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Volumn 769, Issue , 2012, Pages 125-140

Polyglutamine aggregation in huntington and related diseases

Author keywords

[No Author keywords available]

Indexed keywords

HUNTINGTIN; POLYGLUTAMINE;

EID: 84934444551     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4614-5434-2_8     Document Type: Review
Times cited : (13)

References (181)
  • 1
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. The Huntington's disease collaborative research group
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. The Huntington's disease collaborative research group. Cell 1993; 72(6):971-983.
    • (1993) Cell , vol.72 , Issue.6 , pp. 971-983
  • 2
    • 0027164698 scopus 로고
    • Expansion of an unstable trinucleotide CAG repeat in spinocerebellar ataxia type 1
    • Orr HT, Chung MY, Banfi S et al. Expansion of an unstable trinucleotide CAG repeat in spinocerebellar ataxia type 1. Nat Genet 1993; 4(3):221-226.
    • (1993) Nat Genet , vol.4 , Issue.3 , pp. 221-226
    • Orr, H.T.1    Chung, M.Y.2    Banfi, S.3
  • 3
    • 0030294345 scopus 로고    scopus 로고
    • Cloning of the gene for spinocerebellar ataxia 2 reveals a locus with high sensitivity to expanded CAG/glutamine repeats
    • Imbert G, Saudou F, Yvert G et al. Cloning of the gene for spinocerebellar ataxia 2 reveals a locus with high sensitivity to expanded CAG/glutamine repeats. Nat Genet 1996; 14(3):285-291.
    • (1996) Nat Genet , vol.14 , Issue.3 , pp. 285-291
    • Imbert, G.1    Saudou, F.2    Yvert, G.3
  • 4
    • 0030292368 scopus 로고    scopus 로고
    • Identification of the spinocerebellar ataxiatype 2 gene using a direct identification of repeat expansion and cloningtechnique, DIRECT
    • Sanpei K, Takano H, Igarashi S et al. Identification of the spinocerebellar ataxiatype 2 gene using a direct identification of repeat expansion and cloningtechnique, DIRECT. Nat Genet 1996; 14(3):277-284.
    • (1996) Nat Genet , vol.14 , Issue.3 , pp. 277-284
    • Sanpei, K.1    Takano, H.2    Igarashi, S.3
  • 5
    • 0028143527 scopus 로고
    • CAG expansions in a novel gene for Machado-Joseph disease at chromosome 14q32.1
    • Kawaguchi Y, Okamoto T, Taniwaki M et al. CAG expansions in a novel gene for Machado-Joseph disease at chromosome 14q32.1. Nat Genet 1994; 8(3):221-228.
    • (1994) Nat Genet , vol.8 , Issue.3 , pp. 221-228
    • Kawaguchi, Y.1    Okamoto, T.2    Taniwaki, M.3
  • 6
    • 0031012399 scopus 로고    scopus 로고
    • Autosomal dominant cerebellar ataxia (SCA6) associated with small polyglutamine expansions in the alpha 1A-voltage-dependent calcium channel
    • Zhuchenko O, Bailey J, Bonnen P et al. Autosomal dominant cerebellar ataxia (SCA6) associated with small polyglutamine expansions in the alpha 1A-voltage-dependent calcium channel. Nat Genet 1997; 15(1):62-69.
    • (1997) Nat Genet , vol.15 , Issue.1 , pp. 62-69
    • Zhuchenko, O.1    Bailey, J.2    Bonnen, P.3
  • 7
    • 16944364511 scopus 로고    scopus 로고
    • Cloning of the SCA7 gene reveals a highly unstable CAG repeat expansion
    • David G, Abbas N, Stevanin G et al. Cloning of the SCA7 gene reveals a highly unstable CAG repeat expansion. Nat Genet 1997; 17(1):65-70.
    • (1997) Nat Genet , vol.17 , Issue.1 , pp. 65-70
    • David, G.1    Abbas, N.2    Stevanin, G.3
  • 8
    • 0035393427 scopus 로고    scopus 로고
    • SCA17, a novel autosomal dominant cerebellar ataxia caused by an expanded polyglutamine in TATA-binding protein
    • Nakamura K, Jeong SY, Uchihara T et al. SCA17, a novel autosomal dominant cerebellar ataxia caused by an expanded polyglutamine in TATA-binding protein. Hum Mol Genet 2001; 10(14):1441-1448.
    • (2001) Hum Mol Genet , vol.10 , Issue.14 , pp. 1441-1448
    • Nakamura, K.1    Jeong, S.Y.2    Uchihara, T.3
  • 9
    • 0027176364 scopus 로고
    • The relationship between trinucleotide (CAG) repeat length and clinical features of Huntington's disease
    • Andrew SE, Goldberg YP, Kremer B et al. The relationship between trinucleotide (CAG) repeat length and clinical features of Huntington's disease. Nat Genet 1993; 4(4):398-403.
    • (1993) Nat Genet , vol.4 , Issue.4 , pp. 398-403
    • Andrew, S.E.1    Goldberg, Y.P.2    Kremer, B.3
  • 10
    • 0025800526 scopus 로고
    • Androgen receptor gene mutations in X-linked spinal and bulbar muscular atrophy
    • La Spada AR, Wilson EM, Lubahn DB et al. Androgen receptor gene mutations in X-linked spinal and bulbar muscular atrophy. Nature 1991; 352(6330):77-79.
    • (1991) Nature , vol.352 , Issue.6330 , pp. 77-79
    • La Spada, A.R.1    Wilson, E.M.2    Lubahn, D.B.3
  • 11
    • 0028216760 scopus 로고
    • Unstable expansion of CAG repeat in hereditary dentatorubral- pallidoluysian atrophy (DRPLA)
    • Koide R, Ikeuchi T, Onodera O et al. Unstable expansion of CAG repeat in hereditary dentatorubral-pallidoluysian atrophy (DRPLA). Nat Genet 1994; 6(1):9-13.
    • (1994) Nat Genet , vol.6 , Issue.1 , pp. 9-13
    • Koide, R.1    Ikeuchi, T.2    Onodera, O.3
  • 12
    • 0028060244 scopus 로고
    • Structure and expression of the gene responsible for the triplet repeat disorder, dentatorubral and pallidoluysian atrophy (DRPLA)
    • Nagafuchi S, Yanagisawa H, Ohsaki E et al. Structure and expression of the gene responsible for the triplet repeat disorder, dentatorubral and pallidoluysian atrophy (DRPLA). Nat Genet 1994; 8(2):177-182.
    • (1994) Nat Genet , vol.8 , Issue.2 , pp. 177-182
    • Nagafuchi, S.1    Yanagisawa, H.2    Ohsaki, E.3
  • 13
    • 0030795968 scopus 로고    scopus 로고
    • The CAG/polyglutamine tract diseases: Gene products and molecular pathogenesis
    • Koshy BT, Zoghbi HY. The CAG/polyglutamine tract diseases: gene products and molecular pathogenesis. Brain Pathol 1997; 7(3):927-942.
    • (1997) Brain Pathol , vol.7 , Issue.3 , pp. 927-942
    • Koshy, B.T.1    Zoghbi, H.Y.2
  • 14
    • 18544400323 scopus 로고    scopus 로고
    • Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo
    • Scherzinger E, Lurz R, Turmaine M et al. Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo. Cell 1997; 90(3):549-558.
    • (1997) Cell , vol.90 , Issue.3 , pp. 549-558
    • Scherzinger, E.1    Lurz, R.2    Turmaine, M.3
  • 15
    • 0033551063 scopus 로고    scopus 로고
    • Self-assembly ofpolyglutamine-containing huntingtin fragments into amyloid-like fibrils: Implications for Huntington's disease pathology
    • Scherzinger E, Sittler A, Schweiger K et al. Self-assembly ofpolyglutamine-containing huntingtin fragments into amyloid-like fibrils: implications for Huntington's disease pathology. Proc Natl Acad Sci U S A 1999; 96(8):4604-4609.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , Issue.8 , pp. 4604-4609
    • Scherzinger, E.1    Sittler, A.2    Schweiger, K.3
  • 16
    • 0026586167 scopus 로고
    • Amyloid-like properties of a synthetic peptide corresponding to the carboxy terminus of beta-amyloid protein precursor
    • Caputo CB, Fraser PE, Sobel IE et al. Amyloid-like properties of a synthetic peptide corresponding to the carboxy terminus of beta-amyloid protein precursor. Arch Biochem Biophys 1992; 292(1):199-205.
    • (1992) Arch Biochem Biophys , vol.292 , Issue.1 , pp. 199-205
    • Caputo, C.B.1    Fraser, P.E.2    Sobel, I.E.3
  • 17
    • 0021019026 scopus 로고
    • Scrapie prions aggregate to form amyloid-like birefringent rods
    • Prusiner SB, McKinley MP, Bowman KA et al. Scrapie prions aggregate to form amyloid-like birefringent rods. Cell 1983; 35(2 Pt 1):349-358.
    • (1983) Cell , vol.35 , Issue.2 PART 1 , pp. 349-358
    • Prusiner, S.B.1    McKinley, M.P.2    Bowman, K.A.3
  • 18
    • 0032450856 scopus 로고    scopus 로고
    • Amyloid formation by mutant huntingtin: Threshold, progressivity and recruitment of normal polyglutamine proteins
    • Huang CC, Faber PW, Persichetti F et al. Amyloid formation by mutant huntingtin: threshold, progressivity and recruitment of normal polyglutamine proteins. Somat Cell Mol Genet 1998; 24(4):217-233.
    • (1998) Somat Cell Mol Genet , vol.24 , Issue.4 , pp. 217-233
    • Huang, C.C.1    Faber, P.W.2    Persichetti, F.3
  • 19
    • 0032877134 scopus 로고    scopus 로고
    • Analysis of protein aggregation kinetics
    • Ferrone F. Analysis of protein aggregation kinetics. Methods Enzymol 1999; 309:256-274.
    • (1999) Methods Enzymol , vol.309 , pp. 256-274
    • Ferrone, F.1
  • 20
    • 0035881211 scopus 로고    scopus 로고
    • A microtiter plate assay for polyglutamine aggregate extension
    • Berthelier V, Hamilton JB, Chen S et al. A microtiter plate assay for polyglutamine aggregate extension. Anal Biochem 2001; 295(2):227-236.
    • (2001) Anal Biochem , vol.295 , Issue.2 , pp. 227-236
    • Berthelier, V.1    Hamilton, J.B.2    Chen, S.3
  • 21
    • 0034733023 scopus 로고    scopus 로고
    • Alzheimer's disease amyloid propagation by a template-dependent dock-lock mechanism
    • Esler WP, Stimson ER, Jennings JM et al. Alzheimer's disease amyloid propagation by a template-dependent dock-lock mechanism. Biochemistry 2000; 39(21):6288-6295.
    • (2000) Biochemistry , vol.39 , Issue.21 , pp. 6288-6295
    • Esler, W.P.1    Stimson, E.R.2    Jennings, J.M.3
  • 22
    • 0027195933 scopus 로고
    • Seeding "one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett JT, Lansbury PT Jr. Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell 1993; 73(6):1055-1058.
    • (1993) Cell , vol.73 , Issue.6 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury Jr., P.T.2
  • 23
    • 0037015081 scopus 로고    scopus 로고
    • Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation
    • Chen S, Ferrone FA, Wetzel R. Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation. Proc Natl Acad Sci U S A 2002; 99(18):11884-11889.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , Issue.18 , pp. 11884-11889
    • Chen, S.1    Ferrone, F.A.2    Wetzel, R.3
  • 24
    • 67649366306 scopus 로고    scopus 로고
    • Model discrimination and mechanistic interpretation of kinetic data in protein aggregation studies
    • Bernacki JP, Murphy RM. Model discrimination and mechanistic interpretation of kinetic data in protein aggregation studies. Biophys J 2009; 96(7):2871-2887.
    • (2009) Biophys J , vol.96 , Issue.7 , pp. 2871-2887
    • Bernacki, J.P.1    Murphy, R.M.2
  • 25
    • 70349838220 scopus 로고    scopus 로고
    • Examining polyglutamine peptide length: A connection between collapsed conformations and increased aggregation
    • Walters RH, Murphy RM. Examining polyglutamine peptide length: a connection between collapsed conformations and increased aggregation. J Mol Biol 2009; 393(4):978-992.
    • (2009) J Mol Biol , vol.393 , Issue.4 , pp. 978-992
    • Walters, R.H.1    Murphy, R.M.2
  • 26
    • 35848945494 scopus 로고    scopus 로고
    • Reconsidering the mechanism of polyglutamine peptide aggregation
    • Lee CC, Walters RH, Murphy RM. Reconsidering the mechanism of polyglutamine peptide aggregation. Biochemistry 2007; 46(44):12810-12820.
    • (2007) Biochemistry , vol.46 , Issue.44 , pp. 12810-12820
    • Lee, C.C.1    Walters, R.H.2    Murphy, R.M.3
  • 27
    • 77951988103 scopus 로고    scopus 로고
    • Mutant huntingtin fragments form oligomers in a polyglutamine length-dependent manner in vitro and in vivo
    • Legleiter J, Mitchell E, Lotz GP et al. Mutant huntingtin fragments form oligomers in a polyglutamine length-dependent manner in vitro and in vivo. J Biol Chem 2010; 285(19):14777-14790.
    • (2010) J Biol Chem , vol.285 , Issue.19 , pp. 14777-14790
    • Legleiter, J.1    Mitchell, E.2    Lotz, G.P.3
  • 28
    • 16544383250 scopus 로고    scopus 로고
    • Hsp70 and Hsp40 attenuate formation of spherical and annular polyglutamine oligomers by partitioning monomer
    • Wacker JL, Zareie MH, Fong H et al. Hsp70 and Hsp40 attenuate formation of spherical and annular polyglutamine oligomers by partitioning monomer. Nat Struct Mol Biol 2004; 11(12):1215-1222.
    • (2004) Nat Struct Mol Biol , vol.11 , Issue.12 , pp. 1215-1222
    • Wacker, J.L.1    Zareie, M.H.2    Fong, H.3
  • 29
    • 27344435254 scopus 로고    scopus 로고
    • Polyglutamine aggregation nucleation: Thermodynamics of a highly unfavorable protein folding reaction
    • Bhattacharyya AM, Thakur AK, Wetzel R. polyglutamine aggregation nucleation: thermodynamics of a highly unfavorable protein folding reaction. Proc Natl Acad Sci U S A 2005; 102(43):15400-15405.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , Issue.43 , pp. 15400-15405
    • Bhattacharyya, A.M.1    Thakur, A.K.2    Wetzel, R.3
  • 30
    • 69149105917 scopus 로고    scopus 로고
    • Single homopolypeptide chains collapse into mechanically rigid conformations
    • Dougan L, Li J, Badilla CL et al. Single homopolypeptide chains collapse into mechanically rigid conformations. Proc Natl Acad Sci U S A 2009; 106(31):12605-12610.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , Issue.31 , pp. 12605-12610
    • Dougan, L.1    Li, J.2    Badilla, C.L.3
  • 31
    • 33645281939 scopus 로고    scopus 로고
    • Characterizing the conformational ensemble of monomeric polyglutamine
    • Wang X, Vitalis A, Wyczalkowski MA et al. Characterizing the conformational ensemble of monomeric polyglutamine. Proteins 2006; 63(2):297-311.
    • (2006) Proteins , vol.63 , Issue.2 , pp. 297-311
    • Wang, X.1    Vitalis, A.2    Wyczalkowski, M.A.3
  • 32
    • 33750934185 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy shows that monomeric polyglutamine molecules form collapsed structures in aqueous solutions
    • Crick SL, Jayaraman M, Frieden C et al. Fluorescence correlation spectroscopy shows that monomeric polyglutamine molecules form collapsed structures in aqueous solutions. Proc Natl Acad Sci U S A 2006; 103(45):16764-16769.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , Issue.45 , pp. 16764-16769
    • Crick, S.L.1    Jayaraman, M.2    Frieden, C.3
  • 33
    • 0030739464 scopus 로고    scopus 로고
    • Random coil conformation for extended polyglutamine stretches in aqueous soluble monomeric peptides
    • Altschuler EL, Hud NV, Mazrimas JA et al. Random coil conformation for extended polyglutamine stretches in aqueous soluble monomeric peptides. J Pept Res 1997; 50(1):73-75.
    • (1997) J Pept Res , vol.50 , Issue.1 , pp. 73-75
    • Altschuler, E.L.1    Hud, N.V.2    Mazrimas, J.A.3
  • 34
    • 0035800572 scopus 로고    scopus 로고
    • Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity
    • Chen S, Berthelier V, Yang W et al. Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity. J Mol Biol 2001; 311(1):173-182.
    • (2001) J Mol Biol , vol.311 , Issue.1 , pp. 173-182
    • Chen, S.1    Berthelier, V.2    Yang, W.3
  • 35
    • 0037181179 scopus 로고    scopus 로고
    • Solution structure of polyglutamine tracts in GST-polyglutamine fusion proteins
    • Masino L, Kelly G, Leonard K et al. Solution structure of polyglutamine tracts in GST-polyglutamine fusion proteins. FEBS Lett 2002; 513(2-3):267-272.
    • (2002) FEBS Lett , vol.513 , Issue.2-3 , pp. 267-272
    • Masino, L.1    Kelly, G.2    Leonard, K.3
  • 36
    • 54249132105 scopus 로고    scopus 로고
    • Atomistic simulations ofthe effects ofpolyglutamine chain length and solvent quality on conformational equilibria and spontaneous homodimerization
    • Vitalis A, Wang X, Pappu RV. Atomistic simulations ofthe effects ofpolyglutamine chain length and solvent quality on conformational equilibria and spontaneous homodimerization. J Mol Biol 2008; 384(1):279-297.
    • (2008) J Mol Biol , vol.384 , Issue.1 , pp. 279-297
    • Vitalis, A.1    Wang, X.2    Pappu, R.V.3
  • 37
    • 36749056299 scopus 로고    scopus 로고
    • A polymer physics perspective on driving forces and mechanisms for protein aggregation
    • Pappu RV, Wang X, Vitalis A et al. A polymer physics perspective on driving forces and mechanisms for protein aggregation. Arch Biochem Biophys 2008; 469(1):132-141.
    • (2008) Arch Biochem Biophys , vol.469 , Issue.1 , pp. 132-141
    • Pappu, R.V.1    Wang, X.2    Vitalis, A.3
  • 38
    • 1842766144 scopus 로고    scopus 로고
    • Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins
    • Venkatraman P, Wetzel R, Tanaka M et al. Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins. Mol Cell 2004; 14(1):95-104.
    • (2004) Mol Cell , vol.14 , Issue.1 , pp. 95-104
    • Venkatraman, P.1    Wetzel, R.2    Tanaka, M.3
  • 39
    • 0037174879 scopus 로고    scopus 로고
    • Huntingtin spheroids and protofibrils as precursors in polyglutamine fibrilization
    • Poirier MA, Li H, Macosko J et al. Huntingtin spheroids and protofibrils as precursors in polyglutamine fibrilization. J Biol Chem 2002; 277(43):41032-41037.
    • (2002) J Biol Chem , vol.277 , Issue.43 , pp. 41032-41037
    • Ma, P.1    Li, H.2    Macosko, J.3
  • 40
    • 0037062561 scopus 로고    scopus 로고
    • Amyloid-like features of polyglutamine aggregates and their assembly kinetics
    • Chen S, Berthelier V, Hamilton JB et al. Amyloid-like features of polyglutamine aggregates and their assembly kinetics. Biochemistry 2002; 41(23):7391-7399.
    • (2002) Biochemistry , vol.41 , Issue.23 , pp. 7391-7399
    • Chen, S.1    Berthelier, V.2    Hamilton, J.B.3
  • 41
    • 68949127591 scopus 로고    scopus 로고
    • Thermodynamics of beta-sheet formation in polyglutamine
    • Vitalis A, Lyle N, Pappu RV. Thermodynamics of beta-sheet formation in polyglutamine. Biophys J 2009; 97(1):303-311.
    • (2009) Biophys J , vol.97 , Issue.1 , pp. 303-311
    • Vitalis, A.1    Lyle, N.2    Pappu, R.V.3
  • 42
    • 28944446477 scopus 로고    scopus 로고
    • Oligoproline effects on polyglutamine conformation and aggregation
    • Bhattacharyya A, Thakur AK, Chellgren VM et al. Oligoproline effects on polyglutamine conformation and aggregation. J Mol Biol 2006; 355(3):524-535.
    • (2006) J Mol Biol , vol.355 , Issue.3 , pp. 524-535
    • Bhattacharyya, A.1    Thakur, A.K.2    Chellgren, V.M.3
  • 43
    • 67649856863 scopus 로고    scopus 로고
    • Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity
    • Nekooki-Machida Y, Kurosawa M, Nukina N et al. Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity. Proc Natl Acad Sci U S A 2009; 106(24):9679-9684.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , Issue.24 , pp. 9679-9684
    • Nekooki-Machida, Y.1    Kurosawa, M.2    Nukina, N.3
  • 44
    • 0035833997 scopus 로고    scopus 로고
    • An expanded glutamine repeat destabilizes native ataxin-3 structure and mediates formation of parallel beta -fibrils
    • Bevivino AE, Loll PJ. An expanded glutamine repeat destabilizes native ataxin-3 structure and mediates formation of parallel beta -fibrils. Proc Natl Acad SciUSA 2001; 98(21):11955-11960.
    • (2001) Proc Natl Acad SciUSA , vol.98 , Issue.21 , pp. 11955-11960
    • Bevivino, A.E.1    Loll, P.J.2
  • 46
    • 31944449691 scopus 로고    scopus 로고
    • Evidence that Perutz's double-beta-stranded subunit structure for beta-amyloids also applies to their channel-forming structures in membranes
    • Singer SJ, Dewji NN. Evidence that Perutz's double-beta-stranded subunit structure for beta-amyloids also applies to their channel-forming structures in membranes. Proc Natl Acad Sci U S A 2006; 103(5):1546-1550.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , Issue.5 , pp. 1546-1550
    • Singer, S.J.1    Dewji, N.N.2
  • 47
    • 0028283985 scopus 로고
    • Glutamine repeats as polar zippers: Their possible role in inherited neurodegenerative diseases
    • Perutz MF, Johnson T, Suzuki M et al. Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases. Proc Natl Acad Sci U S A 1994; 91(12):5355-5358.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , Issue.12 , pp. 5355-5358
    • Perutz, M.F.1    Johnson, T.2    Suzuki, M.3
  • 48
    • 26444575834 scopus 로고    scopus 로고
    • Polyglutamine homopolymers having 8-45 residues form slablike beta-crystallite assemblies
    • Sharma D, Shinchuk LM, Inouye H et al. Polyglutamine homopolymers having 8-45 residues form slablike beta-crystallite assemblies. Proteins 2005; 61(2):398-411.
    • (2005) Proteins , vol.61 , Issue.2 , pp. 398-411
    • Sharma, D.1    Shinchuk, L.M.2    Inouye, H.3
  • 49
    • 0035976971 scopus 로고    scopus 로고
    • Intra- and intermolecular beta-pleated sheet formation in glutamine-rep eat inserted myoglobin as a model for polyglutamine diseases
    • Tanaka M, Morishima I, Akagi T et al. Intra- and intermolecular beta-pleated sheet formation in glutamine-rep eat inserted myoglobin as a model for polyglutamine diseases. J Biol Chem 2001; 276(48):45470-45475.
    • (2001) J Biol Chem , vol.276 , Issue.48 , pp. 45470-45475
    • Tanaka, M.1    Morishima, I.2    Akagi, T.3
  • 50
    • 14044278010 scopus 로고    scopus 로고
    • New model for crystalline polyglutamine assemblies and their connection with amyloid fibrils
    • Sikorski P, Atkins E. New model for crystalline polyglutamine assemblies and their connection with amyloid fibrils. Biomacromolecules 2005; 6(l):425-432.
    • (2005) Biomacromolecules , vol.6 , Issue.1 , pp. 425-432
    • Sikorski, P.1    Atkins, E.2
  • 51
    • 0037168642 scopus 로고    scopus 로고
    • Mutational analysis of the structural organization of polyglutamine aggregates
    • Thakur AK, Wetzel R. Mutational analysis of the structural organization of polyglutamine aggregates. Proc Natl Acad Sci U S A 2002; 99(26):17014-17019.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , Issue.26 , pp. 17014-17019
    • Thakur, A.K.1    Wetzel, R.2
  • 52
    • 12244285938 scopus 로고    scopus 로고
    • Molecular basis for amyloid fibril formation and stability
    • Makin OS, Atkins E, Sikorski P et al. Molecular basis for amyloid fibril formation and stability. Proc Natl Acad Sci U S A 2005; 102(2):315-320.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , Issue.2 , pp. 315-320
    • Makin, O.S.1    Atkins, E.2    Sikorski, P.3
  • 53
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DiFiglia M, Sapp E, Chase KO et al. Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 1997; 277(5334):1990-1993.
    • (1997) Science , vol.277 , Issue.5334 , pp. 1990-1993
    • Difiglia, M.1    Sapp, E.2    Chase, K.O.3
  • 54
    • 18544410106 scopus 로고    scopus 로고
    • Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation
    • Davies SW, Turmaine M, Cozens BA et al. Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation. Cell 1997; 90(3):537-548.
    • (1997) Cell , vol.90 , Issue.3 , pp. 537-548
    • Davies, S.W.1    Turmaine, M.2    Cozens, B.A.3
  • 55
    • 0032248397 scopus 로고    scopus 로고
    • Pathological mechanisms in Huntington's disease and other polyglutamine expansion diseases
    • Lunkes A, Trottier Y, Mandel JL. Pathological mechanisms in Huntington's disease and other polyglutamine expansion diseases. Essays Biochem 1998; 33:149-163.
    • (1998) Essays Biochem , vol.33 , pp. 149-163
    • Lunkes, A.1    Trottier, Y.2    Mandel, J.L.3
  • 56
    • 77954379810 scopus 로고    scopus 로고
    • Tracking mutant huntingtin aggregation kinetics in cells reveals three major populations that include an invariant oligomer pool
    • Olshina MA, Angley LM, Ramdzan YM et al. Tracking mutant huntingtin aggregation kinetics in cells reveals three major populations that include an invariant oligomer pool. J Biol Chem 2010; 285(28):21807-21816.
    • (2010) J Biol Chem , vol.285 , Issue.28 , pp. 21807-21816
    • Olshina, M.A.1    Angley, L.M.2    Ramdzan, Y.M.3
  • 57
    • 77950932967 scopus 로고    scopus 로고
    • Conformation sensors that distinguish monomeric proteins from oligomers in live cells
    • Ramdzan YM, Nisbet RM, Miller J et al. Conformation sensors that distinguish monomeric proteins from oligomers in live cells. Chem Biol 2010; 17(4):371-379.
    • (2010) Chem Biol , vol.17 , Issue.4 , pp. 371-379
    • Ramdzan, Y.M.1    Nisbet, R.M.2    Miller, J.3
  • 58
    • 77953567262 scopus 로고    scopus 로고
    • A two-step path to inclusion formation of huntingtin peptides revealed by number and brightness analysis
    • Ossato G, Digman MA, Aiken C et al. A two-step path to inclusion formation of huntingtin peptides revealed by number and brightness analysis. Biophys J 2010; 98(12):3078-3085.
    • (2010) Biophys J , vol.98 , Issue.12 , pp. 3078-3085
    • Ossato, G.1    Ma, D.2    Aiken, C.3
  • 59
    • 0037154229 scopus 로고    scopus 로고
    • Requirement of an intact microtubule cytoskeleton for aggregation and inclusion body formation by a mutant huntingtin fragment
    • Muchowski PJ, Ning K, D'Souza-Schorey C et al. Requirement of an intact microtubule cytoskeleton for aggregation and inclusion body formation by a mutant huntingtin fragment. Proc Natl Acad Sci U S A 2002; 99(2):727-732.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , Issue.2 , pp. 727-732
    • Muchowski, P.J.1    Ning, K.2    D'Souza-Schorey, C.3
  • 60
    • 0037388418 scopus 로고    scopus 로고
    • Aggresomes protect cells by enhancing the degradation of toxic polyglutamine-containing protein
    • Taylor JP, Tanaka F, Robitschek J et al. Aggresomes protect cells by enhancing the degradation of toxic polyglutamine-containing protein. Hum Mol Genet 2003; 12(7):749-757.
    • (2003) Hum Mol Genet , vol.12 , Issue.7 , pp. 749-757
    • Taylor, J.P.1    Tanaka, F.2    Robitschek, J.3
  • 61
    • 63249135140 scopus 로고    scopus 로고
    • Single neuron ubiquitin-proteasome dynamics accompanying inclusion body formation in Huntington disease
    • Mitra S, Tsvetkov AS, Finkbeiner S. Single neuron ubiquitin-proteasome dynamics accompanying inclusion body formation in Huntington disease. J Biol Chem 2009; 284(7):4398-4403.
    • (2009) J Biol Chem , vol.284 , Issue.7 , pp. 4398-4403
    • Mitra, S.1    Tsvetkov, A.S.2    Finkbeiner, S.3
  • 62
    • 77949352928 scopus 로고    scopus 로고
    • Acute polyglutamine expression in inducible mouse model unravels ubiquitin/proteasome system impairment and permanent recovery attributable to aggregate formation
    • Ortega Z, Diaz-Hernandez M, Maynard CJ et al. Acute polyglutamine expression in inducible mouse model unravels ubiquitin/proteasome system impairment and permanent recovery attributable to aggregate formation. J Neurosci 2010; 30(10):3675-3688.
    • (2010) J Neurosci , vol.30 , Issue.10 , pp. 3675-3688
    • Ortega, Z.1    Diaz-Hernandez, M.2    Maynard, C.J.3
  • 63
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • Arrasate M, Mitra S, Schweitzer ES et al. Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 2004; 431(7010):805-810.
    • (2004) Nature , vol.431 , Issue.7010 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3
  • 64
    • 50649116818 scopus 로고    scopus 로고
    • Misfolded proteins partition between two distinct quality control compartments
    • Kaganovich D, Kopito R, Frydman J. Misfolded proteins partition between two distinct quality control compartments. Nature 2008; 454(7208):1088-1095.
    • (2008) Nature , vol.454 , Issue.7208 , pp. 1088-1095
    • Kaganovich, D.1    Kopito, R.2    Frydman, J.3
  • 65
    • 0036733778 scopus 로고    scopus 로고
    • Cytoplasmic dynein/dynactin mediates the assembly of aggresomes
    • Johnston JA, Illing ME, Kopito RR. Cytoplasmic dynein/dynactin mediates the assembly of aggresomes. Cell Motil Cytoskeleton 2002; 53(1):26-38.
    • (2002) Cell Motil Cytoskeleton , vol.53 , Issue.1 , pp. 26-38
    • Johnston, J.A.1    Illing, M.E.2    Kopito, R.R.3
  • 66
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • Johnston JA, Ward CL, Kopito RR. Aggresomes: a cellular response to misfolded proteins. J Cell Biol 1998; 143(7):1883-1898.
    • (1998) J Cell Biol , vol.143 , Issue.7 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 67
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito RR. Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol 2000; 10(12):524-530.
    • (2000) Trends Cell Biol , vol.10 , Issue.12 , pp. 524-530
    • Kopito, R.R.1
  • 68
    • 0344466781 scopus 로고    scopus 로고
    • Characterization and dynamics of aggresome formation by a cytosolic GFP-chimera
    • Garcia-Mata R, Bebok Z, Sorscher EJ et al. Characterization and dynamics of aggresome formation by a cytosolic GFP-chimera. J Cell Biol 1999; 146(6):1239-1254.
    • (1999) J Cell Biol , vol.146 , Issue.6 , pp. 1239-1254
    • Garcia-Mata, R.1    Bebok, Z.2    Sorscher, E.J.3
  • 69
    • 0034754875 scopus 로고    scopus 로고
    • Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation
    • Waelter S, Boeddrich A, Lurz R et al. Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation. Mol Biol Cell 2001; 12(5):1393-1407.
    • (2001) Mol Biol Cell , vol.12 , Issue.5 , pp. 1393-1407
    • Waelter, S.1    Boeddrich, A.2    Lurz, R.3
  • 70
    • 70849123017 scopus 로고    scopus 로고
    • Degradation and aggresome formation ofthe Gn tail ofthe apathogenic Tula hantavirus
    • Wang H, Strandin T, Hepojoki J et al. Degradation and aggresome formation ofthe Gn tail ofthe apathogenic Tula hantavirus. J Gen Virol 2009; 90(Pt 12):2995-3001.
    • (2009) J Gen Virol , vol.90 , Issue.PART 12 , pp. 2995-3001
    • Wang, H.1    Strandin, T.2    Hepojoki, J.3
  • 71
    • 0036798685 scopus 로고    scopus 로고
    • Intranuclear ataxin1 inclusions contain both fast- and slow-exchanging components
    • Stenoien DL, Mielke M, Mancini MA. Intranuclear ataxin1 inclusions contain both fast- and slow-exchanging components. Nat Cell Biol 2002; 4(10):806-810.
    • (2002) Nat Cell Biol , vol.4 , Issue.10 , pp. 806-810
    • Stenoien, D.L.1    Mielke, M.2    Mancini, M.A.3
  • 72
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DiFiglia M, Sapp E, Chase KO et al. Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 1997; 277(5334):1990-1993.
    • (1997) Science , vol.277 , Issue.5334 , pp. 1990-1993
    • Difiglia, M.1    Sapp, E.2    Chase, K.O.3
  • 73
    • 74849105740 scopus 로고    scopus 로고
    • Alpha Pix enhances mutant huntingtin aggregation
    • Eriguchi M, Mizuta H, Luo S et al. Alpha Pix enhances mutant huntingtin aggregation. J Neurol Sci 2010; 290(1-2):80-85.
    • (2010) J Neurol Sci , vol.290 , Issue.1-2 , pp. 80-85
    • Eriguchi, M.1    Mizuta, H.2    Luo, S.3
  • 74
    • 50249147874 scopus 로고    scopus 로고
    • Phosphorylation of profilin by ROCK1 regulates polyglutamine aggregation
    • Shao J, Welch WJ, Diprospero NA et al. Phosphorylation of profilin by ROCK1 regulates polyglutamine aggregation. Mol Cell Biol 2008; 28(17):5196-5208.
    • (2008) Mol Cell Biol , vol.28 , Issue.17 , pp. 5196-5208
    • Shao, J.1    Welch, W.J.2    Diprospero, N.A.3
  • 75
    • 43649084649 scopus 로고    scopus 로고
    • Expression of expanded polyglutamine targets profilin for degradation and alters actin dynamics
    • Burnett BG, Andrews J, Ranganathan S et al. Expression of expanded polyglutamine targets profilin for degradation and alters actin dynamics. Neurobiol Dis 2008; 30(3):365-374.
    • (2008) Neurobiol Dis , vol.30 , Issue.3 , pp. 365-374
    • Burnett, B.G.1    Andrews, J.2    Ranganathan, S.3
  • 76
    • 77949412662 scopus 로고    scopus 로고
    • F-actin binding regions on the androgen receptor and huntingtin increase aggregation and alter aggregate characteristics
    • Angeli S, Shao J, Diamond MI. F-actin binding regions on the androgen receptor and huntingtin increase aggregation and alter aggregate characteristics. PLoS One 2010; 5(2):e9053.
    • (2010) PLoS One , vol.5 , Issue.2
    • Angeli, S.1    Shao, J.2    Diamond, M.I.3
  • 77
    • 0035940412 scopus 로고    scopus 로고
    • Caspase 3-cleaved N-terminal fragments of wild-type and mutant huntingtin are present in normal and Huntington's disease brains, associate with membranes, and undergo calpain-dependent proteolysis
    • Kim YJ, Yi Y, Sapp E et al. Caspase 3-cleaved N-terminal fragments of wild-type and mutant huntingtin are present in normal and Huntington's disease brains, associate with membranes, and undergo calpain-dependent proteolysis. Proc Natl Acad Sci U S A 2001; 98(22):12784-12789.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , Issue.22 , pp. 12784-12789
    • Kim, Y.J.1    Yi, Y.2    Sapp, E.3
  • 78
    • 77950584656 scopus 로고    scopus 로고
    • Proteolysis of mutant huntingtin produces an exon 1 fragment that accumulates as an aggregated protein in neuronal nuclei in Huntington disease
    • Landles C, Sathasivam K, Weiss A et al. Proteolysis of mutant huntingtin produces an exon 1 fragment that accumulates as an aggregated protein in neuronal nuclei in Huntington disease. J Biol Chem 2010; 285(12):8808-8823.
    • (2010) J Biol Chem , vol.285 , Issue.12 , pp. 8808-8823
    • Landles, C.1    Sathasivam, K.2    Weiss, A.3
  • 79
    • 53749088439 scopus 로고    scopus 로고
    • Intracellular degradation of misfolded proteins in polyglutamine neurodegenerative diseases
    • Li X, Li H, Li XJ. Intracellular degradation of misfolded proteins in polyglutamine neurodegenerative diseases. Brain Res Rev 2008; 59(1):245-252.
    • (2008) Brain Res Rev , vol.59 , Issue.1 , pp. 245-252
    • Li, X.1    Li, H.2    Li, X.J.3
  • 80
    • 0033037919 scopus 로고    scopus 로고
    • Huntington's disease intranuclear inclusions contain truncated, ubiquitinated huntingtin protein
    • Sieradzan KA, Mechan AO, Jones L et al. Huntington's disease intranuclear inclusions contain truncated, ubiquitinated huntingtin protein. Exp Neurol 1999; 156(1):92-99.
    • (1999) Exp Neurol , vol.156 , Issue.1 , pp. 92-99
    • Sieradzan, K.A.1    Mechan, A.O.2    Jones, L.3
  • 81
    • 17344363559 scopus 로고    scopus 로고
    • Length ofhuntingtin and its polyglutamine tract influences localization and frequency of intracellular aggregates
    • Martindale D, Hackam A, Wieczorek A et al. Length ofhuntingtin and its polyglutamine tract influences localization and frequency of intracellular aggregates. Nat Genet 1998; 18(2):150-154.
    • (1998) Nat Genet , vol.18 , Issue.2 , pp. 150-154
    • Martindale, D.1    Hackam, A.2    Wieczorek, A.3
  • 82
    • 0032101287 scopus 로고    scopus 로고
    • The influence ofhuntingtin protein size onnuclear localization and cellular toxicity
    • Hackam AS, SingarajaR, Wellington CL etal. The influence ofhuntingtin protein size onnuclear localization and cellular toxicity. J Cell Biol 1998; 141(5):1097-1105.
    • (1998) J Cell Biol , vol.141 , Issue.5 , pp. 1097-1105
    • Hackam, A.S.1    Singaraja, R.2    Wellington, C.L.3
  • 83
    • 48049092846 scopus 로고    scopus 로고
    • Activated caspase-6 and caspase-6-cleaved fragments ofhuntingtin specifically colocalize inthe nucleus
    • Warby SC, Doty CN, Graham RK et al. Activated caspase-6 and caspase-6-cleaved fragments ofhuntingtin specifically colocalize inthe nucleus. Hum Mol Genet 2008; 17(15):2390-2404.
    • (2008) Hum Mol Genet , vol.17 , Issue.15 , pp. 2390-2404
    • Warby, S.C.1    Doty, C.N.2    Graham, R.K.3
  • 84
    • 33745003424 scopus 로고    scopus 로고
    • Cleavage at the caspase-6 site is required for neuronal dysfunction and degeneration due to mutant huntingtin
    • Graham RK, Deng Y, Slow EJ et al. Cleavage at the caspase-6 site is required for neuronal dysfunction and degeneration due to mutant huntingtin. Cell 2006; 125(6):1179-1191.
    • (2006) Cell , vol.125 , Issue.6 , pp. 1179-1191
    • Graham, R.K.1    Deng, Y.2    Slow, E.J.3
  • 85
    • 33747633422 scopus 로고    scopus 로고
    • Huntingtin phosphorylation sites mapped by mass spectrometry. Modulation of cleavage and toxicity
    • Schilling B, Gafni J, Torcassi C et al. Huntingtin phosphorylation sites mapped by mass spectrometry. Modulation of cleavage and toxicity. J Biol Chem 2006; 281(33):23686-23697.
    • (2006) J Biol Chem , vol.281 , Issue.33 , pp. 23686-23697
    • Schilling, B.1    Gafni, J.2    Torcassi, C.3
  • 86
    • 70350380989 scopus 로고    scopus 로고
    • Phosphorylation of threonine 3: Implications for Huntingtin aggregation and neurotoxicity
    • Aiken CT, Steffan JS, Guerrero CM et al. Phosphorylation of threonine 3: implications for Huntingtin aggregation and neurotoxicity. J Biol Chem 2009; 284(43):29427-29436.
    • (2009) J Biol Chem , vol.284 , Issue.43 , pp. 29427-29436
    • Aiken, C.T.1    Steffan, J.S.2    Guerrero, C.M.3
  • 87
    • 33846540080 scopus 로고    scopus 로고
    • The first 17 amino acids of Huntingtin modulate its sub-cellular localization, aggregation and effects on calcium homeostasis
    • Rockabrand E, Slepko N, Pantalone A et al. The first 17 amino acids of Huntingtin modulate its sub-cellular localization, aggregation and effects on calcium homeostasis. Hum Mol Genet 2007; 16(1):61-77.
    • (2007) Hum Mol Genet , vol.16 , Issue.1 , pp. 61-77
    • Rockabrand, E.1    Slepko, N.2    Pantalone, A.3
  • 88
    • 11144353613 scopus 로고    scopus 로고
    • Pallos Jet al. SUMO modification of Huntingtin and Huntington's disease pathology
    • Steffan JS, AgrawalN, Pallos Jet al. SUMO modification of Huntingtin and Huntington's disease pathology. Science 2004; 304(5667):100-104.
    • (2004) Science , vol.304 , Issue.5667 , pp. 100-104
    • Steffan, J.S.1    Agrawal, N.2
  • 89
    • 33745627659 scopus 로고    scopus 로고
    • Palmitoylation ofhuntingtin by HIP14 is essential for its trafficking and function
    • Yanai A, Huang K, Kang R et al. Palmitoylation ofhuntingtin by HIP14 is essential for its trafficking and function. Nat Neurosci 2006; 9(6):824-831.
    • (2006) Nat Neurosci , vol.9 , Issue.6 , pp. 824-831
    • Yanai, A.1    Huang, K.2    Kang, R.3
  • 90
    • 63049132756 scopus 로고    scopus 로고
    • Acetylation targets mutant huntingtin to autophagosomes for degradation
    • Jeong H, Then F, Melia TJ Jr et al. Acetylation targets mutant huntingtin to autophagosomes for degradation. Cell 2009; 137(1):60-72.
    • (2009) Cell , vol.137 , Issue.1 , pp. 60-72
    • Jeong, H.1    Then, F.2    Melia Jr., T.J.3
  • 91
    • 0036083379 scopus 로고    scopus 로고
    • The IGF-1/Akt pathway is neuroprotective in Huntington's disease and involves Huntingtin phosphorylation by Akt
    • Humbert S, Bryson EA, Cordelieres FP et al. The IGF-1/Akt pathway is neuroprotective in Huntington's disease and involves Huntingtin phosphorylation by Akt. Dev Cell 2002; 2(6):831-837.
    • (2002) Dev Cell , vol.2 , Issue.6 , pp. 831-837
    • Humbert, S.1    Bryson, E.A.2    Cordelieres, F.P.3
  • 92
    • 0842265636 scopus 로고    scopus 로고
    • The serum- and glucocorticoid-induced kinase SGK inhibits mutant huntingtin-induced toxicity by phosphorylating serine 421 of huntingtin
    • Rangone H, Poizat G, Troncoso J et al. The serum- and glucocorticoid-induced kinase SGK inhibits mutant huntingtin-induced toxicity by phosphorylating serine 421 of huntingtin. Eur J Neurosci 2004; 19(2):273-279.
    • (2004) Eur J Neurosci , vol.19 , Issue.2 , pp. 273-279
    • Rangone, H.1    Poizat, G.2    Troncoso, J.3
  • 93
    • 77955643169 scopus 로고    scopus 로고
    • Molecular mechanisms and potential therapeutical targets in Huntington's disease
    • Zuccato C, Valenza M, Cattaneo E. Molecular mechanisms and potential therapeutical targets in Huntington's disease. Physiol Rev 2010; 90(3):905-981.
    • (2010) Physiol Rev , vol.90 , Issue.3 , pp. 905-981
    • Zuccato, C.1    Valenza, M.2    Cattaneo, E.3
  • 94
    • 1242338856 scopus 로고    scopus 로고
    • Huntingtin-protein interactions and the pathogenesis of Huntington's disease
    • Li SH, Li XJ. Huntingtin-protein interactions and the pathogenesis of Huntington's disease. Trends Genet 2004; 20(3):146-154.
    • (2004) Trends Genet , vol.20 , Issue.3 , pp. 146-154
    • Li, S.H.1    Li, X.J.2
  • 95
    • 0034094873 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegeneration
    • Zoghbi HY, Orr HT. Glutamine repeats and neurodegeneration. Annu Rev Neurosci 2000; 23:217-247.
    • (2000) Annu Rev Neurosci , vol.23 , pp. 217-247
    • Zoghbi, H.Y.1    Orr, H.T.2
  • 96
    • 0034110465 scopus 로고    scopus 로고
    • Expanded polyglutamine peptides alone are intrinsically cytotoxic and cause neurodegeneration in Drosophila
    • Marsh JL, Walker H, Theisen H et al. Expanded polyglutamine peptides alone are intrinsically cytotoxic and cause neurodegeneration in Drosophila. Hum Mol Genet 2000; 9(1):13-25.
    • (2000) Hum Mol Genet , vol.9 , Issue.1 , pp. 13-25
    • Marsh, J.L.1    Walker, H.2    Theisen, H.3
  • 97
    • 84993912315 scopus 로고
    • Increased apoptosis and early embryonic lethality in mice nullizygous for the Huntington's disease gene homologue
    • Zeitlin S, Liu JP, Chapman DL et al. Increased apoptosis and early embryonic lethality in mice nullizygous for the Huntington's disease gene homologue. Nat Genet 1995; 11(2):155-163.
    • (1995) Nat Genet , vol.11 , Issue.2 , pp. 155-163
    • Zeitlin, S.1    Liu, J.P.2    Chapman, D.L.3
  • 98
    • 0033757718 scopus 로고    scopus 로고
    • Inactivation of Hdh in the brain and testis results in progressive neurodegeneration and sterility in mice
    • Dragatsis I, Levine MS, Zeitlin S. Inactivation of Hdh in the brain and testis results in progressive neurodegeneration and sterility in mice. Nat Genet 2000; 26(3):300-306.
    • (2000) Nat Genet , vol.26 , Issue.3 , pp. 300-306
    • Dragatsis, I.1    Levine, M.S.2    Zeitlin, S.3
  • 99
    • 0035127907 scopus 로고    scopus 로고
    • Wild-type huntingtin reduces the cellular toxicity of mutant huntingtin in vivo
    • Leavitt BR, Guttman JA, Hodgson JG et al. Wild-type huntingtin reduces the cellular toxicity of mutant huntingtin in vivo. Am J Hum Genet 2001; 68(2):313-324.
    • (2001) Am J Hum Genet , vol.68 , Issue.2 , pp. 313-324
    • Leavitt, B.R.1    Guttman, J.A.2    Hodgson, J.G.3
  • 100
    • 33846576161 scopus 로고    scopus 로고
    • Wild-type huntingtin ameliorates striatal neuronal atrophy but does not prevent other abnormalities in the YAC128 mouse model of Huntington disease
    • Van Raamsdonk JM, Pearson J, Murphy Z et al. Wild-type huntingtin ameliorates striatal neuronal atrophy but does not prevent other abnormalities in the YAC128 mouse model of Huntington disease. BMC Neurosci 2006; 7:80.
    • (2006) BMC Neurosci , vol.7 , pp. 80
    • Van Raamsdonk, J.M.1    Pearson, J.2    Murphy, Z.3
  • 101
    • 33645100553 scopus 로고    scopus 로고
    • Wild-type huntingtin protects neurons from excitotoxicity
    • Leavitt BR, van Raamsdonk JM, Shehadeh J et al. Wild-type huntingtin protects neurons from excitotoxicity. J Neurochem 2006; 96(4):1121-1129.
    • (2006) J Neurochem , vol.96 , Issue.4 , pp. 1121-1129
    • Leavitt, B.R.1    Van Raamsdonk, J.M.2    Shehadeh, J.3
  • 102
    • 0034933959 scopus 로고    scopus 로고
    • Wild type Huntingtin reduces the cellular toxicity of mutant Huntingtin in mammalian cell models of Huntington's disease
    • Ho LW, Brown R, Maxwell M et al. Wild type Huntingtin reduces the cellular toxicity of mutant Huntingtin in mammalian cell models of Huntington's disease. J Med Genet 2001; 38(7):450-452.
    • (2001) J Med Genet , vol.38 , Issue.7 , pp. 450-452
    • Ho, L.W.1    Brown, R.2    Maxwell, M.3
  • 103
    • 0141926491 scopus 로고    scopus 로고
    • Mutant huntingtin promotes the fibrillogenesis of wild-type huntingtin: A potential mechanism for loss of huntingtin function in Huntington's disease
    • Busch A, Engemann S, Lurz R et al. Mutant huntingtin promotes the fibrillogenesis of wild-type huntingtin: a potential mechanism for loss of huntingtin function in Huntington's disease. J Biol Chem 2003; 278(42):41452-41461.
    • (2003) J Biol Chem , vol.278 , Issue.42 , pp. 41452-41461
    • Busch, A.1    Engemann, S.2    Lurz, R.3
  • 104
    • 0032517816 scopus 로고    scopus 로고
    • Recruitment and the role of nuclear localization in polyglutamine- mediated aggregation
    • Perez MK, Paulson HL, Pendse SJ et al. Recruitment and the role of nuclear localization in polyglutamine-mediated aggregation. J Cell Biol 1998; 143(6):1457-1470.
    • (1998) J Cell Biol , vol.143 , Issue.6 , pp. 1457-1470
    • Perez, M.K.1    Paulson, H.L.2    Pendse, S.J.3
  • 105
    • 0033613212 scopus 로고    scopus 로고
    • Insoluble detergent-resistant aggregates form between pathological and nonpathological lengths of polyglutamine in mammalian cells
    • Kazantsev A, Preisinger E, Dranovsky A et al. Insoluble detergent-resistant aggregates form between pathological and nonpathological lengths of polyglutamine in mammalian cells. Proc Natl Acad Sci U S A 1999; 96(20):11404-11409.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , Issue.20 , pp. 11404-11409
    • Kazantsev, A.1    Preisinger, E.2    Dranovsky, A.3
  • 106
    • 12944263711 scopus 로고    scopus 로고
    • The Huntington's disease protein interacts with p53 and CREB-binding protein and represses transcription
    • Steffan JS, Kazantsev A, Spasic-Boskovic O et al. The Huntington's disease protein interacts with p53 and CREB-binding protein and represses transcription. Proc Natl Acad Sci U S A 2000; 97(12):6763-6768.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , Issue.12 , pp. 6763-6768
    • Steffan, J.S.1    Kazantsev, A.2    Spasic-Boskovic, O.3
  • 107
    • 0035852687 scopus 로고    scopus 로고
    • The Gln-Ala repeat transcriptional activator CA150 interacts with huntingtin: Neuropathologic and genetic evidence for a role in Huntington's disease pathogenesis
    • Holbert S, Denghien I, Kiechle T et al. The Gln-Ala repeat transcriptional activator CA150 interacts with huntingtin: neuropathologic and genetic evidence for a role in Huntington's disease pathogenesis. Proc Natl Acad Sci U S A 2001; 98(4):1811-1816.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , Issue.4 , pp. 1811-1816
    • Holbert, S.1    Denghien, I.2    Kiechle, T.3
  • 108
    • 0035976953 scopus 로고    scopus 로고
    • The role of protein composition in specifying nuclear inclusion formation in polyglutamine disease
    • Chai Y, Wu L, Griffin JD et al. The role of protein composition in specifying nuclear inclusion formation in polyglutamine disease. J Biol Chem 2001; 276(48):44889-44897.
    • (2001) J Biol Chem , vol.276 , Issue.48 , pp. 44889-44897
    • Chai, Y.1    Wu, L.2    Griffin, J.D.3
  • 109
    • 0036797242 scopus 로고    scopus 로고
    • Polyglutamine protein aggregates are dynamic
    • Kim S, Nollen EA, Kitagawa K et al. Polyglutamine protein aggregates are dynamic. Nat Cell Biol 2002; 4(10):826-831.
    • (2002) Nat Cell Biol , vol.4 , Issue.10 , pp. 826-831
    • Kim, S.1    Nollen, E.A.2    Kitagawa, K.3
  • 110
    • 33644850056 scopus 로고    scopus 로고
    • Progressive disruption of cellular protein folding in models of polyglutamine diseases
    • Gidalevitz T, Ben-Zvi A, Ho KH et al. Progressive disruption of cellular protein folding in models of polyglutamine diseases. Science 2006; 311(5766):1471-1474.
    • (2006) Science , vol.311 , Issue.5766 , pp. 1471-1474
    • Gidalevitz, T.1    Ben-Zvi, A.2    Ho, K.H.3
  • 111
    • 59249106080 scopus 로고    scopus 로고
    • Integrating the stress response: Lessons for neurodegenerative diseases from C. elegans
    • Prahlad V, Morimoto RI. Integrating the stress response: lessons for neurodegenerative diseases from C. elegans. Trends Cell Biol 2009; 19(2):52-61.
    • (2009) Trends Cell Biol , vol.19 , Issue.2 , pp. 52-61
    • Prahlad, V.1    Morimoto, R.I.2
  • 112
    • 13944275615 scopus 로고    scopus 로고
    • Polyglutamine expansion of huntingtin impairs its nuclear export
    • Cornett J, Cao F, Wang CE et al. Polyglutamine expansion of huntingtin impairs its nuclear export. Nat Genet 2005; 37(2):198-204.
    • (2005) Nat Genet , vol.37 , Issue.2 , pp. 198-204
    • Cornett, J.1    Cao, F.2    Wang, C.E.3
  • 113
    • 1542267796 scopus 로고    scopus 로고
    • Cytoplasmic aggregates trap polyglutamine-containing proteins and block axonal transport in a Drosophila model of Huntington's disease
    • Lee WC, Yoshihara M, Littleton JT. Cytoplasmic aggregates trap polyglutamine-containing proteins and block axonal transport in a Drosophila model of Huntington's disease. Proc Natl Acad Sci U S A 2004; 101(9):3224-3229.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , Issue.9 , pp. 3224-3229
    • Lee, W.C.1    Yoshihara, M.2    Littleton, J.T.3
  • 114
    • 37449011119 scopus 로고    scopus 로고
    • Corticostriatal synaptic function in mouse models of Huntington's disease: Early effects of huntingtin repeat length and protein load
    • Milnerwood AJ, Raymond LA. Corticostriatal synaptic function in mouse models of Huntington's disease: early effects of huntingtin repeat length and protein load. J Physiol 2007; 585(Pt 3):817-831.
    • (2007) J Physiol , vol.585 , Issue.PART 3 , pp. 817-831
    • Milnerwood, A.J.1    Raymond, L.A.2
  • 115
    • 3042717240 scopus 로고    scopus 로고
    • Cellular toxicity of polyglutamine expansion proteins: Mechanism of transcription factor deactivation
    • Schaffar G, Breuer P, Boteva R et al. Cellular toxicity of polyglutamine expansion proteins: mechanism of transcription factor deactivation. Mol Cell 2004; 15(1):95-105.
    • (2004) Mol Cell , vol.15 , Issue.1 , pp. 95-105
    • Schaffar, G.1    Breuer, P.2    Boteva, R.3
  • 116
    • 0036716277 scopus 로고    scopus 로고
    • Androgen receptor with elongated polyglutamine tract forms aggregates that alter axonal trafficking and mitochondrial distribution in motor neuronal processes
    • Piccioni F, Pinton P, Simeoni S et al. Androgen receptor with elongated polyglutamine tract forms aggregates that alter axonal trafficking and mitochondrial distribution in motor neuronal processes. FASEB J 2002; 16(11):1418-1420.
    • (2002) FASEB J , vol.16 , Issue.11 , pp. 1418-1420
    • Piccioni, F.1    Pinton, P.2    Simeoni, S.3
  • 117
    • 0041656292 scopus 로고    scopus 로고
    • The hunt for huntingtin function: Interaction partners tell many different stories
    • Harjes P, Wanker EE. The hunt for huntingtin function: interaction partners tell many different stories. Trends Biochem Sci 2003; 28(8):425-433.
    • (2003) Trends Biochem Sci , vol.28 , Issue.8 , pp. 425-433
    • Harjes, P.1    Wanker, E.E.2
  • 118
    • 33847302564 scopus 로고    scopus 로고
    • Wild-type huntingtin participates in protein trafficking between the Golgi and the extracellular space
    • Strehlow AN, Li JZ, Myers RM. Wild-type huntingtin participates in protein trafficking between the Golgi and the extracellular space. Hum Mol Genet 2007; 16(4):391-409.
    • (2007) Hum Mol Genet , vol.16 , Issue.4 , pp. 391-409
    • Strehlow, A.N.1    Li, J.Z.2    Myers, R.M.3
  • 119
    • 0034125918 scopus 로고    scopus 로고
    • Poly-L-glutamine forms cation channels: Relevance to the pathogenesis of the polyglutamine diseases
    • Monoi H, Futaki S, Kugimiya S et al. Poly-L-glutamine forms cation channels: relevance to the pathogenesis of the polyglutamine diseases. Biophys J 2000; 78(6):2892-2899.
    • (2000) Biophys J , vol.78 , Issue.6 , pp. 2892-2899
    • Monoi, H.1    Futaki, S.2    Kugimiya, S.3
  • 120
    • 33645104605 scopus 로고    scopus 로고
    • Interaction of huntingtin fragments with brain membranes - Clues to early dysfunction in Huntington's disease
    • Suopanki J, Gotz C, Lutsch G et al. Interaction of huntingtin fragments with brain membranes - clues to early dysfunction in Huntington's disease. J Neurochem 2006; 96(3):870-884.
    • (2006) J Neurochem , vol.96 , Issue.3 , pp. 870-884
    • Suopanki, J.1    Gotz, C.2    Lutsch, G.3
  • 121
    • 59649095699 scopus 로고    scopus 로고
    • Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates
    • Ren P-H, Lauckner JE, Kachirskaia I et al. Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates. Nat Cell Biol 2009; 11(2):219-225.
    • (2009) Nat Cell Biol , vol.11 , Issue.2 , pp. 219-225
    • Ren, P.-H.1    Lauckner, J.E.2    Kachirskaia, I.3
  • 122
    • 68949219079 scopus 로고    scopus 로고
    • Polyglutamine expansion in huntingtin alters its interaction with phospholipids
    • Kegel KB, Sapp E, Alexander J et al. Polyglutamine expansion in huntingtin alters its interaction with phospholipids. J Neurochem 2009; 110(5):1585-1597.
    • (2009) J Neurochem , vol.110 , Issue.5 , pp. 1585-1597
    • Kegel, K.B.1    Sapp, E.2    Alexander, J.3
  • 123
    • 68249127932 scopus 로고    scopus 로고
    • Polyglutamine expansion in huntingtin increases its insertion into lipid bilayers
    • Kegel KB, Schewkunow V, Sapp E et al. Polyglutamine expansion in huntingtin increases its insertion into lipid bilayers. Biochem Biophys Res Commun 2009; 387(3):472-475.
    • (2009) Biochem Biophys Res Commun , vol.387 , Issue.3 , pp. 472-475
    • Kegel, K.B.1    Schewkunow, V.2    Sapp, E.3
  • 124
    • 0036415838 scopus 로고    scopus 로고
    • Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular andtubular protofibrils
    • Lashuel HA, Petre BM, Wall J et al. Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular andtubular protofibrils. J Mol Biol 2002; 322(5):1089-1102.
    • (2002) J Mol Biol , vol.322 , Issue.5 , pp. 1089-1102
    • Lashuel, H.A.1    Petre, B.M.2    Wall, J.3
  • 125
    • 33749633639 scopus 로고    scopus 로고
    • Modeling polyglutamine pathogenesis in C. elegans
    • Brignull HR, Morley JF, Garcia SM et al. Modeling polyglutamine pathogenesis in C. elegans. Methods Enzymol 2006; 412:256-282.
    • (2006) Methods Enzymol , vol.412 , pp. 256-282
    • Brignull, H.R.1    Morley, J.F.2    Garcia, S.M.3
  • 126
    • 84864290342 scopus 로고    scopus 로고
    • Normal aging modulates the neurotoxicity of mutant huntingtin
    • Diguet E, Petit F, Escartin C et al. Normal aging modulates the neurotoxicity of mutant huntingtin. PLoS One 2009; 4(2):e4637.
    • (2009) PLoS One , vol.4 , Issue.2
    • Diguet, E.1    Petit, F.2    Escartin, C.3
  • 127
    • 77956795163 scopus 로고    scopus 로고
    • Widespread protein aggregation as an inherent part of aging in C. elegans
    • David DC, Ollikainen N, Trinidad JC et al. Widespread protein aggregation as an inherent part of aging in C. elegans. PLoS Biol 2010; 8(8):e1000450.
    • (2010) PLoS Biol , vol.8 , Issue.8
    • David, D.C.1    Ollikainen, N.2    Trinidad, J.C.3
  • 128
    • 23344436560 scopus 로고    scopus 로고
    • Regulation ofheat shock gene transcription in neuronal cells
    • Tonkiss J, Calderwood SK. Regulation ofheat shock gene transcription in neuronal cells. Int J Hyperthermia 2005; 21(5):433-444.
    • (2005) Int J Hyperthermia , vol.21 , Issue.5 , pp. 433-444
    • Tonkiss, J.1    Calderwood, S.K.2
  • 129
    • 0034232418 scopus 로고    scopus 로고
    • Regulation of lamp2a levels in the lysosomal membrane
    • Cuervo AM, Dice JF. Regulation of lamp2a levels in the lysosomal membrane. Traffic 2000; l(7):570-583.
    • (2000) Traffic , vol.1 , Issue.7 , pp. 570-583
    • Cuervo, A.M.1    Dice, J.F.2
  • 130
    • 57749116408 scopus 로고    scopus 로고
    • Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity
    • DuennwaldML, Lindquist S. Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity. Genes Dev 2008; 22(23):3308-3319.
    • (2008) Genes Dev , vol.22 , Issue.23 , pp. 3308-3319
    • Duennwald, M.L.1    Lindquist, S.2
  • 131
    • 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 NR, Zemskov EA, Wang G et al. Altered proteasomal function due to the expression of polyglutamine-expanded truncated N-terminal huntingtin induces apoptosis by caspase activation through mitochondrial cytochrome c release. Hum Mol Genet 2001; 10(10):1049-1059.
    • (2001) Hum Mol Genet , vol.10 , Issue.10 , pp. 1049-1059
    • Jana, N.R.1    Zemskov, E.A.2    Wang, G.3
  • 132
    • 49349090155 scopus 로고    scopus 로고
    • Huntington's disease: Degradation of mutant huntingtin by autophagy
    • Sarkar S, Rubinsztein DC. Huntington's disease: degradation of mutant huntingtin by autophagy. FEBS J 2008; 275(17):4263-4270.
    • (2008) FEBS J , vol.275 , Issue.17 , pp. 4263-4270
    • Sarkar, S.1    Rubinsztein, D.C.2
  • 133
    • 77955291545 scopus 로고    scopus 로고
    • Inhibiting the ubiquitin-proteasome system leads to preferential accumulation of toxic N-terminal mutant huntingtin fragments
    • Li X, Wang CE, Huang S et al. Inhibiting the ubiquitin-proteasome system leads to preferential accumulation of toxic N-terminal mutant huntingtin fragments. Hum Mol Genet 2010; 19(12):2445-2455.
    • (2010) Hum Mol Genet , vol.19 , Issue.12 , pp. 2445-2455
    • Li, X.1    Wang, C.E.2    Huang, S.3
  • 134
    • 0141987860 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neurodegenerative diseases: Sometimes the chicken, sometimes the egg
    • Ciechanover A, Brundin P. The ubiquitin proteasome system in neurodegenerative diseases: sometimes the chicken, sometimes the egg. Neuron 2003; 40(2):427-446.
    • (2003) Neuron , vol.40 , Issue.2 , pp. 427-446
    • Ciechanover, A.1    Brundin, P.2
  • 135
    • 0035862754 scopus 로고    scopus 로고
    • Expression of expanded repeat androgen receptor produces neurologic disease in transgenic mice
    • Abel A, Walcott J, Woods J et al. Expression of expanded repeat androgen receptor produces neurologic disease in transgenic mice. Hum Mol Genet 2001; 10(2):107-116.
    • (2001) Hum Mol Genet , vol.10 , Issue.2 , pp. 107-116
    • Abel, A.1    Walcott, J.2    Woods, J.3
  • 136
    • 0032945938 scopus 로고    scopus 로고
    • Polyglutamine-expanded androgen receptors form aggregates that sequester heat shock proteins, proteasome components, and SRC-1, and are suppressed by the HDJ-2 chaperone
    • Stenoien DL, Cummings CJ, Adams HP et al. Polyglutamine-expanded androgen receptors form aggregates that sequester heat shock proteins, proteasome components, and SRC-1, and are suppressed by the HDJ-2 chaperone. Hum Mol Genet 1999; 8(5):731-741.
    • (1999) Hum Mol Genet , vol.8 , Issue.5 , pp. 731-741
    • Stenoien, D.L.1    Cummings, C.J.2    Adams, H.P.3
  • 137
    • 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 et al. Purification of polyglutamine aggregates and identification of elongation factor-1alpha and heat shock protein 84 as aggregate-interacting proteins. J Neurosci 2002; 22(21):9267-9277.
    • (2002) J Neurosci , vol.22 , Issue.21 , pp. 9267-9277
    • Mitsui, K.1    Nakayama, H.2    Akagi, T.3
  • 138
    • 33746487396 scopus 로고    scopus 로고
    • Expanded polyglutamines impair synaptic transmission and ubiquitin-proteasome system in Caenorhabditis elegans
    • Khan LA, Bauer PO, Miyazaki H et al. Expanded polyglutamines impair synaptic transmission and ubiquitin-proteasome system in Caenorhabditis elegans. J Neurochem 2006; 98(2):576-587.
    • (2006) J Neurochem , vol.98 , Issue.2 , pp. 576-587
    • Khan, L.A.1    Bauer, P.O.2    Miyazaki, H.3
  • 139
    • 14644419638 scopus 로고    scopus 로고
    • Neuronal dysfunction in a polyglutamine disease model occurs in the absence of ubiquitin-proteasome system impairment and inversely correlates with the degree of nuclear inclusion formation
    • Bowman AB, Yoo SY, Dantuma NP et al. Neuronal dysfunction in a polyglutamine disease model occurs in the absence of ubiquitin-proteasome system impairment and inversely correlates with the degree of nuclear inclusion formation. Hum Mol Genet 2005; 14(5):679-691.
    • (2005) Hum Mol Genet , vol.14 , Issue.5 , pp. 679-691
    • Bowman, A.B.1    Yoo, S.Y.2    Dantuma, N.P.3
  • 140
    • 65249181587 scopus 로고    scopus 로고
    • The ubiquitin-proteasome reporter GFPu does not accumulate in neurons of the R6/2 transgenic mouse model of Huntington's disease
    • Bett JS, Cook C, Petrucelli L et al. The ubiquitin-proteasome reporter GFPu does not accumulate in neurons of the R6/2 transgenic mouse model of Huntington's disease. PLoS One 2009; 4(4):e5128.
    • (2009) PLoS One , vol.4 , Issue.4
    • Bett, J.S.1    Cook, C.2    Petrucelli, L.3
  • 141
    • 41549129945 scopus 로고    scopus 로고
    • Impaired ubiquitin-proteasome system activity in the synapses of Huntington's disease mice
    • Wang J, Wang CE, Orr A et al. Impaired ubiquitin-proteasome system activity in the synapses of Huntington's disease mice. J Cell Biol 2008; 180(6):1177-1189.
    • (2008) J Cell Biol , vol.180 , Issue.6 , pp. 1177-1189
    • Wang, J.1    Wang, C.E.2    Orr, A.3
  • 142
    • 0032727617 scopus 로고    scopus 로고
    • Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70
    • Warrick JM, Chan HY, Gray-Board GL et al. Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70. Nat Genet 1999; 23(4):425-428.
    • (1999) Nat Genet , vol.23 , Issue.4 , pp. 425-428
    • Warrick, J.M.1    Chan, H.Y.2    Gray-Board, G.L.3
  • 143
    • 0033499931 scopus 로고    scopus 로고
    • Analysis of the role of heat shock protein (Hsp) molecular chaperones in polyglutamine disease
    • Chai Y, Koppenhafer SL, Bonini NM et al. Analysis of the role of heat shock protein (Hsp) molecular chaperones in polyglutamine disease. J Neurosci 1999; 19(23):10338-10347.
    • (1999) J Neurosci , vol.19 , Issue.23 , pp. 10338-10347
    • Chai, Y.1    Koppenhafer, S.L.2    Bonini, N.M.3
  • 144
    • 78649685457 scopus 로고    scopus 로고
    • Hsp70 and Hsp40 functionally interact with soluble mutant huntingtin oligomers in a classic ATP-dependent reaction cycle
    • Lotz GP, Legleiter J, Aron R et al. Hsp70 and Hsp40 functionally interact with soluble mutant huntingtin oligomers in a classic ATP-dependent reaction cycle. J Biol Chem 2010.
    • (2010) J Biol Chem
    • Lotz, G.P.1    Legleiter, J.2    Aron, R.3
  • 145
    • 33748561495 scopus 로고    scopus 로고
    • Chaperonin TRiC promotes the assembly of polyQ expansion proteins into nontoxic oligomers
    • Behrends C, Langer CA, Boteva R et al. Chaperonin TRiC promotes the assembly of polyQ expansion proteins into nontoxic oligomers. Mol Cell 2006; 23(6):887-897.
    • (2006) Mol Cell , vol.23 , Issue.6 , pp. 887-897
    • Behrends, C.1    Langer, C.A.2    Boteva, R.3
  • 146
    • 78649250124 scopus 로고    scopus 로고
    • Early alterations of autophagy in Huntington disease-like mice
    • Heng MY, Detloff PJ, Paulson HL et al. Early alterations of autophagy in Huntington disease-like mice. Autophagy 2010; 6(8):1206-1208.
    • (2010) Autophagy , vol.6 , Issue.8 , pp. 1206-1208
    • Heng, M.Y.1    Detloff, P.J.2    Paulson, H.L.3
  • 147
    • 77956268597 scopus 로고    scopus 로고
    • The evolutionarily conserved interaction between LC3 and p62 selectively mediates autophagy-dependent degradation ofmutant huntingtin
    • Tung YT, Hsu WM, Lee H et al. The evolutionarily conserved interaction between LC3 and p62 selectively mediates autophagy-dependent degradation ofmutant huntingtin. Cell Mol Neurobiol 2010; 30(5):795-806.
    • (2010) Cell Mol Neurobiol , vol.30 , Issue.5 , pp. 795-806
    • Tung, Y.T.1    Hsu, W.M.2    Lee, H.3
  • 148
    • 77951665859 scopus 로고    scopus 로고
    • Cargo recognition failure is responsible for inefficient autophagy in Huntington's disease
    • Martinez-Vicente M, Talloczy Z, Wong E et al. Cargo recognition failure is responsible for inefficient autophagy in Huntington's disease. Nat Neurosci 2010; 13(5):567-576.
    • (2010) Nat Neurosci , vol.13 , Issue.5 , pp. 567-576
    • Martinez-Vicente, M.1    Talloczy, Z.2    Wong, E.3
  • 149
    • 2642586352 scopus 로고    scopus 로고
    • Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease
    • Ravikumar B, Vacher C, Berger Z et al. Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease. Nat Genet 2004; 36(6):585-595.
    • (2004) Nat Genet , vol.36 , Issue.6 , pp. 585-595
    • Ravikumar, B.1    Vacher, C.2    Berger, Z.3
  • 150
    • 33745192802 scopus 로고    scopus 로고
    • Suppression ofbasal autophagy in neural cells causes neurodegenerative disease in mice
    • Hara T, Nakamura K, Matsui M et al. Suppression ofbasal autophagy in neural cells causes neurodegenerative disease in mice. Nature 2006; 441(7095):885-889.
    • (2006) Nature , vol.441 , Issue.7095 , pp. 885-889
    • Hara, T.1    Nakamura, K.2    Matsui, M.3
  • 151
    • 33646800306 scopus 로고    scopus 로고
    • Loss of autophagy in the central nervous system causes neurodegeneration in mice
    • Komatsu M, Waguri S, Chiba T et al. Loss of autophagy in the central nervous system causes neurodegeneration in mice. Nature 2006; 441(7095):880-884.
    • (2006) Nature , vol.441 , Issue.7095 , pp. 880-884
    • Komatsu, M.1    Waguri, S.2    Chiba, T.3
  • 152
    • 77957565855 scopus 로고    scopus 로고
    • Age at onset in Huntington's disease is modified by the autophagy pathway: Implication of the V471A polymorphism in Atg7
    • Metzger S, Saukko M, Van Che H et al. Age at onset in Huntington's disease is modified by the autophagy pathway: implication of the V471A polymorphism in Atg7. Hum Genet 2010; 128(4):453-459.
    • (2010) Hum Genet , vol.128 , Issue.4 , pp. 453-459
    • Metzger, S.1    Saukko, M.2    Van Che, H.3
  • 153
    • 0034307476 scopus 로고    scopus 로고
    • Huntingtin expression stimulates endosomal-lysosomal activity, endosome tubulation, and autophagy
    • Kegel KB, Kim M, Sapp E et al. Huntingtin expression stimulates endosomal-lysosomal activity, endosome tubulation, and autophagy. J Neurosci 2000; 20(19):7268-7278.
    • (2000) J Neurosci , vol.20 , Issue.19 , pp. 7268-7278
    • Kegel, K.B.1    Kim, M.2    Sapp, E.3
  • 154
    • 0030771894 scopus 로고    scopus 로고
    • Huntingtin localization in brains of normal and Huntington's disease patients
    • Sapp E, Schwarz C, Chase K et al. Huntingtin localization in brains of normal and Huntington's disease patients. Ann Neurol 1997; 42(4):604-612.
    • (1997) Ann Neurol , vol.42 , Issue.4 , pp. 604-612
    • Sapp, E.1    Schwarz, C.2    Chase, K.3
  • 155
  • 156
    • 0036792019 scopus 로고    scopus 로고
    • Involvement of lysosomes in the pathogenesis of CAG repeat diseases
    • Yamada M, Tsuji S, Takahashi H. Involvement of lysosomes in the pathogenesis of CAG repeat diseases. Ann Neurol 2002; 52(4):498-503.
    • (2002) Ann Neurol , vol.52 , Issue.4 , pp. 498-503
    • Yamada, M.1    Tsuji, S.2    Takahashi, H.3
  • 157
    • 72149124383 scopus 로고    scopus 로고
    • IKK phosphorylates Huntingtin and targets it for degradation by the proteasome and lysosome
    • Thompson LM, Aiken CT, Kaltenbach LS et al. IKK phosphorylates Huntingtin and targets it for degradation by the proteasome and lysosome. J Cell Biol 2009; 187(7):1083-1099.
    • (2009) J Cell Biol , vol.187 , Issue.7 , pp. 1083-1099
    • Thompson, L.M.1    Aiken, C.T.2    Kaltenbach, L.S.3
  • 158
    • 4344659685 scopus 로고    scopus 로고
    • Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy
    • Cuervo AM, Stefanis L, Fredenburg R et al. Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy. Science 2004; 305(5688):1292-1295.
    • (2004) Science , vol.305 , Issue.5688 , pp. 1292-1295
    • Cuervo, A.M.1    Stefanis, L.2    Fredenburg, R.3
  • 159
    • 45749147456 scopus 로고    scopus 로고
    • RNA toxicity is a component of ataxin-3 degeneration in Drosophila
    • Li LB, Yu Z, Teng X et al. RNA toxicity is a component of ataxin-3 degeneration in Drosophila. Nature 2008; 453(7198):1107-1111.
    • (2008) Nature , vol.453 , Issue.7198 , pp. 1107-1111
    • Li, L.B.1    Yu, Z.2    Teng, X.3
  • 160
    • 0034622926 scopus 로고    scopus 로고
    • Myotonic dystrophy in transgenic mice expressing an expanded CUG repeat
    • Mankodi A, Logigian E, Callahan L et al. Myotonic dystrophy in transgenic mice expressing an expanded CUG repeat. Science 2000; 289(5485):1769-1773.
    • (2000) Science , vol.289 , Issue.5485 , pp. 1769-1773
    • Mankodi, A.1    Logigian, E.2    Callahan, L.3
  • 161
    • 0032837677 scopus 로고    scopus 로고
    • Cis and trans effects of the myotonic dystrophy (DM) mutation in a cell culture model
    • Amack JD, Paguio AP, Mahadevan MS. Cis and trans effects of the myotonic dystrophy (DM) mutation in a cell culture model. Hum Mol Genet 1999; 8(11):1975-1984.
    • (1999) Hum Mol Genet , vol.8 , Issue.11 , pp. 1975-1984
    • Amack, J.D.1    Paguio, A.P.2    Mahadevan, M.S.3
  • 162
    • 0034873099 scopus 로고    scopus 로고
    • Aberrant regulation of insulin receptor alternative splicing is associated with insulin resistance in myotonic dystrophy
    • Savkur RS, Philips AV, Cooper TA. Aberrant regulation of insulin receptor alternative splicing is associated with insulin resistance in myotonic dystrophy. Nat Genet 2001; 29(1):40-47.
    • (2001) Nat Genet , vol.29 , Issue.1 , pp. 40-47
    • Savkur, R.S.1    Philips, A.V.2    Cooper, T.A.3
  • 163
    • 0036347525 scopus 로고    scopus 로고
    • Expanded CUG repeats trigger aberrant splicing of ClC-1 chloride channel pre-mRNA and hyperexcitability of skeletal muscle in myotonic dystrophy
    • Mankodi A, Takahashi MP, Jiang H et al. Expanded CUG repeats trigger aberrant splicing of ClC-1 chloride channel pre-mRNA and hyperexcitability of skeletal muscle in myotonic dystrophy. Mol Cell 2002; 10(1):35-44.
    • (2002) Mol Cell , vol.10 , Issue.1 , pp. 35-44
    • Mankodi, A.1    Takahashi, M.P.2    Jiang, H.3
  • 164
    • 0028947317 scopus 로고
    • Foci of trinucleotide repeat transcripts in nuclei of myotonic dystrophy cells and tissues
    • Taneja KL, McCurrach M, Schalling M et al. Foci of trinucleotide repeat transcripts in nuclei of myotonic dystrophy cells and tissues. J Cell Biol 1995; 128(6):995-1002.
    • (1995) J Cell Biol , vol.128 , Issue.6 , pp. 995-1002
    • Taneja, K.L.1    McCurrach, M.2    Schalling, M.3
  • 165
    • 0035800434 scopus 로고    scopus 로고
    • Myotonic dystrophy type 2 caused by a CCTG expansion in intron 1 of ZNF9
    • Liquori CL, Ricker K, Moseley ML et al. Myotonic dystrophy type 2 caused by a CCTG expansion in intron 1 of ZNF9. Science 2001; 293(5531):864-867.
    • (2001) Science , vol.293 , Issue.5531 , pp. 864-867
    • Liquori, C.L.1    Ricker, K.2    Moseley, M.L.3
  • 166
    • 0032900772 scopus 로고    scopus 로고
    • An untranslated CTG expansion causes a novel form of spinocerebellar ataxia (SCA8)
    • Koob MD, Moseley ML, Schut LJ et al. An untranslated CTG expansion causes a novel form of spinocerebellar ataxia (SCA8). Nat Genet 1999; 21(4):379-384.
    • (1999) Nat Genet , vol.21 , Issue.4 , pp. 379-384
    • Koob, M.D.1    Moseley, M.L.2    Schut, L.J.3
  • 167
    • 0029099168 scopus 로고
    • Construction of human embryonic cDNA libraries: HD, PKD1 and BRCA1 are transcribed widely during embryogenesis
    • Buraczynska MJ, Van Keuren ML, Buraczynska KM et al. Construction of human embryonic cDNA libraries: HD, PKD1 and BRCA1 are transcribed widely during embryogenesis. Cytogenet Cell Genet 1995; 71(2):197-202.
    • (1995) Cytogenet Cell Genet , vol.71 , Issue.2 , pp. 197-202
    • Buraczynska, M.J.1    Van Keuren, M.L.2    Buraczynska, K.M.3
  • 168
    • 0032919205 scopus 로고    scopus 로고
    • Formation of polyglutamine inclusions in non-CNS tissue
    • Sathasivam K, Hobbs C, Turmaine M et al. Formation of polyglutamine inclusions in non-CNS tissue. Hum Mol Genet 1999; 8(5):813-822.
    • (1999) Hum Mol Genet , vol.8 , Issue.5 , pp. 813-822
    • Sathasivam, K.1    Hobbs, C.2    Turmaine, M.3
  • 169
    • 77950547307 scopus 로고    scopus 로고
    • Polyglutamine toxicity in non-neuronal cells
    • Bradford JW, Li S, Li XJ. Polyglutamine toxicity in non-neuronal cells. Cell Res 2010; 20(4):400-407.
    • (2010) Cell Res , vol.20 , Issue.4 , pp. 400-407
    • Bradford, J.W.1    Li, S.2    Li, X.J.3
  • 170
    • 10844273236 scopus 로고    scopus 로고
    • Progressive abnormalities in skeletal muscle and neuromuscular junctions of transgenic mice expressing the Huntington's disease mutation
    • Ribchester RR, Thomson D, Wood NI et al. Progressive abnormalities in skeletal muscle and neuromuscular junctions of transgenic mice expressing the Huntington's disease mutation. Eur J Neurosci 2004; 20(11):3092-3114.
    • (2004) Eur J Neurosci , vol.20 , Issue.11 , pp. 3092-3114
    • Ribchester, R.R.1    Thomson, D.2    Wood, N.I.3
  • 171
    • 0037002444 scopus 로고    scopus 로고
    • Huntington's disease of the endocrine pancreas: Insulin deficiency and diabetes mellitus due to impaired insulin gene expression
    • Andreassen OA, Dedeoglu A, Stanojevic V et al. Huntington's disease of the endocrine pancreas: insulin deficiency and diabetes mellitus due to impaired insulin gene expression. Neurobiol Dis 2002; 11(3): 410-424.
    • (2002) Neurobiol Dis , vol.11 , Issue.3 , pp. 410-424
    • Andreassen, O.A.1    Dedeoglu, A.2    Stanojevic, V.3
  • 172
    • 33846369453 scopus 로고    scopus 로고
    • Cardiac dysfunction in the R6/2 mouse model of Huntington's disease
    • Mihm MJ, Amann DM, Schanbacher BL et al. Cardiac dysfunction in the R6/2 mouse model of Huntington's disease. Neurobiol Dis 2007; 25(2):297-308.
    • (2007) Neurobiol Dis , vol.25 , Issue.2 , pp. 297-308
    • Mihm, M.J.1    Amann, D.M.2    Schanbacher, B.L.3
  • 173
    • 0033009587 scopus 로고    scopus 로고
    • Mice transgenic for an expanded CAG repeat in the Huntington's disease gene develop diabetes
    • Hurlbert MS, Zhou W, Wasmeier C et al. Mice transgenic for an expanded CAG repeat in the Huntington's disease gene develop diabetes. Diabetes 1999; 48(3):649-651.
    • (1999) Diabetes , vol.48 , Issue.3 , pp. 649-651
    • Hurlbert, M.S.1    Zhou, W.2    Wasmeier, C.3
  • 174
    • 77950547661 scopus 로고    scopus 로고
    • Formation of polyglutamine inclusions inawiderange ofnon-CNS tissues in the HdhQ150 knock-in mouse model of Huntington's disease
    • MoffittH, McPhail GD, Woodman B et al. Formation of polyglutamine inclusions inawiderange ofnon-CNS tissues in the HdhQ150 knock-in mouse model of Huntington's disease. PLoS One 2009; 4(11):e8025.
    • (2009) PLoS One , vol.4 , Issue.11
    • Moffitt, H.1    McPhail, G.D.2    Woodman, B.3
  • 175
    • 45549098712 scopus 로고    scopus 로고
    • Asymmetric mitosis: Unequal segregation of proteins destined for degradation
    • Fuentealba LC, Eivers E, Geissert D et al. Asymmetric mitosis: unequal segregation of proteins destined for degradation. Proc Natl Acad Sci U S A 2008; 105(22):7732-7737.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , Issue.22 , pp. 7732-7737
    • Fuentealba, L.C.1    Eivers, E.2    Geissert, D.3
  • 176
    • 33845491748 scopus 로고    scopus 로고
    • Polarised asymmetric inheritance of accumulated protein damage in higher eukaryotes
    • Rujano MA, Bosveld F, Salomons FA et al. Polarised asymmetric inheritance of accumulated protein damage in higher eukaryotes. PLoS Biol 2006; 4(12):e417.
    • (2006) PLoS Biol , vol.4 , Issue.12
    • Rujano, M.A.1    Bosveld, F.2    Salomons, F.A.3
  • 177
    • 0036678146 scopus 로고    scopus 로고
    • The threshold for polyglutamine-expansion protein aggregation and cellulartoxicity is dynamic and influenced by aging in Caenorhabditis elegans
    • Morley JF, Brignull HR, Weyers JJ et al. The threshold for polyglutamine-expansion protein aggregation and cellulartoxicity is dynamic and influenced by aging in Caenorhabditis elegans. Proc Natl Acad Sci U S A 2002; 99(16):10417-10422.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , Issue.16 , pp. 10417-10422
    • Morley, J.F.1    Brignull, H.R.2    Weyers, J.J.3
  • 178
    • 77953510734 scopus 로고    scopus 로고
    • Onset and progression of pathologic atrophy in Huntington disease: A longitudinal MR imaging study
    • Hobbs NZ, Barnes J, Frost C et al. Onset and progression of pathologic atrophy in Huntington disease: a longitudinal MR imaging study. AJNR Am J Neuroradiol 2010; 31(6):1036-1041.
    • (2010) AJNR Am J Neuroradiol , vol.31 , Issue.6 , pp. 1036-1041
    • Hobbs, N.Z.1    Barnes, J.2    Frost, C.3
  • 179
    • 84934435560 scopus 로고    scopus 로고
    • Smaller intracranial volume in prodromal Huntington's disease: Evidence for abnormal neurodevelopment
    • Nopoulos PC, Aylward EH, Ross CA et al. Smaller intracranial volume in prodromal Huntington's disease: evidence for abnormal neurodevelopment. Brain 2010.
    • (2010) Brain
    • Nopoulos, P.C.1    Aylward, E.H.2    Ross, C.A.3
  • 180
    • 76049118555 scopus 로고    scopus 로고
    • Impairment of developmental stem cell-mediated striatal neurogenesis and pluripotency genes in a knock-in model of Huntington's disease
    • Molero AE, Gokhan S, Gonzalez S et al. Impairment of developmental stem cell-mediated striatal neurogenesis and pluripotency genes in a knock-in model of Huntington's disease. Proc Natl Acad Sci U S A 2009; 106(51):21900-21905.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , Issue.51 , pp. 21900-21905
    • Molero, A.E.1    Gokhan, S.2    Gonzalez, S.3
  • 181
    • 67650410543 scopus 로고    scopus 로고
    • Biological and chemical approaches to diseases of proteostasis deficiency
    • Powers ET, Morimoto RI, Dillin A et al. Biological and chemical approaches to diseases of proteostasis deficiency. Ann Rev Biochem 2009; 78(1):959-991.
    • (2009) Ann Rev Biochem , vol.78 , Issue.1 , pp. 959-991
    • Powers, E.T.1    Morimoto, R.I.2    Dillin, A.3


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