고
    • The role of melatonin in sleep disturbances in end-stage Huntington's disease
    • Alders J, Smits M, Kremer B, Naarding P (2009) The role of melatonin in sleep disturbances in end-stage Huntington's disease. J Neuropsychiatry Clin Neurosci 21:226-227
    • (2009) J Neuropsychiatry Clin Neurosci , vol.21 , pp. 226-227
    • Alders, J.1    Smits, M.2    Kremer, B.3    Naarding, P.4
  • 125
    • 71849115710 scopus 로고    scopus 로고
    • Delayed onset of the diurnal melatonin rise in patients with Huntington's disease
    • Aziz NA, Pijl H, Frölich M et al (2009) Delayed onset of the diurnal melatonin rise in patients with Huntington's disease. J Neurol 256:1961-1965
    • (2009) J Neurol , vol.256 , pp. 1961-1965
    • Aziz, N.A.1    Pijl, H.2    Frölich, M.3
  • 127
    • 20144376099 scopus 로고    scopus 로고
    • Melatonin protects against neuronal damage induced by 3-nitropropionic acid in rat striatum
    • DOI 10.1016/j.brainres.2005.03.053, PII S0006899305005147
    • Nam E, Lee SM, Koh SE, Joo WS, Maeng S, Im HI, Kim YS (2005) Melatonin protects against neuronal damage induced by 3-nitropropionic acid in rat striatum. Brain Res 1046:90-96 (Pubitemid 40775877)
    • (2005) Brain Research , vol.1046 , Issue.1-2 , pp. 90-96
    • Nam, E.1    Seung, M.L.2    Seong, E.K.3    Wan, S.J.4    Maeng, S.5    Heh, I.I.6    Yong, S.K.7
  • 128
    • 7644237780 scopus 로고    scopus 로고
    • Protective effect of melatonin on 3-nitropropionic acid-induced oxidative stress in synaptosomes in an animal model of Huntington's disease
    • DOI 10.1111/j.1600-079X.2004.00163.x
    • Túnez I, Montilla P, Del Carmen Muñoz M, Feijóo M, Salcedo M (2004) Protective effect of melatonin on 3-nitropropionic acid-induced oxidative stress in synaptosomes in an animal model of Huntington's disease. J Pineal Res 37:252-256 (Pubitemid 39457046)
    • (2004) Journal of Pineal Research , vol.37 , Issue.4 , pp. 252-256
    • Tunez, I.1    Montilla, P.2    Munoz, M.D.C.3    Feijoo, M.4    Salcedo, M.5
  • 129
    • 75749130798 scopus 로고    scopus 로고
    • Neuroprotective effect of carvedilol and melatonin on 3-nitropropionic acid-induced neurotoxicity in neuroblastoma
    • Tasset I, Espínola C, Medina FJ (2009) Neuroprotective effect of carvedilol and melatonin on 3-nitropropionic acid-induced neurotoxicity in neuroblastoma. J Physiol Biochem 65:291-296
    • (2009) J Physiol Biochem , vol.65 , pp. 291-296
    • Tasset, I.1    Espínola, C.2    Medina, F.J.3
  • 130
    • 71549120441 scopus 로고    scopus 로고
    • 2+ mediated permeability transition and beyond in rat brain astrocytes
    • 2+ mediated permeability transition and beyond in rat brain astrocytes. J Pineal Res 48:20-38
    • (2010) J Pineal Res , vol.48 , pp. 20-38
    • Jou, M.J.1    Peng, T.I.2    Hsu, L.F.3
  • 131
    • 80054040251 scopus 로고    scopus 로고
    • The melatonin MT1 receptor axis modulates mutant Huntingtin-mediated toxicity
    • Wang X, Sirianni A, Pei Z (2011) The melatonin MT1 receptor axis modulates mutant Huntingtin-mediated toxicity. J Neurosci 31:14496-14507
    • (2011) J Neurosci , vol.31 , pp. 14496-14507
    • Wang, X.1    Sirianni, A.2    Pei, Z.3
  • 134
    • 0029888128 scopus 로고    scopus 로고
    • Structure-antioxidant activity relationships of flavonoids and phenolic acids
    • DOI 10.1016/0891-5849(95)02227-9
    • Rice-Evans CA, Miller NJ, Paganga G (1996) Structure-antioxidant activity relationships of flavonoids and phenolic acids. Free Radic Biol Med 20:933-956 (Pubitemid 26157509)
    • (1996) Free Radical Biology and Medicine , vol.20 , Issue.7 , pp. 933-956
    • Rice-Evans, C.A.1    Miller, N.J.2    Paganga, G.3
  • 135
    • 84874547093 scopus 로고    scopus 로고
    • Quercetin up-regulates mitochondrial complex-I activity to protect against programmed cell death in rotenone model of Parkinson's disease in rats
    • Karuppagounder SS, Madathil SK, Pandey M, Haobam R, Rajamma U, Mohanakumar KP (2013) Quercetin up-regulates mitochondrial complex-I activity to protect against programmed cell death in rotenone model of Parkinson's disease in rats. Neuroscience 236:136-148
    • (2013) Neuroscience , vol.236 , pp. 136-148
    • Karuppagounder, S.S.1    Madathil, S.K.2    Pandey, M.3    Haobam, R.4    Rajamma, U.5    Mohanakumar, K.P.6
  • 137
    • 84872260847 scopus 로고    scopus 로고
    • Quercetin supplementation is effective in improving mitochondrial dysfunctions induced by 3-nitropropionic acid: Implications in Huntington's disease
    • Sandhir R, Mehrotra A (2013) Quercetin supplementation is effective in improving mitochondrial dysfunctions induced by 3-nitropropionic acid: implications in Huntington's disease. Biochim Biophys Acta 1832:421-430
    • (2013) Biochim Biophys Acta , vol.1832 , pp. 421-430
    • Sandhir, R.1    Mehrotra, A.2
  • 138
    • 84890485130 scopus 로고    scopus 로고
    • Quercetin improves behavioral deficiencies, restores astrocytes and microglia, and reduces serotonin metabolism in 3-nitropropionic acid-induced rat model of Huntington's disease
    • doi:10.1111/cns.12189
    • Chakraborty J, Singh R, Dutta D, Naskar A, Usha R, Mohanakumar KP (2013) Quercetin improves behavioral deficiencies, restores astrocytes and microglia, and reduces serotonin metabolism in 3-nitropropionic acid-induced rat model of Huntington's disease. CNS Neurosci Ther 20:10-9. doi:10.1111/cns.12189
    • (2013) CNS Neurosci Ther , vol.20 , pp. 10-19
    • Chakraborty, J.1    Singh, R.2    Dutta, D.3    Naskar, A.4    Usha, R.5    Mohanakumar, K.P.6
  • 139
    • 84858998255 scopus 로고    scopus 로고
    • N-Acetylcysteine reverses mitochondrial dysfunctions and behavioral abnormalities in 3-nitropropionic acid-induced Huntington's disease
    • Sandhir R, Sood A, Mehrotra A, Kamboj SS (2012) N-Acetylcysteine reverses mitochondrial dysfunctions and behavioral abnormalities in 3-nitropropionic acid-induced Huntington's disease. Neurodegener Dis 9:145-157
    • (2012) Neurodegener Dis , vol.9 , pp. 145-157
    • Sandhir, R.1    Sood, A.2    Mehrotra, A.3    Kamboj, S.S.4
  • 140
    • 18144452058 scopus 로고    scopus 로고
    • N-acetylcysteine elicited increase in cytochrome c oxidase activity in mice synaptic mitochondria
    • DOI 10.1016/S0006-8993(99)01819-3, PII S0006899399018193
    • Banaclocha M, Martínez N (1999) N-acetylcysteine elicited increase in cytochrome c oxidase activity in mice synaptic mitochondria. Brain Res 842:249-251 (Pubitemid 29447877)
    • (1999) Brain Research , vol.842 , Issue.1 , pp. 249-251
    • Martinez, B.M.1    Martinez, N.2
  • 141
    • 0034678112 scopus 로고    scopus 로고
    • N-acetylcysteine elicited increase in complex I activity in synaptic mitochondria from aged mice: Implications for treatment of Parkinson's disease
    • Banaclocha M (2000) N-acetylcysteine elicited increase in complex I activity in synaptic mitochondria from aged mice: implications for treatment of Parkinson's disease. Brain Res 859:173-175
    • (2000) Brain Res , vol.859 , pp. 173-175
    • Banaclocha, M.1
  • 142
    • 68949206326 scopus 로고    scopus 로고
    • Mitochondrial gene therapy augments mitochondrial physiology in a Parkinson's disease cell model
    • Keeney PM, Quigley CK, Dunham LD (2009) Mitochondrial gene therapy augments mitochondrial physiology in a Parkinson's disease cell model. Hum Gene Ther 20:897-907
    • (2009) Hum Gene Ther , vol.20 , pp. 897-907
    • Keeney, P.M.1    Quigley, C.K.2    Dunham, L.D.3
  • 143
    • 0035968856 scopus 로고    scopus 로고
    • Lipoic acid improves survival in transgenic mouse models of Huntington's disease
    • Andreassen OA, Ferrante RJ, Dedeoglu A, Beal MF (2001) Lipoic acid improves survival in transgenic mouse models of Huntington's disease. Neuroreport 12:3371-3373 (Pubitemid 33010674)
    • (2001) NeuroReport , vol.12 , Issue.15 , pp. 3371-3373
    • Andreassen, O.A.1    Ferrante, R.J.2    Dedeoglu, A.3    Beal, M.F.4
  • 144
    • 2642545019 scopus 로고    scopus 로고
    • Asialoerythropoietin is not effective in the R6/2 line of Huntington's disease mice
    • Gil JM, Leist M, Popovic N, Brundin P, Petersén A (2004) Asialoerythropoietin is not effective in the R6/2 line of Huntington's disease mice. BMC Neurosci 5:17
    • (2004) BMC Neurosci , vol.5 , pp. 17
    • Gil, J.M.1    Leist, M.2    Popovic, N.3    Brundin, P.4    Petersén, A.5
  • 145
  • 146
    • 1642406567 scopus 로고    scopus 로고
    • Paroxetine Retards Disease Onset and Progression in Huntingtin Mutant Mice
    • DOI 10.1002/ana.20075
    • Duan W, Guo Z, Jiang H, Ladenheim B, Xu X, Cadet JL, Mattson MP (2004) Paroxetine retards disease onset and progression in Huntingtin mutant mice. Ann Neurol 55:590-594 (Pubitemid 38391979)
    • (2004) Annals of Neurology , vol.55 , Issue.4 , pp. 590-594
    • Duan, W.1    Guo, Z.2    Jiang, H.3    Ladenheim, B.4    Xu, X.5    Cadet, J.L.6    Mattson, M.P.7
  • 149
    • 85009226418 scopus 로고    scopus 로고
    • A randomized, placebo-controlled trial of coenzyme Q10 and remacemide in Huntington's disease
    • Huntington Study Group
    • Huntington Study Group (2001) A randomized, placebo-controlled trial of coenzyme Q10 and remacemide in Huntington's disease. Neurology 57:397-404
    • (2001) Neurology , vol.57 , pp. 397-404
  • 150
    • 72349098221 scopus 로고    scopus 로고
    • Effects of caffeic acid, rofecoxib, and their combination against quinolinic acid-induced behavioral alterations and disruption in glutathione redox status
    • Kalonia H, Kumar P, Kumar A, Nehru B (2009) Effects of caffeic acid, rofecoxib, and their combination against quinolinic acid-induced behavioral alterations and disruption in glutathione redox status. Neurosci Bull 25:343-352
    • (2009) Neurosci Bull , vol.25 , pp. 343-352
    • Kalonia, H.1    Kumar, P.2    Kumar, A.3    Nehru, B.4
  • 152
    • 33750378660 scopus 로고    scopus 로고
    • Memantine reduces striatal cell death with decreasing calpain level in 3-nitropropionic model of Huntington's disease
    • DOI 10.1016/j.brainres.2006.08.035, PII S0006899306023857
    • Lee ST, Chu K, Park JE, Kang L, Ko SY, Jung KH, Kim M (2006) Memantine reduces striatal cell death with decreasing calpain level in 3-nitropropionic model of Huntington's disease. Brain Res 1118:199-207 (Pubitemid 44633871)
    • (2006) Brain Research , vol.1118 , Issue.1 , pp. 199-207
    • Lee, S.-T.1    Chu, K.2    Park, J.-E.3    Kang, L.4    Ko, S.-Y.5    Jung, K.-H.6    Kim, M.7
  • 156
    • 0038375825 scopus 로고    scopus 로고
    • A randomized trial of amantadine in Huntington disease
    • DOI 10.1001/archneur.60.7.996
    • O'Suilleabhain P, Dewey RB Jr (2003) A randomized trial of amantadine in Huntington disease. Arch Neurol 60:996-998 (Pubitemid 36858360)
    • (2003) Archives of Neurology , vol.60 , Issue.7 , pp. 996-998
    • O'Suilleabhain, P.1    Dewey Jr., R.B.2
  • 161
    • 0038115294 scopus 로고    scopus 로고
    • Creatine therapy provides neuroprotection after onset of clinical symptoms in Huntington's disease transgenic mice
    • DOI 10.1046/j.1471-4159.2003.01706.x
    • Dedeoglu A, Kubilus JK, Yang L, Ferrante KL, Hersch SM, Beal MF, Ferrante RJ (2003) Creatine therapy provides neuroprotection after onset of clinical symptoms in Huntington's disease transgenic mice. J Neurochem 85:1359-1367 (Pubitemid 36702548)
    • (2003) Journal of Neurochemistry , vol.85 , Issue.6 , pp. 1359-1367
    • Dedeoglu, A.1    Kubilus, J.K.2    Yang, L.3    Ferrante, K.L.4    Hersch, S.M.5    Beal, M.F.6    Ferrante, R.J.7
  • 162
    • 0034717594 scopus 로고    scopus 로고
    • Creatine reduces 3-nitropropionic-acid-induced cognitive and motor abnormalities in rats
    • Shear DA, Haik KL, Dunbar GL (2000) Creatine reduces 3-nitropropionic- acid-induced cognitive and motor abnormalities in rats. Neuroreport 11:1833-1837 (Pubitemid 30429120)
    • (2000) NeuroReport , vol.11 , Issue.9 , pp. 1833-1837
    • Shear, D.A.1    Haik, K.L.2    Dunbar, G.L.3
  • 165
    • 84881631358 scopus 로고    scopus 로고
    • Unchanged mitochondrial organization and compartmentation of high-energy phosphates in creatine-deficient GAMT- /- mouse hearts
    • Branovets J, Sepp M, Kotlyarova S et al (2013) Unchanged mitochondrial organization and compartmentation of high-energy phosphates in creatine-deficient GAMT- /- mouse hearts. Am J Physiol Heart Circ Physiol 305:H506-H520
    • (2013) Am J Physiol Heart Circ Physiol , vol.305
    • Branovets, J.1    Sepp, M.2    Kotlyarova, S.3
  • 166
    • 84890357270 scopus 로고    scopus 로고
    • Oxidizing effects of exogenous stressors in Huntington's disease knock-in striatal cells: Protective effect of cystamine and creatine
    • Ribeiro M, Silva AC, Rodrigues J, Naia L, Rego AC (2013) Oxidizing effects of exogenous stressors in Huntington's disease knock-in striatal cells: protective effect of cystamine and creatine. Toxicol Sci 136:487-499
    • (2013) Toxicol Sci , vol.136 , pp. 487-499
    • Ribeiro, M.1    Silva, A.C.2    Rodrigues, J.3    Naia, L.4    Rego, A.C.5
  • 167
    • 0034955984 scopus 로고    scopus 로고
    • Dichloroacetate exerts therapeutic effects in transgenic mouse models of Huntington's disease
    • Andreassen OA, Ferrante RJ, Huang HM et al (2001) Dichloroacetate exerts therapeutic effects in transgenic mouse models of Huntington's disease. Ann Neurol 50:112-117
    • (2001) Ann Neurol , vol.50 , pp. 112-117
    • Andreassen, O.A.1    Ferrante, R.J.2    Huang, H.M.3
  • 168
    • 84859258363 scopus 로고    scopus 로고
    • Modulation of astrocytic mitochondrial function by dichloroacetate improves survival and motor performance in inherited amyotrophic lateral sclerosis
    • Miquel E, Cassina A, Martínez-Palma L et al (2013) Modulation of astrocytic mitochondrial function by dichloroacetate improves survival and motor performance in inherited amyotrophic lateral sclerosis. PLoS One 7:e34776
    • (2013) PLoS One , vol.7
    • Miquel, E.1    Cassina, A.2    Martínez-Palma, L.3
  • 169
    • 4544310434 scopus 로고    scopus 로고
    • Gabapentin-lactam, but not gabapentin, reduces protein aggregates and improves motor performance in a transgenic mouse model of Huntington's disease
    • DOI 10.1007/s00210-004-0959-9
    • Zucker B, Ludin DE, Gerds TA, Lücking CH, Landwehrmeyer GB, Feuerstein TJ (2004) Gabapentin-lactam, but not gabapentin, reduces protein aggregates and improves motor performance in a transgenic mouse model of Huntington's disease. Naunyn Schmiedebergs Arch Pharmacol 370:131-139 (Pubitemid 39222865)
    • (2004) Naunyn-Schmiedeberg's Archives of Pharmacology , vol.370 , Issue.2 , pp. 131-139
    • Zucker, B.1    Ludin, D.E.2    Gerds, T.A.3    Lucking, C.H.4    Landwehrmeyer, G.B.5    Feuerstein, T.J.6
  • 171
    • 33748742446 scopus 로고    scopus 로고
    • Evaluation of clinically relevant glutamate pathway inhibitors in in vitro model of Huntington's disease
    • DOI 10.1016/j.neulet.2006.08.036, PII S0304394006008433
    • Wu J, Tang T, Bezprozvanny I (2006) Evaluation of clinically relevant glutamate pathway inhibitors in in vitro model of Huntington's disease. Neurosci Lett 407:219-223 (Pubitemid 44402868)
    • (2006) Neuroscience Letters , vol.407 , Issue.3 , pp. 219-223
    • Wu, J.1    Tang, T.2    Bezprozvanny, I.3
  • 172
    • 84855564048 scopus 로고    scopus 로고
    • Possible GABAergic mechanism in the neuroprotective effect of gabapentin and lamotrigine against 3-nitropropionic acid induced neurotoxicity
    • Kumar P, Kalonia H, Kumar A (2012) Possible GABAergic mechanism in the neuroprotective effect of gabapentin and lamotrigine against 3-nitropropionic acid induced neurotoxicity. Eur J Pharmacol 674:265-274
    • (2012) Eur J Pharmacol , vol.674 , pp. 265-274
    • Kumar, P.1    Kalonia, H.2    Kumar, A.3
  • 173
    • 0028803390 scopus 로고
    • Effect of riluzole on quinolinate-induced neuronal damage in rats: Comparison with blockers of glutamatergic neurotransmission
    • Mary V, Wahl F, Stutzmann JM (1995) Effect of riluzole on quinolinate-induced neuronal damage in rats: comparison with blockers of glutamatergic neurotransmission. Neurosci Lett 201:92-96
    • (1995) Neurosci Lett , vol.201 , pp. 92-96
    • Mary, V.1    Wahl, F.2    Stutzmann, J.M.3
  • 175
    • 33846819002 scopus 로고    scopus 로고
    • Lamotrigine inhibition of rotenone- or 1-methyl-4-phenylpyridinium- induced mitochondrial damage and cell death
    • DOI 10.1016/j.brainresbull.2006.12.006, PII S0361923006003686
    • Kim YJ, Ko HH, Han ES, Lee CS (2007) Lamotrigine inhibition of rotenone- or 1-methyl-4-phenylpyridinium-induced mitochondrial damage and cell death. Brain Res Bull 71:633-640 (Pubitemid 46209530)
    • (2007) Brain Research Bulletin , vol.71 , Issue.6 , pp. 633-640
    • Kim, Y.J.1    Ko, H.H.2    Han, E.S.3    Lee, C.S.4
  • 177
    • 33644799311 scopus 로고    scopus 로고
    • Levetiracetam: Antiepileptic properties and protective effects on mitochondrial dysfunction in experimental status epilepticus
    • DOI 10.1111/j.1528-1167.2006.00454.x
    • Gibbs JE, Walker MC, Cock HR (2006) Levetiracetam: antiepileptic properties and protective effects on mitochondrial dysfunction in experimental status epilepticus. Epilepsia 47:469-478 (Pubitemid 43351547)
    • (2006) Epilepsia , vol.47 , Issue.3 , pp. 469-478
    • Gibbs, J.E.1    Walker, M.C.2    Cock, H.R.3
  • 178
    • 0042666901 scopus 로고    scopus 로고
    • Chronic lithium chloride treatment has variable effects on motor behaviour and survival of mice transgenic for the Huntington's disease mutation
    • DOI 10.1016/S0361-9230(03)00141-2
    • Wood NI, Morton AJ (2003) Chronic lithium chloride treatment has variable effects on motor behaviour and survival of mice transgenic for the Huntington's disease mutation. Brain Res Bull 61:375-383 (Pubitemid 36945468)
    • (2003) Brain Research Bulletin , vol.61 , Issue.4 , pp. 375-383
    • Wood, N.I.1    Morton, A.J.2
  • 179
    • 58549093742 scopus 로고    scopus 로고
    • Evidence of calpain/cdk5 pathway inhibition by lithium in 3-nitropropionic acid toxicity in vivo and in vitro
    • Crespo-Biel N, Camins A, Pallàs M, Canudas AM (2009) Evidence of calpain/cdk5 pathway inhibition by lithium in 3-nitropropionic acid toxicity in vivo and in vitro. Neuropharmacology 56:422-428
    • (2009) Neuropharmacology , vol.56 , pp. 422-428
    • Crespo-Biel, N.1    Camins, A.2    Pallàs, M.3    Canudas, A.M.4
  • 180
    • 0017738763 scopus 로고
    • Lithium treatment of Huntington's chorea. A placebo controlled clinical trial
    • Vestergaard P, Baastrup PC, Petersson H (1977) Lithium treatment of Huntington's chorea. A placebo-controlled clinical trial. Acta Psychiatr Scand 56:183-188 (Pubitemid 8171880)
    • (1977) Acta Psychiatrica Scandinavica , vol.56 , Issue.3 , pp. 183-188
    • Vestergaard, P.1    Baastrup, P.C.2    Petersson, H.3
  • 182
    • 0034819537 scopus 로고    scopus 로고
    • In vitro effects of lithium and nickel at different levels on Neuro-2a mouse neuroblastoma cells
    • DOI 10.1016/S0887-2333(01)00037-6, PII S0887233301000376
    • Repetto G, del Peso A, Sanz P, Repetto M (2001) In vitro effects of lithium and nickel at different levels on Neuro-2a mouse neuroblastoma cells. Toxicol In Vitro 15:363-368 (Pubitemid 32889659)
    • (2001) Toxicology in Vitro , vol.15 , Issue.4-5 , pp. 363-368
    • Repetto, G.1    Del, P.A.2    Sanz, P.3    Repetto, M.4
  • 190
    • 84894209062 scopus 로고    scopus 로고
    • Rapamycin modulates markers of mitochondrial biogenesis and fatty acid oxidation in the adipose tissue of db/db mice
    • Deepa SS, Walsh ME, Hamilton RT (2013) Rapamycin modulates markers of mitochondrial biogenesis and fatty acid oxidation in the adipose tissue of db/db mice. J Biochem Pharmacol Res 1:114-123
    • (2013) J Biochem Pharmacol Res , vol.1 , pp. 114-123
    • Deepa, S.S.1    Walsh, M.E.2    Hamilton, R.T.3
  • 191
    • 0037133319 scopus 로고    scopus 로고
    • Age-associated mitochondrial oxidative decay: Improvement of carnitine acetyltransferase substrate-binding affinity and activity in brain by feeding old rats acetyl-L-carnitine and/or R-alpha-lipoic acid
    • DOI 10.1073/pnas.261709098
    • Liu J, Killilea DW, Ames BN (2002) Age-associated mitochondrial oxidative decay: improvement of carnitine acetyltransferase substrate-binding affinity and activity in brain by feeding old rats acetyl-L-carnitine and/or R-alpha-lipoic acid. Proc Natl Acad Sci USA 99:1876-1881 (Pubitemid 34168982)
    • (2002) Proceedings of the National Academy of Sciences of the United States of America , vol.99 , Issue.4 , pp. 1876-1881
    • Liu, J.1    Killilea, D.W.2    Ames, B.N.3
  • 193
    • 33847034701 scopus 로고    scopus 로고
    • Mitochondria frozen with trehalose retain a number of biological functions and preserve outer membrane integrity
    • Yamaguchi R, Andreyev A, Murphy AN, Perkins GA, Ellisman MH, Newmeyer DD (2007) Mitochondria frozen with trehalose retain a number of biological functions and preserve outer membrane integrity. Cell Death Differ 14:616-624
    • (2007) Cell Death Differ , vol.14 , pp. 616-624
    • Yamaguchi, R.1    Andreyev, A.2    Murphy, A.N.3    Perkins, G.A.4    Ellisman, M.H.5    Newmeyer, D.D.6


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