메뉴 건너뛰기




Volumn 110, Issue 6, 2009, Pages 1737-1765

The pathogenic mechanisms of polyglutamine diseases and current therapeutic strategies

Author keywords

CAG repeat; Huntingtin; Huntington's disease; Pathogenesis; Polyglutamine; Therapy

Indexed keywords

17 DEMETHOXY 17 (2 DIMETHYLAMINOETHYLAMINO)GELDANAMYCIN; 4 (1 AMINOETHYL) N (4 PYRIDYL)CYCLOHEXANECARBOXAMIDE; AMILORIDE; ANTIOXIDANT; BENZAMIL; BUTYRIC ACID; CLIOQUINOL; CONGO RED; CREATINE; CYSTAMINE; DICHLOROACETIC ACID; HEAT SHOCK PROTEIN; HYDROXAMIC ACID; LITHIUM; MINOCYCLINE; MUTANT PROTEIN; POLYGLUTAMINE; PROTEASOME; REMACEMIDE; RESVERATROL; RILUZOLE; ROLIPRAM; SUMO PROTEIN; TANESPIMYCIN; TAUROURSODEOXYCHOLIC ACID; TEPRENONE; THIOCTIC ACID; TREHALOSE; UBIDECARENONE; UNINDEXED DRUG;

EID: 69949170793     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2009.06302.x     Document Type: Review
Times cited : (152)

References (359)
  • 1
    • 0344406276 scopus 로고    scopus 로고
    • Phenotypes of spinocerebellar ataxia type 6 and familial hemiplegic migraine caused by a unique CACNA1A missense mutation in patients from a large family
    • Alonso I., Barros J., Tuna A., Coelho J., Sequeiros J., Silveira I. Coutinho P. (2003) Phenotypes of spinocerebellar ataxia type 6 and familial hemiplegic migraine caused by a unique CACNA1A missense mutation in patients from a large family. Arch. Neurol. 60, 610 614.
    • (2003) Arch. Neurol. , vol.60 , pp. 610-614
    • Alonso, I.1    Barros, J.2    Tuna, A.3    Coelho, J.4    Sequeiros, J.5    Silveira, I.6    Coutinho, P.7
  • 2
    • 33748741301 scopus 로고    scopus 로고
    • CHIP protects from the neurotoxicity of expanded and wild-type ataxin-1 and promotes their ubiquitination and degradation
    • Al-Ramahi I., Lam Y. C., Chen H. K. et al. (2006) CHIP protects from the neurotoxicity of expanded and wild-type ataxin-1 and promotes their ubiquitination and degradation. J. Biol. Chem. 281, 26714 26724.
    • (2006) J. Biol. Chem. , vol.281 , pp. 26714-26724
    • Al-Ramahi, I.1    Lam, Y.C.2    Chen, H.K.3
  • 3
    • 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. (2001a) Creatine increase survival and delays motor symptoms in a transgenic animal model of Huntington's disease. Neurobiol. Dis. 8, 479 491.
    • (2001) Neurobiol. Dis. , vol.8 , pp. 479-491
    • Andreassen, O.A.1    Dedeoglu, A.2    Ferrante, R.J.3
  • 4
    • 0034955984 scopus 로고    scopus 로고
    • Dichloroacetate exerts therapeutic effects in transgenic mouse models of Huntington's disease
    • Andreassen O. A., Ferrante R. J., Huang H. M. et al. (2001b) Dichloroacetate exerts therapeutic effects in transgenic mouse models of Huntington's disease. Ann. Neurol. 50, 112 117.
    • (2001) Ann. Neurol. , vol.50 , pp. 112-117
    • Andreassen, O.A.1    Ferrante, R.J.2    Huang, H.M.3
  • 5
    • 0033616449 scopus 로고    scopus 로고
    • Androgen receptor immunoreactivity in specific neural regions in normal and hypogonadal male mice: Effect of androgens
    • Apostolinas S., Rajendren G., Dobrjansky A. Gibson M. J. (1999) Androgen receptor immunoreactivity in specific neural regions in normal and hypogonadal male mice: effect of androgens. Brain Res. 817, 19 24.
    • (1999) Brain Res. , vol.817 , pp. 19-24
    • Apostolinas, S.1    Rajendren, G.2    Dobrjansky, A.3    Gibson, M.J.4
  • 7
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • Arrasate M., Mitra S., Schweitzer E. S., Segal M. R. Finkbeiner S. (2004) Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 431, 805 810.
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 8
    • 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., Taylor J., Epand R. M. Truant R. (2007) Huntingtin has a membrane association signal that can modulate huntingtin aggregation, nuclear entry and toxicity. Hum. Mol. Genet. 16, 2600 2615.
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 2600-2615
    • Atwal, R.S.1    Xia, J.2    Pinchev, D.3    Taylor, J.4    Epand, R.M.5    Truant, R.6
  • 9
    • 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. (2005) p53 mediates cellular dysfunction and behavioral abnormalities in Huntington's disease. Neuron 47, 29 41.
    • (2005) Neuron , vol.47 , pp. 29-41
    • Bae, B.I.1    Xu, H.2    Igarashi, S.3
  • 10
    • 0033013126 scopus 로고    scopus 로고
    • Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions
    • Ballinger C. A., Connell P., Wu Y., Hu Z., Thompson L. J., Yin L. Y. Patterson C. (1999) Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions. Mol. Cell. Biol. 19, 4535 4545.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4535-4545
    • Ballinger, C.A.1    Connell, P.2    Wu, Y.3    Hu, Z.4    Thompson, L.J.5    Yin, L.Y.6    Patterson, C.7
  • 11
    • 62549084738 scopus 로고    scopus 로고
    • Phase 2 trial of leuprorelin in patients with spinal and bulbar muscular atrophy
    • Banno H., Katsuno M., Suzuki K. et al. (2009) Phase 2 trial of leuprorelin in patients with spinal and bulbar muscular atrophy. Ann. Neurol. 65, 140 150.
    • (2009) Ann. Neurol. , vol.65 , pp. 140-150
    • Banno, H.1    Katsuno, M.2    Suzuki, K.3
  • 12
    • 31644449783 scopus 로고    scopus 로고
    • Mouse models of triplet repeat diseases
    • Bates G. P. Gonitel R. (2006) Mouse models of triplet repeat diseases. Mol. Biotechnol. 32, 147 158.
    • (2006) Mol. Biotechnol. , vol.32 , pp. 147-158
    • Bates, G.P.1    Gonitel, R.2
  • 13
    • 0042126676 scopus 로고    scopus 로고
    • Experimental therapeutics in Huntington's disease: Are models useful for therapeutic trials?
    • Bates G. P. Hockly E. (2003) Experimental therapeutics in Huntington's disease: are models useful for therapeutic trials? Curr. Opin. Neurol. 16, 465 470.
    • (2003) Curr. Opin. Neurol. , vol.16 , pp. 465-470
    • Bates, G.P.1    Hockly, E.2
  • 14
    • 4344635593 scopus 로고    scopus 로고
    • Large de novo expansion of CAG repeats in patient with sporadic spinocerebellar ataxia type 7
    • Bauer P., Kraus J., Matoska V., Brouckova M., Zumrova A. Goetz P. (2004a) Large de novo expansion of CAG repeats in patient with sporadic spinocerebellar ataxia type 7. J. Neurol. 251, 1023 1024.
    • (2004) J. Neurol. , vol.251 , pp. 1023-1024
    • Bauer, P.1    Kraus, J.2    Matoska, V.3    Brouckova, M.4    Zumrova, A.5    Goetz, P.6
  • 15
    • 7044254730 scopus 로고    scopus 로고
    • Can ataxin-2 be down-regulated by allele-specific de novo DNA methylation in SCA2 patients?
    • Bauer P. O., Zumrova A., Matoska V., Mitsui K. Goetz P. (2004b) Can ataxin-2 be down-regulated by allele-specific de novo DNA methylation in SCA2 patients? Med. Hypotheses 63, 1018 1023.
    • (2004) Med. Hypotheses , vol.63 , pp. 1018-1023
    • Bauer, P.O.1    Zumrova, A.2    Matoska, V.3    Mitsui, K.4    Goetz, P.5
  • 17
    • 24044481691 scopus 로고    scopus 로고
    • Absence of spinocerebellar ataxia type 3/Machado-Joseph disease within ataxic patients in the Czech population
    • Bauer P. O., Zumrova A., Matoska V., Marikova T., Krilova S., Boday A., Singh B. Goetz P. (2005b) Absence of spinocerebellar ataxia type 3/Machado-Joseph disease within ataxic patients in the Czech population. Eur. J. Neurol. 12, 851 857.
    • (2005) Eur. J. Neurol. , vol.12 , pp. 851-857
    • Bauer, P.O.1    Zumrova, A.2    Matoska, V.3    Marikova, T.4    Krilova, S.5    Boday, A.6    Singh, B.7    Goetz, P.8
  • 19
    • 2342598416 scopus 로고    scopus 로고
    • Experimental therapeutics in transgenic mouse models of Huntington's disease
    • Beal M. F. Ferrante R. J. (2004) Experimental therapeutics in transgenic mouse models of Huntington's disease. Nat. Rev. Neurosci. 5, 373 384.
    • (2004) Nat. Rev. Neurosci. , vol.5 , pp. 373-384
    • Beal, M.F.1    Ferrante, R.J.2
  • 20
    • 0027204154 scopus 로고
    • Age-dependent striatal excitotoxic lesions produced by the endogenous mitochondrial inhibitor malonate
    • Beal M. F., Brouillet E., Jenkins B., Henshaw R., Rosen B. Hyman B. T. (1993) Age-dependent striatal excitotoxic lesions produced by the endogenous mitochondrial inhibitor malonate. J. Neurochem. 61, 1147 1150.
    • (1993) J. Neurochem. , vol.61 , pp. 1147-1150
    • Beal, M.F.1    Brouillet, E.2    Jenkins, B.3    Henshaw, R.4    Rosen, B.5    Hyman, B.T.6
  • 21
    • 0031918640 scopus 로고    scopus 로고
    • Intranuclear neuronal inclusions in Huntington's disease and dentatorubral and pallidoluysian atrophy: Correlation between the density of inclusions and IT15 CAG triplet repeat length
    • Becher M. W., Kotzuk J. A., Sharp A. H., Davies S. W., Bates G. P., Price D. L. Ross C. A. (1998) Intranuclear neuronal inclusions in Huntington's disease and dentatorubral and pallidoluysian atrophy: correlation between the density of inclusions and IT15 CAG triplet repeat length. Neurobiol. Dis. 4, 387 397.
    • (1998) Neurobiol. Dis. , vol.4 , pp. 387-397
    • Becher, M.W.1    Kotzuk, J.A.2    Sharp, A.H.3    Davies, S.W.4    Bates, G.P.5    Price, D.L.6    Ross, C.A.7
  • 22
    • 4544335687 scopus 로고    scopus 로고
    • The N-methyl-D-aspartate antagonist memantine retards progression of Huntington's disease
    • Beister A., Kraus P., Kuhn W., Dose M., Weindl A. Gerlach M. (2004) The N-methyl-D-aspartate antagonist memantine retards progression of Huntington's disease. J. Neural Transm. Suppl. 68, 117 122.
    • (2004) J. Neural Transm. Suppl. , vol.68 , pp. 117-122
    • Beister, A.1    Kraus, P.2    Kuhn, W.3    Dose, M.4    Weindl, A.5    Gerlach, M.6
  • 23
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence N. F., Sampat R. M. Kopito R. R. (2001) Impairment of the ubiquitin-proteasome system by protein aggregation. Science 292, 1552 1555.
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 24
    • 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., McFarland K. N., DiRocco D. P., Yohrling G. J., Clark T. W., Bouzou B. Cha J. H. (2008) Huntingtin modulates transcription, occupies gene promoters in vivo, and binds directly to DNA in a polyglutamine-dependent manner. J. Neurosci. 28, 10720 10733.
    • (2008) J. Neurosci. , vol.28 , pp. 10720-10733
    • Benn, C.L.1    Sun, T.2    Sadri-Vakili, G.3    McFarland, K.N.4    Dirocco, D.P.5    Yohrling, G.J.6    Clark, T.W.7    Bouzou, B.8    Cha, J.H.9
  • 27
    • 2542445545 scopus 로고    scopus 로고
    • Caspase-mediated proteolysis of the polyglutamine disease protein ataxin-3
    • Berke S. J., Schmied F. A., Brunt E. R., Ellerby L. M. Paulson H. L. (2004) Caspase-mediated proteolysis of the polyglutamine disease protein ataxin-3. J. Neurochem. 89, 908 918.
    • (2004) J. Neurochem. , vol.89 , pp. 908-918
    • Berke, S.J.1    Schmied, F.A.2    Brunt, E.R.3    Ellerby, L.M.4    Paulson, H.L.5
  • 28
    • 84934876772 scopus 로고    scopus 로고
    • Inositol 1,4,5-tripshosphate receptor, calcium signalling and Huntington's disease
    • Bezprozvanny I. (2007) Inositol 1,4,5-tripshosphate receptor, calcium signalling and Huntington's disease. Subcell. Biochem. 45, 323 335.
    • (2007) Subcell. Biochem. , vol.45 , pp. 323-335
    • Bezprozvanny, I.1
  • 29
    • 4444302167 scopus 로고    scopus 로고
    • Deranged neuronal calcium signaling and Huntington disease
    • Bezprozvanny I. Hayden M. R. (2004) Deranged neuronal calcium signaling and Huntington disease. Biochem. Biophys. Res. Commun. 322, 1310 1317.
    • (2004) Biochem. Biophys. Res. Commun. , vol.322 , pp. 1310-1317
    • Bezprozvanny, I.1    Hayden, M.R.2
  • 31
    • 33745593049 scopus 로고    scopus 로고
    • Activity-dependent dynamics and sequestration of proteasomes in dendritic spines
    • Bingol B. Schuman E. M. (2006) Activity-dependent dynamics and sequestration of proteasomes in dendritic spines. Nature 441, 1144 1148.
    • (2006) Nature , vol.441 , pp. 1144-1148
    • Bingol, B.1    Schuman, E.M.2
  • 32
    • 0028287265 scopus 로고
    • Current advances and trends in the treatment of depression
    • Blier P. de Montigny C. (1994) Current advances and trends in the treatment of depression. Trends Pharmacol. Sci. 15, 220 226.
    • (1994) Trends Pharmacol. Sci. , vol.15 , pp. 220-226
    • Blier, P.1    De Montigny, C.2
  • 34
    • 28744456853 scopus 로고    scopus 로고
    • Silencing polyglutamine degeneration with RNAi
    • Bonini N. M. La Spada A. R. (2005) Silencing polyglutamine degeneration with RNAi. Neuron 48, 715 718.
    • (2005) Neuron , vol.48 , pp. 715-718
    • Bonini, N.M.1    La Spada, A.R.2
  • 35
    • 0029129227 scopus 로고
    • Spinal and bulbar muscular atrophy: A trinucleotide-repeat expansion neurodegenerative disease
    • Brooks B. P. Fischbeck K. H. (1995) Spinal and bulbar muscular atrophy: a trinucleotide-repeat expansion neurodegenerative disease. Trends Neurosci. 18, 459 461.
    • (1995) Trends Neurosci. , vol.18 , pp. 459-461
    • Brooks, B.P.1    Fischbeck, K.H.2
  • 36
    • 0029118136 scopus 로고
    • Chronic mitochondrial energy impairment produces selective striatal degeneration and abnormal choreiform movements in primates
    • Brouillet E., Hantraye P., Ferrante R. J., Dolan R., Leroy-Willig A., Kowall N. W. Beal M. F. (1995) Chronic mitochondrial energy impairment produces selective striatal degeneration and abnormal choreiform movements in primates. Proc. Natl Acad. Sci. USA 92, 7105 7109.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 7105-7109
    • Brouillet, E.1    Hantraye, P.2    Ferrante, R.J.3    Dolan, R.4    Leroy-Willig, A.5    Kowall, N.W.6    Beal, M.F.7
  • 37
    • 33947675275 scopus 로고    scopus 로고
    • Oxidative damage in Huntington's disease pathogenesis
    • Browne S. E. Beal M. F. (2006) Oxidative damage in Huntington's disease pathogenesis. Antioxid. Redox Signal. 8, 2061 2073.
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 2061-2073
    • Browne, S.E.1    Beal, M.F.2
  • 38
    • 33845950366 scopus 로고    scopus 로고
    • The fly as a model for neurodegenerative diseases: Is it worth the jump?
    • Cauchi R. J. van den Heuvel M. (2006) The fly as a model for neurodegenerative diseases: is it worth the jump? Neurodegener. Dis. 3, 338 356.
    • (2006) Neurodegener. Dis. , vol.3 , pp. 338-356
    • Cauchi, R.J.1    Van Den Heuvel, M.2
  • 40
    • 0033499931 scopus 로고    scopus 로고
    • Analysis of the role of heat shock protein (Hsp) molecular chaperones in polyglutamine disease
    • Chai Y., Koppenhafer S. L., Bonini N. M. Paulson H. L. (1999a) Analysis of the role of heat shock protein (Hsp) molecular chaperones in polyglutamine disease. J. Neurosci. 19, 10338 10347.
    • (1999) J. Neurosci. , vol.19 , pp. 10338-10347
    • Chai, Y.1    Koppenhafer, S.L.2    Bonini, N.M.3    Paulson, H.L.4
  • 41
    • 0033030565 scopus 로고    scopus 로고
    • Evidence for proteasome involvement in polyglutamine disease: Localization to nuclear inclusions in SCA3/MJD and suppression of polyglutamine aggregation in vitro
    • Chai Y., Koppenhafer S. L., Shoesmith S. J., Perez M. K. Paulson H. L. (1999b) Evidence for proteasome involvement in polyglutamine disease: localization to nuclear inclusions in SCA3/MJD and suppression of polyglutamine aggregation in vitro. Hum. Mol. Genet. 8, 673 682.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 673-682
    • Chai, Y.1    Koppenhafer, S.L.2    Shoesmith, S.J.3    Perez, M.K.4    Paulson, H.L.5
  • 42
    • 0037101838 scopus 로고    scopus 로고
    • Increased huntingtin protein length reduces the number of polyglutamine-induced gene expression changes in mouse models of Huntington's disease
    • Chan E. Y., Luthi-Carter R., Strand A. et al. (2002) Increased huntingtin protein length reduces the number of polyglutamine-induced gene expression changes in mouse models of Huntington's disease. Hum. Mol. Genet. 11, 1939 1951.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1939-1951
    • Chan, E.Y.1    Luthi-Carter, R.2    Strand, A.3
  • 43
    • 33646136884 scopus 로고    scopus 로고
    • Mutant huntingtin aggregates impair mitochondrial movement and trafficking in cortical neurons
    • Chang D. T., Rintoul G. L., Pandipati S. Reynolds I. J. (2006) Mutant huntingtin aggregates impair mitochondrial movement and trafficking in cortical neurons. Neurobiol. Dis. 22, 388 400.
    • (2006) Neurobiol. Dis. , vol.22 , pp. 388-400
    • Chang, D.T.1    Rintoul, G.L.2    Pandipati, S.3    Reynolds, I.J.4
  • 44
    • 0033912716 scopus 로고    scopus 로고
    • Minocycline inhibits caspase-1 and caspase-3 expression and delays mortality in a transgenic mouse model of Huntington disease
    • Chen M., Ona V. O., Li M. et al. (2000) Minocycline inhibits caspase-1 and caspase-3 expression and delays mortality in a transgenic mouse model of Huntington disease. Nat. Med. 6, 797 801.
    • (2000) Nat. Med. , vol.6 , pp. 797-801
    • Chen, M.1    Ona, V.O.2    Li, M.3
  • 45
    • 0037726598 scopus 로고    scopus 로고
    • Interaction of Akt-phosphorylated ataxin-1 with 14-3-3 mediates neurodegeneration in spinocerebellar ataxia type 1
    • Chen H. K., Fernandez-Funez P., Acevedo S. F. et al. (2003) Interaction of Akt-phosphorylated ataxin-1 with 14-3-3 mediates neurodegeneration in spinocerebellar ataxia type 1. Cell 113, 457 468.
    • (2003) Cell , vol.113 , pp. 457-468
    • Chen, H.K.1    Fernandez-Funez, P.2    Acevedo, S.F.3
  • 48
    • 28444444502 scopus 로고    scopus 로고
    • Polyglutamine is not all: The functional role of the AXH domain in the ataxin-1 protein
    • de Chiara C., Menon R. P., Dal Piaz F., Calder L. Pastore A. (2005) Polyglutamine is not all: the functional role of the AXH domain in the ataxin-1 protein. J. Mol. Biol. 354, 883 893.
    • (2005) J. Mol. Biol. , vol.354 , pp. 883-893
    • De Chiara, C.1    Menon, R.P.2    Dal Piaz, F.3    Calder, L.4    Pastore, A.5
  • 49
    • 3543141113 scopus 로고    scopus 로고
    • Mutant huntingtin directly increases susceptibility of mitochondria to the calcium-induced permeability transition and cytochrome c release
    • Choo Y. S., Johnson G. V., MacDonald M., Detloff P. J. Lesort M. (2004) Mutant huntingtin directly increases susceptibility of mitochondria to the calcium-induced permeability transition and cytochrome c release. Hum. Mol. Genet. 13, 1407 1420.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 1407-1420
    • Choo, Y.S.1    Johnson, G.V.2    MacDonald, M.3    Detloff, P.J.4    Lesort, M.5
  • 50
    • 30744474942 scopus 로고    scopus 로고
    • Polyglutamine-expanded ataxin-3 activates mitochondrial apoptotic pathway by upregulating Bax and downregulating Bcl-xL
    • Chou A. H., Yeh T. H., Kuo Y. L., Kao Y. C., Jou M. J., Hsu C. Y., Tsai S. R., Kakizuka A. Wang H. L. (2006) Polyglutamine-expanded ataxin-3 activates mitochondrial apoptotic pathway by upregulating Bax and downregulating Bcl-xL. Neurobiol. Dis. 21, 333 345.
    • (2006) Neurobiol. Dis. , vol.21 , pp. 333-345
    • Chou, A.H.1    Yeh, T.H.2    Kuo, Y.L.3    Kao, Y.C.4    Jou, M.J.5    Hsu, C.Y.6    Tsai, S.R.7    Kakizuka, A.8    Wang, H.L.9
  • 51
    • 33745879143 scopus 로고    scopus 로고
    • Intracellular protein degradation: From a vague idea thru the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting
    • Ciechanover A. (2006) Intracellular protein degradation: from a vague idea thru the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting. Exp. Biol. Med. (Maywood) 231, 1197 1211. (Pubitemid 44050466)
    • (2006) Experimental Biology and Medicine , vol.231 , Issue.7 , pp. 1197-1211
    • Ciechanover, A.1
  • 52
    • 49149112606 scopus 로고    scopus 로고
    • Huntingtin phosphorylation acts as a molecular switch for anterograde/retrograde transport in neurons
    • Colin E., Zala D., Liot G., Rangone H., Borrell-Pages M., Li X. J., Saudou F. Humbert S. (2008) Huntingtin phosphorylation acts as a molecular switch for anterograde/retrograde transport in neurons. EMBO J. 27, 2124 2134.
    • (2008) EMBO J. , vol.27 , pp. 2124-2134
    • Colin, E.1    Zala, D.2    Liot, G.3    Rangone, H.4    Borrell-Pages, M.5    Li, X.J.6    Saudou, F.7    Humbert, S.8
  • 53
    • 34548329581 scopus 로고    scopus 로고
    • A mutant ataxin-3 fragment results from processing at a site N-terminal to amino acid 190 in brain of Machado-Joseph disease-like transgenic mice
    • Colomer Gould V. F., Goti D., Pearce D. et al. (2007) A mutant ataxin-3 fragment results from processing at a site N-terminal to amino acid 190 in brain of Machado-Joseph disease-like transgenic mice. Neurobiol. Dis. 27, 362 369.
    • (2007) Neurobiol. Dis. , vol.27 , pp. 362-369
    • Colomer Gould, V.F.1    Goti, D.2    Pearce, D.3
  • 54
    • 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. (1998) Truncated N-terminal fragments of huntingtin with expanded glutamine repeats form nuclear and cytoplasmic aggregates in cell culture. Hum. Mol. Genet. 7, 783 790.
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 783-790
    • Cooper, J.K.1    Schilling, G.2    Peters, M.F.3
  • 56
    • 33749042331 scopus 로고    scopus 로고
    • Transcriptional repression of PGC-1alpha by mutant huntingtin leads to mitochondrial dysfunction and neurodegeneration
    • Cui L., Jeong H., Borovecki F., Parkhurst C. N., Tanese N. Krainc D. (2006) Transcriptional repression of PGC-1alpha by mutant huntingtin leads to mitochondrial dysfunction and neurodegeneration. Cell 127, 59 69.
    • (2006) Cell , vol.127 , pp. 59-69
    • Cui, L.1    Jeong, H.2    Borovecki, F.3    Parkhurst, C.N.4    Tanese, N.5    Krainc, D.6
  • 57
    • 0031838352 scopus 로고    scopus 로고
    • Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1
    • Cummings C. J., Mancini M. A., Antalffy B., DeFranco D. B., Orr H. T. Zoghbi H. Y. (1998) Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1. Nat. Genet. 19, 148 154.
    • (1998) Nat. Genet. , vol.19 , pp. 148-154
    • Cummings, C.J.1    Mancini, M.A.2    Antalffy, B.3    Defranco, D.B.4    Orr, H.T.5    Zoghbi, H.Y.6
  • 58
    • 0033391428 scopus 로고    scopus 로고
    • Mutation of the E6-AP ubiquitin ligase reduces nuclear inclusion frequency while accelerating polyglutamine-induced pathology in SCA1 mice
    • Cummings C. J., Reinstein E., Sun Y., Antalffy B., Jiang Y., Ciechanover A., Orr H. T., Beaudet A. L. Zoghbi H. Y. (1999) Mutation of the E6-AP ubiquitin ligase reduces nuclear inclusion frequency while accelerating polyglutamine-induced pathology in SCA1 mice. Neuron 24, 879 892.
    • (1999) Neuron , vol.24 , pp. 879-892
    • Cummings, C.J.1    Reinstein, E.2    Sun, Y.3    Antalffy, B.4    Jiang, Y.5    Ciechanover, A.6    Orr, H.T.7    Beaudet, A.L.8    Zoghbi, H.Y.9
  • 59
    • 0035394668 scopus 로고    scopus 로고
    • Over-expression of inducible HSP70 chaperone suppresses neuropathology and improves motor function in SCA1 mice
    • Cummings C. J., Sun Y., Opal P., Antalffy B., Mestril R., Orr H. T., Dillmann W. H. Zoghbi H. Y. (2001) Over-expression of inducible HSP70 chaperone suppresses neuropathology and improves motor function in SCA1 mice. Hum. Mol. Genet. 10, 1511 1518.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1511-1518
    • Cummings, C.J.1    Sun, Y.2    Opal, P.3    Antalffy, B.4    Mestril, R.5    Orr, H.T.6    Dillmann, W.H.7    Zoghbi, H.Y.8
  • 60
    • 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. (1997) Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation. Cell 90, 537 548.
    • (1997) Cell , vol.90 , pp. 537-548
    • Davies, S.W.1    Turmaine, M.2    Cozens, B.A.3
  • 61
    • 38449083555 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in Huntington's disease and the spinocerebellar ataxias
    • Davies J. E., Sarkar S. Rubinsztein D. C. (2007) The ubiquitin proteasome system in Huntington's disease and the spinocerebellar ataxias. BMC Biochem. 8 (Suppl. 1 S2.
    • (2007) BMC Biochem. , vol.8 , Issue.SUPPL. 1 , pp. 2
    • Davies, J.E.1    Sarkar, S.2    Rubinsztein, D.C.3
  • 62
    • 0037109665 scopus 로고    scopus 로고
    • Therapeutic effects of cystamine in a murine model of Huntington's disease
    • Dedeoglu A., Kubilus J. K., Jeitner T. M. et al. (2002) Therapeutic effects of cystamine in a murine model of Huntington's disease. J. Neurosci. 22, 8942 8950.
    • (2002) J. Neurosci. , vol.22 , pp. 8942-8950
    • Dedeoglu, A.1    Kubilus, J.K.2    Jeitner, T.M.3
  • 64
    • 43649092175 scopus 로고    scopus 로고
    • Beneficial effects of rolipram in the R6/2 mouse model of Huntington's disease
    • DeMarch Z., Giampa C., Patassini S., Bernardi G. Fusco F. R. (2008) Beneficial effects of rolipram in the R6/2 mouse model of Huntington's disease. Neurobiol. Dis. 30, 375 387.
    • (2008) Neurobiol. Dis. , vol.30 , pp. 375-387
    • Demarch, Z.1    Giampa, C.2    Patassini, S.3    Bernardi, G.4    Fusco, F.R.5
  • 65
    • 0036670407 scopus 로고    scopus 로고
    • Huntingtin fragments that aggregate go their separate ways
    • DiFiglia M. (2002) Huntingtin fragments that aggregate go their separate ways. Mol. Cell 10, 224 225.
    • (2002) Mol. Cell , vol.10 , pp. 224-225
    • Difiglia, M.1
  • 66
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DiFiglia M., Sapp E., Chase K. O., Davies S. W., Bates G. P., Vonsattel J. P. Aronin N. (1997) Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 277, 1990 1993.
    • (1997) Science , vol.277 , pp. 1990-1993
    • Difiglia, M.1    Sapp, E.2    Chase, K.O.3    Davies, S.W.4    Bates, G.P.5    Vonsattel, J.P.6    Aronin, N.7
  • 67
    • 3342879140 scopus 로고    scopus 로고
    • Identification of ubiquitin-interacting proteins in purified polyglutamine aggregates
    • Doi H., Mitsui K., Kurosawa M., Machida Y., Kuroiwa Y. Nukina N. (2004) Identification of ubiquitin-interacting proteins in purified polyglutamine aggregates. FEBS Lett. 571, 171 176.
    • (2004) FEBS Lett. , vol.571 , pp. 171-176
    • Doi, H.1    Mitsui, K.2    Kurosawa, M.3    MacHida, Y.4    Kuroiwa, Y.5    Nukina, N.6
  • 68
    • 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. (2008) RNA-binding protein TLS is a major nuclear aggregate-interacting protein in huntingtin exon 1 with expanded polyglutamine-expressing cells. J. Biol. Chem. 283, 6489 6500.
    • (2008) J. Biol. Chem. , vol.283 , pp. 6489-6500
    • Doi, H.1    Okamura, K.2    Bauer, P.O.3
  • 69
    • 0037373633 scopus 로고    scopus 로고
    • Dying for a cause: Invertebrate genetics takes on human neurodegeneration
    • Driscoll M. Gerstbrein B. (2003) Dying for a cause: invertebrate genetics takes on human neurodegeneration. Nat. Rev. Genet. 4, 181 194.
    • (2003) Nat. Rev. Genet. , vol.4 , pp. 181-194
    • Driscoll, M.1    Gerstbrein, B.2
  • 71
    • 43649106471 scopus 로고    scopus 로고
    • Sertraline slows disease progression and increases neurogenesis in N171-82Q mouse model of Huntington's disease
    • Duan W., Peng Q., Masuda N. et al. (2008) Sertraline slows disease progression and increases neurogenesis in N171-82Q mouse model of Huntington's disease. Neurobiol. Dis. 30, 312 322.
    • (2008) Neurobiol. Dis. , vol.30 , pp. 312-322
    • Duan, W.1    Peng, Q.2    Masuda, N.3
  • 72
    • 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. (2002) Sp1 and TAFII130 transcriptional activity disrupted in early Huntington's disease. Science 296, 2238 2243.
    • (2002) Science , vol.296 , pp. 2238-2243
    • Dunah, A.W.1    Jeong, H.2    Griffin, A.3
  • 73
    • 0035179456 scopus 로고    scopus 로고
    • Mutant protein in Huntington disease is resistant to proteolysis in affected brain
    • Dyer R. B. McMurray C. T. (2001) Mutant protein in Huntington disease is resistant to proteolysis in affected brain. Nat. Genet. 29, 270 278.
    • (2001) Nat. Genet. , vol.29 , pp. 270-278
    • Dyer, R.B.1    McMurray, C.T.2
  • 74
    • 0033605746 scopus 로고    scopus 로고
    • Cleavage of atrophin-1 at caspase site aspartic acid 109 modulates cytotoxicity
    • Ellerby L. M., Andrusiak R. L., Wellington C. L. et al. (1999) Cleavage of atrophin-1 at caspase site aspartic acid 109 modulates cytotoxicity. J. Biol. Chem. 274, 8730 8736.
    • (1999) J. Biol. Chem. , vol.274 , pp. 8730-8736
    • Ellerby, L.M.1    Andrusiak, R.L.2    Wellington, C.L.3
  • 75
    • 33745195252 scopus 로고    scopus 로고
    • The two-stage pathway of ataxin-3 fibrillogenesis involves a polyglutamine-independent step
    • Ellisdon A. M., Thomas B. Bottomley S. P. (2006) The two-stage pathway of ataxin-3 fibrillogenesis involves a polyglutamine-independent step. J. Biol. Chem. 281, 16888 16896.
    • (2006) J. Biol. Chem. , vol.281 , pp. 16888-16896
    • Ellisdon, A.M.1    Thomas, B.2    Bottomley, S.P.3
  • 76
    • 3042677641 scopus 로고    scopus 로고
    • Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome
    • Elsasser S., Chandler-Militello D., Muller B., Hanna J. Finley D. (2004) Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome. J. Biol. Chem. 279, 26817 26822.
    • (2004) J. Biol. Chem. , vol.279 , pp. 26817-26822
    • Elsasser, S.1    Chandler-Militello, D.2    Muller, B.3    Hanna, J.4    Finley, D.5
  • 78
    • 34247160537 scopus 로고    scopus 로고
    • Phosphorylation of ataxin-3 by glycogen synthase kinase 3beta at serine 256 regulates the aggregation of ataxin-3
    • Fei E., Jia N., Zhang T. et al. (2007) Phosphorylation of ataxin-3 by glycogen synthase kinase 3beta at serine 256 regulates the aggregation of ataxin-3. Biochem. Biophys. Res. Commun. 357, 487 492.
    • (2007) Biochem. Biophys. Res. Commun. , vol.357 , pp. 487-492
    • Fei, E.1    Jia, N.2    Zhang, T.3
  • 79
    • 37249083913 scopus 로고    scopus 로고
    • Mitochondrial sensitivity and altered calcium handling underlie enhanced NMDA-induced apoptosis in YAC128 model of Huntington's disease
    • Fernandes H. B., Baimbridge K. G., Church J., Hayden M. R. Raymond L. A. (2007) Mitochondrial sensitivity and altered calcium handling underlie enhanced NMDA-induced apoptosis in YAC128 model of Huntington's disease. J. Neurosci. 27, 13614 13623.
    • (2007) J. Neurosci. , vol.27 , pp. 13614-13623
    • Fernandes, H.B.1    Baimbridge, K.G.2    Church, J.3    Hayden, M.R.4    Raymond, L.A.5
  • 80
    • 0034597833 scopus 로고    scopus 로고
    • Identification of genes that modify ataxin-1-induced neurodegeneration
    • Fernandez-Funez P., Nino-Rosales M. L., de Gouyon B. et al. (2000) Identification of genes that modify ataxin-1-induced neurodegeneration. Nature 408, 101 106.
    • (2000) Nature , vol.408 , pp. 101-106
    • Fernandez-Funez, P.1    Nino-Rosales, M.L.2    De Gouyon, B.3
  • 81
    • 67349151319 scopus 로고    scopus 로고
    • Mouse models of Huntington's disease and methodological considerations for therapeutic trials
    • Ferrante R. J. (2009) Mouse models of Huntington's disease and methodological considerations for therapeutic trials. Biochim. Biophys. Acta 1792, 506 520.
    • (2009) Biochim. Biophys. Acta , vol.1792 , pp. 506-520
    • Ferrante, R.J.1
  • 84
    • 0142157600 scopus 로고    scopus 로고
    • Histone deacetylase inhibition by sodium butyrate chemotherapy ameliorates the neurodegenerative phenotype in Huntington's disease mice
    • Ferrante R. J., Kubilus J. K., Lee J. et al. (2003) Histone deacetylase inhibition by sodium butyrate chemotherapy ameliorates the neurodegenerative phenotype in Huntington's disease mice. J. Neurosci. 23, 9418 9427.
    • (2003) J. Neurosci. , vol.23 , pp. 9418-9427
    • Ferrante, R.J.1    Kubilus, J.K.2    Lee, J.3
  • 85
    • 20844455450 scopus 로고    scopus 로고
    • Chemotherapy for the brain: The antitumor antibiotic mithramycin prolongs survival in a mouse model of Huntington's disease
    • Ferrante R. J., Ryu H., Kubilus J. K. et al. (2004) Chemotherapy for the brain: the antitumor antibiotic mithramycin prolongs survival in a mouse model of Huntington's disease. J. Neurosci. 24, 10335 10342.
    • (2004) J. Neurosci. , vol.24 , pp. 10335-10342
    • Ferrante, R.J.1    Ryu, H.2    Kubilus, J.K.3
  • 86
    • 36448930958 scopus 로고    scopus 로고
    • Polyglutamine domain modulates the TBP-TFIIB interaction: Implications for its normal function and neurodegeneration
    • Friedman M. J., Shah A. G., Fang Z. H., Ward E. G., Warren S. T., Li S. Li X. J. (2007) Polyglutamine domain modulates the TBP-TFIIB interaction: implications for its normal function and neurodegeneration. Nat. Neurosci. 10, 1519 1528.
    • (2007) Nat. Neurosci. , vol.10 , pp. 1519-1528
    • Friedman, M.J.1    Shah, A.G.2    Fang, Z.H.3    Ward, E.G.4    Warren, S.T.5    Li, S.6    Li, X.J.7
  • 87
    • 43749091298 scopus 로고    scopus 로고
    • Polyglutamine expansion reduces the association of TATA-binding protein with DNA and induces DNA binding-independent neurotoxicity
    • Friedman M. J., Wang C. E., Li X. J. Li S. (2008) Polyglutamine expansion reduces the association of TATA-binding protein with DNA and induces DNA binding-independent neurotoxicity. J. Biol. Chem. 283, 8283 8290.
    • (2008) J. Biol. Chem. , vol.283 , pp. 8283-8290
    • Friedman, M.J.1    Wang, C.E.2    Li, X.J.3    Li, S.4
  • 88
    • 54449101793 scopus 로고    scopus 로고
    • Heat shock transcription factor 1-activating compounds suppress polyglutamine-induced neurodegeneration through induction of multiple molecular chaperones
    • Fujikake N., Nagai Y., Popiel H. A., Okamoto Y., Yamaguchi M. Toda T. (2008) Heat shock transcription factor 1-activating compounds suppress polyglutamine-induced neurodegeneration through induction of multiple molecular chaperones. J. Biol. Chem. 283, 26188 26197.
    • (2008) J. Biol. Chem. , vol.283 , pp. 26188-26197
    • Fujikake, N.1    Nagai, Y.2    Popiel, H.A.3    Okamoto, Y.4    Yamaguchi, M.5    Toda, T.6
  • 89
    • 65549100291 scopus 로고    scopus 로고
    • Cross-seeding fibrillation of Q/N-rich proteins offers new pathomechanism of polyglutamine diseases
    • Furukawa Y., Kaneko K., Matsumoto G., Kurosawa M. Nukina N. (2009) Cross-seeding fibrillation of Q/N-rich proteins offers new pathomechanism of polyglutamine diseases. J. Neurosci. 29, 5153 5162.
    • (2009) J. Neurosci. , vol.29 , pp. 5153-5162
    • Furukawa, Y.1    Kaneko, K.2    Matsumoto, G.3    Kurosawa, M.4    Nukina, N.5
  • 90
    • 0037096376 scopus 로고    scopus 로고
    • Calpain activation in Huntington's disease
    • Gafni J. Ellerby L. M. (2002) Calpain activation in Huntington's disease. J. Neurosci. 22, 4842 4849.
    • (2002) J. Neurosci. , vol.22 , pp. 4842-4849
    • Gafni, J.1    Ellerby, L.M.2
  • 91
    • 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., Wellington C. L., Hayden M. R. Ellerby L. M. (2004) Inhibition of calpain cleavage of huntingtin reduces toxicity: accumulation of calpain/caspase fragments in the nucleus. J. Biol. Chem. 279, 20211 20220.
    • (2004) J. Biol. Chem. , vol.279 , pp. 20211-20220
    • Gafni, J.1    Hermel, E.2    Young, J.E.3    Wellington, C.L.4    Hayden, M.R.5    Ellerby, L.M.6
  • 92
    • 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. (2005) Neuroprotective effects of phenylbutyrate in the N171-82Q transgenic mouse model of Huntington's disease. J. Biol. Chem. 280, 556 563.
    • (2005) J. Biol. Chem. , vol.280 , pp. 556-563
    • Gardian, G.1    Browne, S.E.2    Choi, D.K.3
  • 93
    • 25844487226 scopus 로고    scopus 로고
    • Diseases of unstable repeat expansion: Mechanisms and common principles
    • Gatchel J. R. Zoghbi H. Y. (2005) Diseases of unstable repeat expansion: mechanisms and common principles. Nat. Rev. Genet. 6, 743 755.
    • (2005) Nat. Rev. Genet. , vol.6 , pp. 743-755
    • Gatchel, J.R.1    Zoghbi, H.Y.2
  • 94
    • 0036173770 scopus 로고    scopus 로고
    • Recruitment and activation of caspase-8 by the Huntingtin-interacting protein Hip-1 and a novel partner Hippi
    • Gervais F. G., Singaraja R., Xanthoudakis S. et al. (2002) Recruitment and activation of caspase-8 by the Huntingtin-interacting protein Hip-1 and a novel partner Hippi. Nat. Cell Biol. 4, 95 105.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 95-105
    • Gervais, F.G.1    Singaraja, R.2    Xanthoudakis, S.3
  • 95
    • 61449226493 scopus 로고    scopus 로고
    • Phosphodiesterase type IV inhibition prevents sequestration of CREB binding protein, protects striatal parvalbumin interneurons and rescues motor deficits in the R6/2 mouse model of Huntington's disease
    • Giampa C., Middei S., Patassini S., Borreca A., Marullo F., Laurenti D., Bernardi G., Ammassari-Teule M. Fusco F. R. (2009) Phosphodiesterase type IV inhibition prevents sequestration of CREB binding protein, protects striatal parvalbumin interneurons and rescues motor deficits in the R6/2 mouse model of Huntington's disease. Eur. J. Neurosci. 29, 902 910.
    • (2009) Eur. J. Neurosci. , vol.29 , pp. 902-910
    • Giampa, C.1    Middei, S.2    Patassini, S.3    Borreca, A.4    Marullo, F.5    Laurenti, D.6    Bernardi, G.7    Ammassari-Teule, M.8    Fusco, F.R.9
  • 96
    • 60549103857 scopus 로고    scopus 로고
    • The R6 lines of transgenic mice: A model for screening new therapies for Huntington's disease
    • Gil J. M. Rego A. C. (2009) The R6 lines of transgenic mice: a model for screening new therapies for Huntington's disease. Brain Res. Rev. 59, 410 431.
    • (2009) Brain Res. Rev. , vol.59 , pp. 410-431
    • Gil, J.M.1    Rego, A.C.2
  • 97
    • 0345118102 scopus 로고    scopus 로고
    • Delayed onset of Huntington's disease in mice in an enriched environment correlates with delayed loss of cannabinoid CB1 receptors
    • Glass M., van Dellen A., Blakemore C., Hannan A. J. Faull R. L. (2004) Delayed onset of Huntington's disease in mice in an enriched environment correlates with delayed loss of cannabinoid CB1 receptors. Neuroscience 123, 207 212.
    • (2004) Neuroscience , vol.123 , pp. 207-212
    • Glass, M.1    Van Dellen, A.2    Blakemore, C.3    Hannan, A.J.4    Faull, R.L.5
  • 98
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • Goldberg A. L. (2003) Protein degradation and protection against misfolded or damaged proteins. Nature 426, 895 899.
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 99
    • 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 S. M., Mez J. et al. (2004) 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. 24, 10266 10279.
    • (2004) J. Neurosci. , vol.24 , pp. 10266-10279
    • Goti, D.1    Katzen, S.M.2    Mez, J.3
  • 100
    • 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. (2006) Cleavage at the caspase-6 site is required for neuronal dysfunction and degeneration due to mutant huntingtin. Cell 125, 1179 1191.
    • (2006) Cell , vol.125 , pp. 1179-1191
    • Graham, R.K.1    Deng, Y.2    Slow, E.J.3
  • 101
    • 46749157501 scopus 로고    scopus 로고
    • Full-length human mutant huntingtin with a stable polyglutamine repeat can elicit progressive and selective neuropathogenesis in BACHD mice
    • Gray M., Shirasaki D. I., Cepeda C. et al. (2008) Full-length human mutant huntingtin with a stable polyglutamine repeat can elicit progressive and selective neuropathogenesis in BACHD mice. J. Neurosci. 28, 6182 6195.
    • (2008) J. Neurosci. , vol.28 , pp. 6182-6195
    • Gray, M.1    Shirasaki, D.I.2    Cepeda, C.3
  • 102
    • 0027507667 scopus 로고
    • Human genetic diseases due to codon reiteration: Relationship to an evolutionary mechanism
    • Green H. (1993) Human genetic diseases due to codon reiteration: relationship to an evolutionary mechanism. Cell 74, 955 956.
    • (1993) Cell , vol.74 , pp. 955-956
    • Green, H.1
  • 103
    • 0033373421 scopus 로고    scopus 로고
    • Bioenergetics in Huntington's disease
    • Grunewald T. Beal M. F. (1999) Bioenergetics in Huntington's disease. Ann. NY Acad. Sci. 893, 203 213.
    • (1999) Ann. NY Acad. Sci. , vol.893 , pp. 203-213
    • Grunewald, T.1    Beal, M.F.2
  • 106
    • 32144436256 scopus 로고    scopus 로고
    • Proteolytic cleavage of polyglutamine-expanded ataxin-3 is critical for aggregation and sequestration of non-expanded ataxin-3
    • Haacke A., Broadley S. A., Boteva R., Tzvetkov N., Hartl F. U. Breuer P. (2006) Proteolytic cleavage of polyglutamine-expanded ataxin-3 is critical for aggregation and sequestration of non-expanded ataxin-3. Hum. Mol. Genet. 15, 555 568.
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 555-568
    • Haacke, A.1    Broadley, S.A.2    Boteva, R.3    Tzvetkov, N.4    Hartl, F.U.5    Breuer, P.6
  • 107
    • 0032946228 scopus 로고    scopus 로고
    • In vitro evidence for both the nucleus and cytoplasm as subcellular sites of pathogenesis in Huntington's disease
    • Hackam A. S., Singaraja R., Zhang T., Gan L. Hayden M. R. (1999) In vitro evidence for both the nucleus and cytoplasm as subcellular sites of pathogenesis in Huntington's disease. Hum. Mol. Genet. 8, 25 33.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 25-33
    • Hackam, A.S.1    Singaraja, R.2    Zhang, T.3    Gan, L.4    Hayden, M.R.5
  • 108
    • 0034731370 scopus 로고    scopus 로고
    • Huntingtin interacting protein 1 induces apoptosis via a novel caspase-dependent death effector domain
    • Hackam A. S., Yassa A. S., Singaraja R. et al. (2000) Huntingtin interacting protein 1 induces apoptosis via a novel caspase-dependent death effector domain. J. Biol. Chem. 275, 41299 41308.
    • (2000) J. Biol. Chem. , vol.275 , pp. 41299-41308
    • Hackam, A.S.1    Yassa, A.S.2    Singaraja, R.3
  • 109
    • 3242695184 scopus 로고    scopus 로고
    • Progressive decrease in chaperone protein levels in a mouse model of Huntington's disease and induction of stress proteins as a therapeutic approach
    • Hay D. G., Sathasivam K., Tobaben S. et al. (2004) Progressive decrease in chaperone protein levels in a mouse model of Huntington's disease and induction of stress proteins as a therapeutic approach. Hum. Mol. Genet. 13, 1389 1405.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 1389-1405
    • Hay, D.G.1    Sathasivam, K.2    Tobaben, S.3
  • 110
    • 3042771651 scopus 로고    scopus 로고
    • Ataxin-7 is a subunit of GCN5 histone acetyltransferase-containing complexes
    • Helmlinger D., Hardy S., Sasorith S. et al. (2004) Ataxin-7 is a subunit of GCN5 histone acetyltransferase-containing complexes. Hum. Mol. Genet. 13, 1257 1265.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 1257-1265
    • Helmlinger, D.1    Hardy, S.2    Sasorith, S.3
  • 111
    • 33144469085 scopus 로고    scopus 로고
    • Glutamine-expanded ataxin-7 alters TFTC/STAGA recruitment and chromatin structure leading to photoreceptor dysfunction
    • Helmlinger D., Hardy S., Abou-Sleymane G. et al. (2006) Glutamine-expanded ataxin-7 alters TFTC/STAGA recruitment and chromatin structure leading to photoreceptor dysfunction. PLoS Biol. 4, 432 445.
    • (2006) PLoS Biol. , vol.4 , pp. 432-445
    • Helmlinger, D.1    Hardy, S.2    Abou-Sleymane, G.3
  • 112
    • 34548161707 scopus 로고    scopus 로고
    • Longitudinal evaluation of the Hdh(CAG)150 knock-in murine model of Huntington's disease
    • Heng M. Y., Tallaksen-Greene S. J., Detloff P. J. Albin R. L. (2007) Longitudinal evaluation of the Hdh(CAG)150 knock-in murine model of Huntington's disease. J. Neurosci. 27, 8989 8998.
    • (2007) J. Neurosci. , vol.27 , pp. 8989-8998
    • Heng, M.Y.1    Tallaksen-Greene, S.J.2    Detloff, P.J.3    Albin, R.L.4
  • 113
    • 51349162486 scopus 로고    scopus 로고
    • Rodent genetic models of Huntington disease
    • Heng M. Y., Detloff P. J. Albin R. L. (2008) Rodent genetic models of Huntington disease. Neurobiol. Dis. 32, 1 9.
    • (2008) Neurobiol. Dis. , vol.32 , pp. 1-9
    • Heng, M.Y.1    Detloff, P.J.2    Albin, R.L.3
  • 114
    • 54549087605 scopus 로고    scopus 로고
    • Extensive early motor and non-motor behavioral deficits are followed by striatal neuronal loss in knock-in Huntington's disease mice
    • Hickey M. A., Kosmalska A., Enayati J., Cohen R., Zeitlin S., Levine M. S. Chesselet M. F. (2008) Extensive early motor and non-motor behavioral deficits are followed by striatal neuronal loss in knock-in Huntington's disease mice. Neuroscience 157, 280 295.
    • (2008) Neuroscience , vol.157 , pp. 280-295
    • Hickey, M.A.1    Kosmalska, A.2    Enayati, J.3    Cohen, R.4    Zeitlin, S.5    Levine, M.S.6    Chesselet, M.F.7
  • 115
    • 0030038266 scopus 로고    scopus 로고
    • Geranylgeranylacetone induces heat shock proteins in cultured guinea pig gastric mucosal cells and rat gastric mucosa
    • DOI 10.1053/gast.1996.v111.pm8690199
    • Hirakawa T., Rokutan K., Nikawa T. Kishi K. (1996) Geranylgeranylacetone induces heat shock proteins in cultured guinea pig gastric mucosal cells and rat gastric mucosa. Gastroenterology 111, 345 357. (Pubitemid 26256722)
    • (1996) Gastroenterology , vol.111 , Issue.2 , pp. 345-357
    • Hirakawa, T.1    Rokutan, K.2    Nikawa, T.3    Kishi, K.4
  • 117
    • 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. (2003) Suberoylanilide hydroxamic acid, a histone deacetylase inhibitor, ameliorates motor deficits in a mouse model of Huntington's disease. Proc. Natl Acad. Sci. USA 100, 2041 2046.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 2041-2046
    • Hockly, E.1    Richon, V.M.2    Woodman, B.3
  • 118
    • 29144498271 scopus 로고    scopus 로고
    • Evaluation of the benzothiazole aggregation inhibitors riluzole and PGL-135 as therapeutics for Huntington's disease
    • Hockly E., Tse J., Barker A. L. et al. (2006) Evaluation of the benzothiazole aggregation inhibitors riluzole and PGL-135 as therapeutics for Huntington's disease. Neurobiol. Dis. 21, 228 236.
    • (2006) Neurobiol. Dis. , vol.21 , pp. 228-236
    • Hockly, E.1    Tse, J.2    Barker, A.L.3
  • 119
    • 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. (1999) A YAC mouse model for Huntington's disease with full-length mutant huntingtin, cytoplasmic toxicity, and selective striatal neurodegeneration. Neuron 23, 181 192.
    • (1999) Neuron , vol.23 , pp. 181-192
    • Hodgson, J.G.1    Agopyan, N.2    Gutekunst, C.A.3
  • 120
    • 25644434918 scopus 로고    scopus 로고
    • Purification of neuronal inclusions of patients with Huntington's disease reveals a broad range of N-terminal fragments of expanded huntingtin and insoluble polymers
    • Hoffner G., Island M. L. Djian P. (2005) Purification of neuronal inclusions of patients with Huntington's disease reveals a broad range of N-terminal fragments of expanded huntingtin and insoluble polymers. J. Neurochem. 95, 125 136.
    • (2005) J. Neurochem. , vol.95 , pp. 125-136
    • Hoffner, G.1    Island, M.L.2    Djian, P.3
  • 122
    • 7144229376 scopus 로고    scopus 로고
    • Spinocerebellar ataxia type 7 (SCA7): A neurodegenerative disorder with neuronal intranuclear inclusions
    • Holmberg M., Duyckaerts C., Durr A. et al. (1998) Spinocerebellar ataxia type 7 (SCA7): a neurodegenerative disorder with neuronal intranuclear inclusions. Hum. Mol. Genet. 7, 913 918.
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 913-918
    • Holmberg, M.1    Duyckaerts, C.2    Durr, A.3
  • 123
    • 23044487281 scopus 로고    scopus 로고
    • Dynamic regulation of molecular chaperone gene expression in polyglutamine disease
    • Huen N. Y. Chan H. Y. (2005) Dynamic regulation of molecular chaperone gene expression in polyglutamine disease. Biochem. Biophys. Res. Commun. 334, 1074 1084.
    • (2005) Biochem. Biophys. Res. Commun. , vol.334 , pp. 1074-1084
    • Huen, N.Y.1    Chan, H.Y.2
  • 124
    • 0035047651 scopus 로고    scopus 로고
    • Therapeutic opportunities in polyglutamine disease
    • Hughes R. E. Olson J. M. (2001) Therapeutic opportunities in polyglutamine disease. Nat. Med. 7, 419 423.
    • (2001) Nat. Med. , vol.7 , pp. 419-423
    • Hughes, R.E.1    Olson, J.M.2
  • 126
    • 85009226418 scopus 로고    scopus 로고
    • A randomized, placebo-controlled trial of coenzyme Q10 and remacemide in Huntington's disease
    • Huntington Study Group
    • Huntington Study Group (2001) A randomized, placebo-controlled trial of coenzyme Q10 and remacemide in Huntington's disease. Neurology 57, 397 404.
    • (2001) Neurology , vol.57 , pp. 397-404
  • 127
    • 0033044001 scopus 로고    scopus 로고
    • Expression of ataxin-2 in brains from normal individuals and patients with Alzheimer's disease and spinocerebellar ataxia 2
    • Huynh D. P., Del Bigio M. R., Ho D. H. Pulst S. M. (1999) Expression of ataxin-2 in brains from normal individuals and patients with Alzheimer's disease and spinocerebellar ataxia 2. Ann. Neurol. 45, 232 241.
    • (1999) Ann. Neurol. , vol.45 , pp. 232-241
    • Huynh, D.P.1    Del Bigio, M.R.2    Ho, D.H.3    Pulst, S.M.4
  • 128
    • 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 D. P., Figueroa K., Hoang N. Pulst S. M. (2000) Nuclear localization or inclusion body formation of ataxin-2 are not necessary for SCA2 pathogenesis in mouse or human. Nat. Genet. 26, 44 50.
    • (2000) Nat. Genet. , vol.26 , pp. 44-50
    • Huynh, D.P.1    Figueroa, K.2    Hoang, N.3    Pulst, S.M.4
  • 129
    • 0037767510 scopus 로고    scopus 로고
    • Expansion of the polyQ repeat in ataxin-2 alters its Golgi localization, disrupts the Golgi complex and causes cell death
    • Huynh D. P., Yang H. T., Vakharia H., Nguyen D. Pulst S. M. (2003) Expansion of the polyQ repeat in ataxin-2 alters its Golgi localization, disrupts the Golgi complex and causes cell death. Hum. Mol. Genet. 12, 1485 1496.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 1485-1496
    • Huynh, D.P.1    Yang, H.T.2    Vakharia, H.3    Nguyen, D.4    Pulst, S.M.5
  • 130
    • 17344362229 scopus 로고    scopus 로고
    • Suppression of aggregate formation and apoptosis by transglutaminase inhibitors in cells expressing truncated DRPLA protein with an expanded polyglutamine stretch
    • Igarashi S., Koide R., Shimohata T. et al. (1998) Suppression of aggregate formation and apoptosis by transglutaminase inhibitors in cells expressing truncated DRPLA protein with an expanded polyglutamine stretch. Nat. Genet. 18, 111 117.
    • (1998) Nat. Genet. , vol.18 , pp. 111-117
    • Igarashi, S.1    Koide, R.2    Shimohata, T.3
  • 131
    • 0030058208 scopus 로고    scopus 로고
    • Expanded polyglutamine in the Machado-Joseph disease protein induces cell death in vitro and in vivo
    • DOI 10.1038/ng0696-196
    • Ikeda H., Yamaguchi M., Sugai S., Aze Y., Narumiya S. Kakizuka A. (1996) Expanded polyglutamine in the Machado-Joseph disease protein induces cell death in vitro and in vivo. Nat. Genet. 13, 196 202. (Pubitemid 26000440)
    • (1996) Nature Genetics , vol.13 , Issue.2 , pp. 196-202
    • Ikeda, H.1    Yamaguchi, M.2    Sugai, S.3    Aze, Y.4    Narumiya, S.5    Kakizuka, A.6
  • 132
    • 0035854652 scopus 로고    scopus 로고
    • HSP-CBF is an NF-Y-dependent coactivator of the heat shock promoters CCAAT boxes
    • Imbriano C., Bolognese F., Gurtner A., Piaggio G. Mantovani R. (2001) HSP-CBF is an NF-Y-dependent coactivator of the heat shock promoters CCAAT boxes. J. Biol. Chem. 276, 26332 26339.
    • (2001) J. Biol. Chem. , vol.276 , pp. 26332-26339
    • Imbriano, C.1    Bolognese, F.2    Gurtner, A.3    Piaggio, G.4    Mantovani, R.5
  • 133
    • 0042591262 scopus 로고    scopus 로고
    • Hsp105alpha suppresses the aggregation of truncated androgen receptor with expanded CAG repeats and cell toxicity
    • Ishihara K., Yamagishi N., Saito Y., Adachi H., Kobayashi Y., Sobue G., Ohtsuka K. Hatayama T. (2003) Hsp105alpha suppresses the aggregation of truncated androgen receptor with expanded CAG repeats and cell toxicity. J. Biol. Chem. 278, 25143 25150.
    • (2003) J. Biol. Chem. , vol.278 , pp. 25143-25150
    • Ishihara, K.1    Yamagishi, N.2    Saito, Y.3    Adachi, H.4    Kobayashi, Y.5    Sobue, G.6    Ohtsuka, K.7    Hatayama, T.8
  • 134
    • 0032769095 scopus 로고    scopus 로고
    • Abundant expression and cytoplasmic aggregations of [alpha]1A voltage-dependent calcium channel protein associated with neurodegeneration in spinocerebellar ataxia type 6
    • Ishikawa K., Fujigasaki H., Saegusa H. et al. (1999) Abundant expression and cytoplasmic aggregations of [alpha]1A voltage-dependent calcium channel protein associated with neurodegeneration in spinocerebellar ataxia type 6. Hum. Mol. Genet. 8, 1185 1193.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 1185-1193
    • Ishikawa, K.1    Fujigasaki, H.2    Saegusa, H.3
  • 135
    • 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. Nukina N. (2000) 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. 9, 2009 2018.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2009-2018
    • Jana, N.R.1    Tanaka, M.2    Wang, G.3    Nukina, N.4
  • 136
    • 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. Nukina N. (2001) Altered proteasomal function due to the expression of polyglutamine-expanded truncated N-terminal huntingtin induces apoptosis by caspase activation through mitochondrial cytochrome c release. Hum. Mol. Genet. 10, 1049 1059.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1049-1059
    • Jana, N.R.1    Zemskov, E.A.2    Wang, G.3    Nukina, N.4
  • 137
    • 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., Kotliarova S., Murata S., Tanaka K. Nukina N. (2005) Co-chaperone CHIP associates with expanded polyglutamine protein and promotes their degradation by proteasomes. J. Biol. Chem. 280, 11635 11640.
    • (2005) J. Biol. Chem. , vol.280 , pp. 11635-11640
    • Jana, N.R.1    Dikshit, P.2    Goswami, A.3    Kotliarova, S.4    Murata, S.5    Tanaka, K.6    Nukina, N.7
  • 138
    • 0031726082 scopus 로고    scopus 로고
    • Spinocerebellar ataxia type 6 with positional vertigo and acetazolamide responsive episodic ataxia
    • Jen J. C., Yue Q., Karrim J., Nelson S. F. Baloh R. W. (1998) Spinocerebellar ataxia type 6 with positional vertigo and acetazolamide responsive episodic ataxia. J. Neurol. Neurosurg. Psychiatry 65, 565 568.
    • (1998) J. Neurol. Neurosurg. Psychiatry , vol.65 , pp. 565-568
    • Jen, J.C.1    Yue, Q.2    Karrim, J.3    Nelson, S.F.4    Baloh, R.W.5
  • 139
    • 0035900793 scopus 로고    scopus 로고
    • CHIP is a U-box-dependent E3 ubiquitin ligase: Identification of Hsc70 as a target for ubiquitylation
    • Jiang J., Ballinger C. A., Wu Y., Dai Q., Cyr D. M., Hohfeld J. Patterson C. (2001) CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation. J. Biol. Chem. 276, 42938 42944.
    • (2001) J. Biol. Chem. , vol.276 , pp. 42938-42944
    • Jiang, J.1    Ballinger, C.A.2    Wu, Y.3    Dai, Q.4    Cyr, D.M.5    Hohfeld, J.6    Patterson, C.7
  • 140
    • 67649500192 scopus 로고    scopus 로고
    • Phosphorylation of ATXN1 at Ser776 in the cerebellum
    • Jorgensen N. D., Andresen J. M., Lagalwar S. et al. (2009) Phosphorylation of ATXN1 at Ser776 in the cerebellum. J. Neurochem. 110, 675 686.
    • (2009) J. Neurochem. , vol.110 , pp. 675-686
    • Jorgensen, N.D.1    Andresen, J.M.2    Lagalwar, S.3
  • 141
    • 0029856046 scopus 로고    scopus 로고
    • Peptides containing glutamine repeats as substrates for transglutaminase-catalyzed cross-linking: Relevance to diseases of the nervous system
    • Kahlem P., Terre C., Green H. Djian P. (1996) Peptides containing glutamine repeats as substrates for transglutaminase-catalyzed cross-linking: relevance to diseases of the nervous system. Proc. Natl Acad. Sci. USA 93, 14580 14585.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 14580-14585
    • Kahlem, P.1    Terre, C.2    Green, H.3    Djian, P.4
  • 142
    • 0032014092 scopus 로고    scopus 로고
    • Transglutaminase action imitates Huntington's disease: Selective polymerization of Huntingtin containing expanded polyglutamine
    • Kahlem P., Green H. Djian P. (1998) Transglutaminase action imitates Huntington's disease: selective polymerization of Huntingtin containing expanded polyglutamine. Mol. Cell 1, 595 601.
    • (1998) Mol. Cell , vol.1 , pp. 595-601
    • Kahlem, P.1    Green, H.2    Djian, P.3
  • 143
    • 22244459510 scopus 로고    scopus 로고
    • Humanin attenuates apoptosis induced by DRPLA proteins with expanded polyglutamine stretches
    • Kariya S., Hirano M., Nagai Y., Furiya Y., Fujikake N., Toda T. Ueno S. (2005) Humanin attenuates apoptosis induced by DRPLA proteins with expanded polyglutamine stretches. J. Mol. Neurosci. 25, 165 169.
    • (2005) J. Mol. Neurosci. , vol.25 , pp. 165-169
    • Kariya, S.1    Hirano, M.2    Nagai, Y.3    Furiya, Y.4    Fujikake, N.5    Toda, T.6    Ueno, S.7
  • 144
    • 0033594894 scopus 로고    scopus 로고
    • Transglutaminase aggregates huntingtin into nonamyloidogenic polymers, and its enzymatic activity increases in Huntington's disease brain nuclei
    • Karpuj M. V., Garren H., Slunt H., Price D. L., Gusella J., Becher M. W. Steinman L. (1999) Transglutaminase aggregates huntingtin into nonamyloidogenic polymers, and its enzymatic activity increases in Huntington's disease brain nuclei. Proc. Natl Acad. Sci. USA 96, 7388 7393.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 7388-7393
    • Karpuj, M.V.1    Garren, H.2    Slunt, H.3    Price, D.L.4    Gusella, J.5    Becher, M.W.6    Steinman, L.7
  • 145
    • 0036172346 scopus 로고    scopus 로고
    • Prolonged survival and decreased abnormal movements in transgenic model of Huntington disease, with administration of the transglutaminase inhibitor cystamine
    • Karpuj M. V., Becher M. W., Springer J. E., Chabas D., Youssef S., Pedotti R., Mitchell D. Steinman L. (2002) Prolonged survival and decreased abnormal movements in transgenic model of Huntington disease, with administration of the transglutaminase inhibitor cystamine. Nat. Med. 8, 143 149.
    • (2002) Nat. Med. , vol.8 , pp. 143-149
    • Karpuj, M.V.1    Becher, M.W.2    Springer, J.E.3    Chabas, D.4    Youssef, S.5    Pedotti, R.6    Mitchell, D.7    Steinman, L.8
  • 146
    • 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. et al. (2002) Testosterone reduction prevents phenotypic expression in a transgenic mouse model of spinal and bulbar muscular atrophy. Neuron 35, 843 854.
    • (2002) Neuron , vol.35 , pp. 843-854
    • Katsuno, M.1    Adachi, H.2    Kume, A.3
  • 147
    • 0038714285 scopus 로고    scopus 로고
    • Leuprorelin rescues polyglutamine-dependent phenotypes in a transgenic mouse model of spinal and bulbar muscular atrophy
    • Katsuno M., Adachi H., Doyu M., Minamiyama M., Sang C., Kobayashi Y., Inukai A. Sobue G. (2003) Leuprorelin rescues polyglutamine-dependent phenotypes in a transgenic mouse model of spinal and bulbar muscular atrophy. Nat. Med. 9, 768 773.
    • (2003) Nat. Med. , vol.9 , pp. 768-773
    • Katsuno, M.1    Adachi, H.2    Doyu, M.3    Minamiyama, M.4    Sang, C.5    Kobayashi, Y.6    Inukai, A.7    Sobue, G.8
  • 150
    • 0034629073 scopus 로고    scopus 로고
    • Genetic suppression of polyglutamine toxicity in Drosophila
    • Kazemi-Esfarjani P. Benzer S. (2000) Genetic suppression of polyglutamine toxicity in Drosophila. Science 287, 1837 1840.
    • (2000) Science , vol.287 , pp. 1837-1840
    • Kazemi-Esfarjani, P.1    Benzer, S.2
  • 151
    • 27744510791 scopus 로고    scopus 로고
    • Huntingtin associates with acidic phospholipids at the plasma membrane
    • Kegel K. B., Sapp E., Yoder J. et al. (2005) Huntingtin associates with acidic phospholipids at the plasma membrane. J. Biol. Chem. 280, 36464 36473.
    • (2005) J. Biol. Chem. , vol.280 , pp. 36464-36473
    • Kegel, K.B.1    Sapp, E.2    Yoder, J.3
  • 152
    • 33746487396 scopus 로고    scopus 로고
    • Expanded polyglutamines impair synaptic transmission and ubiquitin-proteasome system in Caenorhabditis elegans
    • Khan L. A., Bauer P. O., Miyazaki H., Lindenberg K. S., Landwehrmeyer B. G. Nukina N. (2006) Expanded polyglutamines impair synaptic transmission and ubiquitin-proteasome system in Caenorhabditis elegans. J. Neurochem. 98, 576 587.
    • (2006) J. Neurochem. , vol.98 , pp. 576-587
    • Khan, L.A.1    Bauer, P.O.2    Miyazaki, H.3    Lindenberg, K.S.4    Landwehrmeyer, B.G.5    Nukina, N.6
  • 153
    • 0032475941 scopus 로고    scopus 로고
    • Ataxin-1 nuclear localization and aggregation: Role in polyglutamine-induced disease in SCA1 transgenic mice
    • Klement I. A., Skinner P. J., Kaytor M. D., Yi H., Hersch S. M., Clark H. B., Zoghbi H. Y. Orr H. T. (1998) Ataxin-1 nuclear localization and aggregation: role in polyglutamine-induced disease in SCA1 transgenic mice. Cell 95, 41 53.
    • (1998) Cell , vol.95 , 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    Zoghbi, H.Y.7    Orr, H.T.8
  • 154
    • 0034708793 scopus 로고    scopus 로고
    • Chaperones Hsp70 and Hsp40 suppress aggregate formation and apoptosis in cultured neuronal cells expressing truncated androgen receptor protein with expanded polyglutamine tract
    • Kobayashi Y., Kume A., Li M., Doyu M., Hata M., Ohtsuka K. Sobue G. (2000) Chaperones Hsp70 and Hsp40 suppress aggregate formation and apoptosis in cultured neuronal cells expressing truncated androgen receptor protein with expanded polyglutamine tract. J. Biol. Chem. 275, 8772 8778.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8772-8778
    • Kobayashi, Y.1    Kume, A.2    Li, M.3    Doyu, M.4    Hata, M.5    Ohtsuka, K.6    Sobue, G.7
  • 155
    • 20944451721 scopus 로고    scopus 로고
    • Decreased expression of hypothalamic neuropeptides in Huntington disease transgenic mice with expanded polyglutamine-EGFP fluorescent aggregates
    • Kotliarova S., Jana N. R., Sakamoto N. et al. (2005) Decreased expression of hypothalamic neuropeptides in Huntington disease transgenic mice with expanded polyglutamine-EGFP fluorescent aggregates. J. Neurochem. 93, 641 653.
    • (2005) J. Neurochem. , vol.93 , pp. 641-653
    • Kotliarova, S.1    Jana, N.R.2    Sakamoto, N.3
  • 156
    • 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. (1999) Neuronal intranuclear inclusions in spinocerebellar ataxia type 2: triple-labeling immunofluorescent study. Neurosci. Lett. 273, 117 120.
    • (1999) Neurosci. Lett. , vol.273 , pp. 117-120
    • Koyano, S.1    Uchihara, T.2    Fujigasaki, H.3    Nakamura, A.4    Yagishita, S.5    Iwabuchi, K.6
  • 157
    • 0036786139 scopus 로고    scopus 로고
    • Paradoxical absence of nuclear inclusion in cerebellar Purkinje cells of hereditary ataxias linked to CAG expansion
    • Koyano S., Iwabuchi K., Yagishita S., Kuroiwa Y. Uchihara T. (2002) Paradoxical absence of nuclear inclusion in cerebellar Purkinje cells of hereditary ataxias linked to CAG expansion. J. Neurol. Neurosurg. Psychiatry 73, 450 452.
    • (2002) J. Neurol. Neurosurg. Psychiatry , vol.73 , pp. 450-452
    • Koyano, S.1    Iwabuchi, K.2    Yagishita, S.3    Kuroiwa, Y.4    Uchihara, T.5
  • 158
    • 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. (2007) 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. 16, 1845 1861.
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 1845-1861
    • Kuhn, A.1    Goldstein, D.R.2    Hodges, A.3
  • 159
    • 61349156118 scopus 로고    scopus 로고
    • Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis
    • Kwiatkowski T. J. Jr., Bosco D. A., Leclerc A. L. et al. (2009) Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis. Science 323, 1205 1208.
    • (2009) Science , vol.323 , pp. 1205-1208
    • Kwiatkowski, Jr.T.J.1    Bosco, D.A.2    Leclerc, A.L.3
  • 160
    • 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., Harding A. E. Fischbeck K. H. (1991) Androgen receptor gene mutations in X-linked spinal and bulbar muscular atrophy. Nature 352, 77 79.
    • (1991) Nature , vol.352 , pp. 77-79
    • La Spada, A.R.1    Wilson, E.M.2    Lubahn, D.B.3    Harding, A.E.4    Fischbeck, K.H.5
  • 161
    • 17944370599 scopus 로고    scopus 로고
    • Polyglutamine-expanded ataxin-7 antagonizes CRX function and induces cone-rod dystrophy in a mouse model of SCA7
    • La Spada A. R., Fu Y. H., Sopher B. L. et al. (2001) Polyglutamine- expanded ataxin-7 antagonizes CRX function and induces cone-rod dystrophy in a mouse model of SCA7. Neuron 31, 913 927.
    • (2001) Neuron , vol.31 , pp. 913-927
    • La Spada, A.R.1    Fu, Y.H.2    Sopher, B.L.3
  • 162
    • 0041816369 scopus 로고    scopus 로고
    • Kennedy's disease. Phosphorylation of the polyglutamine-expanded form of androgen receptor regulates its cleavage by caspase-3 and enhances cell death
    • LaFevre-Bernt M. A. Ellerby L. M. (2003) Kennedy's disease. Phosphorylation of the polyglutamine-expanded form of androgen receptor regulates its cleavage by caspase-3 and enhances cell death. J. Biol. Chem. 278, 34918 34924.
    • (2003) J. Biol. Chem. , vol.278 , pp. 34918-34924
    • Lafevre-Bernt, M.A.1    Ellerby, L.M.2
  • 163
    • 27644489210 scopus 로고    scopus 로고
    • Rho-kinase inhibition in the therapy of cardiovascular disease
    • Lai A. Frishman W. H. (2005) Rho-kinase inhibition in the therapy of cardiovascular disease. Cardiol. Rev. 13, 285 292.
    • (2005) Cardiol. Rev. , vol.13 , pp. 285-292
    • Lai, A.1    Frishman, W.H.2
  • 164
    • 34948838383 scopus 로고    scopus 로고
    • Riluzole in Huntington's disease: A 3-year, randomized controlled study
    • Landwehrmeyer G. B., Dubois B., de Yebenes J. G. et al. (2007) Riluzole in Huntington's disease: a 3-year, randomized controlled study. Ann. Neurol. 62, 262 272.
    • (2007) Ann. Neurol. , vol.62 , pp. 262-272
    • Landwehrmeyer, G.B.1    Dubois, B.2    De Yebenes, J.G.3
  • 165
  • 166
    • 52949137369 scopus 로고    scopus 로고
    • MiR-19, miR-101 and miR-130 co-regulate ATXN1 levels to potentially modulate SCA1 pathogenesis
    • Lee Y., Samaco R. C., Gatchel J. R., Thaller C., Orr H. T. Zoghbi H. Y. (2008) miR-19, miR-101 and miR-130 co-regulate ATXN1 levels to potentially modulate SCA1 pathogenesis. Nat. Neurosci. 11, 1137 1139.
    • (2008) Nat. Neurosci. , vol.11 , pp. 1137-1139
    • Lee, Y.1    Samaco, R.C.2    Gatchel, J.R.3    Thaller, C.4    Orr, H.T.5    Zoghbi, H.Y.6
  • 167
    • 0037423204 scopus 로고    scopus 로고
    • Cystamine inhibits caspase activity. Implications for the treatment of polyglutamine disorders
    • Lesort M., Lee M., Tucholski J. Johnson G. V. (2003) Cystamine inhibits caspase activity. Implications for the treatment of polyglutamine disorders. J. Biol. Chem. 278, 3825 3830.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3825-3830
    • Lesort, M.1    Lee, M.2    Tucholski, J.3    Johnson, G.V.4
  • 168
    • 0033571743 scopus 로고    scopus 로고
    • Enhanced sensitivity to N-methyl-D-aspartate receptor activation in transgenic and knockin mouse models of Huntington's disease
    • Levine M. S., Klapstein G. J., Koppel A. et al. (2002a) Enhanced sensitivity to N-methyl-D-aspartate receptor activation in transgenic and knockin mouse models of Huntington's disease. J. Neurosci. Res. 58, 515 532.
    • (2002) J. Neurosci. Res. , vol.58 , pp. 515-532
    • Levine, M.S.1    Klapstein, G.J.2    Koppel, A.3
  • 169
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P., Nijhawan D., Budihardjo I., Srinivasula S. M., Ahmad M., Alnemri E. S. Wang X 1997) Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 91, 479 489.
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 171
    • 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., Shelbourne P. F. Li X. J. (2000a) Amino-terminal fragments of mutant huntingtin show selective accumulation in striatal neurons and synaptic toxicity. Nat. Genet. 25, 385 389.
    • (2000) Nat. Genet. , vol.25 , pp. 385-389
    • Li, H.1    Li, S.H.2    Johnston, H.3    Shelbourne, P.F.4    Li, X.J.5
  • 172
    • 0034703874 scopus 로고    scopus 로고
    • Intranuclear huntingtin increases the expression of caspase-1 and induces apoptosis
    • Li S. H., Lam S., Cheng A. L. Li X. J. (2000b) Intranuclear huntingtin increases the expression of caspase-1 and induces apoptosis. Hum. Mol. Genet. 9, 2859 2867.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2859-2867
    • Li, S.H.1    Lam, S.2    Cheng, A.L.3    Li, X.J.4
  • 173
    • 0035503511 scopus 로고    scopus 로고
    • Huntingtin aggregate-associated axonal degeneration is an early pathological event in Huntington's disease mice
    • Li H., Li S. H., Yu Z. X., Shelbourne P. Li X. J. (2001) Huntingtin aggregate-associated axonal degeneration is an early pathological event in Huntington's disease mice. J. Neurosci. 21, 8473 8481.
    • (2001) J. Neurosci. , vol.21 , pp. 8473-8481
    • Li, H.1    Li, S.H.2    Yu, Z.X.3    Shelbourne, P.4    Li, X.J.5
  • 174
    • 0037160106 scopus 로고    scopus 로고
    • Ataxin-3 is a histone-binding protein with two independent transcriptional corepressor activities
    • Li F., Macfarlan T., Pittman R. N. Chakravarti D. (2002a) Ataxin-3 is a histone-binding protein with two independent transcriptional corepressor activities. J. Biol. Chem. 277, 45004 45012.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45004-45012
    • Li, F.1    MacFarlan, T.2    Pittman, R.N.3    Chakravarti, D.4
  • 175
    • 0036173896 scopus 로고    scopus 로고
    • Interaction of Huntington disease protein with transcriptional activator Sp1
    • Li S. H., Cheng A. L., Zhou H., Lam S., Rao M., Li H. Li X. J. (2002b) Interaction of Huntington disease protein with transcriptional activator Sp1. Mol. Cell. Biol. 22, 1277 1287.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1277-1287
    • Li, S.H.1    Cheng, A.L.2    Zhou, H.3    Lam, S.4    Rao, M.5    Li, H.6    Li, X.J.7
  • 176
    • 0042921188 scopus 로고    scopus 로고
    • Abnormal association of mutant huntingtin with synaptic vesicles inhibits glutamate release
    • Li H., Wyman T., Yu Z. X., Li S. H. Li X. J. (2003) Abnormal association of mutant huntingtin with synaptic vesicles inhibits glutamate release. Hum. Mol. Genet. 12, 2021 2030.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 2021-2030
    • Li, H.1    Wyman, T.2    Yu, Z.X.3    Li, S.H.4    Li, X.J.5
  • 177
    • 26844498655 scopus 로고    scopus 로고
    • The use of the R6 transgenic mouse models of Huntington's disease in attempts to develop novel therapeutic strategies
    • Li J. Y., Popovic N. Brundin P. (2005) The use of the R6 transgenic mouse models of Huntington's disease in attempts to develop novel therapeutic strategies. NeuroRx 2, 447 464.
    • (2005) NeuroRx , vol.2 , pp. 447-464
    • Li, J.Y.1    Popovic, N.2    Brundin, P.3
  • 178
    • 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. (2001) Neurological abnormalities in a knock-in mouse model of Huntington's disease. Hum. Mol. Genet. 10, 137 144.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 137-144
    • Lin, C.H.1    Tallaksen-Greene, S.2    Chien, W.M.3
  • 180
    • 0031680014 scopus 로고    scopus 로고
    • A cellular model that recapitulates major pathogenic steps of Huntington's disease
    • Lunkes A. Mandel J. L. (1998) A cellular model that recapitulates major pathogenic steps of Huntington's disease. Hum. Mol. Genet. 7, 1355 1361.
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 1355-1361
    • Lunkes, A.1    Mandel, J.L.2
  • 182
    • 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., Weber C., Devys D., Landwehrmeyer G. B., Mandel J. L. Trottier Y. (2002) Proteases acting on mutant huntingtin generate cleaved products that differentially build up cytoplasmic and nuclear inclusions. Mol. Cell 10, 259 269.
    • (2002) Mol. Cell , vol.10 , pp. 259-269
    • Lunkes, A.1    Lindenberg, K.S.2    Ben-Haiem, L.3    Weber, C.4    Devys, D.5    Landwehrmeyer, G.B.6    Mandel, J.L.7    Trottier, Y.8
  • 183
    • 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. Rubinsztein D. C. (2005) Cdk5 phosphorylation of huntingtin reduces its cleavage by caspases: implications for mutant huntingtin toxicity. J. Cell Biol. 169, 647 656.
    • (2005) J. Cell Biol. , vol.169 , pp. 647-656
    • Luo, S.1    Vacher, C.2    Davies, J.E.3    Rubinsztein, D.C.4
  • 184
    • 0037101837 scopus 로고    scopus 로고
    • Polyglutamine and transcription: Gene expression changes shared by DRPLA and Huntington's disease mouse models reveal context-independent effects
    • Luthi-Carter R., Strand A. D., Hanson S. A. et al. (2002) Polyglutamine and transcription: gene expression changes shared by DRPLA and Huntington's disease mouse models reveal context-independent effects. Hum. Mol. Genet. 11, 1927 1937.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1927-1937
    • Luthi-Carter, R.1    Strand, A.D.2    Hanson, S.A.3
  • 185
    • 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. (1996) Exon 1 of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice. Cell 87, 493 506.
    • (1996) Cell , vol.87 , pp. 493-506
    • Mangiarini, L.1    Sathasivam, K.2    Seller, M.3
  • 186
    • 18444411305 scopus 로고    scopus 로고
    • Childhood-onset ataxia: Testing for large CAG-repeats in SCA2 and SCA7
    • Mao R., Aylsworth A. S., Potter N. et al. (2002) Childhood-onset ataxia: testing for large CAG-repeats in SCA2 and SCA7. Am. J. Med. Genet. 110, 338 345.
    • (2002) Am. J. Med. Genet. , vol.110 , pp. 338-345
    • Mao, R.1    Aylsworth, A.S.2    Potter, N.3
  • 187
    • 65549148646 scopus 로고    scopus 로고
    • Animal models of polyglutamine diseases and therapeutic approaches
    • Marsh J. L., Lukacsovich T. Thompson L. M. (2009) Animal models of polyglutamine diseases and therapeutic approaches. J. Biol. Chem. 284, 7431 7435.
    • (2009) J. Biol. Chem. , vol.284 , pp. 7431-7435
    • Marsh, J.L.1    Lukacsovich, T.2    Thompson, L.M.3
  • 188
    • 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. (1998) Length of huntingtin and its polyglutamine tract influences localization and frequency of intracellular aggregates. Nat. Genet. 18, 150 154.
    • (1998) Nat. Genet. , vol.18 , pp. 150-154
    • Martindale, D.1    Hackam, A.2    Wieczorek, A.3
  • 189
    • 8544260320 scopus 로고    scopus 로고
    • Characterization of the structure and the amyloidogenic properties of the Josephin domain of the polyglutamine-containing protein ataxin-3
    • Masino L., Nicastro G., Menon R. P., Dal Piaz F., Calder L. Pastore A. (2004) Characterization of the structure and the amyloidogenic properties of the Josephin domain of the polyglutamine-containing protein ataxin-3. J. Mol. Biol. 344, 1021 1035.
    • (2004) J. Mol. Biol. , vol.344 , pp. 1021-1035
    • Masino, L.1    Nicastro, G.2    Menon, R.P.3    Dal Piaz, F.4    Calder, L.5    Pastore, A.6
  • 190
    • 17844367134 scopus 로고    scopus 로고
    • The Anp32 family of proteins containing leucine-rich repeats
    • Matilla A. Radrizzani M. (2005) The Anp32 family of proteins containing leucine-rich repeats. Cerebellum 4, 7 18.
    • (2005) Cerebellum , vol.4 , pp. 7-18
    • Matilla, A.1    Radrizzani, M.2
  • 191
    • 0030716768 scopus 로고    scopus 로고
    • The cerebellar leucine-rich acidic nuclear protein interacts with ataxin-1
    • Matilla A., Koshy B. T., Cummings C. J., Isobe T., Orr H. T. Zoghbi H. Y. (1997) The cerebellar leucine-rich acidic nuclear protein interacts with ataxin-1. Nature 389, 974 978.
    • (1997) Nature , vol.389 , pp. 974-978
    • Matilla, A.1    Koshy, B.T.2    Cummings, C.J.3    Isobe, T.4    Orr, H.T.5    Zoghbi, H.Y.6
  • 192
    • 0035891863 scopus 로고    scopus 로고
    • Association of ataxin-7 with the proteasome subunit S4 of the 19S regulatory complex
    • Matilla A., Gorbea C., Einum D. D. et al. (2001) Association of ataxin-7 with the proteasome subunit S4 of the 19S regulatory complex. Hum. Mol. Genet. 10, 2821 2831.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 2821-2831
    • Matilla, A.1    Gorbea, C.2    Einum, D.D.3
  • 194
    • 0034285017 scopus 로고    scopus 로고
    • CREB-binding protein sequestration by expanded polyglutamine
    • McCampbell A., Taylor J. P., Taye A. A. et al. (2000) CREB-binding protein sequestration by expanded polyglutamine. Hum. Mol. Genet. 9, 2197 2202.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2197-2202
    • McCampbell, A.1    Taylor, J.P.2    Taye, A.A.3
  • 195
    • 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., Olivieri M., Li X. J., Li H., Zeitlin S. Chesselet M. F. (2002) Early motor dysfunction and striosomal distribution of huntingtin microaggregates in Huntington's disease knock-in mice. J. Neurosci. 22, 8266 8276.
    • (2002) J. Neurosci. , vol.22 , pp. 8266-8276
    • Menalled, L.B.1    Sison, J.D.2    Wu, Y.3    Olivieri, M.4    Li, X.J.5    Li, H.6    Zeitlin, S.7    Chesselet, M.F.8
  • 196
    • 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., Zeitlin S. Chesselet M. F. (2003) 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. 465, 11 26.
    • (2003) J. Comp. Neurol. , vol.465 , pp. 11-26
    • Menalled, L.B.1    Sison, J.D.2    Dragatsis, I.3    Zeitlin, S.4    Chesselet, M.F.5
  • 197
    • 0038269098 scopus 로고    scopus 로고
    • Polyglutamine expansion induces a protein-damaging stress connecting heat shock protein 70 to the JNK pathway
    • Merienne K., Helmlinger D., Perkin G. R., Devys D. Trottier Y. (2003) Polyglutamine expansion induces a protein-damaging stress connecting heat shock protein 70 to the JNK pathway. J. Biol. Chem. 278, 16957 16967.
    • (2003) J. Biol. Chem. , vol.278 , pp. 16957-16967
    • Merienne, K.1    Helmlinger, D.2    Perkin, G.R.3    Devys, D.4    Trottier, Y.5
  • 198
    • 0031948607 scopus 로고    scopus 로고
    • Cleavage, aggregation and toxicity of the expanded androgen receptor in spinal and bulbar muscular atrophy
    • DOI 10.1093/hmg/7.4.693
    • Merry D. E., Kobayashi Y., Bailey C. K., Taye A. A. Fischbeck K. H. (1998) Cleavage, aggregation and toxicity of the expanded androgen receptor in spinal and bulbar muscular atrophy. Hum. Mol. Genet. 7, 693 701. (Pubitemid 28152269)
    • (1998) Human Molecular Genetics , vol.7 , Issue.4 , pp. 693-701
    • Merry, D.E.1    Kobayashi, Y.2    Bailey, C.K.3    Taye, A.A.4    Fischbeck, K.H.5
  • 199
    • 24744444740 scopus 로고    scopus 로고
    • Mitochondrial respiration and ATP production are significantly impaired in striatal cells expressing mutant huntingtin
    • Milakovic T. Johnson G. V. (2005) Mitochondrial respiration and ATP production are significantly impaired in striatal cells expressing mutant huntingtin. J. Biol. Chem. 280, 30773 30782.
    • (2005) J. Biol. Chem. , vol.280 , pp. 30773-30782
    • Milakovic, T.1    Johnson, G.V.2
  • 201
    • 2942733520 scopus 로고    scopus 로고
    • Sodium butyrate ameliorates phenotypic expression in a transgenic mouse model of spinal and bulbar muscular atrophy
    • Minamiyama M., Katsuno M., Adachi H. et al. (2004) Sodium butyrate ameliorates phenotypic expression in a transgenic mouse model of spinal and bulbar muscular atrophy. Hum. Mol. Genet. 13, 1183 1192.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 1183-1192
    • Minamiyama, M.1    Katsuno, M.2    Adachi, H.3
  • 202
    • 0036848793 scopus 로고    scopus 로고
    • Purification of polyglutamine aggregates and identification of elongation factor-1alpha and heat shock protein 84 as aggregate-interacting proteins
    • Mitsui K., Nakayama H., Akagi T., Nekooki M., Ohtawa K., Takio K., Hashikawa T. Nukina N. (2002) Purification of polyglutamine aggregates and identification of elongation factor-1alpha and heat shock protein 84 as aggregate-interacting proteins. J. Neurosci. 22, 9267 9277.
    • (2002) J. Neurosci. , vol.22 , pp. 9267-9277
    • Mitsui, K.1    Nakayama, H.2    Akagi, T.3    Nekooki, M.4    Ohtawa, K.5    Takio, K.6    Hashikawa, T.7    Nukina, N.8
  • 205
    • 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. (2006) Bidirectional expression of CUG and CAG expansion transcripts and intranuclear polyglutamine inclusions in spinocerebellar ataxia type 8. Nat. Genet. 38, 758 769.
    • (2006) Nat. Genet. , vol.38 , pp. 758-769
    • Moseley, M.L.1    Zu, T.2    Ikeda, Y.3
  • 206
    • 0037014426 scopus 로고    scopus 로고
    • Protein misfolding, amyloid formation, and neurodegeneration: A critical role for molecular chaperones?
    • Muchowski P. J. (2002) Protein misfolding, amyloid formation, and neurodegeneration: a critical role for molecular chaperones? Neuron 35, 9 12.
    • (2002) Neuron , vol.35 , pp. 9-12
    • Muchowski, P.J.1
  • 208
    • 68749103450 scopus 로고    scopus 로고
    • CK2-dependent phosphorylation determines cellular localization and stability of ataxin-3
    • Epub ahead of print, doi:.
    • Mueller T., Breuer P., Schmitt I., Evert B. O. Wullner U. (2009) CK2-dependent phosphorylation determines cellular localization and stability of ataxin-3. Hum. Mol. Genet. Epub ahead of print, doi:.
    • (2009) Hum. Mol. Genet.
    • Mueller, T.1    Breuer, P.2    Schmitt, I.3    Evert, B.O.4    Wullner, U.5
  • 209
    • 69249090927 scopus 로고    scopus 로고
    • SUMO modification of the androgen receptor attenuates polyglutamine-mediated aggregation
    • Mukherjee S., Thomas M., Dadgar N., Lieberman A. P. Iniguez-Lluhl J. A. (2009) SUMO modification of the androgen receptor attenuates polyglutamine-mediated aggregation. J. Biol. Chem. 284, 21296 21306.
    • (2009) J. Biol. Chem. , vol.284 , pp. 21296-21306
    • Mukherjee, S.1    Thomas, M.2    Dadgar, N.3    Lieberman, A.P.4    Iniguez-Lluhl, J.A.5
  • 211
    • 12444292683 scopus 로고    scopus 로고
    • Prevention of polyglutamine oligomerization and neurodegeneration by the peptide inhibitor QBP1 in Drosophila
    • Nagai Y., Fujikake N., Ohno K. et al. (2003) Prevention of polyglutamine oligomerization and neurodegeneration by the peptide inhibitor QBP1 in Drosophila. Hum. Mol. Genet. 12, 1253 1259.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 1253-1259
    • Nagai, Y.1    Fujikake, N.2    Ohno, K.3
  • 215
    • 23844482456 scopus 로고    scopus 로고
    • Clioquinol down-regulates mutant huntingtin expression in vitro and mitigates pathology in a Huntington's disease mouse model
    • Nguyen T., Hamby A. Massa S. M. (2005) Clioquinol down-regulates mutant huntingtin expression in vitro and mitigates pathology in a Huntington's disease mouse model. Proc. Natl Acad. Sci. USA 102, 11840 11845.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 11840-11845
    • Nguyen, T.1    Hamby, A.2    Massa, S.M.3
  • 216
    • 0036606540 scopus 로고    scopus 로고
    • ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats
    • Nishitoh H., Matsuzawa A., Tobiume K., Saegusa K., Takeda K., Inoue K., Hori S., Kakizuka A. Ichijo H. (2002) ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats. Genes Dev. 16, 1345 1355.
    • (2002) Genes Dev. , vol.16 , pp. 1345-1355
    • Nishitoh, H.1    Matsuzawa, A.2    Tobiume, K.3    Saegusa, K.4    Takeda, K.5    Inoue, K.6    Hori, S.7    Kakizuka, A.8    Ichijo, H.9
  • 217
    • 0035937523 scopus 로고    scopus 로고
    • Interference by huntingtin and atrophin-1 with cbp-mediated transcription leading to cellular toxicity
    • Nucifora F. C. Jr., Sasaki M., Peters M. F. et al. (2001) Interference by huntingtin and atrophin-1 with cbp-mediated transcription leading to cellular toxicity. Science 291, 2423 2428.
    • (2001) Science , vol.291 , pp. 2423-2428
    • Nucifora, Jr.F.C.1    Sasaki, M.2    Peters, M.F.3
  • 218
    • 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 F. C. Jr., Ellerby L. M., Wellington C. L. et al. (2003) Nuclear localization of a non-caspase truncation product of atrophin-1, with an expanded polyglutamine repeat, increases cellular toxicity. J. Biol. Chem. 278, 13047 13055.
    • (2003) J. Biol. Chem. , vol.278 , pp. 13047-13055
    • Nucifora, Jr.F.C.1    Ellerby, L.M.2    Wellington, C.L.3
  • 219
    • 0742287915 scopus 로고    scopus 로고
    • CRE-mediated transcription is increased in Huntington's disease transgenic mice
    • Obrietan K. Hoyt K. R. (2004) CRE-mediated transcription is increased in Huntington's disease transgenic mice. J. Neurosci. 24, 791 796.
    • (2004) J. Neurosci. , vol.24 , pp. 791-796
    • Obrietan, K.1    Hoyt, K.R.2
  • 221
    • 0042869974 scopus 로고    scopus 로고
    • Polyglutamine diseases: A transcription disorder?
    • Okazawa H. (2003) Polyglutamine diseases: a transcription disorder? Cell. Mol. Life Sci. 60, 1427 1439.
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 1427-1439
    • Okazawa, H.1
  • 222
    • 18444403420 scopus 로고    scopus 로고
    • Interaction between mutant ataxin-1 and PQBP-1 affects transcription and cell death
    • Okazawa H., Rich T., Chang A. et al. (2002) Interaction between mutant ataxin-1 and PQBP-1 affects transcription and cell death. Neuron 34, 701 713.
    • (2002) Neuron , vol.34 , pp. 701-713
    • Okazawa, H.1    Rich, T.2    Chang, A.3
  • 223
    • 33947200596 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in Huntington's disease: The bioenergetics of isolated and in situ mitochondria from transgenic mice
    • Oliveira J. M., Jekabsons M. B., Chen S., Lin A., Rego A. C., Goncalves J., Ellerby L. M. Nicholls D. G. (2007) Mitochondrial dysfunction in Huntington's disease: the bioenergetics of isolated and in situ mitochondria from transgenic mice. J. Neurochem. 101, 241 249.
    • (2007) J. Neurochem. , vol.101 , pp. 241-249
    • Oliveira, J.M.1    Jekabsons, M.B.2    Chen, S.3    Lin, A.4    Rego, A.C.5    Goncalves, J.6    Ellerby, L.M.7    Nicholls, D.G.8
  • 224
    • 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. (1999) Inhibition of caspase-1 slows disease progression in a mouse model of Huntington's disease. Nature 399, 263 267.
    • (1999) Nature , vol.399 , pp. 263-267
    • Ona, V.O.1    Li, M.2    Vonsattel, J.P.3
  • 225
    • 0035959998 scopus 로고    scopus 로고
    • Qs in the nucleus
    • Orr H. T. (2001) Qs in the nucleus. Neuron 31, 875 876.
    • (2001) Neuron , vol.31 , pp. 875-876
    • Orr, H.T.1
  • 226
    • 40849147435 scopus 로고    scopus 로고
    • N-terminal mutant huntingtin associates with mitochondria and impairs mitochondrial trafficking
    • Orr A. L., Li S., Wang C. E. et al. (2008) N-terminal mutant huntingtin associates with mitochondria and impairs mitochondrial trafficking. J. Neurosci. 28, 2783 2792.
    • (2008) J. Neurosci. , vol.28 , pp. 2783-2792
    • Orr, A.L.1    Li, S.2    Wang, C.E.3
  • 227
    • 33746530608 scopus 로고    scopus 로고
    • Sodium channel beta4 subunit: Down-regulation and possible involvement in neuritic degeneration in Huntington's disease transgenic mice
    • Oyama F., Miyazaki H., Sakamoto N. et al. (2006) Sodium channel beta4 subunit: down-regulation and possible involvement in neuritic degeneration in Huntington's disease transgenic mice. J. Neurochem. 98, 518 529.
    • (2006) J. Neurochem. , vol.98 , pp. 518-529
    • Oyama, F.1    Miyazaki, H.2    Sakamoto, N.3
  • 230
    • 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., Aebischer P., Deglon N., Humbert S. Saudou F. (2006) Inhibition of calcineurin by FK506 protects against polyglutamine-huntingtin toxicity through an increase of huntingtin phosphorylation at S421. J. Neurosci. 26, 1635 1645.
    • (2006) J. Neurosci. , vol.26 , pp. 1635-1645
    • Pardo, R.1    Colin, E.2    Regulier, E.3    Aebischer, P.4    Deglon, N.5    Humbert, S.6    Saudou, F.7
  • 231
    • 4344568680 scopus 로고    scopus 로고
    • Genetic and pharmacological suppression of polyglutamine-dependent neuronal dysfunction in Caenorhabditis elegans
    • Parker J. A., Holbert S., Lambert E., Abderrahmane S. Neri C. (2004) Genetic and pharmacological suppression of polyglutamine-dependent neuronal dysfunction in Caenorhabditis elegans. J. Mol. Neurosci. 23, 61 68.
    • (2004) J. Mol. Neurosci. , vol.23 , pp. 61-68
    • Parker, J.A.1    Holbert, S.2    Lambert, E.3    Abderrahmane, S.4    Neri, C.5
  • 233
    • 0033071176 scopus 로고    scopus 로고
    • Protein fate in neurodegenerative proteinopathies: Polyglutamine diseases join the (mis)fold
    • Paulson H. L. (1999) Protein fate in neurodegenerative proteinopathies: polyglutamine diseases join the (mis)fold. Am. J. Hum. Genet. 64, 339 345.
    • (1999) Am. J. Hum. Genet. , vol.64 , pp. 339-345
    • Paulson, H.L.1
  • 234
    • 0034028473 scopus 로고    scopus 로고
    • Toward an understanding of polyglutamine neurodegeneration
    • Paulson H. L. (2000) Toward an understanding of polyglutamine neurodegeneration. Brain Pathol. 10, 293 299.
    • (2000) Brain Pathol. , vol.10 , pp. 293-299
    • Paulson, H.L.1
  • 235
    • 0030850412 scopus 로고    scopus 로고
    • Intranuclear inclusions of expanded polyglutamine protein in spinocerebellar ataxia type 3
    • Paulson H. L., Perez M. K., Trottier Y. et al. (1997) Intranuclear inclusions of expanded polyglutamine protein in spinocerebellar ataxia type 3. Neuron 19, 333 344.
    • (1997) Neuron , vol.19 , pp. 333-344
    • Paulson, H.L.1    Perez, M.K.2    Trottier, Y.3
  • 236
    • 39249084415 scopus 로고    scopus 로고
    • The antidepressant sertraline improves the phenotype, promotes neurogenesis and increases BDNF levels in the R6/2 Huntington's disease mouse model
    • Peng Q., Masuda N., Jiang M., Li Q., Zhao M., Ross C. A. Duan W. (2008) The antidepressant sertraline improves the phenotype, promotes neurogenesis and increases BDNF levels in the R6/2 Huntington's disease mouse model. Exp. Neurol. 210, 154 163.
    • (2008) Exp. Neurol. , vol.210 , pp. 154-163
    • Peng, Q.1    Masuda, N.2    Jiang, M.3    Li, Q.4    Zhao, M.5    Ross, C.A.6    Duan, W.7
  • 237
    • 0032517816 scopus 로고    scopus 로고
    • Recruitment and the role of nuclear localization in polyglutamine- mediated aggregation
    • Perez M. K., Paulson H. L., Pendse S. J., Saionz S. J., Bonini N. M. Pittman R. N. (1998) Recruitment and the role of nuclear localization in polyglutamine-mediated aggregation. J. Cell Biol. 143, 1457 1470.
    • (1998) J. Cell Biol. , vol.143 , 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
  • 238
    • 0028283985 scopus 로고
    • Glutamine repeats as polar zippers: Their possible role in inherited neurodegenerative diseases
    • Perutz M. F., Johnson T., Suzuki M. Finch J. T. (1994) Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases. Proc. Natl Acad. Sci. USA 91, 5355 5358.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 5355-5358
    • Perutz, M.F.1    Johnson, T.2    Suzuki, M.3    Finch, J.T.4
  • 239
    • 0037117499 scopus 로고    scopus 로고
    • Aggregation of proteins with expanded glutamine and alanine repeats of the glutamine-rich and asparagine-rich domains of Sup35 and of the amyloid beta-peptide of amyloid plaques
    • Perutz M. F., Pope B. J., Owen D., Wanker E. E. Scherzinger E. (2002) Aggregation of proteins with expanded glutamine and alanine repeats of the glutamine-rich and asparagine-rich domains of Sup35 and of the amyloid beta-peptide of amyloid plaques. Proc. Natl Acad. Sci. USA 99, 5596 5600.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 5596-5600
    • Perutz, M.F.1    Pope, B.J.2    Owen, D.3    Wanker, E.E.4    Scherzinger, E.5
  • 241
    • 67349159137 scopus 로고    scopus 로고
    • Five siRNAs targeting three SNPs may provide therapy for three-quarters of Huntington's disease patients
    • Pfister E. L., Kennington L., Straubhaar J. et al. (2009) Five siRNAs targeting three SNPs may provide therapy for three-quarters of Huntington's disease patients. Curr. Biol. 19, 774 778.
    • (2009) Curr. Biol. , vol.19 , pp. 774-778
    • Pfister, E.L.1    Kennington, L.2    Straubhaar, J.3
  • 242
    • 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. (2005) A structure-based analysis of huntingtin mutant polyglutamine aggregation and toxicity: evidence for a compact beta-sheet structure. Hum. Mol. Genet. 14, 765 774.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 765-774
    • Poirier, M.A.1    Jiang, H.2    Ross, C.A.3
  • 245
    • 31444432457 scopus 로고    scopus 로고
    • Polyglutamine expansion inhibits respiration by increasing reactive oxygen species in isolated mitochondria
    • Puranam K. L., Wu G., Strittmatter W. J. Burke J. R. (2006) Polyglutamine expansion inhibits respiration by increasing reactive oxygen species in isolated mitochondria. Biochem. Biophys. Res. Commun. 341, 607 613.
    • (2006) Biochem. Biophys. Res. Commun. , vol.341 , pp. 607-613
    • Puranam, K.L.1    Wu, G.2    Strittmatter, W.J.3    Burke, J.R.4
  • 246
    • 33745200299 scopus 로고    scopus 로고
    • Sp1 is up-regulated in cellular and transgenic models of Huntington disease, and its reduction is neuroprotective
    • Qiu Z., Norflus F., Singh B. et al. (2006) Sp1 is up-regulated in cellular and transgenic models of Huntington disease, and its reduction is neuroprotective. J. Biol. Chem. 281, 16672 16680.
    • (2006) J. Biol. Chem. , vol.281 , pp. 16672-16680
    • Qiu, Z.1    Norflus, F.2    Singh, B.3
  • 248
    • 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., Ross C. A., MacDonald M. E., Saudou F. Humbert S. (2004) The serum- and glucocorticoid-induced kinase SGK inhibits mutant huntingtin-induced toxicity by phosphorylating serine 421 of huntingtin. Eur. J. Neurosci. 19, 273 279.
    • (2004) Eur. J. Neurosci. , vol.19 , pp. 273-279
    • Rangone, H.1    Poizat, G.2    Troncoso, J.3    Ross, C.A.4    MacDonald, M.E.5    Saudou, F.6    Humbert, S.7
  • 250
    • 20444467297 scopus 로고    scopus 로고
    • SUMOylation of the polyglutamine repeat protein, ataxin-1, is dependent on functional nuclear localization signal
    • Riley B. E., Zoghbi H. Y. Orr H. T. (2005) SUMOylation of the polyglutamine repeat protein, ataxin-1, is dependent on functional nuclear localization signal. J. Biol. Chem. 280, 21942 21948.
    • (2005) J. Biol. Chem. , vol.280 , pp. 21942-21948
    • Riley, B.E.1    Zoghbi, H.Y.2    Orr, H.T.3
  • 251
    • 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. (2007) The first 17 amino acids of Huntingtin modulate its sub-cellular localization, aggregation and effects on calcium homeostasis. Hum. Mol. Genet. 16, 61 77.
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 61-77
    • Rockabrand, E.1    Slepko, N.2    Pantalone, A.3
  • 253
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross C. A. Poirier M. A. (2004) Protein aggregation and neurodegenerative disease. Nat. Med. 10 (Suppl. S10 S17.
    • (2004) Nat. Med. , vol.10 , Issue.SUPPL.
    • Ross, C.A.1    Poirier, M.A.2
  • 255
    • 0032904145 scopus 로고    scopus 로고
    • Intracellular inclusions, pathological markers in diseases caused by expanded polyglutamine tracts?
    • Rubinsztein D. C., Wyttenbach A. Rankin J. (1999) Intracellular inclusions, pathological markers in diseases caused by expanded polyglutamine tracts? J. Med. Genet. 36, 265 270.
    • (1999) J. Med. Genet. , vol.36 , pp. 265-270
    • Rubinsztein, D.C.1    Wyttenbach, A.2    Rankin, J.3
  • 257
    • 0033103523 scopus 로고    scopus 로고
    • Caspase-8 is required for cell death induced by expanded polyglutamine repeats
    • Sanchez I., Xu C. J., Juo P., Kakizaka A., Blenis J. Yuan J. (1999) Caspase-8 is required for cell death induced by expanded polyglutamine repeats. Neuron 22, 623 633.
    • (1999) Neuron , vol.22 , pp. 623-633
    • Sanchez, I.1    Xu, C.J.2    Juo, P.3    Kakizaka, A.4    Blenis, J.5    Yuan, J.6
  • 258
    • 0037461730 scopus 로고    scopus 로고
    • Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders
    • Sanchez I., Mahlke C. Yuan J. (2003) Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders. Nature 421, 373 379.
    • (2003) Nature , vol.421 , pp. 373-379
    • Sanchez, I.1    Mahlke, C.2    Yuan, J.3
  • 260
    • 63549136610 scopus 로고    scopus 로고
    • Sumoylation and human disease pathogenesis
    • Sarge K. D. Park-Sarge O. K. (2009) Sumoylation and human disease pathogenesis. Trends Biochem. Sci. 34, 200 205.
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 200-205
    • Sarge, K.D.1    Park-Sarge, O.K.2
  • 261
    • 34247161367 scopus 로고    scopus 로고
    • Trehalose, a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant huntingtin and alpha-synuclein
    • Sarkar S., Davies J. E., Huang Z., Tunnacliffe A. Rubinsztein D. C. (2007a) Trehalose, a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant huntingtin and alpha-synuclein. J. Biol. Chem. 282, 5641 5652.
    • (2007) J. Biol. Chem. , vol.282 , pp. 5641-5652
    • Sarkar, S.1    Davies, J.E.2    Huang, Z.3    Tunnacliffe, A.4    Rubinsztein, D.C.5
  • 262
    • 34248994604 scopus 로고    scopus 로고
    • Small molecules enhance autophagy and reduce toxicity in Huntington's disease models
    • Sarkar S., Perlstein E. O., Imarisio S. et al. (2007b) Small molecules enhance autophagy and reduce toxicity in Huntington's disease models. Nat. Chem. Biol. 3, 331 338.
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 331-338
    • Sarkar, S.1    Perlstein, E.O.2    Imarisio, S.3
  • 263
    • 37849042536 scopus 로고    scopus 로고
    • A rational mechanism for combination treatment of Huntington's disease using lithium and rapamycin
    • Sarkar S., Krishna G., Imarisio S., Saiki S., O'Kane C. J. Rubinsztein D. C. (2008) A rational mechanism for combination treatment of Huntington's disease using lithium and rapamycin. Hum. Mol. Genet. 17, 170 178.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 170-178
    • Sarkar, S.1    Krishna, G.2    Imarisio, S.3    Saiki, S.4    O'Kane, C.J.5    Rubinsztein, D.C.6
  • 264
    • 0032907359 scopus 로고    scopus 로고
    • Transgenic mice harboring a full-length human mutant DRPLA gene exhibit age-dependent intergenerational and somatic instabilities of CAG repeats comparable with those in DRPLA patients
    • Sato T., Oyake M., Nakamura K. et al. (1999) Transgenic mice harboring a full-length human mutant DRPLA gene exhibit age-dependent intergenerational and somatic instabilities of CAG repeats comparable with those in DRPLA patients. Hum. Mol. Genet. 8, 99 106.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 99-106
    • Sato, T.1    Oyake, M.2    Nakamura, K.3
  • 265
    • 0032475931 scopus 로고    scopus 로고
    • Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions
    • Saudou F., Finkbeiner S., Devys D. Greenberg M. E. (1998) Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions. Cell 95, 55 66.
    • (1998) Cell , vol.95 , pp. 55-66
    • Saudou, F.1    Finkbeiner, S.2    Devys, D.3    Greenberg, M.E.4
  • 266
    • 33750831549 scopus 로고    scopus 로고
    • Oral uridine pro-drug PN401 is neuroprotective in the R6/2 and N171-82Q mouse models of Huntington's disease
    • Saydoff J. A., Garcia R. A., Browne S. E. et al. (2006) Oral uridine pro-drug PN401 is neuroprotective in the R6/2 and N171-82Q mouse models of Huntington's disease. Neurobiol. Dis. 24, 455 465.
    • (2006) Neurobiol. Dis. , vol.24 , pp. 455-465
    • Saydoff, J.A.1    Garcia, R.A.2    Browne, S.E.3
  • 268
    • 4043164771 scopus 로고    scopus 로고
    • The metabotropic glutamate receptor 5 antagonist MPEP and the mGluR2 agonist LY379268 modify disease progression in a transgenic mouse model of Huntington's disease
    • Schiefer J., Sprunken A., Puls C., Luesse H. G., Milkereit A., Milkereit E., Johann V. Kosinski C. M. (2004) The metabotropic glutamate receptor 5 antagonist MPEP and the mGluR2 agonist LY379268 modify disease progression in a transgenic mouse model of Huntington's disease. Brain Res. 1019, 246 254.
    • (2004) Brain Res. , vol.1019 , pp. 246-254
    • Schiefer, J.1    Sprunken, A.2    Puls, C.3    Luesse, H.G.4    Milkereit, A.5    Milkereit, E.6    Johann, V.7    Kosinski, C.M.8
  • 269
    • 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. (1999a) Intranuclear inclusions and neuritic aggregates in transgenic mice expressing a mutant N-terminal fragment of huntingtin. Hum. Mol. Genet. 8, 397 407.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 397-407
    • Schilling, G.1    Becher, M.W.2    Sharp, A.H.3
  • 270
    • 0009744392 scopus 로고    scopus 로고
    • Nuclear accumulation of truncated atrophin-1 fragments in a transgenic mouse model of DRPLA
    • Schilling G., Wood J. D., Duan K. et al. (1999b) Nuclear accumulation of truncated atrophin-1 fragments in a transgenic mouse model of DRPLA. Neuron 24, 275 286.
    • (1999) Neuron , vol.24 , pp. 275-286
    • Schilling, G.1    Wood, J.D.2    Duan, K.3
  • 271
    • 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. Borchelt D. R. (2001) Coenzyme Q10 and remacemide hydrochloride ameliorate motor deficits in a Huntington's disease transgenic mouse model. Neurosci. Lett. 315, 149 153.
    • (2001) Neurosci. Lett. , vol.315 , pp. 149-153
    • Schilling, G.1    Coonfield, M.L.2    Ross, C.A.3    Borchelt, D.R.4
  • 272
    • 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. (2006) Huntingtin phosphorylation sites mapped by mass spectrometry. Modulation of cleavage and toxicity. J. Biol. Chem. 281, 23686 23697.
    • (2006) J. Biol. Chem. , vol.281 , pp. 23686-23697
    • Schilling, B.1    Gafni, J.2    Torcassi, C.3
  • 273
    • 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 G. B., Schmitt I. et al. (1998) An isoform of ataxin-3 accumulates in the nucleus of neuronal cells in affected brain regions of SCA3 patients. Brain Pathol. 8, 669 679.
    • (1998) Brain Pathol. , vol.8 , pp. 669-679
    • Schmidt, T.1    Landwehrmeyer, G.B.2    Schmitt, I.3
  • 274
    • 0036198110 scopus 로고    scopus 로고
    • Protein surveillance machinery in brains with spinocerebellar ataxia type 3: Redistribution and differential recruitment of 26S proteasome subunits and chaperones to neuronal intranuclear inclusions
    • Schmidt T., Lindenberg K. S., Krebs A., Schols L., Laccone F., Herms J., Rechsteiner M., Riess O. Landwehrmeyer G. B. (2002) Protein surveillance machinery in brains with spinocerebellar ataxia type 3: redistribution and differential recruitment of 26S proteasome subunits and chaperones to neuronal intranuclear inclusions. Ann. Neurol. 51, 302 310.
    • (2002) Ann. Neurol. , vol.51 , pp. 302-310
    • Schmidt, T.1    Lindenberg, K.S.2    Krebs, A.3    Schols, L.4    Laccone, F.5    Herms, J.6    Rechsteiner, M.7    Riess, O.8    Landwehrmeyer, G.B.9
  • 275
    • 11144356369 scopus 로고    scopus 로고
    • Autosomal dominant cerebellar ataxias: Clinical features, genetics, and pathogenesis
    • Schols L., Bauer P., Schmidt T., Schulte T. Riess O. (2004) Autosomal dominant cerebellar ataxias: clinical features, genetics, and pathogenesis. Lancet Neurol. 3, 291 304.
    • (2004) Lancet Neurol. , vol.3 , pp. 291-304
    • Schols, L.1    Bauer, P.2    Schmidt, T.3    Schulte, T.4    Riess, O.5
  • 276
    • 37849030901 scopus 로고    scopus 로고
    • Polyglutamine diseases: Emerging concepts in pathogenesis and therapy
    • Shao J. Diamond M. I. (2007) Polyglutamine diseases: emerging concepts in pathogenesis and therapy. Hum. Mol. Genet. 16 (Spec No. 2) R115 R123.
    • (2007) Hum. Mol. Genet. , vol.16 , Issue.SPEC. NO. 2
    • Shao, J.1    Diamond, M.I.2
  • 277
    • 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. (1999) A Huntington's disease CAG expansion at the murine Hdh locus is unstable and associated with behavioural abnormalities in mice. Hum. Mol. Genet. 8, 763 774.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 763-774
    • Shelbourne, P.F.1    Killeen, N.2    Hevner, R.F.3
  • 278
    • 0034701797 scopus 로고    scopus 로고
    • A novel protein with RNA-binding motifs interacts with ataxin-2
    • Shibata H., Huynh D. P. Pulst S. M. (2000) A novel protein with RNA-binding motifs interacts with ataxin-2. Hum. Mol. Genet. 9, 1303 1313.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 1303-1313
    • Shibata, H.1    Huynh, D.P.2    Pulst, S.M.3
  • 279
    • 0033818112 scopus 로고    scopus 로고
    • Expanded polyglutamine stretches interact with TAFII130, interfering with CREB-dependent transcription
    • Shimohata T., Nakajima T., Yamada M. et al. (2000) Expanded polyglutamine stretches interact with TAFII130, interfering with CREB-dependent transcription. Nat. Genet. 26, 29 36.
    • (2000) Nat. Genet. , vol.26 , pp. 29-36
    • Shimohata, T.1    Nakajima, T.2    Yamada, M.3
  • 280
    • 0033037919 scopus 로고    scopus 로고
    • Huntington's disease intranuclear inclusions contain truncated, ubiquitinated huntingtin protein
    • Sieradzan K. A., Mechan A. O., Jones L., Wanker E. E., Nukina N. Mann D. M. (1999) Huntington's disease intranuclear inclusions contain truncated, ubiquitinated huntingtin protein. Exp. Neurol. 156, 92 99.
    • (1999) Exp. Neurol. , vol.156 , pp. 92-99
    • Sieradzan, K.A.1    Mechan, A.O.2    Jones, L.3    Wanker, E.E.4    Nukina, N.5    Mann, D.M.6
  • 282
    • 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. (2003) Selective striatal neuronal loss in a YAC128 mouse model of Huntington disease. Hum. Mol. Genet. 12, 1555 1567.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 1555-1567
    • Slow, E.J.1    Van Raamsdonk, J.2    Rogers, D.3
  • 285
    • 56249087909 scopus 로고    scopus 로고
    • Progressive synaptic pathology of motor cortical neurons in a BAC transgenic mouse model of Huntington's disease
    • Spampanato J., Gu X., Yang X. W. Mody I. (2008) Progressive synaptic pathology of motor cortical neurons in a BAC transgenic mouse model of Huntington's disease. Neuroscience 157, 606 620.
    • (2008) Neuroscience , vol.157 , pp. 606-620
    • Spampanato, J.1    Gu, X.2    Yang, X.W.3    Mody, I.4
  • 287
    • 31644439986 scopus 로고    scopus 로고
    • Combination therapy using minocycline and coenzyme Q10 in R6/2 transgenic Huntington's disease mice
    • Stack E. C., Smith K. M., Ryu H. et al. (2006) Combination therapy using minocycline and coenzyme Q10 in R6/2 transgenic Huntington's disease mice. Biochim. Biophys. Acta 1762, 373 380.
    • (2006) Biochim. Biophys. Acta , vol.1762 , pp. 373-380
    • Stack, E.C.1    Smith, K.M.2    Ryu, H.3
  • 288
    • 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. (2007) Modulation of nucleosome dynamics in Huntington's disease. Hum. Mol. Genet. 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
  • 289
    • 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. (2000) The Huntington's disease protein interacts with p53 and CREB-binding protein and represses transcription. Proc. Natl Acad. Sci. USA 97, 6763 6768.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 6763-6768
    • Steffan, J.S.1    Kazantsev, A.2    Spasic-Boskovic, O.3
  • 290
    • 11144353613 scopus 로고    scopus 로고
    • SUMO modification of Huntingtin and Huntington's disease pathology
    • Steffan J. S., Agrawal N., Pallos J. et al. (2004) SUMO modification of Huntingtin and Huntington's disease pathology. Science 304, 100 104.
    • (2004) Science , vol.304 , pp. 100-104
    • Steffan, J.S.1    Agrawal, N.2    Pallos, J.3
  • 291
    • 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 D. L., Cummings C. J., Adams H. P., Mancini M. G., Patel K., DeMartino G. N., Marcelli M., Weigel N. L. Mancini M. A. (1999) 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. 8, 731 741.
    • (1999) Hum. Mol. Genet. , vol.8 , 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    Marcelli, M.7    Weigel, N.L.8    Mancini, M.A.9
  • 292
    • 0036798685 scopus 로고    scopus 로고
    • Intranuclear ataxin1 inclusions contain both fast- and slow-exchanging components
    • Stenoien D. L., Mielke M. Mancini M. A. (2002) Intranuclear ataxin1 inclusions contain both fast- and slow-exchanging components. Nat. Cell Biol. 4, 806 810.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 806-810
    • Stenoien, D.L.1    Mielke, M.2    Mancini, M.A.3
  • 293
    • 33749999530 scopus 로고    scopus 로고
    • Suppression of reactive oxygen species and neurodegeneration by the PGC-1 transcriptional coactivators
    • St-Pierre J., Drori S., Uldry M. et al. (2006) Suppression of reactive oxygen species and neurodegeneration by the PGC-1 transcriptional coactivators. Cell 127, 397 408.
    • (2006) Cell , vol.127 , pp. 397-408
    • St-Pierre, J.1    Drori, S.2    Uldry, M.3
  • 294
    • 27744560978 scopus 로고    scopus 로고
    • A role for both wild-type and expanded ataxin-7 in transcriptional regulation
    • Strom A. L., Forsgren L. Holmberg M. (2005) A role for both wild-type and expanded ataxin-7 in transcriptional regulation. Neurobiol. Dis. 20, 646 655.
    • (2005) Neurobiol. Dis. , vol.20 , pp. 646-655
    • Strom, A.L.1    Forsgren, L.2    Holmberg, M.3
  • 296
    • 34547627141 scopus 로고    scopus 로고
    • Differential effects of polyglutamine proteins on nuclear organization and artificial reporter splicing
    • Sun J., Xu H., Negi S., Subramony S. H. Hebert M. D. (2007) Differential effects of polyglutamine proteins on nuclear organization and artificial reporter splicing. J. Neurosci. Res. 85, 2306 2317.
    • (2007) J. Neurosci. Res. , vol.85 , pp. 2306-2317
    • Sun, J.1    Xu, H.2    Negi, S.3    Subramony, S.H.4    Hebert, M.D.5
  • 297
    • 10744224530 scopus 로고    scopus 로고
    • Neuropathogenic forms of huntingtin and androgen receptor inhibit fast axonal transport
    • Szebenyi G., Morfini G. A., Babcock A. et al. (2003) Neuropathogenic forms of huntingtin and androgen receptor inhibit fast axonal transport. Neuron 40, 41 52.
    • (2003) Neuron , vol.40 , pp. 41-52
    • Szebenyi, G.1    Morfini, G.A.2    Babcock, A.3
  • 299
    • 14644440579 scopus 로고    scopus 로고
    • Neuronal intranuclear inclusions and neuropil aggregates in HdhCAG(150) knockin mice
    • Tallaksen-Greene S. J., Crouse A. B., Hunter J. M., Detloff P. J. Albin R. L. (2005) Neuronal intranuclear inclusions and neuropil aggregates in HdhCAG(150) knockin mice. Neuroscience 131, 843 852.
    • (2005) Neuroscience , vol.131 , pp. 843-852
    • Tallaksen-Greene, S.J.1    Crouse, A.B.2    Hunter, J.M.3    Detloff, P.J.4    Albin, R.L.5
  • 300
    • 0035976971 scopus 로고    scopus 로고
    • Intra- and intermolecular beta-pleated sheet formation in glutamine-repeat inserted myoglobin as a model for polyglutamine diseases
    • Tanaka M., Morishima I., Akagi T., Hashikawa T. Nukina N. (2001) Intra- and intermolecular beta-pleated sheet formation in glutamine-repeat inserted myoglobin as a model for polyglutamine diseases. J. Biol. Chem. 276, 45470 45475.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45470-45475
    • Tanaka, M.1    Morishima, I.2    Akagi, T.3    Hashikawa, T.4    Nukina, N.5
  • 301
    • 0141668882 scopus 로고    scopus 로고
    • Expansion of polyglutamine induces the formation of quasi-aggregate in the early stage of protein fibrillization
    • Tanaka M., Machida Y., Nishikawa Y., Akagi T., Hashikawa T., Fujisawa T. Nukina N. (2003) Expansion of polyglutamine induces the formation of quasi-aggregate in the early stage of protein fibrillization. J. Biol. Chem. 278, 34717 34724.
    • (2003) J. Biol. Chem. , vol.278 , pp. 34717-34724
    • Tanaka, M.1    MacHida, Y.2    Nishikawa, Y.3    Akagi, T.4    Hashikawa, T.5    Fujisawa, T.6    Nukina, N.7
  • 303
    • 0027861082 scopus 로고
    • Coactivators and TAFs: A new class of eukaryotic transcription factors that connect activators to the basal machinery
    • Tanese N. Tjian R. (1993) Coactivators and TAFs: a new class of eukaryotic transcription factors that connect activators to the basal machinery. Cold Spring Harb. Symp. Quant. Biol. 58, 179 185.
    • (1993) Cold Spring Harb. Symp. Quant. Biol. , vol.58 , pp. 179-185
    • Tanese, N.1    Tjian, R.2
  • 304
    • 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., Maximov A., Wang Z., Wellington C. L., Hayden M. R. Bezprozvanny I. (2003) Huntingtin and huntingtin-associated protein 1 influence neuronal calcium signaling mediated by inositol-(1,4,5) triphosphate receptor type 1. Neuron 39, 227 239.
    • (2003) Neuron , vol.39 , pp. 227-239
    • Tang, T.S.1    Tu, H.2    Chan, E.Y.3    Maximov, A.4    Wang, Z.5    Wellington, C.L.6    Hayden, M.R.7    Bezprozvanny, I.8
  • 305
    • 59649118434 scopus 로고    scopus 로고
    • Neuroprotective effects of inositol 1,4,5-trisphosphate receptor C-terminal fragment in a Huntington's disease mouse model
    • Tang T. S., Guo C., Wang H., Chen X. Bezprozvanny I. (2009) Neuroprotective effects of inositol 1,4,5-trisphosphate receptor C-terminal fragment in a Huntington's disease mouse model. J. Neurosci. 29, 1257 1266.
    • (2009) J. Neurosci. , vol.29 , pp. 1257-1266
    • Tang, T.S.1    Guo, C.2    Wang, H.3    Chen, X.4    Bezprozvanny, I.5
  • 307
    • 0037015833 scopus 로고    scopus 로고
    • SUMO-1 co-localized with mutant atrophin-1 with expanded polyglutamines accelerates intranuclear aggregation and cell death
    • Terashima T., Kawai H., Fujitani M., Maeda K. Yasuda H. (2002) SUMO-1 co-localized with mutant atrophin-1 with expanded polyglutamines accelerates intranuclear aggregation and cell death. Neuroreport 13, 2359 2364.
    • (2002) Neuroreport , vol.13 , pp. 2359-2364
    • Terashima, T.1    Kawai, H.2    Fujitani, M.3    Maeda, K.4    Yasuda, H.5
  • 308
    • 64049119303 scopus 로고    scopus 로고
    • Polyglutamine disruption of the huntingtin exon 1 N terminus triggers a complex aggregation mechanism
    • Thakur A. K., Jayaraman M., Mishra R. et al. (2009) Polyglutamine disruption of the huntingtin exon 1 N terminus triggers a complex aggregation mechanism. Nat. Struct. Mol. Biol. 16, 380 389.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 380-389
    • Thakur, A.K.1    Jayaraman, M.2    Mishra, R.3
  • 309
    • 60549084901 scopus 로고    scopus 로고
    • 17-DMAG ameliorates polyglutamine-mediated motor neuron degeneration through well-preserved proteasome function in an SBMA model mouse
    • Tokui K., Adachi H., Waza M. et al. (2009) 17-DMAG ameliorates polyglutamine-mediated motor neuron degeneration through well-preserved proteasome function in an SBMA model mouse. Hum. Mol. Genet. 18, 898 910.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 898-910
    • Tokui, K.1    Adachi, H.2    Waza, M.3
  • 311
    • 14344262672 scopus 로고    scopus 로고
    • Full-length expanded ataxin-3 enhances mitochondrial-mediated cell death and decreases Bcl-2 expression in human neuroblastoma cells
    • Tsai H. F., Tsai H. J. Hsieh M. (2004) Full-length expanded ataxin-3 enhances mitochondrial-mediated cell death and decreases Bcl-2 expression in human neuroblastoma cells. Biochem. Biophys. Res. Commun. 324, 1274 1282.
    • (2004) Biochem. Biophys. Res. Commun. , vol.324 , pp. 1274-1282
    • Tsai, H.F.1    Tsai, H.J.2    Hsieh, M.3
  • 312
    • 23944438950 scopus 로고    scopus 로고
    • The AXH domain of Ataxin-1 mediates neurodegeneration through its interaction with Gfi-1/Senseless proteins
    • Tsuda H., Jafar-Nejad H., Patel A. J. et al. (2005) The AXH domain of Ataxin-1 mediates neurodegeneration through its interaction with Gfi-1/Senseless proteins. Cell 122, 633 644.
    • (2005) Cell , vol.122 , pp. 633-644
    • Tsuda, H.1    Jafar-Nejad, H.2    Patel, A.J.3
  • 313
    • 0034887539 scopus 로고    scopus 로고
    • Non-expanded polyglutamine proteins in intranuclear inclusions of hereditary ataxias - Triple-labeling immunofluorescence study
    • Uchihara T., Fujigasaki H., Koyano S., Nakamura A., Yagishita S. Iwabuchi K. (2001) Non-expanded polyglutamine proteins in intranuclear inclusions of hereditary ataxias - triple-labeling immunofluorescence study. Acta Neuropathol. 102, 149 152.
    • (2001) Acta Neuropathol. , vol.102 , pp. 149-152
    • Uchihara, T.1    Fujigasaki, H.2    Koyano, S.3    Nakamura, A.4    Yagishita, S.5    Iwabuchi, K.6
  • 315
    • 3142566639 scopus 로고    scopus 로고
    • Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system
    • Verma R., Oania R., Graumann J. Deshaies R. J. (2004) Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system. Cell 118, 99 110.
    • (2004) Cell , vol.118 , pp. 99-110
    • Verma, R.1    Oania, R.2    Graumann, J.3    Deshaies, R.J.4
  • 319
    • 0033867992 scopus 로고    scopus 로고
    • Ataxin-3, the MJD1 gene product, interacts with the two human homologs of yeast DNA repair protein RAD23, HHR23A and HHR23B
    • Wang G., Sawai N., Kotliarova S., Kanazawa I. Nukina N. (2000) Ataxin-3, the MJD1 gene product, interacts with the two human homologs of yeast DNA repair protein RAD23, HHR23A and HHR23B. Hum. Mol. Genet. 9, 1795 1803.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 1795-1803
    • Wang, G.1    Sawai, N.2    Kotliarova, S.3    Kanazawa, I.4    Nukina, N.5
  • 321
    • 29044445801 scopus 로고    scopus 로고
    • Polyglutamine-expanded ataxin-7 activates mitochondrial apoptotic pathway of cerebellar neurons by upregulating Bax and downregulating Bcl-x(L)
    • Wang H. L., Yeh T. H., Chou A. H., Kuo Y. L., Luo L. J., He C. Y., Huang P. C. Li A. H. (2006) Polyglutamine-expanded ataxin-7 activates mitochondrial apoptotic pathway of cerebellar neurons by upregulating Bax and downregulating Bcl-x(L). Cell. Signal. 18, 541 552.
    • (2006) Cell. Signal. , vol.18 , pp. 541-552
    • Wang, H.L.1    Yeh, T.H.2    Chou, A.H.3    Kuo, Y.L.4    Luo, L.J.5    He, C.Y.6    Huang, P.C.7    Li, A.H.8
  • 322
    • 58949099388 scopus 로고    scopus 로고
    • Effects of overexpression of huntingtin proteins on mitochondrial integrity
    • Wang H., Lim P. J., Karbowski M. Monteiro M. J. (2009) Effects of overexpression of huntingtin proteins on mitochondrial integrity. Hum. Mol. Genet. 18, 737 752.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 737-752
    • Wang, H.1    Lim, P.J.2    Karbowski, M.3    Monteiro, M.J.4
  • 323
    • 0033791230 scopus 로고    scopus 로고
    • Protein aggregation and pathogenesis of Huntington's disease: Mechanisms and correlations
    • Wanker E. E. (2000) Protein aggregation and pathogenesis of Huntington's disease: mechanisms and correlations. J. Biol. Chem. 381, 937 942.
    • (2000) J. Biol. Chem. , vol.381 , pp. 937-942
    • Wanker, E.E.1
  • 325
    • 0032727617 scopus 로고    scopus 로고
    • Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70
    • Warrick J. M., Chan H. Y., Gray-Board G. L., Chai Y., Paulson H. L. Bonini N. M. (1999) Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70. Nat. Genet. 23, 425 428.
    • (1999) Nat. Genet. , vol.23 , pp. 425-428
    • Warrick, J.M.1    Chan, H.Y.2    Gray-Board, G.L.3    Chai, Y.4    Paulson, H.L.5    Bonini, N.M.6
  • 326
    • 34249675397 scopus 로고    scopus 로고
    • Lithium therapy improves neurological function and hippocampal dendritic arborization in a spinocerebellar ataxia type 1 mouse model
    • Watase K., Gatchel J. R., Sun Y. et al. (2007) Lithium therapy improves neurological function and hippocampal dendritic arborization in a spinocerebellar ataxia type 1 mouse model. PLoS Med. 4, 836 846.
    • (2007) PLoS Med. , vol.4 , pp. 836-846
    • Watase, K.1    Gatchel, J.R.2    Sun, Y.3
  • 328
    • 0033953015 scopus 로고    scopus 로고
    • Caspases and neurodegeneration: On the cutting edge of new therapeutic approaches
    • Wellington C. L. Hayden M. R. (2000) Caspases and neurodegeneration: on the cutting edge of new therapeutic approaches. Clin. Genet. 57, 1 10.
    • (2000) Clin. Genet. , vol.57 , pp. 1-10
    • Wellington, C.L.1    Hayden, M.R.2
  • 329
    • 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. (1998) Caspase cleavage of gene products associated with triplet expansion disorders generates truncated fragments containing the polyglutamine tract. J. Biol. Chem. 273, 9158 9167.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9158-9167
    • Wellington, C.L.1    Ellerby, L.M.2    Hackam, A.S.3
  • 330
    • 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. (2000) Inhibiting caspase cleavage of huntingtin reduces toxicity and aggregate formation in neuronal and nonneuronal cells. J. Biol. Chem. 275, 19831 19838.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19831-19838
    • Wellington, C.L.1    Singaraja, R.2    Ellerby, L.3
  • 331
    • 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. (2002) Caspase cleavage of mutant huntingtin precedes neurodegeneration in Huntington's disease. J. Neurosci. 22, 7862 7872.
    • (2002) J. Neurosci. , vol.22 , pp. 7862-7872
    • Wellington, C.L.1    Ellerby, L.M.2    Gutekunst, C.A.3
  • 332
    • 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. (2006) Thermoregulatory and metabolic defects in Huntington's disease transgenic mice implicate PGC-1alpha in Huntington's disease neurodegeneration. Cell Metab. 4, 349 362.
    • (2006) Cell Metab. , vol.4 , pp. 349-362
    • Weydt, P.1    Pineda, V.V.2    Torrence, A.E.3
  • 333
    • 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. (2000) 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. 9, 503 513.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 503-513
    • Wheeler, V.C.1    White, J.K.2    Gutekunst, C.A.3
  • 334
    • 0037087771 scopus 로고    scopus 로고
    • Early phenotypes that presage late-onset neurodegenerative disease allow testing of modifiers in Hdh CAG knock-in mice
    • Wheeler V. C., Gutekunst C. A., Vrbanac V. et al. (2002) Early phenotypes that presage late-onset neurodegenerative disease allow testing of modifiers in Hdh CAG knock-in mice. Hum. Mol. Genet. 11, 633 640.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 633-640
    • Wheeler, V.C.1    Gutekunst, C.A.2    Vrbanac, V.3
  • 335
    • 42249106042 scopus 로고    scopus 로고
    • Novel targets for Huntington's disease in an mTOR-independent autophagy pathway
    • Williams A., Sarkar S., Cuddon P. et al. (2008) Novel targets for Huntington's disease in an mTOR-independent autophagy pathway. Nat. Chem. Biol. 4, 295 305.
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 295-305
    • Williams, A.1    Sarkar, S.2    Cuddon, P.3
  • 336
    • 60849119525 scopus 로고    scopus 로고
    • In vivo suppression of polyglutamine neurotoxicity by C-terminus of Hsp70-interacting protein (CHIP) supports an aggregation model of pathogenesis
    • Williams A. J., Knutson T. M., Colomer Gould V. F. Paulson H. L. (2009) In vivo suppression of polyglutamine neurotoxicity by C-terminus of Hsp70-interacting protein (CHIP) supports an aggregation model of pathogenesis. Neurobiol. Dis. 33, 342 353.
    • (2009) Neurobiol. Dis. , vol.33 , pp. 342-353
    • Williams, A.J.1    Knutson, T.M.2    Colomer Gould, V.F.3    Paulson, H.L.4
  • 337
    • 53349127249 scopus 로고    scopus 로고
    • Blocking acid-sensing ion channel 1 alleviates Huntington's disease pathology via an ubiquitin-proteasome system-dependent mechanism
    • Wong H. K., Bauer P. O., Kurosawa M. et al. (2008) Blocking acid-sensing ion channel 1 alleviates Huntington's disease pathology via an ubiquitin-proteasome system-dependent mechanism. Hum. Mol. Genet. 17, 3223 3235.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 3223-3235
    • Wong, H.K.1    Bauer, P.O.2    Kurosawa, M.3
  • 338
    • 33846295583 scopus 로고    scopus 로고
    • Systemic administration of Congo red does not improve motor or cognitive function in R6/2 mice
    • Wood N. I., Pallier P. N., Wanderer J. Morton A. J. (2007) Systemic administration of Congo red does not improve motor or cognitive function in R6/2 mice. Neurobiol. Dis. 25, 342 353.
    • (2007) Neurobiol. Dis. , vol.25 , pp. 342-353
    • Wood, N.I.1    Pallier, P.N.2    Wanderer, J.3    Morton, A.J.4
  • 340
    • 0036566675 scopus 로고    scopus 로고
    • Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin
    • Wyttenbach A., Sauvageot O., Carmichael J., Diaz-Latoud C., Arrigo A. P. Rubinsztein D. C. (2002) Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin. Hum. Mol. Genet. 11, 1137 1151.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1137-1151
    • Wyttenbach, A.1    Sauvageot, O.2    Carmichael, J.3    Diaz-Latoud, C.4    Arrigo, A.P.5    Rubinsztein, D.C.6
  • 341
    • 0037701612 scopus 로고    scopus 로고
    • Huntingtin contains a highly conserved nuclear export signal
    • Xia J., Lee D. H., Taylor J., Vandelft M. Truant R. (2003) Huntingtin contains a highly conserved nuclear export signal. Hum. Mol. Genet. 12, 1393 1403.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 1393-1403
    • Xia, J.1    Lee, D.H.2    Taylor, J.3    Vandelft, M.4    Truant, R.5
  • 342
    • 36949022900 scopus 로고    scopus 로고
    • CAG repeat disorder models and human neuropathology: Similarities and differences
    • Yamada M., Sato T., Tsuji S. Takahashi H. (2008) CAG repeat disorder models and human neuropathology: similarities and differences. Acta Neuropathol. 115, 71 86.
    • (2008) Acta Neuropathol. , vol.115 , pp. 71-86
    • Yamada, M.1    Sato, T.2    Tsuji, S.3    Takahashi, H.4
  • 343
    • 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. (2000) Reversal of neuropathology and motor dysfunction in a conditional model of Huntington's disease. Cell 101, 57 66.
    • (2000) Cell , vol.101 , pp. 57-66
    • Yamamoto, A.1    Lucas, J.J.2    Hen, R.3
  • 344
    • 40949135766 scopus 로고    scopus 로고
    • Mutant Huntingtin reduces HSP70 expression through the sequestration of NF-Y transcription factor
    • Yamanaka T., Miyazaki H., Oyama F., Kurosawa M., Washizu C., Doi H. Nukina N. (2008) Mutant Huntingtin reduces HSP70 expression through the sequestration of NF-Y transcription factor. EMBO J. 27, 827 839.
    • (2008) EMBO J. , vol.27 , pp. 827-839
    • Yamanaka, T.1    Miyazaki, H.2    Oyama, F.3    Kurosawa, M.4    Washizu, C.5    Doi, H.6    Nukina, N.7
  • 345
    • 0036850529 scopus 로고    scopus 로고
    • Aggregated polyglutamine peptides delivered to nuclei are toxic to mammalian cells
    • Yang W., Dunlap J. R., Andrews R. B. Wetzel R. (2002) Aggregated polyglutamine peptides delivered to nuclei are toxic to mammalian cells. Hum. Mol. Genet. 11, 2905 2917.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2905-2917
    • Yang, W.1    Dunlap, J.R.2    Andrews, R.B.3    Wetzel, R.4
  • 346
    • 33847738994 scopus 로고    scopus 로고
    • ASC-J9 ameliorates spinal and bulbar muscular atrophy phenotype via degradation of androgen receptor
    • Yang Z., Chang Y. J., Yu I. C. et al. (2007) ASC-J9 ameliorates spinal and bulbar muscular atrophy phenotype via degradation of androgen receptor. Nat. Med. 13, 348 353.
    • (2007) Nat. Med. , vol.13 , pp. 348-353
    • Yang, Z.1    Chang, Y.J.2    Yu, I.C.3
  • 347
    • 33744965475 scopus 로고    scopus 로고
    • Sodium butyrate ameliorates histone hypoacetylation and neurodegenerative phenotypes in a mouse model for DRPLA
    • Ying M., Xu R., Wu X., Zhu H., Zhuang Y., Han M. Xu T. (2006) Sodium butyrate ameliorates histone hypoacetylation and neurodegenerative phenotypes in a mouse model for DRPLA. J. Biol. Chem. 281, 12580 12586.
    • (2006) J. Biol. Chem. , vol.281 , pp. 12580-12586
    • Ying, M.1    Xu, R.2    Wu, X.3    Zhu, H.4    Zhuang, Y.5    Han, M.6    Xu, T.7
  • 348
    • 60849095522 scopus 로고    scopus 로고
    • Polyglutamine-expanded androgen receptor truncation fragments activate a Bax-dependent apoptotic cascade mediated by DP5/Hrk
    • Young J. E., Garden G. A., Martinez R. A. et al. (2009) Polyglutamine-expanded androgen receptor truncation fragments activate a Bax-dependent apoptotic cascade mediated by DP5/Hrk. J. Neurosci. 29, 1987 1997.
    • (2009) J. Neurosci. , vol.29 , pp. 1987-1997
    • Young, J.E.1    Garden, G.A.2    Martinez, R.A.3
  • 349
    • 0037090927 scopus 로고    scopus 로고
    • Huntingtin inclusions do not deplete polyglutamine-containing transcription factors in HD mice
    • Yu Z. X., Li S. H., Nguyen H. P. Li X. J. (2002) Huntingtin inclusions do not deplete polyglutamine-containing transcription factors in HD mice. Hum. Mol. Genet. 11, 905 914.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 905-914
    • Yu, Z.X.1    Li, S.H.2    Nguyen, H.P.3    Li, X.J.4
  • 350
    • 66049150300 scopus 로고    scopus 로고
    • Decreased antioxidant enzyme activity and increased mitochondrial DNA damage in cellular models of Machado-Joseph disease
    • Yu Y. C., Kuo C. L., Cheng W. L., Liu C. S. Hsieh M. (2009) Decreased antioxidant enzyme activity and increased mitochondrial DNA damage in cellular models of Machado-Joseph disease. J. Neurosci. Res. 87, 1884 1891.
    • (2009) J. Neurosci. Res. , vol.87 , pp. 1884-1891
    • Yu, Y.C.1    Kuo, C.L.2    Cheng, W.L.3    Liu, C.S.4    Hsieh, M.5
  • 351
    • 0034641891 scopus 로고    scopus 로고
    • Expanded polyglutamines induce neurodegeneration and trans-neuronal alterations in cerebellum and retina of SCA7 transgenic mice
    • Yvert G., Lindenberg K. S., Picaud S., Landwehrmeyer G. B., Sahel J. A. Mandel J. L. (2000) Expanded polyglutamines induce neurodegeneration and trans-neuronal alterations in cerebellum and retina of SCA7 transgenic mice. Hum. Mol. Genet. 9, 2491 2506.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2491-2506
    • Yvert, G.1    Lindenberg, K.S.2    Picaud, S.3    Landwehrmeyer, G.B.4    Sahel, J.A.5    Mandel, J.L.6
  • 352
    • 0035421417 scopus 로고    scopus 로고
    • SCA7 mouse models show selective stabilization of mutant ataxin-7 and similar cellular responses in different neuronal cell types
    • Yvert G., Lindenberg K. S., Devys D., Helmlinger D., Landwehrmeyer G. B. Mandel J. L. (2001) SCA7 mouse models show selective stabilization of mutant ataxin-7 and similar cellular responses in different neuronal cell types. Hum. Mol. Genet. 10, 1679 1692.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1679-1692
    • Yvert, G.1    Lindenberg, K.S.2    Devys, D.3    Helmlinger, D.4    Landwehrmeyer, G.B.5    Mandel, J.L.6
  • 353
    • 0035888620 scopus 로고    scopus 로고
    • Similarities between spinocerebellar ataxia type 7 (SCA7) cell models and human brain: Proteins recruited in inclusions and activation of caspase-3
    • Zander C., Takahashi J., El Hachimi K. H., Fujigasaki H., Albanese V., Lebre A. S., Stevanin G., Duyckaerts C. Brice A. (2001) Similarities between spinocerebellar ataxia type 7 (SCA7) cell models and human brain: proteins recruited in inclusions and activation of caspase-3. Hum. Mol. Genet. 10, 2569 2579.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 2569-2579
    • Zander, C.1    Takahashi, J.2    El Hachimi, K.H.3    Fujigasaki, H.4    Albanese, V.5    Lebre, A.S.6    Stevanin, G.7    Duyckaerts, C.8    Brice, A.9
  • 354
    • 0041330609 scopus 로고    scopus 로고
    • Impaired degradation of PKCalpha by proteasome in a cellular model of Huntington's disease
    • Zemskov E. A. Nukina N. (2003) Impaired degradation of PKCalpha by proteasome in a cellular model of Huntington's disease. Neuroreport 14, 1435 1438.
    • (2003) Neuroreport , vol.14 , pp. 1435-1438
    • Zemskov, E.A.1    Nukina, N.2
  • 355
    • 0141918859 scopus 로고    scopus 로고
    • Pro-apoptotic protein kinase C delta is associated with intranuclear inclusions in a transgenic model of Huntington's disease
    • Zemskov E. A., Jana N. R., Kurosawa M., Miyazaki H., Sakamoto N., Nekooki M. Nukina N. (2003) Pro-apoptotic protein kinase C delta is associated with intranuclear inclusions in a transgenic model of Huntington's disease. J. Neurochem. 87, 395 406.
    • (2003) J. Neurochem. , vol.87 , pp. 395-406
    • Zemskov, E.A.1    Jana, N.R.2    Kurosawa, M.3    Miyazaki, H.4    Sakamoto, N.5    Nekooki, M.6    Nukina, N.7
  • 356
    • 0035930598 scopus 로고    scopus 로고
    • Chaperone suppression of cellular toxicity of huntingtin is independent of polyglutamine aggregation
    • Zhou H., Li S. H. Li X. J. (2001) Chaperone suppression of cellular toxicity of huntingtin is independent of polyglutamine aggregation. J. Biol. Chem. 276, 48417 48424.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48417-48424
    • Zhou, H.1    Li, S.H.2    Li, X.J.3
  • 357
    • 0034094873 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegeneration
    • Zoghbi H. Y. Orr H. T. (2000) Glutamine repeats and neurodegeneration. Annu. Rev. Neurosci. 23, 217 247.
    • (2000) Annu. Rev. Neurosci. , vol.23 , pp. 217-247
    • Zoghbi, H.Y.1    Orr, H.T.2
  • 358
  • 359
    • 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. (2003) Huntingtin interacts with REST/NRSF to modulate the transcription of NRSE-controlled neuronal genes. Nat. Genet. 35, 76 83.
    • (2003) Nat. Genet. , vol.35 , pp. 76-83
    • Zuccato, C.1    Tartari, M.2    Crotti, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.