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Volumn 100, Issue , 2011, Pages 25-81

Molecular biology of Huntington's disease

Author keywords

[No Author keywords available]

Indexed keywords

NERVE PROTEIN;

EID: 79954522923     PISSN: 00729752     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-444-52014-2.00003-3     Document Type: Book
Times cited : (19)

References (496)
  • 1
    • 56549089781 scopus 로고    scopus 로고
    • Mitochondrial DNA damage is a hallmark of chemically induced and the R6/2 transgenic model of Huntington's disease
    • Acevedo-Torres K., Berrios L., Rosario N., et al. Mitochondrial DNA damage is a hallmark of chemically induced and the R6/2 transgenic model of Huntington's disease. DNA Repair (Amst) 2009, 8:126-136.
    • (2009) DNA Repair (Amst) , vol.8 , pp. 126-136
    • Acevedo-Torres, K.1    Berrios, L.2    Rosario, N.3
  • 2
    • 0036934648 scopus 로고    scopus 로고
    • Calpain activation in neurodegenerative diseases: confocal immunofluorescence study with antibodies specifically recognizing the active form of calpain 2
    • Adamec E., Mohan P., Vonsattel J.P., et al. Calpain activation in neurodegenerative diseases: confocal immunofluorescence study with antibodies specifically recognizing the active form of calpain 2. Acta Neuropathol (Berl) 2002, 104:92-104.
    • (2002) Acta Neuropathol (Berl) , vol.104 , pp. 92-104
    • Adamec, E.1    Mohan, P.2    Vonsattel, J.P.3
  • 3
    • 0036626868 scopus 로고    scopus 로고
    • Homozygosity in Huntington's disease: new ethical dilemma caused by molecular diagnosis
    • Alonso M.E., Yescas P., Rasmussen A., et al. Homozygosity in Huntington's disease: new ethical dilemma caused by molecular diagnosis. Clin Genet 2002, 61:437-442.
    • (2002) Clin Genet , vol.61 , pp. 437-442
    • Alonso, M.E.1    Yescas, P.2    Rasmussen, A.3
  • 4
    • 0027018939 scopus 로고
    • A novel G protein-coupled receptor kinase gene cloned from 4p16.3
    • Ambrose C., James M., Barnes G., et al. A novel G protein-coupled receptor kinase gene cloned from 4p16.3. Hum Mol Genet 1992, 1:697-703.
    • (1992) Hum Mol Genet , vol.1 , pp. 697-703
    • Ambrose, C.1    James, M.2    Barnes, G.3
  • 5
    • 0028260436 scopus 로고
    • Structure and expression of the Huntington's disease gene: evidence against simple inactivation due to an expanded CAG repeat
    • Ambrose C.M., Duyao M.P., 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, 20:27-38.
    • (1994) Somat Cell Mol Genet , vol.20 , pp. 27-38
    • Ambrose, C.M.1    Duyao, M.P.2    Barnes, G.3
  • 6
    • 27144523294 scopus 로고    scopus 로고
    • Inhibition of metabotropic glutamate receptor signaling by the huntingtin-binding protein optineurin
    • Anborgh P.H., Godin C., Pampillo M., et al. Inhibition of metabotropic glutamate receptor signaling by the huntingtin-binding protein optineurin. J Biol Chem 2005, 280:34840-34848.
    • (2005) J Biol Chem , vol.280 , pp. 34840-34848
    • Anborgh, P.H.1    Godin, C.2    Pampillo, M.3
  • 7
    • 0029900762 scopus 로고    scopus 로고
    • Ciliary neurotrophic factor protects striatal output neurons in an animal model of Huntington disease
    • Anderson K.D., Panayotatos N., Corcoran T.L., et al. Ciliary neurotrophic factor protects striatal output neurons in an animal model of Huntington disease. Proc Natl Acad Sci USA 1996, 93:7346-7351.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 7346-7351
    • Anderson, K.D.1    Panayotatos, N.2    Corcoran, T.L.3
  • 8
    • 0029392854 scopus 로고
    • HEAT repeats in the Huntington's disease protein
    • Andrade M.A., Bork P. HEAT repeats in the Huntington's disease protein. Nat Genet 1995, 11:115-116.
    • (1995) Nat Genet , vol.11 , pp. 115-116
    • Andrade, M.A.1    Bork, P.2
  • 9
    • 0035946941 scopus 로고    scopus 로고
    • Comparison of ARM and HEAT protein repeats
    • Andrade M.A., Petosa C., O'Donoghue S.I., et al. Comparison of ARM and HEAT protein repeats. J Mol Biol 2001, 309:1-18.
    • (2001) J Mol Biol , vol.309 , pp. 1-18
    • Andrade, M.A.1    Petosa, C.2    O'Donoghue, S.I.3
  • 10
    • 0034743672 scopus 로고    scopus 로고
    • Creatine increase survival and delays motor symptoms in a transgenic animal model of Huntington's disease
    • Andreassen O.A., Dedeoglu A., Ferrante R.J., et al. Creatine increase survival and delays motor symptoms in a transgenic animal model of Huntington's disease. Neurobiol Dis 2001, 8:479-491.
    • (2001) Neurobiol Dis , vol.8 , pp. 479-491
    • Andreassen, O.A.1    Dedeoglu, A.2    Ferrante, R.J.3
  • 11
    • 34247120606 scopus 로고    scopus 로고
    • The relationship between CAG repeat length and age of onset differs for Huntington's disease patients with juvenile onset or adult onset
    • Andresen J.M., Gayan J., Djousse L., et al. The relationship between CAG repeat length and age of onset differs for Huntington's disease patients with juvenile onset or adult onset. Ann Hum Genet 2007, 71:295-301.
    • (2007) Ann Hum Genet , vol.71 , pp. 295-301
    • Andresen, J.M.1    Gayan, J.2    Djousse, L.3
  • 12
    • 1542300922 scopus 로고    scopus 로고
    • Hyperhomocysteinaemia in treated patients with Huntington's disease homocysteine in HD
    • Andrich J., Saft C., Arz A., et al. Hyperhomocysteinaemia in treated patients with Huntington's disease homocysteine in HD. Mov Disord 2004, 19:226-228.
    • (2004) Mov Disord , vol.19 , pp. 226-228
    • Andrich, J.1    Saft, C.2    Arz, A.3
  • 13
    • 48649083048 scopus 로고    scopus 로고
    • Huntington's disease as caused by 34 CAG repeats
    • Andrich J., Arning L., Wieczorek S., et al. Huntington's disease as caused by 34 CAG repeats. Mov Disord 2008, 23:879-881.
    • (2008) Mov Disord , vol.23 , pp. 879-881
    • Andrich, J.1    Arning, L.2    Wieczorek, S.3
  • 14
    • 34447130222 scopus 로고    scopus 로고
    • Phosphorylation of huntingtin by cyclin-dependent kinase 5 is induced by DNA damage and regulates wild-type and mutant huntingtin toxicity in neurons
    • Anne S.L., Saudou F., Humbert S. Phosphorylation of huntingtin by cyclin-dependent kinase 5 is induced by DNA damage and regulates wild-type and mutant huntingtin toxicity in neurons. J Neurosci 2007, 27:7318-7328.
    • (2007) J Neurosci , vol.27 , pp. 7318-7328
    • Anne, S.L.1    Saudou, F.2    Humbert, S.3
  • 15
    • 0037947662 scopus 로고    scopus 로고
    • A cell-based assay for aggregation inhibitors as therapeutics of polyglutamine-repeat disease and validation in Drosophila
    • Apostol B.L., Kazantsev A., Raffioni S., et al. A cell-based assay for aggregation inhibitors as therapeutics of polyglutamine-repeat disease and validation in Drosophila. Proc Natl Acad Sci U S A 2003, 100:5950-5955.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 5950-5955
    • Apostol, B.L.1    Kazantsev, A.2    Raffioni, S.3
  • 16
    • 42449161835 scopus 로고    scopus 로고
    • ASK1 and MAP2K6 as modifiers of age at onset in Huntington's disease
    • Arning L., Monte D., Hansen W., et al. ASK1 and MAP2K6 as modifiers of age at onset in Huntington's disease. J Mol Med 2008, 86:485-490.
    • (2008) J Mol Med , vol.86 , pp. 485-490
    • Arning, L.1    Monte, D.2    Hansen, W.3
  • 17
    • 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, 15:1193-1201.
    • (1995) Neuron , vol.15 , pp. 1193-1201
    • Aronin, N.1    Chase, K.2    Young, C.3
  • 18
    • 35448994487 scopus 로고    scopus 로고
    • Huntingtin has a membrane association signal that can modulate huntingtin aggregation, nuclear entry and toxicity
    • Atwal R.S., Xia J., Pinchev D., et al. Huntingtin has a membrane association signal that can modulate huntingtin aggregation, nuclear entry and toxicity. Hum Mol Genet 2007, 16:2600-2615.
    • (2007) Hum Mol Genet , vol.16 , pp. 2600-2615
    • Atwal, R.S.1    Xia, J.2    Pinchev, D.3
  • 19
    • 0035888618 scopus 로고    scopus 로고
    • The HD mutation causes progressive lethal neurological disease in mice expressing reduced levels of huntingtin
    • Auerbach W., Hurlbert M.S., Hilditch-Maguire P., et al. The HD mutation causes progressive lethal neurological disease in mice expressing reduced levels of huntingtin. Hum Mol Genet 2001, 10:2515-2523.
    • (2001) Hum Mol Genet , vol.10 , pp. 2515-2523
    • Auerbach, W.1    Hurlbert, M.S.2    Hilditch-Maguire, P.3
  • 20
    • 57449113230 scopus 로고    scopus 로고
    • Msx1 expression regulation by its own antisense RNA: consequence on tooth development and bone regeneration
    • Babajko S., Petit S., Fernandes I., et al. Msx1 expression regulation by its own antisense RNA: consequence on tooth development and bone regeneration. Cells Tissues Organs 2009, 189:115-121.
    • (2009) Cells Tissues Organs , vol.189 , pp. 115-121
    • Babajko, S.1    Petit, S.2    Fernandes, I.3
  • 21
    • 21544450545 scopus 로고    scopus 로고
    • P53 mediates cellular dysfunction and behavioral abnormalities in Huntington's disease
    • Bae B.I., 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
  • 22
    • 0028017992 scopus 로고
    • Identification and characterization of the gene causing type 1 spinocerebellar ataxia
    • Banfi S., Servadio A., Chung M.Y., et al. Identification and characterization of the gene causing type 1 spinocerebellar ataxia. Nat Genet 1994, 7:513-520.
    • (1994) Nat Genet , vol.7 , pp. 513-520
    • Banfi, S.1    Servadio, A.2    Chung, M.Y.3
  • 23
    • 0030001072 scopus 로고    scopus 로고
    • Expansion of polyglutamine repeat in huntingtin leads to abnormal protein interactions involving calmodulin
    • Bao J., Sharp A.H., Wagster M.V., et al. Expansion of polyglutamine repeat in huntingtin leads to abnormal protein interactions involving calmodulin. Proc Natl Acad Sci U S A 1996, 93:5037-5042.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 5037-5042
    • Bao, J.1    Sharp, A.H.2    Wagster, M.V.3
  • 24
    • 2442506955 scopus 로고    scopus 로고
    • Early striatal dendrite deficits followed by neuron loss with advanced age in the absence of anterograde cortical brain-derived neurotrophic factor
    • Baquet Z.C., Gorski J.A., Jones K.R. Early striatal dendrite deficits followed by neuron loss with advanced age in the absence of anterograde cortical brain-derived neurotrophic factor. J Neurosci 2004, 24:4250-4258.
    • (2004) J Neurosci , vol.24 , pp. 4250-4258
    • Baquet, Z.C.1    Gorski, J.A.2    Jones, K.R.3
  • 26
    • 33644830913 scopus 로고    scopus 로고
    • Differential contributions of Caenorhabditis elegans histone deacetylases to huntingtin polyglutamine toxicity
    • Bates E.A., Victor M., Jones A.K., et al. Differential contributions of Caenorhabditis elegans histone deacetylases to huntingtin polyglutamine toxicity. J Neurosci 2006, 26:2830-2838.
    • (2006) J Neurosci , vol.26 , pp. 2830-2838
    • Bates, E.A.1    Victor, M.2    Jones, A.K.3
  • 27
    • 0025275405 scopus 로고
    • A yeast artificial chromosome telomere clone spanning a possible location of the Huntington disease gene
    • Bates G.P., MacDonald M.E., Baxendale S., et al. A yeast artificial chromosome telomere clone spanning a possible location of the Huntington disease gene. Am J Hum Genet 1990, 46:762-775.
    • (1990) Am J Hum Genet , vol.46 , pp. 762-775
    • Bates, G.P.1    MacDonald, M.E.2    Baxendale, S.3
  • 28
    • 0029018046 scopus 로고
    • Comparative sequence analysis of the human and pufferfish Huntington's disease genes
    • Baxendale S., Abdulla S., Elgar G., et al. Comparative sequence analysis of the human and pufferfish Huntington's disease genes. Nat Genet 1995, 10:67-75.
    • (1995) Nat Genet , vol.10 , pp. 67-75
    • Baxendale, S.1    Abdulla, S.2    Elgar, G.3
  • 29
    • 0022446150 scopus 로고
    • Replication of the neurochemical characteristics of Huntington's disease by quinolinic acid
    • Beal M.F., Kowall N.W., Ellison D.W., et al. 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.W.3
  • 30
    • 0027204154 scopus 로고
    • Age-dependent striatal excitotoxic lesions produced by the endogenous mitochondrial inhibitor malonate
    • Beal M.F., Brouillet E., Jenkins B., et al. Age-dependent striatal excitotoxic lesions produced by the endogenous mitochondrial inhibitor malonate. J Neurochem 1993, 61:1147-1150.
    • (1993) J Neurochem , vol.61 , pp. 1147-1150
    • Beal, M.F.1    Brouillet, E.2    Jenkins, B.3
  • 31
    • 0027433553 scopus 로고
    • Neurochemical and histologic characterization of striatal excitotoxic lesions produced by the mitochondrial toxin 3-nitropropionic acid
    • Beal M.F., Brouillet E., Jenkins B.G., 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.G.3
  • 32
    • 4544335687 scopus 로고    scopus 로고
    • The N-methyl-d-aspartate antagonist memantine retards progression of Huntington's disease
    • Beister A., Kraus P., Kuhn W., et al. The N-methyl-d-aspartate antagonist memantine retards progression of Huntington's disease. J Neural Transm Suppl 2004, 117-122.
    • (2004) J Neural Transm Suppl , pp. 117-122
    • Beister, A.1    Kraus, P.2    Kuhn, W.3
  • 33
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence N.F., Sampat R.M., Kopito R.R. Impairment of the ubiquitin-proteasome system by protein aggregation. Science 2001, 292:1552-1555.
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 34
    • 27544477225 scopus 로고    scopus 로고
    • Contribution of nuclear and extranuclear polyQ to neurological phenotypes in mouse models of Huntington's disease
    • Benn C.L., Landles C., Li H., et al. Contribution of nuclear and extranuclear polyQ to neurological phenotypes in mouse models of Huntington's disease. Hum Mol Genet 2005, 14:3065-3078.
    • (2005) Hum Mol Genet , vol.14 , pp. 3065-3078
    • Benn, C.L.1    Landles, C.2    Li, H.3
  • 35
    • 54849422301 scopus 로고    scopus 로고
    • Huntingtin modulates transcription, occupies gene promoters in vivo, and binds directly to DNA in a polyglutamine-dependent manner
    • Benn C.L., Sun T., Sadri-Vakili G., et al. Huntingtin modulates transcription, occupies gene promoters in vivo, and binds directly to DNA in a polyglutamine-dependent manner. J Neurosci 2008, 28:10720-10733.
    • (2008) J Neurosci , vol.28 , pp. 10720-10733
    • Benn, C.L.1    Sun, T.2    Sadri-Vakili, G.3
  • 36
    • 13244258435 scopus 로고    scopus 로고
    • Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation
    • Bennett E.J., Bence N.F., Jayakumar R., et al. Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation. Mol Cell 2005, 17:351-365.
    • (2005) Mol Cell , vol.17 , pp. 351-365
    • Bennett, E.J.1    Bence, N.F.2    Jayakumar, R.3
  • 37
    • 34547807613 scopus 로고    scopus 로고
    • Global changes to the ubiquitin system in Huntington's disease
    • Bennett E.J., Shaler T.A., Woodman B., et al. Global changes to the ubiquitin system in Huntington's disease. Nature 2007, 448:704-708.
    • (2007) Nature , vol.448 , pp. 704-708
    • Bennett, E.J.1    Shaler, T.A.2    Woodman, B.3
  • 38
    • 0029085920 scopus 로고
    • The identification of a functional nuclear localization signal in the Huntington disease protein
    • Bessert D.A., Gutridge K.L., Dunbar J.C., et al. The identification of a functional nuclear localization signal in the Huntington disease protein. Brain Res Mol Brain Res 1995, 33:165-173.
    • (1995) Brain Res Mol Brain Res , vol.33 , pp. 165-173
    • Bessert, D.A.1    Gutridge, K.L.2    Dunbar, J.C.3
  • 39
    • 29644433718 scopus 로고    scopus 로고
    • Proteasome impairment does not contribute to pathogenesis in R6/2 Huntington's disease mice: exclusion of proteasome activator REGgamma as a therapeutic target
    • Bett J.S., Goellner G.M., Woodman B., et al. Proteasome impairment does not contribute to pathogenesis in R6/2 Huntington's disease mice: exclusion of proteasome activator REGgamma as a therapeutic target. Hum Mol Genet 2006, 15:33-44.
    • (2006) Hum Mol Genet , vol.15 , pp. 33-44
    • Bett, J.S.1    Goellner, G.M.2    Woodman, B.3
  • 40
    • 9444286388 scopus 로고    scopus 로고
    • Expression of normal and mutant huntingtin in the developing brain
    • Bhide P.G., Day M., Sapp E., et al. Expression of normal and mutant huntingtin in the developing brain. J Neurosci 1996, 16:5523-5535.
    • (1996) J Neurosci , vol.16 , pp. 5523-5535
    • Bhide, P.G.1    Day, M.2    Sapp, E.3
  • 41
    • 0037775906 scopus 로고    scopus 로고
    • Calpain is a major cell death effector in selective striatal degeneration induced in vivo by 3-nitropropionate: implications for Huntington's disease
    • Bizat N., Hermel J.M., Boyer F., et al. Calpain is a major cell death effector in selective striatal degeneration induced in vivo by 3-nitropropionate: implications for Huntington's disease. J Neurosci 2003, 23:5020-5030.
    • (2003) J Neurosci , vol.23 , pp. 5020-5030
    • Bizat, N.1    Hermel, J.M.2    Boyer, F.3
  • 42
    • 58049217323 scopus 로고    scopus 로고
    • Unexpected link between anaphase promoting complex and the toxicity of expanded polyglutamines expressed in yeast
    • Bocharova N.A., Sokolov S.S., Knorre D.A., et al. Unexpected link between anaphase promoting complex and the toxicity of expanded polyglutamines expressed in yeast. Cell Cycle 2008, 7:3943-3946.
    • (2008) Cell Cycle , vol.7 , pp. 3943-3946
    • Bocharova, N.A.1    Sokolov, S.S.2    Knorre, D.A.3
  • 43
    • 61349125667 scopus 로고    scopus 로고
    • Protein aggregation and neurodegeneration: clues from a Yeast model of Huntington's disease
    • Bocharova N., Chave-Cox R., Sokolov S., et al. Protein aggregation and neurodegeneration: clues from a Yeast model of Huntington's disease. Biochemistry (Mosc) 2009, 74:231-234.
    • (2009) Biochemistry (Mosc) , vol.74 , pp. 231-234
    • Bocharova, N.1    Chave-Cox, R.2    Sokolov, S.3
  • 44
    • 0028900665 scopus 로고
    • Systemic 3-nitropropionic acid: behavioral deficits and striatal damage in adult rats
    • Borlongan C.V., Koutouzis T.K., Randall T.S., et al. Systemic 3-nitropropionic acid: behavioral deficits and striatal damage in adult rats. Brain Res Bull 1995, 36:549-556.
    • (1995) Brain Res Bull , vol.36 , pp. 549-556
    • Borlongan, C.V.1    Koutouzis, T.K.2    Randall, T.S.3
  • 45
    • 0031909798 scopus 로고    scopus 로고
    • Huntingtin interacts with cystathionine beta-synthase
    • Boutell J.M., Wood J.D., Harper P.S., et al. Huntingtin interacts with cystathionine beta-synthase. Hum Mol Genet 1998, 7:371-378.
    • (1998) Hum Mol Genet , vol.7 , pp. 371-378
    • Boutell, J.M.1    Wood, J.D.2    Harper, P.S.3
  • 46
    • 0032833981 scopus 로고    scopus 로고
    • Aberrant interactions of transcriptional repressor proteins with the Huntington's disease gene product, huntingtin
    • Boutell J.M., Thomas P., Neal J.W., 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
  • 47
    • 0029034503 scopus 로고
    • Expansion of a (CAG)n repeat region in a sporadic case of HD
    • Bozza A., Malagu S., Calzolari E., et al. Expansion of a (CAG)n repeat region in a sporadic case of HD. Acta Neurol Scand 1995, 92:132-134.
    • (1995) Acta Neurol Scand , vol.92 , pp. 132-134
    • Bozza, A.1    Malagu, S.2    Calzolari, E.3
  • 48
    • 0021883670 scopus 로고
    • Regional mitochondrial respiratory activity in Huntington's disease brain
    • Brennan W.A., Bird E.D., Aprille J.R. Regional mitochondrial respiratory activity in Huntington's disease brain. J Neurochem 1985, 44:1948-1950.
    • (1985) J Neurochem , vol.44 , pp. 1948-1950
    • Brennan, W.A.1    Bird, E.D.2    Aprille, J.R.3
  • 49
    • 0026566108 scopus 로고
    • Molecular basis of myotonic dystrophy: expansion of a trinucleotide (CTG) repeat at the 3' end of a transcript encoding a protein kinase family member
    • Brook J.D., McCurrach M.E., Harley H.G., et al. Molecular basis of myotonic dystrophy: expansion of a trinucleotide (CTG) repeat at the 3' end of a transcript encoding a protein kinase family member. Cell 1992, 68:799-808.
    • (1992) Cell , vol.68 , pp. 799-808
    • Brook, J.D.1    McCurrach, M.E.2    Harley, H.G.3
  • 50
    • 0027448161 scopus 로고
    • Age-dependent vulnerability of the striatum to the mitochondrial toxin 3-nitropropionic acid
    • Brouillet E., Jenkins B.G., Hyman B.T., et al. Age-dependent vulnerability of the striatum to the mitochondrial toxin 3-nitropropionic acid. J Neurochem 1993, 60:356-359.
    • (1993) J Neurochem , vol.60 , pp. 356-359
    • Brouillet, E.1    Jenkins, B.G.2    Hyman, B.T.3
  • 51
    • 33947675275 scopus 로고    scopus 로고
    • Oxidative damage in Huntington's disease pathogenesis
    • Browne S.E., Beal M.F. Oxidative damage in Huntington's disease pathogenesis. Antioxid Redox Signal 2006, 8:2061-2073.
    • (2006) Antioxid Redox Signal , vol.8 , pp. 2061-2073
    • Browne, S.E.1    Beal, M.F.2
  • 52
    • 0030919567 scopus 로고    scopus 로고
    • Oxidative damage and metabolic dysfunction in Huntington's disease: selective vulnerability of the basal ganglia
    • Browne S.E., Bowling A.C., 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
  • 53
    • 53349129398 scopus 로고    scopus 로고
    • Neocortical expression of mutant huntingtin is not required for alterations in striatal gene expression or motor dysfunction in a transgenic mouse
    • Brown T.B., Bogush A.I., Ehrlich M.E. Neocortical expression of mutant huntingtin is not required for alterations in striatal gene expression or motor dysfunction in a transgenic mouse. Hum Mol Genet 2008, 17:3095-3104.
    • (2008) Hum Mol Genet , vol.17 , pp. 3095-3104
    • Brown, T.B.1    Bogush, A.I.2    Ehrlich, M.E.3
  • 54
    • 0025860287 scopus 로고
    • Exon amplification: a strategy to isolate mammalian genes based on RNA splicing
    • Buckler A.J., Chang D.D., Graw S.L., et al. Exon amplification: a strategy to isolate mammalian genes based on RNA splicing. Proc Natl Acad Sci U S A 1991, 88:4005-4009.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 4005-4009
    • Buckler, A.J.1    Chang, D.D.2    Graw, S.L.3
  • 55
    • 0029664992 scopus 로고    scopus 로고
    • Huntingtin and DRPLA proteins selectively interact with the enzyme GAPDH
    • Burke J.R., Enghild J.J., Martin M.E., et al. Huntingtin and DRPLA proteins selectively interact with the enzyme GAPDH. Nat Med 1996, 2:347-350.
    • (1996) Nat Med , vol.2 , pp. 347-350
    • Burke, J.R.1    Enghild, J.J.2    Martin, M.E.3
  • 56
    • 0021917344 scopus 로고
    • Distribution of phosphate-activated glutaminase, succinic dehydrogenase, pyruvate dehydrogenase and gamma-glutamyl transpeptidase in post-mortem brain from Huntington's disease and agonal cases
    • Butterworth J., Yates C.M., Reynolds G.P. Distribution of phosphate-activated glutaminase, succinic dehydrogenase, pyruvate dehydrogenase and gamma-glutamyl transpeptidase in post-mortem brain from Huntington's disease and agonal cases. J Neurol Sci 1985, 67:161-171.
    • (1985) J Neurol Sci , vol.67 , pp. 161-171
    • Butterworth, J.1    Yates, C.M.2    Reynolds, G.P.3
  • 57
    • 0142027842 scopus 로고    scopus 로고
    • Mutations in yeast replication proteins that increase CAG/CTG expansions also increase repeat fragility
    • Callahan J.L., Andrews K.J., Zakian V.A., et al. Mutations in yeast replication proteins that increase CAG/CTG expansions also increase repeat fragility. Mol Cell Biol 2003, 23:7849-7860.
    • (2003) Mol Cell Biol , vol.23 , pp. 7849-7860
    • Callahan, J.L.1    Andrews, K.J.2    Zakian, V.A.3
  • 58
    • 0032527592 scopus 로고    scopus 로고
    • Generation and characterization of embryonic striatal conditionally immortalized ST14A cells
    • Cattaneo E., Conti L. Generation and characterization of embryonic striatal conditionally immortalized ST14A cells. J Neurosci Res 1998, 53:223-234.
    • (1998) J Neurosci Res , vol.53 , pp. 223-234
    • Cattaneo, E.1    Conti, L.2
  • 59
    • 35348877164 scopus 로고    scopus 로고
    • Transcriptional signatures in Huntington's disease
    • Cha J.H. Transcriptional signatures in Huntington's disease. Prog Neurobiol 2007, 83:228-248.
    • (2007) Prog Neurobiol , vol.83 , pp. 228-248
    • Cha, J.H.1
  • 60
    • 0032568517 scopus 로고    scopus 로고
    • Altered brain neurotransmitter receptors in transgenic mice expressing a portion of an abnormal human huntington disease gene
    • Cha J.H., Kosinski C.M., Kerner J.A., 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, 95:6480-6485.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 6480-6485
    • Cha, J.H.1    Kosinski, C.M.2    Kerner, J.A.3
  • 62
    • 27644525713 scopus 로고    scopus 로고
    • Antisense transcription and heterochromatin at the DM1 CTG repeats are constrained by CTCF
    • Cho D.H., Thienes C.P., Mahoney S.E., et al. Antisense transcription and heterochromatin at the DM1 CTG repeats are constrained by CTCF. Mol Cell 2005, 20:483-489.
    • (2005) Mol Cell , vol.20 , pp. 483-489
    • Cho, D.H.1    Thienes, C.P.2    Mahoney, S.E.3
  • 63
    • 0034990512 scopus 로고    scopus 로고
    • Tissue transglutaminase selectively modifies proteins associated with truncated mutant huntingtin in intact cells
    • Chun W., Lesort M., Tucholski J., et al. Tissue transglutaminase selectively modifies proteins associated with truncated mutant huntingtin in intact cells. Neurobiol Dis 2001, 8:391-404.
    • (2001) Neurobiol Dis , vol.8 , pp. 391-404
    • Chun, W.1    Lesort, M.2    Tucholski, J.3
  • 64
    • 0030981183 scopus 로고    scopus 로고
    • Analysis of the 5' upstream sequence of the Huntington's disease (HD) gene shows six new rare alleles which are unrelated to the age at onset of HD
    • Coles R., Leggo J., Rubinsztein D.C. Analysis of the 5' upstream sequence of the Huntington's disease (HD) gene shows six new rare alleles which are unrelated to the age at onset of HD. J Med Genet 1997, 34:371-374.
    • (1997) J Med Genet , vol.34 , pp. 371-374
    • Coles, R.1    Leggo, J.2    Rubinsztein, D.C.3
  • 65
    • 0031897917 scopus 로고    scopus 로고
    • Functional analysis of the Huntington's disease (HD) gene promoter
    • Coles R., Caswell R., Rubinsztein D.C. Functional analysis of the Huntington's disease (HD) gene promoter. Hum Mol Genet 1998, 7:791-800.
    • (1998) Hum Mol Genet , vol.7 , pp. 791-800
    • Coles, R.1    Caswell, R.2    Rubinsztein, D.C.3
  • 66
    • 0034727404 scopus 로고    scopus 로고
    • 12-O-tetradecanoyl-phorbol-13-acetate down-regulates the Huntingtin promoter at Sp1 sites
    • Coles R., Birdsall M., Wyttenbach A., et al. 12-O-tetradecanoyl-phorbol-13-acetate down-regulates the Huntingtin promoter at Sp1 sites. Neuroreport 2000, 11:3157-3161.
    • (2000) Neuroreport , vol.11 , pp. 3157-3161
    • Coles, R.1    Birdsall, M.2    Wyttenbach, A.3
  • 67
    • 49149112606 scopus 로고    scopus 로고
    • Huntingtin phosphorylation acts as a molecular switch for anterograde/retrograde transport in neurons
    • Colin E., Zala D., Liot G., et al. Huntingtin phosphorylation acts as a molecular switch for anterograde/retrograde transport in neurons. Embo J 2008, 27:2124-2134.
    • (2008) Embo J , vol.27 , pp. 2124-2134
    • Colin, E.1    Zala, D.2    Liot, G.3
  • 68
    • 7144253143 scopus 로고    scopus 로고
    • Truncated N-terminal fragments of huntingtin with expanded glutamine repeats form nuclear and cytoplasmic aggregates in cell culture
    • Cooper J.K., Schilling G., Peters M.F., 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
  • 69
    • 13944275615 scopus 로고    scopus 로고
    • Polyglutamine expansion of huntingtin impairs its nuclear export
    • Cornett J., Cao F., Wang C.E., et al. Polyglutamine expansion of huntingtin impairs its nuclear export. Nat Genet 2005, 37:198-204.
    • (2005) Nat Genet , vol.37 , pp. 198-204
    • Cornett, J.1    Cao, F.2    Wang, C.E.3
  • 70
    • 16944364511 scopus 로고    scopus 로고
    • Cloning of the SCA7 gene reveals a highly unstable CAG repeat expansion
    • David G., Abbas N., Stevanin G., et al. Cloning of the SCA7 gene reveals a highly unstable CAG repeat expansion. Nat Genet 1997, 17:65-70.
    • (1997) Nat Genet , vol.17 , pp. 65-70
    • David, G.1    Abbas, N.2    Stevanin, G.3
  • 71
    • 18544410106 scopus 로고    scopus 로고
    • Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation
    • Davies S.W., Turmaine M., Cozens B.A., et al. Formation of neuronal intranuclear inclusions 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
  • 72
    • 0036580677 scopus 로고    scopus 로고
    • Lentiviral-mediated delivery of mutant huntingtin in the striatum of rats induces a selective neuropathology modulated by polyglutamine repeat size, huntingtin expression levels, and protein length
    • de Almeida L.P., Ross C.A., Zala D., et al. Lentiviral-mediated delivery of mutant huntingtin in the striatum of rats induces a selective neuropathology modulated by polyglutamine repeat size, huntingtin expression levels, and protein length. J Neurosci 2002, 22:3473-3483.
    • (2002) J Neurosci , vol.22 , pp. 3473-3483
    • de Almeida, L.P.1    Ross, C.A.2    Zala, D.3
  • 73
    • 33845898194 scopus 로고    scopus 로고
    • Ubiquitin-conjugating enzyme E2-25K increases aggregate formation and cell death in polyglutamine diseases
    • de Pril R., Fischer D.F., Roos R.A., et al. Ubiquitin-conjugating enzyme E2-25K increases aggregate formation and cell death in polyglutamine diseases. Mol Cell Neurosci 2007, 34:10-19.
    • (2007) Mol Cell Neurosci , vol.34 , pp. 10-19
    • de Pril, R.1    Fischer, D.F.2    Roos, R.A.3
  • 74
    • 0027378051 scopus 로고
    • Dynamic mutation in Dutch Huntington's disease patients: increased paternal repeat instability extending to within the normal size range
    • De Rooij K.E., De Koning Gans P.A., Skraastad M.I., et al. Dynamic mutation in Dutch Huntington's disease patients: increased paternal repeat instability extending to within the normal size range. J Med Genet 1993, 30:996-1002.
    • (1993) J Med Genet , vol.30 , pp. 996-1002
    • De Rooij, K.E.1    De Koning Gans, P.A.2    Skraastad, M.I.3
  • 75
    • 0347064159 scopus 로고    scopus 로고
    • Neuronal induction of the immunoproteasome in Huntington's disease
    • Diaz-Hernandez M., Hernandez F., Martin-Aparicio E., et al. Neuronal induction of the immunoproteasome in Huntington's disease. J Neurosci 2003, 23:11653-11661.
    • (2003) J Neurosci , vol.23 , pp. 11653-11661
    • Diaz-Hernandez, M.1    Hernandez, F.2    Martin-Aparicio, E.3
  • 76
    • 59649109467 scopus 로고    scopus 로고
    • Decreased BDNF levels are a major contributor to the embryonic phenotype of huntingtin knockdown zebrafish
    • Diekmann H., Anichtchik O., Fleming A., et al. Decreased BDNF levels are a major contributor to the embryonic phenotype of huntingtin knockdown zebrafish. J Neurosci 2009, 29:1343-1349.
    • (2009) J Neurosci , vol.29 , pp. 1343-1349
    • Diekmann, H.1    Anichtchik, O.2    Fleming, A.3
  • 77
    • 57649228989 scopus 로고    scopus 로고
    • Congenital hydrocephalus associated with abnormal subcommissural organ in mice lacking huntingtin in Wnt1 cell lineages
    • Dietrich P., Shanmugasundaram R., Shuyu E., et al. Congenital hydrocephalus associated with abnormal subcommissural organ in mice lacking huntingtin in Wnt1 cell lineages. Hum Mol Genet 2009, 18:142-150.
    • (2009) Hum Mol Genet , vol.18 , pp. 142-150
    • Dietrich, P.1    Shanmugasundaram, R.2    Shuyu, E.3
  • 78
    • 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
  • 79
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DiFiglia M., Sapp E., Chase K.O., et al. Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 1997, 277:1990-1993.
    • (1997) Science , vol.277 , pp. 1990-1993
    • DiFiglia, M.1    Sapp, E.2    Chase, K.O.3
  • 80
    • 36749033738 scopus 로고    scopus 로고
    • Therapeutic silencing of mutant huntingtin with siRNA attenuates striatal and cortical neuropathology and behavioral deficits
    • DiFiglia M., Sena-Esteves M., Chase K., et al. Therapeutic silencing of mutant huntingtin with siRNA attenuates striatal and cortical neuropathology and behavioral deficits. Proc Natl Acad Sci U S A 2007, 104:17204-17209.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 17204-17209
    • DiFiglia, M.1    Sena-Esteves, M.2    Chase, K.3
  • 81
    • 37549033947 scopus 로고    scopus 로고
    • Genome-wide demethylation promotes triplet repeat instability independently of homologous recombination
    • Dion V., Lin Y., Price B.A., et al. Genome-wide demethylation promotes triplet repeat instability independently of homologous recombination. DNA Repair (Amst) 2008, 7:313-320.
    • (2008) DNA Repair (Amst) , vol.7 , pp. 313-320
    • Dion, V.1    Lin, Y.2    Price, B.A.3
  • 82
    • 2942587013 scopus 로고    scopus 로고
    • Mouse Huntington's disease homolog mRNA levels: variation and allele effects
    • Dixon K.T., Cearley J.A., Hunter J.M., et al. Mouse Huntington's disease homolog mRNA levels: variation and allele effects. Gene Expr 2004, 11:221-231.
    • (2004) Gene Expr , vol.11 , pp. 221-231
    • Dixon, K.T.1    Cearley, J.A.2    Hunter, J.M.3
  • 83
    • 2542560500 scopus 로고    scopus 로고
    • DNA elements important for CAG*CTG repeat thresholds in Saccharomyces cerevisiae
    • Dixon M.J., Lahue R.S. DNA elements important for CAG*CTG repeat thresholds in Saccharomyces cerevisiae. Nucleic Acids Res 2004, 32:1289-1297.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1289-1297
    • Dixon, M.J.1    Lahue, R.S.2
  • 84
    • 0030025601 scopus 로고    scopus 로고
    • Codon repeats in genes associated with human diseases: fewer repeats in the genes of nonhuman primates and nucleotide substitutions concentrated at the sites of reiteration
    • Djian P., Hancock J.M., Chana H.S. Codon repeats in genes associated with human diseases: fewer repeats in the genes of nonhuman primates and nucleotide substitutions concentrated at the sites of reiteration. Proc Natl Acad Sci U S A 1996, 93:417-421.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 417-421
    • Djian, P.1    Hancock, J.M.2    Chana, H.S.3
  • 85
    • 10744225124 scopus 로고    scopus 로고
    • Interaction of normal and expanded CAG repeat sizes influences age at onset of Huntington disease
    • Djousse L., Knowlton B., Hayden M., et al. Interaction of normal and expanded CAG repeat sizes influences age at onset of Huntington disease. Am J Med Genet A 2003, 119A:279-282.
    • (2003) Am J Med Genet A , vol.119 A , pp. 279-282
    • Djousse, L.1    Knowlton, B.2    Hayden, M.3
  • 86
    • 3042678165 scopus 로고    scopus 로고
    • Evidence for a modifier of onset age in Huntington disease linked to the HD gene in 4p16
    • Djousse L., Knowlton B., Hayden M.R., et al. Evidence for a modifier of onset age in Huntington disease linked to the HD gene in 4p16. Neurogenetics 2004, 5:109-114.
    • (2004) Neurogenetics , vol.5 , pp. 109-114
    • Djousse, L.1    Knowlton, B.2    Hayden, M.R.3
  • 87
    • 44449177217 scopus 로고    scopus 로고
    • RNA-binding protein TLS is a major nuclear aggregate-interacting protein in huntingtin exon 1 with expanded polyglutamine-expressing cells
    • Doi H., Okamura K., Bauer P.O., et al. RNA-binding protein TLS is a major nuclear aggregate-interacting protein in huntingtin exon 1 with expanded polyglutamine-expressing cells. J Biol Chem 2008, 283:6489-6500.
    • (2008) J Biol Chem , vol.283 , pp. 6489-6500
    • Doi, H.1    Okamura, K.2    Bauer, P.O.3
  • 88
    • 2642646258 scopus 로고    scopus 로고
    • Mouse mutant embryos lacking huntingtin are rescued from lethality by wild-type extraembryonic tissues
    • Dragatsis I., Efstratiadis A., Zeitlin S. Mouse mutant embryos lacking huntingtin are rescued from lethality by wild-type extraembryonic tissues. Development 1998, 125:1529-1539.
    • (1998) Development , vol.125 , pp. 1529-1539
    • Dragatsis, I.1    Efstratiadis, A.2    Zeitlin, S.3
  • 89
    • 0033757718 scopus 로고    scopus 로고
    • Inactivation of Hdh in the brain and testis results in progressive neurodegeneration and sterility in mice
    • Dragatsis I., Levine M.S., Zeitlin S. Inactivation of Hdh in the brain and testis results in progressive neurodegeneration and sterility in mice. Nat Genet 2000, 26:300-306.
    • (2000) Nat Genet , vol.26 , pp. 300-306
    • Dragatsis, I.1    Levine, M.S.2    Zeitlin, S.3
  • 90
    • 60849109193 scopus 로고    scopus 로고
    • CAG repeat lengths > or =335 attenuate the phenotype in the R6/2 Huntington's disease transgenic mouse
    • Dragatsis I., Goldovitz D., Del Mar N., et al. CAG repeat lengths > or =335 attenuate the phenotype in the R6/2 Huntington's disease transgenic mouse. Neurobiol Dis 2009, 33:315-330.
    • (2009) Neurobiol Dis , vol.33 , pp. 315-330
    • Dragatsis, I.1    Goldovitz, D.2    Del Mar, N.3
  • 91
    • 57449091694 scopus 로고    scopus 로고
    • Intergenerational and striatal CAG repeat instability in Huntington's disease knock-in mice involve different DNA repair genes
    • Dragileva E., Hendricks A., Teed A., et al. Intergenerational and striatal CAG repeat instability in Huntington's disease knock-in mice involve different DNA repair genes. Neurobiol Dis 2009, 33:37-47.
    • (2009) Neurobiol Dis , vol.33 , pp. 37-47
    • Dragileva, E.1    Hendricks, A.2    Teed, A.3
  • 92
    • 0029040355 scopus 로고
    • In situ evidence for DNA fragmentation in Huntington's disease striatum and Alzheimer's disease temporal lobes
    • Dragunow M., Faull R.L., Lawlor P., et al. In situ evidence for DNA fragmentation in Huntington's disease striatum and Alzheimer's disease temporal lobes. Neuroreport 1995, 6:1053-1057.
    • (1995) Neuroreport , vol.6 , pp. 1053-1057
    • Dragunow, M.1    Faull, R.L.2    Lawlor, P.3
  • 93
    • 0037150687 scopus 로고    scopus 로고
    • Sp1 and TAFII130 transcriptional activity disrupted in early Huntington's disease
    • Dunah A.W., Jeong H., Griffin A., et al. Sp1 and TAFII130 transcriptional activity disrupted in early Huntington's disease. Science 2002, 296:2238-2243.
    • (2002) Science , vol.296 , pp. 2238-2243
    • Dunah, A.W.1    Jeong, H.2    Griffin, A.3
  • 94
    • 0028015996 scopus 로고
    • IT15 gene expression in fetal human brain
    • Dure L.S., Landwehrmeyer G.B., Golden J., et al. IT15 gene expression in fetal human brain. Brain Res 1994, 659:33-41.
    • (1994) Brain Res , vol.659 , pp. 33-41
    • Dure, L.S.1    Landwehrmeyer, G.B.2    Golden, J.3
  • 95
    • 9244225693 scopus 로고    scopus 로고
    • Spinocerebellar ataxia 3 and Machado-Joseph disease: clinical, molecular, and neuropathological features
    • Durr A., Stevanin G., Cancel G., et al. Spinocerebellar ataxia 3 and Machado-Joseph disease: clinical, molecular, and neuropathological features. Ann Neurol 1996, 39:490-499.
    • (1996) Ann Neurol , vol.39 , pp. 490-499
    • Durr, A.1    Stevanin, G.2    Cancel, G.3
  • 96
    • 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
  • 97
    • 0027157977 scopus 로고
    • A gene from chromosome 4p16.3 with similarity to a superfamily of transporter proteins
    • Duyao M.P., Taylor S.A., Buckler A.J., et al. A gene from chromosome 4p16.3 with similarity to a superfamily of transporter proteins. Hum Mol Genet 1993, 2:673-676.
    • (1993) Hum Mol Genet , vol.2 , pp. 673-676
    • Duyao, M.P.1    Taylor, S.A.2    Buckler, A.J.3
  • 98
    • 0029082383 scopus 로고
    • Inactivation of the mouse Huntington's disease gene homolog Hdh
    • Duyao M.P., Auerbach A.B., Ryan A., et al. Inactivation of the mouse Huntington's disease gene homolog Hdh. Science 1995, 269:407-410.
    • (1995) Science , vol.269 , pp. 407-410
    • Duyao, M.P.1    Auerbach, A.B.2    Ryan, A.3
  • 99
    • 0035179456 scopus 로고    scopus 로고
    • Mutant protein in Huntington disease is resistant to proteolysis in affected brain
    • Dyer R.B., McMurray C.T. Mutant protein in Huntington disease is resistant to proteolysis in affected brain. Nat Genet 2001, 29:270-278.
    • (2001) Nat Genet , vol.29 , pp. 270-278
    • Dyer, R.B.1    McMurray, C.T.2
  • 100
    • 0026551039 scopus 로고
    • Genetic variation at five trimeric and tetrameric tandem repeat loci in four human population groups
    • Edwards A., Hammond H.A., Jin L., et al. Genetic variation at five trimeric and tetrameric tandem repeat loci in four human population groups. Genomics 1992, 12:241-253.
    • (1992) Genomics , vol.12 , pp. 241-253
    • Edwards, A.1    Hammond, H.A.2    Jin, L.3
  • 101
    • 0035125552 scopus 로고    scopus 로고
    • ST14A cells have properties of a medium-size spiny neuron
    • Ehrlich M.E., Conti L., Toselli M., et al. ST14A cells have properties of a medium-size spiny neuron. Exp Neurol 2001, 167:215-226.
    • (2001) Exp Neurol , vol.167 , pp. 215-226
    • Ehrlich, M.E.1    Conti, L.2    Toselli, M.3
  • 102
    • 33748744375 scopus 로고    scopus 로고
    • Green tea (-)-epigallocatechin-gallate modulates early events in huntingtin misfolding and reduces toxicity in Huntington's disease models
    • Ehrnhoefer D.E., Duennwald M., Markovic P., et al. Green tea (-)-epigallocatechin-gallate modulates early events in huntingtin misfolding and reduces toxicity in Huntington's disease models. Hum Mol Genet 2006, 15:2743-2751.
    • (2006) Hum Mol Genet , vol.15 , pp. 2743-2751
    • Ehrnhoefer, D.E.1    Duennwald, M.2    Markovic, P.3
  • 103
    • 0023633397 scopus 로고
    • Amino acid neurotransmitter abnormalities in Huntington's disease and the quinolinic acid animal model of Huntington's disease
    • Ellison D.W., Beal M.F., Mazurek M.F., et al. Amino acid neurotransmitter abnormalities in Huntington's disease and the quinolinic acid animal model of Huntington's disease. Brain 1987, 110:1657-1673.
    • (1987) Brain , vol.110 , pp. 1657-1673
    • Ellison, D.W.1    Beal, M.F.2    Mazurek, M.F.3
  • 104
    • 0030906578 scopus 로고    scopus 로고
    • Protective effect of encapsulated cells producing neurotrophic factor CNTF in a monkey model of Huntington's disease
    • Emerich D.F., Winn S.R., Hantraye P.M., et al. Protective effect of encapsulated cells producing neurotrophic factor CNTF in a monkey model of Huntington's disease. Nature 1997, 386:395-399.
    • (1997) Nature , vol.386 , pp. 395-399
    • Emerich, D.F.1    Winn, S.R.2    Hantraye, P.M.3
  • 105
    • 0031662269 scopus 로고    scopus 로고
    • Huntingtin interacts with a family of WW domain proteins
    • Faber P.W., Barnes G.T., Srinidhi J., et al. Huntingtin interacts with a family of WW domain proteins. Hum Mol Genet 1998, 7:1463-1474.
    • (1998) Hum Mol Genet , vol.7 , pp. 1463-1474
    • Faber, P.W.1    Barnes, G.T.2    Srinidhi, J.3
  • 106
    • 0033524413 scopus 로고    scopus 로고
    • Polyglutamine-mediated dysfunction and apoptotic death of a Caenorhabditis elegans sensory neuron
    • Faber P.W., Alter J.R., MacDonald M.E., et al. Polyglutamine-mediated dysfunction and apoptotic death of a Caenorhabditis elegans sensory neuron. Proc Natl Acad Sci U S A 1999, 96:179-184.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 179-184
    • Faber, P.W.1    Alter, J.R.2    MacDonald, M.E.3
  • 107
    • 0037168585 scopus 로고    scopus 로고
    • Glutamine/proline-rich PQE-1 proteins protect Caenorhabditis elegans neurons from huntingtin polyglutamine neurotoxicity
    • Faber P.W., Voisine C., King D.C., et al. Glutamine/proline-rich PQE-1 proteins protect Caenorhabditis elegans neurons from huntingtin polyglutamine neurotoxicity. Proc Natl Acad Sci U S A 2002, 99:17131-17136.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 17131-17136
    • Faber, P.W.1    Voisine, C.2    King, D.C.3
  • 108
    • 0027361698 scopus 로고
    • The normal Huntington disease (HD) allele, or a closely linked gene, influences age at onset of HD
    • Farrer L.A., Cupples L.A., Wiater P., et al. The normal Huntington disease (HD) allele, or a closely linked gene, influences age at onset of HD. Am J Hum Genet 1993, 53:125-130.
    • (1993) Am J Hum Genet , vol.53 , pp. 125-130
    • Farrer, L.A.1    Cupples, L.A.2    Wiater, P.3
  • 109
    • 30044438329 scopus 로고    scopus 로고
    • P53 tumor suppressor protein regulates the levels of huntingtin gene expression
    • Feng Z., Jin S., Zupnick A., et al. p53 tumor suppressor protein regulates the levels of huntingtin gene expression. Oncogene 2006, 25:1-7.
    • (2006) Oncogene , vol.25 , pp. 1-7
    • Feng, Z.1    Jin, S.2    Zupnick, A.3
  • 110
    • 0023080626 scopus 로고
    • Morphologic and histochemical characteristics of a spared subset of striatal neurons in Huntington's disease
    • Ferrante R.J., Kowall N.W., Beal M.F., et al. Morphologic and histochemical characteristics of a spared subset of striatal neurons in Huntington's disease. J Neuropathol Exp Neurol 1987, 46:12-27.
    • (1987) J Neuropathol Exp Neurol , vol.46 , pp. 12-27
    • Ferrante, R.J.1    Kowall, N.W.2    Beal, M.F.3
  • 111
    • 0036523110 scopus 로고    scopus 로고
    • Therapeutic effects of coenzyme Q10 and remacemide in transgenic mouse models of Huntington's disease
    • Ferrante R.J., Andreassen O.A., Dedeoglu A., et al. Therapeutic effects of coenzyme Q10 and remacemide in transgenic mouse models of Huntington's disease. J Neurosci 2002, 22:1592-1599.
    • (2002) J Neurosci , vol.22 , pp. 1592-1599
    • Ferrante, R.J.1    Andreassen, O.A.2    Dedeoglu, A.3
  • 112
    • 0025985496 scopus 로고
    • A candidate gene for X-linked spinal muscular atrophy
    • Fischbeck K.H., Souders D., La Spada A. A candidate gene for X-linked spinal muscular atrophy. Adv Neurol 1991, 56:209-213.
    • (1991) Adv Neurol , vol.56 , pp. 209-213
    • Fischbeck, K.H.1    Souders, D.2    La Spada, A.3
  • 113
    • 49549101116 scopus 로고    scopus 로고
    • Zebrafish as a new animal model for movement disorders
    • Flinn L., Bretaud S., Lo C., et al. Zebrafish as a new animal model for movement disorders. J Neurochem 2008, 106:1991-1997.
    • (2008) J Neurochem , vol.106 , pp. 1991-1997
    • Flinn, L.1    Bretaud, S.2    Lo, C.3
  • 114
    • 42549134402 scopus 로고    scopus 로고
    • AAV vector-mediated RNAi of mutant huntingtin expression is neuroprotective in a novel genetic rat model of Huntington's disease
    • Franich N.R., Fitzsimons H.L., Fong D.M., et al. AAV vector-mediated RNAi of mutant huntingtin expression is neuroprotective in a novel genetic rat model of Huntington's disease. Mol Ther 2008, 16:947-956.
    • (2008) Mol Ther , vol.16 , pp. 947-956
    • Franich, N.R.1    Fitzsimons, H.L.2    Fong, D.M.3
  • 115
    • 13444253858 scopus 로고    scopus 로고
    • Structure-forming CAG/CTG repeat sequences are sensitive to breakage in the absence of Mrc1 checkpoint function and S-phase checkpoint signaling: implications for trinucleotide repeat expansion diseases
    • Freudenreich C.H., Lahiri M. Structure-forming CAG/CTG repeat sequences are sensitive to breakage in the absence of Mrc1 checkpoint function and S-phase checkpoint signaling: implications for trinucleotide repeat expansion diseases. Cell Cycle 2004, 3:1370-1374.
    • (2004) Cell Cycle , vol.3 , pp. 1370-1374
    • Freudenreich, C.H.1    Lahiri, M.2
  • 116
    • 0037417220 scopus 로고    scopus 로고
    • Apoptosis and caspases in neurodegenerative diseases
    • Friedlander R.M. Apoptosis and caspases in neurodegenerative diseases. N Engl J Med 2003, 348:1365-1375.
    • (2003) N Engl J Med , vol.348 , pp. 1365-1375
    • Friedlander, R.M.1
  • 117
    • 0027468487 scopus 로고
    • Effects of biologically delivered NGF, BDNF and bFGF on striatal excitotoxic lesions
    • Frim D.M., Uhler T.A., Short M.P., et al. Effects of biologically delivered NGF, BDNF and bFGF on striatal excitotoxic lesions. NeuroReport 1993, 4:367-370.
    • (1993) NeuroReport , vol.4 , pp. 367-370
    • Frim, D.M.1    Uhler, T.A.2    Short, M.P.3
  • 118
    • 0028276809 scopus 로고
    • Implanted fibroblasts genetically engineered to produce brain-derived neurotrophic factor prevent 1-methyl-4-phenylpyridinium toxicity to dopaminergic neurons in the rat
    • Frim D.M., Uhler T.A., Galpern W.R., et al. Implanted fibroblasts genetically engineered to produce brain-derived neurotrophic factor prevent 1-methyl-4-phenylpyridinium toxicity to dopaminergic neurons in the rat. Proc Natl Acad Sci U S A 1994, 91:5104-5108.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 5104-5108
    • Frim, D.M.1    Uhler, T.A.2    Galpern, W.R.3
  • 119
    • 0034783914 scopus 로고    scopus 로고
    • CAG repeat expansion in the TATA box-binding protein gene causes autosomal dominant cerebellar ataxia
    • Fujigasaki H., Martin J.J., De Deyn P.P., et al. CAG repeat expansion in the TATA box-binding protein gene causes autosomal dominant cerebellar ataxia. Brain 2001, 124:1939-1947.
    • (2001) Brain , vol.124 , pp. 1939-1947
    • Fujigasaki, H.1    Martin, J.J.2    De Deyn, P.P.3
  • 120
    • 0026598119 scopus 로고
    • An unstable triplet repeat in a gene related to myotonic muscular dystrophy
    • Fu Y.H., Pizzuti A., Fenwick R.G., et al. An unstable triplet repeat in a gene related to myotonic muscular dystrophy. Science 1992, 255:1256-1258.
    • (1992) Science , vol.255 , pp. 1256-1258
    • Fu, Y.H.1    Pizzuti, A.2    Fenwick, R.G.3
  • 121
    • 0037096376 scopus 로고    scopus 로고
    • Calpain activation in Huntington's disease
    • Gafni J., Ellerby L.M. Calpain activation in Huntington's disease. J Neurosci 2002, 22:4842-4849.
    • (2002) J Neurosci , vol.22 , pp. 4842-4849
    • Gafni, J.1    Ellerby, L.M.2
  • 122
    • 2442631459 scopus 로고    scopus 로고
    • Inhibition of calpain cleavage of huntingtin reduces toxicity: accumulation of calpain/caspase fragments in the nucleus
    • Gafni J., Hermel E., Young J.E., et al. Inhibition of calpain cleavage of huntingtin reduces toxicity: accumulation of calpain/caspase fragments in the nucleus. J Biol Chem 2004, 279:20211-20220.
    • (2004) J Biol Chem , vol.279 , pp. 20211-20220
    • Gafni, J.1    Hermel, E.2    Young, J.E.3
  • 123
    • 19944431703 scopus 로고    scopus 로고
    • Neuroprotective effects of phenylbutyrate in the N171-82Q transgenic mouse model of Huntington's disease
    • Gardian G., Browne S.E., Choi D.K., et al. Neuroprotective effects of phenylbutyrate in the N171-82Q transgenic mouse model of Huntington's disease. J Biol Chem 2005, 280:556-563.
    • (2005) J Biol Chem , vol.280 , pp. 556-563
    • Gardian, G.1    Browne, S.E.2    Choi, D.K.3
  • 124
    • 3142636768 scopus 로고    scopus 로고
    • Huntingtin controls neurotrophic support and survival of neurons by enhancing BDNF vesicular transport along microtubules
    • Gauthier L.R., Charrin B.C., Borrell-Pages M., et al. Huntingtin controls neurotrophic support and survival of neurons by enhancing BDNF vesicular transport along microtubules. Cell 2004, 118:127-138.
    • (2004) Cell , vol.118 , pp. 127-138
    • Gauthier, L.R.1    Charrin, B.C.2    Borrell-Pages, M.3
  • 125
    • 48949118889 scopus 로고    scopus 로고
    • Genomewide linkage scan reveals novel loci modifying age of onset of Huntington's disease in the Venezuelan HD kindreds
    • Gayan J., Brocklebank D., Andresen J.M., et al. Genomewide linkage scan reveals novel loci modifying age of onset of Huntington's disease in the Venezuelan HD kindreds. Genet Epidemiol 2008, 32:445-453.
    • (2008) Genet Epidemiol , vol.32 , pp. 445-453
    • Gayan, J.1    Brocklebank, D.2    Andresen, J.M.3
  • 126
    • 57649158657 scopus 로고    scopus 로고
    • Impaired regulation of brain mitochondria by extramitochondrial Ca2+ in transgenic Huntington disease rats
    • Gellerich F.N., Gizatullina Z., Nguyen H.P., et al. Impaired regulation of brain mitochondria by extramitochondrial Ca2+ in transgenic Huntington disease rats. J Biol Chem 2008, 283:30715-30724.
    • (2008) J Biol Chem , vol.283 , pp. 30715-30724
    • Gellerich, F.N.1    Gizatullina, Z.2    Nguyen, H.P.3
  • 127
    • 23444458415 scopus 로고
    • Transcriptional activation modulated by homopolymeric glutamine and proline stretches
    • Gerber H.P., Seipel K., Georgiev O., et al. Transcriptional activation modulated by homopolymeric glutamine and proline stretches. Science 1994, 263:808-811.
    • (1994) Science , vol.263 , pp. 808-811
    • Gerber, H.P.1    Seipel, K.2    Georgiev, O.3
  • 128
    • 0030944114 scopus 로고    scopus 로고
    • The prevalence and wide clinical spectrum of the spinocerebellar ataxia type 2 trinucleotide repeat in patients with autosomal dominant cerebellar ataxia
    • Geschwind D.H., Perlman S., Figueroa C.P., et al. The prevalence and wide clinical spectrum of the spinocerebellar ataxia type 2 trinucleotide repeat in patients with autosomal dominant cerebellar ataxia. Am J Hum Genet 1997, 60:842-850.
    • (1997) Am J Hum Genet , vol.60 , pp. 842-850
    • Geschwind, D.H.1    Perlman, S.2    Figueroa, C.P.3
  • 129
    • 4444301185 scopus 로고    scopus 로고
    • SUMO and ubiquitin in the nucleus: different functions, similar mechanisms?
    • Gill G. SUMO and ubiquitin in the nucleus: different functions, similar mechanisms?. Genes Dev 2004, 18:2046-2059.
    • (2004) Genes Dev , vol.18 , pp. 2046-2059
    • Gill, G.1
  • 130
    • 0025077291 scopus 로고
    • Neural grafts and pharmacological intervention in a model of Huntington's disease
    • Giordano M., Ford L.M., Shipley M.T., et al. Neural grafts and pharmacological intervention in a model of Huntington's disease. Brain Res Bull 1990, 25:453-465.
    • (1990) Brain Res Bull , vol.25 , pp. 453-465
    • Giordano, M.1    Ford, L.M.2    Shipley, M.T.3
  • 131
    • 33751193268 scopus 로고    scopus 로고
    • Huntingtin gene evolution in Chordata and its peculiar features in the ascidian Ciona genus
    • Gissi C., Pesole G., Cattaneo E., et al. Huntingtin gene evolution in Chordata and its peculiar features in the ascidian Ciona genus. BMC Genomics 2006, 7:288.
    • (2006) BMC Genomics , vol.7 , pp. 288
    • Gissi, C.1    Pesole, G.2    Cattaneo, E.3
  • 132
    • 0028882406 scopus 로고
    • Detection of the Machado-Joseph disease/spinocerebellar ataxia three trinucleotide repeat expansion in families with autosomal dominant motor disorders, including the Drew family of Walworth
    • Giunti P., Sweeney M.G., Harding A.E. Detection of the Machado-Joseph disease/spinocerebellar ataxia three trinucleotide repeat expansion in families with autosomal dominant motor disorders, including the Drew family of Walworth. Brain 1995, 118:1077-1085.
    • (1995) Brain , vol.118 , pp. 1077-1085
    • Giunti, P.1    Sweeney, M.G.2    Harding, A.E.3
  • 133
    • 0004799163 scopus 로고    scopus 로고
    • Molecular and clinical study of 18 families with ADCA type II: evidence for genetic heterogeneity and de novo mutation
    • Giunti P., Stevanin G., Worth P.F., et al. Molecular and clinical study of 18 families with ADCA type II: evidence for genetic heterogeneity and de novo mutation. Am J Hum Genet 1999, 64:1594-1603.
    • (1999) Am J Hum Genet , vol.64 , pp. 1594-1603
    • Giunti, P.1    Stevanin, G.2    Worth, P.F.3
  • 134
    • 4644231870 scopus 로고    scopus 로고
    • A protein interaction network links GIT1, an enhancer of huntingtin aggregation, to Huntington's disease
    • Goehler H., Lalowski M., Stelzl U., et al. A protein interaction network links GIT1, an enhancer of huntingtin aggregation, to Huntington's disease. Mol Cell 2004, 15:853-865.
    • (2004) Mol Cell , vol.15 , pp. 853-865
    • Goehler, H.1    Lalowski, M.2    Stelzl, U.3
  • 135
    • 0037131263 scopus 로고    scopus 로고
    • Calcium-dependent cleavage of endogenous wild-type huntingtin in primary cortical neurons
    • Goffredo D., Rigamonti D., Tartari M., et al. Calcium-dependent cleavage of endogenous wild-type huntingtin in primary cortical neurons. J Biol Chem 2002, 277:39594-39598.
    • (2002) J Biol Chem , vol.277 , pp. 39594-39598
    • Goffredo, D.1    Rigamonti, D.2    Tartari, M.3
  • 136
    • 0027482789 scopus 로고
    • Familial predisposition to recurrent mutations causing Huntington's disease: genetic risk to sibs of sporadic cases
    • Goldberg Y.P., Andrew S.E., Theilmann J., et al. Familial predisposition to recurrent mutations causing Huntington's disease: genetic risk to sibs of sporadic cases. J Med Genet 1993, 30:987-990.
    • (1993) J Med Genet , vol.30 , pp. 987-990
    • Goldberg, Y.P.1    Andrew, S.E.2    Theilmann, J.3
  • 137
    • 0027467024 scopus 로고
    • Identification of an Alu retrotransposition event in close proximity to a strong candidate gene for Huntington's disease
    • Goldberg Y.P., Rommens J.M., Andrew S.E., et al. Identification of an Alu retrotransposition event in close proximity to a strong candidate gene for Huntington's disease. Nature 1993, 362:370-373.
    • (1993) Nature , vol.362 , pp. 370-373
    • Goldberg, Y.P.1    Rommens, J.M.2    Andrew, S.E.3
  • 138
    • 0027359989 scopus 로고
    • Molecular analysis of new mutations for Huntington's disease: intermediate alleles and sex of origin effects
    • Goldberg Y.P., Kremer B., Andrew S.E., et al. Molecular analysis of new mutations for Huntington's disease: intermediate alleles and sex of origin effects. Nat Genet 1993, 5:174-179.
    • (1993) Nat Genet , vol.5 , pp. 174-179
    • Goldberg, Y.P.1    Kremer, B.2    Andrew, S.E.3
  • 139
    • 9344227302 scopus 로고    scopus 로고
    • Cleavage of huntingtin by apopain, a proapoptotic cysteine protease, is modulated by the polyglutamine tract
    • Goldberg Y.P., Nicholson D.W., Rasper D.M., et al. Cleavage of huntingtin by apopain, a proapoptotic cysteine protease, is modulated by the polyglutamine tract. Nat Genet 1996, 13:442-449.
    • (1996) Nat Genet , vol.13 , pp. 442-449
    • Goldberg, Y.P.1    Nicholson, D.W.2    Rasper, D.M.3
  • 141
    • 0027445452 scopus 로고
    • "Cryptic" repeating triplets of purines and pyrimidines (cRRY(i)) are frequent and polymorphic: analysis of coding cRRY(i) in the proopiomelanocortin (POMC) and TATA-binding protein (TBP) genes
    • Gostout B., Liu Q., Sommer S.S. "Cryptic" repeating triplets of purines and pyrimidines (cRRY(i)) are frequent and polymorphic: analysis of coding cRRY(i) in the proopiomelanocortin (POMC) and TATA-binding protein (TBP) genes. Am J Hum Genet 1993, 52:1182-1190.
    • (1993) Am J Hum Genet , vol.52 , pp. 1182-1190
    • Gostout, B.1    Liu, Q.2    Sommer, S.S.3
  • 142
    • 30744459353 scopus 로고    scopus 로고
    • Levels of mutant huntingtin influence the phenotypic severity of Huntington disease in YAC128 mouse models
    • Graham R.K., Slow E.J., Deng Y., et al. Levels of mutant huntingtin influence the phenotypic severity of Huntington disease in YAC128 mouse models. Neurobiol Dis 2006, 21:444-455.
    • (2006) Neurobiol Dis , vol.21 , pp. 444-455
    • Graham, R.K.1    Slow, E.J.2    Deng, Y.3
  • 143
    • 33745003424 scopus 로고    scopus 로고
    • Cleavage at the caspase-6 site is required for neuronal dysfunction and degeneration due to mutant huntingtin
    • Graham R.K., Deng Y., Slow E.J., et al. Cleavage at the caspase-6 site is required for neuronal dysfunction and degeneration due to mutant huntingtin. Cell 2006, 125:1179-1191.
    • (2006) Cell , vol.125 , pp. 1179-1191
    • Graham, R.K.1    Deng, Y.2    Slow, E.J.3
  • 144
    • 0028836272 scopus 로고
    • Characterization of the excitotoxic potential of the reversible succinate dehydrogenase inhibitor malonate
    • Greene J.G., Greenamyre J.T. Characterization of the excitotoxic potential of the reversible succinate dehydrogenase inhibitor malonate. J Neurochem 1995, 64:430-436.
    • (1995) J Neurochem , vol.64 , pp. 430-436
    • Greene, J.G.1    Greenamyre, J.T.2
  • 145
    • 0029875381 scopus 로고    scopus 로고
    • Mitochondrial defect in Huntington's disease caudate nucleus
    • Gu M., Gash M.T., Mann V.M., et al. Mitochondrial defect in Huntington's disease caudate nucleus. Ann Neurol 1996, 39:385-389.
    • (1996) Ann Neurol , vol.39 , pp. 385-389
    • Gu, M.1    Gash, M.T.2    Mann, V.M.3
  • 146
    • 0021028244 scopus 로고
    • A polymorphic DNA marker genetically linked to Huntington's disease
    • Gusella J.F., Wexler N.S., Conneally P.M., et al. A polymorphic DNA marker genetically linked to Huntington's disease. Nature 1983, 306:234-238.
    • (1983) Nature , vol.306 , pp. 234-238
    • Gusella, J.F.1    Wexler, N.S.2    Conneally, P.M.3
  • 147
    • 0021211053 scopus 로고
    • DNA markers for nervous system diseases
    • Gusella J.F., Tanzi R.E., Anderson M.A., et al. DNA markers for nervous system diseases. Science 1984, 225:1320-1326.
    • (1984) Science , vol.225 , pp. 1320-1326
    • Gusella, J.F.1    Tanzi, R.E.2    Anderson, M.A.3
  • 148
    • 0022403677 scopus 로고
    • Deletion of Huntington's disease-linked G8 (D4S10) locus in Wolf-Hirschhorn syndrome
    • Gusella J.F., Tanzi R.E., Bader P.I., et al. Deletion of Huntington's disease-linked G8 (D4S10) locus in Wolf-Hirschhorn syndrome. Nature 1985, 318:75-78.
    • (1985) Nature , vol.318 , pp. 75-78
    • Gusella, J.F.1    Tanzi, R.E.2    Bader, P.I.3
  • 149
    • 0029152808 scopus 로고
    • Identification and localization of huntingtin in brain and human lymphoblastoid cell lines with anti-fusion protein antibodies
    • Gutekunst C.A., Levey A.I., Heilman C.J., 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, 92:8710-8714.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 8710-8714
    • Gutekunst, C.A.1    Levey, A.I.2    Heilman, C.J.3
  • 150
    • 0033119123 scopus 로고    scopus 로고
    • Nuclear and neuropil aggregates in Huntington's disease: relationship to neuropathology
    • Gutekunst C.A., Li S.H., Yi H., et al. Nuclear and neuropil aggregates in Huntington's disease: relationship to neuropathology. J Neurosci 1999, 19:2522-2534.
    • (1999) J Neurosci , vol.19 , pp. 2522-2534
    • Gutekunst, C.A.1    Li, S.H.2    Yi, H.3
  • 151
    • 0032101287 scopus 로고    scopus 로고
    • The influence of huntingtin protein size on nuclear localization and cellular toxicity
    • Hackam A.S., Singaraja R., Wellington C.L., 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
  • 152
    • 0025279038 scopus 로고
    • A primate model of Huntington's disease: behavioral and anatomical studies of unilateral excitotoxic lesions of the caudate-putamen in the baboon
    • Hantraye P., Riche D., Maziere M., et al. A primate model of Huntington's disease: behavioral and anatomical studies of unilateral excitotoxic lesions of the caudate-putamen in the baboon. Exp Neurol 1990, 108:91-104.
    • (1990) Exp Neurol , vol.108 , pp. 91-104
    • Hantraye, P.1    Riche, D.2    Maziere, M.3
  • 153
    • 0026594055 scopus 로고
    • Intrastriatal transplantation of cross-species fetal striatal cells reduces abnormal movements in a primate model of Huntington disease
    • Hantraye P., Riche D., Maziere M., et al. Intrastriatal transplantation of cross-species fetal striatal cells reduces abnormal movements in a primate model of Huntington disease. Proc Natl Acad Sci U S A 1992, 89:4187-4191.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 4187-4191
    • Hantraye, P.1    Riche, D.2    Maziere, M.3
  • 154
    • 0034649661 scopus 로고    scopus 로고
    • FIP-2, a coiled-coil protein, links Huntingtin to Rab8 and modulates cellular morphogenesis
    • Hattula K., Peranen J. FIP-2, a coiled-coil protein, links Huntingtin to Rab8 and modulates cellular morphogenesis. Curr Biol 2000, 10:1603-1606.
    • (2000) Curr Biol , vol.10 , pp. 1603-1606
    • Hattula, K.1    Peranen, J.2
  • 155
    • 0028333034 scopus 로고
    • Malonate produces striatal lesions by indirect NMDA receptor activation
    • Henshaw R., Jenkins B.G., Schulz J.B., et al. Malonate produces striatal lesions by indirect NMDA receptor activation. Brain Res 1994, 647:161-166.
    • (1994) Brain Res , vol.647 , pp. 161-166
    • Henshaw, R.1    Jenkins, B.G.2    Schulz, J.B.3
  • 156
    • 58149385090 scopus 로고    scopus 로고
    • Enhanced sensitivity of striatal neurons to axonal transport defects induced by mutant huntingtin
    • Her L.S., Goldstein L.S. Enhanced sensitivity of striatal neurons to axonal transport defects induced by mutant huntingtin. J Neurosci 2008, 28:13662-13672.
    • (2008) J Neurosci , vol.28 , pp. 13662-13672
    • Her, L.S.1    Goldstein, L.S.2
  • 157
    • 11144357398 scopus 로고    scopus 로고
    • Specific caspase interactions and amplification are involved in selective neuronal vulnerability in Huntington's disease
    • Hermel E., Gafni J., Propp S.S., et al. Specific caspase interactions and amplification are involved in selective neuronal vulnerability in Huntington's disease. Cell Death Differ 2004, 11:424-438.
    • (2004) Cell Death Differ , vol.11 , pp. 424-438
    • Hermel, E.1    Gafni, J.2    Propp, S.S.3
  • 158
    • 33644927838 scopus 로고    scopus 로고
    • Creatine in Huntington disease is safe, tolerable, bioavailable in brain and reduces serum 8OH2'dG
    • Hersch S.M., Gevorkian S., Marder K., et al. Creatine in Huntington disease is safe, tolerable, bioavailable in brain and reduces serum 8OH2'dG. Neurology 2006, 66:250-252.
    • (2006) Neurology , vol.66 , pp. 250-252
    • Hersch, S.M.1    Gevorkian, S.2    Marder, K.3
  • 159
    • 0034703860 scopus 로고    scopus 로고
    • Huntingtin: an iron-regulated protein essential for normal nuclear and perinuclear organelles
    • Hilditch-Maguire P., Trettel F., Passani L.A., et al. Huntingtin: an iron-regulated protein essential for normal nuclear and perinuclear organelles. Hum Mol Genet 2000, 9:2789-2797.
    • (2000) Hum Mol Genet , vol.9 , pp. 2789-2797
    • Hilditch-Maguire, P.1    Trettel, F.2    Passani, L.A.3
  • 160
    • 0037452775 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid, a histone deacetylase inhibitor, ameliorates motor deficits in a mouse model of Huntington's disease
    • Hockly E., Richon V.M., 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, 100:2041-2046.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 2041-2046
    • Hockly, E.1    Richon, V.M.2    Woodman, B.3
  • 161
    • 33644783812 scopus 로고    scopus 로고
    • Regional and cellular gene expression changes in human Huntington's disease brain
    • Hodges A., Strand A.D., Aragaki A.K., et al. Regional and cellular gene expression changes in human Huntington's disease brain. Hum Mol Genet 2006, 15:965-977.
    • (2006) Hum Mol Genet , vol.15 , pp. 965-977
    • Hodges, A.1    Strand, A.D.2    Aragaki, A.K.3
  • 162
    • 10544222019 scopus 로고    scopus 로고
    • Human huntingtin derived from YAC transgenes compensates for loss of murine huntingtin by rescue of the embryonic lethal phenotype
    • Hodgson J.G., Smith D.J., McCutcheon K., et al. Human huntingtin derived from YAC transgenes compensates for loss of murine huntingtin by rescue of the embryonic lethal phenotype. Hum Mol Genet 1996, 5:1875-1885.
    • (1996) Hum Mol Genet , vol.5 , pp. 1875-1885
    • Hodgson, J.G.1    Smith, D.J.2    McCutcheon, K.3
  • 163
    • 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 J.G., Agopyan N., Gutekunst C.A., et al. 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
  • 164
    • 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, 115:941-948.
    • (2002) J Cell Sci , vol.115 , pp. 941-948
    • Hoffner, G.1    Kahlem, P.2    Djian, P.3
  • 165
    • 58549096941 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the common marmoset huntingtin gene
    • Hohjoh H., Akari H., Fujiwara Y., et al. Molecular cloning and characterization of the common marmoset huntingtin gene. Gene 2009, 432:60-66.
    • (2009) Gene , vol.432 , pp. 60-66
    • Hohjoh, H.1    Akari, H.2    Fujiwara, Y.3
  • 166
    • 0035852687 scopus 로고    scopus 로고
    • The Gln-Ala repeat transcriptional activator CA150 interacts with huntingtin: neuropathologic and genetic evidence for a role in Huntington's disease pathogenesis
    • Holbert S., Denghien I., Kiechle T., et al. The Gln-Ala repeat transcriptional activator CA150 interacts with huntingtin: neuropathologic and genetic evidence for a role in Huntington's disease pathogenesis. Proc Natl Acad Sci U S A 2001, 98:1811-1816.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 1811-1816
    • Holbert, S.1    Denghien, I.2    Kiechle, T.3
  • 167
    • 0344838402 scopus 로고    scopus 로고
    • Cdc42-interacting protein 4 binds to huntingtin: neuropathologic and biological evidence for a role in Huntington's disease
    • Holbert S., Dedeoglu A., Humbert S., et al. Cdc42-interacting protein 4 binds to huntingtin: neuropathologic and biological evidence for a role in Huntington's disease. Proc Natl Acad Sci U S A 2003, 100:2712-2717.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 2712-2717
    • Holbert, S.1    Dedeoglu, A.2    Humbert, S.3
  • 168
    • 0032533876 scopus 로고    scopus 로고
    • Isolation and characterization of the rat huntingtin promoter
    • Holzmann C., Maueler W., Petersohn D., et al. Isolation and characterization of the rat huntingtin promoter. Biochem J 1998, 336:227-234.
    • (1998) Biochem J , vol.336 , pp. 227-234
    • Holzmann, C.1    Maueler, W.2    Petersohn, D.3
  • 169
    • 0035882406 scopus 로고    scopus 로고
    • Functional characterization of the human Huntington's disease gene promoter
    • Holzmann C., Schmidt T., Thiel G., et al. Functional characterization of the human Huntington's disease gene promoter. Brain Res Mol Brain Res 2001, 92:85-97.
    • (2001) Brain Res Mol Brain Res , vol.92 , pp. 85-97
    • Holzmann, C.1    Schmidt, T.2    Thiel, G.3
  • 170
    • 0027759564 scopus 로고
    • Characterization and localization of the Huntington disease gene product
    • Hoogeveen A.T., Willemsen R., Meyer N., et al. Characterization and localization of the Huntington disease gene product. Hum Mol Genet 1993, 2:2069-2073.
    • (1993) Hum Mol Genet , vol.2 , pp. 2069-2073
    • Hoogeveen, A.T.1    Willemsen, R.2    Meyer, N.3
  • 171
    • 33746056889 scopus 로고    scopus 로고
    • Huntingtin interacts with the receptor sorting family protein GASP2
    • Horn S.C., Lalowski M., Goehler H., et al. Huntingtin interacts with the receptor sorting family protein GASP2. J Neural Transm 2006, 113:1081-1090.
    • (2006) J Neural Transm , vol.113 , pp. 1081-1090
    • Horn, S.C.1    Lalowski, M.2    Goehler, H.3
  • 172
    • 0032450856 scopus 로고    scopus 로고
    • Amyloid formation by mutant huntingtin: threshold, progressivity and recruitment of normal polyglutamine proteins
    • Huang C.C., Faber P.W., Persichetti F., et al. Amyloid formation by mutant huntingtin: threshold, progressivity and recruitment of normal polyglutamine proteins. Somat Cell Mol Genet 1998, 24:217-233.
    • (1998) Somat Cell Mol Genet , vol.24 , pp. 217-233
    • Huang, C.C.1    Faber, P.W.2    Persichetti, F.3
  • 173
    • 10444287633 scopus 로고    scopus 로고
    • Huntingtin-interacting protein HIP14 is a palmitoyl transferase involved in palmitoylation and trafficking of multiple neuronal proteins
    • Huang K., Yanai A., Kang R., et al. Huntingtin-interacting protein HIP14 is a palmitoyl transferase involved in palmitoylation and trafficking of multiple neuronal proteins. Neuron 2004, 44:977-986.
    • (2004) Neuron , vol.44 , pp. 977-986
    • Huang, K.1    Yanai, A.2    Kang, R.3
  • 174
    • 0036083379 scopus 로고    scopus 로고
    • The IGF-1/Akt pathway is neuroprotective in Huntington's disease and involves Huntingtin phosphorylation by Akt
    • Humbert S., Bryson E.A., Cordelieres F.P., et al. The IGF-1/Akt pathway is neuroprotective in Huntington's disease and involves Huntingtin phosphorylation by Akt. Dev Cell 2002, 2:831-837.
    • (2002) Dev Cell , vol.2 , pp. 831-837
    • Humbert, S.1    Bryson, E.A.2    Cordelieres, F.P.3
  • 175
    • 34249802905 scopus 로고    scopus 로고
    • Ubiquitin-proteasome system alterations in a striatal cell model of huntington's disease
    • Hunter J.M., Lesort M., Johnson G.V. Ubiquitin-proteasome system alterations in a striatal cell model of huntington's disease. J Neurosci Res 2007, 85:1774-1788.
    • (2007) J Neurosci Res , vol.85 , pp. 1774-1788
    • Hunter, J.M.1    Lesort, M.2    Johnson, G.V.3
  • 176
    • 85009226418 scopus 로고    scopus 로고
    • Huntington Study Group A randomized, placebo-controlled trial of coenzyme Q10 and remacemide in Huntington's disease
    • 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
  • 177
    • 0345600893 scopus 로고    scopus 로고
    • Huntington Study Group Dosage effects of riluzole in Huntington's disease: a multicenter placebo-controlled study
    • Huntington Study Group Dosage effects of riluzole in Huntington's disease: a multicenter placebo-controlled study. Neurology 2003, 61:1551-1556.
    • (2003) Neurology , vol.61 , pp. 1551-1556
  • 178
  • 179
    • 0000723251 scopus 로고
    • Huntington's Disease Collaborative Research Group A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • Huntington's Disease Collaborative Research Group 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
  • 180
    • 0029022840 scopus 로고
    • Abnormal gene product identified in Huntington's disease lymphocytes and brain
    • Ide K., Nukina N., Masuda N., et al. Abnormal gene product identified in Huntington's disease lymphocytes and brain. Biochem Biophys Res Commun 1995, 209:1119-1125.
    • (1995) Biochem Biophys Res Commun , vol.209 , pp. 1119-1125
    • Ide, K.1    Nukina, N.2    Masuda, N.3
  • 181
    • 0037961686 scopus 로고    scopus 로고
    • Inducible PC12 cell model of Huntington's disease shows toxicity and decreased histone acetylation
    • Igarashi S., Morita H., Bennett K.M., et al. Inducible PC12 cell model of Huntington's disease shows toxicity and decreased histone acetylation. Neuroreport 2003, 14:565-568.
    • (2003) Neuroreport , vol.14 , pp. 565-568
    • Igarashi, S.1    Morita, H.2    Bennett, K.M.3
  • 182
    • 61449238441 scopus 로고    scopus 로고
    • Bidirectional expression of the SCA8 expansion mutation: One mutation, two genes
    • Ikeda Y., Daughters R.S., Ranum L.P. Bidirectional expression of the SCA8 expansion mutation: One mutation, two genes. Cerebellum 2008, 7:150-158.
    • (2008) Cerebellum , vol.7 , pp. 150-158
    • Ikeda, Y.1    Daughters, R.S.2    Ranum, L.P.3
  • 183
    • 0030294345 scopus 로고    scopus 로고
    • Cloning of the gene for spinocerebellar ataxia 2 reveals a locus with high sensitivity to expanded CAG/glutamine repeats
    • Imbert G., Saudou F., Yvert G., et al. Cloning of the gene for spinocerebellar ataxia 2 reveals a locus with high sensitivity to expanded CAG/glutamine repeats. Nat Genet 1996, 14:285-291.
    • (1996) Nat Genet , vol.14 , pp. 285-291
    • Imbert, G.1    Saudou, F.2    Yvert, G.3
  • 184
    • 0024533531 scopus 로고
    • A primate model of Huntington's disease: cross-species implantation of striatal precursor cells to the excitotoxically lesioned baboon caudate-putamen
    • Isacson O., Riche D., Hantraye P., et al. A primate model of Huntington's disease: cross-species implantation of striatal precursor cells to the excitotoxically lesioned baboon caudate-putamen. Exp Brain Res 1989, 75:213-220.
    • (1989) Exp Brain Res , vol.75 , pp. 213-220
    • Isacson, O.1    Riche, D.2    Hantraye, P.3
  • 185
    • 0035882460 scopus 로고    scopus 로고
    • Age-dependent and tissue-specific CAG repeat instability occurs in mouse knock-in for a mutant Huntington's disease gene
    • Ishiguro H., Yamada K., Sawada H., et al. Age-dependent and tissue-specific CAG repeat instability occurs in mouse knock-in for a mutant Huntington's disease gene. J Neurosci Res 2001, 65:289-297.
    • (2001) J Neurosci Res , vol.65 , pp. 289-297
    • Ishiguro, H.1    Yamada, K.2    Sawada, H.3
  • 186
    • 16944366032 scopus 로고    scopus 로고
    • Japanese families with autosomal dominant pure cerebellar ataxia map to chromosome 19p13.1-p13.2 and are strongly associated with mild CAG expansions in the spinocerebellar ataxia type 6 gene in chromosome 19p13.1
    • Ishikawa K., Tanaka H., Saito M., et al. Japanese families with autosomal dominant pure cerebellar ataxia map to chromosome 19p13.1-p13.2 and are strongly associated with mild CAG expansions in the spinocerebellar ataxia type 6 gene in chromosome 19p13.1. Am J Hum Genet 1997, 61:336-346.
    • (1997) Am J Hum Genet , vol.61 , pp. 336-346
    • Ishikawa, K.1    Tanaka, H.2    Saito, M.3
  • 187
    • 0032168160 scopus 로고    scopus 로고
    • Polyglutamine-expanded human huntingtin transgenes induce degeneration of Drosophila photoreceptor neurons
    • Jackson G.R., 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
  • 188
    • 15244363187 scopus 로고    scopus 로고
    • BAG-1 associates with the polyglutamine-expanded huntingtin aggregates
    • Jana N.R., Nukina N. BAG-1 associates with the polyglutamine-expanded huntingtin aggregates. Neurosci Lett 2005, 378:171-175.
    • (2005) Neurosci Lett , vol.378 , pp. 171-175
    • Jana, N.R.1    Nukina, N.2
  • 189
    • 0034641589 scopus 로고    scopus 로고
    • Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: their role in suppression of aggregation and cellular toxicity
    • Jana N.R., Tanaka M., Wang G., et al. Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: their role in suppression of aggregation and cellular toxicity. Hum Mol Genet 2000, 9:2009-2018.
    • (2000) Hum Mol Genet , vol.9 , pp. 2009-2018
    • Jana, N.R.1    Tanaka, M.2    Wang, G.3
  • 190
    • 0035336658 scopus 로고    scopus 로고
    • Altered proteasomal function due to the expression of polyglutamine-expanded truncated N-terminal huntingtin induces apoptosis by caspase activation through mitochondrial cytochrome c release
    • Jana N.R., Zemskov E.A., Wang G., et al. Altered proteasomal function due to the expression of polyglutamine-expanded truncated N-terminal huntingtin induces apoptosis by caspase activation through mitochondrial cytochrome c release. Hum Mol Genet 2001, 10:1049-1059.
    • (2001) Hum Mol Genet , vol.10 , pp. 1049-1059
    • Jana, N.R.1    Zemskov, E.A.2    Wang, G.3
  • 191
    • 15744387323 scopus 로고    scopus 로고
    • Co-chaperone CHIP associates with expanded polyglutamine protein and promotes their degradation by proteasomes
    • Jana N.R., Dikshit P., Goswami A., et al. Co-chaperone CHIP associates with expanded polyglutamine protein and promotes their degradation by proteasomes. J Biol Chem 2005, 280:11635-11640.
    • (2005) J Biol Chem , vol.280 , pp. 11635-11640
    • Jana, N.R.1    Dikshit, P.2    Goswami, A.3
  • 192
    • 63049132756 scopus 로고    scopus 로고
    • Acetylation targets mutant huntingtin to autophagosomes for degradation
    • Jeong H., Then F., Melia T.J., et al. Acetylation targets mutant huntingtin to autophagosomes for degradation. Cell 2009, 137:60-72.
    • (2009) Cell , vol.137 , pp. 60-72
    • Jeong, H.1    Then, F.2    Melia, T.J.3
  • 193
    • 0028904293 scopus 로고
    • Evidence from antibody studies that the CAG repeat in the Huntington disease gene is expressed in the protein
    • Jou Y.S., Myers R.M. Evidence from antibody studies that the CAG repeat in the Huntington disease gene is expressed in the protein. Hum Mol Genet 1995, 4:465-469.
    • (1995) Hum Mol Genet , vol.4 , pp. 465-469
    • Jou, Y.S.1    Myers, R.M.2
  • 194
    • 0034625562 scopus 로고    scopus 로고
    • The expanded CAG repeat associated with juvenile Huntington disease shows a common origin of most or all neurons and glia in human cerebrum
    • Kahlem P., Djian P. The expanded CAG repeat associated with juvenile Huntington disease shows a common origin of most or all neurons and glia in human cerebrum. Neurosci Lett 2000, 286:203-207.
    • (2000) Neurosci Lett , vol.286 , pp. 203-207
    • Kahlem, P.1    Djian, P.2
  • 195
    • 9444239187 scopus 로고    scopus 로고
    • Huntingtin is ubiquitinated and interacts with a specific ubiquitin-conjugating enzyme
    • Kalchman M.A., Graham R.K., Xia G., et al. Huntingtin is ubiquitinated and interacts with a specific ubiquitin-conjugating enzyme. J Biol Chem 1996, 271:19385-19394.
    • (1996) J Biol Chem , vol.271 , pp. 19385-19394
    • Kalchman, M.A.1    Graham, R.K.2    Xia, G.3
  • 196
    • 0030986659 scopus 로고    scopus 로고
    • HIP1, a human homologue of S. cerevisiae Sla2p, interacts with membrane-associated huntingtin in the brain
    • Kalchman M.A., Koide H.B., 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
  • 197
    • 34249715853 scopus 로고    scopus 로고
    • Huntingtin interacting proteins are genetic modifiers of neurodegeneration
    • Kaltenbach L.S., Romero E., Becklin R.R., et al. Huntingtin interacting proteins are genetic modifiers of neurodegeneration. PLoS Genet 2007, 3:e82.
    • (2007) PLoS Genet , vol.3
    • Kaltenbach, L.S.1    Romero, E.2    Becklin, R.R.3
  • 198
    • 57749183941 scopus 로고    scopus 로고
    • Neural palmitoyl-proteomics reveals dynamic synaptic palmitoylation
    • Kang R., Wan J., Arstikaitis P., et al. Neural palmitoyl-proteomics reveals dynamic synaptic palmitoylation. Nature 2008, 456:904-909.
    • (2008) Nature , vol.456 , pp. 904-909
    • Kang, R.1    Wan, J.2    Arstikaitis, P.3
  • 199
    • 33744781583 scopus 로고    scopus 로고
    • Selective striatal neuron loss and alterations in behavior correlate with impaired striatal function in Huntington's disease transgenic rats
    • Kantor O., Temel Y., Holzmann C., et al. Selective striatal neuron loss and alterations in behavior correlate with impaired striatal function in Huntington's disease transgenic rats. Neurobiol Dis 2006, 22:538-547.
    • (2006) Neurobiol Dis , vol.22 , pp. 538-547
    • Kantor, O.1    Temel, Y.2    Holzmann, C.3
  • 200
    • 0032517139 scopus 로고    scopus 로고
    • Characterization of the Huntington's disease (HD) gene homologue in the zebrafish Danio rerio
    • Karlovich C.A., John R.M., Ramirez L., et al. Characterization of the Huntington's disease (HD) gene homologue in the zebrafish Danio rerio. Gene 1998, 217:117-125.
    • (1998) Gene , vol.217 , pp. 117-125
    • Karlovich, C.A.1    John, R.M.2    Ramirez, L.3
  • 201
    • 0141594767 scopus 로고    scopus 로고
    • Neural expression of the Huntington's disease gene as a chordate evolutionary novelty
    • Kauffman J.S., Zinovyeva A., Yagi K., et al. Neural expression of the Huntington's disease gene as a chordate evolutionary novelty. J Exp Zoolog B Mol Dev Evol 2003, 297:57-64.
    • (2003) J Exp Zoolog B Mol Dev Evol , vol.297 , pp. 57-64
    • Kauffman, J.S.1    Zinovyeva, A.2    Yagi, K.3
  • 202
    • 0028143527 scopus 로고
    • CAG expansions in a novel gene for Machado-Joseph disease at chromosome 14q32.1
    • Kawaguchi Y., Okamoto T., Taniwaki M., et al. CAG expansions in a novel gene for Machado-Joseph disease at chromosome 14q32.1. Nat Genet 1994, 8:221-228.
    • (1994) Nat Genet , vol.8 , pp. 221-228
    • Kawaguchi, Y.1    Okamoto, T.2    Taniwaki, M.3
  • 203
    • 18544379477 scopus 로고    scopus 로고
    • A bivalent Huntingtin binding peptide suppresses polyglutamine aggregation and pathogenesis in Drosophila
    • Kazantsev A., Walker H.A., Slepko N., et al. A bivalent Huntingtin binding peptide suppresses polyglutamine aggregation and pathogenesis in Drosophila. Nat Genet 2002, 30:367-376.
    • (2002) Nat Genet , vol.30 , pp. 367-376
    • Kazantsev, A.1    Walker, H.A.2    Slepko, N.3
  • 204
    • 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
  • 205
    • 0034307476 scopus 로고    scopus 로고
    • Huntingtin expression stimulates endosomal-lysosomal activity, endosome tubulation, and autophagy
    • Kegel K.B., Kim M., Sapp E., et al. Huntingtin expression stimulates endosomal-lysosomal activity, endosome tubulation, and autophagy. J Neurosci 2000, 20:7268-7278.
    • (2000) J Neurosci , vol.20 , pp. 7268-7278
    • Kegel, K.B.1    Kim, M.2    Sapp, E.3
  • 206
    • 18544368523 scopus 로고    scopus 로고
    • Huntingtin is present in the nucleus, interacts with the transcriptional corepressor C-terminal binding protein, and represses transcription
    • Kegel K.B., Meloni A.R., Yi Y., et al. Huntingtin is present in the nucleus, interacts with the transcriptional corepressor C-terminal binding protein, and represses transcription. J Biol Chem 2002, 277:7466-7476.
    • (2002) J Biol Chem , vol.277 , pp. 7466-7476
    • Kegel, K.B.1    Meloni, A.R.2    Yi, Y.3
  • 207
    • 2442702838 scopus 로고    scopus 로고
    • AAV-mediated gene delivery of BDNF or GDNF is neuroprotective in a model of Huntington disease
    • Kells A.P., Fong D.M., Dragunow M., et al. AAV-mediated gene delivery of BDNF or GDNF is neuroprotective in a model of Huntington disease. Mol Ther 2004, 9:682-688.
    • (2004) Mol Ther , vol.9 , pp. 682-688
    • Kells, A.P.1    Fong, D.M.2    Dragunow, M.3
  • 208
    • 0034641887 scopus 로고    scopus 로고
    • Dramatic mutation instability in HD mouse striatum: does polyglutamine load contribute to cell-specific vulnerability in Huntington's disease?
    • Kennedy L., Shelbourne P.F. Dramatic mutation instability in HD mouse striatum: does polyglutamine load contribute to cell-specific vulnerability in Huntington's disease?. Hum Mol Genet 2000, 9:2539-2544.
    • (2000) Hum Mol Genet , vol.9 , pp. 2539-2544
    • Kennedy, L.1    Shelbourne, P.F.2
  • 209
    • 0346752132 scopus 로고    scopus 로고
    • Dramatic tissue-specific mutation length increases are an early molecular event in Huntington disease pathogenesis
    • Kennedy L., Evans E., Chen C.M., et al. Dramatic tissue-specific mutation length increases are an early molecular event in Huntington disease pathogenesis. Hum Mol Genet 2003, 12:3359-3367.
    • (2003) Hum Mol Genet , vol.12 , pp. 3359-3367
    • Kennedy, L.1    Evans, E.2    Chen, C.M.3
  • 210
    • 33847694688 scopus 로고    scopus 로고
    • Autopsy-proven Huntington's disease with 29 trinucleotide repeats
    • Kenney C., Powell S., Jankovic J. Autopsy-proven Huntington's disease with 29 trinucleotide repeats. Mov Disord 2007, 22:127-130.
    • (2007) Mov Disord , vol.22 , pp. 127-130
    • Kenney, C.1    Powell, S.2    Jankovic, J.3
  • 211
    • 0032587646 scopus 로고    scopus 로고
    • Forskolin and dopamine D1 receptor activation increase huntingtin's association with endosomes in immortalized neuronal cells of striatal origin
    • Kim M., Velier J., Chase K., et al. Forskolin and dopamine D1 receptor activation increase huntingtin's association with endosomes in immortalized neuronal cells of striatal origin. Neuroscience 1999, 89:1159-1167.
    • (1999) Neuroscience , vol.89 , pp. 1159-1167
    • Kim, M.1    Velier, J.2    Chase, K.3
  • 212
    • 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 H.S., 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
  • 213
    • 0042190049 scopus 로고    scopus 로고
    • Huntingtin is degraded to small fragments by calpain after ischemic injury
    • Kim M., Roh J.K., Yoon B.W., et al. Huntingtin is degraded to small fragments by calpain after ischemic injury. Exp Neurol 2003, 183:109-115.
    • (2003) Exp Neurol , vol.183 , pp. 109-115
    • Kim, M.1    Roh, J.K.2    Yoon, B.W.3
  • 214
    • 43049168861 scopus 로고    scopus 로고
    • Altered histone monoubiquitylation mediated by mutant huntingtin induces transcriptional dysregulation
    • Kim M.O., Chawla P., Overland R.P., et al. Altered histone monoubiquitylation mediated by mutant huntingtin induces transcriptional dysregulation. J Neurosci 2008, 28:3947-3957.
    • (2008) J Neurosci , vol.28 , pp. 3947-3957
    • Kim, M.O.1    Chawla, P.2    Overland, R.P.3
  • 215
    • 0035940412 scopus 로고    scopus 로고
    • Caspase 3-cleaved N-terminal fragments of wild-type and mutant huntingtin are present in normal and Huntington's disease brains, associate with membranes, and undergo calpain-dependent proteolysis
    • Kim Y.J., Yi Y., Sapp E., et al. Caspase 3-cleaved N-terminal fragments of wild-type and mutant huntingtin are present in normal and Huntington's disease brains, associate with membranes, and undergo calpain-dependent proteolysis. Proc Natl Acad Sci U S A 2001, 98:12784-12789.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 12784-12789
    • Kim, Y.J.1    Yi, Y.2    Sapp, E.3
  • 216
    • 33646121970 scopus 로고    scopus 로고
    • Lysosomal proteases are involved in generation of N-terminal huntingtin fragments
    • Kim Y.J., Sapp E., Cuiffo B.G., et al. Lysosomal proteases are involved in generation of N-terminal huntingtin fragments. Neurobiol Dis 2006, 22:346-356.
    • (2006) Neurobiol Dis , vol.22 , pp. 346-356
    • Kim, Y.J.1    Sapp, E.2    Cuiffo, B.G.3
  • 217
    • 0028216760 scopus 로고
    • Unstable expansion of CAG repeat in hereditary dentatorubral-pallidoluysian atrophy (DRPLA)
    • Koide R., Ikeuchi T., Onodera O., et al. Unstable expansion of CAG repeat in hereditary dentatorubral-pallidoluysian atrophy (DRPLA). Nat Genet 1994, 6:9-13.
    • (1994) Nat Genet , vol.6 , pp. 9-13
    • Koide, R.1    Ikeuchi, T.2    Onodera, O.3
  • 218
    • 0032885515 scopus 로고    scopus 로고
    • A neurological disease caused by an expanded CAG trinucleotide repeat in the TATA-binding protein gene: a new polyglutamine disease?
    • Koide R., Kobayashi S., Shimohata T., et al. A neurological disease caused by an expanded CAG trinucleotide repeat in the TATA-binding protein gene: a new polyglutamine disease?. Hum Mol Genet 1999, 8:2047-2053.
    • (1999) Hum Mol Genet , vol.8 , pp. 2047-2053
    • Koide, R.1    Kobayashi, S.2    Shimohata, T.3
  • 219
    • 0032900772 scopus 로고    scopus 로고
    • An untranslated CTG expansion causes a novel form of spinocerebellar ataxia (SCA8)
    • Koob M.D., Moseley M.L., Schut L.J., et al. An untranslated CTG expansion causes a novel form of spinocerebellar ataxia (SCA8). Nat Genet 1999, 21:379-384.
    • (1999) Nat Genet , vol.21 , pp. 379-384
    • Koob, M.D.1    Moseley, M.L.2    Schut, L.J.3
  • 220
    • 0031044805 scopus 로고    scopus 로고
    • Energy metabolism defects in Huntington's disease and effects of coenzyme Q10
    • Koroshetz W.J., Jenkins B.G., Rosen B.R., et al. 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
  • 221
    • 0031127812 scopus 로고    scopus 로고
    • Huntingtin immunoreactivity in the rat neostriatum: differential accumulation in projection and interneurons
    • Kosinski C.M., Cha J.H., Young A.B., et al. Huntingtin immunoreactivity in the rat neostriatum: differential accumulation in projection and interneurons. Exp Neurol 1997, 144:239-247.
    • (1997) Exp Neurol , vol.144 , pp. 239-247
    • Kosinski, C.M.1    Cha, J.H.2    Young, A.B.3
  • 222
    • 38049100631 scopus 로고    scopus 로고
    • Features of trinucleotide repeat instability in vivo
    • Kovtun I.V., McMurray C.T. Features of trinucleotide repeat instability in vivo. Cell Res 2008, 18:198-213.
    • (2008) Cell Res , vol.18 , pp. 198-213
    • Kovtun, I.V.1    McMurray, C.T.2
  • 223
    • 0034893312 scopus 로고    scopus 로고
    • Structural features of trinucleotide repeats associated with DNA expansion
    • Kovtun I.V., Goellner G., McMurray C.T. Structural features of trinucleotide repeats associated with DNA expansion. Biochem Cell Biol 2001, 79:325-336.
    • (2001) Biochem Cell Biol , vol.79 , pp. 325-336
    • Kovtun, I.V.1    Goellner, G.2    McMurray, C.T.3
  • 224
    • 0028316870 scopus 로고
    • A worldwide study of the Huntington's disease mutation. The sensitivity and specificity of measuring CAG repeats
    • Kremer B., Goldberg P., Andrew S.E., et al. A worldwide study of the Huntington's disease mutation. The sensitivity and specificity of measuring CAG repeats. N Engl J Med 1994, 330:1401-1406.
    • (1994) N Engl J Med , vol.330 , pp. 1401-1406
    • Kremer, B.1    Goldberg, P.2    Andrew, S.E.3
  • 225
    • 0034652127 scopus 로고    scopus 로고
    • Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins
    • Krobitsch S., Lindquist S. Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins. Proc Natl Acad Sci U S A 2000, 97:1589-1594.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 1589-1594
    • Krobitsch, S.1    Lindquist, S.2
  • 226
    • 0021909713 scopus 로고
    • Local cerebral glucose utilization in symptomatic and presymptomatic Huntington's disease
    • Kuhl D.E., Markham C.H., Metter E.J., et al. Local cerebral glucose utilization in symptomatic and presymptomatic Huntington's disease. Res Publ Assoc Res Nerv Ment Dis 1985, 63:199-209.
    • (1985) Res Publ Assoc Res Nerv Ment Dis , vol.63 , pp. 199-209
    • Kuhl, D.E.1    Markham, C.H.2    Metter, E.J.3
  • 227
    • 34547839797 scopus 로고    scopus 로고
    • Mutant huntingtin's effects on striatal gene expression in mice recapitulate changes observed in human Huntington's disease brain and do not differ with mutant huntingtin length or wild-type huntingtin dosage
    • Kuhn A., Goldstein D.R., Hodges A., et al. Mutant huntingtin's effects on striatal gene expression in mice recapitulate changes observed in human Huntington's disease brain and do not differ with mutant huntingtin length or wild-type huntingtin dosage. Hum Mol Genet 2007, 16:1845-1861.
    • (2007) Hum Mol Genet , vol.16 , pp. 1845-1861
    • Kuhn, A.1    Goldstein, D.R.2    Hodges, A.3
  • 228
    • 0033546889 scopus 로고    scopus 로고
    • DNA analysis of Huntington's disease: five years of experience in Germany, Austria, and Switzerland
    • Laccone F., Engel U., Holinski-Feder E., et al. DNA analysis of Huntington's disease: five years of experience in Germany, Austria, and Switzerland. Neurology 1999, 53:801-806.
    • (1999) Neurology , vol.53 , pp. 801-806
    • Laccone, F.1    Engel, U.2    Holinski-Feder, E.3
  • 229
    • 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 G.A., 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, 21:9112-9123.
    • (2001) J Neurosci , vol.21 , pp. 9112-9123
    • Laforet, G.A.1    Sapp, E.2    Chase, K.3
  • 230
    • 0028891145 scopus 로고
    • Huntington's Disease Gene: Regional and cellular expression in brain of normal and affected individuals
    • Landwehrmeyer G.B., McNeil S.M., Dure L.S., et al. Huntington's Disease Gene: Regional and cellular expression in brain of normal and affected individuals. Ann Neurol 1995, 37:218-230.
    • (1995) Ann Neurol , vol.37 , pp. 218-230
    • Landwehrmeyer, G.B.1    McNeil, S.M.2    Dure, L.S.3
  • 231
    • 0025800526 scopus 로고
    • Androgen receptor gene mutations in X-linked spinal and bulbar muscular atrophy
    • La Spada A.R., Wilson E.M., Lubahn D.B., et al. Androgen receptor gene mutations in X-linked spinal and bulbar muscular atrophy. Nature 1991, 352:77-79.
    • (1991) Nature , vol.352 , pp. 77-79
    • La Spada, A.R.1    Wilson, E.M.2    Lubahn, D.B.3
  • 232
    • 0027023516 scopus 로고
    • Meiotic stability and genotype-phenotype correlation of the trinucleotide repeat in X-linked spinal and bulbar muscular atrophy
    • La Spada A.R., Roling D.B., Harding A.E., et al. Meiotic stability and genotype-phenotype correlation of the trinucleotide repeat in X-linked spinal and bulbar muscular atrophy. Nat Genet 1992, 2:301-304.
    • (1992) Nat Genet , vol.2 , pp. 301-304
    • La Spada, A.R.1    Roling, D.B.2    Harding, A.E.3
  • 233
    • 0035127907 scopus 로고    scopus 로고
    • Wild-type huntingtin reduces the cellular toxicity of mutant huntingtin in vivo
    • Leavitt B.R., Guttman J.A., Hodgson J.G., et al. Wild-type huntingtin reduces the cellular toxicity of mutant huntingtin in vivo. Am J Hum Genet 2001, 68:313-324.
    • (2001) Am J Hum Genet , vol.68 , pp. 313-324
    • Leavitt, B.R.1    Guttman, J.A.2    Hodgson, J.G.3
  • 234
    • 0036928594 scopus 로고    scopus 로고
    • An upstream open reading frame impedes translation of the huntingtin gene
    • Lee J., Park E.H., Couture G., et al. An upstream open reading frame impedes translation of the huntingtin gene. Nucleic Acids Res 2002, 30:5110-5119.
    • (2002) Nucleic Acids Res , vol.30 , pp. 5110-5119
    • Lee, J.1    Park, E.H.2    Couture, G.3
  • 235
    • 37649005234 scopus 로고    scopus 로고
    • Autophagy in the pathogenesis of disease
    • Levine B., Kroemer G. Autophagy in the pathogenesis of disease. Cell 2008, 132:27-42.
    • (2008) Cell , vol.132 , pp. 27-42
    • Levine, B.1    Kroemer, G.2
  • 236
    • 0034426013 scopus 로고    scopus 로고
    • Amino-terminal fragments of mutant huntingtin show selective accumulation in striatal neurons and synaptic toxicity
    • Li H., Li S.H., Johnston H., et al. Amino-terminal fragments of mutant huntingtin show selective accumulation in striatal neurons and synaptic toxicity. Nat Genet 2000, 25:385-389.
    • (2000) Nat Genet , vol.25 , pp. 385-389
    • Li, H.1    Li, S.H.2    Johnston, H.3
  • 237
    • 0041385579 scopus 로고    scopus 로고
    • A genome scan for modifiers of age at onset in Huntington disease: The HD MAPS study
    • Li J.L., Hayden M.R., Almqvist E.W., et al. A genome scan for modifiers of age at onset in Huntington disease: The HD MAPS study. Am J Hum Genet 2003, 73:682-687.
    • (2003) Am J Hum Genet , vol.73 , pp. 682-687
    • Li, J.L.1    Hayden, M.R.2    Almqvist, E.W.3
  • 238
    • 0027484673 scopus 로고
    • Huntington's Disease Gene (IT15) is widely expressed in human and rat tissues
    • Li S.H., Schilling G., Young W.S., et al. Huntington's Disease Gene (IT15) is widely expressed in human and rat tissues. Neuron 1993, 11:985-993.
    • (1993) Neuron , vol.11 , pp. 985-993
    • Li, S.H.1    Schilling, G.2    Young, W.S.3
  • 239
    • 0032519646 scopus 로고    scopus 로고
    • Interaction of huntingtin-associated protein with dynactin P150Glued
    • Li S.H., Gutekunst C.A., Hersch S.M., et al. Interaction of huntingtin-associated protein with dynactin P150Glued. J Neurosci 1998, 18:1261-1269.
    • (1998) J Neurosci , vol.18 , pp. 1261-1269
    • Li, S.H.1    Gutekunst, C.A.2    Hersch, S.M.3
  • 240
    • 0032563107 scopus 로고    scopus 로고
    • A human HAP1 homologue. Cloning, expression, and interaction with huntingtin
    • Li S.H., Hosseini S.H., Gutekunst C.A., et al. A human HAP1 homologue. Cloning, expression, and interaction with huntingtin. J Biol Chem 1998, 273:19220-19227.
    • (1998) J Biol Chem , vol.273 , pp. 19220-19227
    • Li, S.H.1    Hosseini, S.H.2    Gutekunst, C.A.3
  • 241
    • 0033168302 scopus 로고    scopus 로고
    • Cellular defects and altered gene expression in PC12 cells stably expressing mutant huntingtin
    • Li S.H., Cheng A.L., Li H., et al. Cellular defects and altered gene expression in PC12 cells stably expressing mutant huntingtin. J Neurosci 1999, 19:5159-5172.
    • (1999) J Neurosci , vol.19 , pp. 5159-5172
    • Li, S.H.1    Cheng, A.L.2    Li, H.3
  • 242
    • 0032855148 scopus 로고    scopus 로고
    • A putative Drosophila homolog of the Huntington's disease gene
    • Li Z., Karlovich C.A., Fish M.P., et al. A putative Drosophila homolog of the Huntington's disease gene. Hum Mol Genet 1999, 8:1807-1815.
    • (1999) Hum Mol Genet , vol.8 , pp. 1807-1815
    • Li, Z.1    Karlovich, C.A.2    Fish, M.P.3
  • 243
    • 0036173896 scopus 로고    scopus 로고
    • Interaction of Huntington disease protein with transcriptional activator Sp1
    • Li S.H., Cheng A.L., Zhou H., et al. Interaction of Huntington disease protein with transcriptional activator Sp1. Mol Cell Biol 2002, 22:1277-1287.
    • (2002) Mol Cell Biol , vol.22 , pp. 1277-1287
    • Li, S.H.1    Cheng, A.L.2    Zhou, H.3
  • 244
    • 0028803757 scopus 로고
    • A huntingtin-associated protein enriched in brain with implications for pathology
    • Li X.J., Li S.H., Sharp A.H., et al. A huntingtin-associated protein enriched in brain with implications for pathology. Nature 1995, 378:398-402.
    • (1995) Nature , vol.378 , pp. 398-402
    • Li, X.J.1    Li, S.H.2    Sharp, A.H.3
  • 245
    • 33744921670 scopus 로고    scopus 로고
    • Expression and characterization of full-length human huntingtin, an elongated HEAT repeat protein
    • Li W., Serpell L.C., Carter W.J., et al. Expression and characterization of full-length human huntingtin, an elongated HEAT repeat protein. J Biol Chem 2006, 281:15916-15922.
    • (2006) J Biol Chem , vol.281 , pp. 15916-15922
    • Li, W.1    Serpell, L.C.2    Carter, W.J.3
  • 246
    • 0027370252 scopus 로고
    • Differential 3' polyadenylation of the Huntington disease gene results in two mRNA species with variable tissue expression
    • Lin B., Rommens J.M., Graham R.K., et al. Differential 3' polyadenylation of the Huntington disease gene results in two mRNA species with variable tissue expression. Hum Mol Genet 1993, 2:1541-1545.
    • (1993) Hum Mol Genet , vol.2 , pp. 1541-1545
    • Lin, B.1    Rommens, J.M.2    Graham, R.K.3
  • 247
    • 0028049296 scopus 로고
    • Sequence of the murine Huntington disease gene: evidence for conservation, alternate splicing and polymorphism in a triplet (CCG) repeat [corrected]
    • Lin B., Nasir J., MacDonald H., et al. Sequence of the murine Huntington disease gene: evidence for conservation, alternate splicing and polymorphism in a triplet (CCG) repeat [corrected]. Hum Mol Genet 1994, 3:85-92.
    • (1994) Hum Mol Genet , vol.3 , pp. 85-92
    • Lin, B.1    Nasir, J.2    MacDonald, H.3
  • 248
    • 0028920823 scopus 로고
    • Structural analysis of the 5' region of mouse and human Huntington disease genes reveals conservation of putative promoter region and di- and trinucleotide polymorphisms
    • Lin B., Nasir J., Kalchman M.A., et al. Structural analysis of the 5' region of mouse and human Huntington disease genes reveals conservation of putative promoter region and di- and trinucleotide polymorphisms. Genomics 1995, 25:707-715.
    • (1995) Genomics , vol.25 , pp. 707-715
    • Lin, B.1    Nasir, J.2    Kalchman, M.A.3
  • 249
    • 0035862896 scopus 로고    scopus 로고
    • Neurological abnormalities in a knock-in mouse model of Huntington's disease
    • Lin C.H., Tallaksen-Greene S., Chien W.M., et al. Neurological abnormalities in a knock-in mouse model of Huntington's disease. Hum Mol Genet 2001, 10:137-144.
    • (2001) Hum Mol Genet , vol.10 , pp. 137-144
    • Lin, C.H.1    Tallaksen-Greene, S.2    Chien, W.M.3
  • 250
    • 0026322296 scopus 로고
    • New DNA markers in the Huntington's disease gene candidate region
    • Lin C.S., Altherr M., Bates G., et al. New DNA markers in the Huntington's disease gene candidate region. Somat Cell Mol Genet 1991, 17:481-488.
    • (1991) Somat Cell Mol Genet , vol.17 , pp. 481-488
    • Lin, C.S.1    Altherr, M.2    Bates, G.3
  • 251
    • 65249130165 scopus 로고    scopus 로고
    • Transcription destabilizes triplet repeats
    • Lin Y., Hubert L., Wilson J.H. Transcription destabilizes triplet repeats. Mol Carcinog 2008, 48:350-361.
    • (2008) Mol Carcinog , vol.48 , pp. 350-361
    • Lin, Y.1    Hubert, L.2    Wilson, J.H.3
  • 252
    • 44649135155 scopus 로고    scopus 로고
    • Regulation of the sumoylation system in gene expression
    • Liu B., Shuai K. Regulation of the sumoylation system in gene expression. Curr Opin Cell Biol 2008, 20:288-293.
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 288-293
    • Liu, B.1    Shuai, K.2
  • 253
    • 0000790724 scopus 로고    scopus 로고
    • SH3 domain-dependent association of huntingtin with epidermal growth factor receptor signaling complexes
    • Liu Y.F., Deth R.C., Devys D. SH3 domain-dependent association of huntingtin with epidermal growth factor receptor signaling complexes. J Biol Chem 1997, 272:8121-8124.
    • (1997) J Biol Chem , vol.272 , pp. 8121-8124
    • Liu, Y.F.1    Deth, R.C.2    Devys, D.3
  • 254
    • 0001583878 scopus 로고    scopus 로고
    • Activation of MLK2-mediated signaling cascades by polyglutamine-expanded huntingtin
    • Liu Y.F., Dorow D., Marshall J. Activation of MLK2-mediated signaling cascades by polyglutamine-expanded huntingtin. J Biol Chem 2000, 275:19035-19040.
    • (2000) J Biol Chem , vol.275 , pp. 19035-19040
    • Liu, Y.F.1    Dorow, D.2    Marshall, J.3
  • 255
    • 33745593763 scopus 로고    scopus 로고
    • Genetic background modifies nuclear mutant huntingtin accumulation and HD CAG repeat instability in Huntington's disease knock-in mice
    • Lloret A., Dragileva E., Teed A., et al. Genetic background modifies nuclear mutant huntingtin accumulation and HD CAG repeat instability in Huntington's disease knock-in mice. Hum Mol Genet 2006, 15:2015-2024.
    • (2006) Hum Mol Genet , vol.15 , pp. 2015-2024
    • Lloret, A.1    Dragileva, E.2    Teed, A.3
  • 256
    • 19244384619 scopus 로고    scopus 로고
    • Frequency of the different mutations causing spinocerebellar ataxia (SCA1, SCA2, MJD/SCA3 and DRPLA) in a large group of Brazilian patients
    • Lopes-Cendes I., Teive H.G., Calcagnotto M.E., et al. Frequency of the different mutations causing spinocerebellar ataxia (SCA1, SCA2, MJD/SCA3 and DRPLA) in a large group of Brazilian patients. Arq Neuropsiquiatr 1997, 55:519-529.
    • (1997) Arq Neuropsiquiatr , vol.55 , pp. 519-529
    • Lopes-Cendes, I.1    Teive, H.G.2    Calcagnotto, M.E.3
  • 257
    • 0030968169 scopus 로고    scopus 로고
    • Patterns of meiotic variability of the (CAG)n repeat in the Huntington disease gene
    • Lucotte G., Gerard N., Aouizerate A., et al. Patterns of meiotic variability of the (CAG)n repeat in the Huntington disease gene. Genet Couns 1997, 8:77-81.
    • (1997) Genet Couns , vol.8 , pp. 77-81
    • Lucotte, G.1    Gerard, N.2    Aouizerate, A.3
  • 258
    • 34548406422 scopus 로고    scopus 로고
    • Huntingtin-deficient zebrafish exhibit defects in iron utilization and development
    • Lumsden A.L., Henshall T.L., Dayan S., et al. Huntingtin-deficient zebrafish exhibit defects in iron utilization and development. Hum Mol Genet 2007, 16:1905-1920.
    • (2007) Hum Mol Genet , vol.16 , pp. 1905-1920
    • Lumsden, A.L.1    Henshall, T.L.2    Dayan, S.3
  • 259
    • 0031680014 scopus 로고    scopus 로고
    • A cellular model that recapitulates major pathogenic steps of Huntington's disease
    • Lunkes A., Mandel J.L. 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
  • 260
    • 0032248397 scopus 로고    scopus 로고
    • Pathological mechanisms in Huntington's disease and other polyglutamine expansion diseases
    • Lunkes A., Trottier Y., Mandel J.L. Pathological mechanisms in Huntington's disease and other polyglutamine expansion diseases. Essays Biochem 1998, 33:149-163.
    • (1998) Essays Biochem , vol.33 , pp. 149-163
    • Lunkes, A.1    Trottier, Y.2    Mandel, J.L.3
  • 261
    • 0036671821 scopus 로고    scopus 로고
    • Proteases acting on mutant huntingtin generate cleaved products that differentially build up cytoplasmic and nuclear inclusions
    • Lunkes A., Lindenberg K.S., Ben-Haiem L., et al. Proteases acting on mutant huntingtin generate cleaved products that differentially build up cytoplasmic and nuclear inclusions. Mol Cell 2002, 10:259-269.
    • (2002) Mol Cell , vol.10 , pp. 259-269
    • Lunkes, A.1    Lindenberg, K.S.2    Ben-Haiem, L.3
  • 262
    • 66949178049 scopus 로고    scopus 로고
    • Huntingtin promotes cell survival by preventing Pak2 cleavage
    • Luo S., Rubinsztein D.C. Huntingtin promotes cell survival by preventing Pak2 cleavage. J Cell Sci 2009, 122:875-885.
    • (2009) J Cell Sci , vol.122 , pp. 875-885
    • Luo, S.1    Rubinsztein, D.C.2
  • 263
    • 22344439156 scopus 로고    scopus 로고
    • Cdk5 phosphorylation of huntingtin reduces its cleavage by caspases: implications for mutant huntingtin toxicity
    • Luo S., Vacher C., Davies J.E., et al. Cdk5 phosphorylation of huntingtin reduces its cleavage by caspases: implications for mutant huntingtin toxicity. J Cell Biol 2005, 169:647-656.
    • (2005) J Cell Biol , vol.169 , pp. 647-656
    • Luo, S.1    Vacher, C.2    Davies, J.E.3
  • 264
    • 40549095312 scopus 로고    scopus 로고
    • P21-activated kinase 1 promotes soluble mutant huntingtin self-interaction and enhances toxicity
    • Luo S., Mizuta H., Rubinsztein D.C. p21-activated kinase 1 promotes soluble mutant huntingtin self-interaction and enhances toxicity. Hum Mol Genet 2008, 17:895-905.
    • (2008) Hum Mol Genet , vol.17 , pp. 895-905
    • Luo, S.1    Mizuta, H.2    Rubinsztein, D.C.3
  • 265
    • 0034702030 scopus 로고    scopus 로고
    • Decreased expression of striatal signaling genes in a mouse model of Huntington's disease
    • Luthi-Carter R., Strand A., Peters N.L., et al. Decreased expression of striatal signaling genes in a mouse model of Huntington's disease. Hum Mol Genet 2000, 9:1259-1271.
    • (2000) Hum Mol Genet , vol.9 , pp. 1259-1271
    • Luthi-Carter, R.1    Strand, A.2    Peters, N.L.3
  • 266
    • 1542674455 scopus 로고    scopus 로고
    • Huntingtin: alive and well and working in middle management
    • MacDonald M.E. Huntingtin: alive and well and working in middle management. Sci STKE 2003, pe48.
    • (2003) Sci STKE
    • MacDonald, M.E.1
  • 267
    • 0026864956 scopus 로고
    • The Huntington's disease candidate region exhibits many different haplotypes
    • MacDonald M.E., Novelletto A., Lin C., et al. The Huntington's disease candidate region exhibits many different haplotypes. Nat Genet 1992, 1:99-103.
    • (1992) Nat Genet , vol.1 , pp. 99-103
    • MacDonald, M.E.1    Novelletto, A.2    Lin, C.3
  • 268
    • 0027363951 scopus 로고
    • Gametic but not somatic instability of CAG repeat length in Huntington's disease
    • MacDonald M.E., Barnes G., Srinidhi J., et al. Gametic but not somatic instability of CAG repeat length in Huntington's disease. J Med Genet 1993, 30:982-986.
    • (1993) J Med Genet , vol.30 , pp. 982-986
    • MacDonald, M.E.1    Barnes, G.2    Srinidhi, J.3
  • 269
    • 0027436470 scopus 로고
    • Molecular analysis and clinical correlations of the Huntington's disease mutation
    • MacMillan J.C., Snell R.G., Tyler A., et al. Molecular analysis and clinical correlations of the Huntington's disease mutation. Lancet 1993, 342:954-958.
    • (1993) Lancet , vol.342 , pp. 954-958
    • MacMillan, J.C.1    Snell, R.G.2    Tyler, A.3
  • 270
    • 31544472070 scopus 로고    scopus 로고
    • Huntingtin fragmentation and increased caspase 3, 8 and 9 activities in lymphoblasts with heterozygous and homozygous Huntington's disease mutation
    • Maglione V., Cannella M., Gradini R., et al. Huntingtin fragmentation and increased caspase 3, 8 and 9 activities in lymphoblasts with heterozygous and homozygous Huntington's disease mutation. Mech Ageing Dev 2006, 127:213-216.
    • (2006) Mech Ageing Dev , vol.127 , pp. 213-216
    • Maglione, V.1    Cannella, M.2    Gradini, R.3
  • 271
    • 0026603841 scopus 로고
    • Myotonic dystrophy mutation: an unstable CTG repeat in the 3' untranslated region of the gene
    • Mahadevan M., Tsilfidis C., Sabourin L., et al. Myotonic dystrophy mutation: an unstable CTG repeat in the 3' untranslated region of the gene. Science 1992, 255:1253-1255.
    • (1992) Science , vol.255 , pp. 1253-1255
    • Mahadevan, M.1    Tsilfidis, C.2    Sabourin, L.3
  • 272
    • 38649110478 scopus 로고    scopus 로고
    • Increased caspase-2, calpain activations and decreased mitochondrial complex II activity in cells expressing exogenous huntingtin exon 1 containing CAG repeat in the pathogenic range
    • Majumder P., Raychaudhuri S., Chattopadhyay B., et al. Increased caspase-2, calpain activations and decreased mitochondrial complex II activity in cells expressing exogenous huntingtin exon 1 containing CAG repeat in the pathogenic range. Cell Mol Neurobiol 2007, 27:1127-1145.
    • (2007) Cell Mol Neurobiol , vol.27 , pp. 1127-1145
    • Majumder, P.1    Raychaudhuri, S.2    Chattopadhyay, B.3
  • 273
    • 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 K., 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, K.2    Seller, M.3
  • 274
    • 0031056685 scopus 로고    scopus 로고
    • Instability of highly expanded CAG repeats in mice transgenic for the Huntington's disease mutation
    • Mangiarini L., Sathasivam K., Mahal A., et al. Instability of highly expanded CAG repeats in mice transgenic for the Huntington's disease mutation. Nat Genet 1997, 15:197-200.
    • (1997) Nat Genet , vol.15 , pp. 197-200
    • Mangiarini, L.1    Sathasivam, K.2    Mahal, A.3
  • 275
    • 0033578220 scopus 로고    scopus 로고
    • Instability of the CAG repeat in immortalized fibroblast cell cultures from Huntington's disease transgenic mice
    • Manley K., Pugh J., Messer A. Instability of the CAG repeat in immortalized fibroblast cell cultures from Huntington's disease transgenic mice. Brain Res 1999, 835:74-79.
    • (1999) Brain Res , vol.835 , pp. 74-79
    • Manley, K.1    Pugh, J.2    Messer, A.3
  • 276
    • 0032708840 scopus 로고    scopus 로고
    • Msh2 deficiency prevents in vivo somatic instability of the CAG repeat in Huntington disease transgenic mice
    • Manley K., Shirley T.L., Flaherty L., et al. Msh2 deficiency prevents in vivo somatic instability of the CAG repeat in Huntington disease transgenic mice. Nat Genet 1999, 23:471-473.
    • (1999) Nat Genet , vol.23 , pp. 471-473
    • Manley, K.1    Shirley, T.L.2    Flaherty, L.3
  • 277
    • 0025078573 scopus 로고
    • Mitochondrial function and parental sex effect in Huntington's disease
    • Mann V.M., Cooper J.M., Javoy-Agid F., et al. Mitochondrial function and parental sex effect in Huntington's disease. Lancet 1990, 336:749.
    • (1990) Lancet , vol.336 , pp. 749
    • Mann, V.M.1    Cooper, J.M.2    Javoy-Agid, F.3
  • 278
    • 0029057609 scopus 로고
    • Comparison of cathepsin protease activities in brain tissue from normal cases and cases with Alzheimer's disease, Lewy body dementia, Parkinson's disease and Huntington's disease
    • Mantle D., Falkous G., Ishiura S., et al. Comparison of cathepsin protease activities in brain tissue from normal cases and cases with Alzheimer's disease, Lewy body dementia, Parkinson's disease and Huntington's disease. J Neurol Sci 1995, 131:65-70.
    • (1995) J Neurol Sci , vol.131 , pp. 65-70
    • Mantle, D.1    Falkous, G.2    Ishiura, S.3
  • 279
    • 17844389364 scopus 로고    scopus 로고
    • The wide spectrum of spinocerebellar ataxias (SCAs)
    • Manto M.U. The wide spectrum of spinocerebellar ataxias (SCAs). Cerebellum 2005, 4:2-6.
    • (2005) Cerebellum , vol.4 , pp. 2-6
    • Manto, M.U.1
  • 280
    • 33645450264 scopus 로고    scopus 로고
    • Cystamine and cysteamine prevent 3-NP-induced mitochondrial depolarization of Huntington's disease knock-in striatal cells
    • Mao Z., Choo Y.S., Lesort M. Cystamine and cysteamine prevent 3-NP-induced mitochondrial depolarization of Huntington's disease knock-in striatal cells. Eur J Neurosci 2006, 23:1701-1710.
    • (2006) Eur J Neurosci , vol.23 , pp. 1701-1710
    • Mao, Z.1    Choo, Y.S.2    Lesort, M.3
  • 281
    • 0042423684 scopus 로고    scopus 로고
    • Stimulation of NeuroD activity by huntingtin and huntingtin-associated proteins HAP1 and MLK2
    • Marcora E., Gowan K., Lee J.E. Stimulation of NeuroD activity by huntingtin and huntingtin-associated proteins HAP1 and MLK2. Proc Natl Acad Sci U S A 2003, 100:9578-9583.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 9578-9583
    • Marcora, E.1    Gowan, K.2    Lee, J.E.3
  • 282
    • 9144245757 scopus 로고    scopus 로고
    • Huntington's Disease-like 2 (HDL2) in North America and Japan
    • Margolis R.L., Holmes S.E., Rosenblatt A., et al. Huntington's Disease-like 2 (HDL2) in North America and Japan. Ann Neurol 2004, 56:670-674.
    • (2004) Ann Neurol , vol.56 , pp. 670-674
    • Margolis, R.L.1    Holmes, S.E.2    Rosenblatt, A.3
  • 283
    • 0035940532 scopus 로고    scopus 로고
    • Pathogenic effect of an intermediate-size SCA-6 allele (CAG)(19) in a homozygous patient
    • Mariotti C., Gellera C., Grisoli M., et al. Pathogenic effect of an intermediate-size SCA-6 allele (CAG)(19) in a homozygous patient. Neurology 2001, 57:1502-1504.
    • (2001) Neurology , vol.57 , pp. 1502-1504
    • Mariotti, C.1    Gellera, C.2    Grisoli, M.3
  • 284
    • 0034110465 scopus 로고    scopus 로고
    • Expanded polyglutamine peptides alone are intrinsically cytotoxic and cause neurodegeneration in Drosophila
    • Marsh J.L., Walker H., Theisen H., et al. Expanded polyglutamine peptides alone are intrinsically cytotoxic and cause neurodegeneration in Drosophila. Hum Mol Genet 2000, 9:13-25.
    • (2000) Hum Mol Genet , vol.9 , pp. 13-25
    • Marsh, J.L.1    Walker, H.2    Theisen, H.3
  • 285
    • 0036974461 scopus 로고    scopus 로고
    • Nuclear localization of N-terminal mutant huntingtin is cell cycle dependent
    • Martin-Aparicio E., Avila J., Lucas J.J. Nuclear localization of N-terminal mutant huntingtin is cell cycle dependent. Eur J Neurosci 2002, 16:355-359.
    • (2002) Eur J Neurosci , vol.16 , pp. 355-359
    • Martin-Aparicio, E.1    Avila, J.2    Lucas, J.J.3
  • 286
    • 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
  • 287
    • 0029905329 scopus 로고    scopus 로고
    • Protection of the neostriatum against excitotoxic damage by neurotrophin-producing, genetically modified neural stem cells
    • Martinez-Serrano A., Bjorklund A. Protection of the neostriatum against excitotoxic damage by neurotrophin-producing, genetically modified neural stem cells. J Neurosci 1996, 16:4604-4616.
    • (1996) J Neurosci , vol.16 , pp. 4604-4616
    • Martinez-Serrano, A.1    Bjorklund, A.2
  • 288
    • 0034306571 scopus 로고    scopus 로고
    • Identification and characterization of the miniature pig Huntington's disease gene homolog: evidence for conservation and polymorphism in the CAG triplet repeat
    • Matsuyama N., Hadano S., Onoe K., et al. Identification and characterization of the miniature pig Huntington's disease gene homolog: evidence for conservation and polymorphism in the CAG triplet repeat. Genomics 2000, 69:72-85.
    • (2000) Genomics , vol.69 , pp. 72-85
    • Matsuyama, N.1    Hadano, S.2    Onoe, K.3
  • 289
    • 8544255538 scopus 로고    scopus 로고
    • Molecular features of the CAG repeats of spinocerebellar ataxia 6 (SCA6)
    • Matsuyama Z., Kawakami H., Maruyama H., et al. Molecular features of the CAG repeats of spinocerebellar ataxia 6 (SCA6). Hum Mol Genet 1997, 6:1283-1287.
    • (1997) Hum Mol Genet , vol.6 , pp. 1283-1287
    • Matsuyama, Z.1    Kawakami, H.2    Maruyama, H.3
  • 290
    • 0031964359 scopus 로고    scopus 로고
    • Neuroprotective effects of creatine and cyclocreatine in animal models of Huntington's disease
    • Matthews R.T., Yang L., Jenkins B.G., et al. Neuroprotective effects of creatine and cyclocreatine in animal models of Huntington's disease. J Neurosci 1998, 18:156-163.
    • (1998) J Neurosci , vol.18 , pp. 156-163
    • Matthews, R.T.1    Yang, L.2    Jenkins, B.G.3
  • 291
    • 0023147905 scopus 로고
    • Reduced cerebral glucose metabolism in asymptomatic subjects at risk for Huntington's disease
    • Mazziotta J.C., Phelps M.E., Pahl J.J., et al. Reduced cerebral glucose metabolism in asymptomatic subjects at risk for Huntington's disease. N Engl J Med 1987, 316:357-362.
    • (1987) N Engl J Med , vol.316 , pp. 357-362
    • Mazziotta, J.C.1    Phelps, M.E.2    Pahl, J.J.3
  • 292
    • 0035909999 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors reduce polyglutamine toxicity
    • McCampbell A., Taye A.A., Whitty L., et al. Histone deacetylase inhibitors reduce polyglutamine toxicity. Proc Natl Acad Sci U S A 2001, 98:15179-15184.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 15179-15184
    • McCampbell, A.1    Taye, A.A.2    Whitty, L.3
  • 293
    • 0023236147 scopus 로고
    • Wolf-Hirschhorn locus is distal to D4S10 on short arm of chromosome 4
    • McKeown C., Read A.P., Dodge A., et al. Wolf-Hirschhorn locus is distal to D4S10 on short arm of chromosome 4. J Med Genet 1987, 24:410-412.
    • (1987) J Med Genet , vol.24 , pp. 410-412
    • McKeown, C.1    Read, A.P.2    Dodge, A.3
  • 294
    • 0037107191 scopus 로고    scopus 로고
    • Early motor dysfunction and striosomal distribution of huntingtin microaggregates in Huntington's disease knock-in mice
    • Menalled L.B., Sison J.D., Wu Y., et al. Early motor dysfunction and striosomal distribution of huntingtin microaggregates in Huntington's disease knock-in mice. J Neurosci 2002, 22:8266-8276.
    • (2002) J Neurosci , vol.22 , pp. 8266-8276
    • Menalled, L.B.1    Sison, J.D.2    Wu, Y.3
  • 295
    • 0041691176 scopus 로고    scopus 로고
    • Time course of early motor and neuropathological anomalies in a knock-in mouse model of Huntington's disease with 140 CAG repeats
    • Menalled L.B., Sison J.D., Dragatsis I., et al. Time course of early motor and neuropathological anomalies in a knock-in mouse model of Huntington's disease with 140 CAG repeats. J Comp Neurol 2003, 465:11-26.
    • (2003) J Comp Neurol , vol.465 , pp. 11-26
    • Menalled, L.B.1    Sison, J.D.2    Dragatsis, I.3
  • 296
    • 0035869544 scopus 로고    scopus 로고
    • Tissue-specific proteolysis of Huntingtin (htt) in human brain: evidence of enhanced levels of N- and C-terminal htt fragments in Huntington's disease striatum
    • Mende-Mueller L.M., Toneff T., Hwang S.R., et al. Tissue-specific proteolysis of Huntingtin (htt) in human brain: evidence of enhanced levels of N- and C-terminal htt fragments in Huntington's disease striatum. J Neurosci 2001, 21:1830-1837.
    • (2001) J Neurosci , vol.21 , pp. 1830-1837
    • Mende-Mueller, L.M.1    Toneff, T.2    Hwang, S.R.3
  • 297
    • 0037053566 scopus 로고    scopus 로고
    • Huntington toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1
    • Meriin A.B., Zhang X., He X., et al. Huntington toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1. J Cell Biol 2002, 157:997-1004.
    • (2002) J Cell Biol , vol.157 , pp. 997-1004
    • Meriin, A.B.1    Zhang, X.2    He, X.3
  • 298
    • 33746961204 scopus 로고    scopus 로고
    • Genetic analysis of candidate genes modifying the age-at-onset in Huntington's disease
    • Metzger S., Bauer P., Tomiuk J., et al. Genetic analysis of candidate genes modifying the age-at-onset in Huntington's disease. Hum Genet 2006, 120:285-292.
    • (2006) Hum Genet , vol.120 , pp. 285-292
    • Metzger, S.1    Bauer, P.2    Tomiuk, J.3
  • 299
    • 33644658207 scopus 로고    scopus 로고
    • The S18Y polymorphism in the UCHL1 gene is a genetic modifier in Huntington's disease
    • Metzger S., Bauer P., Tomiuk J., et al. The S18Y polymorphism in the UCHL1 gene is a genetic modifier in Huntington's disease. Neurogenetics 2006, 7:27-30.
    • (2006) Neurogenetics , vol.7 , pp. 27-30
    • Metzger, S.1    Bauer, P.2    Tomiuk, J.3
  • 300
    • 41849097772 scopus 로고    scopus 로고
    • Huntingtin-associated protein-1 is a modifier of the age-at-onset of Huntington's disease
    • Metzger S., Rong J., Nguyen H.P., et al. Huntingtin-associated protein-1 is a modifier of the age-at-onset of Huntington's disease. Hum Mol Genet 2008, 17:1137-1146.
    • (2008) Hum Mol Genet , vol.17 , pp. 1137-1146
    • Metzger, S.1    Rong, J.2    Nguyen, H.P.3
  • 301
    • 0034639717 scopus 로고    scopus 로고
    • Huntingtin is required for normal hematopoiesis
    • Metzler M., Helgason C.D., Dragatsis I., et al. Huntingtin is required for normal hematopoiesis. Hum Mol Genet 2000, 9:387-394.
    • (2000) Hum Mol Genet , vol.9 , pp. 387-394
    • Metzler, M.1    Helgason, C.D.2    Dragatsis, I.3
  • 302
    • 27144558034 scopus 로고    scopus 로고
    • CHIP suppresses polyglutamine aggregation and toxicity in vitro and in vivo
    • Miller V.M., Nelson R.F., Gouvion C.M., et al. CHIP suppresses polyglutamine aggregation and toxicity in vitro and in vivo. J Neurosci 2005, 25:9152-9161.
    • (2005) J Neurosci , vol.25 , pp. 9152-9161
    • Miller, V.M.1    Nelson, R.F.2    Gouvion, C.M.3
  • 303
    • 43149120469 scopus 로고    scopus 로고
    • E6-AP promotes misfolded polyglutamine proteins for proteasomal degradation and suppresses polyglutamine protein aggregation and toxicity
    • Mishra A., Dikshit P., Purkayastha S., et al. E6-AP promotes misfolded polyglutamine proteins for proteasomal degradation and suppresses polyglutamine protein aggregation and toxicity. J Biol Chem 2008, 283:7648-7656.
    • (2008) J Biol Chem , vol.283 , pp. 7648-7656
    • Mishra, A.1    Dikshit, P.2    Purkayastha, S.3
  • 304
    • 0024396320 scopus 로고
    • Transcriptional regulation in mammalian cells by sequence-specific DNA binding proteins
    • Mitchell P.J., Tjian R. Transcriptional regulation in mammalian cells by sequence-specific DNA binding proteins. Science 1989, 245:371-378.
    • (1989) Science , vol.245 , pp. 371-378
    • Mitchell, P.J.1    Tjian, R.2
  • 305
    • 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 N.A., Charles V., et al. PACSIN 1 interacts with huntingtin and is absent from synaptic varicosities in presymptomatic Huntington's disease brains. Hum Mol Genet 2002, 11:2547-2558.
    • (2002) Hum Mol Genet , vol.11 , pp. 2547-2558
    • Modregger, J.1    DiProspero, N.A.2    Charles, V.3
  • 306
    • 0037423214 scopus 로고    scopus 로고
    • Characterization of Endophilin B1b, a brain-specific membrane-associated lysophosphatidic acid acyl transferase with properties distinct from endophilin A1
    • Modregger J., Schmidt A.A., Ritter B., et al. Characterization of Endophilin B1b, a brain-specific membrane-associated lysophosphatidic acid acyl transferase with properties distinct from endophilin A1. J Biol Chem 2003, 278:4160-4167.
    • (2003) J Biol Chem , vol.278 , pp. 4160-4167
    • Modregger, J.1    Schmidt, A.A.2    Ritter, B.3
  • 307
    • 67649826155 scopus 로고    scopus 로고
    • Pathogenic huntingtin inhibits fast axonal transport by activating JNK3 and phosphorylating kinesin
    • Morfini G.A., You Y.M., Pollema S.L., et al. Pathogenic huntingtin inhibits fast axonal transport by activating JNK3 and phosphorylating kinesin. Nat Neurosci 2009, 12:864-871.
    • (2009) Nat Neurosci , vol.12 , pp. 864-871
    • Morfini, G.A.1    You, Y.M.2    Pollema, S.L.3
  • 308
    • 33746394263 scopus 로고    scopus 로고
    • Genotype-dependent priming to self- and xeno-cannibalism in heterozygous and homozygous lymphoblasts from patients with Huntington's disease
    • Mormone E., Matarrese P., Tinari A., et al. Genotype-dependent priming to self- and xeno-cannibalism in heterozygous and homozygous lymphoblasts from patients with Huntington's disease. J Neurochem 2006, 98:1090-1099.
    • (2006) J Neurochem , vol.98 , pp. 1090-1099
    • Mormone, E.1    Matarrese, P.2    Tinari, A.3
  • 309
    • 60849120450 scopus 로고    scopus 로고
    • Paradoxical delay in the onset of disease caused by super-long CAG repeat expansions in R6/2 mice
    • Morton A.J., Glynn D., Leavens W., et al. Paradoxical delay in the onset of disease caused by super-long CAG repeat expansions in R6/2 mice. Neurobiol Dis 2009, 33:331-341.
    • (2009) Neurobiol Dis , vol.33 , pp. 331-341
    • Morton, A.J.1    Glynn, D.2    Leavens, W.3
  • 310
    • 33745545413 scopus 로고    scopus 로고
    • Bidirectional expression of CUG and CAG expansion transcripts and intranuclear polyglutamine inclusions in spinocerebellar ataxia type 8
    • Moseley M.L., Zu T., Ikeda Y., et al. Bidirectional expression of CUG and CAG expansion transcripts and intranuclear polyglutamine inclusions in spinocerebellar ataxia type 8. Nat Genet 2006, 38:758-769.
    • (2006) Nat Genet , vol.38 , pp. 758-769
    • Moseley, M.L.1    Zu, T.2    Ikeda, Y.3
  • 311
    • 0037154229 scopus 로고    scopus 로고
    • Requirement of an intact microtubule cytoskeleton for aggregation and inclusion body formation by a mutant huntingtin fragment
    • Muchowski P.J., Ning K., D'Souza-Schorey C., et al. Requirement of an intact microtubule cytoskeleton for aggregation and inclusion body formation by a mutant huntingtin fragment. Proc Natl Acad Sci U S A 2002, 99:727-732.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 727-732
    • Muchowski, P.J.1    Ning, K.2    D'Souza-Schorey, C.3
  • 312
    • 54949140807 scopus 로고    scopus 로고
    • Protective role of Engrailed in a Drosophila model of Huntington's disease
    • Mugat B., Parmentier M.L., Bonneaud N., et al. Protective role of Engrailed in a Drosophila model of Huntington's disease. Hum Mol Genet 2008, 17:3601-3616.
    • (2008) Hum Mol Genet , vol.17 , pp. 3601-3616
    • Mugat, B.1    Parmentier, M.L.2    Bonneaud, N.3
  • 313
    • 1942437991 scopus 로고    scopus 로고
    • SUMO: a regulator of gene expression and genome integrity
    • Muller S., Ledl A., Schmidt D. SUMO: a regulator of gene expression and genome integrity. Oncogene 2004, 23:1998-2008.
    • (2004) Oncogene , vol.23 , pp. 1998-2008
    • Muller, S.1    Ledl, A.2    Schmidt, D.3
  • 314
    • 23844525922 scopus 로고    scopus 로고
    • Huntington's disease genetics
    • Myers R.H. Huntington's disease genetics. NeuroRx 2004, 1:255-262.
    • (2004) NeuroRx , vol.1 , pp. 255-262
    • Myers, R.H.1
  • 316
    • 0028060244 scopus 로고
    • Structure and expression of the gene responsible for the triplet repeat disorder, dentatorubral and pallidoluysian atrophy (DRPLA)
    • Nagafuchi S., Yanagisawa H., Ohsaki E., et al. Structure and expression of the gene responsible for the triplet repeat disorder, dentatorubral and pallidoluysian atrophy (DRPLA). Nat Genet 1994, 8:177-182.
    • (1994) Nat Genet , vol.8 , pp. 177-182
    • Nagafuchi, S.1    Yanagisawa, H.2    Ohsaki, E.3
  • 317
    • 0028335386 scopus 로고
    • Dentatorubral and pallidoluysian atrophy expansion of an unstable CAG trinucleotide on chromosome 12p
    • Nagafuchi S., Yanagisawa H., Sato K., et al. Dentatorubral and pallidoluysian atrophy expansion of an unstable CAG trinucleotide on chromosome 12p. Nat Genet 1994, 6:14-18.
    • (1994) Nat Genet , vol.6 , pp. 14-18
    • Nagafuchi, S.1    Yanagisawa, H.2    Sato, K.3
  • 318
    • 0035393427 scopus 로고    scopus 로고
    • SCA17, a novel autosomal dominant cerebellar ataxia caused by an expanded polyglutamine in TATA-binding protein
    • Nakamura K., Jeong S.Y., Uchihara T., et al. SCA17, a novel autosomal dominant cerebellar ataxia caused by an expanded polyglutamine in TATA-binding protein. Hum Mol Genet 2001, 10:1441-1448.
    • (2001) Hum Mol Genet , vol.10 , pp. 1441-1448
    • Nakamura, K.1    Jeong, S.Y.2    Uchihara, T.3
  • 319
    • 0036451840 scopus 로고    scopus 로고
    • The HD mutation does not alter neuronal death in the striatum of Hdh(Q92) knock-in mice after mild focal ischemia
    • Namura S., Hirt L., Wheeler V.C., et al. The HD mutation does not alter neuronal death in the striatum of Hdh(Q92) knock-in mice after mild focal ischemia. Neurobiol Dis 2002, 11:147-154.
    • (2002) Neurobiol Dis , vol.11 , pp. 147-154
    • Namura, S.1    Hirt, L.2    Wheeler, V.C.3
  • 320
    • 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 S.B., O'Kusky J.R., et al. Targeted disruption of the Huntington's disease gene results in embryonic lethality and behavioral and morphological changes in heterozygotes. Cell 1995, 81:811-823.
    • (1995) Cell , vol.81 , pp. 811-823
    • Nasir, J.1    Floresco, S.B.2    O'Kusky, J.R.3
  • 321
    • 0033782987 scopus 로고    scopus 로고
    • HEAT repeats associated with condensins, cohesins, and other complexes involved in chromosome-related functions
    • Neuwald A.F., Hirano T. HEAT repeats associated with condensins, cohesins, and other complexes involved in chromosome-related functions. Genome Res 2000, 10:1445-1452.
    • (2000) Genome Res , vol.10 , pp. 1445-1452
    • Neuwald, A.F.1    Hirano, T.2
  • 322
    • 33750210519 scopus 로고    scopus 로고
    • Behavioral abnormalities precede neuropathological markers in rats transgenic for Huntington's disease
    • Nguyen H.P., Kobbe P., Rahne H., et al. Behavioral abnormalities precede neuropathological markers in rats transgenic for Huntington's disease. Hum Mol Genet 2006, 15:3177-3194.
    • (2006) Hum Mol Genet , vol.15 , pp. 3177-3194
    • Nguyen, H.P.1    Kobbe, P.2    Rahne, H.3
  • 323
    • 58449127187 scopus 로고    scopus 로고
    • Age-dependent gene expression profile and protein expression in a transgenic rat model of Huntington's disease
    • Nguyen H.P., Metzger S., Holzmann C., et al. Age-dependent gene expression profile and protein expression in a transgenic rat model of Huntington's disease. Proteomics--Clinical Application 2008, 2:1638-1650.
    • (2008) Proteomics--Clinical Application , vol.2 , pp. 1638-1650
    • Nguyen, H.P.1    Metzger, S.2    Holzmann, C.3
  • 324
    • 0035937523 scopus 로고    scopus 로고
    • Interference by huntingtin and atrophin-1 with cbp-mediated transcription leading to cellular toxicity
    • Nucifora F.C., Sasaki M., Peters M.F., et al. Interference by huntingtin and atrophin-1 with cbp-mediated transcription leading to cellular toxicity. Science 2001, 291:2423-2428.
    • (2001) Science , vol.291 , pp. 2423-2428
    • Nucifora, F.C.1    Sasaki, M.2    Peters, M.F.3
  • 325
    • 0742287915 scopus 로고    scopus 로고
    • CRE-mediated transcription is increased in Huntington's disease transgenic mice
    • Obrietan K., Hoyt K.R. CRE-mediated transcription is increased in Huntington's disease transgenic mice. J Neurosci 2004, 24:791-796.
    • (2004) J Neurosci , vol.24 , pp. 791-796
    • Obrietan, K.1    Hoyt, K.R.2
  • 326
    • 0033550705 scopus 로고    scopus 로고
    • Neuronal degeneration in the basal ganglia and loss of pallido-subthalamic synapses in mice with targeted disruption of the Huntington's disease gene
    • O'Kusky J.R., Nasir J., Cicchetti F., et al. Neuronal degeneration in the basal ganglia and loss of pallido-subthalamic synapses in mice with targeted disruption of the Huntington's disease gene. Brain Res 1999, 818:468-479.
    • (1999) Brain Res , vol.818 , pp. 468-479
    • O'Kusky, J.R.1    Nasir, J.2    Cicchetti, F.3
  • 327
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • Olsen J.V., Blagoev B., Gnad F., et al. Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 2006, 127:635-648.
    • (2006) Cell , vol.127 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3
  • 328
    • 0033587128 scopus 로고    scopus 로고
    • Inhibition of caspase-1 slows disease progression in a mouse model of Huntington's disease
    • Ona V.O., Li M., Vonsattel J.P., 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
  • 329
    • 11144354038 scopus 로고    scopus 로고
    • Huntingtin Interacting Protein 1 mutations lead to abnormal hematopoiesis, spinal defects and cataracts
    • Oravecz-Wilson K.I., Kiel M.J., Li L., et al. Huntingtin Interacting Protein 1 mutations lead to abnormal hematopoiesis, spinal defects and cataracts. Hum Mol Genet 2004, 13:851-867.
    • (2004) Hum Mol Genet , vol.13 , pp. 851-867
    • Oravecz-Wilson, K.I.1    Kiel, M.J.2    Li, L.3
  • 330
    • 0027164698 scopus 로고
    • Expansion of an unstable trinucleotide CAG repeat in spinocerebellar ataxia type 1
    • Orr H.T., Chung M.Y., Banfi S., et al. Expansion of an unstable trinucleotide CAG repeat in spinocerebellar ataxia type 1. Nat Genet 1993, 4:221-226.
    • (1993) Nat Genet , vol.4 , pp. 221-226
    • Orr, H.T.1    Chung, M.Y.2    Banfi, S.3
  • 331
    • 0001547829 scopus 로고
    • Historical note on hereditary chorea
    • Osler W. Historical note on hereditary chorea. Neurographs 1908, 1:113-116.
    • (1908) Neurographs , vol.1 , pp. 113-116
    • Osler, W.1
  • 332
    • 34547136437 scopus 로고    scopus 로고
    • Expression of mutated Huntingtin fragment in the putamen is sufficient to produce abnormal movement in non-human primates
    • Palfi S., Brouillet E., Jarraya B., et al. Expression of mutated Huntingtin fragment in the putamen is sufficient to produce abnormal movement in non-human primates. Mol Ther 2007, 15:1444-1451.
    • (2007) Mol Ther , vol.15 , pp. 1444-1451
    • Palfi, S.1    Brouillet, E.2    Jarraya, B.3
  • 333
    • 0036327065 scopus 로고    scopus 로고
    • Early mitochondrial calcium defects in Huntington's disease are a direct effect of polyglutamines
    • Panov A.V., Gutekunst C.A., Leavitt B.R., et al. Early mitochondrial calcium defects in Huntington's disease are a direct effect of polyglutamines. Nat Neurosci 2002, 5:731-736.
    • (2002) Nat Neurosci , vol.5 , pp. 731-736
    • Panov, A.V.1    Gutekunst, C.A.2    Leavitt, B.R.3
  • 334
    • 14244264746 scopus 로고    scopus 로고
    • Ca2+-induced permeability transition in human lymphoblastoid cell mitochondria from normal and Huntington's disease individuals
    • Panov A.V., Lund S., Greenamyre J.T. Ca2+-induced permeability transition in human lymphoblastoid cell mitochondria from normal and Huntington's disease individuals. Mol Cell Biochem 2005, 269:143-152.
    • (2005) Mol Cell Biochem , vol.269 , pp. 143-152
    • Panov, A.V.1    Lund, S.2    Greenamyre, J.T.3
  • 335
    • 32544432052 scopus 로고    scopus 로고
    • Inhibition of calcineurin by FK506 protects against polyglutamine-huntingtin toxicity through an increase of huntingtin phosphorylation at S421
    • Pardo R., Colin E., Regulier E., et al. Inhibition of calcineurin by FK506 protects against polyglutamine-huntingtin toxicity through an increase of huntingtin phosphorylation at S421. J Neurosci 2006, 26:1635-1645.
    • (2006) J Neurosci , vol.26 , pp. 1635-1645
    • Pardo, R.1    Colin, E.2    Regulier, E.3
  • 336
    • 0025087726 scopus 로고
    • Evidence for a defect in NADH: ubiquinone oxidoreductase (complex I) in Huntington's disease
    • Parker W.D., Boyson S.J., Luder A.S., et al. Evidence for a defect in NADH: ubiquinone oxidoreductase (complex I) in Huntington's disease. Neurology 1990, 40:1231-1234.
    • (1990) Neurology , vol.40 , pp. 1231-1234
    • Parker, W.D.1    Boyson, S.J.2    Luder, A.S.3
  • 337
    • 0035878553 scopus 로고    scopus 로고
    • Double-stranded RNA-dependent protein kinase, PKR, binds preferentially to Huntington's disease (HD) transcripts and is activated in HD tissue
    • Peel A.L., Rao R.V., Cottrell B.A., et al. Double-stranded RNA-dependent protein kinase, PKR, binds preferentially to Huntington's disease (HD) transcripts and is activated in HD tissue. Hum Mol Genet 2001, 10:1531-1538.
    • (2001) Hum Mol Genet , vol.10 , pp. 1531-1538
    • Peel, A.L.1    Rao, R.V.2    Cottrell, B.A.3
  • 338
    • 0030601657 scopus 로고    scopus 로고
    • Glial cell line-derived neurotrophic factor protects striatal calbindin-immunoreactive neurons from excitotoxic damage
    • Perez-Navarro E., Arenas E., Reiriz J., et al. Glial cell line-derived neurotrophic factor protects striatal calbindin-immunoreactive neurons from excitotoxic damage. Neuroscience 1996, 75:345-352.
    • (1996) Neuroscience , vol.75 , pp. 345-352
    • Perez-Navarro, E.1    Arenas, E.2    Reiriz, J.3
  • 339
    • 0028677475 scopus 로고
    • Huntington's disease CAG trinucleotide repeats in pathologically confirmed post-mortem brains
    • Persichetti F., Srinidhi J., Kanaley L., et al. Huntington's disease CAG trinucleotide repeats in pathologically confirmed post-mortem brains. Neurobiol Dis 1994, 1:159-166.
    • (1994) Neurobiol Dis , vol.1 , pp. 159-166
    • Persichetti, F.1    Srinidhi, J.2    Kanaley, L.3
  • 340
    • 0029295607 scopus 로고
    • Normal and expanded Huntington's disease gene alleles produce distinguishable proteins due to translation across the CAG repeat
    • Persichetti F., Ambrose C.M., Ge P., et al. Normal and expanded Huntington's disease gene alleles produce distinguishable proteins due to translation across the CAG repeat. Mol Med 1995, 1:374-383.
    • (1995) Mol Med , vol.1 , pp. 374-383
    • Persichetti, F.1    Ambrose, C.M.2    Ge, P.3
  • 341
    • 0030175161 scopus 로고    scopus 로고
    • Differential expression of normal and mutant Huntington's disease gene alleles
    • Persichetti F., Carlee L., Faber P.W., et al. Differential expression of normal and mutant Huntington's disease gene alleles. Neurobiol Dis 1996, 3:183-190.
    • (1996) Neurobiol Dis , vol.3 , pp. 183-190
    • Persichetti, F.1    Carlee, L.2    Faber, P.W.3
  • 342
    • 0028283985 scopus 로고
    • Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases
    • Perutz M.F., Johnson T., Suzuki M., et al. Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases. Proc Natl Acad Sci U S A 1994, 91:5355-5358.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 5355-5358
    • Perutz, M.F.1    Johnson, T.2    Suzuki, M.3
  • 343
    • 0035793637 scopus 로고    scopus 로고
    • Isolation of a 40-kDa Huntingtin-associated protein
    • Peters M.F., Ross C.A. Isolation of a 40-kDa Huntingtin-associated protein. J Biol Chem 2001, 276:3188-3194.
    • (2001) J Biol Chem , vol.276 , pp. 3188-3194
    • Peters, M.F.1    Ross, C.A.2
  • 344
    • 33847317865 scopus 로고    scopus 로고
    • Cellular and subcellular localization of Huntingtin [corrected] aggregates in the brain of a rat transgenic for Huntington disease
    • Petrasch-Parwez E., Nguyen H.P., Lobbecke-Schumacher M., et al. Cellular and subcellular localization of Huntingtin [corrected] aggregates in the brain of a rat transgenic for Huntington disease. J Comp Neurol 2007, 501:716-730.
    • (2007) J Comp Neurol , vol.501 , pp. 716-730
    • Petrasch-Parwez, E.1    Nguyen, H.P.2    Lobbecke-Schumacher, M.3
  • 345
    • 15544372340 scopus 로고    scopus 로고
    • A structure-based analysis of huntingtin mutant polyglutamine aggregation and toxicity: evidence for a compact beta-sheet structure
    • Poirier M.A., Jiang H., Ross C.A. A structure-based analysis of huntingtin mutant polyglutamine aggregation and toxicity: evidence for a compact beta-sheet structure. Hum Mol Genet 2005, 14:765-774.
    • (2005) Hum Mol Genet , vol.14 , pp. 765-774
    • Poirier, M.A.1    Jiang, H.2    Ross, C.A.3
  • 346
    • 0029072690 scopus 로고
    • Evidence for apoptotic cell death in Huntington disease and excitotoxic animal models
    • Portera-Cailliau C., Hedreen J.C., Price D.L., et al. Evidence for apoptotic cell death in Huntington disease and excitotoxic animal models. J Neurosci 1995, 15:3775-3787.
    • (1995) J Neurosci , vol.15 , pp. 3775-3787
    • Portera-Cailliau, C.1    Hedreen, J.C.2    Price, D.L.3
  • 347
    • 45149115090 scopus 로고    scopus 로고
    • Proteasomes cleave at multiple sites within polyglutamine tracts: activation by PA28gamma(K188E)
    • Pratt G., Rechsteiner M. Proteasomes cleave at multiple sites within polyglutamine tracts: activation by PA28gamma(K188E). J Biol Chem 2008, 283:12919-12925.
    • (2008) J Biol Chem , vol.283 , pp. 12919-12925
    • Pratt, G.1    Rechsteiner, M.2
  • 348
    • 0031863098 scopus 로고    scopus 로고
    • Exon trapping and sequence-based methods of gene finding in transcript mapping of human 4p16.3
    • Pribill I., Barnes G.T., Chen J., et al. Exon trapping and sequence-based methods of gene finding in transcript mapping of human 4p16.3. Somat Cell Mol Genet 1997, 23:413-427.
    • (1997) Somat Cell Mol Genet , vol.23 , pp. 413-427
    • Pribill, I.1    Barnes, G.T.2    Chen, J.3
  • 349
    • 0030292488 scopus 로고    scopus 로고
    • Moderate expansion of a normally biallelic trinucleotide repeat in spinocerebellar ataxia type 2
    • Pulst S.M., Nechiporuk A., Nechiporuk T., et al. Moderate expansion of a normally biallelic trinucleotide repeat in spinocerebellar ataxia type 2. Nat Genet 1996, 14:269-276.
    • (1996) Nat Genet , vol.14 , pp. 269-276
    • Pulst, S.M.1    Nechiporuk, A.2    Nechiporuk, T.3
  • 350
    • 34047130772 scopus 로고    scopus 로고
    • Proteome analysis of soluble nuclear proteins reveals that HMGB1/2 suppress genotoxic stress in polyglutamine diseases
    • Qi M.L., Tagawa K., Enokido Y., et al. Proteome analysis of soluble nuclear proteins reveals that HMGB1/2 suppress genotoxic stress in polyglutamine diseases. Nat Cell Biol 2007, 9:402-414.
    • (2007) Nat Cell Biol , vol.9 , pp. 402-414
    • Qi, M.L.1    Tagawa, K.2    Enokido, Y.3
  • 351
    • 0348013126 scopus 로고    scopus 로고
    • Autophagy regulates the processing of amino terminal huntingtin fragments
    • Qin Z.H., Wang Y., Kegel K.B., et al. Autophagy regulates the processing of amino terminal huntingtin fragments. Hum Mol Genet 2003, 12:3231-3244.
    • (2003) Hum Mol Genet , vol.12 , pp. 3231-3244
    • Qin, Z.H.1    Wang, Y.2    Kegel, K.B.3
  • 352
    • 0842265636 scopus 로고    scopus 로고
    • The serum- and glucocorticoid-induced kinase SGK inhibits mutant huntingtin-induced toxicity by phosphorylating serine 421 of huntingtin
    • Rangone H., Poizat G., Troncoso J., et al. The serum- and glucocorticoid-induced kinase SGK inhibits mutant huntingtin-induced toxicity by phosphorylating serine 421 of huntingtin. Eur J Neurosci 2004, 19:273-279.
    • (2004) Eur J Neurosci , vol.19 , pp. 273-279
    • Rangone, H.1    Poizat, G.2    Troncoso, J.3
  • 353
    • 37549065909 scopus 로고    scopus 로고
    • N-terminal proteolysis of full-length mutant huntingtin in an inducible PC12 cell model of Huntington's disease
    • Ratovitski T., Nakamura M., D'Ambola J., et al. N-terminal proteolysis of full-length mutant huntingtin in an inducible PC12 cell model of Huntington's disease. Cell Cycle 2007, 6:2970-2981.
    • (2007) Cell Cycle , vol.6 , pp. 2970-2981
    • Ratovitski, T.1    Nakamura, M.2    D'Ambola, J.3
  • 354
    • 0036566266 scopus 로고    scopus 로고
    • Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy
    • Ravikumar B., Duden R., Rubinsztein D.C. Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy. Hum Mol Genet 2002, 11:1107-1117.
    • (2002) Hum Mol Genet , vol.11 , pp. 1107-1117
    • Ravikumar, B.1    Duden, R.2    Rubinsztein, D.C.3
  • 355
    • 0038364056 scopus 로고    scopus 로고
    • Raised intracellular glucose concentrations reduce aggregation and cell death caused by mutant huntingtin exon 1 by decreasing mTOR phosphorylation and inducing autophagy
    • Ravikumar B., Stewart A., Kita H., et al. Raised intracellular glucose concentrations reduce aggregation and cell death caused by mutant huntingtin exon 1 by decreasing mTOR phosphorylation and inducing autophagy. Hum Mol Genet 2003, 12:985-994.
    • (2003) Hum Mol Genet , vol.12 , pp. 985-994
    • Ravikumar, B.1    Stewart, A.2    Kita, H.3
  • 356
    • 37849012236 scopus 로고    scopus 로고
    • HYPK, a Huntingtin interacting protein, reduces aggregates and apoptosis induced by N-terminal Huntingtin with 40 glutamines in Neuro2a cells and exhibits chaperone-like activity
    • Raychaudhuri S., Sinha M., Mukhopadhyay D., et al. HYPK, a Huntingtin interacting protein, reduces aggregates and apoptosis induced by N-terminal Huntingtin with 40 glutamines in Neuro2a cells and exhibits chaperone-like activity. Hum Mol Genet 2008, 17:240-255.
    • (2008) Hum Mol Genet , vol.17 , pp. 240-255
    • Raychaudhuri, S.1    Sinha, M.2    Mukhopadhyay, D.3
  • 357
    • 17344367977 scopus 로고    scopus 로고
    • Behavioural abnormalities and selective neuronal loss in HD transgenic mice expressing mutated full-length HD cDNA
    • Reddy P.H., 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
  • 358
    • 0033614772 scopus 로고    scopus 로고
    • Transgenic mice expressing mutated full-length HD cDNA: a paradigm for locomotor changes and selective neuronal loss in Huntington's disease
    • Reddy P.H., Charles V., Williams M., et al. Transgenic mice expressing mutated full-length HD cDNA: a paradigm for locomotor changes and selective neuronal loss in Huntington's disease. Philos Trans R Soc Lond B Biol Sci 1999, 354:1035-1045.
    • (1999) Philos Trans R Soc Lond B Biol Sci , vol.354 , pp. 1035-1045
    • Reddy, P.H.1    Charles, V.2    Williams, M.3
  • 359
    • 0242609127 scopus 로고    scopus 로고
    • Early and reversible neuropathology induced by tetracycline-regulated lentiviral overexpression of mutant huntingtin in rat striatum
    • Regulier E., Trottier Y., Perrin V., et al. Early and reversible neuropathology induced by tetracycline-regulated lentiviral overexpression of mutant huntingtin in rat striatum. Hum Mol Genet 2003, 12:2827-2836.
    • (2003) Hum Mol Genet , vol.12 , pp. 2827-2836
    • Regulier, E.1    Trottier, Y.2    Perrin, V.3
  • 360
    • 8544235014 scopus 로고    scopus 로고
    • SCA6 is caused by moderate CAG expansion in the alpha1A-voltage-dependent calcium channel gene
    • Riess O., Schols L., Bottger H., et al. SCA6 is caused by moderate CAG expansion in the alpha1A-voltage-dependent calcium channel gene. Hum Mol Genet 1997, 6:1289-1293.
    • (1997) Hum Mol Genet , vol.6 , pp. 1289-1293
    • Riess, O.1    Schols, L.2    Bottger, H.3
  • 361
    • 0031128793 scopus 로고    scopus 로고
    • SCA2 trinucleotide expansion in German SCA patients
    • Riess O., Laccone F.A., Gispert S., et al. SCA2 trinucleotide expansion in German SCA patients. Neurogenetics 1997, 1:59-64.
    • (1997) Neurogenetics , vol.1 , pp. 59-64
    • Riess, O.1    Laccone, F.A.2    Gispert, S.3
  • 362
    • 0034657112 scopus 로고    scopus 로고
    • Wild-type huntingtin protects from apoptosis upstream of caspase-3
    • Rigamonti D., Bauer J.H., De-Fraja C., et al. Wild-type huntingtin protects from apoptosis upstream of caspase-3. J Neurosci 2000, 20:3705-3713.
    • (2000) J Neurosci , vol.20 , pp. 3705-3713
    • Rigamonti, D.1    Bauer, J.H.2    De-Fraja, C.3
  • 363
    • 33846540080 scopus 로고    scopus 로고
    • The first 17 amino acids of Huntingtin modulate its sub-cellular localization, aggregation and effects on calcium homeostasis
    • Rockabrand E., Slepko N., Pantalone A., et al. The first 17 amino acids of Huntingtin modulate its sub-cellular localization, aggregation and effects on calcium homeostasis. Hum Mol Genet 2007, 16:61-77.
    • (2007) Hum Mol Genet , vol.16 , pp. 61-77
    • Rockabrand, E.1    Slepko, N.2    Pantalone, A.3
  • 364
    • 0029997090 scopus 로고    scopus 로고
    • Phenotypic characterization of individuals with 30-40 CAG repeats in the Huntington disease (HD) gene reveals HD cases with 36 repeats and apparently normal elderly individuals with 36-39 repeats
    • Rubinsztein D.C., Leggo J., Coles R., et al. Phenotypic characterization of individuals with 30-40 CAG repeats in the Huntington disease (HD) gene reveals HD cases with 36 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
  • 365
    • 41949137715 scopus 로고    scopus 로고
    • A comparison of huntington disease and huntington disease-like 2 neuropathology
    • Rudnicki D.D., Pletnikova O., Vonsattel J.P., et al. A comparison of huntington disease and huntington disease-like 2 neuropathology. J Neuropathol Exp Neurol 2008, 67:366-374.
    • (2008) J Neuropathol Exp Neurol , vol.67 , pp. 366-374
    • Rudnicki, D.D.1    Pletnikova, O.2    Vonsattel, J.P.3
  • 366
    • 55749107270 scopus 로고    scopus 로고
    • Dysregulation of gene expression in primary neuron models of Huntington's disease shows that polyglutamine-related effects on the striatal transcriptome may not be dependent on brain circuitry
    • Runne H., Regulier E., Kuhn A., et al. Dysregulation of gene expression in primary neuron models of Huntington's disease shows that polyglutamine-related effects on the striatal transcriptome may not be dependent on brain circuitry. J Neurosci 2008, 28:9723-9731.
    • (2008) J Neurosci , vol.28 , pp. 9723-9731
    • Runne, H.1    Regulier, E.2    Kuhn, A.3
  • 367
    • 33744504676 scopus 로고    scopus 로고
    • Mechanisms of disease: Histone modifications in Huntington's disease
    • Sadri-Vakili G., Cha J.H. Mechanisms of disease: Histone modifications in Huntington's disease. Nat Clin Pract Neurol 2006, 2:330-338.
    • (2006) Nat Clin Pract Neurol , vol.2 , pp. 330-338
    • Sadri-Vakili, G.1    Cha, J.H.2
  • 368
    • 33745190716 scopus 로고    scopus 로고
    • Huntingtin inclusions do not down-regulate specific genes in the R6/2 Huntington's disease mouse
    • Sadri-Vakili G., Menon A.S., Farrell L.A., et al. Huntingtin inclusions do not down-regulate specific genes in the R6/2 Huntington's disease mouse. Eur J Neurosci 2006, 23:3171-3175.
    • (2006) Eur J Neurosci , vol.23 , pp. 3171-3175
    • Sadri-Vakili, G.1    Menon, A.S.2    Farrell, L.A.3
  • 369
    • 34447317536 scopus 로고    scopus 로고
    • Histones associated with downregulated genes are hypo-acetylated in Huntington's disease models
    • Sadri-Vakili G., Bouzou B., Benn C.L., et al. Histones associated with downregulated genes are hypo-acetylated in Huntington's disease models. Hum Mol Genet 2007, 16:1293-1306.
    • (2007) Hum Mol Genet , vol.16 , pp. 1293-1306
    • Sadri-Vakili, G.1    Bouzou, B.2    Benn, C.L.3
  • 370
    • 0033103523 scopus 로고    scopus 로고
    • Caspase-8 is required for cell death induced by expanded polyglutamine repeats
    • Sanchez I., Xu C.J., Juo P., et al. 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
  • 371
    • 0037461730 scopus 로고    scopus 로고
    • Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders
    • Sanchez I., Mahlke C., Yuan J. Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders. Nature 2003, 421:373-379.
    • (2003) Nature , vol.421 , pp. 373-379
    • Sanchez, I.1    Mahlke, C.2    Yuan, J.3
  • 372
    • 0030292368 scopus 로고    scopus 로고
    • Identification of the spinocerebellar ataxia type 2 gene using a direct identification of repeat expansion and cloning technique, DIRECT
    • Sanpei K., Takano H., Igarashi S., et al. Identification of the spinocerebellar ataxia type 2 gene using a direct identification of repeat expansion and cloning technique, DIRECT. Nat Genet 1996, 14:277-284.
    • (1996) Nat Genet , vol.14 , pp. 277-284
    • Sanpei, K.1    Takano, H.2    Igarashi, S.3
  • 373
    • 0030771894 scopus 로고    scopus 로고
    • Huntingtin localization in brains of normal and Huntington's disease patients
    • Sapp E., Schwarz C., Chase K., et al. Huntingtin localization in brains of normal and Huntington's disease patients. Ann Neurol 1997, 42:604-612.
    • (1997) Ann Neurol , vol.42 , pp. 604-612
    • Sapp, E.1    Schwarz, C.2    Chase, K.3
  • 374
    • 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., et al. 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
  • 375
    • 49449091708 scopus 로고    scopus 로고
    • Huntington's disease protein contributes to RNA-mediated gene silencing through association with Argonaute and P bodies
    • Savas J.N., Makusky A., Ottosen S., et al. Huntington's disease protein contributes to RNA-mediated gene silencing through association with Argonaute and P bodies. Proc Natl Acad Sci U S A 2008, 105:10820-10825.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 10820-10825
    • Savas, J.N.1    Makusky, A.2    Ottosen, S.3
  • 376
    • 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
  • 377
    • 0033032999 scopus 로고    scopus 로고
    • Mitochondrial involvement in Parkinson's disease, Huntington's disease, hereditary spastic paraplegia and Friedreich's ataxia
    • Schapira A.H. Mitochondrial involvement in Parkinson's disease, Huntington's disease, hereditary spastic paraplegia and Friedreich's ataxia. Biochim Biophys Acta 1999, 1410:159-170.
    • (1999) Biochim Biophys Acta , vol.1410 , pp. 159-170
    • Schapira, A.H.1
  • 378
    • 34247869645 scopus 로고    scopus 로고
    • Identification of anti-prion compounds as efficient inhibitors of polyglutamine protein aggregation in a zebrafish model
    • Schiffer N.W., Broadley S.A., Hirschberger T., et al. Identification of anti-prion compounds as efficient inhibitors of polyglutamine protein aggregation in a zebrafish model. J Biol Chem 2007, 282:9195-9203.
    • (2007) J Biol Chem , vol.282 , pp. 9195-9203
    • Schiffer, N.W.1    Broadley, S.A.2    Hirschberger, T.3
  • 379
    • 33747633422 scopus 로고    scopus 로고
    • Huntingtin phosphorylation sites mapped by mass spectrometry. Modulation of cleavage and toxicity
    • Schilling B., Gafni J., Torcassi C., et al. Huntingtin phosphorylation sites mapped by mass spectrometry. Modulation of cleavage and toxicity. J Biol Chem 2006, 281:23686-23697.
    • (2006) J Biol Chem , vol.281 , pp. 23686-23697
    • Schilling, B.1    Gafni, J.2    Torcassi, C.3
  • 380
    • 0029092340 scopus 로고
    • Expression of the Huntington's disease (IT15) protein product in HD patients
    • Schilling G., Sharp A.H., Loev S.J., et al. Expression of the Huntington's disease (IT15) protein product in HD patients. Hum Mol Genet 1995, 4:1365-1371.
    • (1995) Hum Mol Genet , vol.4 , pp. 1365-1371
    • Schilling, G.1    Sharp, A.H.2    Loev, S.J.3
  • 381
    • 0033054555 scopus 로고    scopus 로고
    • Intranuclear inclusions and neuritic aggregates in transgenic mice expressing a mutant N-terminal fragment of huntingtin
    • Schilling G., Becher M.W., Sharp A.H., 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
  • 382
    • 0035960544 scopus 로고    scopus 로고
    • Coenzyme Q10 and remacemide hydrochloride ameliorate motor deficits in a Huntington's disease transgenic mouse model
    • Schilling G., Coonfield M.L., Ross C.A., et al. Coenzyme Q10 and remacemide hydrochloride ameliorate motor deficits in a Huntington's disease transgenic mouse model. Neurosci Lett 2001, 315:149-153.
    • (2001) Neurosci Lett , vol.315 , pp. 149-153
    • Schilling, G.1    Coonfield, M.L.2    Ross, C.A.3
  • 383
    • 4344636957 scopus 로고    scopus 로고
    • Nuclear-targeting of mutant huntingtin fragments produces Huntington's disease-like phenotypes in transgenic mice
    • Schilling G., Savonenko A.V., Klevytska A., et al. Nuclear-targeting of mutant huntingtin fragments produces Huntington's disease-like phenotypes in transgenic mice. Hum Mol Genet 2004, 13:1599-1610.
    • (2004) Hum Mol Genet , vol.13 , pp. 1599-1610
    • Schilling, G.1    Savonenko, A.V.2    Klevytska, A.3
  • 384
    • 0029079428 scopus 로고
    • Expression of the Huntington disease gene in rodents: cloning the rat homologue and evidence for downregulation in non-neuronal tissues during development
    • Schmitt I., Bachner D., Megow D., et al. Expression of the Huntington disease gene in rodents: cloning the rat homologue and evidence for downregulation in non-neuronal tissues during development. Hum Mol Genet 1995, 4:1173-1182.
    • (1995) Hum Mol Genet , vol.4 , pp. 1173-1182
    • Schmitt, I.1    Bachner, D.2    Megow, D.3
  • 385
    • 0028988941 scopus 로고
    • Trinucleotide expansion within the MJD1 gene presents clinically as spinocerebellar ataxia and occurs most frequently in German SCA patients
    • Schols L., Vieira-Saecker A.M., Schols S., et al. Trinucleotide expansion within the MJD1 gene presents clinically as spinocerebellar ataxia and occurs most frequently in German SCA patients. Hum Mol Genet 1995, 4:1001-1005.
    • (1995) Hum Mol Genet , vol.4 , pp. 1001-1005
    • Schols, L.1    Vieira-Saecker, A.M.2    Schols, S.3
  • 386
    • 0031960474 scopus 로고    scopus 로고
    • Spinocerebellar ataxia type 6: genotype and phenotype in German kindreds
    • Schols L., Kruger R., Amoiridis G., et al. Spinocerebellar ataxia type 6: genotype and phenotype in German kindreds. J Neurol Neurosurg Psychiatry 1998, 64:67-73.
    • (1998) J Neurol Neurosurg Psychiatry , vol.64 , pp. 67-73
    • Schols, L.1    Kruger, R.2    Amoiridis, G.3
  • 387
    • 0020702374 scopus 로고
    • Quinolinic acid: an endogenous metabolite that produces axon-sparing lesions in rat brain
    • Schwarcz R., Whetsell W.O., Mangano R.M. Quinolinic acid: an endogenous metabolite that produces axon-sparing lesions in rat brain. Science 1983, 219:316-318.
    • (1983) Science , vol.219 , pp. 316-318
    • Schwarcz, R.1    Whetsell, W.O.2    Mangano, R.M.3
  • 388
    • 33748321965 scopus 로고    scopus 로고
    • Predictive testing for Huntington disease: interpretation and significance of intermediate alleles
    • Semaka A., Creighton S., Warby S., et al. Predictive testing for Huntington disease: interpretation and significance of intermediate alleles. Clin Genet 2006, 70:283-294.
    • (2006) Clin Genet , vol.70 , pp. 283-294
    • Semaka, A.1    Creighton, S.2    Warby, S.3
  • 389
    • 4444303263 scopus 로고    scopus 로고
    • Generalized brain and skin proteasome inhibition in Huntington's disease
    • Seo H., Sonntag K.C., Isacson O. Generalized brain and skin proteasome inhibition in Huntington's disease. Ann Neurol 2004, 56:319-328.
    • (2004) Ann Neurol , vol.56 , pp. 319-328
    • Seo, H.1    Sonntag, K.C.2    Isacson, O.3
  • 390
    • 26444441008 scopus 로고    scopus 로고
    • HD CAG repeat implicates a dominant property of huntingtin in mitochondrial energy metabolism
    • Seong I.S., Ivanova E., Lee J.M., et al. HD CAG repeat implicates a dominant property of huntingtin in mitochondrial energy metabolism. Hum Mol Genet 2005, 14:2871-2880.
    • (2005) Hum Mol Genet , vol.14 , pp. 2871-2880
    • Seong, I.S.1    Ivanova, E.2    Lee, J.M.3
  • 391
    • 0029034511 scopus 로고
    • Widespread expression of Huntington's disease gene (IT15) protein product
    • Sharp A.H., Loev S.J., Schilling G., et al. Widespread expression of 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
  • 392
    • 0032949459 scopus 로고    scopus 로고
    • A Huntington's disease CAG expansion at the murine Hdh locus is unstable and associated with behavioural abnormalities in mice
    • Shelbourne P.F., Killeen N., Hevner R.F., et al. A Huntington's disease CAG expansion at the murine Hdh locus is unstable and associated with behavioural abnormalities in mice. Hum Mol Genet 1999, 8:763-774.
    • (1999) Hum Mol Genet , vol.8 , pp. 763-774
    • Shelbourne, P.F.1    Killeen, N.2    Hevner, R.F.3
  • 393
    • 34447324387 scopus 로고    scopus 로고
    • Triplet repeat mutation length gains correlate with cell-type specific vulnerability in Huntington disease brain
    • Shelbourne P.F., Keller-McGandy C., Bi W.L., et al. Triplet repeat mutation length gains correlate with cell-type specific vulnerability in Huntington disease brain. Hum Mol Genet 2007, 16:1133-1142.
    • (2007) Hum Mol Genet , vol.16 , pp. 1133-1142
    • Shelbourne, P.F.1    Keller-McGandy, C.2    Bi, W.L.3
  • 394
    • 33744916798 scopus 로고    scopus 로고
    • Regulation of intracellular accumulation of mutant Huntingtin by Beclin 1
    • Shibata M., Lu T., Furuya T., et al. Regulation of intracellular accumulation of mutant Huntingtin by Beclin 1. J Biol Chem 2006, 281:14474-14485.
    • (2006) J Biol Chem , vol.281 , pp. 14474-14485
    • Shibata, M.1    Lu, T.2    Furuya, T.3
  • 395
    • 0033037919 scopus 로고    scopus 로고
    • Huntington's disease intranuclear inclusions contain truncated, ubiquitinated huntingtin protein
    • Sieradzan K.A., Mechan A.O., Jones L., et al. Huntington's disease intranuclear inclusions contain truncated, ubiquitinated huntingtin protein. Exp Neurol 1999, 156:92-99.
    • (1999) Exp Neurol , vol.156 , pp. 92-99
    • Sieradzan, K.A.1    Mechan, A.O.2    Jones, L.3
  • 396
    • 64449085303 scopus 로고    scopus 로고
    • Live axonal transport disruption by mutant huntingtin fragments in Drosophila motor neuron axons
    • Sinadinos C., Burbidge-King T., Soh D., et al. Live axonal transport disruption by mutant huntingtin fragments in Drosophila motor neuron axons. Neurobiol Dis 2009, 34:389-395.
    • (2009) Neurobiol Dis , vol.34 , pp. 389-395
    • Sinadinos, C.1    Burbidge-King, T.2    Soh, D.3
  • 397
    • 0036850524 scopus 로고    scopus 로고
    • HIP14, a novel ankyrin domain-containing protein, links huntingtin to intracellular trafficking and endocytosis
    • Singaraja R.R., Hadano S., Metzler M., et al. HIP14, a novel ankyrin domain-containing protein, links huntingtin to intracellular trafficking and endocytosis. Hum Mol Genet 2002, 11:2815-2828.
    • (2002) Hum Mol Genet , vol.11 , pp. 2815-2828
    • Singaraja, R.R.1    Hadano, S.2    Metzler, M.3
  • 398
    • 0037101839 scopus 로고    scopus 로고
    • Early transcriptional profiles in huntingtin-inducible striatal cells by microarray analyses
    • Sipione S., Rigamonti D., Valenza M., et al. Early transcriptional profiles in huntingtin-inducible striatal cells by microarray analyses. Hum Mol Genet 2002, 11:1953-1965.
    • (2002) Hum Mol Genet , vol.11 , pp. 1953-1965
    • Sipione, S.1    Rigamonti, D.2    Valenza, M.3
  • 399
    • 0032186107 scopus 로고    scopus 로고
    • SH3GL3 associates with the Huntingtin exon 1 protein and promotes the formation of polygln-containing protein aggregates
    • Sittler A., Walter S., Wedemeyer N., et al. SH3GL3 associates with the Huntingtin exon 1 protein and promotes the formation of polygln-containing protein aggregates. Mol Cell 1998, 2:427-436.
    • (1998) Mol Cell , vol.2 , pp. 427-436
    • Sittler, A.1    Walter, S.2    Wedemeyer, N.3
  • 400
    • 10744227174 scopus 로고    scopus 로고
    • Selective striatal neuronal loss in a YAC128 mouse model of Huntington disease
    • Slow E.J., van Raamsdonk J., Rogers D., et al. Selective striatal neuronal loss in a YAC128 mouse model of Huntington disease. Hum Mol Genet 2003, 12:1555-1567.
    • (2003) Hum Mol Genet , vol.12 , pp. 1555-1567
    • Slow, E.J.1    van Raamsdonk, J.2    Rogers, D.3
  • 401
    • 0026753352 scopus 로고
    • A recombination event that redefines the Huntington disease region
    • Snell R.G., Thompson L.M., Tagle D.A., et al. A recombination event that redefines the Huntington disease region. Am J Hum Genet 1992, 51:357-362.
    • (1992) Am J Hum Genet , vol.51 , pp. 357-362
    • Snell, R.G.1    Thompson, L.M.2    Tagle, D.A.3
  • 402
    • 33749557821 scopus 로고    scopus 로고
    • Cytotoxicity of a mutant huntingtin fragment in yeast involves early alterations in mitochondrial OXPHOS complexes II and III
    • Solans A., Zambrano A., Rodriguez M., et al. Cytotoxicity of a mutant huntingtin fragment in yeast involves early alterations in mitochondrial OXPHOS complexes II and III. Hum Mol Genet 2006, 15:3063-3081.
    • (2006) Hum Mol Genet , vol.15 , pp. 3063-3081
    • Solans, A.1    Zambrano, A.2    Rodriguez, M.3
  • 403
    • 0037155198 scopus 로고    scopus 로고
    • Expression of full-length polyglutamine-expanded Huntingtin disrupts growth factor receptor signaling in rat pheochromocytoma (PC12) cells
    • Song C., Perides G., Liu Y.F. Expression of full-length polyglutamine-expanded Huntingtin disrupts growth factor receptor signaling in rat pheochromocytoma (PC12) cells. J Biol Chem 2002, 277:6703-6707.
    • (2002) J Biol Chem , vol.277 , pp. 6703-6707
    • Song, C.1    Perides, G.2    Liu, Y.F.3
  • 404
    • 0037379416 scopus 로고    scopus 로고
    • Homozygosity for CAG mutation in Huntington disease is associated with a more severe clinical course
    • Squitieri F., Gellera C., Cannella M., et al. Homozygosity for CAG mutation in Huntington disease is associated with a more severe clinical course. Brain 2003, 126:946-955.
    • (2003) Brain , vol.126 , pp. 946-955
    • Squitieri, F.1    Gellera, C.2    Cannella, M.3
  • 405
    • 34447302317 scopus 로고    scopus 로고
    • Modulation of nucleosome dynamics in Huntington's disease
    • Stack E.C., Del Signore S.J., Luthi-Carter R., et al. Modulation of nucleosome dynamics in Huntington's disease. Hum Mol Genet 2007, 16:1164-1175.
    • (2007) Hum Mol Genet , vol.16 , pp. 1164-1175
    • Stack, E.C.1    Del Signore, S.J.2    Luthi-Carter, R.3
  • 406
    • 12944263711 scopus 로고    scopus 로고
    • The Huntington's disease protein interacts with p53 and CREB-binding protein and represses transcription
    • Steffan J.S., Kazantsev A., Spasic-Boskovic O., et al. The Huntington's disease protein interacts with p53 and CREB-binding protein and represses transcription. Proc Natl Acad Sci U S A 2000, 97:6763-6768.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 6763-6768
    • Steffan, J.S.1    Kazantsev, A.2    Spasic-Boskovic, O.3
  • 407
    • 0035909330 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors arrest polyglutamine-dependent neurodegeneration in Drosophila
    • Steffan J.S., Bodai L., Pallos J., et al. Histone deacetylase inhibitors arrest polyglutamine-dependent neurodegeneration in Drosophila. Nature 2001, 413:739-743.
    • (2001) Nature , vol.413 , pp. 739-743
    • Steffan, J.S.1    Bodai, L.2    Pallos, J.3
  • 408
    • 11144353613 scopus 로고    scopus 로고
    • SUMO modification of Huntingtin and Huntington's disease pathology
    • Steffan J.S., Agrawal N., Pallos J., et al. SUMO modification of Huntingtin and Huntington's disease pathology. Science 2004, 304:100-104.
    • (2004) Science , vol.304 , pp. 100-104
    • Steffan, J.S.1    Agrawal, N.2    Pallos, J.3
  • 409
    • 25144498379 scopus 로고    scopus 로고
    • A human protein-protein interaction network: a resource for annotating the proteome
    • Stelzl U., Worm U., Lalowski M., et al. A human protein-protein interaction network: a resource for annotating the proteome. Cell 2005, 122:957-968.
    • (2005) Cell , vol.122 , pp. 957-968
    • Stelzl, U.1    Worm, U.2    Lalowski, M.3
  • 410
    • 0031712507 scopus 로고    scopus 로고
    • De novo expansion of intermediate alleles in spinocerebellar ataxia 7
    • Stevanin G., Giunti P., Belal G.D., et al. De novo expansion of intermediate alleles in spinocerebellar ataxia 7. Hum Mol Genet 1998, 7:1809-1813.
    • (1998) Hum Mol Genet , vol.7 , pp. 1809-1813
    • Stevanin, G.1    Giunti, P.2    Belal, G.D.3
  • 411
    • 0037819516 scopus 로고    scopus 로고
    • Huntington's disease-like phenotype due to trinucleotide repeat expansions in the TBP and JPH3 genes
    • Stevanin G., Fujigasaki H., Lebre A.S., et al. Huntington's disease-like phenotype due to trinucleotide repeat expansions in the TBP and JPH3 genes. Brain 2003, 126:1599-1603.
    • (2003) Brain , vol.126 , pp. 1599-1603
    • Stevanin, G.1    Fujigasaki, H.2    Lebre, A.S.3
  • 412
    • 0027377151 scopus 로고
    • Correlation between the onset age of Huntington's disease and length of the trinucleotide repeat in IT-15
    • Stine O.C., Pleasant N., Franz M.L., et al. Correlation between the onset age 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
  • 413
    • 0028855131 scopus 로고
    • Expression of the mutant allele of IT-15 (the HD gene) in striatum and cortex of Huntington's disease patients
    • Stine O.C., Li S.H., Pleasant N., et al. Expression of the mutant allele of IT-15 (the HD gene) in striatum and cortex of Huntington's disease patients. Hum Mol Genet 1995, 4:15-18.
    • (1995) Hum Mol Genet , vol.4 , pp. 15-18
    • Stine, O.C.1    Li, S.H.2    Pleasant, N.3
  • 414
    • 25844526181 scopus 로고    scopus 로고
    • Gene expression in Huntington's disease skeletal muscle: a potential biomarker
    • Strand A.D., Aragaki A.K., Shaw D., et al. Gene expression in Huntington's disease skeletal muscle: a potential biomarker. Hum Mol Genet 2005, 14:1863-1876.
    • (2005) Hum Mol Genet , vol.14 , pp. 1863-1876
    • Strand, A.D.1    Aragaki, A.K.2    Shaw, D.3
  • 415
    • 0027432418 scopus 로고
    • Widespread expression of the human and rat Huntington's disease gene in brain and nonneural tissues
    • Strong T.V., Tagle D.A., Valdes J.M., et al. Widespread expression of the human and rat Huntington's disease gene in brain and nonneural tissues. Nat Genet 1993, 5:259-265.
    • (1993) Nat Genet , vol.5 , pp. 259-265
    • Strong, T.V.1    Tagle, D.A.2    Valdes, J.M.3
  • 416
    • 1042289730 scopus 로고    scopus 로고
    • Decreased cAMP response element-mediated transcription: an early event in exon 1 and full-length cell models of Huntington's disease that contributes to polyglutamine pathogenesis
    • Sugars K.L., Brown R., Cook L.J., et al. Decreased cAMP response element-mediated transcription: an early event in exon 1 and full-length cell models of Huntington's disease that contributes to polyglutamine pathogenesis. J Biol Chem 2004, 279:4988-4999.
    • (2004) J Biol Chem , vol.279 , pp. 4988-4999
    • Sugars, K.L.1    Brown, R.2    Cook, L.J.3
  • 417
    • 0035897405 scopus 로고    scopus 로고
    • Identities of sequestered proteins in aggregates from cells with induced polyglutamine expression
    • Suhr S.T., Senut M.C., Whitelegge J.P., et al. Identities of sequestered proteins in aggregates from cells with induced polyglutamine expression. J Cell Biol 2001, 153:283-294.
    • (2001) J Cell Biol , vol.153 , pp. 283-294
    • Suhr, S.T.1    Senut, M.C.2    Whitelegge, J.P.3
  • 418
    • 0036451321 scopus 로고    scopus 로고
    • Polyglutamine repeat length-dependent proteolysis of huntingtin
    • Sun B., Fan W., Balciunas A., et al. Polyglutamine repeat length-dependent proteolysis of huntingtin. Neurobiol Dis 2002, 11:111-122.
    • (2002) Neurobiol Dis , vol.11 , pp. 111-122
    • Sun, B.1    Fan, W.2    Balciunas, A.3
  • 419
    • 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 P.H., et al. Polyglutamine-expanded huntingtin promotes sensitization of N-methyl-d-aspartate receptors via post-synaptic density 95. J Biol Chem 2001, 276:24713-24718.
    • (2001) J Biol Chem , vol.276 , pp. 24713-24718
    • Sun, Y.1    Savanenin, A.2    Reddy, P.H.3
  • 420
    • 33645104605 scopus 로고    scopus 로고
    • Interaction of huntingtin fragments with brain membranes - clues to early dysfunction in Huntington's disease
    • Suopanki J., Gotz C., Lutsch G., et al. Interaction of huntingtin fragments with brain membranes - clues to early dysfunction in Huntington's disease. J Neurochem 2006, 96:870-884.
    • (2006) J Neurochem , vol.96 , pp. 870-884
    • Suopanki, J.1    Gotz, C.2    Lutsch, G.3
  • 421
    • 0025962030 scopus 로고
    • Prolonged infusion of quinolinic acid into rat striatum as an excitotoxic model of neurodegenerative disease
    • Susel Z., Engber T.M., Kuo S., et al. Prolonged infusion of quinolinic acid into rat striatum as an excitotoxic model of neurodegenerative disease. Neurosci Lett 1991, 121:234-238.
    • (1991) Neurosci Lett , vol.121 , pp. 234-238
    • Susel, Z.1    Engber, T.M.2    Kuo, S.3
  • 422
    • 54249158324 scopus 로고    scopus 로고
    • Ubiquitin, the proteasome and protein degradation in neuronal function and dysfunction
    • Tai H.C., Schuman E.M. Ubiquitin, the proteasome and protein degradation in neuronal function and dysfunction. Nat Rev Neurosci 2008, 9:826-838.
    • (2008) Nat Rev Neurosci , vol.9 , pp. 826-838
    • Tai, H.C.1    Schuman, E.M.2
  • 423
    • 0141742228 scopus 로고    scopus 로고
    • The predominantly HEAT-like motif structure of huntingtin and its association and coincident nuclear entry with dorsal, an NF-kB/Rel/dorsal family transcription factor
    • Takano H., Gusella J.F. The predominantly HEAT-like motif structure of huntingtin and its association and coincident nuclear entry with dorsal, an NF-kB/Rel/dorsal family transcription factor. BMC Neurosci 2002, 3:15.
    • (2002) BMC Neurosci , vol.3 , pp. 15
    • Takano, H.1    Gusella, J.F.2
  • 424
    • 0029009456 scopus 로고
    • Evidence for inter-generational instability in the CAG repeat in the MJD1 gene and for conserved haplotypes at flanking markers amongst Japanese and Caucasian subjects with Machado-Joseph disease
    • Takiyama Y., Igarashi S., Rogaeva E.A., et al. Evidence for inter-generational instability in the CAG repeat in the MJD1 gene and for conserved haplotypes at flanking markers amongst Japanese and Caucasian subjects with Machado-Joseph disease. Hum Mol Genet 1995, 4:1137-1146.
    • (1995) Hum Mol Genet , vol.4 , pp. 1137-1146
    • Takiyama, Y.1    Igarashi, S.2    Rogaeva, E.A.3
  • 425
    • 0032581184 scopus 로고    scopus 로고
    • A Japanese family with spinocerebellar ataxia type 6 which includes three individuals homozygous for an expanded CAG repeat in the SCA6/CACNL1A4 gene
    • Takiyama Y., Sakoe K., Namekawa M., et al. A Japanese family with spinocerebellar ataxia type 6 which includes three individuals homozygous for an expanded CAG repeat in the SCA6/CACNL1A4 gene. J Neurol Sci 1998, 158:141-147.
    • (1998) J Neurol Sci , vol.158 , pp. 141-147
    • Takiyama, Y.1    Sakoe, K.2    Namekawa, M.3
  • 426
    • 1342325378 scopus 로고    scopus 로고
    • Novel nuclear shuttle proteins, HDBP1 and HDBP2, bind to neuronal cell-specific cis-regulatory element in the promoter for the human Huntington's disease gene
    • Tanaka K., Shouguchi-Miyata J., Miyamoto N., et al. Novel nuclear shuttle proteins, HDBP1 and HDBP2, bind to neuronal cell-specific cis-regulatory element in the promoter for the human Huntington's disease gene. J Biol Chem 2004, 279:7275-7286.
    • (2004) J Biol Chem , vol.279 , pp. 7275-7286
    • Tanaka, K.1    Shouguchi-Miyata, J.2    Miyamoto, N.3
  • 427
    • 30744439549 scopus 로고    scopus 로고
    • Progressive phenotype and nuclear accumulation of an amino-terminal cleavage fragment in a transgenic mouse model with inducible expression of full-length mutant huntingtin
    • Tanaka Y., Igarashi S., Nakamura M., et al. Progressive phenotype and nuclear accumulation of an amino-terminal cleavage fragment in a transgenic mouse model with inducible expression of full-length mutant huntingtin. Neurobiol Dis 2006, 21:381-391.
    • (2006) Neurobiol Dis , vol.21 , pp. 381-391
    • Tanaka, Y.1    Igarashi, S.2    Nakamura, M.3
  • 428
    • 0041963057 scopus 로고    scopus 로고
    • Huntingtin and huntingtin-associated protein 1 influence neuronal calcium signaling mediated by inositol-(1, 4, 5) triphosphate receptor type 1
    • Tang T.S., Tu H., Chan E.Y., et al. Huntingtin and huntingtin-associated protein 1 influence neuronal calcium signaling mediated by inositol-(1, 4, 5) triphosphate receptor type 1. Neuron 2003, 39:227-239.
    • (2003) Neuron , vol.39 , pp. 227-239
    • Tang, T.S.1    Tu, H.2    Chan, E.Y.3
  • 429
    • 38949137395 scopus 로고    scopus 로고
    • Phylogenetic comparison of huntingtin homologues reveals the appearance of a primitive polyQ in sea urchin
    • Tartari M., Gissi C., Lo Sardo V., et al. Phylogenetic comparison of huntingtin homologues reveals the appearance of a primitive polyQ in sea urchin. Mol Biol Evol 2008, 25:330-338.
    • (2008) Mol Biol Evol , vol.25 , pp. 330-338
    • Tartari, M.1    Gissi, C.2    Lo Sardo, V.3
  • 430
    • 0026865262 scopus 로고
    • A dinucleotide repeat polymorphism at the D4S127 locus
    • Taylor S.A., Barnes G.T., MacDonald M.E., et al. A dinucleotide repeat polymorphism at the D4S127 locus. Hum Mol Genet 1992, 1:142.
    • (1992) Hum Mol Genet , vol.1 , pp. 142
    • Taylor, S.A.1    Barnes, G.T.2    MacDonald, M.E.3
  • 431
    • 0026951329 scopus 로고
    • Cloning of the α-adducin gene from the Huntington's disease candidate region of chromosome 4 by exon amplification
    • Taylor S.A.M., Snell R.G., Buckler A., et al. Cloning of the α-adducin gene from the Huntington's disease candidate region of chromosome 4 by exon amplification. Nat Genet 1992, 2:223-227.
    • (1992) Nat Genet , vol.2 , pp. 223-227
    • Taylor, S.A.M.1    Snell, R.G.2    Buckler, A.3
  • 432
    • 0027381482 scopus 로고
    • Molecular analysis of juvenile Huntington disease: the major influence on (CAG)n repeat length is the sex of the affected parent
    • Telenius H., Kremer H.P., Theilmann J., et al. Molecular analysis of juvenile Huntington disease: the major influence on (CAG)n repeat length is the sex of the affected parent. Hum Mol Genet 1993, 2:1535-1540.
    • (1993) Hum Mol Genet , vol.2 , pp. 1535-1540
    • Telenius, H.1    Kremer, H.P.2    Theilmann, J.3
  • 433
    • 0028339385 scopus 로고
    • Somatic and gonadal mosaicism of the Huntington disease gene CAG repeat in brain and sperm
    • Telenius H., Kremer B., Goldberg Y.P., et al. Somatic and gonadal mosaicism of the Huntington disease gene CAG repeat in brain and sperm. Nat Genet 1994, 6:409-414.
    • (1994) Nat Genet , vol.6 , pp. 409-414
    • Telenius, H.1    Kremer, B.2    Goldberg, Y.P.3
  • 434
    • 0028986597 scopus 로고
    • Somatic mosaicism in sperm is associated with intergenerational (CAG)n changes in Huntington disease
    • Telenius H., Almqvist E., Kremer B., et al. Somatic mosaicism in sperm is associated with intergenerational (CAG)n changes in Huntington disease. Hum Mol Genet 1995, 4:189-195.
    • (1995) Hum Mol Genet , vol.4 , pp. 189-195
    • Telenius, H.1    Almqvist, E.2    Kremer, B.3
  • 435
    • 33747760663 scopus 로고    scopus 로고
    • Motor and cognitive improvement by deep brain stimulation in a transgenic rat model of Huntington's disease
    • Temel Y., Cao C., Vlamings R., et al. Motor and cognitive improvement by deep brain stimulation in a transgenic rat model of Huntington's disease. Neurosci Lett 2006, 406:138-141.
    • (2006) Neurosci Lett , vol.406 , pp. 138-141
    • Temel, Y.1    Cao, C.2    Vlamings, R.3
  • 436
    • 0037168642 scopus 로고    scopus 로고
    • Mutational analysis of the structural organization of polyglutamine aggregates
    • Thakur A.K., Wetzel R. Mutational analysis of the structural organization of polyglutamine aggregates. Proc Natl Acad Sci U S A 2002, 99:17014-17019.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 17014-17019
    • Thakur, A.K.1    Wetzel, R.2
  • 437
    • 0034703869 scopus 로고    scopus 로고
    • Dominant phenotypes produced by the HD mutation in STHdh(Q111) striatal cells
    • Trettel F., Rigamonti D., Hilditch-Maguire P., et al. Dominant phenotypes produced by the HD mutation in STHdh(Q111) striatal cells. Hum Mol Genet 2000, 9:2799-2809.
    • (2000) Hum Mol Genet , vol.9 , pp. 2799-2809
    • Trettel, F.1    Rigamonti, D.2    Hilditch-Maguire, P.3
  • 438
    • 0028234720 scopus 로고
    • Instability of CAG repeats in Huntington's disease: relation to parental transmission and age of onset
    • Trottier Y., Biancalana V., Mandel J.L. Instability of CAG repeats in Huntington's disease: relation to parental transmission and age of onset. J Med Genet 1994, 31:377-382.
    • (1994) J Med Genet , vol.31 , pp. 377-382
    • Trottier, Y.1    Biancalana, V.2    Mandel, J.L.3
  • 439
    • 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, 10:104-110.
    • (1995) Nat Genet , vol.10 , pp. 104-110
    • Trottier, Y.1    Devys, D.2    Imbert, G.3
  • 440
    • 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
  • 441
    • 49349110821 scopus 로고    scopus 로고
    • Huntington's disease: revisiting the aggregation hypothesis in polyglutamine neurodegenerative diseases
    • Truant R., Atwal R.S., Desmond C., et al. Huntington's disease: revisiting the aggregation hypothesis in polyglutamine neurodegenerative diseases. Febs J 2008, 275:4252-4262.
    • (2008) Febs J , vol.275 , pp. 4252-4262
    • Truant, R.1    Atwal, R.S.2    Desmond, C.3
  • 442
    • 33845357970 scopus 로고    scopus 로고
    • Mutant huntingtin inhibits clathrin-independent endocytosis and causes accumulation of cholesterol in vitro and in vivo
    • Trushina E., Singh R.D., Dyer R.B., et al. Mutant huntingtin inhibits clathrin-independent endocytosis and causes accumulation of cholesterol in vitro and in vivo. Hum Mol Genet 2006, 15:3578-3591.
    • (2006) Hum Mol Genet , vol.15 , pp. 3578-3591
    • Trushina, E.1    Singh, R.D.2    Dyer, R.B.3
  • 443
    • 0030819255 scopus 로고    scopus 로고
    • Huntington's disease gene product, huntingtin, associates with microtubules in vitro
    • Tukamoto T., Nukina N., Ide K., et al. Huntington's disease gene product, huntingtin, associates with microtubules in vitro. Brain Res Mol Brain Res 1997, 51:8-14.
    • (1997) Brain Res Mol Brain Res , vol.51 , pp. 8-14
    • Tukamoto, T.1    Nukina, N.2    Ide, K.3
  • 444
    • 0035543870 scopus 로고    scopus 로고
    • Production of transgenic miniature pigs by pronuclear microinjection
    • Uchida M., Shimatsu Y., Onoe K., et al. Production of transgenic miniature pigs by pronuclear microinjection. Transgenic Res 2001, 10:577-582.
    • (2001) Transgenic Res , vol.10 , pp. 577-582
    • Uchida, M.1    Shimatsu, Y.2    Onoe, K.3
  • 445
    • 0032897760 scopus 로고    scopus 로고
    • Impaired synaptic plasticity in mice carrying the Huntington's disease mutation
    • Usdin M.T., Shelbourne P.F., Myers R.M., et al. Impaired synaptic plasticity in mice carrying the Huntington's disease mutation. Hum Mol Genet 1999, 8:839-846.
    • (1999) Hum Mol Genet , vol.8 , pp. 839-846
    • Usdin, M.T.1    Shelbourne, P.F.2    Myers, R.M.3
  • 446
    • 33947286031 scopus 로고    scopus 로고
    • Phenotypic abnormalities in the YAC128 mouse model of Huntington disease are penetrant on multiple genetic backgrounds and modulated by strain
    • Van Raamsdonk J.M., Metzler M., Slow E., et al. Phenotypic abnormalities in the YAC128 mouse model of Huntington disease are penetrant on multiple genetic backgrounds and modulated by strain. Neurobiol Dis 2007, 26:189-200.
    • (2007) Neurobiol Dis , vol.26 , pp. 189-200
    • Van Raamsdonk, J.M.1    Metzler, M.2    Slow, E.3
  • 447
    • 0642334395 scopus 로고    scopus 로고
    • Aberrant A2A receptor function in peripheral blood cells in Huntington's disease
    • Varani K., Abbracchio M.P., Cannella M., et al. Aberrant A2A receptor function in peripheral blood cells in Huntington's disease. Faseb J 2003, 17:2148-2150.
    • (2003) Faseb J , vol.17 , pp. 2148-2150
    • Varani, K.1    Abbracchio, M.P.2    Cannella, M.3
  • 448
    • 0031867231 scopus 로고    scopus 로고
    • Wild-type and mutant huntingtins function in vesicle trafficking in the secretory and endocytic pathways
    • Velier J., Kim M., Schwarz C., et al. Wild-type and mutant huntingtins function in vesicle trafficking in the secretory and endocytic pathways. Exp Neurol 1998, 152:34-40.
    • (1998) Exp Neurol , vol.152 , pp. 34-40
    • Velier, J.1    Kim, M.2    Schwarz, C.3
  • 449
    • 1842766144 scopus 로고    scopus 로고
    • Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins
    • Venkatraman P., Wetzel R., Tanaka M., et al. Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins. Mol Cell 2004, 14:95-104.
    • (2004) Mol Cell , vol.14 , pp. 95-104
    • Venkatraman, P.1    Wetzel, R.2    Tanaka, M.3
  • 450
    • 0141959170 scopus 로고    scopus 로고
    • Creatine supplementation in Huntington's disease: a placebo-controlled pilot trial
    • Verbessem P., Lemiere J., Eijnde B.O., et al. Creatine supplementation in Huntington's disease: a placebo-controlled pilot trial. Neurology 2003, 61:925-930.
    • (2003) Neurology , vol.61 , pp. 925-930
    • Verbessem, P.1    Lemiere, J.2    Eijnde, B.O.3
  • 451
    • 0025905795 scopus 로고
    • Identification of a gene (FMR-1) containing a CGG repeat coincident with a breakpoint cluster region exhibiting length variation in fragile X syndrome
    • Verkerk A.J., Pieretti M., Sutcliffe J.S., et al. Identification of a gene (FMR-1) containing a CGG repeat coincident with a breakpoint cluster region exhibiting length variation in fragile X syndrome. Cell 1991, 65:905-914.
    • (1991) Cell , vol.65 , pp. 905-914
    • Verkerk, A.J.1    Pieretti, M.2    Sutcliffe, J.S.3
  • 452
    • 0033612390 scopus 로고    scopus 로고
    • Structural view of the Ran-Importin beta interaction at 2.3 A resolution
    • Vetter I.R., Arndt A., Kutay U., et al. Structural view of the Ran-Importin beta interaction at 2.3 A resolution. Cell 1999, 97:635-646.
    • (1999) Cell , vol.97 , pp. 635-646
    • Vetter, I.R.1    Arndt, A.2    Kutay, U.3
  • 453
    • 0037444426 scopus 로고    scopus 로고
    • Transgenic rat model of Huntington's disease
    • von Horsten S., Schmitt I., Nguyen H.P., et al. Transgenic rat model of Huntington's disease. Hum Mol Genet 2003, 12:617-624.
    • (2003) Hum Mol Genet , vol.12 , pp. 617-624
    • von Horsten, S.1    Schmitt, I.2    Nguyen, H.P.3
  • 454
    • 36949012566 scopus 로고    scopus 로고
    • Huntington disease models and human neuropathology: similarities and differences
    • Vonsattel J.P. Huntington disease models and human neuropathology: similarities and differences. Acta Neuropathol 2008, 115:55-69.
    • (2008) Acta Neuropathol , vol.115 , pp. 55-69
    • Vonsattel, J.P.1
  • 455
    • 41549129945 scopus 로고    scopus 로고
    • Impaired ubiquitin-proteasome system activity in the synapses of Huntington's disease mice
    • Wang J., Wang C.E., Orr A., et al. Impaired ubiquitin-proteasome system activity in the synapses of Huntington's disease mice. J Cell Biol 2008, 180:1177-1189.
    • (2008) J Cell Biol , vol.180 , pp. 1177-1189
    • Wang, J.1    Wang, C.E.2    Orr, A.3
  • 456
    • 0031056478 scopus 로고    scopus 로고
    • HIP-I: a huntingtin interacting protein isolated by the yeast two-hybrid system
    • Wanker E.E., Rovira C., Scherzinger E., et al. HIP-I: a huntingtin interacting protein isolated by the yeast two-hybrid system. Hum Mol Genet 1997, 6:487-495.
    • (1997) Hum Mol Genet , vol.6 , pp. 487-495
    • Wanker, E.E.1    Rovira, C.2    Scherzinger, E.3
  • 457
    • 20444448900 scopus 로고    scopus 로고
    • Huntingtin phosphorylation on serine 421 is significantly reduced in the striatum and by polyglutamine expansion in vivo
    • Warby S.C., Chan E.Y., Metzler M., et al. Huntingtin phosphorylation on serine 421 is significantly reduced in the striatum and by polyglutamine expansion in vivo. Hum Mol Genet 2005, 14:1569-1577.
    • (2005) Hum Mol Genet , vol.14 , pp. 1569-1577
    • Warby, S.C.1    Chan, E.Y.2    Metzler, M.3
  • 458
    • 59049093839 scopus 로고    scopus 로고
    • Phosphorylation of huntingtin reduces the accumulation of its nuclear fragments
    • Warby S.C., Doty C.N., Graham R.K., et al. Phosphorylation of huntingtin reduces the accumulation of its nuclear fragments. Mol Cell Neurosci 2008, 40:121-127.
    • (2008) Mol Cell Neurosci , vol.40 , pp. 121-127
    • Warby, S.C.1    Doty, C.N.2    Graham, R.K.3
  • 459
    • 48049092846 scopus 로고    scopus 로고
    • Activated caspase-6 and caspase-6-cleaved fragments of huntingtin specifically colocalize in the nucleus
    • Warby S.C., Doty C.N., Graham R.K., et al. Activated caspase-6 and caspase-6-cleaved fragments of huntingtin specifically colocalize in the nucleus. Hum Mol Genet 2008, 17:2390-2404.
    • (2008) Hum Mol Genet , vol.17 , pp. 2390-2404
    • Warby, S.C.1    Doty, C.N.2    Graham, R.K.3
  • 460
    • 0034665029 scopus 로고    scopus 로고
    • De novo expansion of a CAG repeat in a Japanese patient with sporadic Huntington's disease
    • Watanabe M., Satoh A., Kanemoto M., et al. De novo expansion of a CAG repeat in a Japanese patient with sporadic Huntington's disease. J Neurol Sci 2000, 178:159-162.
    • (2000) J Neurol Sci , vol.178 , pp. 159-162
    • Watanabe, M.1    Satoh, A.2    Kanemoto, M.3
  • 461
    • 0030787762 scopus 로고    scopus 로고
    • Toward understanding the molecular pathology of Huntington's disease
    • Wellington C.L., Brinkman R.R., O'Kusky J.R., et al. Toward understanding the molecular pathology of Huntington's disease. Brain Pathol 1997, 7:979-1002.
    • (1997) Brain Pathol , vol.7 , pp. 979-1002
    • Wellington, C.L.1    Brinkman, R.R.2    O'Kusky, J.R.3
  • 462
    • 0032502715 scopus 로고    scopus 로고
    • Caspase cleavage of gene products associated with triplet expansion disorders generates truncated fragments containing the polyglutamine tract
    • Wellington C.L., Ellerby L.M., Hackam A.S., 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
  • 463
    • 0034733607 scopus 로고    scopus 로고
    • Inhibiting caspase cleavage of huntingtin reduces toxicity and aggregate formation in neuronal and nonneuronal cells
    • Wellington C.L., Singaraja R., Ellerby L., et al. Inhibiting caspase cleavage of huntingtin reduces toxicity and aggregate formation in neuronal and nonneuronal 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
  • 464
    • 0037107151 scopus 로고    scopus 로고
    • Caspase cleavage of mutant huntingtin precedes neurodegeneration in Huntington's disease
    • Wellington C.L., Ellerby L.M., Gutekunst C.A., et al. Caspase cleavage of mutant huntingtin precedes neurodegeneration in Huntington's disease. J Neurosci 2002, 22:7862-7872.
    • (2002) J Neurosci , vol.22 , pp. 7862-7872
    • Wellington, C.L.1    Ellerby, L.M.2    Gutekunst, C.A.3
  • 465
    • 20144366969 scopus 로고    scopus 로고
    • HSJ1 is a neuronal shuttling factor for the sorting of chaperone clients to the proteasome
    • Westhoff B., Chapple J.P., van der Spuy J., et al. HSJ1 is a neuronal shuttling factor for the sorting of chaperone clients to the proteasome. Curr Biol 2005, 15:1058-1064.
    • (2005) Curr Biol , vol.15 , pp. 1058-1064
    • Westhoff, B.1    Chapple, J.P.2    van der Spuy, J.3
  • 466
    • 0021950633 scopus 로고
    • A DNA polymorphism for Huntington's disease marks the future
    • Wexler N.S., Conneally P.M., Housman D., et al. A DNA polymorphism for Huntington's disease marks the future. Arch Neurol 1985, 42:20-24.
    • (1985) Arch Neurol , vol.42 , pp. 20-24
    • Wexler, N.S.1    Conneally, P.M.2    Housman, D.3
  • 467
    • 33750437278 scopus 로고    scopus 로고
    • Thermoregulatory and metabolic defects in Huntington's disease transgenic mice implicate PGC-1alpha in Huntington's disease neurodegeneration
    • Weydt P., Pineda V.V., Torrence A.E., et al. Thermoregulatory and metabolic defects in Huntington's disease transgenic mice implicate PGC-1alpha in Huntington's disease neurodegeneration. Cell Metab 2006, 4:349-362.
    • (2006) Cell Metab , vol.4 , pp. 349-362
    • Weydt, P.1    Pineda, V.V.2    Torrence, A.E.3
  • 468
    • 58649094617 scopus 로고    scopus 로고
    • The gene coding for PGC-1alpha modifies age at onset in Huntington's Disease
    • Weydt P., Soyal S.M., Gellera C., et al. The gene coding for PGC-1alpha modifies age at onset in Huntington's Disease. Mol Neurodegener 2009, 4:3.
    • (2009) Mol Neurodegener , vol.4 , pp. 3
    • Weydt, P.1    Soyal, S.M.2    Gellera, C.3
  • 469
    • 0032938295 scopus 로고    scopus 로고
    • Length-dependent gametic CAG repeat instability in the Huntington's disease knock-in mouse
    • Wheeler V.C., Auerbach W., White J.K., et al. Length-dependent gametic CAG repeat instability in the Huntington's disease knock-in mouse. Hum Mol Genet 1999, 8:115-122.
    • (1999) Hum Mol Genet , vol.8 , pp. 115-122
    • Wheeler, V.C.1    Auerbach, W.2    White, J.K.3
  • 470
    • 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 V.C., White J.K., Gutekunst C.A., 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
  • 471
    • 0037321290 scopus 로고    scopus 로고
    • Mismatch repair gene Msh2 modifies the timing of early disease in Hdh(Q111) striatum
    • Wheeler V.C., Lebel L.A., Vrbanac V., et al. Mismatch repair gene Msh2 modifies the timing of early disease in Hdh(Q111) striatum. Hum Mol Genet 2003, 12:273-281.
    • (2003) Hum Mol Genet , vol.12 , pp. 273-281
    • Wheeler, V.C.1    Lebel, L.A.2    Vrbanac, V.3
  • 472
    • 0030613177 scopus 로고    scopus 로고
    • Huntingtin is required for neurogenesis and is not impaired by the Huntington's disease CAG expansion
    • White J.K., Auerbach W., Duyao M.P., 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
  • 473
    • 3843125621 scopus 로고    scopus 로고
    • Genetic testing and mental health: the model of Huntington disease
    • Williams J.K., Schutte D.L. Genetic testing and mental health: the model of Huntington disease. Online J Issues Nurs 2000, 5:3.
    • (2000) Online J Issues Nurs , vol.5 , pp. 3
    • Williams, J.K.1    Schutte, D.L.2
  • 474
    • 55549086868 scopus 로고    scopus 로고
    • The deubiquitinating enzyme ataxin-3, a polyglutamine disease protein, edits Lys63 linkages in mixed linkage ubiquitin chains
    • Winborn B.J., Travis S.M., Todi S.V., et al. The deubiquitinating enzyme ataxin-3, a polyglutamine disease protein, edits Lys63 linkages in mixed linkage ubiquitin chains. J Biol Chem 2008, 283:26436-26443.
    • (2008) J Biol Chem , vol.283 , pp. 26436-26443
    • Winborn, B.J.1    Travis, S.M.2    Todi, S.V.3
  • 475
    • 0028006676 scopus 로고
    • 3-Nitropropionic acid toxicity in the striatum
    • Wullner U., Young A.B., Penney J.B., et al. 3-Nitropropionic acid toxicity in the striatum. J Neurochem 1994, 63:1772-1781.
    • (1994) J Neurochem , vol.63 , pp. 1772-1781
    • Wullner, U.1    Young, A.B.2    Penney, J.B.3
  • 476
    • 0035880474 scopus 로고    scopus 로고
    • Polyglutamine expansions cause decreased CRE-mediated transcription and early gene expression changes prior to cell death in an inducible cell model of Huntington's disease
    • Wyttenbach A., Swartz J., Kita H., et al. Polyglutamine expansions cause decreased CRE-mediated transcription and early gene expression changes prior to cell death in an inducible cell model of Huntington's disease. Hum Mol Genet 2001, 10:1829-1845.
    • (2001) Hum Mol Genet , vol.10 , pp. 1829-1845
    • Wyttenbach, A.1    Swartz, J.2    Kita, H.3
  • 477
    • 0037701612 scopus 로고    scopus 로고
    • Huntingtin contains a highly conserved nuclear export signal
    • Xia J., Lee D.H., Taylor J., et al. Huntingtin contains a highly conserved nuclear export signal. Hum Mol Genet 2003, 12:1393-1403.
    • (2003) Hum Mol Genet , vol.12 , pp. 1393-1403
    • Xia, J.1    Lee, D.H.2    Taylor, J.3
  • 478
    • 0034737299 scopus 로고    scopus 로고
    • Reversal of neuropathology and motor dysfunction in a conditional model of Huntington's disease
    • Yamamoto A., Lucas J.J., 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
  • 479
    • 33745627659 scopus 로고    scopus 로고
    • Palmitoylation of huntingtin by HIP14 is essential for its trafficking and function
    • Yanai A., Huang K., Kang R., et al. Palmitoylation of huntingtin by HIP14 is essential for its trafficking and function. Nat Neurosci 2006, 9:824-831.
    • (2006) Nat Neurosci , vol.9 , pp. 824-831
    • Yanai, A.1    Huang, K.2    Kang, R.3
  • 480
    • 33846696670 scopus 로고    scopus 로고
    • Ubiquitin ligase Hrd1 enhances the degradation and suppresses the toxicity of polyglutamine-expanded huntingtin
    • Yang H., Zhong X., Ballar P., et al. Ubiquitin ligase Hrd1 enhances the degradation and suppresses the toxicity of polyglutamine-expanded huntingtin. Exp Cell Res 2007, 313:538-550.
    • (2007) Exp Cell Res , vol.313 , pp. 538-550
    • Yang, H.1    Zhong, X.2    Ballar, P.3
  • 481
    • 45149105779 scopus 로고    scopus 로고
    • Towards a transgenic model of Huntington's disease in a non-human primate
    • Yang S.H., Cheng P.H., Banta H., et al. Towards a transgenic model of Huntington's disease in a non-human primate. Nature 2008, 453:921-924.
    • (2008) Nature , vol.453 , pp. 921-924
    • Yang, S.H.1    Cheng, P.H.2    Banta, H.3
  • 482
    • 33744532300 scopus 로고    scopus 로고
    • Neurochemistry of Huntington's disease
    • Oxford Medical Publications, London, G.P. Bates, P.S. Harper, A.L. Jones (Eds.)
    • Yohrling G.J., Cha J.H. Neurochemistry of Huntington's disease. Huntington's Disease 2002, 276-308. Oxford Medical Publications, London. 3rd Edn. G.P. Bates, P.S. Harper, A.L. Jones (Eds.).
    • (2002) Huntington's Disease , pp. 276-308
    • Yohrling, G.J.1    Cha, J.H.2
  • 483
    • 0038512215 scopus 로고    scopus 로고
    • Mutant huntingtin increases nuclear corepressor function and enhances ligand-dependent nuclear hormone receptor activation
    • Yohrling G.J., Farrell L.A., Hollenberg A.N., et al. Mutant huntingtin increases nuclear corepressor function and enhances ligand-dependent nuclear hormone receptor activation. Mol Cell Neurosci 2003, 23:28-38.
    • (2003) Mol Cell Neurosci , vol.23 , pp. 28-38
    • Yohrling, G.J.1    Farrell, L.A.2    Hollenberg, A.N.3
  • 484
    • 0022553413 scopus 로고
    • PET scan investigations of Huntington's disease: cerebral metabolic correlates of neurological features and functional decline
    • Young A.B., Penney J.B., Starosta-Rubinstein S., et al. PET scan investigations of Huntington's disease: cerebral metabolic correlates of neurological features and functional decline. Ann Neurol 1986, 20:296-303.
    • (1986) Ann Neurol , vol.20 , pp. 296-303
    • Young, A.B.1    Penney, J.B.2    Starosta-Rubinstein, S.3
  • 485
    • 57049184027 scopus 로고    scopus 로고
    • Phosphorylation of mutant huntingtin at S421 restores anterograde and retrograde transport in neurons
    • Zala D., Colin E., Rangone H., et al. Phosphorylation of mutant huntingtin at S421 restores anterograde and retrograde transport in neurons. Hum Mol Genet 2008, 17:3837-3846.
    • (2008) Hum Mol Genet , vol.17 , pp. 3837-3846
    • Zala, D.1    Colin, E.2    Rangone, H.3
  • 486
    • 84993912315 scopus 로고
    • Increased apoptosis and early embryonic lethality in mice nullizygous for the Huntington's disease gene homologue
    • Zeitlin S., Liu J.P., Chapman D.L., et al. Increased apoptosis and early embryonic lethality in mice nullizygous for the Huntington's disease gene homologue. Nat Genet 1995, 11:155-163.
    • (1995) Nat Genet , vol.11 , pp. 155-163
    • Zeitlin, S.1    Liu, J.P.2    Chapman, D.L.3
  • 487
    • 43549111889 scopus 로고    scopus 로고
    • Elucidating a normal function of huntingtin by functional and microarray analysis of huntingtin-null mouse embryonic fibroblasts
    • Zhang H., Das S., Li Q.Z., et al. Elucidating a normal function of huntingtin by functional and microarray analysis of huntingtin-null mouse embryonic fibroblasts. BMC Neurosci 2008, 9:38.
    • (2008) BMC Neurosci , vol.9 , pp. 38
    • Zhang, H.1    Das, S.2    Li, Q.Z.3
  • 488
    • 20044390015 scopus 로고    scopus 로고
    • A potent small molecule inhibits polyglutamine aggregation in Huntington's disease neurons and suppresses neurodegeneration in vivo
    • Zhang X., Smith D.L., Meriin A.B., 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, 102:892-897.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 892-897
    • Zhang, X.1    Smith, D.L.2    Meriin, A.B.3
  • 489
    • 0141891952 scopus 로고    scopus 로고
    • Huntingtin forms toxic NH2-terminal fragment complexes that are promoted by the age-dependent decrease in proteasome activity
    • Zhou H., Cao F., Wang Z., et al. Huntingtin forms toxic NH2-terminal fragment complexes that are promoted by the age-dependent decrease in proteasome activity. J Cell Biol 2003, 163:109-118.
    • (2003) J Cell Biol , vol.163 , pp. 109-118
    • Zhou, H.1    Cao, F.2    Wang, Z.3
  • 490
    • 0031012399 scopus 로고    scopus 로고
    • Autosomal dominant cerebellar ataxia (SCA6) associated with small polyglutamine expansions in the alpha 1A-voltage-dependent calcium channel
    • Zhuchenko O., Bailey J., Bonnen P., et al. Autosomal dominant cerebellar ataxia (SCA6) associated with small polyglutamine expansions in the alpha 1A-voltage-dependent calcium channel. Nat Genet 1997, 15:62-69.
    • (1997) Nat Genet , vol.15 , pp. 62-69
    • Zhuchenko, O.1    Bailey, J.2    Bonnen, P.3
  • 491
    • 52949138674 scopus 로고    scopus 로고
    • On the nature of human housekeeping genes
    • Zhu J., He F., Hu S., et al. On the nature of human housekeeping genes. Trends Genet 2008, 24:481-484.
    • (2008) Trends Genet , vol.24 , pp. 481-484
    • Zhu, J.1    He, F.2    Hu, S.3
  • 492
    • 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, 293:493-498.
    • (2001) Science , vol.293 , pp. 493-498
    • Zuccato, C.1    Ciammola, A.2    Rigamonti, D.3
  • 493
    • 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
  • 494
    • 0035076389 scopus 로고    scopus 로고
    • Different types of repeat expansion in the TATA-binding protein gene are associated with a new form of inherited ataxia
    • Zuhlke C., Hellenbroich Y., Dalski A., et al. Different types of repeat expansion in the TATA-binding protein gene are associated with a new form of inherited ataxia. Eur J Hum Genet 2001, 9:160-164.
    • (2001) Eur J Hum Genet , vol.9 , pp. 160-164
    • Zuhlke, C.1    Hellenbroich, Y.2    Dalski, A.3
  • 495
    • 85047698133 scopus 로고    scopus 로고
    • Spinocerebellar ataxia type 1 (SCA1): phenotype-genotype correlation studies in intermediate alleles
    • Zuhlke C., Dalski A., Hellenbroich Y., et al. Spinocerebellar ataxia type 1 (SCA1): phenotype-genotype correlation studies in intermediate alleles. Eur J Hum Genet 2002, 10:204-209.
    • (2002) Eur J Hum Genet , vol.10 , pp. 204-209
    • Zuhlke, C.1    Dalski, A.2    Hellenbroich, Y.3
  • 496
    • 0037321835 scopus 로고    scopus 로고
    • Phenotypical variability of expanded alleles in the TATA-binding protein gene. Reduced penetrance in SCA17?
    • Zuhlke C., Gehlken U., Hellenbroich Y., et al. Phenotypical variability of expanded alleles in the TATA-binding protein gene. Reduced penetrance in SCA17?. J Neurol 2003, 250:161-163.
    • (2003) J Neurol , vol.250 , pp. 161-163
    • Zuhlke, C.1    Gehlken, U.2    Hellenbroich, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.