메뉴 건너뛰기




Volumn 33, Issue 3, 2006, Pages 278-291

Canadian association of neurosciences review: Polyglutamine expansion neurodegenerative diseases

Author keywords

[No Author keywords available]

Indexed keywords

4 (1 AMINOETHYL) N (4 PYRIDYL)CYCLOHEXANECARBOXAMIDE; ATAXIN 1; ATAXIN 7; CYCLOOXYGENASE 1 INHIBITOR; CYCLOOXYGENASE 2 INHIBITOR; ETORICOXIB; IMATINIB; POLYGLUTAMINE; PROTEASOME; PROTEIN TYROSINE KINASE INHIBITOR; REPETITIVE DNA;

EID: 33748475640     PISSN: 03171671     EISSN: None     Source Type: Journal    
DOI: 10.1017/S031716710000514X     Document Type: Review
Times cited : (10)

References (193)
  • 1
    • 0027256423 scopus 로고
    • Direct detection of novel expanded trinucleotide repeats in the human genome
    • Schalling M, Hudson TJ, Buetow KH, Housman DE. Direct detection of novel expanded trinucleotide repeats in the human genome. Nat Genet. 1993; 4(2): 135-9.
    • (1993) Nat Genet , vol.4 , Issue.2 , pp. 135-139
    • Schalling, M.1    Hudson, T.J.2    Buetow, K.H.3    Housman, D.E.4
  • 2
    • 0028147293 scopus 로고
    • Expression of (cac)n/(gtg)n simple repetitive sequences in mRNA of human lymphocytes
    • Epplen C, Epplen J T. Expression of (cac)n/(gtg)n simple repetitive sequences in mRNA of human lymphocytes. Hum Genet. 1994; 93(1): 35-41.
    • (1994) Hum Genet , vol.93 , Issue.1 , pp. 35-41
    • Epplen, C.1    Epplen, J.T.2
  • 3
    • 0025800526 scopus 로고
    • Androgen receptor gene mutations in X-linked spinal and bulbar muscular atrophy
    • La Spada AR, Wilson EM, Lubahn DB, Harding AE, Fischbeck KH. Androgen receptor gene mutations in X-linked spinal and bulbar muscular atrophy. Nature. 1991; 352(6330): 77-9.
    • (1991) Nature , vol.352 , Issue.6330 , pp. 77-79
    • La Spada, A.R.1    Wilson, E.M.2    Lubahn, D.B.3    Harding, A.E.4    Fischbeck, K.H.5
  • 4
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • The Huntington's Disease Collaborative Research Group
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. The Huntington's Disease Collaborative Research Group. Cell. 1993; 72(6): 971-83.
    • (1993) Cell , vol.72 , Issue.6 , pp. 971-983
  • 5
    • 0028143527 scopus 로고
    • CAG expansions in a novel gene for Machado-Joseph disease at chromosome 14q32.1
    • Kawaguchi Y, Okamoto T, Taniwaki M, Aizawa M, Inoue M, Katayama S, et al. CAG expansions in a novel gene for Machado-Joseph disease at chromosome 14q32.1. Nat Genet. 1994; 8(3): 221-8.
    • (1994) Nat Genet , vol.8 , Issue.3 , pp. 221-228
    • Kawaguchi, Y.1    Okamoto, T.2    Taniwaki, M.3    Aizawa, M.4    Inoue, M.5    Katayama, S.6
  • 7
    • 0028009935 scopus 로고
    • Enzymatic amplification of synthetic oligodeoxyribonucleotides: Implications for triplet repeat expansions in the human genome
    • Behn-Krappa A, Doerfler W. Enzymatic amplification of synthetic oligodeoxyribonucleotides: implications for triplet repeat expansions in the human genome. Hum Mutat. 1994; 3(1): 19-24.
    • (1994) Hum Mutat , vol.3 , Issue.1 , pp. 19-24
    • Behn-Krappa, A.1    Doerfler, W.2
  • 8
    • 0029035710 scopus 로고
    • Gametic and somatic tissue-specific heterogeneity of the expanded SCA1 CAG repeat in spinocerebellar ataxia type 1
    • Chong SS, McCall AE, Cota J, Subramony SH, Orr HT, Hughes MR, et al. Gametic and somatic tissue-specific heterogeneity of the expanded SCA1 CAG repeat in spinocerebellar ataxia type 1. Nat Genet. 1995; 10(3): 344-50.
    • (1995) Nat Genet , vol.10 , Issue.3 , pp. 344-350
    • Chong, S.S.1    McCall, A.E.2    Cota, J.3    Subramony, S.H.4    Orr, H.T.5    Hughes, M.R.6
  • 9
    • 0029151475 scopus 로고
    • Marked phenotypic heterogeneity associated with expansion of a CAG repeat sequence at the spinocerebellar ataxia 3/Machado-Joseph disease locus
    • Cancel G, Abbas N, Stevanin G, Durr A, Chneiweiss H, Neri C, et al. Marked phenotypic heterogeneity associated with expansion of a CAG repeat sequence at the spinocerebellar ataxia 3/Machado-Joseph disease locus. Am J Hum Genet. 1995; 57(4): 809-16.
    • (1995) Am J Hum Genet , vol.57 , Issue.4 , pp. 809-816
    • Cancel, G.1    Abbas, N.2    Stevanin, G.3    Durr, A.4    Chneiweiss, H.5    Neri, C.6
  • 10
    • 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(5): 377-82.
    • (1994) J Med Genet , vol.31 , Issue.5 , pp. 377-382
    • Trottier, Y.1    Biancalana, V.2    Mandel, J.L.3
  • 11
    • 3042678165 scopus 로고    scopus 로고
    • Evidence for a modifier of onset age in Huntington disease linked to the HD gene in 4pl6
    • Djousse L, Knowlton B, Hayden MR, Almqvist EW, Brinkman RR, Ross CA, et al. Evidence for a modifier of onset age in Huntington disease linked to the HD gene in 4pl6. Neurogenetics. 2004; 5(2): 109-14.
    • (2004) Neurogenetics , vol.5 , Issue.2 , pp. 109-114
    • Djousse, L.1    Knowlton, B.2    Hayden, M.R.3    Almqvist, E.W.4    Brinkman, R.R.5    Ross, C.A.6
  • 12
    • 0041385579 scopus 로고    scopus 로고
    • A genome scan for modifiers of age at onset in Huntington disease: The HD MAPS study
    • Li JL, Hayden MR, Almqvist EW, Brinkman RR, Durr A, Dode C, et al. A genome scan for modifiers of age at onset in Huntington disease: The HD MAPS study. Am J Hum Genet. 2003; 73(3): 682-7.
    • (2003) Am J Hum Genet , vol.73 , Issue.3 , pp. 682-687
    • Li, J.L.1    Hayden, M.R.2    Almqvist, E.W.3    Brinkman, R.R.4    Durr, A.5    Dode, C.6
  • 13
    • 0028058252 scopus 로고
    • Effects of the sex of myotonic dystrophy patients on the unstable triplet repeat in their affected offspring
    • Ashizawa T, Dunne PW, Ward PA, Seltzer WK, Richards CS, Effects of the sex of myotonic dystrophy patients on the unstable triplet repeat in their affected offspring. Neurology. 1994; 44(1): 120-2.
    • (1994) Neurology , vol.44 , Issue.1 , pp. 120-122
    • Ashizawa, T.1    Dunne, P.W.2    Ward, P.A.3    Seltzer, W.K.4    Richards, C.S.5
  • 14
    • 0029298231 scopus 로고
    • Gain of glutamines, gain of function?
    • Housman D, Gain of glutamines, gain of function? Nat Genet. 1995; 10(1): 3-4.
    • (1995) Nat Genet , vol.10 , Issue.1 , pp. 3-4
    • Housman, D.1
  • 16
    • 0033926497 scopus 로고    scopus 로고
    • United Kingdom experience with presymptomatic testing of individuals at 25% risk for Huntington's disease
    • Benjamin CM, Lashwood A. United Kingdom experience with presymptomatic testing of individuals at 25% risk for Huntington's disease. Clin Genet. 2000; 58(1): 41-9.
    • (2000) Clin Genet , vol.58 , Issue.1 , pp. 41-49
    • Benjamin, C.M.1    Lashwood, A.2
  • 17
    • 1842477303 scopus 로고    scopus 로고
    • A new model for prediction of the age of onset and penetrance for Huntington's disease based on CAG length
    • Langbehn DR, Brinkman RR, Falush D, Paulsen JS, Hayden MR. A new model for prediction of the age of onset and penetrance for Huntington's disease based on CAG length. Clin Genet. 2004; 65(4): 267-77.
    • (2004) Clin Genet , vol.65 , Issue.4 , pp. 267-277
    • Langbehn, D.R.1    Brinkman, R.R.2    Falush, D.3    Paulsen, J.S.4    Hayden, M.R.5
  • 18
    • 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, Cozens B, Harper A, Hetherington C, 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(3): 493-506.
    • (1996) Cell , vol.87 , Issue.3 , pp. 493-506
    • Mangiarini, L.1    Sathasivam, K.2    Seller, M.3    Cozens, B.4    Harper, A.5    Hetherington, C.6
  • 19
    • 5444248681 scopus 로고    scopus 로고
    • Recovery from polyglutamine-induced neurodegeneration in conditional SCA1 transgenic mice
    • Zu T, Duvick LA, Kaytor MD, Berlinger MS, Zoghbi HY, Clark HB, et al. Recovery from polyglutamine-induced neurodegeneration in conditional SCA1 transgenic mice. J Neurosci. 2004; 24(40): 8853-61.
    • (2004) J Neurosci , vol.24 , Issue.40 , pp. 8853-8861
    • Zu, T.1    Duvick, L.A.2    Kaytor, M.D.3    Berlinger, M.S.4    Zoghbi, H.Y.5    Clark, H.B.6
  • 20
    • 0037846441 scopus 로고    scopus 로고
    • Serine 776 of ataxin-1 is critical for polyglutamine-induced disease in SCA1 transgenic mice
    • Emamian ES, Kaytor MD, Duvick LA, Zu T, Tousey SK, Zoghbi HY, et al. Serine 776 of ataxin-1 is critical for polyglutamine-induced disease in SCA1 transgenic mice. Neuron. 2003; 38(3): 375-87.
    • (2003) Neuron , vol.38 , Issue.3 , pp. 375-387
    • Emamian, E.S.1    Kaytor, M.D.2    Duvick, L.A.3    Zu, T.4    Tousey, S.K.5    Zoghbi, H.Y.6
  • 21
    • 0032475941 scopus 로고    scopus 로고
    • Ataxin-1 nuclear localization and aggregation: Role in polyglutamine-induced disease in SCA1 transgenic mice
    • Klement IA, Skinner PJ, Kaytor MD, Yi H, Hersch SM, Clark HB, et al. Ataxin-1 nuclear localization and aggregation: role in polyglutamine-induced disease in SCA1 transgenic mice. Cell. 1998; 95(1): 41-53.
    • (1998) Cell , vol.95 , Issue.1 , pp. 41-53
    • Klement, I.A.1    Skinner, P.J.2    Kaytor, M.D.3    Yi, H.4    Hersch, S.M.5    Clark, H.B.6
  • 22
    • 0029163222 scopus 로고
    • SCA1 transgenic mice: A model for neurodegeneration caused by an expanded CAG trinucleotide repeat
    • Burright EN, Clark HB, Servadio A, Matilla T, Feddersen RM, Yunis WS, et al. SCA1 transgenic mice: a model for neurodegeneration caused by an expanded CAG trinucleotide repeat. Cell. 1995; 82(6): 937-48.
    • (1995) Cell , vol.82 , Issue.6 , pp. 937-948
    • Burright, E.N.1    Clark, H.B.2    Servadio, A.3    Matilla, T.4    Feddersen, R.M.5    Yunis, W.S.6
  • 23
    • 0034612220 scopus 로고    scopus 로고
    • Inhibition of huntingtin fibrillogenesis by specific antibodies and small molecules: Implications for Huntington's disease therapy
    • Heiser V, Scherzinger E, Boeddrich A, Nordhoff E, Lurz R, Schugardt N, et al. Inhibition of huntingtin fibrillogenesis by specific antibodies and small molecules: implications for Huntington's disease therapy. Proc Natl Acad Sci USA. 2000; 97(12): 6739-44.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.12 , pp. 6739-6744
    • Heiser, V.1    Scherzinger, E.2    Boeddrich, A.3    Nordhoff, E.4    Lurz, R.5    Schugardt, N.6
  • 24
    • 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 DL, Meriin AB, Engemann S, Russel DE, Roark M, et al. A potent small molecule inhibits polyglutamine aggregation in Huntington's disease neurons and suppresses neurodegeneration in vivo. Proc Natl Acad Sci USA. 2005; 102(3): 892-7.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.3 , pp. 892-897
    • Zhang, X.1    Smith, D.L.2    Meriin, A.B.3    Engemann, S.4    Russel, D.E.5    Roark, M.6
  • 25
    • 0030470459 scopus 로고    scopus 로고
    • Glutamine repeats and inherited neurodegenerative diseases: Molecular aspects
    • Perutz MF, Glutamine repeats and inherited neurodegenerative diseases: molecular aspects. Curr Opin Struct Biol. 1996; 6(6): 848-58.
    • (1996) Curr Opin Struct Biol , vol.6 , Issue.6 , pp. 848-858
    • Perutz, M.F.1
  • 26
    • 18544410106 scopus 로고    scopus 로고
    • Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation
    • Davies SW, Turmaine M, Cozens BA, DiFiglia M, Sharp AH, Ross CA, et al. Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation. Cell. 1997; 90(3): 537-48.
    • (1997) Cell , vol.90 , Issue.3 , pp. 537-548
    • Davies, S.W.1    Turmaine, M.2    Cozens, B.A.3    Difiglia, M.4    Sharp, A.H.5    Ross, C.A.6
  • 27
    • 0034163497 scopus 로고    scopus 로고
    • Long glutamine tracts cause nuclear localization of a novel form of huntingtin in medium spiny striatal neurons in HdhQ92 and HdhQ111 knock-in mice
    • Wheeler VC, White JK, Gutekunst CA, Vrbanac V, Weaver M, Li X J, 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(4): 503-13.
    • (2000) Hum Mol Genet , vol.9 , Issue.4 , pp. 503-513
    • Wheeler, V.C.1    White, J.K.2    Gutekunst, C.A.3    Vrbanac, V.4    Weaver, M.5    Li, X.J.6
  • 28
    • 0037701612 scopus 로고    scopus 로고
    • Huntingtin contains a highly conserved nuclear export signal
    • Xia J, Lee D H, Taylor J, Vandelft M, Truant R. Huntingtin contains a highly conserved nuclear export signal. Hum Mol Genet. 2003; 12(12): 1393-403.
    • (2003) Hum Mol Genet , vol.12 , Issue.12 , pp. 1393-1403
    • Xia, J.1    Lee, D.H.2    Taylor, J.3    Vandelft, M.4    Truant, R.5
  • 29
    • 0037014426 scopus 로고    scopus 로고
    • Protein misfolding, amyloid formation, and neurodegeneration: A critical role for molecular chaperones?
    • Muchowski PJ. Protein misfolding, amyloid formation, and neurodegeneration: a critical role for molecular chaperones? Neuron. 2002; 35(1): 9-12.
    • (2002) Neuron , vol.35 , Issue.1 , pp. 9-12
    • Muchowski, P.J.1
  • 30
    • 15544372340 scopus 로고    scopus 로고
    • A structure-based analysis of huntingtin mutant polyglutamine aggregation and toxicity: Evidence for a compact beta-sheet structure
    • Poirier MA, Jiang H, Ross CA. A structure-based analysis of huntingtin mutant polyglutamine aggregation and toxicity: evidence for a compact beta-sheet structure. Hum Mol Genet. 2005; 14(6): 765-74.
    • (2005) Hum Mol Genet , vol.14 , Issue.6 , pp. 765-774
    • Poirier, M.A.1    Jiang, H.2    Ross, C.A.3
  • 31
    • 17344371397 scopus 로고    scopus 로고
    • Short GCG expansions in the PABP2 gene cause oculopharyngeal muscular dystrophy
    • Brais B, Bouchard JP, Xie YG, Rochefort DL, Chretien N, Tome FM, et al. Short GCG expansions in the PABP2 gene cause oculopharyngeal muscular dystrophy. Nat Genet. 1998; 18(2): 164-7.
    • (1998) Nat Genet , vol.18 , Issue.2 , pp. 164-167
    • Brais, B.1    Bouchard, J.P.2    Xie, Y.G.3    Rochefort, D.L.4    Chretien, N.5    Tome, F.M.6
  • 33
    • 0036590137 scopus 로고    scopus 로고
    • A novel stable polyalanine [poly(A)] expansion in the HOXA13 gene associated with hand-foot-genital syndrome: Proper function of poly(A)-harbouring transcription factors depends on a critical repeat length?
    • Utsch B, Becker K, Brock D, Lentze MJ, Bidlingmaier F, Ludwig M. A novel stable polyalanine [poly(A)] expansion in the HOXA13 gene associated with hand-foot-genital syndrome: proper function of poly(A)-harbouring transcription factors depends on a critical repeat length? Hum Genet. 2002; 110(5): 488-94.
    • (2002) Hum Genet , vol.110 , Issue.5 , pp. 488-494
    • Utsch, B.1    Becker, K.2    Brock, D.3    Lentze, M.J.4    Bidlingmaier, F.5    Ludwig, M.6
  • 34
    • 0037318857 scopus 로고    scopus 로고
    • FOXL2 and BPES: Mutational hotspots, phenotypic variability, and revision of the genotype-phenotype correlation
    • De Baere E, Beysen D, Oley C, Lorenz B, Cocquet J, De Sutter P, et al. FOXL2 and BPES: mutational hotspots, phenotypic variability, and revision of the genotype-phenotype correlation. Am J Hum Genet. 2003; 72(2): 478-87.
    • (2003) Am J Hum Genet , vol.72 , Issue.2 , pp. 478-487
    • De Baere, E.1    Beysen, D.2    Oley, C.3    Lorenz, B.4    Cocquet, J.5    De Sutter, P.6
  • 35
    • 0026716545 scopus 로고
    • Demise of a neuronal population in Huntington's disease and the importance of hyponeuronogenesis
    • Kremer HP, Kremer GH. Demise of a neuronal population in Huntington's disease and the importance of hyponeuronogenesis. Clin Neurol Neurosurg. 1992; 94 Suppl: S7-8.
    • (1992) Clin Neurol Neurosurg , vol.94 , Issue.SUPPL.
    • Kremer, H.P.1    Kremer, G.H.2
  • 36
    • 0004075694 scopus 로고
    • Berlin; New York: Springer-Verlag, xvii
    • Hayden MR, Huntington's chorea. 1981, Berlin; New York: Springer-Verlag, xvii. 192.
    • (1981) Huntington's Chorea , pp. 192
    • Hayden, M.R.1
  • 38
    • 0030771894 scopus 로고    scopus 로고
    • Huntingtin localization in brains of normal and Huntington's disease patients
    • Sapp E, Schwarz C, Chase K, Bhide PG, Young AB, Penney J, et al. Huntingtin localization in brains of normal and Huntington's disease patients. Ann Neurol. 1997; 42(4): 604-12.
    • (1997) Ann Neurol , vol.42 , Issue.4 , pp. 604-612
    • Sapp, E.1    Schwarz, C.2    Chase, K.3    Bhide, P.G.4    Young, A.B.5    Penney, J.6
  • 39
    • 33748441393 scopus 로고    scopus 로고
    • Huntington's disease: Targeting the triad
    • Raymond LA G, A. Huntington's disease: Targeting the triad. Canadian Journal of Diagnosis. 2005; April: 82-7.
    • (2005) Canadian Journal of Diagnosis , vol.APRIL , pp. 82-87
    • Raymond, L.A.G.1
  • 40
    • 0029947377 scopus 로고    scopus 로고
    • Reevaluation of the exact CAG repeat length in hereditary cerebellar ataxias using highly denaturing conditions and long PCR
    • Maruyama H, Kawakami H, Nakamura S. Reevaluation of the exact CAG repeat length in hereditary cerebellar ataxias using highly denaturing conditions and long PCR. Hum Genet. 1996; 97(5): 591-5.
    • (1996) Hum Genet , vol.97 , Issue.5 , pp. 591-595
    • Maruyama, H.1    Kawakami, H.2    Nakamura, S.3
  • 41
    • 0027327418 scopus 로고
    • Trinucleotide repeat elongation in the Huntingtin gene in Huntington disease patients from 71 Danish families
    • Norremolle A, Riess O, Epplen JT, Fenger K, Hasholt L, Sorensen SA. Trinucleotide repeat elongation in the Huntingtin gene in Huntington disease patients from 71 Danish families. Hum Mol Genet. 1993; 2(9): 1475-6.
    • (1993) Hum Mol Genet , vol.2 , Issue.9 , pp. 1475-1476
    • Norremolle, A.1    Riess, O.2    Epplen, J.T.3    Fenger, K.4    Hasholt, L.5    Sorensen, S.A.6
  • 42
    • 0028972448 scopus 로고
    • Polyglutamine expansion as a pathological epitope in Huntington's disease and four dominant cerebellar ataxias
    • Trottier Y, Lutz Y, Stevanin G, Imbert G, Devys D, Cancel G, et al. Polyglutamine expansion as a pathological epitope in Huntington's disease and four dominant cerebellar ataxias. Nature. 1995; 378(6555): 403-6.
    • (1995) Nature , vol.378 , Issue.6555 , pp. 403-406
    • Trottier, Y.1    Lutz, Y.2    Stevanin, G.3    Imbert, G.4    Devys, D.5    Cancel, G.6
  • 43
    • 0031056478 scopus 로고    scopus 로고
    • HIP-I: A huntingtin interacting protein isolated by the yeast two-hybrid system
    • Wanker EE, Rovira C, Scherzinger E, Hasenbank R, Walter S, Tait D, et al. HIP-I: a huntingtin interacting protein isolated by the yeast two-hybrid system. Hum Mol Genet. 1997; 6(3): 487-95.
    • (1997) Hum Mol Genet , vol.6 , Issue.3 , pp. 487-495
    • Wanker, E.E.1    Rovira, C.2    Scherzinger, E.3    Hasenbank, R.4    Walter, S.5    Tait, D.6
  • 44
    • 0028803757 scopus 로고
    • A huntingtin-associated protein enriched in brain with implications for pathology
    • Li XJ, Li SH, Sharp AH, Nucifora FC, Jr., Schilling G, Lanahan A, et al. A huntingtin-associated protein enriched in brain with implications for pathology. Nature. 1995; 378(6555): 398-402.
    • (1995) Nature , vol.378 , Issue.6555 , pp. 398-402
    • Li, X.J.1    Li, S.H.2    Sharp, A.H.3    Nucifora Jr., F.C.4    Schilling, G.5    Lanahan, A.6
  • 46
    • 0034284565 scopus 로고    scopus 로고
    • Huntingtin's WW domain partners in Huntington's disease post-mortem brain fulfill genetic criteria for direct involvement in Huntington's disease pathogenesis
    • Passani LA, Bedford MT, Faber PW, McGinnis KM, Sharp AH, Gusella JF, et al. Huntingtin's WW domain partners in Huntington's disease post-mortem brain fulfill genetic criteria for direct involvement in Huntington's disease pathogenesis. Hum Mol Genet. 2000; 9(14): 2175-82.
    • (2000) Hum Mol Genet , vol.9 , Issue.14 , pp. 2175-2182
    • Passani, L.A.1    Bedford, M.T.2    Faber, P.W.3    McGinnis, K.M.4    Sharp, A.H.5    Gusella, J.F.6
  • 48
    • 0036633295 scopus 로고    scopus 로고
    • The endocytic machinery at an interface with the actin cytoskeleton: A dynamic, hip intersection
    • McPherson PS. The endocytic machinery at an interface with the actin cytoskeleton: a dynamic, hip intersection. Trends Cell Biol. 2002; 12(7): 312-5.
    • (2002) Trends Cell Biol , vol.12 , Issue.7 , pp. 312-315
    • McPherson, P.S.1
  • 49
    • 17144442805 scopus 로고    scopus 로고
    • Hip, hip, hippi!
    • Ferner V. Hip, hip, hippi! Nat Cell Biol. 2002; 4(2): E30.
    • (2002) Nat Cell Biol , vol.4 , Issue.2
    • Ferner, V.1
  • 50
    • 0035839021 scopus 로고    scopus 로고
    • E3 ligase activity of RING finger proteins that interact with Hip-2, a human ubiquitin-conjugating enzyme
    • Lee SJ, Choi JY, Sung YM, Park H, Rhim H, Kang S. E3 ligase activity of RING finger proteins that interact with Hip-2, a human ubiquitin-conjugating enzyme. FEBS Lett. 2001; 503(1): 61-4.
    • (2001) FEBS Lett , vol.503 , Issue.1 , pp. 61-64
    • Lee, S.J.1    Choi, J.Y.2    Sung, Y.M.3    Park, H.4    Rhim, H.5    Kang, S.6
  • 51
    • 0035852687 scopus 로고    scopus 로고
    • The Gin-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, Rosenblatt A, Wellington C, Hayden MR, et al. The Gin-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(4): 1811-6.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , Issue.4 , pp. 1811-1816
    • Holbert, S.1    Denghien, I.2    Kiechle, T.3    Rosenblatt, A.4    Wellington, C.5    Hayden, M.R.6
  • 52
    • 3142523461 scopus 로고    scopus 로고
    • COP and clathrin-coated vesicle budding: Different pathways, common approaches
    • McMahon HT, Mills IG. COP and clathrin-coated vesicle budding: different pathways, common approaches. Curr Opin Cell Biol. 2004; 16(4): 379-91.
    • (2004) Curr Opin Cell Biol , vol.16 , Issue.4 , pp. 379-391
    • McMahon, H.T.1    Mills, I.G.2
  • 53
    • 4344589711 scopus 로고    scopus 로고
    • Kinetic regulation of vesicle endocytosis at synapses
    • Wu LG. Kinetic regulation of vesicle endocytosis at synapses. Trends Neurosci. 2004; 27(9): 548-54.
    • (2004) Trends Neurosci , vol.27 , Issue.9 , pp. 548-554
    • Wu, L.G.1
  • 54
    • 13244275403 scopus 로고    scopus 로고
    • Lipid regulation of the synaptic vesicle cycle
    • Rohrbough J, Broadie K. Lipid regulation of the synaptic vesicle cycle. Nat Rev Neurosci. 2005; 6(2): 139-50.
    • (2005) Nat Rev Neurosci , vol.6 , Issue.2 , pp. 139-150
    • Rohrbough, J.1    Broadie, K.2
  • 55
    • 0038686017 scopus 로고    scopus 로고
    • Cytoskeletal motors and cargo in membrane trafficking: Opportunities for high specificity in drug intervention
    • Phelps MA, Foraker AB, Swaan PW. Cytoskeletal motors and cargo in membrane trafficking: opportunities for high specificity in drug intervention. Drug Discov Today. 2003; 8(11): 494-502.
    • (2003) Drug Discov Today , vol.8 , Issue.11 , pp. 494-502
    • Phelps, M.A.1    Foraker, A.B.2    Swaan, P.W.3
  • 56
    • 0037415613 scopus 로고    scopus 로고
    • Dynactin polices two-way organelle traffic
    • Dell KR. Dynactin polices two-way organelle traffic. J Cell Biol. 2003; 160(3): 291-3.
    • (2003) J Cell Biol , vol.160 , Issue.3 , pp. 291-293
    • Dell, K.R.1
  • 57
    • 32644434386 scopus 로고    scopus 로고
    • Huntingtin-HAP40 complex is a novel Rab5 effector that regulates early endosome motility and is up-regulated in Huntington's disease
    • Pal A, Severin F, Lommer B, Shevchenko A, Zerial M. Huntingtin-HAP40 complex is a novel Rab5 effector that regulates early endosome motility and is up-regulated in Huntington's disease. J Cell Biol. 2006; 172(4): 605-18.
    • (2006) J Cell Biol , vol.172 , Issue.4 , pp. 605-618
    • Pal, A.1    Severin, F.2    Lommer, B.3    Shevchenko, A.4    Zerial, M.5
  • 58
    • 0028989602 scopus 로고
    • Huntingtin is a cytoplasmic protein associated with vesicles in human and rat brain neurons
    • DiFiglia M, Sapp E, Chase K, Schwarz C, Meloni A, Young C, et al. Huntingtin is a cytoplasmic protein associated with vesicles in human and rat brain neurons. Neuron. 1995; 14(5): 1075-81.
    • (1995) Neuron , vol.14 , Issue.5 , pp. 1075-1081
    • DiFiglia, M.1    Sapp, E.2    Chase, K.3    Schwarz, C.4    Meloni, A.5    Young, C.6
  • 59
    • 0029816724 scopus 로고    scopus 로고
    • Subcellular localization of the Huntington's disease gene product in cell lines by immunofluorescence and biochemical subcellular fractionation
    • De Rooij KE, Dorsman JC, Smoor MA, Den Dunnen JT, Van Ommen GJ. Subcellular localization of the Huntington's disease gene product in cell lines by immunofluorescence and biochemical subcellular fractionation. Hum Mol Genet. 1996; 5(8): 1093-9.
    • (1996) Hum Mol Genet , vol.5 , Issue.8 , pp. 1093-1099
    • De Rooij, K.E.1    Dorsman, J.C.2    Smoor, M.A.3    Den Dunnen, J.T.4    Van Ommen, G.J.5
  • 60
    • 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, Goffredo D, Valenza M, Conti L, et al. Huntingtin interacts with REST/NRSF to modulate the transcription of NRSE-controlled neuronal genes. Nat Genet. 2003; 35(1): 76-83.
    • (2003) Nat Genet , vol.35 , Issue.1 , pp. 76-83
    • Zuccato, C.1    Tartari, M.2    Crotti, A.3    Goffredo, D.4    Valenza, M.5    Conti, L.6
  • 61
    • 0036882107 scopus 로고    scopus 로고
    • The enigma of Huntington's disease
    • Cattaneo E, Rigamonti D, Zuccato C, The enigma of Huntington's disease. Sci Am. 2002; 287(6): 92-7.
    • (2002) Sci Am , vol.287 , Issue.6 , pp. 92-97
    • Cattaneo, E.1    Rigamonti, D.2    Zuccato, C.3
  • 62
    • 0035919701 scopus 로고    scopus 로고
    • Loss of huntingtin-mediated BDNF gene transcription in Huntington's disease
    • Zuccato C, Ciammola A, Rigamonti D, Leavitt BR, Goffredo D, Conti L, et al. Loss of huntingtin-mediated BDNF gene transcription in Huntington's disease. Science. 2001; 293(5529): 493-8.
    • (2001) Science , vol.293 , Issue.5529 , pp. 493-498
    • Zuccato, C.1    Ciammola, A.2    Rigamonti, D.3    Leavitt, B.R.4    Goffredo, D.5    Conti, L.6
  • 63
    • 0033789409 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor, neurotrophin-3, and neurotrophin-4/5 prevent the death of striatal projection neurons in a rodent model of Huntington's disease
    • Perez-Navarro E, Canudas AM, Akerund P, Alberch J, Arenas E. Brain-derived neurotrophic factor, neurotrophin-3, and neurotrophin-4/5 prevent the death of striatal projection neurons in a rodent model of Huntington's disease. J Neurochem. 2000; 75(5): 2190-9.
    • (2000) J Neurochem , vol.75 , Issue.5 , pp. 2190-2199
    • Perez-Navarro, E.1    Canudas, A.M.2    Akerund, P.3    Alberch, J.4    Arenas, E.5
  • 64
    • 0033544840 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor-mediated protection of striatal neurons in an excitotoxic rat model of Huntington's disease, as demonstrated by adenoviral gene transfer
    • Bemelmans AP, Horellou P, Pradier L, Brunet I, Colin P, Mallet J. Brain-derived neurotrophic factor-mediated protection of striatal neurons in an excitotoxic rat model of Huntington's disease, as demonstrated by adenoviral gene transfer. Hum Gene Ther. 1999; 10(18): 2987-97.
    • (1999) Hum Gene Ther , vol.10 , Issue.18 , pp. 2987-2997
    • Bemelmans, A.P.1    Horellou, P.2    Pradier, L.3    Brunet, I.4    Colin, P.5    Mallet, J.6
  • 65
    • 0037631378 scopus 로고    scopus 로고
    • Nuclear localization of a non-caspase truncation product of atrophin-1, with an expanded polyglutamine repeat, increases cellular toxicity
    • Nucifora FC, Jr, Ellerby LM, Wellington CL, Wood JD, Herring WJ, Sawa A, et al. Nuclear localization of a non-caspase truncation product of atrophin-1, with an expanded polyglutamine repeat, increases cellular toxicity. J Biol Chem. 2003; 278(15): 13047-55.
    • (2003) J Biol Chem , vol.278 , Issue.15 , pp. 13047-13055
    • Nucifora Jr., F.C.1    Ellerby, L.M.2    Wellington, C.L.3    Wood, J.D.4    Herring, W.J.5    Sawa, A.6
  • 66
    • 12944263711 scopus 로고    scopus 로고
    • The Huntington's disease protein interacts with p53 and CREB-binding protein and represses transcription
    • Steffan JS, Kazantsev A, Spasic-Boskovic O, Greenwald M, Zhu Y Z, Gohler H, et al. The Huntington's disease protein interacts with p53 and CREB-binding protein and represses transcription. Proc Natl Acad Sci USA. 2000; 97(12): 6763-8.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.12 , pp. 6763-6768
    • Steffan, J.S.1    Kazantsev, A.2    Spasic-Boskovic, O.3    Greenwald, M.4    Zhu, Y.Z.5    Gohler, H.6
  • 67
    • 3142636768 scopus 로고    scopus 로고
    • Huntingtin controls neurotrophic support and survival of neurons by enhancing BDNF vesicular transport along microtubules
    • Gauthier LR, Charrin BC, Borrell-Pages M, Dompierre JP, Rangone H, Cordelieres FP, et al. Huntingtin controls neurotrophic support and survival of neurons by enhancing BDNF vesicular transport along microtubules. Cell. 2004; 118(1): 127-38.
    • (2004) Cell , vol.118 , Issue.1 , pp. 127-138
    • Gauthier, L.R.1    Charrin, B.C.2    Borrell-Pages, M.3    Dompierre, J.P.4    Rangone, H.5    Cordelieres, F.P.6
  • 68
    • 84993912315 scopus 로고
    • Increased apoptosis and early embryonic lethality in mice nullizygous for the Huntington's disease gene homologue
    • Zeitlin S, Liu JP, Chapman DL, Papaioannou VE, Efstratiadis A. Increased apoptosis and early embryonic lethality in mice nullizygous for the Huntington's disease gene homologue. Nat Genet. 1995; 11(2): 155-63.
    • (1995) Nat Genet , vol.11 , Issue.2 , pp. 155-163
    • Zeitlin, S.1    Liu, J.P.2    Chapman, D.L.3    Papaioannou, V.E.4    Efstratiadis, A.5
  • 69
    • 0030035931 scopus 로고    scopus 로고
    • Huntingtin: New marker along the road to death?
    • Rosen A. Huntingtin: new marker along the road to death? Nat Genet. 1996; 13(4): 380-2.
    • (1996) Nat Genet , vol.13 , Issue.4 , pp. 380-382
    • Rosen, A.1
  • 70
    • 0032502715 scopus 로고    scopus 로고
    • Caspase cleavage of gene products associated with triplet expansion disorders generates truncated fragments containing the polyglutamine tract
    • Wellington CL, Ellerby LM, Hackam AS, Margolis RL, Trifiro MA, Singaraja R, et al. Caspase cleavage of gene products associated with triplet expansion disorders generates truncated fragments containing the polyglutamine tract. J Biol Chem. 1998; 273(15): 9158-67.
    • (1998) J Biol Chem , vol.273 , Issue.15 , pp. 9158-9167
    • Wellington, C.L.1    Ellerby, L.M.2    Hackam, A.S.3    Margolis, R.L.4    Trifiro, M.A.5    Singaraja, R.6
  • 71
    • 0034571171 scopus 로고    scopus 로고
    • Huntington's disease: The challenge for cell biologists
    • Tobin AJ, Signer ER. Huntington's disease: the challenge for cell biologists. Trends Cell Biol. 2000; 10(12): 531-6.
    • (2000) Trends Cell Biol , vol.10 , Issue.12 , pp. 531-536
    • Tobin, A.J.1    Signer, E.R.2
  • 72
    • 2442702838 scopus 로고    scopus 로고
    • AAV-mediated gene delivery of BDNF or GDNF is neuroprotective in a model of Huntington disease
    • Kells AP, Fong DM, Dragunow M, During MJ, Young D, Connor B. AAV-mediated gene delivery of BDNF or GDNF is neuroprotective in a model of Huntington disease. Mol Ther. 2004; 9(5): 682-8.
    • (2004) Mol Ther , vol.9 , Issue.5 , pp. 682-688
    • Kells, A.P.1    Fong, D.M.2    Dragunow, M.3    During, M.J.4    Young, D.5    Connor, B.6
  • 75
    • 2442511737 scopus 로고    scopus 로고
    • High throughput screening and characterization of HIV-1 entry inhibitors targeting gp41: Theories and techniques
    • Liu S, Jiang S. High throughput screening and characterization of HIV-1 entry inhibitors targeting gp41: theories and techniques. Curr Pharm Des. 2004; 10(15): 1827-43.
    • (2004) Curr Pharm des , vol.10 , Issue.15 , pp. 1827-1843
    • Liu, S.1    Jiang, S.2
  • 76
    • 0031197207 scopus 로고    scopus 로고
    • Recent advances in antiviral research: Identification of inhibitors of the herpesvirus proteases
    • Flynn DL, Abood NA, Holwerda BC. Recent advances in antiviral research: identification of inhibitors of the herpesvirus proteases. Curr Opin Chem Biol. 1997; 1(2): 190-6.
    • (1997) Curr Opin Chem Biol , vol.1 , Issue.2 , pp. 190-196
    • Flynn, D.L.1    Abood, N.A.2    Holwerda, B.C.3
  • 78
    • 18544379477 scopus 로고    scopus 로고
    • A bivalent Huntingtin binding peptide suppresses polyglutamine aggregation and pathogenesis in Drosophila
    • Kazantsev A, Walker HA, Slepko N, Bear JE, Preisinger E, Steffan JS, et al. A bivalent Huntingtin binding peptide suppresses polyglutamine aggregation and pathogenesis in Drosophila. Nat Genet. 2002; 30(4): 367-76.
    • (2002) Nat Genet , vol.30 , Issue.4 , pp. 367-376
    • Kazantsev, A.1    Walker, H.A.2    Slepko, N.3    Bear, J.E.4    Preisinger, E.5    Steffan, J.S.6
  • 79
    • 18744369020 scopus 로고    scopus 로고
    • Identification of benzothiazoles as potential polyglutamine aggregation inhibitors of Huntington's disease by using an automated filter retardation assay
    • Heiser V, Engemann S, Brocker W, Dunkel I, Boeddrich A, Waelter S, et al. Identification of benzothiazoles as potential polyglutamine aggregation inhibitors of Huntington's disease by using an automated filter retardation assay. Proc Natl Acad Sci USA. 2002; 99 Suppl 4: S16400-6.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.SUPPL. 4
    • Heiser, V.1    Engemann, S.2    Brocker, W.3    Dunkel, I.4    Boeddrich, A.5    Waelter, S.6
  • 80
    • 0242657586 scopus 로고    scopus 로고
    • A rapid cellular FRET assay of polyglutamine aggregation identifies a novel inhibitor
    • Pollitt SK, Pallos J, Shao J, Desai UA, Ma AA, Thompson LM, et al. A rapid cellular FRET assay of polyglutamine aggregation identifies a novel inhibitor. Neuron. 2003; 40(4): 685-94.
    • (2003) Neuron , vol.40 , Issue.4 , pp. 685-694
    • Pollitt, S.K.1    Pallos, J.2    Shao, J.3    Desai, U.A.4    Ma, A.A.5    Thompson, L.M.6
  • 81
    • 0037154165 scopus 로고    scopus 로고
    • Effects of intracellular expression of anti-huntingtin antibodies of various specificities on mutant huntingtin aggregation and toxicity
    • Khoshnan A, Ko J, Patterson PH. Effects of intracellular expression of anti-huntingtin antibodies of various specificities on mutant huntingtin aggregation and toxicity. Proc Natl Acad Sci USA. 2002; 99(2): 1002-7.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.2 , pp. 1002-1007
    • Khoshnan, A.1    Ko, J.2    Patterson, P.H.3
  • 82
    • 0842322740 scopus 로고    scopus 로고
    • Huntingtin bodies sequester vesicle-associated proteins by a polyproline-dependent interaction
    • Qin ZH, Wang Y, Sapp E, Cuiffo B, Wanker E, Hayden MR, et al. Huntingtin bodies sequester vesicle-associated proteins by a polyproline-dependent interaction. J Neurosci. 2004; 24(1): 269-81.
    • (2004) J Neurosci , vol.24 , Issue.1 , pp. 269-281
    • Qin, Z.H.1    Wang, Y.2    Sapp, E.3    Cuiffo, B.4    Wanker, E.5    Hayden, M.R.6
  • 83
    • 12944335007 scopus 로고    scopus 로고
    • Reversal of a full-length mutant huntingtin neuronal cell phenotype by chemical inhibitors of polyglutamine-mediated aggregation
    • Wang J, Gines S, MacDonald ME, Gusella JF. Reversal of a full-length mutant huntingtin neuronal cell phenotype by chemical inhibitors of polyglutamine-mediated aggregation. BMC Neurosci. 2005; 6(1): 1.
    • (2005) BMC Neurosci , vol.6 , Issue.1 , pp. 1
    • Wang, J.1    Gines, S.2    MacDonald, M.E.3    Gusella, J.F.4
  • 84
    • 0141642242 scopus 로고    scopus 로고
    • Histone deacerylase activity is retained in primary neurons expressing mutant huntingtin protein
    • Hoshino M, Tagawa K, Okuda T, Murata M, Oyanagi K, Arai N, et al. Histone deacerylase activity is retained in primary neurons expressing mutant huntingtin protein. J Neurochem. 2003; 87(1): 257-67.
    • (2003) J Neurochem , vol.87 , Issue.1 , pp. 257-267
    • Hoshino, M.1    Tagawa, K.2    Okuda, T.3    Murata, M.4    Oyanagi, K.5    Arai, N.6
  • 85
    • 0035909330 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors arrest polyglutamine-dependent neurodegeneration in Drosophila
    • Steffan JS, Bodai L, Pallos J, Poelman M, McCampbell A, Apostol BL, et al. Histone deacetylase inhibitors arrest polyglutamine-dependent neurodegeneration in Drosophila. Nature. 2001; 413(6857): 739-43.
    • (2001) Nature , vol.413 , Issue.6857 , pp. 739-743
    • Steffan, J.S.1    Bodai, L.2    Pallos, J.3    Poelman, M.4    McCampbell, A.5    Apostol, B.L.6
  • 86
    • 0142157600 scopus 로고    scopus 로고
    • Histone deacerylase inhibition by sodium butyrate chemotherapy ameliorates the neurodegenerative phenotype in Huntington's disease mice
    • Ferrante RJ, Kubilus JK, Lee J, Ryu H, Beesen A, Zucker B, et al. Histone deacerylase inhibition by sodium butyrate chemotherapy ameliorates the neurodegenerative phenotype in Huntington's disease mice. J Neurosci. 2003; 23(28): 9418-27.
    • (2003) J Neurosci , vol.23 , Issue.28 , pp. 9418-9427
    • Ferrante, R.J.1    Kubilus, J.K.2    Lee, J.3    Ryu, H.4    Beesen, A.5    Zucker, B.6
  • 87
    • 33645235438 scopus 로고    scopus 로고
    • Pharmacologinal promotion of inclusion formation: A therapeutic approach for Huntington's and Parkinson's diseases
    • Bodner RA, Outeiro TF, Altmann S, Maxwell MM, Cho SH, Hyman BT, et al. Pharmacologinal promotion of inclusion formation: a therapeutic approach for Huntington's and Parkinson's diseases. Proc Natl Acad Sci USA. 2006; 103(1): 4246-51.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.1 , pp. 4246-4251
    • Bodner, R.A.1    Outeiro, T.F.2    Altmann, S.3    Maxwell, M.M.4    Cho, S.H.5    Hyman, B.T.6
  • 88
    • 0037079065 scopus 로고    scopus 로고
    • Chemical genetic screening approaches to neurobiology
    • Stockwell BR. Chemical genetic screening approaches to neurobiology. Neuron. 2002; 36(4): 559-62.
    • (2002) Neuron , vol.36 , Issue.4 , pp. 559-562
    • Stockwell, B.R.1
  • 89
    • 4644283464 scopus 로고    scopus 로고
    • Molecular biology of erythropoietin
    • Jelkmann W, Molecular biology of erythropoietin. Intern Med. 2004; 43(8): 649-59.
    • (2004) Intern Med , vol.43 , Issue.8 , pp. 649-659
    • Jelkmann, W.1
  • 90
    • 4444280869 scopus 로고    scopus 로고
    • Prospects for new drugs for chronic obstructive pulmonary disease
    • Barnes PJ, Hansel TT. Prospects for new drugs for chronic obstructive pulmonary disease. Lancet. 2004; 364(9438): 985-96.
    • (2004) Lancet , vol.364 , Issue.9438 , pp. 985-996
    • Barnes, P.J.1    Hansel, T.T.2
  • 91
    • 5744232398 scopus 로고    scopus 로고
    • New pharmacological perspectives and therapeutic potential of PPAR-gamma agonists
    • Alarcon de la Lastra C, Sanchez-Fidalgo S, Villegas I, Motilva V. New pharmacological perspectives and therapeutic potential of PPAR-gamma agonists. Curr Pharm Des. 2004; 10(28): 3505-24.
    • (2004) Curr Pharm des , vol.10 , Issue.28 , pp. 3505-3524
    • Alarcon De La Lastra, C.1    Sanchez-Fidalgo, S.2    Villegas, I.3    Motilva, V.4
  • 93
    • 2942676455 scopus 로고    scopus 로고
    • Estrogens and their receptors in breast cancer progression: A dual role in cancer proliferation and invasion
    • Platet N, Cathiard AM, Gleizes M, Garcia M. Estrogens and their receptors in breast cancer progression: a dual role in cancer proliferation and invasion. Crit Rev Oncol Hematol. 2004; 51(1): 55-67.
    • (2004) Crit Rev Oncol Hematol , vol.51 , Issue.1 , pp. 55-67
    • Platet, N.1    Cathiard, A.M.2    Gleizes, M.3    Garcia, M.4
  • 94
    • 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 EA, Cordelieres FP, Connors NC, Datta SR, Finkbeiner S, et al. The IGF-1/Akt pathway is neuroprotective in Huntington's disease and involves Huntingtin phosphorylation by Akt. Dev Cell. 2002; 2(6): 831-7.
    • (2002) Dev Cell , vol.2 , Issue.6 , pp. 831-837
    • Humbert, S.1    Bryson, E.A.2    Cordelieres, F.P.3    Connors, N.C.4    Datta, S.R.5    Finkbeiner, S.6
  • 95
    • 0346749473 scopus 로고    scopus 로고
    • Enhanced Akt signaling is an early pro-survival response that reflects N-methyl-D-aspartate receptor activation in Huntington's disease knock-in striatal cells
    • Gines S, Ivanova E, Seong IS, Saura CA, MacDonald ME. Enhanced Akt signaling is an early pro-survival response that reflects N-methyl-D-aspartate receptor activation in Huntington's disease knock-in striatal cells. J Biol Chem. 2003; 278(50): 50514-22.
    • (2003) J Biol Chem , vol.278 , Issue.50 , pp. 50514-50522
    • Gines, S.1    Ivanova, E.2    Seong, I.S.3    Saura, C.A.4    MacDonald, M.E.5
  • 96
    • 0030793341 scopus 로고    scopus 로고
    • Expression of NMDA receptor-1 (NR1) and huntingtin in striatal neurons which colocalize somatostatin, neuropeptide Y, and NADPH diaphorase: A double-label histochemical and immunohistochemical study
    • Kumar U, Asotra K, Patel SC, Patel YC. Expression of NMDA receptor-1 (NR1) and huntingtin in striatal neurons which colocalize somatostatin, neuropeptide Y, and NADPH diaphorase: a double-label histochemical and immunohistochemical study. Exp Neurol. 1997; 145(2 Pt 1): 412-24.
    • (1997) Exp Neurol , vol.145 , Issue.2 PART 1 , pp. 412-424
    • Kumar, U.1    Asotra, K.2    Patel, S.C.3    Patel, Y.C.4
  • 97
    • 0032971311 scopus 로고    scopus 로고
    • Subtype-specific enhancement of NMDA receptor currents by mutant huntingtin
    • Chen N, Luo T, Wellington C, Metzler M, McCutcheon K, Hayden MR, et al. Subtype-specific enhancement of NMDA receptor currents by mutant huntingtin. J Neurochem. 1999; 72(5): 1890-8.
    • (1999) J Neurochem , vol.72 , Issue.5 , pp. 1890-1898
    • Chen, N.1    Luo, T.2    Wellington, C.3    Metzler, M.4    McCutcheon, K.5    Hayden, M.R.6
  • 99
    • 27144523294 scopus 로고    scopus 로고
    • Inhibition of metabotropic glutamate receptor signaling by the huntingtin-binding protein optineurin
    • Anborgh PH, Godin C, Pampillo M, Dhami GK, Dale LB, Cregan SP, et al. Inhibition of metabotropic glutamate receptor signaling by the huntingtin-binding protein optineurin. J Biol Chem. 2005; 280(41): 34840-8.
    • (2005) J Biol Chem , vol.280 , Issue.41 , pp. 34840-34848
    • Anborgh, P.H.1    Godin, C.2    Pampillo, M.3    Dhami, G.K.4    Dale, L.B.5    Cregan, S.P.6
  • 100
    • 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 JF. 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(1): 15.
    • (2002) BMC Neurosci , vol.3 , Issue.1 , pp. 15
    • Takano, H.1    Gusella, J.F.2
  • 101
    • 4644307407 scopus 로고    scopus 로고
    • Activation of the IkappaB kinase complex and nuclear factor-kappaB contributes to mutant huntingtin neurotoxicity
    • Khoshnan A, Ko J, Watkin EE, Paige LA, Reinhart PH, Patterson PH. Activation of the IkappaB kinase complex and nuclear factor-kappaB contributes to mutant huntingtin neurotoxicity. J Neurosci. 2004; 24(37): 7999-8008.
    • (2004) J Neurosci , vol.24 , Issue.37 , pp. 7999-8008
    • Khoshnan, A.1    Ko, J.2    Watkin, E.E.3    Paige, L.A.4    Reinhart, P.H.5    Patterson, P.H.6
  • 102
    • 4143112468 scopus 로고    scopus 로고
    • Expanded huntingtin activates the c-Jun terminal kinase/c-Jun pathway prior to aggregate formation in striatal neurons in culture
    • Garcia M, Charvin D, Caboche J. Expanded huntingtin activates the c-Jun terminal kinase/c-Jun pathway prior to aggregate formation in striatal neurons in culture. Neuroscience. 2004; 127(4): 859-70.
    • (2004) Neuroscience , vol.127 , Issue.4 , pp. 859-870
    • Garcia, M.1    Charvin, D.2    Caboche, J.3
  • 103
    • 4444302167 scopus 로고    scopus 로고
    • Deranged neuronal calcium signaling and Huntington disease
    • Bezprozvanny I, Hayden MR. Deranged neuronal calcium signaling and Huntington disease. Biochem Biophys Res Commun. 2004; 322(4): 1310-7.
    • (2004) Biochem Biophys Res Commun , vol.322 , Issue.4 , pp. 1310-1317
    • Bezprozvanny, I.1    Hayden, M.R.2
  • 104
    • 14044264256 scopus 로고    scopus 로고
    • Disturbed Ca2+ signaling and apoptosis of medium spiny neurons in Huntington's disease
    • Tang TS, Slow E, Lupu V, Stavrovskaya IG, Sugimori M, Llinas R, et al. Disturbed Ca2+ signaling and apoptosis of medium spiny neurons in Huntington's disease. Proc Natl Acad Sci USA. 2005; 102(7): 2602-7.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.7 , pp. 2602-2607
    • Tang, T.S.1    Slow, E.2    Lupu, V.3    Stavrovskaya, I.G.4    Sugimori, M.5    Llinas, R.6
  • 105
    • 14244264746 scopus 로고    scopus 로고
    • Ca2+-induced permeability transition in human lymphoblastoid cell mitochondria from normal and Huntington's disease individuals
    • Panov AV, Lund S, Greenamyre JT. Ca2+-induced permeability transition in human lymphoblastoid cell mitochondria from normal and Huntington's disease individuals. Mol Cell Biochem. 2005; 269(1-2): 143-52.
    • (2005) Mol Cell Biochem , vol.269 , Issue.1-2 , pp. 143-152
    • Panov, A.V.1    Lund, S.2    Greenamyre, J.T.3
  • 106
    • 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, Ashizawa T, Stockton DW, Amos C, et al. Autosomal dominant cerebellar ataxia (SCA6) associated with small polyglutamine expansions in the alpha 1A-voltage-dependent calcium channel. Nat Genet. 1997; 15(1): 62-9.
    • (1997) Nat Genet , vol.15 , Issue.1 , pp. 62-69
    • Zhuchenko, O.1    Bailey, J.2    Bonnen, P.3    Ashizawa, T.4    Stockton, D.W.5    Amos, C.6
  • 107
    • 5144226158 scopus 로고    scopus 로고
    • Polyglutamine repeats of spinocerebellar ataxia 6 impair the cell-death-preventing effect of CaV2.1 Ca2+ channel-loss-of-function cellular model of SCA6
    • Matsuyama Z, Yanagisawa NK, Aoki Y, Black JL 3rd, Lennon VA, Mori Y, et al. Polyglutamine repeats of spinocerebellar ataxia 6 impair the cell-death-preventing effect of CaV2.1 Ca2+ channel-loss-of-function cellular model of SCA6. Neurobiol Dis. 2004; 17(2): 198-204.
    • (2004) Neurobiol Dis , vol.17 , Issue.2 , pp. 198-204
    • Matsuyama, Z.1    Yanagisawa, N.K.2    Aoki, Y.3    Black III, J.L.4    Lennon, V.A.5    Mori, Y.6
  • 108
    • 0026704216 scopus 로고
    • Androgen receptor mutants that affect normal growth and development
    • Brinkmann AO, Trapman J. Androgen receptor mutants that affect normal growth and development. Cancer Surv. 1992; 14: 95-111.
    • (1992) Cancer Surv , vol.14 , pp. 95-111
    • Brinkmann, A.O.1    Trapman, J.2
  • 109
    • 2942590668 scopus 로고    scopus 로고
    • Androgen insensitivity syndrome and Klinefelter's syndrome: Sex and gender considerations
    • Diamond M, Watson LA. Androgen insensitivity syndrome and Klinefelter's syndrome: sex and gender considerations. Child Adolesc Psychiatr Clin N Am. 2004; 13(3): 623-40, viii.
    • (2004) Child Adolesc Psychiatr Clin N Am , vol.13 , Issue.3 , pp. 623-640
    • Diamond, M.1    Watson, L.A.2
  • 110
    • 0018883281 scopus 로고
    • Early events in the biosynthesis of secretory and membrane proteins: The signal hypothesis
    • Lingappa VR, Blobel G. Early events in the biosynthesis of secretory and membrane proteins: the signal hypothesis. Recent Prog Horm Res. 1980; 36: 451-75.
    • (1980) Recent Prog Horm Res , vol.36 , pp. 451-475
    • Lingappa, V.R.1    Blobel, G.2
  • 111
    • 0142211276 scopus 로고    scopus 로고
    • Identification and characterization of a ligand-regulated nuclear export signal in androgen receptor
    • Saporita AJ, Zhang Q, Navai N, Dincer Z, Hahn J, Cai X, et al. Identification and characterization of a ligand-regulated nuclear export signal in androgen receptor. J Biol Chem. 2003; 278(43): 41998-2005.
    • (2003) J Biol Chem , vol.278 , Issue.43 , pp. 41998-42005
    • Saporita, A.J.1    Zhang, Q.2    Navai, N.3    Dincer, Z.4    Hahn, J.5    Cai, X.6
  • 112
    • 20144362557 scopus 로고    scopus 로고
    • Widespread nuclear and cytoplasmic accumulation of mutant androgen receptor in SBMA patients
    • Adachi H, Katsuno M, Minamiyama M, Waza M, Sang C, Nakagomi Y, et al. Widespread nuclear and cytoplasmic accumulation of mutant androgen receptor in SBMA patients. Brain. 2005; 128(Pt 3): 659-70.
    • (2005) Brain , vol.128 , Issue.PART 3 , pp. 659-670
    • Adachi, H.1    Katsuno, M.2    Minamiyama, M.3    Waza, M.4    Sang, C.5    Nakagomi, Y.6
  • 113
    • 0030850412 scopus 로고    scopus 로고
    • Intranuclear inclusions of expanded polyglutamine protein in spinocerebellar ataxia type 3
    • Paulson HL, Perez MK, Trottier Y, Trojanowski JQ, Subramony SH, Das SS, et al. Intranuclear inclusions of expanded polyglutamine protein in spinocerebellar ataxia type 3. Neuron. 1997; 19(2): 333-44.
    • (1997) Neuron , vol.19 , Issue.2 , pp. 333-344
    • Paulson, H.L.1    Perez, M.K.2    Trottier, Y.3    Trojanowski, J.Q.4    Subramony, S.H.5    Das, S.S.6
  • 114
    • 0035897405 scopus 로고    scopus 로고
    • Identities of sequestered proteins in aggregates from cells with induced polyglutamine expression
    • Suhr ST, Senut MC, Whitelegge JP, Faull KF, Cuizon DB, Gage FH. Identities of sequestered proteins in aggregates from cells with induced polyglutamine expression. J Cell Biol. 2001; 153(2): 283-94.
    • (2001) J Cell Biol , vol.153 , Issue.2 , pp. 283-294
    • Suhr, S.T.1    Senut, M.C.2    Whitelegge, J.P.3    Faull, K.F.4    Cuizon, D.B.5    Gage, F.H.6
  • 115
    • 0032945938 scopus 로고    scopus 로고
    • Polyglutamine-expanded androgen receptors form aggregates that sequester heat shock proteins, proteasome components and SRC-1, and are suppressed by the HDJ-2 chaperone
    • Stenoien DL, Cummings CJ, Adams HP, Mancini MG, Patel K, DeMartino GN, et al. Polyglutamine-expanded androgen receptors form aggregates that sequester heat shock proteins, proteasome components and SRC-1, and are suppressed by the HDJ-2 chaperone. Hum Mol Genet. 1999; 8(5): 731-41.
    • (1999) Hum Mol Genet , vol.8 , Issue.5 , pp. 731-741
    • Stenoien, D.L.1    Cummings, C.J.2    Adams, H.P.3    Mancini, M.G.4    Patel, K.5    DeMartino, G.N.6
  • 116
    • 18644379256 scopus 로고    scopus 로고
    • Testosterone reduction prevents phenotypic expression in a transgenic mouse model of spinal and bulbar muscular atrophy
    • Katsuno M, Adachi H, Kume A, Li M, Nakagomi Y, Niwa H, et al. Testosterone reduction prevents phenotypic expression in a transgenic mouse model of spinal and bulbar muscular atrophy. Neuron. 2002; 35(5): 843-54.
    • (2002) Neuron , vol.35 , Issue.5 , pp. 843-854
    • Katsuno, M.1    Adachi, H.2    Kume, A.3    Li, M.4    Nakagomi, Y.5    Niwa, H.6
  • 117
    • 0037194896 scopus 로고    scopus 로고
    • Androgen-dependent neurodegeneration by polyglutamine-expanded human androgen receptor in Drosophila
    • Takeyama K, Ito S, Yamamoto A, Tanimoto H, Furutani T, Kanaka H, et al. Androgen-dependent neurodegeneration by polyglutamine-expanded human androgen receptor in Drosophila. Neuron. 2002; 35(5): 855-64.
    • (2002) Neuron , vol.35 , Issue.5 , pp. 855-864
    • Takeyama, K.1    Ito, S.2    Yamamoto, A.3    Tanimoto, H.4    Furutani, T.5    Kanaka, H.6
  • 118
    • 2542483769 scopus 로고    scopus 로고
    • Spinal and bulbar muscular atrophy: Ligand-dependent pathogenesis and therapeutic perspectives
    • Katsuno M, Adachi H, Tanaka F, Sobue G. Spinal and bulbar muscular atrophy: ligand-dependent pathogenesis and therapeutic perspectives. J Mol Med. 2004; 82(5): 298-307.
    • (2004) J Mol Med , vol.82 , Issue.5 , pp. 298-307
    • Katsuno, M.1    Adachi, H.2    Tanaka, F.3    Sobue, G.4
  • 119
    • 10644263551 scopus 로고    scopus 로고
    • Randomized trial of leuprorelin and flutamide in male patients with hepatocellular carcinoma treated with tamoxifen
    • Randomized trial of leuprorelin and flutamide in male patients with hepatocellular carcinoma treated with tamoxifen. Hepatology. 2004; 40(6): 1361-9.
    • (2004) Hepatology , vol.40 , Issue.6 , pp. 1361-1369
  • 120
    • 0030613177 scopus 로고    scopus 로고
    • Huntingtin is required for neurogenesis and is not impaired by the Huntington's disease CAG expansion
    • White JK, Auerbach W, Duyao MP, Vonsattel JP, Gusella JF, Joyner AL, et al. Huntingtin is required for neurogenesis and is not impaired by the Huntington's disease CAG expansion. Nat Genet. 1997; 17(4): 404-10.
    • (1997) Nat Genet , vol.17 , Issue.4 , pp. 404-410
    • White, J.K.1    Auerbach, W.2    Duyao, M.P.3    Vonsattel, J.P.4    Gusella, J.F.5    Joyner, A.L.6
  • 121
    • 0028891145 scopus 로고
    • Huntington's disease gene: Regional and cellular expression in brain of normal and affected individuals
    • Landwehrmeyer GB, McNeil SM, Dure LS 4th, Ge P, Aizawa H, Huang Q, et al. Huntington's disease gene: regional and cellular expression in brain of normal and affected individuals. Ann Neurol. 1995; 37(2): 218-30.
    • (1995) Ann Neurol , vol.37 , Issue.2 , pp. 218-230
    • Landwehrmeyer, G.B.1    McNeil, S.M.2    Dure IV, L.S.3    Ge, P.4    Aizawa, H.5    Huang, Q.6
  • 122
    • 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, Osuga H, Showguchi-Miyata J, Gondo Y, 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(1): 72-85.
    • (2000) Genomics , vol.69 , Issue.1 , pp. 72-85
    • Matsuyama, N.1    Hadano, S.2    Onoe, K.3    Osuga, H.4    Showguchi-Miyata, J.5    Gondo, Y.6
  • 123
    • 0035475788 scopus 로고    scopus 로고
    • SCA1 molecular genetics: A history of a 13 year collaboration against glutamines
    • Orr HT, Zoghbi HY. SCA1 molecular genetics: a history of a 13 year collaboration against glutamines. Hum Mol Genet. 2001; 10(20): 2307-11.
    • (2001) Hum Mol Genet , vol.10 , Issue.20 , pp. 2307-2311
    • Orr, H.T.1    Zoghbi, H.Y.2
  • 124
    • 0032228186 scopus 로고    scopus 로고
    • The complex clinical and genetic classification of inherited ataxias. I. Dominant ataxias
    • Di Donato S. The complex clinical and genetic classification of inherited ataxias. I. Dominant ataxias. Ital J Neurol Sci, 1998; 19(6): 335-43.
    • (1998) Ital J Neurol Sci , vol.19 , Issue.6 , pp. 335-343
    • Di Donato, S.1
  • 125
    • 3543031667 scopus 로고    scopus 로고
    • Pathways to motor incoordination: The inherited ataxias
    • Taroni F, Di Donato S. Pathways to motor incoordination: the inherited ataxias. Nat Rev Neurosci. 2004; 5(8): 641-55.
    • (2004) Nat Rev Neurosci , vol.5 , Issue.8 , pp. 641-655
    • Taroni, F.1    Di Donato, S.2
  • 126
    • 9344245162 scopus 로고    scopus 로고
    • Frequency of spinocerebellar ataxia type 1, dentatorubropallidoluysian atrophy, and Machado-Joseph disease mutations in a large group of spinocerebellar ataxia patients
    • Silveira I, Lopes-Cendes I, Kish S, Maciel P, Gaspar C, Coutinho P, et al. Frequency of spinocerebellar ataxia type 1, dentatorubropallidoluysian atrophy, and Machado-Joseph disease mutations in a large group of spinocerebellar ataxia patients. Neurology. 1996; 46(1): 214-8.
    • (1996) Neurology , vol.46 , Issue.1 , pp. 214-218
    • Silveira, I.1    Lopes-Cendes, I.2    Kish, S.3    Maciel, P.4    Gaspar, C.5    Coutinho, P.6
  • 128
    • 0043127451 scopus 로고    scopus 로고
    • Dominant ataxias and Friedreich ataxia: An update
    • Albin RL. Dominant ataxias and Friedreich ataxia: an update. Curr Opin Neurol. 2003; 16(4): 507-14.
    • (2003) Curr Opin Neurol , vol.16 , Issue.4 , pp. 507-514
    • Albin, R.L.1
  • 129
    • 11144356369 scopus 로고    scopus 로고
    • Autosomal dominant cerebellar ataxias: Clinical features, genetics, and pathogenesis
    • Schols L, Bauer P, Schmidt T, Schulte T, Riess O. Autosomal dominant cerebellar ataxias: clinical features, genetics, and pathogenesis. Lancet Neurol. 2004; 3(5): 291-304.
    • (2004) Lancet Neurol , vol.3 , Issue.5 , pp. 291-304
    • Schols, L.1    Bauer, P.2    Schmidt, T.3    Schulte, T.4    Riess, O.5
  • 130
    • 0034094873 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegeneration
    • Zoghbi HY, Orr HT, Glutamine repeats and neurodegeneration. Annu Rev Neurosci. 2000; 23: 217-47.
    • (2000) Annu Rev Neurosci , vol.23 , pp. 217-247
    • Zoghbi, H.Y.1    Orr, H.T.2
  • 131
    • 0029245258 scopus 로고
    • Spinocerebellar ataxia type 1
    • Zoghbi HY, Orr HT. Spinocerebellar ataxia type 1. Semin Cell Biol. 1995; 6(1): 29-35.
    • (1995) Semin Cell Biol , vol.6 , Issue.1 , pp. 29-35
    • Zoghbi, H.Y.1    Orr, H.T.2
  • 132
    • 0031469707 scopus 로고    scopus 로고
    • Ectopically expressed CAG repeats cause intranuclear inclusions and a progressive late onset neurological phenotype in the mouse
    • Ordway JM, Tallaksen-Greene S, Gutekunst CA, Bernstein EM, Cearley JA, Wiener HW, et al. Ectopically expressed CAG repeats cause intranuclear inclusions and a progressive late onset neurological phenotype in the mouse. Cell. 1997; 91(6): 753-63.
    • (1997) Cell , vol.91 , Issue.6 , pp. 753-763
    • Ordway, J.M.1    Tallaksen-Greene, S.2    Gutekunst, C.A.3    Bernstein, E.M.4    Cearley, J.A.5    Wiener, H.W.6
  • 133
  • 134
    • 0037726598 scopus 로고    scopus 로고
    • Interaction of Akt-phosphorylated ataxin-1 with 14-3-3 mediates neurodegeneration in spinocerebellar ataxia type 1
    • Chen HK, Fernandez-Funez P, Acevedo SF, Lam YC, Kaytor MD, Fernandez MH, et al. Interaction of Akt-phosphorylated ataxin-1 with 14-3-3 mediates neurodegeneration in spinocerebellar ataxia type 1. Cell. 2003; 113(4): 457-68.
    • (2003) Cell , vol.113 , Issue.4 , pp. 457-468
    • Chen, H.K.1    Fernandez-Funez, P.2    Acevedo, S.F.3    Lam, Y.C.4    Kaytor, M.D.5    Fernandez, M.H.6
  • 136
    • 0035168621 scopus 로고    scopus 로고
    • The spinocerebellar ataxia type 1 protein, ataxin-1, has RNA-binding activity that is inversely affected by the length of its polyglutamine tract
    • Yue S, Serra HG, Zoghbi HY, Orr HT. The spinocerebellar ataxia type 1 protein, ataxin-1, has RNA-binding activity that is inversely affected by the length of its polyglutamine tract. Hum Mol Genet. 2001; 10(1): 25-30.
    • (2001) Hum Mol Genet , vol.10 , Issue.1 , pp. 25-30
    • Yue, S.1    Serra, H.G.2    Zoghbi, H.Y.3    Orr, H.T.4
  • 137
    • 1642447764 scopus 로고    scopus 로고
    • Ataxin 1, a SCA1 neurodegenerative disorder protein, is functionally linked to the silencing mediator of retinoid and thyroid hormone receptors
    • Tsai CC, Kao HY, Mitzutani A, Banayo E, Rajan H, McKeown M, et al. Ataxin 1, a SCA1 neurodegenerative disorder protein, is functionally linked to the silencing mediator of retinoid and thyroid hormone receptors. Proc Natl Acad Sci USA. 2004; 101(12): 4047-52.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.12 , pp. 4047-4052
    • Tsai, C.C.1    Kao, H.Y.2    Mitzutani, A.3    Banayo, E.4    Rajan, H.5    McKeown, M.6
  • 138
    • 0036798685 scopus 로고    scopus 로고
    • Intranuclear ataxin1 inclusions contain both fast- and slow-exchanging components
    • Stenoien DL, Mielke M, Mancini MA. Intranuclear ataxin1 inclusions contain both fast- and slow-exchanging components. Nat Cell Biol. 2002; 4(10): 806-10.
    • (2002) Nat Cell Biol , vol.4 , Issue.10 , pp. 806-810
    • Stenoien, D.L.1    Mielke, M.2    Mancini, M.A.3
  • 141
    • 0032840052 scopus 로고    scopus 로고
    • Neuronal intranuclear inclusions in spinocerebellar ataxia type 2: Triple-labeling immunofluorescent study
    • Koyano S, Uchihara T, Fujigasaki H, Nakamura A, Yagishita S, Iwabuchi K. Neuronal intranuclear inclusions in spinocerebellar ataxia type 2: triple-labeling immunofluorescent study. Neurosci Lett. 1999; 273(2): 117-20.
    • (1999) Neurosci Lett , vol.273 , Issue.2 , pp. 117-120
    • Koyano, S.1    Uchihara, T.2    Fujigasaki, H.3    Nakamura, A.4    Yagishita, S.5    Iwabuchi, K.6
  • 142
    • 0033811788 scopus 로고    scopus 로고
    • Nuclear localization or inclusion body formation of ataxin-2 are not necessary for SCA2 pathogenesis in mouse or human
    • Huynh DP, Figueroa K, Hoang N, Pulst SM. Nuclear localization or inclusion body formation of ataxin-2 are not necessary for SCA2 pathogenesis in mouse or human. Nat Genet. 2000; 26(1): 44-50.
    • (2000) Nat Genet , vol.26 , Issue.1 , pp. 44-50
    • Huynh, D.P.1    Figueroa, K.2    Hoang, N.3    Pulst, S.M.4
  • 143
    • 0034701797 scopus 로고    scopus 로고
    • A novel protein with RNA-binding motifs interacts with ataxin-2
    • Shibata H, Huynh DP, Pulst SM. A novel protein with RNA-binding motifs interacts with ataxin-2. Hum Mol Genet. 2000; 9(9): 1303-13.
    • (2000) Hum Mol Genet , vol.9 , Issue.9 , pp. 1303-1313
    • Shibata, H.1    Huynh, D.P.2    Pulst, S.M.3
  • 144
    • 3242890363 scopus 로고    scopus 로고
    • Structural and functional analysis of ataxin-2 and ataxin-3
    • Albrecht M, Golatta M, Wullner U, Lengauer T. Structural and functional analysis of ataxin-2 and ataxin-3. Eur J Biochem. 2004; 271(15): 3155-70.
    • (2004) Eur J Biochem , vol.271 , Issue.15 , pp. 3155-3170
    • Albrecht, M.1    Golatta, M.2    Wullner, U.3    Lengauer, T.4
  • 145
    • 12344317072 scopus 로고    scopus 로고
    • An integrative approach to gain insights into the cellular function of human ataxin-2
    • Ralser M, Albrecht M, Nonhoff U, Lengauer T, Lehrach H, Krobitsch S. An integrative approach to gain insights into the cellular function of human ataxin-2. J Mol Biol. 2005; 346(1): 203-14.
    • (2005) J Mol Biol , vol.346 , Issue.1 , pp. 203-214
    • Ralser, M.1    Albrecht, M.2    Nonhoff, U.3    Lengauer, T.4    Lehrach, H.5    Krobitsch, S.6
  • 146
    • 0026527447 scopus 로고
    • Shuttling of pre-mRNA binding proteins between nucleus and cytoplasm
    • Pinol-Roma S, Dreyfuss G. Shuttling of pre-mRNA binding proteins between nucleus and cytoplasm. Nature. 1992; 355(6362): 730-2.
    • (1992) Nature , vol.355 , Issue.6362 , pp. 730-732
    • Pinol-Roma, S.1    Dreyfuss, G.2
  • 148
    • 0029816723 scopus 로고    scopus 로고
    • The fragile X mental retardation protein is a ribonucleoprotein containing both nuclear localization and nuclear export signals
    • Eberhart DE, Malter HE, Feng Y, Warren ST. The fragile X mental retardation protein is a ribonucleoprotein containing both nuclear localization and nuclear export signals. Hum Mol Genet. 1996; 5(8): 1083-91.
    • (1996) Hum Mol Genet , vol.5 , Issue.8 , pp. 1083-1091
    • Eberhart, D.E.1    Malter, H.E.2    Feng, Y.3    Warren, S.T.4
  • 149
    • 18044379515 scopus 로고    scopus 로고
    • Microarray identification of FMRP-associated brain mRNAs and altered mRNA translational profiles in fragile X syndrome
    • Brown V, Jin P, Ceman S, Darnell JC, O'Donnell WT, Tenenbaum S A, et al. Microarray identification of FMRP-associated brain mRNAs and altered mRNA translational profiles in fragile X syndrome. Cell. 2001; 107(4): 477-87.
    • (2001) Cell , vol.107 , Issue.4 , pp. 477-487
    • Brown, V.1    Jin, P.2    Ceman, S.3    Darnell, J.C.4    O'Donnell, W.T.5    Tenenbaum, S.A.6
  • 150
    • 0242497663 scopus 로고    scopus 로고
    • CLIP identifies Nova-regulated RNA networks in the brain
    • Ule J, Jensen KB, Ruggiu M, Mele A, Ule A, Darnell RB. CLIP identifies Nova-regulated RNA networks in the brain. Science. 2003; 302(5648): 1212-5.
    • (2003) Science , vol.302 , Issue.5648 , pp. 1212-1215
    • Ule, J.1    Jensen, K.B.2    Ruggiu, M.3    Mele, A.4    Ule, A.5    Darnell, R.B.6
  • 151
    • 0035908996 scopus 로고    scopus 로고
    • NXF5, a novel member of the nuclear RNA export factor family, is lost in a male patient with a syndromic form of mental retardation
    • Jun L, Frints S, Duhamel H, Herold A, Abad-Rodrigues J, Dotti C, et al. NXF5, a novel member of the nuclear RNA export factor family, is lost in a male patient with a syndromic form of mental retardation. Curr Biol. 2001; 11(18): 1381-91.
    • (2001) Curr Biol , vol.11 , Issue.18 , pp. 1381-1391
    • Jun, L.1    Frints, S.2    Duhamel, H.3    Herold, A.4    Abad-Rodrigues, J.5    Dotti, C.6
  • 152
    • 0033867386 scopus 로고    scopus 로고
    • CAG repeat length in RAI1 is associated with age at onset variability in spinocerebellar ataxia type 2 (SCA2)
    • Hayes S, Turecki G, Brisebois K, Lopes-Cendes I, Gaspar C, Riess O, et al. CAG repeat length in RAI1 is associated with age at onset variability in spinocerebellar ataxia type 2 (SCA2). Hum Mol Genet. 2000; 9(12): 1753-8.
    • (2000) Hum Mol Genet , vol.9 , Issue.12 , pp. 1753-1758
    • Hayes, S.1    Turecki, G.2    Brisebois, K.3    Lopes-Cendes, I.4    Gaspar, C.5    Riess, O.6
  • 153
    • 0028169646 scopus 로고
    • Autosomal dominant cerebellar ataxia with retinal degeneration: Clinical, neuropathologic, and genetic analysis of a large kindred
    • Gouw LG, Digre KB, Harris CP, Haines JH, Ptacek LJ. Autosomal dominant cerebellar ataxia with retinal degeneration: clinical, neuropathologic, and genetic analysis of a large kindred. Neurology. 1994; 44(8): 1441-7.
    • (1994) Neurology , vol.44 , Issue.8 , pp. 1441-1447
    • Gouw, L.G.1    Digre, K.B.2    Harris, C.P.3    Haines, J.H.4    Ptacek, L.J.5
  • 155
    • 0037421691 scopus 로고    scopus 로고
    • SCA7 knockin mice model human SCA7 and reveal gradual accumulation of mutant ataxin-7 in neurons and abnormalities in short-term plasticity
    • Yoo SY, Pennesi ME, Weeber EJ, Xu B, Atkinson R, Chen S, et al. SCA7 knockin mice model human SCA7 and reveal gradual accumulation of mutant ataxin-7 in neurons and abnormalities in short-term plasticity. Neuron. 2003; 37(3): 383-401.
    • (2003) Neuron , vol.37 , Issue.3 , pp. 383-401
    • Yoo, S.Y.1    Pennesi, M.E.2    Weeber, E.J.3    Xu, B.4    Atkinson, R.5    Chen, S.6
  • 156
    • 0344531461 scopus 로고    scopus 로고
    • Insights into the molecular basis of polyglutamine neurodegeneration from studies of a spinocerebellar ataxia type 7 mouse model
    • Grote SK, La Spada AR. Insights into the molecular basis of polyglutamine neurodegeneration from studies of a spinocerebellar ataxia type 7 mouse model. Cytogenet Genome Res. 2003; 100(1-4): 164-74.
    • (2003) Cytogenet Genome Res , vol.100 , Issue.1-4 , pp. 164-174
    • Grote, S.K.1    La Spada, A.R.2
  • 157
    • 0347287040 scopus 로고    scopus 로고
    • Interference of Crx-dependent transcription by ataxin-7 involves interaction between the glutamine regions and requires the ataxin-7 carboxy-terminal region for nuclear localization
    • Chen S, Peng GH, Wang X, Smith AC, Grote SK, Sopher BL, et al. Interference of Crx-dependent transcription by ataxin-7 involves interaction between the glutamine regions and requires the ataxin-7 carboxy-terminal region for nuclear localization. Hum Mol Genet. 2004; 13(1): 53-67.
    • (2004) Hum Mol Genet , vol.13 , Issue.1 , pp. 53-67
    • Chen, S.1    Peng, G.H.2    Wang, X.3    Smith, A.C.4    Grote, S.K.5    Sopher, B.L.6
  • 158
    • 3042771651 scopus 로고    scopus 로고
    • Ataxin-7 is a subunit of GCN5 histone acetyltransferase-containing complexes
    • Helmlinger D, Hardy S, Sasorith S, Klein F, Robert F, Weber C, et al. Ataxin-7 is a subunit of GCN5 histone acetyltransferase-containing complexes. Hum Mol Genet. 2004; 13(12): 1257-65.
    • (2004) Hum Mol Genet , vol.13 , Issue.12 , pp. 1257-1265
    • Helmlinger, D.1    Hardy, S.2    Sasorith, S.3    Klein, F.4    Robert, F.5    Weber, C.6
  • 159
    • 33646378692 scopus 로고    scopus 로고
    • Ataxin-7 can export from the nucleus via a conserved exportin-dependent signal
    • Taylor J, Grote SK, Xia J, Vandelft M, Graczyk J, Ellerby LM, et al. Ataxin-7 can export from the nucleus via a conserved exportin-dependent signal. J Biol Chem. 2006; 281(5): 2730-9.
    • (2006) J Biol Chem , vol.281 , Issue.5 , pp. 2730-2739
    • Taylor, J.1    Grote, S.K.2    Xia, J.3    Vandelft, M.4    Graczyk, J.5    Ellerby, L.M.6
  • 160
    • 14644419638 scopus 로고    scopus 로고
    • Neuronal dysfunction in a polyglutamine disease model occurs in the absence of ubiquitin-proteasome system impairment and inversely correlates with the degree of nuclear inclusion formation
    • Bowman AB, Yoo SY, Dantuma NP, Zoghbi HY. Neuronal dysfunction in a polyglutamine disease model occurs in the absence of ubiquitin-proteasome system impairment and inversely correlates with the degree of nuclear inclusion formation. Hum Mol Genet. 2005; 14(5): 679-91.
    • (2005) Hum Mol Genet , vol.14 , Issue.5 , pp. 679-691
    • Bowman, A.B.1    Yoo, S.Y.2    Dantuma, N.P.3    Zoghbi, H.Y.4
  • 161
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • Arrasate M, Mitra S, Schweitzer ES, Segal MR, Finkbeiner S. Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature. 2004; 431(7010): 805-10.
    • (2004) Nature , vol.431 , Issue.7010 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 162
    • 0034643861 scopus 로고    scopus 로고
    • Conserved phosphoprotein interaction motif is functionally interchangeable between ataxin-7 and arrestins
    • Mushegian AR, Vishnivetskiy SA, Gurevich VV. Conserved phosphoprotein interaction motif is functionally interchangeable between ataxin-7 and arrestins. Biochemistry. 2000; 39(23): 6809-13.
    • (2000) Biochemistry , vol.39 , Issue.23 , pp. 6809-6813
    • Mushegian, A.R.1    Vishnivetskiy, S.A.2    Gurevich, V.V.3
  • 163
    • 17644402459 scopus 로고    scopus 로고
    • Transduction of receptor signals by beta-arrestins
    • Lefkowitz RJ, Shenoy SK. Transduction of receptor signals by beta-arrestins. Science, 2005; 308(5721): 512-7.
    • (2005) Science , vol.308 , Issue.5721 , pp. 512-517
    • Lefkowitz, R.J.1    Shenoy, S.K.2
  • 164
    • 0028080406 scopus 로고
    • Trinucleotide repeat expansion in neurological disease
    • La Spada AR, Paulson HL, Fischbeck KH. Trinucleotide repeat expansion in neurological disease. Ann Neurol. 1994; 36(6): 814-22.
    • (1994) Ann Neurol , vol.36 , Issue.6 , pp. 814-822
    • La Spada, A.R.1    Paulson, H.L.2    Fischbeck, K.H.3
  • 165
    • 4043175666 scopus 로고    scopus 로고
    • Behavioral disorder, dementia, ataxia, and rigidity in a large family with TATA box-binding protein mutation
    • Bruni AC, Takahashi-Fujigasaki J, Maltecca F, Foncin JF, Servadio A, Casari G, et al. Behavioral disorder, dementia, ataxia, and rigidity in a large family with TATA box-binding protein mutation. Arch Neurol. 2004; 61(8): 1314-20.
    • (2004) Arch Neurol , vol.61 , Issue.8 , pp. 1314-1320
    • Bruni, A.C.1    Takahashi-Fujigasaki, J.2    Maltecca, F.3    Foncin, J.F.4    Servadio, A.5    Casari, G.6
  • 166
    • 0032517816 scopus 로고    scopus 로고
    • Recruitment and the role of nuclear localization in polyglutamine- mediated aggregation
    • Perez MK, Paulson HL, Pendse SJ, Saionz SJ, Bonini NM, Pittman RN. Recruitment and the role of nuclear localization in polyglutamine-mediated aggregation. J Cell Biol. 1998; 143(6): 1457-70.
    • (1998) J Cell Biol , vol.143 , Issue.6 , pp. 1457-1470
    • Perez, M.K.1    Paulson, H.L.2    Pendse, S.J.3    Saionz, S.J.4    Bonini, N.M.5    Pittman, R.N.6
  • 167
    • 3442890310 scopus 로고    scopus 로고
    • Basal ganglia involvement of a patient with SCA 17-a new form of autosomal dominant spinocerebellar ataxia
    • Gunther P, Storch A, Schwarz J, Sabri O, Steinbach P, Wagner A, et al. Basal ganglia involvement of a patient with SCA 17-a new form of autosomal dominant spinocerebellar ataxia. J Neurol. 2004; 251(7): 896-7.
    • (2004) J Neurol , vol.251 , Issue.7 , pp. 896-897
    • Gunther, P.1    Storch, A.2    Schwarz, J.3    Sabri, O.4    Steinbach, P.5    Wagner, A.6
  • 168
    • 1542360717 scopus 로고    scopus 로고
    • Focal dystonia as a presenting sign of spinocerebellar ataxia 17
    • Hagenah JM, Zuhlke C, Hellenbroich Y, Heide W, Klein C. Focal dystonia as a presenting sign of spinocerebellar ataxia 17. Mov Disord. 2004; 19(2): 217-20.
    • (2004) Mov Disord , vol.19 , Issue.2 , pp. 217-220
    • Hagenah, J.M.1    Zuhlke, C.2    Hellenbroich, Y.3    Heide, W.4    Klein, C.5
  • 169
    • 17844379460 scopus 로고    scopus 로고
    • The genomic structure and expression of MJD, the Machado-Joseph disease gene
    • Ichikawa Y, Goto J, Hattori M, Toyoda A, Ishii K, Jeong SY, et al. The genomic structure and expression of MJD, the Machado-Joseph disease gene. J Hum Genet. 2001; 46(7): 413-22.
    • (2001) J Hum Genet , vol.46 , Issue.7 , pp. 413-422
    • Ichikawa, Y.1    Goto, J.2    Hattori, M.3    Toyoda, A.4    Ishii, K.5    Jeong, S.Y.6
  • 170
    • 0035125109 scopus 로고    scopus 로고
    • Ancestral origins of the Machado-Joseph disease mutation: A worldwide haplotype study
    • Gaspar C, Lopes-Cendes I, Hayes S, Goto J, Arvidsson K, Dias A, et al. Ancestral origins of the Machado-Joseph disease mutation: a worldwide haplotype study. Am J Hum Genet. 2001; 68(2): 523-8.
    • (2001) Am J Hum Genet , vol.68 , Issue.2 , pp. 523-528
    • Gaspar, C.1    Lopes-Cendes, I.2    Hayes, S.3    Goto, J.4    Arvidsson, K.5    Dias, A.6
  • 171
    • 9244225693 scopus 로고    scopus 로고
    • Spinocerebellar ataxia 3 and Machado-Joseph disease: Clinical, molecular, and neuropathological features
    • Durr A, Stevanin G, Cancel G, Duyckaerts C, Abbas N, Didierjean O, et al. Spinocerebellar ataxia 3 and Machado-Joseph disease: clinical, molecular, and neuropathological features. Ann Neurol. 1996; 39(4): 490-9.
    • (1996) Ann Neurol , vol.39 , Issue.4 , pp. 490-499
    • Durr, A.1    Stevanin, G.2    Cancel, G.3    Duyckaerts, C.4    Abbas, N.5    Didierjean, O.6
  • 172
    • 13244258435 scopus 로고    scopus 로고
    • Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation
    • Bennett EJ, Bence NF, Jayakumar R, Kopito RR. Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation. Mol Cell. 2005; 17(3): 351-65.
    • (2005) Mol Cell , vol.17 , Issue.3 , pp. 351-365
    • Bennett, E.J.1    Bence, N.F.2    Jayakumar, R.3    Kopito, R.R.4
  • 173
    • 22844451581 scopus 로고    scopus 로고
    • Proteasome function is inhibited by polyglutamine-expanded ataxin-1, the SCA1 gene product
    • Park Y, Hong S, Kim S J, Kang S. Proteasome function is inhibited by polyglutamine-expanded ataxin-1, the SCA1 gene product. Mol Cells. 2005; 19(1): 23-30.
    • (2005) Mol Cells , vol.19 , Issue.1 , pp. 23-30
    • Park, Y.1    Hong, S.2    Kim, S.J.3    Kang, S.4
  • 174
    • 15444372240 scopus 로고    scopus 로고
    • The polyglutamine neurodegenerative protein ataxin 3 regulates aggresome formation
    • Burnett BG, Pittman RN. The polyglutamine neurodegenerative protein ataxin 3 regulates aggresome formation. Proc Natl Acad Sci USA. 2005; 102(12): 4330-5.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.12 , pp. 4330-4335
    • Burnett, B.G.1    Pittman, R.N.2
  • 175
    • 20844462057 scopus 로고    scopus 로고
    • A mutant ataxin-3 putative-cleavage fragment in brains of Machado-Joseph disease patients and transgenic mice is cytotoxic above a critical concentration
    • Goti D, Katzen SM, Mez J, Kurtis N, Kiluk J, Ben-Haiem L, et al. A mutant ataxin-3 putative-cleavage fragment in brains of Machado-Joseph disease patients and transgenic mice is cytotoxic above a critical concentration. J Neurosci. 2004; 24(45): 10266-79.
    • (2004) J Neurosci , vol.24 , Issue.45 , pp. 10266-10279
    • Goti, D.1    Katzen, S.M.2    Mez, J.3    Kurtis, N.4    Kiluk, J.5    Ben-Haiem, L.6
  • 176
    • 7344234800 scopus 로고    scopus 로고
    • An isoform of ataxin-3 accumulates in the nucleus of neuronal cells in affected brain regions of SCA3 patients
    • Schmidt T, Landwehrmeyer GB, Schmitt I, Trottier Y, Auburger G, Laccone F, et al. An isoform of ataxin-3 accumulates in the nucleus of neuronal cells in affected brain regions of SCA3 patients. Brain Pathol. 1998; 8(4): 669-79.
    • (1998) Brain Pathol , vol.8 , Issue.4 , pp. 669-679
    • Schmidt, T.1    Landwehrmeyer, G.B.2    Schmitt, I.3    Trottier, Y.4    Auburger, G.5    Laccone, F.6
  • 177
    • 0037047123 scopus 로고    scopus 로고
    • Live-cell imaging reveals divergent intracellular dynamics of polyglutamine disease proteins and supports a sequestration model of pathogenesis
    • Chai Y, Shao J, Miller VM, Williams A, Paulson HL. Live-cell imaging reveals divergent intracellular dynamics of polyglutamine disease proteins and supports a sequestration model of pathogenesis. Proc Natl Acad Sci USA. 2002; 99(14): 9310-5.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.14 , pp. 9310-9315
    • Chai, Y.1    Shao, J.2    Miller, V.M.3    Williams, A.4    Paulson, H.L.5
  • 178
    • 0034641593 scopus 로고    scopus 로고
    • CAG tract of MJD-1 may be prone to frameshifts causing polyalanine accumulation
    • Gaspar C, Jannatipour M, Dion P, Laganiere J, Sequeiros J, Brais B, et al. CAG tract of MJD-1 may be prone to frameshifts causing polyalanine accumulation. Hum Mol Genet. 2000; 9(13): 1957-66.
    • (2000) Hum Mol Genet , vol.9 , Issue.13 , pp. 1957-1966
    • Gaspar, C.1    Jannatipour, M.2    Dion, P.3    Laganiere, J.4    Sequeiros, J.5    Brais, B.6
  • 179
    • 0027180041 scopus 로고
    • Machado-Joseph disease is genetically different from Holguin dominant ataxia (SCA2)
    • Silveira I, Manaia A, Melki J, Magarino C, Lunkes A, Hernandez A, et al. Machado-Joseph disease is genetically different from Holguin dominant ataxia (SCA2). Genomics. 1993; 17(3): 556-9.
    • (1993) Genomics , vol.17 , Issue.3 , pp. 556-559
    • Silveira, I.1    Manaia, A.2    Melki, J.3    Magarino, C.4    Lunkes, A.5    Hernandez, A.6
  • 180
    • 0035228528 scopus 로고    scopus 로고
    • Hereditary ataxias in Cuba. Historical, epidemiological, clinical, electrophysiological and quantitative neurological features
    • Velazquez-Perez L, Garcia R, Santos FN, Paneque HM, Medina HE, Hechavarria PR. [Hereditary ataxias in Cuba. Historical, epidemiological, clinical, electrophysiological and quantitative neurological features]. Rev Neurol, 2001; 32(1): 71-6.
    • (2001) Rev Neurol , vol.32 , Issue.1 , pp. 71-76
    • Velazquez-Perez, L.1    Garcia, R.2    Santos, F.N.3    Paneque, H.M.4    Medina, H.E.5    Hechavarria, P.R.6
  • 181
    • 0028815025 scopus 로고
    • DNA analysis in hereditary dentatorubral-pallidoluysian atrophy: Correlation between CAG repeat length and phenotypic variation and the molecular basis of anticipation
    • Komure O, Sano A, Nishino N, Yamauchi N, Ueno S, Kondoh K, et al. DNA analysis in hereditary dentatorubral-pallidoluysian atrophy: correlation between CAG repeat length and phenotypic variation and the molecular basis of anticipation. Neurology. 1995; 45(1): 143-9.
    • (1995) Neurology , vol.45 , Issue.1 , pp. 143-149
    • Komure, O.1    Sano, A.2    Nishino, N.3    Yamauchi, N.4    Ueno, S.5    Kondoh, K.6
  • 182
    • 0032545261 scopus 로고    scopus 로고
    • Different complex formations of dentatorubral-pallidoluysian atrophy (DRPLA) protein in human and rat neurons
    • Yazawa I, Hazeki N, Kanazawa I. Different complex formations of dentatorubral-pallidoluysian atrophy (DRPLA) protein in human and rat neurons. Biochem Biophys Res Commun. 1998; 253(2): 209-13.
    • (1998) Biochem Biophys Res Commun , vol.253 , Issue.2 , pp. 209-213
    • Yazawa, I.1    Hazeki, N.2    Kanazawa, I.3
  • 183
    • 0034332649 scopus 로고    scopus 로고
    • Aberrant phosphorylation of dentatorubral-pallidoluysian atrophy (DRPLA) protein complex in brain tissue
    • Yazawa I. Aberrant phosphorylation of dentatorubral-pallidoluysian atrophy (DRPLA) protein complex in brain tissue. Biochem J. 2000; 351 Pt 3: 587-93.
    • (2000) Biochem J , vol.351 , Issue.PART 3 , pp. 587-593
    • Yazawa, I.1
  • 184
    • 0009744392 scopus 로고    scopus 로고
    • Nuclear accumulation of truncated atrophin-1 fragments in a transgenic mouse model of DRPLA
    • Schilling G, Wood JD, Duan K, Slunt HH, Gonzales V, Yamada M, et al. Nuclear accumulation of truncated atrophin-1 fragments in a transgenic mouse model of DRPLA. Neuron. 1999; 24(1): 275-86.
    • (1999) Neuron , vol.24 , Issue.1 , pp. 275-286
    • Schilling, G.1    Wood, J.D.2    Duan, K.3    Slunt, H.H.4    Gonzales, V.5    Yamada, M.6
  • 185
    • 0035937523 scopus 로고    scopus 로고
    • Interference by huntingtin and atrophin-1 with cbp-mediated transcription leading to cellular toxicity
    • Nucifora FC, Jr, Sasaki M, Peters MF, Huang H, Cooper JK, Yamada M, et al. Interference by huntingtin and atrophin-1 with cbp-mediated transcription leading to cellular toxicity. Science. 2001; 291(5512): 2423-8.
    • (2001) Science , vol.291 , Issue.5512 , pp. 2423-2428
    • Nucifora Jr., F.C.1    Sasaki, M.2    Peters, M.F.3    Huang, H.4    Cooper, J.K.5    Yamada, M.6
  • 186
    • 0141794493 scopus 로고    scopus 로고
    • Nucleocytplasmic shuttling of Huntingtin and Huntington's disease
    • Truant R. Nucleocytplasmic Shuttling of Huntingtin and Huntington's Disease. Clin. Neuro. Res. 2003; 3: 157-164.
    • (2003) Clin Neuro Res , vol.3 , pp. 157-164
    • Truant, R.1
  • 187
    • 0034737299 scopus 로고    scopus 로고
    • Reversal of neuropathology and motor dysfunction in a conditional model of Huntington's disease
    • Yamamoto A, Lucas JJ, Hen R. Reversal of neuropathology and motor dysfunction in a conditional model of Huntington's disease. Cell. 2000; 101(1): 57-66.
    • (2000) Cell , vol.101 , Issue.1 , pp. 57-66
    • Yamamoto, A.1    Lucas, J.J.2    Hen, R.3
  • 188
    • 0035889973 scopus 로고    scopus 로고
    • Proteasomal-dependent aggregate reversal and absence of cell death in a conditional mouse model of Huntington's disease
    • Martin-Aparicio E, Yamamoto A, Hernandez F, Hen R, Avila J, Lucas JJ. Proteasomal-dependent aggregate reversal and absence of cell death in a conditional mouse model of Huntington's disease. J Neurosci. 2001; 21(22): 8772-81.
    • (2001) J Neurosci , vol.21 , Issue.22 , pp. 8772-8781
    • Martin-Aparicio, E.1    Yamamoto, A.2    Hernandez, F.3    Hen, R.4    Avila, J.5    Lucas, J.J.6
  • 189
    • 4043137264 scopus 로고    scopus 로고
    • RNAi quashes polyQ
    • Caplen NJ. RNAi quashes polyQ. Nat Med. 2004; 10(8): 775-6.
    • (2004) Nat Med , vol.10 , Issue.8 , pp. 775-776
    • Caplen, N.J.1
  • 190
    • 4043057946 scopus 로고    scopus 로고
    • RNAi suppresses polyglutamine-induced neurodegeneration in a model of spinocerebellar ataxia
    • Xia H, Mao Q, Eliason SL, Harper SQ, Martins IH, Orr HT, et al. RNAi suppresses polyglutamine-induced neurodegeneration in a model of spinocerebellar ataxia. Nat Med. 2004; 10(8): 816-20.
    • (2004) Nat Med , vol.10 , Issue.8 , pp. 816-820
    • Xia, H.1    Mao, Q.2    Eliason, S.L.3    Harper, S.Q.4    Martins, I.H.5    Orr, H.T.6
  • 191
    • 3042841606 scopus 로고    scopus 로고
    • Sequence-dependent and independent inhibition specific for mutant ataxin-3 by small interfering RNA
    • Li Y, Yokota T, Matsumura R, Taira K, Mizusawa H. Sequence-dependent and independent inhibition specific for mutant ataxin-3 by small interfering RNA. Ann Neurol. 2004; 56(1): 124-9.
    • (2004) Ann Neurol , vol.56 , Issue.1 , pp. 124-129
    • Li, Y.1    Yokota, T.2    Matsumura, R.3    Taira, K.4    Mizusawa, H.5
  • 192
    • 0042838272 scopus 로고    scopus 로고
    • Use of adeno-associated viral vector for delivery of small interfering RNA
    • Tomar RS, Matta H, Chaudhary PM. Use of adeno-associated viral vector for delivery of small interfering RNA. Oncogene. 2003; 22(36): 5712-5.
    • (2003) Oncogene , vol.22 , Issue.36 , pp. 5712-5715
    • Tomar, R.S.1    Matta, H.2    Chaudhary, P.M.3
  • 193
    • 13644255422 scopus 로고    scopus 로고
    • Lentiviral vectors for treating and modeling human CNS disorders
    • Azzouz M, Kingsman SM, Mazarakis ND. Lentiviral vectors for treating and modeling human CNS disorders. J Gene Med. 2004; 6(9): 951-62.
    • (2004) J Gene Med , vol.6 , Issue.9 , pp. 951-962
    • Azzouz, M.1    Kingsman, S.M.2    Mazarakis, N.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.