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Volumn 28, Issue 6, 2007, Pages 487-494

Mechanisms of neuronal death in Huntington's disease. Second part: Therapeutic challenges;Mécanismes de mort neuronale dans la maladie de Huntington. Seconde partie: Aspects thérapeutiques

Author keywords

Huntingtin; Huntington's disease; Neuronal death

Indexed keywords

ALPHA TOCOPHEROL; BUTYRIC ACID; CELECOXIB; CREATINE; CYSTAMINE; HISTONE DEACETYLASE INHIBITOR; IDEBENONE; MERCAPTAMINE; MINOCYCLINE; MITHRAMYCIN; RAPAMYCIN; REMACEMIDE; RESVERATROL; RILUZOLE; TREHALOSE; UBIQUINONE; VORINOSTAT;

EID: 37649009901     PISSN: 00353639     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (4)

References (222)
  • 2
  • 3
    • 0026928944 scopus 로고
    • New insights into the clinical features, pathogenesis and molecular genetics of Huntington disease
    • Kremer B, Weber B, Hayden MR : New insights into the clinical features, pathogenesis and molecular genetics of Huntington disease. Brain Pathol 1992 ; 2 : 321-35
    • (1992) Brain Pathol , vol.2 , pp. 321-335
    • Kremer, B.1    Weber, B.2    Hayden, M.R.3
  • 7
    • 0023227209 scopus 로고
    • Sparing of acetylcholinesterase-containing striatal neurons in Huntington's disease
    • Ferrante RJ, Beal MF, Kowall NW, Richardson EP Jr, Martin JB : Sparing of acetylcholinesterase-containing striatal neurons in Huntington's disease. Brain Res 1987 ; 411 : 162-6
    • (1987) Brain Res , vol.411 , pp. 162-166
    • Ferrante, R.J.1    Beal, M.F.2    Kowall, N.W.3    Richardson Jr, E.P.4    Martin, J.B.5
  • 9
    • 0032860432 scopus 로고    scopus 로고
    • The selective vulnerability of striatopallidal neurons
    • Mitchell IJ, Cooper AJ, Griffiths MR : The selective vulnerability of striatopallidal neurons. Prog Neurobiol 1999 ; 59 : 691-719
    • (1999) Prog Neurobiol , vol.59 , pp. 691-719
    • Mitchell, I.J.1    Cooper, A.J.2    Griffiths, M.R.3
  • 10
    • 4644245086 scopus 로고    scopus 로고
    • In vivo evidence of cerebellar atrophy and cerebral white matter loss in Huntington disease
    • Fennema-Notestine C, Archibald SL, Jacobson MW et al. : In vivo evidence of cerebellar atrophy and cerebral white matter loss in Huntington disease. Neurology 2004 ; 63 : 989-95
    • (2004) Neurology , vol.63 , pp. 989-995
    • Fennema-Notestine, C.1    Archibald, S.L.2    Jacobson, M.W.3
  • 11
    • 1042276562 scopus 로고    scopus 로고
    • Evidence for more widespread cerebral pathology in early HD : An MRI-based morphometry analysis
    • Kassubek J, Gaus W, Landwehrmeyer GB : Evidence for more widespread cerebral pathology in early HD : an MRI-based morphometry analysis. Neurology 2004 ; 62 : 523-4
    • (2004) Neurology , vol.62 , pp. 523-524
    • Kassubek, J.1    Gaus, W.2    Landwehrmeyer, G.B.3
  • 12
    • 33747602312 scopus 로고    scopus 로고
    • Hypothalamic-endocrine aspects in Huntington's disease
    • Petersen A, Bjorkqvist M : Hypothalamic-endocrine aspects in Huntington's disease. Eur J Neurosci 2006 ; 24 : 961-7
    • (2006) Eur J Neurosci , vol.24 , pp. 961-967
    • Petersen, A.1    Bjorkqvist, M.2
  • 13
    • 0035111235 scopus 로고    scopus 로고
    • Early and progressive accumulation of reactive microglia in the Huntington disease brain
    • Sapp E, Kegel KB, Aronin N et al. : Early and progressive accumulation of reactive microglia in the Huntington disease brain. J Neuropathol Exp Neurol 2001 ; 60 : 161-72
    • (2001) J Neuropathol Exp Neurol , vol.60 , pp. 161-172
    • Sapp, E.1    Kegel, K.B.2    Aronin, N.3
  • 14
    • 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
    • The Huntington's disease collaborative research group : A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. The Huntington's Disease Collaborative Research Group. Cell 1993 ; 72 : 971-83
    • (1993) Cell , vol.72 , pp. 971-983
  • 15
    • 8144228406 scopus 로고    scopus 로고
    • Trinucleotide repeats and neurodegenerative disease
    • Everett CM, Wood NW : Trinucleotide repeats and neurodegenerative disease. Brain 2004 ; 127 : 2385-405
    • (2004) Brain , vol.127 , pp. 2385-2405
    • Everett, C.M.1    Wood, N.W.2
  • 17
    • 0034329159 scopus 로고    scopus 로고
    • Molecular genetics : Unmasking polyglutamine triggers in neurodegenerative disease
    • Gusella JF, McDonald ME : Molecular genetics : unmasking polyglutamine triggers in neurodegenerative disease. Nat Rev Neurosci 2000 ; 1 : 109-15
    • (2000) Nat Rev Neurosci , vol.1 , pp. 109-115
    • Gusella, J.F.1    McDonald, M.E.2
  • 19
    • 0027261537 scopus 로고
    • Relationship between trinucleotide repeat expansion and phenotypic variation in Huntington's disease
    • Snell RG, MacMillan JC, Cheadle JP et al. : Relationship between trinucleotide repeat expansion and phenotypic variation in Huntington's disease. Nat Genet 1993 ; 4 : 393-97
    • (1993) Nat Genet , vol.4 , pp. 393-397
    • Snell, R.G.1    MacMillan, J.C.2    Cheadle, J.P.3
  • 20
    • 12144288251 scopus 로고    scopus 로고
    • Wexler NS, Lorimer J, Porter J et al. : Venezuelan kindreds reveal that genetic and environmental factors modulate Huntington's disease age of onset. Proc Natl Acad Sci U S A 2004 ; 101 : 3498-503
    • Wexler NS, Lorimer J, Porter J et al. : Venezuelan kindreds reveal that genetic and environmental factors modulate Huntington's disease age of onset. Proc Natl Acad Sci U S A 2004 ; 101 : 3498-503
  • 24
    • 0032867615 scopus 로고    scopus 로고
    • Evidence for the GluR6 gene associated with younger onset age of Huntington's disease
    • MacDonald ME, Vonsattel JP, Shrinidhi J et al. : Evidence for the GluR6 gene associated with younger onset age of Huntington's disease. Neurology 199 ; 53 : 1330-2
    • Neurology , vol.199 , Issue.53 , pp. 1330-1332
    • MacDonald, M.E.1    Vonsattel, J.P.2    Shrinidhi, J.3
  • 25
    • 25444453003 scopus 로고    scopus 로고
    • Association between BDNF Val66Met polymorphism and age at onset in Huntington disease
    • Alberch J, Lopez M, Badenas C et al. : Association between BDNF Val66Met polymorphism and age at onset in Huntington disease. Neurology 2005 : 964-6
    • (2005) Neurology , pp. 964-966
    • Alberch, J.1    Lopez, M.2    Badenas, C.3
  • 26
    • 33750209146 scopus 로고    scopus 로고
    • No evidence of association between BDNF gene variants and age-at-onset of Huntington's disease
    • Di Maria E, Marasco A, Tartari M et al. : No evidence of association between BDNF gene variants and age-at-onset of Huntington's disease. Neurobiol Dis 2006 ; 24 : 274-9
    • (2006) Neurobiol Dis , vol.24 , pp. 274-279
    • Di Maria, E.1    Marasco, A.2    Tartari, M.3
  • 27
    • 33749988016 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor does not influence age at neurologic onset of Huntington's disease
    • Kishikawa S, Li JL, Gillis T et al. : Brain-derived neurotrophic factor does not influence age at neurologic onset of Huntington's disease. Neurobiol Dis 2006 ; 24 : 280-5
    • (2006) Neurobiol Dis , vol.24 , pp. 280-285
    • Kishikawa, S.1    Li, J.L.2    Gillis, T.3
  • 28
    • 0038042172 scopus 로고    scopus 로고
    • Modulation of age at onset in Huntington's disease and spinocerebellar ataxia type 2 patients originated from eastern India
    • Chattopadhyay B, Ghosh S, Gangopadhyay PK et al. : Modulation of age at onset in Huntington's disease and spinocerebellar ataxia type 2 patients originated from eastern India. Neurosci Lett 2003 ; 345 : 93-6
    • (2003) Neurosci Lett , vol.345 , pp. 93-96
    • Chattopadhyay, B.1    Ghosh, S.2    Gangopadhyay, P.K.3
  • 29
    • 33644658207 scopus 로고    scopus 로고
    • The S18Y polymorphism in the UCHL1 gene is a genetic modifier in Huntington's disease
    • Metzger S, Bauer R Tomiuk J et al. : The S18Y polymorphism in the UCHL1 gene is a genetic modifier in Huntington's disease. Neurogenetics 2006 : 27-30
    • (2006) Neurogenetics , pp. 27-30
    • Metzger, S.1    Bauer, R.2    Tomiuk, J.3
  • 30
    • 11844250016 scopus 로고    scopus 로고
    • Modulation of age at onset of Huntington disease patients by variations in TP53 and human caspase activated DNase (hCAD) genes
    • Chattopadhyay B, Baksi K, Mukhopadhyay S, Bhattacharyya NP : Modulation of age at onset of Huntington disease patients by variations in TP53 and human caspase activated DNase (hCAD) genes. Neurosci Lett 2005 ; 374 : 81-6
    • (2005) Neurosci Lett , vol.374 , pp. 81-86
    • Chattopadhyay, B.1    Baksi, K.2    Mukhopadhyay, S.3    Bhattacharyya, N.P.4
  • 31
    • 0029055601 scopus 로고
    • Cellular localization of the Huntington's disease protein and discrimination of the normal and mutated form
    • Trottier Y, Devys D, Imbert G et al. : Cellular localization of the Huntington's disease protein and discrimination of the normal and mutated form. Nat Genet 1995 ; 10 : 104-10
    • (1995) Nat Genet , vol.10 , pp. 104-110
    • Trottier, Y.1    Devys, D.2    Imbert, G.3
  • 32
    • 0030950980 scopus 로고    scopus 로고
    • Heterogeneous topographic and cellular distribution of huntingtin expression in the normal human neostriatum
    • Ferrante RJ, Gutekunst CA, Persichetti F et al. : Heterogeneous topographic and cellular distribution of huntingtin expression in the normal human neostriatum. J Neurosci 1997 ; 17 : 3052-63
    • (1997) J Neurosci , vol.17 , pp. 3052-3063
    • Ferrante, R.J.1    Gutekunst, C.A.2    Persichetti, F.3
  • 33
    • 15144351709 scopus 로고    scopus 로고
    • Differential distribution of the normal and mutated forms of huntingtin in the human brain
    • Gourfinkel-An I, Cancel G, Trottier Y et al. : Differential distribution of the normal and mutated forms of huntingtin in the human brain. Ann Neurol 1997 ; 42 : 712-9
    • (1997) Ann Neurol , vol.42 , pp. 712-719
    • Gourfinkel-An, I.1    Cancel, G.2    Trottier, Y.3
  • 34
    • 0028829596 scopus 로고
    • CAG expansion affects the expression of mutant Huntingtin in the Huntington's disease brain
    • Aronin N, Chase K, Young C et al. : CAG expansion affects the expression of mutant Huntingtin in the Huntington's disease brain. Neuron 1995 ; 15 : 1193-201
    • (1995) Neuron , vol.15 , pp. 1193-1201
    • Aronin, N.1    Chase, K.2    Young, C.3
  • 35
    • 0028891145 scopus 로고
    • Huntington's disease gene : Regional and cellular expression in brain of normal and affected individuals
    • Landwehrmeyer GB, McNeil SM, Dure LS et al. : Huntington's disease gene : regional and cellular expression in brain of normal and affected individuals. Ann Neurol 1995 ; 37 : 218-30
    • (1995) Ann Neurol , vol.37 , pp. 218-230
    • Landwehrmeyer, G.B.1    McNeil, S.M.2    Dure, L.S.3
  • 36
    • 0041656292 scopus 로고    scopus 로고
    • The hunt for huntingtin function : Interaction partners tell many different stories
    • Harjes P, Wanker EE : The hunt for huntingtin function : interaction partners tell many different stories. Trends Biochem Sci 2003 ; 28 : 425-33
    • (2003) Trends Biochem Sci , vol.28 , pp. 425-433
    • Harjes, P.1    Wanker, E.E.2
  • 37
    • 0035816627 scopus 로고    scopus 로고
    • Polyglutamine-expanded huntingtin promotes sensitization of N-methyl-D-aspartate receptors via post-synaptic density 95
    • Sun Y, Savanenin A, Reddy PH, Liu YF : Polyglutamine-expanded huntingtin promotes sensitization of N-methyl-D-aspartate receptors via post-synaptic density 95. J Biol Chem 2001 ; 276 : 24713-8
    • (2001) J Biol Chem , vol.276 , pp. 24713-24718
    • Sun, Y.1    Savanenin, A.2    Reddy, P.H.3    Liu, Y.F.4
  • 38
    • 3142636768 scopus 로고    scopus 로고
    • Huntingtin controls neurotrophic support and survival of neurons by enhancing BDNF vesicular transport along microtubules
    • Gauthier LR, Charrin BC, Borrell-Pages M et al. : Huntingtin controls neurotrophic support and survival of neurons by enhancing BDNF vesicular transport along microtubules. Cell 2004 ; 118 : 127-38
    • (2004) Cell , vol.118 , pp. 127-138
    • Gauthier, L.R.1    Charrin, B.C.2    Borrell-Pages, M.3
  • 39
    • 0034657112 scopus 로고    scopus 로고
    • Wild-type huntingtin protects from apoptosis upstream of caspase-3
    • Rigamonti D, Bauer JH, De Fraja C et al. : Wild-type huntingtin protects from apoptosis upstream of caspase-3. J Neurosci 2000 ; 20 : 3705-13
    • (2000) J Neurosci , vol.20 , pp. 3705-3713
    • Rigamonti, D.1    Bauer, J.H.2    De Fraja, C.3
  • 40
    • 0035805504 scopus 로고    scopus 로고
    • Huntingtin's neuroprotective activity occurs via inhibition of procaspase-9 processing
    • Rigamonti D, Sipione S, Goffredo D, Zuccato C, Fossale E, Cattaneo E : Huntingtin's neuroprotective activity occurs via inhibition of procaspase-9 processing. J Biol Chem 2001 ; 276 : 14545-8
    • (2001) J Biol Chem , vol.276 , pp. 14545-14548
    • Rigamonti, D.1    Sipione, S.2    Goffredo, D.3    Zuccato, C.4    Fossale, E.5    Cattaneo, E.6
  • 41
    • 33845720388 scopus 로고    scopus 로고
    • Zhang Y, Leavitt BR, van Raamsdonk JM et al. : Huntingtin inhibits caspase-3 activation. EMBO J 2006 ; sous presse
    • Zhang Y, Leavitt BR, van Raamsdonk JM et al. : Huntingtin inhibits caspase-3 activation. EMBO J 2006 ; sous presse
  • 42
    • 0029082383 scopus 로고    scopus 로고
    • Duyao MP, Auerbach AB, Ryan A et al. : Inactivation of the mouse Huntington's disease gene homolog Hdh. Science 1995 ; 269 : 407-10
    • Duyao MP, Auerbach AB, Ryan A et al. : Inactivation of the mouse Huntington's disease gene homolog Hdh. Science 1995 ; 269 : 407-10
  • 43
    • 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. : Targeted disruption of the Huntington's disease gene results in embryonic lethality and behavioral and morphological changes in heterozygotes. Cell 1995 ; 81 : 811-23
    • (1995) Cell , vol.81 , pp. 811-823
    • Nasir, J.1    Floresco, S.B.2    O'Kusky, J.R.3
  • 44
    • 84993912315 scopus 로고
    • Increased apoptosis and early embryonic lethality in mice nullizygous for the Huntington's disease gene homologue
    • Zeitlin S, Liu JP, Chapman DL, Papaioannou VE, Efstratiadis A : Increased apoptosis and early embryonic lethality in mice nullizygous for the Huntington's disease gene homologue. Nat Genet 1995 ; 11 : 155-63
    • (1995) Nat Genet , vol.11 , pp. 155-163
    • Zeitlin, S.1    Liu, J.P.2    Chapman, D.L.3    Papaioannou, V.E.4    Efstratiadis, A.5
  • 45
    • 0033757718 scopus 로고    scopus 로고
    • Inactivation of Hdh in the brain and testis results in progressive neurodegeneration and sterility in mice
    • Dragatsis I, Levine MS, Zeitlin S : Inactivation of Hdh in the brain and testis results in progressive neurodegeneration and sterility in mice. Nat Genet 2000 ; 26 : 300-6
    • (2000) Nat Genet , vol.26 , pp. 300-306
    • Dragatsis, I.1    Levine, M.S.2    Zeitlin, S.3
  • 46
    • 0035919701 scopus 로고    scopus 로고
    • Loss of huntingtin-mediated BDNF gene transcription in Huntington's disease
    • Zuccato C, Ciammola A, Rigamonti D et al. : Loss of huntingtin-mediated BDNF gene transcription in Huntington's disease. Science 2001 ; 293 : 493-8
    • (2001) Science , vol.293 , pp. 493-498
    • Zuccato, C.1    Ciammola, A.2    Rigamonti, D.3
  • 47
    • 0041353535 scopus 로고    scopus 로고
    • Huntingtin interacts with REST/NRSF to modulate the transcription of NRSE-controlled neuronal genes
    • Zuccato C, Tartari M, Crotti A et al. : Huntingtin interacts with REST/NRSF to modulate the transcription of NRSE-controlled neuronal genes. Nat Genet 2003 ; 35 : 76-83
    • (2003) Nat Genet , vol.35 , pp. 76-83
    • Zuccato, C.1    Tartari, M.2    Crotti, A.3
  • 48
    • 28644433087 scopus 로고    scopus 로고
    • Normal huntingtin function : An alternative approach to Huntington's disease
    • Cattaneo E, Zuccato C, Tartari M : Normal huntingtin function : an alternative approach to Huntington's disease. Nat Rev Neurosci 2005 ; 6 : 919-30
    • (2005) Nat Rev Neurosci , vol.6 , pp. 919-930
    • Cattaneo, E.1    Zuccato, C.2    Tartari, M.3
  • 49
    • 0037292586 scopus 로고    scopus 로고
    • Dysfunction of wild-type huntingtin in Huntington disease
    • Cattaneo E : Dysfunction of wild-type huntingtin in Huntington disease. News Physiol Sci 2003 ; 18 : 34-7
    • (2003) News Physiol Sci , vol.18 , pp. 34-37
    • Cattaneo, E.1
  • 50
    • 29644433445 scopus 로고    scopus 로고
    • Selective Degeneration and Nuclear Localization of Mutant Huntingtin in the YAC128 Mouse Model of Huntington Disease
    • Van Raamsdonk JM, Murphy Z, Slow EJ, Leavitt BR, Hayden MR : Selective Degeneration and Nuclear Localization of Mutant Huntingtin in the YAC128 Mouse Model of Huntington Disease. Hum Mol Genet 2005 ; 14 : 3823-35
    • (2005) Hum Mol Genet , vol.14 , pp. 3823-3835
    • Van Raamsdonk, J.M.1    Murphy, Z.2    Slow, E.J.3    Leavitt, B.R.4    Hayden, M.R.5
  • 51
    • 1242338856 scopus 로고    scopus 로고
    • Li SH, Li XJ : Huntingtin-protein interactions and the pathogenesis of Huntington's disease. Trends Genet 2004 ; 3 : 146-54
    • Li SH, Li XJ : Huntingtin-protein interactions and the pathogenesis of Huntington's disease. Trends Genet 2004 ; 3 : 146-54
  • 52
    • 0032912386 scopus 로고    scopus 로고
    • Recent advances on the pathogensis of Huntington's disease
    • Petersen A, Mani K, Brundin P : Recent advances on the pathogensis of Huntington's disease. Exp Neurol 1999 ; 157 : 1-18
    • (1999) Exp Neurol , vol.157 , pp. 1-18
    • Petersen, A.1    Mani, K.2    Brundin, P.3
  • 53
    • 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 : Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions. Cell 1998 ; 95 : 55-66
    • (1998) Cell , vol.95 , pp. 55-66
    • Saudou, F.1    Finkbeiner, S.2    Devys, D.3    Greenberg, M.E.4
  • 54
    • 0032248397 scopus 로고    scopus 로고
    • Pathological mechanisms in Huntingtion's disease and other polyglutamine expansion diseases
    • Lunkes A, Trottier Y, Mandel JL : Pathological mechanisms in Huntingtion's disease and other polyglutamine expansion diseases. Essays Biochem 1998 ; 33 : 149-63
    • (1998) Essays Biochem , vol.33 , pp. 149-163
    • Lunkes, A.1    Trottier, Y.2    Mandel, J.L.3
  • 55
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DiFiglia M, Sapp E, Chase KO et al. : Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 1997 ; 277 : 1990-3
    • (1997) Science , vol.277 , pp. 1990-1993
    • DiFiglia, M.1    Sapp, E.2    Chase, K.O.3
  • 56
    • 0032987513 scopus 로고    scopus 로고
    • Axonal transport of N-terminal huntingtin suggests early pathology of corticostriatal projections in Huntington disease
    • Sapp E, Penney J, Young A, Aronin N, Vonsattel JP, DiFiglia M : Axonal transport of N-terminal huntingtin suggests early pathology of corticostriatal projections in Huntington disease. J Neuropathol Exp Neurol 1999 ; 58 : 165-73
    • (1999) J Neuropathol Exp Neurol , vol.58 , pp. 165-173
    • Sapp, E.1    Penney, J.2    Young, A.3    Aronin, N.4    Vonsattel, J.P.5    DiFiglia, M.6
  • 58
    • 85177152626 scopus 로고    scopus 로고
    • Peruttz MF, Johnson T, Suzuki M, Fich JT : Glutamine repeats as polar zippers : their possible role in inherited neurodegenerative diseases. Proc Natl Acad Sci U S A 1994 ; 91 : 5355-8
    • Peruttz MF, Johnson T, Suzuki M, Fich JT : Glutamine repeats as polar zippers : their possible role in inherited neurodegenerative diseases. Proc Natl Acad Sci U S A 1994 ; 91 : 5355-8
  • 59
    • 0029059477 scopus 로고
    • Incorporation of glutamine repeats makes protein oligomerize : Implications for neurodegenerative diseases
    • Stott K, Blackburn JM, Butler PJG, Perutz M : Incorporation of glutamine repeats makes protein oligomerize : implications for neurodegenerative diseases. Proc Natl Acad Sci U S A 1995 ; 92 : 6509-13
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 6509-6513
    • Stott, K.1    Blackburn, J.M.2    Butler, P.J.G.3    Perutz, M.4
  • 60
    • 0036172346 scopus 로고    scopus 로고
    • Prolonged survival and decreased abnormal movements in transgenic model of Huntington disease, with administration of the transglutaminase inhibitor cystamine
    • Karpuj MV, Becher MW, Springer JE et al. : Prolonged survival and decreased abnormal movements in transgenic model of Huntington disease, with administration of the transglutaminase inhibitor cystamine. Nat Med 2002 ; 8 : 143-9
    • (2002) Nat Med , vol.8 , pp. 143-149
    • Karpuj, M.V.1    Becher, M.W.2    Springer, J.E.3
  • 62
    • 13444273499 scopus 로고    scopus 로고
    • Development of novel therapies for Huntington's disease : Hope and challenge
    • Qin ZH, Wang J, Gu ZL : Development of novel therapies for Huntington's disease : hope and challenge. Acta Pharmacol Sin 2005 ; 26 : 129-42
    • (2005) Acta Pharmacol Sin , vol.26 , pp. 129-142
    • Qin, Z.H.1    Wang, J.2    Gu, Z.L.3
  • 63
    • 0033119123 scopus 로고    scopus 로고
    • Nuclear and neuropil aggregates in Huntington's disease : Relationship to neuropathology
    • Gutekunst CA, Li SH, Yi H et al. : Nuclear and neuropil aggregates in Huntington's disease : relationship to neuropathology. J Neurosci 1999 ; 19 : 2522-34
    • (1999) J Neurosci , vol.19 , pp. 2522-2534
    • Gutekunst, C.A.1    Li, S.H.2    Yi, H.3
  • 64
    • 33745003424 scopus 로고    scopus 로고
    • Cleavage at the caspase-6 site is required for neuronal dysfunction and degeneration due to mutant huntingtin
    • Graham RK, Deng Y, Slow EJ et al. : Cleavage at the caspase-6 site is required for neuronal dysfunction and degeneration due to mutant huntingtin. Cell 2006 ; 125 : 1179-91
    • (2006) Cell , vol.125 , pp. 1179-1191
    • Graham, R.K.1    Deng, Y.2    Slow, E.J.3
  • 65
    • 2642586352 scopus 로고    scopus 로고
    • Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease
    • Ravikumar B, Vacher C, Berger Z et al. : Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease. Nat Genet 2004 ; 36 : 585-95
    • (2004) Nat Genet , vol.36 , pp. 585-595
    • Ravikumar, B.1    Vacher, C.2    Berger, Z.3
  • 66
    • 3042717240 scopus 로고    scopus 로고
    • Cellular toxicity of polyglutamine expansion proteins : Mechanism of transcription factor deactivation
    • Schaffar G, Breuer P, Boteva R et al. : Cellular toxicity of polyglutamine expansion proteins : mechanism of transcription factor deactivation. Mol Cell 2004 ; 15 : 95-105
    • (2004) Mol Cell , vol.15 , pp. 95-105
    • Schaffar, G.1    Breuer, P.2    Boteva, R.3
  • 67
    • 0032590053 scopus 로고    scopus 로고
    • Huntington aggregates may not predict neuronal death in Huntington's disease
    • Kuemmerle S, Gutekunst CA, Klein AM et al. : Huntington aggregates may not predict neuronal death in Huntington's disease. Ann Neurol 1999 ; 46 : 842-9
    • (1999) Ann Neurol , vol.46 , pp. 842-849
    • Kuemmerle, S.1    Gutekunst, C.A.2    Klein, A.M.3
  • 68
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • Arrasate M, Mitra S, Schweitzer ES, Segal MR, Finkbeiner S : Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 2004 ; 431 : 805-10
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 69
    • 23844472610 scopus 로고    scopus 로고
    • Slow EJ, Graham RK, Osmand AP et al. : Absence of behavioral abnormalities and neurodegeneration in vivo despite widespread neuronal huntingtin inclusions. Proc Natl Acad Sci U S A 2005 ; 102 : 11402-7
    • Slow EJ, Graham RK, Osmand AP et al. : Absence of behavioral abnormalities and neurodegeneration in vivo despite widespread neuronal huntingtin inclusions. Proc Natl Acad Sci U S A 2005 ; 102 : 11402-7
  • 70
    • 0029926199 scopus 로고    scopus 로고
    • Reduction in enkephalin and substance P messenger RNA in the striatum of early grade Huntington's disease : A detailed cellular in situ hybridization study
    • Augood SJ, Faull RL, Love DR, Emson PC : Reduction in enkephalin and substance P messenger RNA in the striatum of early grade Huntington's disease : a detailed cellular in situ hybridization study. Neuroscience 1996 ; 72 : 1023-36
    • (1996) Neuroscience , vol.72 , pp. 1023-1036
    • Augood, S.J.1    Faull, R.L.2    Love, D.R.3    Emson, P.C.4
  • 71
    • 0029895292 scopus 로고    scopus 로고
    • Striatal D1 and D2 dopamine receptor loss in asymptomatic mutation carriers of Huntington's disease
    • Weeks RA, Piccini P, Harding AE, Brooks DJ : Striatal D1 and D2 dopamine receptor loss in asymptomatic mutation carriers of Huntington's disease. Ann Neurol 1996 ; 40 : 49-54
    • (1996) Ann Neurol , vol.40 , pp. 49-54
    • Weeks, R.A.1    Piccini, P.2    Harding, A.E.3    Brooks, D.J.4
  • 72
    • 0030612119 scopus 로고    scopus 로고
    • Dopamine D1 and D2 receptor gene expression in the striatum in Huntington's disease
    • Augood SJ, Faull RL, Emson PC : Dopamine D1 and D2 receptor gene expression in the striatum in Huntington's disease. Ann Neurol 1997 ; 42 : 215-21
    • (1997) Ann Neurol , vol.42 , pp. 215-221
    • Augood, S.J.1    Faull, R.L.2    Emson, P.C.3
  • 73
    • 0032568517 scopus 로고    scopus 로고
    • Cha JH, Kosinski CM, Kerner JA et al. : Altered brain neurotransmitter receptors in transgenic mice expressing a portion of an abnormal human huntington disease gene. Proc Natl Acad Sci U S A 1998 ; 95 : 6480-5
    • Cha JH, Kosinski CM, Kerner JA et al. : Altered brain neurotransmitter receptors in transgenic mice expressing a portion of an abnormal human huntington disease gene. Proc Natl Acad Sci U S A 1998 ; 95 : 6480-5
  • 74
    • 0033614761 scopus 로고    scopus 로고
    • Altered neurotransmitter receptor expression in transgenic mouse models of Huntington's disease
    • Cha JH, Frey AS, Alsdorf SA et al. : Altered neurotransmitter receptor expression in transgenic mouse models of Huntington's disease. Philos Trans R Soc Lond B Biol Sci 1999 ; 354 : 981-9
    • (1999) Philos Trans R Soc Lond B Biol Sci , vol.354 , pp. 981-989
    • Cha, J.H.1    Frey, A.S.2    Alsdorf, S.A.3
  • 75
    • 0034612255 scopus 로고    scopus 로고
    • Bibb JA, Yan Z, Svenningsson P et al. : Severe deficiencies in dopamine signaling in presymptomatic Huntington's disease mice. Proc Natl Acad Sci U S A 2000 ; 97 : 6809-14
    • Bibb JA, Yan Z, Svenningsson P et al. : Severe deficiencies in dopamine signaling in presymptomatic Huntington's disease mice. Proc Natl Acad Sci U S A 2000 ; 97 : 6809-14
  • 76
    • 0034047444 scopus 로고    scopus 로고
    • Cannabinoid receptor messenger RNA levels decrease in a subset of neurons of the lateral striatum, cortex and hippocampus of transgenic Huntington's disease mice
    • Denovan-Wright EM, Robertson HA : Cannabinoid receptor messenger RNA levels decrease in a subset of neurons of the lateral striatum, cortex and hippocampus of transgenic Huntington's disease mice. Neuroscience 2000 ; 98 : 705-13
    • (2000) Neuroscience , vol.98 , pp. 705-713
    • Denovan-Wright, E.M.1    Robertson, H.A.2
  • 77
    • 0037101835 scopus 로고    scopus 로고
    • Dysregulation of gene expression in the R6/2 model of polyglutamine disease : Parallel changes in muscle and brain
    • Luthi-Carter R, Hanson SA, Strand AD et al. : Dysregulation of gene expression in the R6/2 model of polyglutamine disease : parallel changes in muscle and brain. Hum Mol Genet 2002 ; 11 : 1911-26
    • (2002) Hum Mol Genet , vol.11 , pp. 1911-1926
    • Luthi-Carter, R.1    Hanson, S.A.2    Strand, A.D.3
  • 78
    • 0037097287 scopus 로고    scopus 로고
    • differential D1 and D2 receptor-mediated effects on immediate early gene induction in a transgenic mouse model of Huntington's disease
    • Spektor BS, Miller DW, Hollingsworth ZR et al. : differential D1 and D2 receptor-mediated effects on immediate early gene induction in a transgenic mouse model of Huntington's disease. Brain Res Mol Brain Res 2002 ; 102 : 118-28
    • (2002) Brain Res Mol Brain Res , vol.102 , pp. 118-128
    • Spektor, B.S.1    Miller, D.W.2    Hollingsworth, Z.R.3
  • 79
    • 0037101837 scopus 로고    scopus 로고
    • Polyglutamine and transcription : Gene expression changes shared by DRPLA and Huntington's disease mouse model reveal context-dependent independent-effects
    • Luthi-Carter R, Strand AD, Hanson SA et al. : Polyglutamine and transcription : gene expression changes shared by DRPLA and Huntington's disease mouse model reveal context-dependent independent-effects. Hum Mol Genet 2002 ; 11 : 1927-37
    • (2002) Hum Mol Genet , vol.11 , pp. 1927-1937
    • Luthi-Carter, R.1    Strand, A.D.2    Hanson, S.A.3
  • 80
    • 0141828353 scopus 로고    scopus 로고
    • Mechanisms of transcriptional dysregulation in Huntington's disease
    • Luthi-Carter R, Cha JHJ : Mechanisms of transcriptional dysregulation in Huntington's disease. Clinical Neuroscience Research 2003 ; 3 : 165-77
    • (2003) Clinical Neuroscience Research , vol.3 , pp. 165-177
    • Luthi-Carter, R.1    Cha, J.H.J.2
  • 81
    • 0035937523 scopus 로고    scopus 로고
    • Interference by huntingtin and atrophin-1 with cbp-mediated transcription leading to cellular toxicity
    • Nucifora FC Jr, Sasaki M, Peters MF et al. : Interference by huntingtin and atrophin-1 with cbp-mediated transcription leading to cellular toxicity. Science 2001 ; 291 : 2423-8
    • (2001) Science , vol.291 , pp. 2423-2428
    • Nucifora Jr, F.C.1    Sasaki, M.2    Peters, M.F.3
  • 82
    • 12244298155 scopus 로고    scopus 로고
    • Cell death triggered by polyglutamine-expanded huntingtin in a neuronal cell line is associated with degradation of CREB-binding protein
    • Jiang H, Nucifora FC Jr, Ross CA, DeFranco DB : Cell death triggered by polyglutamine-expanded huntingtin in a neuronal cell line is associated with degradation of CREB-binding protein. Hum Mol Genet 2003 ; 12 : 1-12
    • (2003) Hum Mol Genet , vol.12 , pp. 1-12
    • Jiang, H.1    Nucifora Jr, F.C.2    Ross, C.A.3    DeFranco, D.B.4
  • 83
    • 0035909330 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors arrest polyglutamine-dependent neurodegeneration in Drosophila
    • Steffan JS, Bodai L, Pallos J et al. : Histone deacetylase inhibitors arrest polyglutamine-dependent neurodegeneration in Drosophila. Nature 2001 ; 413 : 739-43
    • (2001) Nature , vol.413 , pp. 739-743
    • Steffan, J.S.1    Bodai, L.2    Pallos, J.3
  • 84
    • 0036578784 scopus 로고    scopus 로고
    • Disruption of CREB function in brain leads to neurodegeneration
    • Mantamadiotis T, Lemberger T, Bleckmann SC et al. : Disruption of CREB function in brain leads to neurodegeneration. Nat Genet 2002 ; 31 : 47-54
    • (2002) Nat Genet , vol.31 , pp. 47-54
    • Mantamadiotis, T.1    Lemberger, T.2    Bleckmann, S.C.3
  • 85
    • 29244462838 scopus 로고    scopus 로고
    • In vitro analysis of huntingtin-mediated transcriptional repression reveals multiple transcription factor targets
    • Zhai W, Jeong H, Cui L, Krainc D, Tjian R : In vitro analysis of huntingtin-mediated transcriptional repression reveals multiple transcription factor targets. Cell 2005 ; 123 : 1241-53
    • (2005) Cell , vol.123 , pp. 1241-1253
    • Zhai, W.1    Jeong, H.2    Cui, L.3    Krainc, D.4    Tjian, R.5
  • 86
    • 0037198698 scopus 로고    scopus 로고
    • Disruption of dynein/dynactin inhibits axonal transport in motor neurons causing late-onset progressive degeneration
    • LaMonte BH, Wallace KE, Holloway BA et al. : Disruption of dynein/dynactin inhibits axonal transport in motor neurons causing late-onset progressive degeneration. Neuron 2002 ; 34 : 715-27
    • (2002) Neuron , vol.34 , pp. 715-727
    • LaMonte, B.H.1    Wallace, K.E.2    Holloway, B.A.3
  • 87
    • 0042512291 scopus 로고    scopus 로고
    • Disruption of cellular transport : A common cause of neurodegeneration ?
    • Crosby AH : Disruption of cellular transport : a common cause of neurodegeneration ? Lancet Neurol 2003 ; 2 : 311-6
    • (2003) Lancet Neurol , vol.2 , pp. 311-316
    • Crosby, A.H.1
  • 88
    • 17844378486 scopus 로고    scopus 로고
    • Axonal transport failure in neurodegenerative disorders : The case of Huntington's disease
    • Charrin BC, Saudou F, Humbert S : Axonal transport failure in neurodegenerative disorders : the case of Huntington's disease. Pathol Biol (Paris) 2005 ; 53 : 189-92
    • (2005) Pathol Biol (Paris) , vol.53 , pp. 189-192
    • Charrin, B.C.1    Saudou, F.2    Humbert, S.3
  • 89
    • 0028989602 scopus 로고
    • Huntingtin is a cytoplasmic protein associated with vesicles in human and rat brain neurons
    • DiFiglia M, Sapp E, Chase K et al. : Huntingtin is a cytoplasmic protein associated with vesicles in human and rat brain neurons. Neuron 1995 ; 14 : 1075-81
    • (1995) Neuron , vol.14 , pp. 1075-1081
    • DiFiglia, M.1    Sapp, E.2    Chase, K.3
  • 90
    • 0030878098 scopus 로고    scopus 로고
    • Fast transport and retrograde movement of huntingtin and HAP1 in axons
    • Block-Galarza J, Chase KO, Sapp E et al. : Fast transport and retrograde movement of huntingtin and HAP1 in axons. Neuroreport 1997 ; 8 : 2247-51
    • (1997) Neuroreport , vol.8 , pp. 2247-2251
    • Block-Galarza, J.1    Chase, K.O.2    Sapp, E.3
  • 91
    • 85177155795 scopus 로고    scopus 로고
    • Gutekunst CA, Levey AI, Heilman CJ et al. : Identification and localization of huntingtin in brain and human lymphoblastoid cell lines with anti-fusion protein antibodies. Proc Natl Acad Sci U S A 1995 ; 92 : 8710-4
    • Gutekunst CA, Levey AI, Heilman CJ et al. : Identification and localization of huntingtin in brain and human lymphoblastoid cell lines with anti-fusion protein antibodies. Proc Natl Acad Sci U S A 1995 ; 92 : 8710-4
  • 92
    • 0030986659 scopus 로고    scopus 로고
    • HIP1, a human homologue of S. cerevisiae Sla2p, interacts with membrane-associated huntingtin in the brain
    • Kalchman MA, Koide HB, McCutcheon K et al. : HIP1, a human homologue of S. cerevisiae Sla2p, interacts with membrane-associated huntingtin in the brain. Nat Genet 1997 ; 16 : 44-53
    • (1997) Nat Genet , vol.16 , pp. 44-53
    • Kalchman, M.A.1    Koide, H.B.2    McCutcheon, K.3
  • 93
    • 0031056478 scopus 로고    scopus 로고
    • HIP-I : A huntingtin interacting protein isolated by the yeast two-hybrid system
    • Wanker EE, Rovira C, Scherzinger E et al. : HIP-I : a huntingtin interacting protein isolated by the yeast two-hybrid system. Hum Mol Genet 1997 ; 6 : 487-95
    • (1997) Hum Mol Genet , vol.6 , pp. 487-495
    • Wanker, E.E.1    Rovira, C.2    Scherzinger, E.3
  • 94
    • 0036500862 scopus 로고    scopus 로고
    • Perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with beta-tubulin : Relevance to Huntington's disease
    • Hoffner G, Kahlem P, Djian P : Perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with beta-tubulin : relevance to Huntington's disease. J Cell Sci 2002 ; 115 : 941-8
    • (2002) J Cell Sci , vol.115 , pp. 941-948
    • Hoffner, G.1    Kahlem, P.2    Djian, P.3
  • 95
    • 0036796261 scopus 로고    scopus 로고
    • PACSIN 1 interacts with huntingtin and is absent from synaptic varicosities in presymptomatic Huntington's disease brains
    • Modregger J, DiProspero NA, Charles V, Tagle DA, Plomann M : PACSIN 1 interacts with huntingtin and is absent from synaptic varicosities in presymptomatic Huntington's disease brains. Hum Mol Genet 2002 ; 11 : 2547-58
    • (2002) Hum Mol Genet , vol.11 , pp. 2547-2558
    • Modregger, J.1    DiProspero, N.A.2    Charles, V.3    Tagle, D.A.4    Plomann, M.5
  • 96
    • 0036850524 scopus 로고    scopus 로고
    • HIP14, a novel ankyrin domain-containing protein, links huntingtin to intracellular trafficking and endocytosis
    • Singaraja RR, Hadano S, Metzler M et al. : HIP14, a novel ankyrin domain-containing protein, links huntingtin to intracellular trafficking and endocytosis. Hum Mol Genet 2002 ; 11 : 2815-28
    • (2002) Hum Mol Genet , vol.11 , pp. 2815-2828
    • Singaraja, R.R.1    Hadano, S.2    Metzler, M.3
  • 97
    • 0141750470 scopus 로고    scopus 로고
    • Disruption of axonal transport by loss of huntingtin or expression of pathogenic polyQ proteins in Drosophila
    • Gunawardena S, Her LS, Brusch RG et al. : Disruption of axonal transport by loss of huntingtin or expression of pathogenic polyQ proteins in Drosophila. Neuron 2003 ; 40 : 25-40
    • (2003) Neuron , vol.40 , pp. 25-40
    • Gunawardena, S.1    Her, L.S.2    Brusch, R.G.3
  • 98
    • 0842269058 scopus 로고    scopus 로고
    • Cargo-carrying motor vehicles on the neuronal highway : Transport pathways and neurodegenerative disease
    • Gunawardena S, Goldstein LS : Cargo-carrying motor vehicles on the neuronal highway : transport pathways and neurodegenerative disease. J Neurobiol 2004 ; 58 : 258-71
    • (2004) J Neurobiol , vol.58 , pp. 258-271
    • Gunawardena, S.1    Goldstein, L.S.2
  • 99
    • 0034426013 scopus 로고    scopus 로고
    • Amino-terminal fragments of mutant huntingtin show selective accumulation in striatal neurons and synaptic toxicity
    • Li H, Li SH, Johnston H, Shelbourne PF, Li XJ : Amino-terminal fragments of mutant huntingtin show selective accumulation in striatal neurons and synaptic toxicity. Nat Genet 2000 ; 25 : 385-9
    • (2000) Nat Genet , vol.25 , pp. 385-389
    • Li, H.1    Li, S.H.2    Johnston, H.3    Shelbourne, P.F.4    Li, X.J.5
  • 100
    • 10744224530 scopus 로고    scopus 로고
    • Neuropathogenic forms of huntingtin and androgen receptor inhibit fast axonal transport
    • Szebenyi G, Morfini GA, Babcock A et al. : Neuropathogenic forms of huntingtin and androgen receptor inhibit fast axonal transport. Neuron 2003 ; 40 : 41-52
    • (2003) Neuron , vol.40 , pp. 41-52
    • Szebenyi, G.1    Morfini, G.A.2    Babcock, A.3
  • 101
    • 1542267796 scopus 로고    scopus 로고
    • Lee WC, Yoshihara M, Littleton JT : Cytoplasmic aggregates trap polyglutamine-containing proteins and block axonal transport in a Drosophila model of Huntington's disease. Proc Natl Acad Sci U S A 2004 ; 101 : 3224-9
    • Lee WC, Yoshihara M, Littleton JT : Cytoplasmic aggregates trap polyglutamine-containing proteins and block axonal transport in a Drosophila model of Huntington's disease. Proc Natl Acad Sci U S A 2004 ; 101 : 3224-9
  • 102
    • 4444316194 scopus 로고    scopus 로고
    • Mutant huntingtin impairs axonal trafficking in mammalian neurons in vivo and in vitro
    • Trushina E, Dyer RB, Badger JD et al. : Mutant huntingtin impairs axonal trafficking in mammalian neurons in vivo and in vitro. Mol Cell Biol 2004 ; 24 : 8195-209
    • (2004) Mol Cell Biol , vol.24 , pp. 8195-8209
    • Trushina, E.1    Dyer, R.B.2    Badger, J.D.3
  • 103
    • 0344413576 scopus 로고    scopus 로고
    • Role of NR2B-type NMDA receptors in selective neurodegeneration in Huntington disease
    • Li L, Fan M, Icton CD et al. : Role of NR2B-type NMDA receptors in selective neurodegeneration in Huntington disease. Neurobiol Aging 2003 ; 24 : 1113-21
    • (2003) Neurobiol Aging , vol.24 , pp. 1113-1121
    • Li, L.1    Fan, M.2    Icton, C.D.3
  • 104
    • 0035158533 scopus 로고    scopus 로고
    • Progressive depletion of complexin II in a transgenic mouse model of Huntington's disease
    • Morton AJ, Edwardson JM : Progressive depletion of complexin II in a transgenic mouse model of Huntington's disease. J Neurochem 2001 ; 76 : 166-72
    • (2001) J Neurochem , vol.76 , pp. 166-172
    • Morton, A.J.1    Edwardson, J.M.2
  • 105
    • 0036173770 scopus 로고    scopus 로고
    • Recruitment and activation of caspase-8 by the Huntingtin-interacting protein Hip-1 and a novel partner Hippi
    • Gervais FG, Singaraja R, Xanthoudakis S et al. : Recruitment and activation of caspase-8 by the Huntingtin-interacting protein Hip-1 and a novel partner Hippi. Nat Cell Biol 2002 ; 4 : 95-105
    • (2002) Nat Cell Biol , vol.4 , pp. 95-105
    • Gervais, F.G.1    Singaraja, R.2    Xanthoudakis, S.3
  • 106
    • 0037150687 scopus 로고    scopus 로고
    • Sp1 and TAFII130 transcriptional activity disrupted in early Huntington's disease
    • Dunah AW, Jeong H, Griffin A, Kim YM, Standaert DG, Hersch SM : Sp1 and TAFII130 transcriptional activity disrupted in early Huntington's disease. Science 2002 ; 296 : 2238-43
    • (2002) Science , vol.296 , pp. 2238-2243
    • Dunah, A.W.1    Jeong, H.2    Griffin, A.3    Kim, Y.M.4    Standaert, D.G.5    Hersch, S.M.6
  • 107
    • 0642334395 scopus 로고    scopus 로고
    • Abberant A2A receptor function in peripheral blood cells in Huntington's disease
    • Varani K, Abbracchio MP, Cannella M et al. : Abberant A2A receptor function in peripheral blood cells in Huntington's disease. FASEB J 2003 ; 17 : 2148-50
    • (2003) FASEB J , vol.17 , pp. 2148-2150
    • Varani, K.1    Abbracchio, M.P.2    Cannella, M.3
  • 108
    • 33745134073 scopus 로고    scopus 로고
    • Eraly and transient alteration of A2A receptor signalling in a mouse mode of Huntington's disease
    • Tarditi A, Camurri A, Varani K et al. : Eraly and transient alteration of A2A receptor signalling in a mouse mode of Huntington's disease. Neurobiol Dis 2006 ; 23 : 44-53
    • (2006) Neurobiol Dis , vol.23 , pp. 44-53
    • Tarditi, A.1    Camurri, A.2    Varani, K.3
  • 109
    • 0035816627 scopus 로고    scopus 로고
    • Polyglutamine-expanded huntingtin promotes sensitization of NMDA receptors via post-synaptic density 95
    • Sun Y, Savanenin A, Reddy PH, Liu YF : Polyglutamine-expanded huntingtin promotes sensitization of NMDA receptors via post-synaptic density 95. J Biol Chem 2001 ; 276 : 24713-8
    • (2001) J Biol Chem , vol.276 , pp. 24713-24718
    • Sun, Y.1    Savanenin, A.2    Reddy, P.H.3    Liu, Y.F.4
  • 110
    • 0019991784 scopus 로고
    • Cerebral metabolism and atrophy in Huntington's disease determined by 18FDG and computed tomographic scan
    • Kuhl DE, Phelps ME, Markham CH, Metter EJ, Riege WH, Winter J : Cerebral metabolism and atrophy in Huntington's disease determined by 18FDG and computed tomographic scan. Ann Neurol 1982 ; 12 : 425-34
    • (1982) Ann Neurol , vol.12 , pp. 425-434
    • Kuhl, D.E.1    Phelps, M.E.2    Markham, C.H.3    Metter, E.J.4    Riege, W.H.5    Winter, J.6
  • 111
    • 0022641113 scopus 로고
    • Positron emission tomography in the early diagnosis of Huntington's disease
    • Hayden MR, Martin WR, Stoessl AJ et al. : Positron emission tomography in the early diagnosis of Huntington's disease. Neurology 1986 ; 36 : 888-94
    • (1986) Neurology , vol.36 , pp. 888-894
    • Hayden, M.R.1    Martin, W.R.2    Stoessl, A.J.3
  • 112
    • 0023147905 scopus 로고
    • Reduced cerebral glucose metabolism in asymptomatic subjects at risk for Huntington's disease
    • Mazziotta JC, Phelps ME, Pahl JJ et al. : Reduced cerebral glucose metabolism in asymptomatic subjects at risk for Huntington's disease. N Engl J Med 1987 ; 316 : 357-62
    • (1987) N Engl J Med , vol.316 , pp. 357-362
    • Mazziotta, J.C.1    Phelps, M.E.2    Pahl, J.J.3
  • 113
    • 0025009430 scopus 로고
    • A comparison of neurological, metabolic, structural, and genetic evaluations in persons at risk for Huntington's disease
    • Grafton ST, Mazziotta JC, Pahl JJ et al. : A comparison of neurological, metabolic, structural, and genetic evaluations in persons at risk for Huntington's disease. Ann Neurol 1990 ; 28 : 614-21
    • (1990) Ann Neurol , vol.28 , pp. 614-621
    • Grafton, S.T.1    Mazziotta, J.C.2    Pahl, J.J.3
  • 114
    • 0027741301 scopus 로고
    • Evidence for impairment of energy metabolism in vivo in Huntington's disease using localized 1H NMR spectroscopy
    • Jenkins BG, Koroshetz WJ, Beal MF, Rosen BR : Evidence for impairment of energy metabolism in vivo in Huntington's disease using localized 1H NMR spectroscopy. Neurology 1993 ; 43 : 2689-95
    • (1993) Neurology , vol.43 , pp. 2689-2695
    • Jenkins, B.G.1    Koroshetz, W.J.2    Beal, M.F.3    Rosen, B.R.4
  • 115
    • 0031044805 scopus 로고    scopus 로고
    • Energy metabolism defects in Huntington's disease and effects of coenzyme Q10
    • Koroshetz WJ, Jenkins BG, Rosen BR, Beal MF : Energy metabolism defects in Huntington's disease and effects of coenzyme Q10. Ann Neurol 1997 ; 41 : 160-5
    • (1997) Ann Neurol , vol.41 , pp. 160-165
    • Koroshetz, W.J.1    Jenkins, B.G.2    Rosen, B.R.3    Beal, M.F.4
  • 116
    • 0031596998 scopus 로고    scopus 로고
    • 1H NMR spectroscopy studies of Huntington's disease : Correlations with CAG repeat numbers
    • Jenkins BG, Rosas HD, Chen YC et al. : 1H NMR spectroscopy studies of Huntington's disease : correlations with CAG repeat numbers. Neurology 1998 ; 50 : 1357-65
    • (1998) Neurology , vol.50 , pp. 1357-1365
    • Jenkins, B.G.1    Rosas, H.D.2    Chen, Y.C.3
  • 117
    • 0033914747 scopus 로고    scopus 로고
    • Abnormal in vivo skeletal muscle energy metabolism in Huntington's disease and dentatorubropa-llidoluysian atrophy
    • Lodi R, Schapira AH, Manners D et al. : Abnormal in vivo skeletal muscle energy metabolism in Huntington's disease and dentatorubropa-llidoluysian atrophy. Ann Neurol 2000 ; 48 : 72-6
    • (2000) Ann Neurol , vol.48 , pp. 72-76
    • Lodi, R.1    Schapira, A.H.2    Manners, D.3
  • 118
    • 22844440902 scopus 로고    scopus 로고
    • Mitochondrial impairment in patients and asymptomatic mutation carriers of Huntington's disease
    • Saft C, Zange J, Andrich J et al. : Mitochondrial impairment in patients and asymptomatic mutation carriers of Huntington's disease. Mov Disord 2005 ; 20 : 674-9
    • (2005) Mov Disord , vol.20 , pp. 674-679
    • Saft, C.1    Zange, J.2    Andrich, J.3
  • 120
    • 0030919567 scopus 로고    scopus 로고
    • Oxidative damage and metabolic dysfunction in Huntington's disease : Selective vulnerability of the basal ganglia
    • Browne SE, Bowling AC, MacGarvey U et al. : Oxidative damage and metabolic dysfunction in Huntington's disease : selective vulnerability of the basal ganglia. Ann Neurol 1997 ; 41 : 646-53
    • (1997) Ann Neurol , vol.41 , pp. 646-653
    • Browne, S.E.1    Bowling, A.C.2    MacGarvey, U.3
  • 122
    • 33745392939 scopus 로고    scopus 로고
    • Involvement of mitochondrial complex II defects in neuronal death produced by N-terminus fragment of mutated huntingtin
    • Benchoua A, Trioulier Y, Zala D et al. : Involvement of mitochondrial complex II defects in neuronal death produced by N-terminus fragment of mutated huntingtin. Mol Biol Cell 2006 ; 17 : 1652-63
    • (2006) Mol Biol Cell , vol.17 , pp. 1652-1663
    • Benchoua, A.1    Trioulier, Y.2    Zala, D.3
  • 123
    • 29144468251 scopus 로고    scopus 로고
    • 3-Nitropropionic acid : A mitochondrial toxin to uncover physiopathological mechanisms underlying striatal degeneration in Huntington's disease
    • Brouillet E, Jacquard C, Bizat N, Blum D : 3-Nitropropionic acid : a mitochondrial toxin to uncover physiopathological mechanisms underlying striatal degeneration in Huntington's disease. J Neurochem 2005 ; 95 : 1521-40
    • (2005) J Neurochem , vol.95 , pp. 1521-1540
    • Brouillet, E.1    Jacquard, C.2    Bizat, N.3    Blum, D.4
  • 124
    • 0032851595 scopus 로고    scopus 로고
    • Increased apoptosis of Huntington disease lymphoblasts associated with repeat length-dependent mitochondrial depolarization
    • Sawa A, Wiegand GW, Cooper J et al. : Increased apoptosis of Huntington disease lymphoblasts associated with repeat length-dependent mitochondrial depolarization. Nat Med 1999 ; 5 : 1194-8
    • (1999) Nat Med , vol.5 , pp. 1194-1198
    • Sawa, A.1    Wiegand, G.W.2    Cooper, J.3
  • 125
    • 0036327065 scopus 로고    scopus 로고
    • Early mitochondrial calcium defects in Huntington's disease are a direct effect of polyglutamines
    • Panov AV, Gutekunst CA, Leavitt BR et al. : Early mitochondrial calcium defects in Huntington's disease are a direct effect of polyglutamines. Nat Neurosci 2002 ; 5 : 731-6
    • (2002) Nat Neurosci , vol.5 , pp. 731-736
    • Panov, A.V.1    Gutekunst, C.A.2    Leavitt, B.R.3
  • 126
    • 3543141113 scopus 로고    scopus 로고
    • Mutant huntingtin directly increases susceptibility of mitochondria to the calcium-induced permeability transition and cytochrome c release
    • Choo YS, Johnson GV, MacDonald M, Detloff PJ, Lesort M : Mutant huntingtin directly increases susceptibility of mitochondria to the calcium-induced permeability transition and cytochrome c release. Hum Mol Genet 2004 ; 13 : 1407-20
    • (2004) Hum Mol Genet , vol.13 , pp. 1407-1420
    • Choo, Y.S.1    Johnson, G.V.2    MacDonald, M.3    Detloff, P.J.4    Lesort, M.5
  • 127
    • 1842533573 scopus 로고    scopus 로고
    • Striatal cells from mutant huntingtin knock-in mice are selectively vulnerable to mitochondrial complex II inhibitor-induced cell death through a non-apoptotic pathway
    • Ruan Q, Lesort M, MacDonald ME, Johnson GV : Striatal cells from mutant huntingtin knock-in mice are selectively vulnerable to mitochondrial complex II inhibitor-induced cell death through a non-apoptotic pathway. Hum Mol Genet 2004 ; 13 : 669-81
    • (2004) Hum Mol Genet , vol.13 , pp. 669-681
    • Ruan, Q.1    Lesort, M.2    MacDonald, M.E.3    Johnson, G.V.4
  • 128
    • 21544450545 scopus 로고    scopus 로고
    • p53 mediates cellular dysfunction and behavioral abnormalities in Huntington's disease
    • Bae BI, Xu H, Igarashi S et al. : p53 mediates cellular dysfunction and behavioral abnormalities in Huntington's disease. Neuron 2005 ; 47 : 29-41
    • (2005) Neuron , vol.47 , pp. 29-41
    • Bae, B.I.1    Xu, H.2    Igarashi, S.3
  • 129
    • 0014682523 scopus 로고
    • Brain lesions in an infant rhesus monkey treated with monsodium glutamate
    • Olney JW, Sharpe LG : Brain lesions in an infant rhesus monkey treated with monsodium glutamate. Science 1969 ; 166 : 386-8
    • (1969) Science , vol.166 , pp. 386-388
    • Olney, J.W.1    Sharpe, L.G.2
  • 130
    • 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 : Replication of the neurochemical characteristics of Huntington's disease by quinolinic acid. Nature 1986 ; 321 : 168-71
    • (1986) Nature , vol.321 , pp. 168-171
    • Beal, M.F.1    Kowall, N.W.2    Ellison, D.W.3    Mazurek, M.F.4    Swartz, K.J.5    Martin, J.B.6
  • 131
    • 0024533140 scopus 로고
    • Differential sparing of somatostatin-neuropeptide Y and cholinergic neurons following striatal excitotoxin lesions
    • Beal MF, Kowall NW, Swartz KJ, Ferrante RJ, Martin JB : Differential sparing of somatostatin-neuropeptide Y and cholinergic neurons following striatal excitotoxin lesions. Synapse 1989 ; 3 : 38-47
    • (1989) Synapse , vol.3 , pp. 38-47
    • Beal, M.F.1    Kowall, N.W.2    Swartz, K.J.3    Ferrante, R.J.4    Martin, J.B.5
  • 132
    • 0026043565 scopus 로고
    • Chronic quinolinic acid lesions in rats closely resemble Huntington's disease
    • Beal MF, Ferrante RJ, Swartz KJ, Kowall NW : Chronic quinolinic acid lesions in rats closely resemble Huntington's disease. J Neurosci 1991 ; 11 : 1649-59
    • (1991) J Neurosci , vol.11 , pp. 1649-1659
    • Beal, M.F.1    Ferrante, R.J.2    Swartz, K.J.3    Kowall, N.W.4
  • 133
    • 0027396021 scopus 로고
    • Excitotoxin lesions in primates as a model for Huntington's disease : Histopathologic and neurochemical characterization
    • Ferrante RJ, Kowall NW, Cipolloni PB, Storey E, Beal MF : Excitotoxin lesions in primates as a model for Huntington's disease : histopathologic and neurochemical characterization. Exp Neurol 1993 ; 119 : 46-71
    • (1993) Exp Neurol , vol.119 , pp. 46-71
    • Ferrante, R.J.1    Kowall, N.W.2    Cipolloni, P.B.3    Storey, E.4    Beal, M.F.5
  • 134
    • 0032815680 scopus 로고    scopus 로고
    • Replicating Huntington's disease phenotype in experimental animals
    • Brouillet E, Conde F, Beal MF, Hantraye P : Replicating Huntington's disease phenotype in experimental animals. Prog Neurobiol 1999 ; 59 : 427-68
    • (1999) Prog Neurobiol , vol.59 , pp. 427-468
    • Brouillet, E.1    Conde, F.2    Beal, M.F.3    Hantraye, P.4
  • 135
    • 0030997707 scopus 로고    scopus 로고
    • Quantifiable bradykinesia, gait abnormalities and Huntington's disease-like striatal lesions in rats chronically treated with 3-nitropropionic acid
    • Guyot MC, Hantraye P, Dolan R, Palfi S, Maziere M, Brouillet E : Quantifiable bradykinesia, gait abnormalities and Huntington's disease-like striatal lesions in rats chronically treated with 3-nitropropionic acid. Neuroscience 1997 ; 79 : 45-56
    • (1997) Neuroscience , vol.79 , pp. 45-56
    • Guyot, M.C.1    Hantraye, P.2    Dolan, R.3    Palfi, S.4    Maziere, M.5    Brouillet, E.6
  • 136
    • 0037107346 scopus 로고    scopus 로고
    • The adenosine A1 receptor agonist adenosine amine congener exerts a neuroprotective effect against the development of striatal lesions and motor impairments in the 3-nitropropionic acid model of neurotoxicity
    • Blum D, Gall D, Galas MC, D'Alcantara P, Bantubungi K, Schiffmann SN : The adenosine A1 receptor agonist adenosine amine congener exerts a neuroprotective effect against the development of striatal lesions and motor impairments in the 3-nitropropionic acid model of neurotoxicity. J Neurosci 2002 ; 22 : 9122-33
    • (2002) J Neurosci , vol.22 , pp. 9122-9133
    • Blum, D.1    Gall, D.2    Galas, M.C.3    D'Alcantara, P.4    Bantubungi, K.5    Schiffmann, S.N.6
  • 137
    • 0033740346 scopus 로고    scopus 로고
    • Neuronal death enhanced by N-methyl-D-aspartate antagonists
    • Ikonomidou C, Stefovska V, Turski L : Neuronal death enhanced by N-methyl-D-aspartate antagonists. Proc Natl Acad Sci U S A 2000 ; 97 : 12885-90
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 12885-12890
    • Ikonomidou, C.1    Stefovska, V.2    Turski, L.3
  • 138
    • 0026939298 scopus 로고
    • Role of excitotoxicity in human neurological disease
    • Beal MF : Role of excitotoxicity in human neurological disease. Curr Opin Neurobiol 1992 ; 2 : 657-62
    • (1992) Curr Opin Neurobiol , vol.2 , pp. 657-662
    • Beal, M.F.1
  • 139
    • 0027686249 scopus 로고
    • Puttfarcken P : Oxidative stress, glutamate, and neurodegenerative disorders
    • Coyle JT, Puttfarcken P : Oxidative stress, glutamate, and neurodegenerative disorders. Science 1993 ; 262 : 689-95
    • (1993) Science , vol.262 , pp. 689-695
    • Coyle, J.T.1
  • 140
    • 0028762647 scopus 로고
    • Excitatory amino acids as a final common pathway for neurologic disorders
    • Lipton SA, Rosenberg PA : Excitatory amino acids as a final common pathway for neurologic disorders. N Engl J Med 1994 ; 330 : 613-22
    • (1994) N Engl J Med , vol.330 , pp. 613-622
    • Lipton, S.A.1    Rosenberg, P.A.2
  • 141
    • 0033571743 scopus 로고    scopus 로고
    • Enhanced sensitivity to N-methyl-D-aspartate receptor activation in transgenic and knockin mouse models of Huntington's disease
    • Levine MS, Klapstein GJ, Koppel A et al. : Enhanced sensitivity to N-methyl-D-aspartate receptor activation in transgenic and knockin mouse models of Huntington's disease. J Neurosci Res 1999 ; 58 : 515-32
    • (1999) J Neurosci Res , vol.58 , pp. 515-532
    • Levine, M.S.1    Klapstein, G.J.2    Koppel, A.3
  • 142
    • 0035889535 scopus 로고    scopus 로고
    • NMDA receptor function in mouse models of Huntington disease
    • Cepeda C, Ariano MA, Calvert CR et al. : NMDA receptor function in mouse models of Huntington disease. J Neurosci Res 2001 ; 66 : 525-39
    • (2001) J Neurosci Res , vol.66 , pp. 525-539
    • Cepeda, C.1    Ariano, M.A.2    Calvert, C.R.3
  • 143
    • 0035575858 scopus 로고    scopus 로고
    • Changes in cortical and striatal neurons predict behavioral and electrophysiological abnormalities in a transgenic murine model of Huntington's disease
    • Laforet GA, Sapp E, Chase K et al. : Changes in cortical and striatal neurons predict behavioral and electrophysiological abnormalities in a transgenic murine model of Huntington's disease. J Neurosci 2001 ; 21 : 9112-23
    • (2001) J Neurosci , vol.21 , pp. 9112-9123
    • Laforet, G.A.1    Sapp, E.2    Chase, K.3
  • 144
    • 5044224807 scopus 로고    scopus 로고
    • Genetic mouse models of Huntington's and Parkinson's diseases : Illuminating but imperfect
    • Levine MS, Cepeda C, Hickey MA, Fleming SM, Chesselet MF : Genetic mouse models of Huntington's and Parkinson's diseases : illuminating but imperfect. Trends Neurosci 2004 ; 27 : 691-7
    • (2004) Trends Neurosci , vol.27 , pp. 691-697
    • Levine, M.S.1    Cepeda, C.2    Hickey, M.A.3    Fleming, S.M.4    Chesselet, M.F.5
  • 145
    • 0037075624 scopus 로고    scopus 로고
    • Increased sensitivity to N-methyl-D-aspartate receptor-mediated excitotoxicity in a mouse model of Huntington's disease
    • Zeron MM, Hansson O, Chen N et al. : Increased sensitivity to N-methyl-D-aspartate receptor-mediated excitotoxicity in a mouse model of Huntington's disease. Neuron 2002 ; 33 : 849-60
    • (2002) Neuron , vol.33 , pp. 849-860
    • Zeron, M.M.1    Hansson, O.2    Chen, N.3
  • 146
    • 0346749473 scopus 로고    scopus 로고
    • Enhanced Akt signaling is an early pro-survival response that reflects N-methyl-D-aspartate receptor activation in Huntington's disease knock-in striatal cells
    • Gines S, Ivanova E, Seong IS, Saura CA, MacDonald ME : Enhanced Akt signaling is an early pro-survival response that reflects N-methyl-D-aspartate receptor activation in Huntington's disease knock-in striatal cells. J Biol Chem 2003 ; 278 : 50514-22
    • (2003) J Biol Chem , vol.278 , pp. 50514-50522
    • Gines, S.1    Ivanova, E.2    Seong, I.S.3    Saura, C.A.4    MacDonald, M.E.5
  • 147
    • 29144460321 scopus 로고    scopus 로고
    • Expression of mutant huntingtin in glial cells contributes to neuronal excitotoxicity
    • Shin JY, Fang ZH, Yu ZX, Wang CE, Li SH, Li XJ : Expression of mutant huntingtin in glial cells contributes to neuronal excitotoxicity. J Cell Biol 2005 ; 171 : 1001-12
    • (2005) J Cell Biol , vol.171 , pp. 1001-1012
    • Shin, J.Y.1    Fang, Z.H.2    Yu, Z.X.3    Wang, C.E.4    Li, S.H.5    Li, X.J.6
  • 149
    • 0344413576 scopus 로고    scopus 로고
    • Role of NR2B-type NMDA receptors in selective neurodegeneration in Huntington's disease
    • Li L, Fan M, Icton CD et al. : Role of NR2B-type NMDA receptors in selective neurodegeneration in Huntington's disease. Neurobiol Aging 2003 ; 24 : 1113-21
    • (2003) Neurobiol Aging , vol.24 , pp. 1113-1121
    • Li, L.1    Fan, M.2    Icton, C.D.3
  • 150
    • 9644270316 scopus 로고    scopus 로고
    • Neostriatal and cortical quinolinate levels are increased in early grade Huntington's disease
    • Guidetti P, Luthi-Carter RE, Augood SJ, Schwarcz R : Neostriatal and cortical quinolinate levels are increased in early grade Huntington's disease. Neurobiol Dis 2004 ; 17 : 455-61
    • (2004) Neurobiol Dis , vol.17 , pp. 455-461
    • Guidetti, P.1    Luthi-Carter, R.E.2    Augood, S.J.3    Schwarcz, R.4
  • 151
    • 18144406846 scopus 로고    scopus 로고
    • Giorgini F, Guidetti P, Nguyen Q, Bennett SC, Muchowski PJ : A genomic screen in yeast implicates kynurenine 3-monooxygenase as a therapeutic target for Huntington disease. Nat Genet 2005 ; 37 : 526-31
    • Giorgini F, Guidetti P, Nguyen Q, Bennett SC, Muchowski PJ : A genomic screen in yeast implicates kynurenine 3-monooxygenase as a therapeutic target for Huntington disease. Nat Genet 2005 ; 37 : 526-31
  • 152
    • 4444302167 scopus 로고    scopus 로고
    • Deranged neuronal calcium signaling and Huntington disease
    • Bezprozvanny I, Hayden MR : Deranged neuronal calcium signaling and Huntington disease. Biochem Biophys Res Commun 2004 ; 322 : 1310-7
    • (2004) Biochem Biophys Res Commun , vol.322 , pp. 1310-1317
    • Bezprozvanny, I.1    Hayden, M.R.2
  • 153
    • 0041963057 scopus 로고    scopus 로고
    • Tang TS, Tu H, Chan EY et al. : Huntingtin and huntingtin-associated protein 1 influence neuronal calcium signaling mediated by inositol-(1,4,5) triphosphate receptor type 1. Neuron 2003 ; 39 : 227-39
    • Tang TS, Tu H, Chan EY et al. : Huntingtin and huntingtin-associated protein 1 influence neuronal calcium signaling mediated by inositol-(1,4,5) triphosphate receptor type 1. Neuron 2003 ; 39 : 227-39
  • 154
    • 0037096376 scopus 로고    scopus 로고
    • Calpain activation in Huntington's disease
    • Gafni J, Ellerby LM : Calpain activation in Huntington's disease. J Neurosci 2002 ; 22 : 4842-9
    • (2002) J Neurosci , vol.22 , pp. 4842-4849
    • Gafni, J.1    Ellerby, L.M.2
  • 155
    • 14044264256 scopus 로고    scopus 로고
    • Tang TS, Slow E, Lupu V et al. : Disturbed Ca2+ signaling and apoptosis of medium spiny neurons in Huntington's disease. Proc Natl Acad Sci U S A 2005 ; 102 : 2602-7
    • Tang TS, Slow E, Lupu V et al. : Disturbed Ca2+ signaling and apoptosis of medium spiny neurons in Huntington's disease. Proc Natl Acad Sci U S A 2005 ; 102 : 2602-7
  • 156
    • 0030937126 scopus 로고    scopus 로고
    • Decreases in evoked overflow of dopamine in rat striatum after neurotoxic doses of metamphetamine
    • Cass WA : Decreases in evoked overflow of dopamine in rat striatum after neurotoxic doses of metamphetamine. J Pharmacol Exp Ther 1997 ; 280 : 105-13
    • (1997) J Pharmacol Exp Ther , vol.280 , pp. 105-113
    • Cass, W.A.1
  • 157
    • 24744434920 scopus 로고    scopus 로고
    • Unravelling a role for dopamine in Huntington's disease : The dual role of reactive oxygen species and D2 receptor stimulation
    • Charvin D, Vanhoutte P, Pages C, Borrelli E, Caboche J : Unravelling a role for dopamine in Huntington's disease : the dual role of reactive oxygen species and D2 receptor stimulation. Proc Natl Acad Sci U S A 2005 ; 102 : 12218-23
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 12218-12223
    • Charvin, D.1    Vanhoutte, P.2    Pages, C.3    Borrelli, E.4    Caboche, J.5
  • 158
    • 33845612662 scopus 로고    scopus 로고
    • Dopamine enhances motor and neuropathological consequences of polyglutamine expanded huntingtin
    • Cyr M, Sotnikova TD, Gainetdinov RR, Caron MG : Dopamine enhances motor and neuropathological consequences of polyglutamine expanded huntingtin. FASEB J 2006 ; 20 : 2541-3
    • (2006) FASEB J , vol.20 , pp. 2541-2543
    • Cyr, M.1    Sotnikova, T.D.2    Gainetdinov, R.R.3    Caron, M.G.4
  • 159
    • 0032413345 scopus 로고    scopus 로고
    • 6-hydroxydopamine injections into the nigrostriatal pathway attenuate striatal malonate and 3-nitropropionic acid lesions
    • Maragos WF, Jakel RJ, Pang Z, Geddes JW 6-hydroxydopamine injections into the nigrostriatal pathway attenuate striatal malonate and 3-nitropropionic acid lesions. Exp Neurol 1998 ; 154 : 637-44
    • (1998) Exp Neurol , vol.154 , pp. 637-644
    • Maragos, W.F.1    Jakel, R.J.2    Pang, Z.3    Geddes, J.W.4
  • 160
    • 0032402138 scopus 로고    scopus 로고
    • Dopamine modulates the susceptibility of striatal neurons to 3-nitropropionic acid in the rat model of Huntington's disease
    • Reynolds DS, Carter RJ, Morton AJ : Dopamine modulates the susceptibility of striatal neurons to 3-nitropropionic acid in the rat model of Huntington's disease. J Neurosci 1998 ; 18 : 10116-27
    • (1998) J Neurosci , vol.18 , pp. 10116-10127
    • Reynolds, D.S.1    Carter, R.J.2    Morton, A.J.3
  • 161
    • 0038231381 scopus 로고    scopus 로고
    • Adenosine receptors and Huntington's disease : Implications for pathogenesis and therapeutics
    • Blum D, Hourez R, Galas MC, Popoli P, Schiffmann SN : Adenosine receptors and Huntington's disease : implications for pathogenesis and therapeutics. Lancet Neurol 2003 ; 2 : 366-74
    • (2003) Lancet Neurol , vol.2 , pp. 366-374
    • Blum, D.1    Hourez, R.2    Galas, M.C.3    Popoli, P.4    Schiffmann, S.N.5
  • 162
    • 0038113064 scopus 로고    scopus 로고
    • A dual role of adenosine A2A receptors in 3-nitropropionic acid-induced striatal lesions : Implications for the neuroprotective potential of A2A antagonists
    • Blum D, Galas MC, Pintor A et al. : A dual role of adenosine A2A receptors in 3-nitropropionic acid-induced striatal lesions : implications for the neuroprotective potential of A2A antagonists. J Neurosci 2003 ; 23 : 5361-9
    • (2003) J Neurosci , vol.23 , pp. 5361-5369
    • Blum, D.1    Galas, M.C.2    Pintor, A.3
  • 163
    • 0036522987 scopus 로고    scopus 로고
    • Blockade of striatal adenosine A2A receptor reduces, through a presynaptic mechanism, quinolinic acid-induced excitotoxicity : Possible relevance to neuroprotective interventions in neurodegenerative diseases of the striatum
    • Popoli P, Pintor A, Domenici MR et al. : Blockade of striatal adenosine A2A receptor reduces, through a presynaptic mechanism, quinolinic acid-induced excitotoxicity : possible relevance to neuroprotective interventions in neurodegenerative diseases of the striatum. J Neurosci 2002 ; 22 : 1967-75
    • (2002) J Neurosci , vol.22 , pp. 1967-1975
    • Popoli, P.1    Pintor, A.2    Domenici, M.R.3
  • 164
    • 20244362093 scopus 로고    scopus 로고
    • CGS21680 attenuates symptoms of Huntington's disease in a transgenic mouse model
    • Chou SY, Lee YC, Chen HM et al. : CGS21680 attenuates symptoms of Huntington's disease in a transgenic mouse model. J Neurochem 2005 ; 93 : 310-20
    • (2005) J Neurochem , vol.93 , pp. 310-320
    • Chou, S.Y.1    Lee, Y.C.2    Chen, H.M.3
  • 165
    • 37649008929 scopus 로고    scopus 로고
    • Functions, dysfunctions and possible therapeutic relevance of adenosine A2A receptors in Hutington's disease
    • sous presse
    • Popoli P Blum D, Martire A, Ledent C, Ceruti S, Abbracchio MP : Functions, dysfunctions and possible therapeutic relevance of adenosine A2A receptors in Hutington's disease. Prog Neurobiol 2006 (sous presse)
    • (2006) Prog Neurobiol
    • Popoli, P.1    Blum, D.2    Martire, A.3    Ledent, C.4    Ceruti, S.5    Abbracchio, M.P.6
  • 166
    • 18844441689 scopus 로고    scopus 로고
    • Emerging chemotherapeutic strategies for Huntington's disease
    • Ryu H, Ferrante RJ : Emerging chemotherapeutic strategies for Huntington's disease. Expert Opin Emerg Drugs 2005 ; 10 : 345-63
    • (2005) Expert Opin Emerg Drugs , vol.10 , pp. 345-363
    • Ryu, H.1    Ferrante, R.J.2
  • 167
    • 33646248382 scopus 로고    scopus 로고
    • CYTE-I-HD : Phase I dose finding and tolerability study of systeamine (cystagon) in Hutington's disease
    • Dubinsky R, Gray C : CYTE-I-HD : phase I dose finding and tolerability study of systeamine (cystagon) in Hutington's disease. Mov Disord 2006 ; 21 : 530-3
    • (2006) Mov Disord , vol.21 , pp. 530-533
    • Dubinsky, R.1    Gray, C.2
  • 168
    • 33646421164 scopus 로고    scopus 로고
    • Cystamine and cysteamine increase brain levels of BDNF in Huntington's disease via HSJ1b and transglutaminase
    • Borrell-Pages M, Canals JM, Cordelieres FP et al. : Cystamine and cysteamine increase brain levels of BDNF in Huntington's disease via HSJ1b and transglutaminase. J Clin Invest 2006 ; 116 : 140-24
    • (2006) J Clin Invest , vol.116 , pp. 140-124
    • Borrell-Pages, M.1    Canals, J.M.2    Cordelieres, F.P.3
  • 169
    • 31544454404 scopus 로고    scopus 로고
    • Rapamycin alleviates toxicity of different aggregate-prone proteins
    • Berger Z, Ravikumar B, Menzies FM et al. : Rapamycin alleviates toxicity of different aggregate-prone proteins. Hum Mol Genet 2006 ; 15 : 433-42
    • (2006) Hum Mol Genet , vol.15 , pp. 433-442
    • Berger, Z.1    Ravikumar, B.2    Menzies, F.M.3
  • 170
    • 0034537290 scopus 로고    scopus 로고
    • Autophagy as a regulated pathway of cellular degradation
    • Klionsky DJ, Emr SD : Autophagy as a regulated pathway of cellular degradation. Science 2000 ; 290 : 1717-21
    • (2000) Science , vol.290 , pp. 1717-1721
    • Klionsky, D.J.1    Emr, S.D.2
  • 171
    • 0036566266 scopus 로고    scopus 로고
    • Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy
    • Ravikumar B, Duden R, Rubinsztein DC : Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy. Hum Mol Genet 2002 ; 11 : 1107-17
    • (2002) Hum Mol Genet , vol.11 , pp. 1107-1117
    • Ravikumar, B.1    Duden, R.2    Rubinsztein, D.C.3
  • 172
    • 2642586352 scopus 로고    scopus 로고
    • Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease
    • Ravikumar B, Vacher C, Berger Z et al. : Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease. Nat Genet 2004 ; 36 : 585-95
    • (2004) Nat Genet , vol.36 , pp. 585-595
    • Ravikumar, B.1    Vacher, C.2    Berger, Z.3
  • 173
    • 25444483066 scopus 로고    scopus 로고
    • Lithium induces autophagy by inhibiting inositol monophosphatase
    • Sarkar S, Floto RA, Berger Z et al. : Lithium induces autophagy by inhibiting inositol monophosphatase. J Cell Biol 2005 ; 170 : 1101-11
    • (2005) J Cell Biol , vol.170 , pp. 1101-1111
    • Sarkar, S.1    Floto, R.A.2    Berger, Z.3
  • 174
    • 34247161367 scopus 로고    scopus 로고
    • Trehalose, a novel mTOR- independent autophagy enhancer, accelerates the clearance of mutant huntingtin and alpha-synuclein
    • Sarkar S, Davies JE, Huang Z, Tunnacliffe A, Rubinsztein DC : Trehalose, a novel mTOR- independent autophagy enhancer, accelerates the clearance of mutant huntingtin and alpha-synuclein. J Biol Chem 2007 ; 282 : 5641-52
    • (2007) J Biol Chem , vol.282 , pp. 5641-5652
    • Sarkar, S.1    Davies, J.E.2    Huang, Z.3    Tunnacliffe, A.4    Rubinsztein, D.C.5
  • 175
    • 34248994604 scopus 로고    scopus 로고
    • Small molecules enhance autophagy and reduce toxicity in Huntington's disease models
    • Sarkar S, Perlstein EO, Imarisio S et al. : Small molecules enhance autophagy and reduce toxicity in Huntington's disease models. Nat Chem Biol 2007 ; 3 : 331-8
    • (2007) Nat Chem Biol , vol.3 , pp. 331-338
    • Sarkar, S.1    Perlstein, E.O.2    Imarisio, S.3
  • 176
    • 20044390015 scopus 로고    scopus 로고
    • Zhang X, Smith DL, Meriin AB et al. : A potent small molecule inhibits polyglutamine aggregation in Huntington's disease neurons and suppresses neurodegeneration in vivo. Proc Natl Acad Sci U S A 2005 ; 102 : 892-7
    • Zhang X, Smith DL, Meriin AB et al. : A potent small molecule inhibits polyglutamine aggregation in Huntington's disease neurons and suppresses neurodegeneration in vivo. Proc Natl Acad Sci U S A 2005 ; 102 : 892-7
  • 177
    • 18744369020 scopus 로고    scopus 로고
    • Heiser V, Engemann S, Brocker W et al. : Identification of benzothiazoles as potential polyglutamine aggregation inhibitors of Huntington's disease by using an automated filter retardation assay. Proc Natl Acad Sci U S A 2002 ; 99 : 16400-6
    • Heiser V, Engemann S, Brocker W et al. : Identification of benzothiazoles as potential polyglutamine aggregation inhibitors of Huntington's disease by using an automated filter retardation assay. Proc Natl Acad Sci U S A 2002 ; 99 : 16400-6
  • 178
    • 33846351654 scopus 로고    scopus 로고
    • Selective inhibitors of death in mutant huntingtin cells
    • Varma H, Voisine C, DeMarco CT et al. : Selective inhibitors of death in mutant huntingtin cells. Nat Chem Biol 2007 ; 2 : 99-100
    • (2007) Nat Chem Biol , vol.2 , pp. 99-100
    • Varma, H.1    Voisine, C.2    DeMarco, C.T.3
  • 179
    • 0142157600 scopus 로고    scopus 로고
    • Histone deacetylase inhibition by sodium butyrate chemotherapy ameliorates the neurodegenerative phenotype in Huntington's disease mice
    • Ferrante RJ, Kubilus JK, Lee J et al. : Histone deacetylase inhibition by sodium butyrate chemotherapy ameliorates the neurodegenerative phenotype in Huntington's disease mice. J Neurosci 2003 ; 23 : 9418-27
    • (2003) J Neurosci , vol.23 , pp. 9418-9427
    • Ferrante, R.J.1    Kubilus, J.K.2    Lee, J.3
  • 180
    • 0037452775 scopus 로고    scopus 로고
    • Hockly E, Richon VM, Woodman B et al. : Suberoylanilide hydroxamic acid, a histone deacetylase inhibitor, ameliorates motor deficits in a mouse model of Huntington's disease. Proc Natl Acad Sci U S A 2003 ; 100 : 2041-6
    • Hockly E, Richon VM, Woodman B et al. : Suberoylanilide hydroxamic acid, a histone deacetylase inhibitor, ameliorates motor deficits in a mouse model of Huntington's disease. Proc Natl Acad Sci U S A 2003 ; 100 : 2041-6
  • 181
    • 19944431703 scopus 로고    scopus 로고
    • Neuroprotective Effects of Phenylbutyrate in the N171-82Q Transgenic Mouse Model of Huntington's Disease
    • Gardian G, Browne SE, Choi DK et al. : Neuroprotective Effects of Phenylbutyrate in the N171-82Q Transgenic Mouse Model of Huntington's Disease. J Biol Chem 2005 ; 280 : 556-63
    • (2005) J Biol Chem , vol.280 , pp. 556-563
    • Gardian, G.1    Browne, S.E.2    Choi, D.K.3
  • 182
    • 0036523110 scopus 로고    scopus 로고
    • Therapeutic effects of coenzyme Q10 and remacemide in transgenic mouse models of Huntington's disease
    • Ferrante RJ, Andreassen OA, Dedeoglu A et al. : Therapeutic effects of coenzyme Q10 and remacemide in transgenic mouse models of Huntington's disease. J Neurosci 2002 ; 22 : 1592-9
    • (2002) J Neurosci , vol.22 , pp. 1592-1599
    • Ferrante, R.J.1    Andreassen, O.A.2    Dedeoglu, A.3
  • 183
    • 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 : A randomized, placebo-controlled trial of coenzyme Q10 and remacemide in Huntington's disease. Neurology 2001 ; 57 : 397-404
    • (2001) Neurology , vol.57 , pp. 397-404
  • 184
    • 2942527444 scopus 로고    scopus 로고
    • Integrating fetal neural transplants into a therapeutic strategy : The example of Huntington's disease
    • Peschanski M, Bachoud-Levi AC, Hantraye P : Integrating fetal neural transplants into a therapeutic strategy : the example of Huntington's disease. Brain 2004 ; 127 : 1219-28
    • (2004) Brain , vol.127 , pp. 1219-1228
    • Peschanski, M.1    Bachoud-Levi, A.C.2    Hantraye, P.3
  • 185
    • 15444378095 scopus 로고    scopus 로고
    • Cell therapy in Huntington's disease
    • Dunnett SB, Rosser AE : Cell therapy in Huntington's disease. Neurorx 2004 ; 1 : 394-405
    • (2004) Neurorx , vol.1 , pp. 394-405
    • Dunnett, S.B.1    Rosser, A.E.2
  • 186
    • 0029011778 scopus 로고
    • Rationale for intrastriatal grafting of striatal neuroblasts in patients with Huntington's disease
    • Peschanski M, Cesaro P, Hantraye P : Rationale for intrastriatal grafting of striatal neuroblasts in patients with Huntington's disease. Neuroscience 1995 ; 68 : 273-85
    • (1995) Neuroscience , vol.68 , pp. 273-285
    • Peschanski, M.1    Cesaro, P.2    Hantraye, P.3
  • 188
    • 0031902287 scopus 로고    scopus 로고
    • Fetal striatal allografts reverse cognitive deficits in a primate model of Huntington disease
    • Palfi S, Conde F, Riche D et al. : Fetal striatal allografts reverse cognitive deficits in a primate model of Huntington disease. Nat Med 1998 ; 4 : 963-6
    • (1998) Nat Med , vol.4 , pp. 963-966
    • Palfi, S.1    Conde, F.2    Riche, D.3
  • 189
    • 0035553923 scopus 로고    scopus 로고
    • Neural transplantation : Restoring complex circuitry in the striatum
    • Fricker-Gates RA, Lundberg C, Dunnett SB : Neural transplantation : restoring complex circuitry in the striatum. Restor Neurol Neurosci 2001 ; 19 : 119-38
    • (2001) Restor Neurol Neurosci , vol.19 , pp. 119-138
    • Fricker-Gates, R.A.1    Lundberg, C.2    Dunnett, S.B.3
  • 190
    • 0021226160 scopus 로고
    • Functional neuronal replacement by grafted striatal neurones in the ibotenic acid-lesioned rat striatum
    • Isacson O, Brundin P, Kelly PA, Gage FH, Bjorklund A : Functional neuronal replacement by grafted striatal neurones in the ibotenic acid-lesioned rat striatum. Nature 1984 ; 311 : 458-60
    • (1984) Nature , vol.311 , pp. 458-460
    • Isacson, O.1    Brundin, P.2    Kelly, P.A.3    Gage, F.H.4    Bjorklund, A.5
  • 191
    • 0032211289 scopus 로고    scopus 로고
    • Striatal transplantation in a transgenic mouse model of Huntington's disease
    • Dunnett SB, Carter RJ, Watts C et al. : Striatal transplantation in a transgenic mouse model of Huntington's disease. Exp Neurol 1998 ; 154 : 31-40
    • (1998) Exp Neurol , vol.154 , pp. 31-40
    • Dunnett, S.B.1    Carter, R.J.2    Watts, C.3
  • 193
    • 0033940773 scopus 로고    scopus 로고
    • Behavioral recovery after transplantation into a rat model of Huntington's disease : Dependence on anatomical connectivity and extensive postoperative training
    • Brasted PJ, Watts C, Torres EM, Robbins TW, Dunnett SB : Behavioral recovery after transplantation into a rat model of Huntington's disease : dependence on anatomical connectivity and extensive postoperative training. Behav Neurosci 2000 ; 114 : 431-6
    • (2000) Behav Neurosci , vol.114 , pp. 431-436
    • Brasted, P.J.1    Watts, C.2    Torres, E.M.3    Robbins, T.W.4    Dunnett, S.B.5
  • 194
    • 0023900877 scopus 로고
    • Striatal grafts in rats with unilateral neostriatal lesions. II. In vivo monitoring of GABA release in globus pallidus and substantia nigra
    • Sirinathsinghji DJ, Dunnett SB, Isacson O, Clarke DJ, Kendrick K, Bjorklund A : Striatal grafts in rats with unilateral neostriatal lesions. II. In vivo monitoring of GABA release in globus pallidus and substantia nigra. Neuroscience 1988 ; 24 : 803-11
    • (1988) Neuroscience , vol.24 , pp. 803-811
    • Sirinathsinghji, D.J.1    Dunnett, S.B.2    Isacson, O.3    Clarke, D.J.4    Kendrick, K.5    Bjorklund, A.6
  • 195
    • 0026603230 scopus 로고
    • Anatomy and connectivity of intrastriatal striatal transplants
    • Wictorin K : Anatomy and connectivity of intrastriatal striatal transplants. Prog Neurobiol 1992 ; 38 : 611-39
    • (1992) Prog Neurobiol , vol.38 , pp. 611-639
    • Wictorin, K.1
  • 196
    • 0027460630 scopus 로고
    • Characterization of GABA release from intrastriatal striatal transplants : Dependence on host-derived afferents
    • Campbell K, Kalen P, Wictorin K, Lundberg C, Mandel RJ, Bjorklund A : Characterization of GABA release from intrastriatal striatal transplants : dependence on host-derived afferents. Neuroscience 1993 ; 53 : 403-15
    • (1993) Neuroscience , vol.53 , pp. 403-415
    • Campbell, K.1    Kalen, P.2    Wictorin, K.3    Lundberg, C.4    Mandel, R.J.5    Bjorklund, A.6
  • 197
    • 0032890301 scopus 로고    scopus 로고
    • Embryonic striatal grafts restore neuronal activity of the globus pallidus in a rodent model of Huntington's disease
    • Nakao N, Ogura M, Nakai K, Itakura T : Embryonic striatal grafts restore neuronal activity of the globus pallidus in a rodent model of Huntington's disease. Neuroscience 1999 ; 88 : 469-77
    • (1999) Neuroscience , vol.88 , pp. 469-477
    • Nakao, N.1    Ogura, M.2    Nakai, K.3    Itakura, T.4
  • 198
    • 0034015127 scopus 로고    scopus 로고
    • Fetal tissue transplants in animal models of Huntington's disease : The effects on damaged neuronal circuitry and behavioral deficits
    • Nakao N, Itakura T : Fetal tissue transplants in animal models of Huntington's disease : the effects on damaged neuronal circuitry and behavioral deficits. Prog Neurobiol 2000 ; 61 : 313-38
    • (2000) Prog Neurobiol , vol.61 , pp. 313-338
    • Nakao, N.1    Itakura, T.2
  • 199
    • 0037066096 scopus 로고    scopus 로고
    • Bilateral human fetal striatal transplantation in Huntington's disease
    • Hauser RA, Furtado S, Cimino CR et al. : Bilateral human fetal striatal transplantation in Huntington's disease. Neurology 2002 ; 58 : 687-95
    • (2002) Neurology , vol.58 , pp. 687-695
    • Hauser, R.A.1    Furtado, S.2    Cimino, C.R.3
  • 200
    • 0031887047 scopus 로고    scopus 로고
    • Safety of intrastriatal neurotransplantation for Huntington's disease patients
    • Kopyov OV, Jacques S, Lieberman A, Duma CM, Eagle KS : Safety of intrastriatal neurotransplantation for Huntington's disease patients. Exp Neurol 1998 ; 149 : 97-108
    • (1998) Exp Neurol , vol.149 , pp. 97-108
    • Kopyov, O.V.1    Jacques, S.2    Lieberman, A.3    Duma, C.M.4    Eagle, K.S.5
  • 201
    • 0034627143 scopus 로고    scopus 로고
    • Motor and cognitive improvements in patients with Huntington's disease after neural transplantation
    • Bachoud-Levi AC, Remy P, Nguyen JP et al. : Motor and cognitive improvements in patients with Huntington's disease after neural transplantation. Lancet 2000 ; 356 : 1975-9
    • (2000) Lancet , vol.356 , pp. 1975-1979
    • Bachoud-Levi, A.C.1    Remy, P.2    Nguyen, J.P.3
  • 202
    • 0034105443 scopus 로고    scopus 로고
    • Porcine xenografts in Parkinson's disease and Huntington's disease patients : Preliminary results
    • Fink JS, Schumacher JM, Ellias SL et al. : Porcine xenografts in Parkinson's disease and Huntington's disease patients : preliminary results. Cell Transplant 2000 ; 9 : 273-8.
    • (2000) Cell Transplant , vol.9 , pp. 273-278
    • Fink, J.S.1    Schumacher, J.M.2    Ellias, S.L.3
  • 203
    • 0036904801 scopus 로고    scopus 로고
    • Unilateral transplantation of human primary fetal tissue in four patients with Huntington's disease : NEST-UK safety report ISRCTN no 36485475
    • Rosser AE, Barker RA, Harrower T et al. : Unilateral transplantation of human primary fetal tissue in four patients with Huntington's disease : NEST-UK safety report ISRCTN no 36485475. J Neurol Neurosurg Psychiatry 2002 ; 73 : 678-85
    • (2002) J Neurol Neurosurg Psychiatry , vol.73 , pp. 678-685
    • Rosser, A.E.1    Barker, R.A.2    Harrower, T.3
  • 204
    • 9144221004 scopus 로고    scopus 로고
    • Striatal neural grafting improves cortical metabolism in Huntington's disease patients
    • Gaura V, Bachoud-Levi AC, Ribeiro MJ et al. : Striatal neural grafting improves cortical metabolism in Huntington's disease patients. Brain 2004 ; 127 : 65-72
    • (2004) Brain , vol.127 , pp. 65-72
    • Gaura, V.1    Bachoud-Levi, A.C.2    Ribeiro, M.J.3
  • 205
    • 0033595502 scopus 로고    scopus 로고
    • Influence of lamotrigine on progression of early Huntington disease : A randomized clinical trial
    • Kremer B, Clark CM, Almqvist EW et al. : Influence of lamotrigine on progression of early Huntington disease : a randomized clinical trial. Neurology 1999 ; 53 : 1000-11
    • (1999) Neurology , vol.53 , pp. 1000-1011
    • Kremer, B.1    Clark, C.M.2    Almqvist, E.W.3
  • 206
    • 33644967927 scopus 로고    scopus 로고
    • Effect of fetal neural transplants in patients with Huntington's disease 6 years after surgery : A long-term follow-up study
    • Bachoud-Levi AC, Gaura V, Brugieres P et al. : Effect of fetal neural transplants in patients with Huntington's disease 6 years after surgery : a long-term follow-up study. Lancet Neurol 2006 ; 5 : 303-9
    • (2006) Lancet Neurol , vol.5 , pp. 303-309
    • Bachoud-Levi, A.C.1    Gaura, V.2    Brugieres, P.3
  • 208
    • 0032854992 scopus 로고    scopus 로고
    • The IGF-I amino-terminal tripeptide glycine-proline-glutamate (GPE) is neuroprotective to striatum in the quinolinic acid lesion animal model of Huntington's disease
    • Alexi T, Hughes PE, Roon-Mom WM et al. : The IGF-I amino-terminal tripeptide glycine-proline-glutamate (GPE) is neuroprotective to striatum in the quinolinic acid lesion animal model of Huntington's disease. Exp Neurol 1999 ; 159 : 84-97
    • (1999) Exp Neurol , vol.159 , pp. 84-97
    • Alexi, T.1    Hughes, P.E.2    Roon-Mom, W.M.3
  • 209
    • 0033789409 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor, neurotrophin-3, and neurotrophin-4/5 prevent the death of striatal projection neurons in a rodent model of Huntington's disease
    • Perez-Navarro E, Canudas AM, Akerund P, Alberch J, Arenas E : Brain-derived neurotrophic factor, neurotrophin-3, and neurotrophin-4/5 prevent the death of striatal projection neurons in a rodent model of Huntington's disease. J Neurochem 2000 ; 75 : 2190-9
    • (2000) J Neurochem , vol.75 , pp. 2190-2199
    • Perez-Navarro, E.1    Canudas, A.M.2    Akerund, P.3    Alberch, J.4    Arenas, E.5
  • 210
    • 0343091556 scopus 로고    scopus 로고
    • Neurturin protects striatal projection neurons but not interneurons in a rat model of Huntington's disease
    • Perez Navaro E, Akerud P, Marco S et al. : Neurturin protects striatal projection neurons but not interneurons in a rat model of Huntington's disease. Neuroscience 2000 ; 98 : 89-96
    • (2000) Neuroscience , vol.98 , pp. 89-96
    • Perez Navaro, E.1    Akerud, P.2    Marco, S.3
  • 211
    • 0036094145 scopus 로고    scopus 로고
    • Neuroprotection by neurotrophins and GDNF family members in the excitotoxic model of Huntington's disease
    • Alberch J, Perez-Navarro E, Canals JM : Neuroprotection by neurotrophins and GDNF family members in the excitotoxic model of Huntington's disease. Brain Res Bull 2002 ; 57 : 817-22
    • (2002) Brain Res Bull , vol.57 , pp. 817-822
    • Alberch, J.1    Perez-Navarro, E.2    Canals, J.M.3
  • 213
    • 0034690615 scopus 로고    scopus 로고
    • Restauration of cognitive and motor functions by ciliary neurotrophic factor in a primate model of Huntington's disease
    • Mittoux V, Joseph JM, Conde F et al. : Restauration of cognitive and motor functions by ciliary neurotrophic factor in a primate model of Huntington's disease. Hum Gene Ther 2000 ; 11 : 1177-87
    • (2000) Hum Gene Ther , vol.11 , pp. 1177-1187
    • Mittoux, V.1    Joseph, J.M.2    Conde, F.3
  • 214
    • 0034979217 scopus 로고    scopus 로고
    • Neuroprotective effect of a CNTF-expressing lentiviral vector in the quinolinic acid rat model of Huntington's disease
    • Almeida LP, Zala D, Aebischer P, Deglon N : Neuroprotective effect of a CNTF-expressing lentiviral vector in the quinolinic acid rat model of Huntington's disease. Neurobiol Dis 2001 ; 8 : 433-46
    • (2001) Neurobiol Dis , vol.8 , pp. 433-446
    • Almeida, L.P.1    Zala, D.2    Aebischer, P.3    Deglon, N.4
  • 215
    • 1842868523 scopus 로고    scopus 로고
    • Dose-dependent neuroprotective effect of ciliary neurotrophic factor delivered via tetracycline-regulated lentiviral vectors in the quinolinic acid rat model of Huntington's disease
    • Regulier E, Pereira A, Sommer B, Aebischer P, Deglon N : Dose-dependent neuroprotective effect of ciliary neurotrophic factor delivered via tetracycline-regulated lentiviral vectors in the quinolinic acid rat model of Huntington's disease. Hum Gene Ther 2002 ; 13 : 1981-90
    • (2002) Hum Gene Ther , vol.13 , pp. 1981-1990
    • Regulier, E.1    Pereira, A.2    Sommer, B.3    Aebischer, P.4    Deglon, N.5
  • 216
    • 0036615771 scopus 로고    scopus 로고
    • Corticostriatopallidal neuroprotection by adenovirus-mediated ciliary neurotrophic factor gene transfer in a rat model of progressive striatal degeneration
    • Mittoux V, Ouary S, Monville C et al. : Corticostriatopallidal neuroprotection by adenovirus-mediated ciliary neurotrophic factor gene transfer in a rat model of progressive striatal degeneration. J Neurosci 2002 ; 22 : 4478-86
    • (2002) J Neurosci , vol.22 , pp. 4478-4486
    • Mittoux, V.1    Ouary, S.2    Monville, C.3
  • 217
    • 0030344755 scopus 로고    scopus 로고
    • The problems of delivering neuroactive molecules to the CNS
    • Tan SA, Aebischer P : The problems of delivering neuroactive molecules to the CNS. Ciba Found Symp 1996 ; 196 : 211-36
    • Ciba Found Symp 1996 , vol.196 , pp. 211-236
    • Tan, S.A.1    Aebischer, P.2
  • 218
    • 0030911441 scopus 로고    scopus 로고
    • Cellular delivery of human CNTF prevents motor and cognitive dysfunction in a rodent model of Huntington's disease
    • Emerich DF, Cain CK, Greco C et al. : Cellular delivery of human CNTF prevents motor and cognitive dysfunction in a rodent model of Huntington's disease. Cell Transplant 1997 ; 6 : 249-66
    • (1997) Cell Transplant , vol.6 , pp. 249-266
    • Emerich, D.F.1    Cain, C.K.2    Greco, C.3
  • 219
    • 0030906578 scopus 로고    scopus 로고
    • Protective effect of encapsulated cells producing neurotrophic factor CNTF in a monkey model of Huntington's disease
    • Emerich DF, Winn SR, Hantraye PM et al. : Protective effect of encapsulated cells producing neurotrophic factor CNTF in a monkey model of Huntington's disease. Nature 1997 ; 386 : 395-9
    • (1997) Nature , vol.386 , pp. 395-399
    • Emerich, D.F.1    Winn, S.R.2    Hantraye, P.M.3
  • 220
    • 15844381714 scopus 로고    scopus 로고
    • Intrathecal delivery of CNTF using encapsulated genetically modified xenogeneic cells in amyotrophic lateral sclerosis patients
    • Aebischer P, Schluep M, Deglon N et al. : Intrathecal delivery of CNTF using encapsulated genetically modified xenogeneic cells in amyotrophic lateral sclerosis patients. Nat Med 1996 ; 2 : 696-9
    • (1996) Nat Med , vol.2 , pp. 696-699
    • Aebischer, P.1    Schluep, M.2    Deglon, N.3
  • 221
    • 5644295321 scopus 로고    scopus 로고
    • Neuroprotective gene therapy for Huntington's disease, using polymer-encapsulated cells engineered to secrete human ciliary neurotrophic factor : Results of a phase I study
    • Bloch J, Bachoud-Levi AC, Deglon N et al. : Neuroprotective gene therapy for Huntington's disease, using polymer-encapsulated cells engineered to secrete human ciliary neurotrophic factor : results of a phase I study. Hum Gene Ther 2004 ; 15 : 968-75
    • (2004) Hum Gene Ther , vol.15 , pp. 968-975
    • Bloch, J.1    Bachoud-Levi, A.C.2    Deglon, N.3
  • 222
    • 2342598416 scopus 로고    scopus 로고
    • Experimental therapeutics in transgenic mouse models of Huntington's disease
    • Beal MF, Ferrante RJ : Experimental therapeutics in transgenic mouse models of Huntington's disease. Nat Rev Neurosci 2004 ; 5 : 373-84
    • (2004) Nat Rev Neurosci , vol.5 , pp. 373-384
    • Beal, M.F.1    Ferrante, R.J.2


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