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Volumn 1, Issue 1-2, 2001, Pages 142-152

Huntington's disease

Author keywords

Glutamine; Huntington; Movement; Neurodegeneration; Psychiatric; Trinucleotide repeat

Indexed keywords


EID: 0001337742     PISSN: 15662772     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1566-2772(00)00014-1     Document Type: Article
Times cited : (32)

References (102)
  • 3
    • 0025290717 scopus 로고
    • Huntington's disease in Venezuela: Seven years of follow-up on symptomatic and asymptomatic individuals
    • Penney Jr JB, Young AB, Shoulson I, et al. Huntington's disease in Venezuela: seven years of follow-up on symptomatic and asymptomatic individuals. Mov Disord 1990;5:93-99.
    • (1990) Mov Disord , vol.5 , pp. 93-99
    • Penney Jr., J.B.1    Young, A.B.2    Shoulson, I.3
  • 4
    • 0023935740 scopus 로고
    • Differential cognitive impairment in Alzheimer disease and Huntington's disease
    • Brandt J, Folstein SE, Folstein MF. Differential cognitive impairment in Alzheimer disease and Huntington's disease. Ann Neurol 1988;23:555-561.
    • (1988) Ann Neurol , vol.23 , pp. 555-561
    • Brandt, J.1    Folstein, S.E.2    Folstein, M.F.3
  • 7
    • 0034094873 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegeneration
    • Zoghbi HY, Orr HT. Glutamine repeats and neurodegeneration. Annu Rev Neurosci 2000;23:217-247.
    • (2000) Annu Rev Neurosci , vol.23 , pp. 217-247
    • Zoghbi, H.Y.1    Orr, H.T.2
  • 8
    • 0030868770 scopus 로고    scopus 로고
    • Reviews in molecular medicine: Huntington disease and the related disorder, dentatorubral-pallidoluysian atrophy (DRPLA)
    • Ross CA, Margolis RL, Rosenblatt A, Ranen NG, Becher MW, Aylward E. Reviews in molecular medicine: Huntington disease and the related disorder, dentatorubral-pallidoluysian atrophy (DRPLA). Medicine 1997;76:305-338.
    • (1997) Medicine , vol.76 , pp. 305-338
    • Ross, C.A.1    Margolis, R.L.2    Rosenblatt, A.3    Ranen, N.G.4    Becher, M.W.5    Aylward, E.6
  • 9
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • Group HDCR. A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell 1993;72:971-983.
    • (1993) Cell , vol.72 , pp. 971-983
  • 10
    • 0030948716 scopus 로고    scopus 로고
    • The genetic defect causing Huntington's disease: Repeated in other contexts?
    • Gusella JF, Persichetti F, MacDonald ME. The genetic defect causing Huntington's disease: repeated in other contexts? Mol Med 1997;3:238-246.
    • (1997) Mol Med , vol.3 , pp. 238-246
    • Gusella, J.F.1    Persichetti, F.2    MacDonald, M.E.3
  • 11
    • 0029089172 scopus 로고
    • When more is less: Pathogenesis of glutamine repeat neurodegenerative diseases
    • Ross CA. When more is less: pathogenesis of glutamine repeat neurodegenerative diseases. Neuron 1995;15:493-496.
    • (1995) Neuron , vol.15 , pp. 493-496
    • Ross, C.A.1
  • 12
    • 0028260436 scopus 로고
    • Structure and expression of the Huntington's disease gene: Evidence against simple inactivation due to an expanded CAG repeat
    • Ambrose CM, Duyao MP, Barnes G, et al. Structure and expression of the Huntington's disease gene: evidence against simple inactivation due to an expanded CAG repeat. Somat Cell Mol Genet 1994;20:27-28.
    • (1994) Somat Cell Mol Genet , vol.20 , pp. 27-28
    • Ambrose, C.M.1    Duyao, M.P.2    Barnes, G.3
  • 13
    • 0029997090 scopus 로고    scopus 로고
    • Phenotypic characterization of individuals with 30-40 CAG repeats and apparently normal elderly individuals with 36-39 repeats
    • Rubinsztein DC, Leggo J, Coles R, et al. Phenotypic characterization of individuals with 30-40 CAG repeats and apparently normal elderly individuals with 36-39 repeats. Am J Hum Genet 1996;59:16-22.
    • (1996) Am J Hum Genet , vol.59 , pp. 16-22
    • Rubinsztein, D.C.1    Leggo, J.2    Coles, R.3
  • 14
    • 0029908301 scopus 로고    scopus 로고
    • Anticipation - An old idea in new genes
    • McInnis MG. Anticipation - an old idea in new genes. Am J Hum Genet 1996;59:973-979.
    • (1996) Am J Hum Genet , vol.59 , pp. 973-979
    • McInnis, M.G.1
  • 15
    • 0027240431 scopus 로고
    • Trinucleotide repeat length instability and age of onset in Huntington's disease
    • Duyao M, Ambrose C, Myers R, et al. Trinucleotide repeat length instability and age of onset in Huntington's disease. Nat Genet 1993;4:387-392.
    • (1993) Nat Genet , vol.4 , pp. 387-392
    • Duyao, M.1    Ambrose, C.2    Myers, R.3
  • 16
    • 0027377151 scopus 로고
    • Correlation between the onset of Huntington's disease and length of the trinucleotide repeat in IT-15
    • Stine OC, Pleasant N, Franz ML, Abbott MH, Folstein SE, Ross CA. Correlation between the onset of Huntington's disease and length of the trinucleotide repeat in IT-15. Hum Mol Genet 1993;2:1547-1549.
    • (1993) Hum Mol Genet , vol.2 , pp. 1547-1549
    • Stine, O.C.1    Pleasant, N.2    Franz, M.L.3    Abbott, M.H.4    Folstein, S.E.5    Ross, C.A.6
  • 17
    • 0029130324 scopus 로고
    • Anticipation and instability of (CAG)n repeats in IT-15 in parent-offspring pairs with Huntington's disease
    • Ranen NG, Stine OC, Abbott MH, et al. Anticipation and instability of (CAG)n repeats in IT-15 in parent-offspring pairs with Huntington's disease. Am J Hum Genet 1995;57:593-602.
    • (1995) Am J Hum Genet , vol.57 , pp. 593-602
    • Ranen, N.G.1    Stine, O.C.2    Abbott, M.H.3
  • 18
    • 0027176364 scopus 로고
    • The relationship between trinucleotide (CAG) repeat length and clinical features of Huntington's disease
    • Andrew SE, Goldberg YP, Kremer B, et al. The relationship between trinucleotide (CAG) repeat length and clinical features of Huntington's disease. Nat Genet 1993;4:398-403.
    • (1993) Nat Genet , vol.4 , pp. 398-403
    • Andrew, S.E.1    Goldberg, Y.P.2    Kremer, B.3
  • 19
    • 0028985055 scopus 로고
    • Diagnosis of 'sporadic' Huntington's disease
    • Durr A, Dode C, Hahn V, et al. Diagnosis of 'sporadic' Huntington's disease. J Neurol Sci 1995;129:51-55.
    • (1995) J Neurol Sci , vol.129 , pp. 51-55
    • Durr, A.1    Dode, C.2    Hahn, V.3
  • 20
    • 0031037349 scopus 로고    scopus 로고
    • Longitudinal change in basal ganglia volume in patients with Huntington's disease
    • Aylward EH, Li Q, Stine OC, et al. Longitudinal change in basal ganglia volume in patients with Huntington's disease. Neurology 1997;48:394-399.
    • (1997) Neurology , vol.48 , pp. 394-399
    • Aylward, E.H.1    Li, Q.2    Stine, O.C.3
  • 21
    • 0028099274 scopus 로고
    • Trinucleotide repeat length and progression of illness in Huntington's disease
    • Kieburtz K, MacDonald M, Shih C, et al. Trinucleotide repeat length and progression of illness in Huntington's disease. J Med Genet 1994;31:872-874.
    • (1994) J Med Genet , vol.31 , pp. 872-874
    • Kieburtz, K.1    MacDonald, M.2    Shih, C.3
  • 22
    • 0030069713 scopus 로고    scopus 로고
    • Relationship between trinucleotide repeats and neuropathological changes in Huntington disease
    • Furtado S, Suchowersky O, Rewcastle B, Graham L, Klimek ML, Garber A. Relationship between trinucleotide repeats and neuropathological changes in Huntington disease. Ann Neurol 1996;39:132-136.
    • (1996) Ann Neurol , vol.39 , pp. 132-136
    • Furtado, S.1    Suchowersky, O.2    Rewcastle, B.3    Graham, L.4    Klimek, M.L.5    Garber, A.6
  • 24
    • 0026717486 scopus 로고
    • Preferential loss of striato external pallidal projection neurons in presymptomatic Huntington' s disease
    • Albin RL, Reiner A, Anderson KD, et al. Preferential loss of striato external pallidal projection neurons in presymptomatic Huntington' s disease. Ann Neurol 1992;31:425-430.
    • (1992) Ann Neurol , vol.31 , pp. 425-430
    • Albin, R.L.1    Reiner, A.2    Anderson, K.D.3
  • 27
    • 0023865274 scopus 로고
    • Clinical and neuropathologic assessment of severity in Huntington disease
    • Myers RH, Vonsattel J-P, Stevens TJ, et al. Clinical and neuropathologic assessment of severity in Huntington disease. Neurology 1988;38:341-347.
    • (1988) Neurology , vol.38 , pp. 341-347
    • Myers, R.H.1    Vonsattel, J.-P.2    Stevens, T.J.3
  • 28
    • 0025885733 scopus 로고
    • Neuronal loss in layers V and VI of cerebral cortex in Huntington's disease
    • Hedreen JC, Peyser CE, Folstein SE, Ross CA. Neuronal loss in layers V and VI of cerebral cortex in Huntington's disease. Neurosci Lett 1991;133:257-261.
    • (1991) Neurosci Lett , vol.133 , pp. 257-261
    • Hedreen, J.C.1    Peyser, C.E.2    Folstein, S.E.3    Ross, C.A.4
  • 29
    • 0021921929 scopus 로고
    • A Golgi study of the human neostriatum: Neurons and afferent fibers
    • Graveland GA, Williams RS, DiFiglia M. A Golgi study of the human neostriatum: neurons and afferent fibers. J Comp Neurol 1985;234:317-333.
    • (1985) J Comp Neurol , vol.234 , pp. 317-333
    • Graveland, G.A.1    Williams, R.S.2    DiFiglia, M.3
  • 30
    • 0027377217 scopus 로고
    • Evidence for neuronal degeneration and dendritic plasticity in cortical pyramidal neurons of Huntington' s disease: A quantitative Golgi study
    • Sotrel A, Williams RS, Kaufmann WE, Myers RH. Evidence for neuronal degeneration and dendritic plasticity in cortical pyramidal neurons of Huntington' s disease: a quantitative Golgi study. Neurology 1993;43:2088-2986.
    • (1993) Neurology , vol.43 , pp. 2088-2986
    • Sotrel, A.1    Williams, R.S.2    Kaufmann, W.E.3    Myers, R.H.4
  • 31
    • 0021891247 scopus 로고
    • Huntington's disease: Two families with differing clinical features show linkage to the G8 probe
    • Folstein SE, Phillips III JA, Meyers DA, et al. Huntington's disease: two families with differing clinical features show linkage to the G8 probe. Science 1985;229:776-779.
    • (1985) Science , vol.229 , pp. 776-779
    • Folstein, S.E.1    Phillips III, J.A.2    Meyers, D.A.3
  • 32
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neuntes in brain
    • DiFiglia M, Sapp E, Chase KO, et al. Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neuntes in brain. Science 1997;277:1990-1993.
    • (1997) Science , vol.277 , pp. 1990-1993
    • DiFiglia, M.1    Sapp, E.2    Chase, K.O.3
  • 33
    • 0031918640 scopus 로고    scopus 로고
    • Intranuclear neuronal inclusions in Huntington's disease and dentatorubral and pallidoluysian atrophy: Correlation between the density of inclusions and IT15 CAG triplet repeat length
    • Becher MW, Kotzuk JA, Sharp AH, et al. Intranuclear neuronal inclusions in Huntington's disease and dentatorubral and pallidoluysian atrophy: correlation between the density of inclusions and IT15 CAG triplet repeat length. Neurobiol Dis 1998;4:387-397.
    • (1998) Neurobiol Dis , vol.4 , pp. 387-397
    • Becher, M.W.1    Kotzuk, J.A.2    Sharp, A.H.3
  • 35
    • 18544410106 scopus 로고    scopus 로고
    • Formation of neuronal intranuclear inclusions (Nil) underlies the neurological dysfunction in mice transgenic for the HD mutation
    • Davies SW, Turmaine M, Cozens BA, et al. Formation of neuronal intranuclear inclusions (Nil) underlies the neurological dysfunction in mice transgenic for the HD mutation. Cell 1997;90:537-548.
    • (1997) Cell , vol.90 , pp. 537-548
    • Davies, S.W.1    Turmaine, M.2    Cozens, B.A.3
  • 36
    • 0023115076 scopus 로고
    • Homozygotes for Huntington's disease
    • Wexler NS, Young AB, Tanzi RE, et al. Homozygotes for Huntington's disease. Nature 1987;326:194-197.
    • (1987) Nature , vol.326 , pp. 194-197
    • Wexler, N.S.1    Young, A.B.2    Tanzi, R.E.3
  • 37
    • 0033525036 scopus 로고    scopus 로고
    • Molecular and cellular genetics of fragile X syndrome
    • Kaufmann WE, Reiss AL. Molecular and cellular genetics of fragile X syndrome. Am J Med Genet 1999;88:11-24.
    • (1999) Am J Med Genet , vol.88 , pp. 11-24
    • Kaufmann, W.E.1    Reiss, A.L.2
  • 38
    • 0030613177 scopus 로고    scopus 로고
    • Huntingtin is required for neurogenesis and is not impaired by the Huntington' s disease CAG expansion
    • White JK, Auerbach W, Duyao MP, et al. Huntingtin is required for neurogenesis and is not impaired by the Huntington' s disease CAG expansion. Nat Genet 1997;17:404-410.
    • (1997) Nat Genet , vol.17 , pp. 404-410
    • White, J.K.1    Auerbach, W.2    Duyao, M.P.3
  • 39
    • 0022446150 scopus 로고
    • Replication of the neurochemical characteristics of Huntington's disease by quinolinic acid
    • Beal MF, Kowall NW, Ellison DZW, Mazurek MF, Swartz KJ, Martin JB. Replication of the neurochemical characteristics of Huntington's disease by quinolinic acid. Nature 1986;321:168-171.
    • (1986) Nature , vol.321 , pp. 168-171
    • Beal, M.F.1    Kowall, N.W.2    Ellison, D.Z.W.3    Mazurek, M.F.4    Swartz, K.J.5    Martin, J.B.6
  • 40
    • 0027433553 scopus 로고
    • Neurochemical and histologic characterization of striatal excitotoxic lesions produced by the mitochondrial toxin 3-nitropropionic acid
    • Beal MF, Brouillet E, Jenkins B, et al. Neurochemical and histologic characterization of striatal excitotoxic lesions produced by the mitochondrial toxin 3-nitropropionic acid. J Neurosci 1993;13:4181-4192.
    • (1993) J Neurosci , vol.13 , pp. 4181-4192
    • Beal, M.F.1    Brouillet, E.2    Jenkins, B.3
  • 41
    • 0033373421 scopus 로고    scopus 로고
    • Bioenergetics in Huntington's disease
    • Grunewald T, Beal MF. Bioenergetics in Huntington's disease. Ann N Y Acad Sci 1999;893:203-213.
    • (1999) Ann N Y Acad Sci , vol.893 , pp. 203-213
    • Grunewald, T.1    Beal, M.F.2
  • 43
    • 0033938117 scopus 로고    scopus 로고
    • Life and death decisions: Regulation of apoptosis by proteolysis of signaling molecules
    • Utz PJ, Anderson P. Life and death decisions: regulation of apoptosis by proteolysis of signaling molecules. Cell Death Differ 2000;7:589-602.
    • (2000) Cell Death Differ , vol.7 , pp. 589-602
    • Utz, P.J.1    Anderson, P.2
  • 44
    • 0034051284 scopus 로고    scopus 로고
    • Mechanisms of neurodegenerative disorders: Part 2: control of cell death
    • Wolozin B, Behl C. Mechanisms of neurodegenerative disorders: part 2: control of cell death. Arch Neurol 2000;57:801-804.
    • (2000) Arch Neurol , vol.57 , pp. 801-804
    • Wolozin, B.1    Behl, C.2
  • 45
    • 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;41:160-165.
    • (1997) Ann Neurol , vol.41 , pp. 160-165
    • Koroshetz, W.J.1    Jenkins, B.G.2    Rosen, B.R.3    Beal, M.F.4
  • 46
    • 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;41:646-653.
    • (1997) Ann Neurol , vol.41 , pp. 646-653
    • Browne, S.E.1    Bowling, A.C.2    MacGarvey, U.3
  • 48
    • 0029034511 scopus 로고
    • Widespread expression of the Huntington's disease gene (IT15) protein product
    • Sharp AH, Loev SJ, Schilling G, et al. Widespread expression of the Huntington's disease gene (IT15) protein product. Neuron 1995;14:1065-1074.
    • (1995) Neuron , vol.14 , pp. 1065-1074
    • Sharp, A.H.1    Loev, S.J.2    Schilling, G.3
  • 49
    • 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;14:1075-1081.
    • (1995) Neuron , vol.14 , pp. 1075-1081
    • DiFiglia, M.1    Sapp, E.2    Chase, K.3
  • 50
    • 0028972448 scopus 로고
    • Polyglutamine expansion as a pathological epitope in Huntington's disease and four dominant cerebellar ataxias
    • Trottier Y, Lutz Y, Stevanin G, et al. Polyglutamine expansion as a pathological epitope in Huntington's disease and four dominant cerebellar ataxias. Nature 1995;378:403-406.
    • (1995) Nature , vol.378 , pp. 403-406
    • Trottier, Y.1    Lutz, Y.2    Stevanin, G.3
  • 51
    • 1842336432 scopus 로고    scopus 로고
    • Wild-type and mutant huntingtin localize to the golgi complex and to vesicles in the peripheral cytoplasm in fibroblasts of control and HD patients
    • Velier J, Schwarz C, Young C, et al. Wild-type and mutant huntingtin localize to the golgi complex and to vesicles in the peripheral cytoplasm in fibroblasts of control and HD patients. Soc Neurosci Abstracts 1996;22:226.
    • (1996) Soc Neurosci Abstracts , vol.22 , pp. 226
    • Velier, J.1    Schwarz, C.2    Young, C.3
  • 52
    • 0032103078 scopus 로고    scopus 로고
    • Huntingtin: A single bait hooks many species
    • Gusella JF, MacDonald ME. Huntingtin: a single bait hooks many species. Curr Opin Neurobiol 1998;8:425-430.
    • (1998) Curr Opin Neurobiol , vol.8 , pp. 425-430
    • Gusella, J.F.1    MacDonald, M.E.2
  • 53
    • 0029664992 scopus 로고    scopus 로고
    • Huntingtin and DRPLA proteins selectively interact with the enzyme GAPDH
    • Burke JR, Enghild JJ, Martin ME, et al. Huntingtin and DRPLA proteins selectively interact with the enzyme GAPDH. Nat Med 1996;347:350.
    • (1996) Nat Med , vol.347 , pp. 350
    • Burke, J.R.1    Enghild, J.J.2    Martin, M.E.3
  • 54
    • 0032833981 scopus 로고    scopus 로고
    • Aberrant interactions of transcriptional repressor proteins with the Huntington's disease gene product, huntingtin
    • Boutell JM, Thomas P, Neal JW, et al. Aberrant interactions of transcriptional repressor proteins with the Huntington's disease gene product, huntingtin. Hum Mol Genet 1999;8:1647-1655.
    • (1999) Hum Mol Genet , vol.8 , pp. 1647-1655
    • Boutell, J.M.1    Thomas, P.2    Neal, J.W.3
  • 55
    • 0027507667 scopus 로고
    • Human genetic diseases due to codon reiteration: Relationship to an evolutionary mechanism
    • Green H. Human genetic diseases due to codon reiteration: relationship to an evolutionary mechanism. Cell 1993;74:955-956.
    • (1993) Cell , vol.74 , pp. 955-956
    • Green, H.1
  • 56
    • 0030840917 scopus 로고    scopus 로고
    • cDNAs with long CAG trinucleotide repeats from human brain
    • Margolis RL, Abraham MA, Gatchell SB, et al. cDNAs with long CAG trinucleotide repeats from human brain. Hum Genet 1997;100:114-122.
    • (1997) Hum Genet , vol.100 , pp. 114-122
    • Margolis, R.L.1    Abraham, M.A.2    Gatchell, S.B.3
  • 57
    • 0027988041 scopus 로고
    • Polar zippers: Their role in human disease
    • London: Cambridge University Press
    • Perutz M. Polar zippers: their role in human disease. Protein science, 3rd ed. London: Cambridge University Press, 1994. pp. 1629-1637.
    • (1994) Protein Science, 3rd Ed. , pp. 1629-1637
    • Perutz, M.1
  • 58
    • 0029856046 scopus 로고    scopus 로고
    • Peptides containing glutamine repeats as substrates for transglutaminase-catalyzed cross-linking: Relevance to diseases of the nervous system
    • Kahlem P, Terre C, Green H, Djian P. Peptides containing glutamine repeats as substrates for transglutaminase-catalyzed cross-linking: relevance to diseases of the nervous system. Proc Natl Acad Sci USA 1996;93:14580-14585.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 14580-14585
    • Kahlem, P.1    Terre, C.2    Green, H.3    Djian, P.4
  • 59
    • 0032568502 scopus 로고    scopus 로고
    • Huntingtin aggregation monitored by dynamic light scattering
    • Georgalis Y, Starikov EB, Hollenbach B, et al. Huntingtin aggregation monitored by dynamic light scattering. Proc Natl Acad Sci USA 1998;95:6118-6121.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6118-6121
    • Georgalis, Y.1    Starikov, E.B.2    Hollenbach, B.3
  • 60
    • 0033551063 scopus 로고    scopus 로고
    • Self-assembly of polyglutamine-containing huntingtin fragments into amyloid-like fibrils: Implications for Huntington' s disease pathology
    • Scherzinger E, Sittler A, Schweiger K, et al. Self-assembly of polyglutamine-containing huntingtin fragments into amyloid-like fibrils: implications for Huntington' s disease pathology. Proc Natl Acad Sci USA 1999;96:4604-4609.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 4604-4609
    • Scherzinger, E.1    Sittler, A.2    Schweiger, K.3
  • 61
    • 0032847708 scopus 로고    scopus 로고
    • Nuclear targeting of mutant huntingtin increases toxicity
    • Peters MF, Nucifora Jr FC, Kushi J, et al. Nuclear targeting of mutant huntingtin increases toxicity. Mol Cell Neurosci 1999;14:121-128.
    • (1999) Mol Cell Neurosci , vol.14 , pp. 121-128
    • Peters, M.F.1    Nucifora Jr., F.C.2    Kushi, J.3
  • 62
    • 0031680014 scopus 로고    scopus 로고
    • A cellular model that recapitulates major pathogenic steps of Huntington's disease
    • Lunkes A, Mandel JL. A cellular model that recapitulates major pathogenic steps of Huntington's disease. Hum Mol Genet 1998;7:1355-1361.
    • (1998) Hum Mol Genet , vol.7 , pp. 1355-1361
    • Lunkes, A.1    Mandel, J.L.2
  • 63
    • 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
  • 64
    • 0033556160 scopus 로고    scopus 로고
    • Generation of neuronal intranuclear inclusions by polyglutamine-GFP: Analysis of inclusion clearance and toxicity as a function of polyglutamine length
    • Moulder KL, Onodera O, Burke JR, Strittmatter WJ, Johnson Jr EM. Generation of neuronal intranuclear inclusions by polyglutamine-GFP: analysis of inclusion clearance and toxicity as a function of polyglutamine length. J Neurosci 1999;19:705-715.
    • (1999) J Neurosci , vol.19 , pp. 705-715
    • Moulder, K.L.1    Onodera, O.2    Burke, J.R.3    Strittmatter, W.J.4    Johnson Jr., E.M.5
  • 65
    • 0032101287 scopus 로고    scopus 로고
    • The influence of huntingtin protein size on nuclear localization and cellular toxicity
    • Hackam AS, Singaraja R, Wellington CL, et al. The influence of huntingtin protein size on nuclear localization and cellular toxicity. J Cell Biol 1998;141:1097-1105.
    • (1998) J Cell Biol , vol.141 , pp. 1097-1105
    • Hackam, A.S.1    Singaraja, R.2    Wellington, C.L.3
  • 66
    • 17344363559 scopus 로고    scopus 로고
    • Length of huntingtin and its polyglutamine tract influences localization and frequency of intracellular aggregates
    • Martindale D, Hackam A, Wieczorek A, et al. Length of huntingtin and its polyglutamine tract influences localization and frequency of intracellular aggregates. Nat Genet 1998;18:150-154.
    • (1998) Nat Genet , vol.18 , pp. 150-154
    • Martindale, D.1    Hackam, A.2    Wieczorek, A.3
  • 67
    • 7144253143 scopus 로고    scopus 로고
    • Truncated N-terminal fragments of huntingtin with expanded glutamine repeats form nuclear and cytoplasmic aggregates in cell culture
    • Cooper JK, Schilling G, Peters MF, et al. Truncated N-terminal fragments of huntingtin with expanded glutamine repeats form nuclear and cytoplasmic aggregates in cell culture. Hum Mol Genet 1998;7:783-790.
    • (1998) Hum Mol Genet , vol.7 , pp. 783-790
    • Cooper, J.K.1    Schilling, G.2    Peters, M.F.3
  • 68
    • 0033081766 scopus 로고    scopus 로고
    • Mutant huntingtin expression in clonal striatal cells: Dissociation of inclusion formation and neuronal survival by caspase inhibition
    • Kim M, Lee HS, LaForet G, et al. Mutant huntingtin expression in clonal striatal cells: dissociation of inclusion formation and neuronal survival by caspase inhibition. J Neurosci 1999;19:964-973.
    • (1999) J Neurosci , vol.19 , pp. 964-973
    • Kim, M.1    Lee, H.S.2    LaForet, G.3
  • 69
    • 0032811511 scopus 로고    scopus 로고
    • Ultrastructural localization and progressive formation of neuropil aggregates in Huntington's disease transgenic mice
    • Li H, Li SH, Cheng AL, Mangiarini L, Bates GP, Li XJ. Ultrastructural localization and progressive formation of neuropil aggregates in Huntington's disease transgenic mice. Hum Mol Genet 1999;8:1227-1236.
    • (1999) Hum Mol Genet , vol.8 , pp. 1227-1236
    • Li, H.1    Li, S.H.2    Cheng, A.L.3    Mangiarini, L.4    Bates, G.P.5    Li, X.J.6
  • 70
    • 0032502715 scopus 로고    scopus 로고
    • Caspase cleavage of gene products associated with triplet expansion disorders generates truncated fragments containing the polyglutamine tract
    • Wellington CL, Ellerby LM, Hackam AS, et al. Caspase cleavage of gene products associated with triplet expansion disorders generates truncated fragments containing the polyglutamine tract. J Biol Chem 1998;273:9158-9167.
    • (1998) J Biol Chem , vol.273 , pp. 9158-9167
    • Wellington, C.L.1    Ellerby, L.M.2    Hackam, A.S.3
  • 71
    • 0033953015 scopus 로고    scopus 로고
    • Caspases and neurodegeneration: On the cutting edge of new therapeutic approaches
    • Wellington CL, Hayden MR. Caspases and neurodegeneration: on the cutting edge of new therapeutic approaches. Clin Genet 2000;57:1-10.
    • (2000) Clin Genet , vol.57 , pp. 1-10
    • Wellington, C.L.1    Hayden, M.R.2
  • 72
    • 0034733607 scopus 로고    scopus 로고
    • Inhibiting caspase cleavage of huntingtin reduces toxicity and aggregate formation in neuronal and non-neuronal cells
    • Wellington CL, Singaraja R, Ellerby L, et al. Inhibiting caspase cleavage of huntingtin reduces toxicity and aggregate formation in neuronal and non-neuronal cells. J Biol Chem 2000;275:19831-19838.
    • (2000) J Biol Chem , vol.275 , pp. 19831-19838
    • Wellington, C.L.1    Singaraja, R.2    Ellerby, L.3
  • 73
    • 0033103523 scopus 로고    scopus 로고
    • Caspase-8 is required for cell death induced by expanded polyglutamine repeats
    • Sanchez I, Xu CJ, Juo P, Kakizaka A, Blenis J, Yuan J. Caspase-8 is required for cell death induced by expanded polyglutamine repeats. Neuron 1999;22:623-633.
    • (1999) Neuron , vol.22 , pp. 623-633
    • Sanchez, I.1    Xu, C.J.2    Juo, P.3    Kakizaka, A.4    Blenis, J.5    Yuan, J.6
  • 74
    • 0033605746 scopus 로고    scopus 로고
    • Cleavage of atrophin-1 at caspase site aspartic acid 109 modulates cytotoxicity
    • Ellerby LM, Andrusiak RL, Wellington CL, et al. Cleavage of atrophin-1 at caspase site aspartic acid 109 modulates cytotoxicity. J Biol Chem 1999;274:8730-8736.
    • (1999) J Biol Chem , vol.274 , pp. 8730-8736
    • Ellerby, L.M.1    Andrusiak, R.L.2    Wellington, C.L.3
  • 75
    • 16044373842 scopus 로고    scopus 로고
    • Exon 1 of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice
    • Mangiarini L, Sathasivam S, Seller M, et al. Exon 1 of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice. Cell 1996;87:493-506.
    • (1996) Cell , vol.87 , pp. 493-506
    • Mangiarini, L.1    Sathasivam, S.2    Seller, M.3
  • 76
    • 0033560924 scopus 로고    scopus 로고
    • Characterization of progressive motor deficits in mice transgenic for the human Huntington's disease mutation
    • Carter RJ, Lione LA, Humby T, et al. Characterization of progressive motor deficits in mice transgenic for the human Huntington's disease mutation. J Neurosci 1999;19:3248-3257.
    • (1999) J Neurosci , vol.19 , pp. 3248-3257
    • Carter, R.J.1    Lione, L.A.2    Humby, T.3
  • 77
    • 0034234519 scopus 로고    scopus 로고
    • Abnormal synaptic plasticity and impaired spatial cognition in mice transgenic for exon 1 of the human Huntington's disease mutation
    • Murphy KP, Carter RJ, Lione LA, et al. Abnormal synaptic plasticity and impaired spatial cognition in mice transgenic for exon 1 of the human Huntington's disease mutation. J Neurosci 2000;20:5115-5123.
    • (2000) J Neurosci , vol.20 , pp. 5115-5123
    • Murphy, K.P.1    Carter, R.J.2    Lione, L.A.3
  • 78
    • 0033054555 scopus 로고    scopus 로고
    • Intranuclear inclusions and neuritic aggregates in transgenic mice expressing a mutant N-terminal fragment of huntingtin
    • Schilling G, Becher MW, Sharp AH, et al. Intranuclear inclusions and neuritic aggregates in transgenic mice expressing a mutant N-terminal fragment of huntingtin. Hum Mol Genet 1999;8:397-407.
    • (1999) Hum Mol Genet , vol.8 , pp. 397-407
    • Schilling, G.1    Becher, M.W.2    Sharp, A.H.3
  • 79
    • 17344367977 scopus 로고    scopus 로고
    • Behavioural abnormalities and selective neuronal loss in HD transgenic mice expressing mutated full-length HD cDNA
    • Reddy PH, Williams M, Charles V, et al. Behavioural abnormalities and selective neuronal loss in HD transgenic mice expressing mutated full-length HD cDNA. Nat Genet 1998;20:198-202.
    • (1998) Nat Genet , vol.20 , pp. 198-202
    • Reddy, P.H.1    Williams, M.2    Charles, V.3
  • 80
    • 0033136692 scopus 로고    scopus 로고
    • A YAC mouse model for Huntington's disease with full-length mutant huntingtin, cytoplasmic toxicity, and selective striatal neurodegeneration
    • Hodgson JG, Agopyan N, Gutekunst CA, Leavitt BR, LePiane F, Singaraja R. A YAC mouse model for Huntington's disease with full-length mutant huntingtin, cytoplasmic toxicity, and selective striatal neurodegeneration. Neuron 1999;23:181-192.
    • (1999) Neuron , vol.23 , pp. 181-192
    • Hodgson, J.G.1    Agopyan, N.2    Gutekunst, C.A.3    Leavitt, B.R.4    LePiane, F.5    Singaraja, R.6
  • 81
    • 0034163497 scopus 로고    scopus 로고
    • Long glutamine tracts cause nuclear localization of a novel form of huntingtin in medium spiny striatal neurons in HdhQ92 and HdhQ111 knock-in mice
    • Wheeler VC, White JK, Gutekunst CA, et al. Long glutamine tracts cause nuclear localization of a novel form of huntingtin in medium spiny striatal neurons in HdhQ92 and HdhQ111 knock-in mice. Hum Mol Genet 2000;9:503-513.
    • (2000) Hum Mol Genet , vol.9 , pp. 503-513
    • Wheeler, V.C.1    White, J.K.2    Gutekunst, C.A.3
  • 82
    • 0033848272 scopus 로고    scopus 로고
    • Expression of Huntingtin-associated protein-1 in neuronal cells implicates a role in neuritic growth
    • Li SH, Li H, Torre ER, Li XJ. Expression of Huntingtin-associated protein-1 in neuronal cells implicates a role in neuritic growth. Mol Cell Neurosci 2000;16:168-183.
    • (2000) Mol Cell Neurosci , vol.16 , pp. 168-183
    • Li, S.H.1    Li, H.2    Torre, E.R.3    Li, X.J.4
  • 83
    • 0034737299 scopus 로고    scopus 로고
    • Reversal of neuropathology and motor dysfunction in a conditional model of Huntington's disease
    • Yamamoto A, Lucas JJ, Hen R. Reversal of neuropathology and motor dysfunction in a conditional model of Huntington's disease. Cell 2000;101:57-66.
    • (2000) Cell , vol.101 , pp. 57-66
    • Yamamoto, A.1    Lucas, J.J.2    Hen, R.3
  • 84
    • 18544392423 scopus 로고    scopus 로고
    • Expanded polyglutamine protein forms nuclear inclusions and causes neural degeneration in Drosophila
    • Warrick JM, Paulson HL, Gray-Board GL, et al. Expanded polyglutamine protein forms nuclear inclusions and causes neural degeneration in Drosophila. Cell 1998;93:939-949.
    • (1998) Cell , vol.93 , pp. 939-949
    • Warrick, J.M.1    Paulson, H.L.2    Gray-Board, G.L.3
  • 85
    • 0032168160 scopus 로고    scopus 로고
    • Polyglutamine-expanded human huntingtin transgenes induce degeneration of Drosophila photoreceptor neurons
    • Jackson GR, Salecker I, Dong X, et al. Polyglutamine-expanded human huntingtin transgenes induce degeneration of Drosophila photoreceptor neurons. Neuron 1998;21:633-642.
    • (1998) Neuron , vol.21 , pp. 633-642
    • Jackson, G.R.1    Salecker, I.2    Dong, X.3
  • 86
    • 0034629073 scopus 로고    scopus 로고
    • Genetic suppression of polyglutamine toxicity in Drosophila
    • Kazemi-Esfarjani P, Benzer S. Genetic suppression of polyglutamine toxicity in Drosophila. Science 2000;287:1837-1840.
    • (2000) Science , vol.287 , pp. 1837-1840
    • Kazemi-Esfarjani, P.1    Benzer, S.2
  • 87
    • 0032727617 scopus 로고    scopus 로고
    • Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70
    • Warrick JM, Chan HY, Gray-Board GL, Chai Y, Paulson HL, Bonini NM. Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70. Nat Genet 1999;23:425-428.
    • (1999) Nat Genet , vol.23 , pp. 425-428
    • Warrick, J.M.1    Chan, H.Y.2    Gray-Board, G.L.3    Chai, Y.4    Paulson, H.L.5    Bonini, N.M.6
  • 88
    • 0033524413 scopus 로고    scopus 로고
    • Polyglutamine-mediated dysfunction and apoptotic death of a Caenorhabditis elegans sensory neuron
    • Faber PW, Alter JR, MacDonald ME, Hart AC. Polyglutamine-mediated dysfunction and apoptotic death of a Caenorhabditis elegans sensory neuron. Proc Natl Acad Sci USA 1999;96:179-184.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 179-184
    • Faber, P.W.1    Alter, J.R.2    MacDonald, M.E.3    Hart, A.C.4
  • 89
    • 0034705224 scopus 로고    scopus 로고
    • Polyglutamine aggregates alter protein folding homeostasis in Caenorhabditis elegans
    • Satyal SH, Schmidt E, Kitagawa K, et al. Polyglutamine aggregates alter protein folding homeostasis in Caenorhabditis elegans. Proc Natl Acad Sci USA 2000;97:5750-5755.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 5750-5755
    • Satyal, S.H.1    Schmidt, E.2    Kitagawa, K.3
  • 90
    • 0024556360 scopus 로고
    • A controlled clinical trial of baclofen as protective therapy in early Huntington's disease
    • Shoulson I, Odoroff C, Oakes D, et al. A controlled clinical trial of baclofen as protective therapy in early Huntington's disease. Ann Neurol 1989;25:252-259.
    • (1989) Ann Neurol , vol.25 , pp. 252-259
    • Shoulson, I.1    Odoroff, C.2    Oakes, D.3
  • 91
    • 9244263519 scopus 로고    scopus 로고
    • A controlled trial of remacemide hydrochloride in Huntington's disease
    • Kieburtz K, Feigin A, McDermott M, et al. A controlled trial of remacemide hydrochloride in Huntington's disease. Mov Disord 1996;11:273-277.
    • (1996) Mov Disord , vol.11 , pp. 273-277
    • Kieburtz, K.1    Feigin, A.2    McDermott, M.3
  • 92
    • 0029988363 scopus 로고    scopus 로고
    • Assessment of Coenzyme Q10 tolerability in Huntington's disease
    • Feigin A, Keiburtz K, Como P, et al. Assessment of Coenzyme Q10 tolerability in Huntington's disease. Mov Disord 1996;11:321-323.
    • (1996) Mov Disord , vol.11 , pp. 321-323
    • Feigin, A.1    Keiburtz, K.2    Como, P.3
  • 93
    • 9544255791 scopus 로고    scopus 로고
    • A controlled trial of idebenone in Huntington's disease
    • Ranen NG, Peyser CE, Coyle J, et al. A controlled trial of idebenone in Huntington's disease. Mov Disord 1996;11:549-554.
    • (1996) Mov Disord , vol.11 , pp. 549-554
    • Ranen, N.G.1    Peyser, C.E.2    Coyle, J.3
  • 94
    • 0028856571 scopus 로고
    • Trial of d-alpha-tocopherol in Huntington's disease
    • Peyser CE, Folstein MF, Chase GA, et al. Trial of d-alpha-tocopherol in Huntington's disease. Am J Psychiatry 1995;152:1771-1775.
    • (1995) Am J Psychiatry , vol.152 , pp. 1771-1775
    • Peyser, C.E.1    Folstein, M.F.2    Chase, G.A.3
  • 95
    • 0034612220 scopus 로고    scopus 로고
    • Inhibition of huntingtin fibrillogenesis by specific antibodies and small molecules: Implications for Huntington's disease therapy
    • Heiser V, Scherzinger E, Boeddrich A, et al. Inhibition of huntingtin fibrillogenesis by specific antibodies and small molecules: implications for Huntington's disease therapy. Proc Natl Acad Sci USA 2000;97:6739-6744.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6739-6744
    • Heiser, V.1    Scherzinger, E.2    Boeddrich, A.3
  • 97
    • 0033587128 scopus 로고    scopus 로고
    • Inhibition of caspase-1 slows disease progression in a mouse model of Huntington's disease
    • Ona VO, Li M, Vonsattel JP, Andrews LJ, et al. Inhibition of caspase-1 slows disease progression in a mouse model of Huntington's disease. Nature 1999;399:263-267.
    • (1999) Nature , vol.399 , pp. 263-267
    • Ona, V.O.1    Li, M.2    Vonsattel, J.P.3    Andrews, L.J.4
  • 98
    • 0034660457 scopus 로고    scopus 로고
    • Neuroprotective effects of creatine in a transgenic mouse model of Huntington's disease
    • Ferrante RJ, Andreassen OA, Jenkins BG, et al. Neuroprotective effects of creatine in a transgenic mouse model of Huntington's disease. J Neurosci 2000;20:4389-4397.
    • (2000) J Neurosci , vol.20 , pp. 4389-4397
    • Ferrante, R.J.1    Andreassen, O.A.2    Jenkins, B.G.3
  • 99
    • 0033912716 scopus 로고    scopus 로고
    • Minocycline inhibits caspase-1 and caspase-3 expression and delays mortality in a transgenic mouse model of Huntington disease
    • Chen M, Ona VO, Li M, et al. Minocycline inhibits caspase-1 and caspase-3 expression and delays mortality in a transgenic mouse model of Huntington disease. Nat Med 2000;6:797-801.
    • (2000) Nat Med , vol.6 , pp. 797-801
    • Chen, M.1    Ona, V.O.2    Li, M.3


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