메뉴 건너뛰기




Volumn 120, Issue 4, 2010, Pages 419-437

Neurotoxic protein oligomerisation associated with polyglutamine diseases

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; POLYGLUTAMINE; REACTIVE OXYGEN METABOLITE;

EID: 77956184558     PISSN: 00016322     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00401-010-0703-0     Document Type: Review
Times cited : (61)

References (189)
  • 1
    • 18344399938 scopus 로고    scopus 로고
    • Transgenic mice with an expanded CAG repeat controlled by the human AR promoter show polyglutamine nuclear inclusions and neuronal dysfunction without neuronal cell death
    • 11331614
    • H Adachi A Kume M Li, et al. 2001 Transgenic mice with an expanded CAG repeat controlled by the human AR promoter show polyglutamine nuclear inclusions and neuronal dysfunction without neuronal cell death Hum Mol Genet 10 1039 1048 11331614
    • (2001) Hum Mol Genet , vol.10 , pp. 1039-1048
    • Adachi, H.1    Kume, A.2    Li, M.3
  • 2
    • 70350380989 scopus 로고    scopus 로고
    • Phosphorylation of threonine-3: Implications for huntingtin aggregation and neurotoxicity
    • 19710014
    • CT Aiken JS Steffan CM Guerrero, et al. 2009 Phosphorylation of threonine-3: implications for huntingtin aggregation and neurotoxicity J Biol Chem 284 29427 29436 19710014
    • (2009) J Biol Chem , vol.284 , pp. 29427-29436
    • Aiken, C.T.1    Steffan, J.S.2    Guerrero, C.M.3
  • 3
    • 59149084113 scopus 로고    scopus 로고
    • Metal-dependent generation of reactive oxygen species from amyloid proteins implicated in neurodegenerative disease
    • 19021543
    • D Allsop J Mayes S Moore A Masad BJ Tabner 2008 Metal-dependent generation of reactive oxygen species from amyloid proteins implicated in neurodegenerative disease Biochem Soc Trans 36 1293 1298 19021543
    • (2008) Biochem Soc Trans , vol.36 , pp. 1293-1298
    • Allsop, D.1    Mayes, J.2    Moore, S.3    Masad, A.4    Tabner, B.J.5
  • 4
    • 0030739464 scopus 로고    scopus 로고
    • Random coil conformation for extended polyglutamine stretches in aqueous soluble monomeric peptides
    • 9273890
    • EL Altschuler NV Hud JA Mazrimas B Rupp 1997 Random coil conformation for extended polyglutamine stretches in aqueous soluble monomeric peptides J Pept Res 50 73 75 9273890
    • (1997) J Pept Res , vol.50 , pp. 73-75
    • Altschuler, E.L.1    Hud, N.V.2    Mazrimas, J.A.3    Rupp, B.4
  • 5
    • 0028260436 scopus 로고
    • Structure and expression of the Huntington's disease gene: Evidence against simple inactivation due to an expanded CAG repeat
    • 8197474
    • CM Ambrose MP Duyao G Barnes, et al. 1994 Structure and expression of the Huntington's disease gene: evidence against simple inactivation due to an expanded CAG repeat Somat Cell Mol Genet 20 27 38 8197474
    • (1994) Somat Cell Mol Genet , vol.20 , pp. 27-38
    • Ambrose, C.M.1    Duyao, M.P.2    Barnes, G.3
  • 6
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • 15483602
    • M Arrasate S Mitra ES Schweitzer MR Segal S Finkbeiner 2004 Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death Nature 431 805 810 15483602
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 7
    • 35448994487 scopus 로고    scopus 로고
    • Huntingtin has a membrane association signal that can modulate huntingtin aggregation, nuclear entry and toxicity
    • 17704510
    • RS Atwal J Xia D Pinchev J Taylor RM Epand R Truant 2007 Huntingtin has a membrane association signal that can modulate huntingtin aggregation, nuclear entry and toxicity Hum Mol Genet 16 2600 2615 17704510
    • (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
  • 8
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • 18276881
    • WE Balch RI Morimoto A Dillin JW Kelly 2008 Adapting proteostasis for disease intervention Science 319 916 919 18276881
    • (2008) Science , vol.319 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 9
    • 34548510580 scopus 로고    scopus 로고
    • The length dependence of the PolyQ-mediated protein aggregation
    • 17591778
    • S Barton R Jacak SD Khare F Ding NV Dokholyan 2007 The length dependence of the PolyQ-mediated protein aggregation J Biol Chem 282 25487 25492 17591778
    • (2007) J Biol Chem , vol.282 , pp. 25487-25492
    • Barton, S.1    Jacak, R.2    Khare, S.D.3    Ding, F.4    Dokholyan, N.V.5
  • 10
    • 69949170793 scopus 로고    scopus 로고
    • The pathogenic mechanisms of polyglutamine diseases and current therapeutic strategies
    • 19650870
    • PO Bauer N Nukina 2009 The pathogenic mechanisms of polyglutamine diseases and current therapeutic strategies J Neurochem 110 1737 1765 19650870
    • (2009) J Neurochem , vol.110 , pp. 1737-1765
    • Bauer, P.O.1    Nukina, N.2
  • 11
    • 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
    • 9666478
    • MW Becher JA Kotzuk AH Sharp, et al. 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 9666478
    • (1998) Neurobiol Dis , vol.4 , pp. 387-397
    • Becher, M.W.1    Kotzuk, J.A.2    Sharp, A.H.3
  • 12
    • 0034678342 scopus 로고    scopus 로고
    • Cytoplasmic localization and the choice of ligand determine aggregate formation by androgen receptor with amplified polyglutamine stretch
    • 10769019
    • M Becker E Martin J Schneikert HF Krug ACB Cato 2000 Cytoplasmic localization and the choice of ligand determine aggregate formation by androgen receptor with amplified polyglutamine stretch J Cell Biol 149 255 262 10769019
    • (2000) J Cell Biol , vol.149 , pp. 255-262
    • Becker, M.1    Martin, E.2    Schneikert, J.3    Krug, H.F.4    Cato, A.C.B.5
  • 13
    • 33748561495 scopus 로고    scopus 로고
    • Chaperonin TRiC promotes the assembly of polyQ expansion proteins into nontoxic oligomers
    • 16973440
    • C Behrends CA Langer R Boteva, et al. 2006 Chaperonin TRiC promotes the assembly of polyQ expansion proteins into nontoxic oligomers Mol Cell 23 887 897 16973440
    • (2006) Mol Cell , vol.23 , pp. 887-897
    • Behrends, C.1    Langer, C.A.2    Boteva, R.3
  • 14
    • 13244258435 scopus 로고    scopus 로고
    • Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation
    • 15694337
    • EJ Bennett NF Bence R Jayakumar RR Kopito 2005 Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation Mol Cell 17 351 365 15694337
    • (2005) Mol Cell , vol.17 , pp. 351-365
    • Bennett, E.J.1    Bence, N.F.2    Jayakumar, R.3    Kopito, R.R.4
  • 15
    • 0035833997 scopus 로고    scopus 로고
    • An expanded glutamine repeat destabilizes native ataxin-3 structure and mediates formation of parallel beta-fibrils
    • 11572942
    • AE Bevivino PJ Loll 2001 An expanded glutamine repeat destabilizes native ataxin-3 structure and mediates formation of parallel beta-fibrils Proc Natl Acad Sci USA 98 11955 11960 11572942
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 11955-11960
    • Bevivino, A.E.1    Loll, P.J.2
  • 16
    • 28944446477 scopus 로고    scopus 로고
    • Oligoproline effects on polyglutamine conformation and aggregation
    • 16321399
    • A Bhattacharyya AK Thakur VM Chellgren, et al. 2006 Oligoproline effects on polyglutamine conformation and aggregation J Mol Biol 355 524 535 16321399
    • (2006) J Mol Biol , vol.355 , pp. 524-535
    • Bhattacharyya, A.1    Thakur, A.K.2    Chellgren, V.M.3
  • 17
    • 27344435254 scopus 로고    scopus 로고
    • Polyglutamine aggregation nucleation: Thermodynamics of a highly unfavorable protein folding reaction
    • 16230628
    • AM Bhattacharyya AK Thakur R Wetzel 2005 Polyglutamine aggregation nucleation: thermodynamics of a highly unfavorable protein folding reaction Proc Natl Acad Sci USA 102 15400 15405 16230628
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 15400-15405
    • Bhattacharyya, A.M.1    Thakur, A.K.2    Wetzel, R.3
  • 18
    • 33947164372 scopus 로고    scopus 로고
    • Puromycin-sensitive aminopeptidase is the major peptidase responsible for digesting polyglutamine sequences released by proteasomes during protein degradation
    • 17318184
    • N Bhutani P Venkatraman AL Goldberg 2007 Puromycin-sensitive aminopeptidase is the major peptidase responsible for digesting polyglutamine sequences released by proteasomes during protein degradation EMBO J 26 1385 1396 17318184
    • (2007) EMBO J , vol.26 , pp. 1385-1396
    • Bhutani, N.1    Venkatraman, P.2    Goldberg, A.L.3
  • 19
    • 58049217323 scopus 로고    scopus 로고
    • Unexpected link between anaphase promoting complex and the toxicity of expanded polyglutamines expressed in yeast
    • 19066445
    • NA Bocharova SS Sokolov DA Knorre VP Skulachev FF Severin 2008 Unexpected link between anaphase promoting complex and the toxicity of expanded polyglutamines expressed in yeast Cell Cycle 7 3943 3946 19066445
    • (2008) Cell Cycle , vol.7 , pp. 3943-3946
    • Bocharova, N.A.1    Sokolov, S.S.2    Knorre, D.A.3    Skulachev, V.P.4    Severin, F.F.5
  • 20
    • 33645235438 scopus 로고    scopus 로고
    • Pharmacological promotion of inclusion formation: A therapeutic approach for Huntington's and Parkinson's diseases
    • 16537516
    • RA Bodner TF Outeiro S Altmann, et al. 2006 Pharmacological promotion of inclusion formation: a therapeutic approach for Huntington's and Parkinson's diseases Proc Natl Acad Sci USA 103 4246 4251 16537516
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 4246-4251
    • Bodner, R.A.1    Outeiro, T.F.2    Altmann, S.3
  • 21
    • 76049118058 scopus 로고    scopus 로고
    • Expression of mutant huntingtin in mouse brain astrocytes causes age-dependent neurological symptoms
    • 20018729
    • J Bradford J-Y Shin M Roberts C-E Wang X-J Li S Li 2009 Expression of mutant huntingtin in mouse brain astrocytes causes age-dependent neurological symptoms Proc Natl Acad Sci USA 106 22480 22485 20018729
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 22480-22485
    • Bradford, J.1    Shin, J.-Y.2    Roberts, M.3    Wang, C.-E.4    Li, X.-J.5    Li, S.6
  • 22
    • 77951238141 scopus 로고    scopus 로고
    • Mutant huntingtin in glial cells exacerbates neurological symptoms of huntington disease mice
    • 20145253
    • J Bradford J-Y Shin M Roberts, et al. 2010 Mutant huntingtin in glial cells exacerbates neurological symptoms of huntington disease mice J Biol Chem 285 10653 10661 20145253
    • (2010) J Biol Chem , vol.285 , pp. 10653-10661
    • Bradford, J.1    Shin, J.-Y.2    Roberts, M.3
  • 23
    • 0345099501 scopus 로고    scopus 로고
    • The polyglutamine neurodegenerative protein ataxin-3 binds polyubiquitylated proteins and has ubiquitin protease activity
    • 14559776
    • B Burnett F Li RN Pittman 2003 The polyglutamine neurodegenerative protein ataxin-3 binds polyubiquitylated proteins and has ubiquitin protease activity Hum Mol Genet 12 3195 3205 14559776
    • (2003) Hum Mol Genet , vol.12 , pp. 3195-3205
    • Burnett, B.1    Li, F.2    Pittman, R.N.3
  • 24
    • 0141926491 scopus 로고    scopus 로고
    • Mutant huntingtin promotes the fibrillogenesis of wild-type huntingtin
    • 12888569
    • A Busch S Engemann R Lurz H Okazawa H Lehrach EE Wanker 2003 Mutant huntingtin promotes the fibrillogenesis of wild-type huntingtin J Biol Chem 278 41452 41461 12888569
    • (2003) J Biol Chem , vol.278 , pp. 41452-41461
    • Busch, A.1    Engemann, S.2    Lurz, R.3    Okazawa, H.4    Lehrach, H.5    Wanker, E.E.6
  • 25
    • 28644433087 scopus 로고    scopus 로고
    • Normal huntingtin function: An alternative approach to Huntington's disease
    • 16288298
    • E Cattaneo C Zuccato M Tartari 2005 Normal huntingtin function: an alternative approach to Huntington's disease Nat Rev Neurosci 6 919 930 16288298
    • (2005) Nat Rev Neurosci , vol.6 , pp. 919-930
    • Cattaneo, E.1    Zuccato, C.2    Tartari, M.3
  • 26
    • 0037047123 scopus 로고    scopus 로고
    • Live-cell imaging reveals divergent intracellular dynamics of polyglutamine disease proteins and supports a sequestration model of pathogenesis
    • 12084819
    • Y Chai J Shao VM Miller A Williams HL Paulson 2002 Live-cell imaging reveals divergent intracellular dynamics of polyglutamine disease proteins and supports a sequestration model of pathogenesis Proc Natl Acad Sci USA 99 9310 9315 12084819
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 9310-9315
    • Chai, Y.1    Shao, J.2    Miller, V.M.3    Williams, A.4    Paulson, H.L.5
  • 27
    • 0034726119 scopus 로고    scopus 로고
    • Alpha-synuclein immunoreactivity of huntingtin polyglutamine aggregates in striatum and cortex of Huntington's disease patients and transgenic mouse models
    • 10899401
    • V Charles E Mezey PH Reddy, et al. 2000 Alpha-synuclein immunoreactivity of huntingtin polyglutamine aggregates in striatum and cortex of Huntington's disease patients and transgenic mouse models Neurosci Lett 289 29 32 10899401
    • (2000) Neurosci Lett , vol.289 , pp. 29-32
    • Charles, V.1    Mezey, E.2    Reddy, P.H.3
  • 28
    • 33646137562 scopus 로고    scopus 로고
    • Decreased association of the transcription factor Sp1 with genes downregulated in Huntington's disease
    • 16442295
    • AS Chen-Plotkin G Sadri-Vakili GJ Yohrling, et al. 2006 Decreased association of the transcription factor Sp1 with genes downregulated in Huntington's disease Neurobiol Dis 22 233 241 16442295
    • (2006) Neurobiol Dis , vol.22 , pp. 233-241
    • Chen-Plotkin, A.S.1    Sadri-Vakili, G.2    Yohrling, G.J.3
  • 29
    • 0037726598 scopus 로고    scopus 로고
    • Interaction of Akt-phosphorylated Ataxin-1 with 14-3-3 mediates neurodegeneration in spinocerebellar ataxia type 1
    • 12757707
    • H-K Chen P Fernandez-Funez SF Acevedo, et al. 2003 Interaction of Akt-phosphorylated Ataxin-1 with 14-3-3 mediates neurodegeneration in spinocerebellar ataxia type 1 Cell 113 457 468 12757707
    • (2003) Cell , vol.113 , pp. 457-468
    • Chen, H.-K.1    Fernandez-Funez, P.2    Acevedo, S.F.3
  • 30
    • 0037062561 scopus 로고    scopus 로고
    • Amyloid-like features of polyglutamine aggregates and their assembly kinetics
    • 12044172
    • S Chen V Berthelier JB Hamilton B O'Nuallai R Wetzel 2002 Amyloid-like features of polyglutamine aggregates and their assembly kinetics Biochemistry 41 7391 7399 12044172
    • (2002) Biochemistry , vol.41 , pp. 7391-7399
    • Chen, S.1    Berthelier, V.2    Hamilton, J.B.3    O'Nuallai, B.4    Wetzel, R.5
  • 31
    • 0035800572 scopus 로고    scopus 로고
    • Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity
    • 11469866
    • S Chen V Berthelier W Yang R Wetzel 2001 Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity J Mol Biol 311 173 182 11469866
    • (2001) J Mol Biol , vol.311 , pp. 173-182
    • Chen, S.1    Berthelier, V.2    Yang, W.3    Wetzel, R.4
  • 32
    • 0037015081 scopus 로고    scopus 로고
    • Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation
    • 12186976
    • S Chen FA Ferrone R Wetzel 2002 Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation Proc Natl Acad Sci USA 99 11884 11889 12186976
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 11884-11889
    • Chen, S.1    Ferrone, F.A.2    Wetzel, R.3
  • 33
    • 13944275615 scopus 로고    scopus 로고
    • Polyglutamine expansion of huntingtin impairs its nuclear export
    • 15654337
    • J Cornett F Cao C-E Wang, et al. 2005 Polyglutamine expansion of huntingtin impairs its nuclear export Nat Genet 37 198 204 15654337
    • (2005) Nat Genet , vol.37 , pp. 198-204
    • Cornett, J.1    Cao, F.2    Wang, C.-E.3
  • 34
    • 33750934185 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy shows that monomeric polyglutamine molecules form collapsed structures in aqueous solutions
    • 17075061
    • SL Crick M Jayaraman C Frieden R Wetzel RV Pappu 2006 Fluorescence correlation spectroscopy shows that monomeric polyglutamine molecules form collapsed structures in aqueous solutions Proc Natl Acad Sci USA 103 16764 16769 17075061
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 16764-16769
    • Crick, S.L.1    Jayaraman, M.2    Frieden, C.3    Wetzel, R.4    Pappu, R.V.5
  • 35
    • 33645253160 scopus 로고    scopus 로고
    • Atomic force microscopy analysis of the huntington protein nanofibril formation
    • 17292058
    • PR Dahlgren MA Karymov J Bankston, et al. 2005 Atomic force microscopy analysis of the huntington protein nanofibril formation Nanomedicine 1 52 57 17292058
    • (2005) Nanomedicine , vol.1 , pp. 52-57
    • Dahlgren, P.R.1    Karymov, M.A.2    Bankston, J.3
  • 36
    • 0034703397 scopus 로고    scopus 로고
    • Identification and characterization of an ataxin-1-interacting protein: A1Up, a ubiquitin-like nuclear protein
    • 11001934
    • JD Davidson B Riley EN Burright LA Duvick HY Zoghbi HT Orr 2000 Identification and characterization of an ataxin-1-interacting protein: A1Up, a ubiquitin-like nuclear protein Hum Mol Genet 9 2305 2312 11001934
    • (2000) Hum Mol Genet , vol.9 , pp. 2305-2312
    • Davidson, J.D.1    Riley, B.2    Burright, E.N.3    Duvick, L.A.4    Zoghbi, H.Y.5    Orr, H.T.6
  • 37
    • 18544410106 scopus 로고    scopus 로고
    • Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation
    • 9267033
    • S Davies M Turmaine B Cozens, et al. 1997 Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation Cell 90 537 548 9267033
    • (1997) Cell , vol.90 , pp. 537-548
    • Davies, S.1    Turmaine, M.2    Cozens, B.3
  • 38
    • 33845898194 scopus 로고    scopus 로고
    • Ubiquitin-conjugating enzyme E2-25 K increases aggregate formation and cell death in polyglutamine diseases
    • 17092742
    • R de Pril DF Fischer RAC Roos FW van Leeuwen 2007 Ubiquitin-conjugating enzyme E2-25 K increases aggregate formation and cell death in polyglutamine diseases Mol Cell Neurosci 34 10 19 17092742
    • (2007) Mol Cell Neurosci , vol.34 , pp. 10-19
    • De Pril, R.1    Fischer, D.F.2    Roos, R.A.C.3    Van Leeuwen, F.W.4
  • 39
    • 26444575834 scopus 로고    scopus 로고
    • Polyglutamine homopolymers having 8-45 residues form slablike beta-crystallite assemblies
    • S Deepak MS Leonid I Hideyo W Ronald AK Daniel 2005 Polyglutamine homopolymers having 8-45 residues form slablike beta-crystallite assemblies Proteins 61 398 411
    • (2005) Proteins , vol.61 , pp. 398-411
    • Deepak, S.1    Leonid, M.S.2    Hideyo, I.3    Ronald, W.4    Daniel, A.K.5
  • 40
    • 34249698045 scopus 로고    scopus 로고
    • Mapping of the epitope of monoclonal antibody 2B4 to the proline-rich region of human huntingtin, a region critical for aggregation and toxicity
    • 17373643
    • B Dehay C Weber Y Trottier A Bertolotti 2007 Mapping of the epitope of monoclonal antibody 2B4 to the proline-rich region of human huntingtin, a region critical for aggregation and toxicity Biotechnol J 2 559 564 17373643
    • (2007) Biotechnol J , vol.2 , pp. 559-564
    • Dehay, B.1    Weber, C.2    Trottier, Y.3    Bertolotti, A.4
  • 41
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • 9302293
    • M DiFiglia E Sapp K Chase, et al. 1997 Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain Science 277 1990 1993 9302293
    • (1997) Science , vol.277 , pp. 1990-1993
    • Difiglia, M.1    Sapp, E.2    Chase, K.3
  • 42
    • 0028989602 scopus 로고
    • Huntingtin is a cytoplasmic protein associated with vesicles in human and rat brain neurons
    • 7748555
    • M DiFiglia E Sapp K Chase, et al. 1995 Huntingtin is a cytoplasmic protein associated with vesicles in human and rat brain neurons Neuron 14 1075 1081 7748555
    • (1995) Neuron , vol.14 , pp. 1075-1081
    • Difiglia, M.1    Sapp, E.2    Chase, K.3
  • 43
    • 0042691818 scopus 로고    scopus 로고
    • Ataxin-3 interactions with Rad23 and valosin-containing protein and its associations with ubiquitin chains and the proteasome are consistent with a role in ubiquitin-mediated proteolysis
    • 12944474
    • EW Doss-Pepe ES Stenroos WG Johnson K Madura 2003 Ataxin-3 interactions with Rad23 and valosin-containing protein and its associations with ubiquitin chains and the proteasome are consistent with a role in ubiquitin-mediated proteolysis Mol Cell Biol 23 6469 6483 12944474
    • (2003) Mol Cell Biol , vol.23 , pp. 6469-6483
    • Doss-Pepe, E.W.1    Stenroos, E.S.2    Johnson, W.G.3    Madura, K.4
  • 44
    • 69149105917 scopus 로고    scopus 로고
    • Single homopolypeptide chains collapse into mechanically rigid conformations
    • 19549822
    • L Dougan J Li CL Badilla BJ Berne JM Fernandez 2009 Single homopolypeptide chains collapse into mechanically rigid conformations Proc Natl Acad Sci USA 106 12605 12610 19549822
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 12605-12610
    • Dougan, L.1    Li, J.2    Badilla, C.L.3    Berne, B.J.4    Fernandez, J.M.5
  • 46
    • 33745195252 scopus 로고    scopus 로고
    • The two-stage pathway of ataxin-3 fibrillogenesis involves a polyglutamine-independent step
    • 16624810
    • AM Ellisdon B Thomas SP Bottomley 2006 The two-stage pathway of ataxin-3 fibrillogenesis involves a polyglutamine-independent step J Biol Chem 281 16888 16896 16624810
    • (2006) J Biol Chem , vol.281 , pp. 16888-16896
    • Ellisdon, A.M.1    Thomas, B.2    Bottomley, S.P.3
  • 47
    • 0037846441 scopus 로고    scopus 로고
    • Serine 776 of ataxin-1 is critical for polyglutamine-induced disease in SCA1 transgenic mice
    • 12741986
    • ES Emamian MD Kaytor LA Duvick, et al. 2003 Serine 776 of ataxin-1 is critical for polyglutamine-induced disease in SCA1 transgenic mice Neuron 38 375 387 12741986
    • (2003) Neuron , vol.38 , pp. 375-387
    • Emamian, E.S.1    Kaytor, M.D.2    Duvick, L.A.3
  • 48
    • 0033524413 scopus 로고    scopus 로고
    • Polyglutamine-mediated dysfunction and apoptotic death of a Caenorhabditis elegans sensory neuron
    • 9874792
    • PW Faber JR Alter ME MacDonald AC Hart 1999 Polyglutamine-mediated dysfunction and apoptotic death of a Caenorhabditis elegans sensory neuron Proc Natl Acad Sci USA 96 179 184 9874792
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 179-184
    • Faber, P.W.1    Alter, J.R.2    MacDonald, M.E.3    Hart, A.C.4
  • 49
    • 34247160537 scopus 로고    scopus 로고
    • Phosphorylation of ataxin-3 by glycogen synthase kinase 3 beta at serine 256 regulates the aggregation of ataxin-3
    • 17434145
    • E Fei N Jia T Zhang, et al. 2007 Phosphorylation of ataxin-3 by glycogen synthase kinase 3 beta at serine 256 regulates the aggregation of ataxin-3 Biochem Biophys Res Com 357 487 492 17434145
    • (2007) Biochem Biophys Res Com , vol.357 , pp. 487-492
    • Fei, E.1    Jia, N.2    Zhang, T.3
  • 50
    • 0034597833 scopus 로고    scopus 로고
    • Identification of genes that modify ataxin-1-induced neurodegeneration
    • 11081516
    • P Fernandez-Funez ML Nino-Rosales B de Gouyon, et al. 2000 Identification of genes that modify ataxin-1-induced neurodegeneration Nature 408 101 106 11081516
    • (2000) Nature , vol.408 , pp. 101-106
    • Fernandez-Funez, P.1    Nino-Rosales, M.L.2    De Gouyon, B.3
  • 51
    • 7044238416 scopus 로고    scopus 로고
    • Neurodegenerative diseases: A decade of discoveries paves the way for therapeutic breakthroughs
    • 15459709
    • MS Forman JQ Trojanowski VMY Lee 2004 Neurodegenerative diseases: a decade of discoveries paves the way for therapeutic breakthroughs Nat Med 10 1055 1063 15459709
    • (2004) Nat Med , vol.10 , pp. 1055-1063
    • Forman, M.S.1    Trojanowski, J.Q.2    Lee, V.M.Y.3
  • 52
    • 55349106939 scopus 로고    scopus 로고
    • Mechanisms of copper ion mediated huntington's disease progression
    • 17396163
    • JH Fox JA Kama G Lieberman, et al. 2007 Mechanisms of copper ion mediated huntington's disease progression PLoS One 2 e334 17396163
    • (2007) PLoS One , vol.2 , pp. 334
    • Fox, J.H.1    Kama, J.A.2    Lieberman, G.3
  • 53
    • 0035503901 scopus 로고    scopus 로고
    • Spinocerebellar ataxia type 6: Channelopathy or glutamine repeat disorder?
    • 11719255
    • M Frontali 2001 Spinocerebellar ataxia type 6: channelopathy or glutamine repeat disorder? Brain Res Bull 56 227 231 11719255
    • (2001) Brain Res Bull , vol.56 , pp. 227-231
    • Frontali, M.1
  • 54
    • 70349581486 scopus 로고    scopus 로고
    • The expanding realm of prion phenomena in neurodegenerative disease
    • 19448400
    • B Frost MI Diamond 2009 The expanding realm of prion phenomena in neurodegenerative disease Prion 3 74 77 19448400
    • (2009) Prion , vol.3 , pp. 74-77
    • Frost, B.1    Diamond, M.I.2
  • 56
    • 26244434741 scopus 로고    scopus 로고
    • Towards a structural understanding of the fibrillization pathway in Machado-Joseph's disease: Trapping early oligomers of non-expanded ataxin-3
    • 16194547
    • L Gales L Cortes C Almeida, et al. 2005 Towards a structural understanding of the fibrillization pathway in Machado-Joseph's disease: trapping early oligomers of non-expanded ataxin-3 J Mol Biol 353 642 654 16194547
    • (2005) J Mol Biol , vol.353 , pp. 642-654
    • Gales, L.1    Cortes, L.2    Almeida, C.3
  • 57
    • 3142636768 scopus 로고    scopus 로고
    • Huntingtin controls neurotrophic support and survival of neurons by enhancing BDNF vesicular transport along microtubules
    • 15242649
    • LR Gauthier BC Charrin M Borrell-Pagès, et al. 2004 Huntingtin controls neurotrophic support and survival of neurons by enhancing BDNF vesicular transport along microtubules Cell 118 127 138 15242649
    • (2004) Cell , vol.118 , pp. 127-138
    • Gauthier, L.R.1    Charrin, B.C.2    Borrell-Pagès, M.3
  • 58
    • 33644850056 scopus 로고    scopus 로고
    • Progressive disruption of cellular protein folding in models of polyglutamine diseases
    • 16469881
    • T Gidalevitz A Ben-Zvi KH Ho HR Brignull RI Morimoto 2006 Progressive disruption of cellular protein folding in models of polyglutamine diseases Science 311 1471 1474 16469881
    • (2006) Science , vol.311 , pp. 1471-1474
    • Gidalevitz, T.1    Ben-Zvi, A.2    Ho, K.H.3    Brignull, H.R.4    Morimoto, R.I.5
  • 59
    • 77949765699 scopus 로고    scopus 로고
    • Pathogenic polyglutamine tracts are potent inducers of spontaneous Sup35 and Rnq1 amyloidogenesis
    • 20224794
    • H Goehler A Droge R Lurz S Schnoegl YO Chernoff EE Wanker 2010 Pathogenic polyglutamine tracts are potent inducers of spontaneous Sup35 and Rnq1 amyloidogenesis PLoS One 5 e9642 20224794
    • (2010) PLoS One , vol.5 , pp. 9642
    • Goehler, H.1    Droge, A.2    Lurz, R.3    Schnoegl, S.4    Chernoff, Y.O.5    Wanker, E.E.6
  • 60
    • 37349007785 scopus 로고    scopus 로고
    • Time-lapse analysis of aggregate formation in an inducible PC12 cell model of Huntington's disease reveals time-dependent aggregate formation that transiently delays cell death
    • 18158109
    • B Gong MCY Lim J Wanderer A Wyttenbach AJ Morton 2008 Time-lapse analysis of aggregate formation in an inducible PC12 cell model of Huntington's disease reveals time-dependent aggregate formation that transiently delays cell death Brain Res Bull 75 146 157 18158109
    • (2008) Brain Res Bull , vol.75 , pp. 146-157
    • Gong, B.1    Lim, M.C.Y.2    Wanderer, J.3    Wyttenbach, A.4    Morton, A.J.5
  • 61
    • 0141750470 scopus 로고    scopus 로고
    • Disruption of axonal transport by loss of huntingtin or expression of pathogenic PolyQ proteins in drosophila
    • 14527431
    • S Gunawardena L-S Her RG Brusch, et al. 2003 Disruption of axonal transport by loss of huntingtin or expression of pathogenic PolyQ proteins in drosophila Neuron 40 25 40 14527431
    • (2003) Neuron , vol.40 , pp. 25-40
    • Gunawardena, S.1    Her, L.-S.2    Brusch, R.G.3
  • 62
    • 0032101287 scopus 로고    scopus 로고
    • The influence of huntingtin protein size on nuclear localization and cellular toxicity
    • 9606203
    • AS Hackam R Singaraja CL Wellington, et al. 1998 The influence of huntingtin protein size on nuclear localization and cellular toxicity J Cell Biol 141 1097 1105 9606203
    • (1998) J Cell Biol , vol.141 , pp. 1097-1105
    • Hackam, A.S.1    Singaraja, R.2    Wellington, C.L.3
  • 63
    • 0031970977 scopus 로고    scopus 로고
    • The fatal attraction of polyglutamine-containing proteins
    • 9650759
    • AS Hackam CL Wellington MR Hayden 1998 The fatal attraction of polyglutamine-containing proteins Clin Genet 53 233 242 9650759
    • (1998) Clin Genet , vol.53 , pp. 233-242
    • Hackam, A.S.1    Wellington, C.L.2    Hayden, M.R.3
  • 64
    • 77953283266 scopus 로고    scopus 로고
    • Metallothioneins and copper metabolism are candidate therapeutic targets in Huntington's disease
    • 20298220
    • S Hands R Mason MU Sajjad F Giorgini A Wyttenbach 2010 Metallothioneins and copper metabolism are candidate therapeutic targets in Huntington's disease Biochem Soc Trans 38 552 558 20298220
    • (2010) Biochem Soc Trans , vol.38 , pp. 552-558
    • Hands, S.1    Mason, R.2    Sajjad, M.U.3    Giorgini, F.4    Wyttenbach, A.5
  • 65
    • 49549096453 scopus 로고    scopus 로고
    • Polyglutamine gene function and dysfunction in the ageing brain
    • 18582603
    • S Hands C Sinadinos A Wyttenbach 2008 Polyglutamine gene function and dysfunction in the ageing brain Biochim Biophys Acta 1779 507 521 18582603
    • (2008) Biochim Biophys Acta , vol.1779 , pp. 507-521
    • Hands, S.1    Sinadinos, C.2    Wyttenbach, A.3
  • 66
    • 0038576863 scopus 로고    scopus 로고
    • A method to assess compositional bias in biological sequences and its application to prion-like glutamine/asparagine-rich domains in eukaryotic proteomes
    • 12801414
    • P Harrison M Gerstein 2003 A method to assess compositional bias in biological sequences and its application to prion-like glutamine/asparagine-rich domains in eukaryotic proteomes Genome Biol 4 R40 12801414
    • (2003) Genome Biol , vol.4 , pp. 40
    • Harrison, P.1    Gerstein, M.2
  • 67
    • 33144469085 scopus 로고    scopus 로고
    • Glutamine-expanded Ataxin-7 alters TFTC/STAGA recruitment and chromatin structure leading to photoreceptor dysfunction
    • 16494529
    • D Helmlinger S Hardy G Abou-Sleymane, et al. 2006 Glutamine-expanded Ataxin-7 alters TFTC/STAGA recruitment and chromatin structure leading to photoreceptor dysfunction PLoS Biol 4 e67 16494529
    • (2006) PLoS Biol , vol.4 , pp. 67
    • Helmlinger, D.1    Hardy, S.2    Abou-Sleymane, G.3
  • 70
    • 7144229376 scopus 로고    scopus 로고
    • Spinocerebellar ataxia type 7 (SCA7): A neurodegenerative disorder with neuronal intranuclear inclusions
    • 9536097
    • M Holmberg C Duyckaerts A Durr, et al. 1998 Spinocerebellar ataxia type 7 (SCA7): a neurodegenerative disorder with neuronal intranuclear inclusions Hum Mol Genet 7 913 918 9536097
    • (1998) Hum Mol Genet , vol.7 , pp. 913-918
    • Holmberg, M.1    Duyckaerts, C.2    Durr, A.3
  • 71
    • 0036083379 scopus 로고    scopus 로고
    • The IGF-1/Akt pathway is neuroprotective in Huntington's Disease and involves huntingtin phosphorylation by Akt
    • 12062094
    • S Humbert EA Bryson FP Cordelières, et al. 2002 The IGF-1/Akt pathway is neuroprotective in Huntington's Disease and involves huntingtin phosphorylation by Akt Dev Cell 2 831 837 12062094
    • (2002) Dev Cell , vol.2 , pp. 831-837
    • Humbert, S.1    Bryson, E.A.2    Cordelières, F.P.3
  • 72
    • 33748588165 scopus 로고    scopus 로고
    • Inhibition of protein aggregation in vitro and in vivo by a natural osmoprotectant
    • 16899544
    • Z Ignatova LM Gierasch 2006 Inhibition of protein aggregation in vitro and in vivo by a natural osmoprotectant Proc Natl Acad Sci USA 103 13357 13361 16899544
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 13357-13361
    • Ignatova, Z.1    Gierasch, L.M.2
  • 73
    • 37549011420 scopus 로고    scopus 로고
    • In-cell aggregation of a polyglutamine-containing chimera is a multistep process initiated by the flanking sequence
    • 17942400
    • Z Ignatova AK Thakur R Wetzel LM Gierasch 2007 In-cell aggregation of a polyglutamine-containing chimera is a multistep process initiated by the flanking sequence J Biol Chem 282 36736 36743 17942400
    • (2007) J Biol Chem , vol.282 , pp. 36736-36743
    • Ignatova, Z.1    Thakur, A.K.2    Wetzel, R.3    Gierasch, L.M.4
  • 74
    • 0030058208 scopus 로고    scopus 로고
    • Expanded polyglutamine in the Machado-Joseph disease protein induces cell death in vitro and in vivo
    • 8640226
    • H Ikeda M Yamaguchi S Sugai Y Aze S Narumiya A Kakizuka 1996 Expanded polyglutamine in the Machado-Joseph disease protein induces cell death in vitro and in vivo Nat Genet 13 196 202 8640226
    • (1996) Nat Genet , vol.13 , pp. 196-202
    • Ikeda, H.1    Yamaguchi, M.2    Sugai, S.3    Aze, Y.4    Narumiya, S.5    Kakizuka, A.6
  • 75
    • 24944482408 scopus 로고    scopus 로고
    • Increased susceptibility of cytoplasmic over nuclear polyglutamine aggregates to autophagic degradation
    • 16141322
    • A Iwata JC Christianson M Bucci, et al. 2005 Increased susceptibility of cytoplasmic over nuclear polyglutamine aggregates to autophagic degradation Proc Natl Acad Sci USA 102 13135 13140 16141322
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 13135-13140
    • Iwata, A.1    Christianson, J.C.2    Bucci, M.3
  • 76
    • 70349194529 scopus 로고    scopus 로고
    • The impact of ataxin-1-like histidine insertions on polyglutamine aggregation
    • 19541676
    • M Jayaraman R Kodali R Wetzel 2009 The impact of ataxin-1-like histidine insertions on polyglutamine aggregation Protein Eng Des Sel 22 469 478 19541676
    • (2009) Protein Eng des Sel , vol.22 , pp. 469-478
    • Jayaraman, M.1    Kodali, R.2    Wetzel, R.3
  • 77
    • 63049132756 scopus 로고    scopus 로고
    • Acetylation targets mutant huntingtin to autophagosomes for degradation
    • 19345187
    • H Jeong F Then TJ Melia, et al. 2009 Acetylation targets mutant huntingtin to autophagosomes for degradation Cell 137 60 72 19345187
    • (2009) Cell , vol.137 , pp. 60-72
    • Jeong, H.1    Then, F.2    Melia, T.J.3
  • 78
    • 68949219079 scopus 로고    scopus 로고
    • Polyglutamine expansion in huntingtin alters its interaction with phospholipids
    • 19566678
    • KB Kegel E Sapp J Alexander, et al. 2009 Polyglutamine expansion in huntingtin alters its interaction with phospholipids J Neurochem 110 1585 1597 19566678
    • (2009) J Neurochem , vol.110 , pp. 1585-1597
    • Kegel, K.B.1    Sapp, E.2    Alexander, J.3
  • 79
    • 68249127932 scopus 로고    scopus 로고
    • Polyglutamine expansion in huntingtin increases its insertion into lipid bilayers
    • 19607813
    • KB Kegel V Schewkunow E Sapp, et al. 2009 Polyglutamine expansion in huntingtin increases its insertion into lipid bilayers Biochem Biophys Res Comm 387 472 475 19607813
    • (2009) Biochem Biophys Res Comm , vol.387 , pp. 472-475
    • Kegel, K.B.1    Schewkunow, V.2    Sapp, E.3
  • 82
    • 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
    • 11675509
    • YJ Kim Y Yi E Sapp, et al. 2001 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 USA 98 12784 12789 11675509
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 12784-12789
    • Kim, Y.J.1    Yi, Y.2    Sapp, E.3
  • 83
    • 33749176269 scopus 로고    scopus 로고
    • Cytosolic chaperonin prevents polyglutamine toxicity with altering the aggregation state
    • 16980958
    • A Kitamura H Kubota C-G Pack, et al. 2006 Cytosolic chaperonin prevents polyglutamine toxicity with altering the aggregation state Nat Cell Biol 8 1163 1169 16980958
    • (2006) Nat Cell Biol , vol.8 , pp. 1163-1169
    • Kitamura, A.1    Kubota, H.2    Pack, C.-G.3
  • 84
    • 0032590053 scopus 로고    scopus 로고
    • Huntington aggregates may not predict neuronal death in Huntington's disease
    • 10589536
    • S Kuemmerle CA Gutekunst AM Klein, et al. 1999 Huntington aggregates may not predict neuronal death in Huntington's disease Ann Neurol 46 842 849 10589536
    • (1999) Ann Neurol , vol.46 , pp. 842-849
    • Kuemmerle, S.1    Gutekunst, C.A.2    Klein, A.M.3
  • 85
    • 66449106372 scopus 로고    scopus 로고
    • Conformational targeting of fibrillar polyglutamine proteins in live cells escalates aggregation and cytotoxicity
    • 19492089
    • E Kvam BL Nannenga MS Wang Z Jia MR Sierks A Messer 2009 Conformational targeting of fibrillar polyglutamine proteins in live cells escalates aggregation and cytotoxicity PLoS One 4 e5727 19492089
    • (2009) PLoS One , vol.4 , pp. 5727
    • Kvam, E.1    Nannenga, B.L.2    Wang, M.S.3    Jia, Z.4    Sierks, M.R.5    Messer, A.6
  • 86
    • 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
    • 20086007
    • C Landles K Sathasivam A Weiss, et al. 2010 Proteolysis of mutant huntingtin produces an exon 1 fragment that accumulates as an aggregated protein in neuronal nuclei in Huntington Disease J Biol Chem 285 8808 8823 20086007
    • (2010) J Biol Chem , vol.285 , pp. 8808-8823
    • Landles, C.1    Sathasivam, K.2    Weiss, A.3
  • 87
    • 0036415838 scopus 로고    scopus 로고
    • Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils
    • 12367530
    • HA Lashuel BM Petre J Wall, et al. 2002 Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils J Mol Biol 322 1089 1102 12367530
    • (2002) J Mol Biol , vol.322 , pp. 1089-1102
    • Lashuel, H.A.1    Petre, B.M.2    Wall, J.3
  • 88
    • 0031609016 scopus 로고    scopus 로고
    • Modeling protein homopolymeric repeats: Possible polyglutamine structural motifs for Huntington's disease
    • 9783215
    • RH Lathrop M Casale DJ Tobias JL Marsh L Thompson 1998 Modeling protein homopolymeric repeats: possible polyglutamine structural motifs for Huntington's disease Proc Int Conf Intell Syst Mol Biol 6 105 114 9783215
    • (1998) Proc Int Conf Intell Syst Mol Biol , vol.6 , pp. 105-114
    • Lathrop, R.H.1    Casale, M.2    Tobias, D.J.3    Marsh, J.L.4    Thompson, L.5
  • 89
    • 35848945494 scopus 로고    scopus 로고
    • Reconsidering the mechanism of polyglutamine peptide aggregation
    • 17929830
    • CC Lee RH Walters RM Murphy 2007 Reconsidering the mechanism of polyglutamine peptide aggregation Biochemistry 46 12810 12820 17929830
    • (2007) Biochemistry , vol.46 , pp. 12810-12820
    • Lee, C.C.1    Walters, R.H.2    Murphy, R.M.3
  • 90
    • 34548399406 scopus 로고    scopus 로고
    • Unbiased gene expression analysis implicates the huntingtin polyglutamine tract in extra-mitochondrial energy metabolism
    • 17708681
    • J-M Lee EV Ivanova IS Seong, et al. 2007 Unbiased gene expression analysis implicates the huntingtin polyglutamine tract in extra-mitochondrial energy metabolism PLoS Genet 3 e135 17708681
    • (2007) PLoS Genet , vol.3 , pp. 135
    • Lee, J.-M.1    Ivanova, E.V.2    Seong, I.S.3
  • 91
    • 34548290480 scopus 로고    scopus 로고
    • Cellular prion protein (PrPC) protects neuronal cells from the effect of huntingtin aggregation
    • 17635996
    • K-J Lee A Panzera D Rogawski LE Greene E Eisenberg 2007 Cellular prion protein (PrPC) protects neuronal cells from the effect of huntingtin aggregation J Cell Sci 120 2663 2671 17635996
    • (2007) J Cell Sci , vol.120 , pp. 2663-2671
    • Lee, K.-J.1    Panzera, A.2    Rogawski, D.3    Greene, L.E.4    Eisenberg, E.5
  • 92
    • 1542267796 scopus 로고    scopus 로고
    • Cytoplasmic aggregates trap polyglutamine-containing proteins and block axonal transport in a Drosophila model of Huntington's disease
    • 14978262
    • W-CM Lee M Yoshihara JT Littleton 2004 Cytoplasmic aggregates trap polyglutamine-containing proteins and block axonal transport in a Drosophila model of Huntington's disease Proc Natl Acad Sci USA 101 3224 3229 14978262
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 3224-3229
    • W-Cm, L.1    Yoshihara, M.2    Littleton, J.T.3
  • 93
    • 69249139853 scopus 로고    scopus 로고
    • Monoclonal antibodies recognize distinct conformational epitopes formed by polyglutamine in a mutant huntingtin fragment
    • 19491400
    • J Legleiter GP Lotz J Miller, et al. 2009 Monoclonal antibodies recognize distinct conformational epitopes formed by polyglutamine in a mutant huntingtin fragment J Biol Chem 284 21647 21658 19491400
    • (2009) J Biol Chem , vol.284 , pp. 21647-21658
    • Legleiter, J.1    Lotz, G.P.2    Miller, J.3
  • 94
    • 77951988103 scopus 로고    scopus 로고
    • Mutant Huntingtin fragments form oligomers in a polyglutamine length-dependent manner in vitro and in vivo
    • 20220138
    • J Legleiter E Mitchell GP Lotz, et al. 2010 Mutant Huntingtin fragments form oligomers in a polyglutamine length-dependent manner in vitro and in vivo J Biol Chem 285 14777 14790 20220138
    • (2010) J Biol Chem , vol.285 , pp. 14777-14790
    • Legleiter, J.1    Mitchell, E.2    Lotz, G.P.3
  • 95
    • 15144342225 scopus 로고    scopus 로고
    • Nuclear inclusions of the androgen receptor protein in spinal and bulbar muscular atrophy
    • 9708548
    • M Li S Miwa Y Kobayashi, et al. 1998 Nuclear inclusions of the androgen receptor protein in spinal and bulbar muscular atrophy Ann Neurol 44 249 254 9708548
    • (1998) Ann Neurol , vol.44 , pp. 249-254
    • Li, M.1    Miwa, S.2    Kobayashi, Y.3
  • 96
    • 0033025958 scopus 로고    scopus 로고
    • Distribution of inclusions in neuronal nuclei and dystrophic neurites in Huntington disease brain
    • ML Maat-Shieman JC Dorsman MA Smoor, et al. 1999 Distribution of inclusions in neuronal nuclei and dystrophic neurites in Huntington disease brain J Neuropathol Exp Neurol 58 129 137
    • (1999) J Neuropathol Exp Neurol , vol.58 , pp. 129-137
    • Maat-Shieman, M.L.1    Dorsman, J.C.2    Smoor, M.A.3
  • 98
    • 10744221735 scopus 로고    scopus 로고
    • Intergenerational instability and marked anticipation in SCA-17
    • 14638975
    • F Maltecca A Filla I Castaldo, et al. 2003 Intergenerational instability and marked anticipation in SCA-17 Neurology 61 1441 1443 14638975
    • (2003) Neurology , vol.61 , pp. 1441-1443
    • Maltecca, F.1    Filla, A.2    Castaldo, I.3
  • 99
    • 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
    • 8898202
    • L Mangiarini K Sathasivam M Seller, 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 8898202
    • (1996) Cell , vol.87 , pp. 493-506
    • Mangiarini, L.1    Sathasivam, K.2    Seller, M.3
  • 100
    • 17844389364 scopus 로고    scopus 로고
    • The wide spectrum of spinocerebellar ataxias (SCAs)
    • 15895552
    • M-U Manto 2005 The wide spectrum of spinocerebellar ataxias (SCAs) Cerebellum 4 2 6 15895552
    • (2005) Cerebellum , vol.4 , pp. 2-6
    • Manto, M.-U.1
  • 101
    • 33747032067 scopus 로고    scopus 로고
    • Spontaneous formation of annular structures observed in molecular dynamics simulations of polyglutamine peptides
    • 16678490
    • AJ Marchut CK Hall 2006 Spontaneous formation of annular structures observed in molecular dynamics simulations of polyglutamine peptides Comput Biol Chem 30 215 218 16678490
    • (2006) Comput Biol Chem , vol.30 , pp. 215-218
    • Marchut, A.J.1    Hall, C.K.2
  • 102
    • 0034110465 scopus 로고    scopus 로고
    • Expanded polyglutamine peptides alone are intrinsically cytotoxic and cause neurodegeneration in Drosophila
    • 10587574
    • JL Marsh H Walker H Theisen, et al. 2000 Expanded polyglutamine peptides alone are intrinsically cytotoxic and cause neurodegeneration in Drosophila Hum Mol Genet 9 13 25 10587574
    • (2000) Hum Mol Genet , vol.9 , pp. 13-25
    • Marsh, J.L.1    Walker, H.2    Theisen, H.3
  • 103
    • 0037181179 scopus 로고    scopus 로고
    • Solution structure of polyglutamine tracts in GST-polyglutamine fusion proteins
    • 11904162
    • L Masino G Kelly K Leonard Y Trottier A Pastore 2002 Solution structure of polyglutamine tracts in GST-polyglutamine fusion proteins FEBS Lett 513 267 272 11904162
    • (2002) FEBS Lett , vol.513 , pp. 267-272
    • Masino, L.1    Kelly, G.2    Leonard, K.3    Trottier, Y.4    Pastore, A.5
  • 104
    • 0036669907 scopus 로고    scopus 로고
    • Glutamine repeats: Structural hypotheses and neurodegeneration
    • 12196134
    • L Masino A Pastore 2002 Glutamine repeats: structural hypotheses and neurodegeneration Biochem Soc Trans 30 548 551 12196134
    • (2002) Biochem Soc Trans , vol.30 , pp. 548-551
    • Masino, L.1    Pastore, A.2
  • 105
    • 3042540196 scopus 로고    scopus 로고
    • Molecular mechanisms of androgen receptor-mediated gene regulation: Structure-function analysis of the AF-1 domain
    • 15163303
    • I McEwan 2004 Molecular mechanisms of androgen receptor-mediated gene regulation: structure-function analysis of the AF-1 domain Endocr Relat Cancer 11 281 293 15163303
    • (2004) Endocr Relat Cancer , vol.11 , pp. 281-293
    • McEwan, I.1
  • 106
    • 0037053566 scopus 로고    scopus 로고
    • Huntingtin toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1
    • 12058016
    • AB Meriin X Zhang X He GP Newnam YO Chernoff MY Sherman 2002 Huntingtin toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1 J Cell Biol 157 997 1004 12058016
    • (2002) J Cell Biol , vol.157 , pp. 997-1004
    • Meriin, A.B.1    Zhang, X.2    He, X.3    Newnam, G.P.4    Chernoff, Y.O.5    Sherman, M.Y.6
  • 107
    • 37449011119 scopus 로고    scopus 로고
    • Corticostriatal synaptic function in mouse models of Huntington's disease: Early effects of huntingtin repeat length and protein load
    • 17947312
    • AJ Milnerwood LA Raymond 2007 Corticostriatal synaptic function in mouse models of Huntington's disease: early effects of huntingtin repeat length and protein load J Physiol 585 817 831 17947312
    • (2007) J Physiol , vol.585 , pp. 817-831
    • Milnerwood, A.J.1    Raymond, L.A.2
  • 108
    • 0029088140 scopus 로고
    • New tubular single-stranded helix of poly-l-amino acids suggested by molecular mechanics calculations: I. Homopolypeptides in isolated environments
    • 8519967
    • H Monoi 1995 New tubular single-stranded helix of poly-l-amino acids suggested by molecular mechanics calculations: I. Homopolypeptides in isolated environments Biophys J 69 1130 1141 8519967
    • (1995) Biophys J , vol.69 , pp. 1130-1141
    • Monoi, H.1
  • 109
    • 0034125918 scopus 로고    scopus 로고
    • Poly-l-glutamine forms cation channels: Relevance to the pathogenesis of the polyglutamine diseases
    • 10827970
    • H Monoi S Futaki S-I Kugimiya H Minakata K Yoshihara 2000 Poly-l-glutamine forms cation channels: relevance to the pathogenesis of the polyglutamine diseases Biophys J 78 2892 2899 10827970
    • (2000) Biophys J , vol.78 , pp. 2892-2899
    • Monoi, H.1    Futaki, S.2    Kugimiya, S.-I.3    Minakata, H.4    Yoshihara, K.5
  • 110
    • 0037154229 scopus 로고    scopus 로고
    • Requirement of an intact microtubule cytoskeleton for aggregation and inclusion body formation by a mutant huntingtin fragment
    • 11792857
    • PJ Muchowski K Ning C D'Souza-Schorey S Fields 2002 Requirement of an intact microtubule cytoskeleton for aggregation and inclusion body formation by a mutant huntingtin fragment Proc Natl Acad Sci USA 99 727 732 11792857
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 727-732
    • Muchowski, P.J.1    Ning, K.2    D'Souza-Schorey, C.3    Fields, S.4
  • 111
    • 23344440853 scopus 로고    scopus 로고
    • Formation of morphologically similar globular aggregates from diverse aggregation-prone proteins in mammalian cells
    • 16040812
    • H Mukai T Isagawa E Goyama, et al. 2005 Formation of morphologically similar globular aggregates from diverse aggregation-prone proteins in mammalian cells Proc Natl Acad Sci USA 102 10887 10892 16040812
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 10887-10892
    • Mukai, H.1    Isagawa, T.2    Goyama, E.3
  • 112
    • 69249090927 scopus 로고    scopus 로고
    • Small ubiquitin-like modifier (SUMO) modification of the androgen receptor attenuates polyglutamine-mediated aggregation
    • 19497852
    • S Mukherjee M Thomas N Dadgar AP Lieberman JA Iniquez-Lluhi 2009 Small ubiquitin-like modifier (SUMO) modification of the androgen receptor attenuates polyglutamine-mediated aggregation J Biol Chem 284 21296 21306 19497852
    • (2009) J Biol Chem , vol.284 , pp. 21296-21306
    • Mukherjee, S.1    Thomas, M.2    Dadgar, N.3    Lieberman, A.P.4    Iniquez-Lluhi, J.A.5
  • 113
    • 34247247115 scopus 로고    scopus 로고
    • A toxic monomeric conformer of the polyglutamine protein
    • 17369839
    • Y Nagai T Inui HA Popiel, et al. 2007 A toxic monomeric conformer of the polyglutamine protein Nat Struct Mol Biol 14 332 340 17369839
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 332-340
    • Nagai, Y.1    Inui, T.2    Popiel, H.A.3
  • 114
    • 67649856863 scopus 로고    scopus 로고
    • Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity
    • 19487684
    • Y Nekooki-Machida M Kurosawa N Nukina K Ito T Oda M Tanaka 2009 Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity Proc Natl Acad Sci USA 106 9679 9684 19487684
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 9679-9684
    • Nekooki-Machida, Y.1    Kurosawa, M.2    Nukina, N.3    Ito, K.4    Oda, T.5    Tanaka, M.6
  • 115
    • 34247229733 scopus 로고    scopus 로고
    • Ataxin-2 interacts with the DEAD/H-Box RNA helicase DDX6 and interferes with P-bodies and stress granules
    • 17392519
    • U Nonhoff M Ralser F Welzel, et al. 2007 Ataxin-2 interacts with the DEAD/H-Box RNA helicase DDX6 and interferes with P-bodies and stress granules Mol Biol Cell 18 1385 1396 17392519
    • (2007) Mol Biol Cell , vol.18 , pp. 1385-1396
    • Nonhoff, U.1    Ralser, M.2    Welzel, F.3
  • 116
    • 70349295278 scopus 로고    scopus 로고
    • Structure neurotoxicity relationships of amyloid-beta protein oligomers
    • 19706468
    • K Ono MM Condron DB Teplow 2009 Structure neurotoxicity relationships of amyloid-beta protein oligomers Proc Natl Acad Sci USA 106 14745 14750 19706468
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 14745-14750
    • Ono, K.1    Condron, M.M.2    Teplow, D.B.3
  • 117
    • 40849147435 scopus 로고    scopus 로고
    • N-terminal mutant huntingtin associates with mitochondria and impairs mitochondrial trafficking
    • 18337408
    • AL Orr S Li C-E Wang, et al. 2008 N-terminal mutant huntingtin associates with mitochondria and impairs mitochondrial trafficking J Neurosci 28 2783 2792 18337408
    • (2008) J Neurosci , vol.28 , pp. 2783-2792
    • Orr, A.L.1    Li, S.2    Wang, C.-E.3
  • 118
    • 34547692622 scopus 로고    scopus 로고
    • Trinucleotide repeat disorders
    • 17417937
    • HT Orr HY Zoghbi 2007 Trinucleotide repeat disorders Ann Rev Neurosci 30 575 621 17417937
    • (2007) Ann Rev Neurosci , vol.30 , pp. 575-621
    • Orr, H.T.1    Zoghbi, H.Y.2
  • 119
    • 25444456100 scopus 로고    scopus 로고
    • Modified single-stranded oligonucleotides inhibit aggregate formation and toxicity induced by expanded polyglutamine
    • 15456939
    • H Parekh-Olmedo J Wang J Gusella E Kmiec 2004 Modified single-stranded oligonucleotides inhibit aggregate formation and toxicity induced by expanded polyglutamine J Mol Neurosci 24 257 267 15456939
    • (2004) J Mol Neurosci , vol.24 , pp. 257-267
    • Parekh-Olmedo, H.1    Wang, J.2    Gusella, J.3    Kmiec, E.4
  • 120
    • 0030850412 scopus 로고    scopus 로고
    • Intranuclear inclusions of expanded polyglutamine protein in spinocerebellar ataxia type 3
    • 9292723
    • HL Paulson MK Perez Y Trottier, et al. 1997 Intranuclear inclusions of expanded polyglutamine protein in spinocerebellar ataxia type 3 Neuron 19 333 344 9292723
    • (1997) Neuron , vol.19 , pp. 333-344
    • Paulson, H.L.1    Perez, M.K.2    Trottier, Y.3
  • 121
    • 33745637954 scopus 로고    scopus 로고
    • Microglial activation correlates with severity in Huntington disease: A clinical and PET study
    • 16769933
    • N Pavese A Gerhard YF Tai, et al. 2006 Microglial activation correlates with severity in Huntington disease: a clinical and PET study Neurology 66 1638 1643 16769933
    • (2006) Neurology , vol.66 , pp. 1638-1643
    • Pavese, N.1    Gerhard, A.2    Tai, Y.F.3
  • 122
  • 124
    • 0028283985 scopus 로고
    • Glutamine repeats as polar zippers: Their possible role in inherited neurodegenerative diseases
    • 8202492
    • MF Perutz T Johnson M Suzuki JT Finch 1994 Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases Proc Natl Acad Sci USA 91 5355 5358 8202492
    • (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
  • 125
    • 15544372340 scopus 로고    scopus 로고
    • A structure-based analysis of huntingtin mutant polyglutamine aggregation and toxicity: Evidence for a compact beta-sheet structure
    • 15689354
    • MA Poirier H Jiang CA Ross 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 15689354
    • (2005) Hum Mol Genet , vol.14 , pp. 765-774
    • Poirier, M.A.1    Jiang, H.2    Ross, C.A.3
  • 126
    • 0037174879 scopus 로고    scopus 로고
    • Huntingtin spheroids and protofibrils as precursors in polyglutamine fibrilization
    • 12171927
    • MA Poirier H Li J Macosko S Cai M Amzel CA Ross 2002 Huntingtin spheroids and protofibrils as precursors in polyglutamine fibrilization J Biol Chem 277 41032 41037 12171927
    • (2002) J Biol Chem , vol.277 , pp. 41032-41037
    • Poirier, M.A.1    Li, H.2    MacOsko, J.3    Cai, S.4    Amzel, M.5    Ross, C.A.6
  • 127
    • 11144358201 scopus 로고    scopus 로고
    • Disruption of the toxic conformation of the expanded polyglutamine stretch leads to suppression of aggregate formation and cytotoxicity
    • 15094397
    • HA Popiel Y Nagai O Onodera, et al. 2004 Disruption of the toxic conformation of the expanded polyglutamine stretch leads to suppression of aggregate formation and cytotoxicity Biochem Biophys Res Comm 317 1200 1206 15094397
    • (2004) Biochem Biophys Res Comm , vol.317 , pp. 1200-1206
    • Popiel, H.A.1    Nagai, Y.2    Onodera, O.3
  • 128
    • 45149115090 scopus 로고    scopus 로고
    • Proteasomes cleave at multiple sites within polyglutamine tracts
    • 18343811
    • G Pratt M Rechsteiner 2008 Proteasomes cleave at multiple sites within polyglutamine tracts J Biol Chem 283 12919 12925 18343811
    • (2008) J Biol Chem , vol.283 , pp. 12919-12925
    • Pratt, G.1    Rechsteiner, M.2
  • 129
    • 70349422148 scopus 로고    scopus 로고
    • Role of mitochondrial dysfunction in the pathogenesis of Huntington's disease
    • 19622387
    • RA Quintanilla GVW Johnson 2009 Role of mitochondrial dysfunction in the pathogenesis of Huntington's disease Brain Res Bull 80 242 247 19622387
    • (2009) Brain Res Bull , vol.80 , pp. 242-247
    • Quintanilla, R.A.1    Johnson, G.V.W.2
  • 130
    • 42749092501 scopus 로고    scopus 로고
    • Expression of the small heat shock protein family in the mouse CNS: Differential anatomical and biochemical compartmentalization
    • 18384969
    • S Quraishe A Asuni WC Boelens V O'Connor A Wyttenbach 2008 Expression of the small heat shock protein family in the mouse CNS: differential anatomical and biochemical compartmentalization Neuroscience 153 483 491 18384969
    • (2008) Neuroscience , vol.153 , pp. 483-491
    • Quraishe, S.1    Asuni, A.2    Boelens, W.C.3    O'Connor, V.4    Wyttenbach, A.5
  • 131
    • 0842265636 scopus 로고    scopus 로고
    • The serum- and glucocorticoid-induced kinase SGK inhibits mutant huntingtin-induced toxicity by phosphorylating serine 421 of huntingtin
    • 14725621
    • H Rangone G Poizat J Troncoso, et al. 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 14725621
    • (2004) Eur J Neurosci , vol.19 , pp. 273-279
    • Rangone, H.1    Poizat, G.2    Troncoso, J.3
  • 132
    • 70350380897 scopus 로고    scopus 로고
    • Mimicking proteasomal release of polyglutamine peptides initiates aggregation and toxicity
    • 19690053
    • M Raspe J Gillis H Krol, et al. 2009 Mimicking proteasomal release of polyglutamine peptides initiates aggregation and toxicity J Cell Sci 122 3262 3271 19690053
    • (2009) J Cell Sci , vol.122 , pp. 3262-3271
    • Raspe, M.1    Gillis, J.2    Krol, H.3
  • 133
    • 0038364056 scopus 로고    scopus 로고
    • Raised intracellular glucose concentrations reduce aggregation and cell death caused by mutant huntingtin exon 1 by decreasing mTOR phosphorylation and inducing autophagy
    • 12700167
    • B Ravikumar A Stewart H Kita K Kato R Duden DC Rubinsztein 2003 Raised intracellular glucose concentrations reduce aggregation and cell death caused by mutant huntingtin exon 1 by decreasing mTOR phosphorylation and inducing autophagy Hum Mol Genet 12 985 994 12700167
    • (2003) Hum Mol Genet , vol.12 , pp. 985-994
    • Ravikumar, B.1    Stewart, A.2    Kita, H.3    Kato, K.4    Duden, R.5    Rubinsztein, D.C.6
  • 134
    • 59649095699 scopus 로고    scopus 로고
    • Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates
    • 19151706
    • P-H Ren JE Lauckner I Kachirskaia JE Heuser R Melki RR Kopito 2009 Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates Nat Cell Biol 11 219 225 19151706
    • (2009) Nat Cell Biol , vol.11 , pp. 219-225
    • Ren, P.-H.1    Lauckner, J.E.2    Kachirskaia, I.3    Heuser, J.E.4    Melki, R.5    Kopito, R.R.6
  • 135
    • 34147142944 scopus 로고    scopus 로고
    • Destabilization of non-pathological variants of ataxin-3 by metal ions results in aggregation/fibrillogenesis
    • 17300980
    • F Ricchelli P Fusi P Tortora, et al. 2007 Destabilization of non-pathological variants of ataxin-3 by metal ions results in aggregation/fibrillogenesis Int J Biochem Cell Biol 39 966 977 17300980
    • (2007) Int J Biochem Cell Biol , vol.39 , pp. 966-977
    • Ricchelli, F.1    Fusi, P.2    Tortora, P.3
  • 136
    • 33846540080 scopus 로고    scopus 로고
    • The first 17 amino acids of Huntingtin modulate its sub-cellular localization, aggregation and effects on calcium homeostasis
    • 17135277
    • E Rockabrand N Slepko A Pantalone, 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 17135277
    • (2007) Hum Mol Genet , vol.16 , pp. 61-77
    • Rockabrand, E.1    Slepko, N.2    Pantalone, A.3
  • 137
    • 3042718947 scopus 로고    scopus 로고
    • Targeting expression of expanded polyglutamine proteins to the endoplasmic reticulum or mitochondria prevents their aggregation
    • 15210964
    • E Rousseau B Dehay L Ben-Haïem Y Trottier M Morange A Bertolotti 2004 Targeting expression of expanded polyglutamine proteins to the endoplasmic reticulum or mitochondria prevents their aggregation Proc Natl Acad Sci USA 101 9648 9653 15210964
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 9648-9653
    • Rousseau, E.1    Dehay, B.2    Ben-Haïem, L.3    Trottier, Y.4    Morange, M.5    Bertolotti, A.6
  • 138
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • 17051204
    • DC Rubinsztein 2006 The roles of intracellular protein-degradation pathways in neurodegeneration Nature 443 780 786 17051204
    • (2006) Nature , vol.443 , pp. 780-786
    • Rubinsztein, D.C.1
  • 139
    • 0035111235 scopus 로고    scopus 로고
    • Early and progressive accumulation of reactive microglia in the Huntington disease brain
    • 11273004
    • E Sapp KB Kegel N Aronin, et al. 2001 Early and progressive accumulation of reactive microglia in the Huntington disease brain J Neuropathol Exp Neurol 60 161 172 11273004
    • (2001) J Neuropathol Exp Neurol , vol.60 , pp. 161-172
    • Sapp, E.1    Kegel, K.B.2    Aronin, N.3
  • 140
    • 0032987513 scopus 로고    scopus 로고
    • Axonal transport of N-terminal huntingtin suggests early pathology of corticostriatal projections in Huntington disease
    • 10029099
    • E Sapp J Penney A Young N Aronin J-P Vonsattel M DiFiglia 1999 Axonal transport of N-terminal huntingtin suggests early pathology of corticostriatal projections in Huntington disease J Neuropathol Exp Neurol 58 165 173 10029099
    • (1999) J Neuropathol Exp Neurol , vol.58 , pp. 165-173
    • Sapp, E.1    Penney, J.2    Young, A.3    Aronin, N.4    Vonsattel, J.-P.5    Difiglia, M.6
  • 141
    • 69949102831 scopus 로고    scopus 로고
    • Huntington's disease: The current state of research with peripheral tissues
    • 19460373
    • J Sassone C Colciago G Cislaghi V Silani A Ciammola 2009 Huntington's disease: the current state of research with peripheral tissues Exp Neurol 219 385 397 19460373
    • (2009) Exp Neurol , vol.219 , pp. 385-397
    • Sassone, J.1    Colciago, C.2    Cislaghi, G.3    Silani, V.4    Ciammola, A.5
  • 142
    • 0032919205 scopus 로고    scopus 로고
    • Formation of polyglutamine inclusions in non-CNS tissue
    • 10196370
    • K Sathasivam C Hobbs M Turmaine, et al. 1999 Formation of polyglutamine inclusions in non-CNS tissue Hum Mol Genet 8 813 822 10196370
    • (1999) Hum Mol Genet , vol.8 , pp. 813-822
    • Sathasivam, K.1    Hobbs, C.2    Turmaine, M.3
  • 143
    • 77649297870 scopus 로고    scopus 로고
    • Identical oligomeric and fibrillar structures captured from the brains of R6/2 and knock-in mouse models of Huntington's disease
    • 19825844
    • K Sathasivam A Lane J Legleiter, et al. 2010 Identical oligomeric and fibrillar structures captured from the brains of R6/2 and knock-in mouse models of Huntington's disease Hum Mol Genet 19 65 78 19825844
    • (2010) Hum Mol Genet , vol.19 , pp. 65-78
    • Sathasivam, K.1    Lane, A.2    Legleiter, J.3
  • 144
    • 0036962392 scopus 로고    scopus 로고
    • A drosophila homolog of the polyglutamine disease gene sca2 is a dosage-sensitive regulator of actin filament formation
    • 12524342
    • TF Satterfield SM Jackson LJ Pallanck 2002 A drosophila homolog of the polyglutamine disease gene sca2 is a dosage-sensitive regulator of actin filament formation Genetics 162 1687 1702 12524342
    • (2002) Genetics , vol.162 , pp. 1687-1702
    • Satterfield, T.F.1    Jackson, S.M.2    Pallanck, L.J.3
  • 145
    • 0032475931 scopus 로고    scopus 로고
    • Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions
    • 9778247
    • F Saudou S Finkbeiner D Devys ME Greenberg 1998 Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions Cell 95 55 66 9778247
    • (1998) Cell , vol.95 , pp. 55-66
    • Saudou, F.1    Finkbeiner, S.2    Devys, D.3    Greenberg, M.E.4
  • 146
    • 70349199064 scopus 로고    scopus 로고
    • Multi-domain misfolding: Understanding the aggregation pathway of polyglutamine proteins
    • 19589877
    • HM Saunders SP Bottomley 2009 Multi-domain misfolding: understanding the aggregation pathway of polyglutamine proteins Protein Eng Des Sel 22 447 451 19589877
    • (2009) Protein Eng des Sel , vol.22 , pp. 447-451
    • Saunders, H.M.1    Bottomley, S.P.2
  • 147
    • 18544400323 scopus 로고    scopus 로고
    • Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo
    • 9267034
    • E Scherzinger R Lurz M Turmaine, et al. 1997 Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo Cell 90 549 558 9267034
    • (1997) Cell , vol.90 , pp. 549-558
    • Scherzinger, E.1    Lurz, R.2    Turmaine, M.3
  • 148
    • 34247869645 scopus 로고    scopus 로고
    • Identification of anti-prion compounds as efficient inhibitors of polyglutamine protein aggregation in a zebrafish model
    • 17170113
    • NW Schiffer SA Broadley T Hirschberger, et al. 2007 Identification of anti-prion compounds as efficient inhibitors of polyglutamine protein aggregation in a zebrafish model J Biol Chem 282 9195 9203 17170113
    • (2007) J Biol Chem , vol.282 , pp. 9195-9203
    • Schiffer, N.W.1    Broadley, S.A.2    Hirschberger, T.3
  • 149
    • 57649138454 scopus 로고    scopus 로고
    • N-terminal polyglutamine-containing fragments inhibit androgen receptor transactivation function
    • 18844449
    • NW Schiffer J Ceraline FU Hartl SA Broadley 2008 N-terminal polyglutamine-containing fragments inhibit androgen receptor transactivation function Biol Chem 389 1455 1466 18844449
    • (2008) Biol Chem , vol.389 , pp. 1455-1466
    • Schiffer, N.W.1    Ceraline, J.2    Hartl, F.U.3    Broadley, S.A.4
  • 150
    • 33747633422 scopus 로고    scopus 로고
    • Huntingtin phosphorylation sites mapped by mass spectrometry
    • 16782707
    • B Schilling J Gafni C Torcassi, et al. 2006 Huntingtin phosphorylation sites mapped by mass spectrometry J Biol Chem 281 23686 23697 16782707
    • (2006) J Biol Chem , vol.281 , pp. 23686-23697
    • Schilling, B.1    Gafni, J.2    Torcassi, C.3
  • 151
    • 0037406093 scopus 로고    scopus 로고
    • Role of histidine interruption in mitigating the pathological effects of long polyglutamine stretches in SCA1: A molecular approach
    • 12717018
    • S Sen D Dash S Pasha SK Brahmachari 2003 Role of histidine interruption in mitigating the pathological effects of long polyglutamine stretches in SCA1: a molecular approach Protein Sci 12 953 962 12717018
    • (2003) Protein Sci , vol.12 , pp. 953-962
    • Sen, S.1    Dash, D.2    Pasha, S.3    Brahmachari, S.K.4
  • 152
    • 0032776447 scopus 로고    scopus 로고
    • Peptide models for inherited neurodegenerative disorders: Conformation and aggregation properties of long polyglutamine peptides with and without interruptions
    • 10452554
    • D Sharma S Sharma S Pasha SK Brahmachari 1999 Peptide models for inherited neurodegenerative disorders: conformation and aggregation properties of long polyglutamine peptides with and without interruptions FEBS Lett 456 181 185 10452554
    • (1999) FEBS Lett , vol.456 , pp. 181-185
    • Sharma, D.1    Sharma, S.2    Pasha, S.3    Brahmachari, S.K.4
  • 153
    • 14044278010 scopus 로고    scopus 로고
    • New model for crystalline polyglutamine assemblies and their connection with amyloid fibrils
    • P Sikorski E Atkins 2005 New model for crystalline polyglutamine assemblies and their connection with amyloid fibrils Biomacromolecule 6 425 432
    • (2005) Biomacromolecule , vol.6 , pp. 425-432
    • Sikorski, P.1    Atkins, E.2
  • 154
    • 0032052003 scopus 로고    scopus 로고
    • Huntingtin protein colocalizes with lesions of neurodegenerative diseases: An investigation in Huntington's, Alzheimer's, and Pick's Diseases
    • 9527890
    • SK Singhrao P Thomas JD Wood, et al. 1998 Huntingtin protein colocalizes with lesions of neurodegenerative diseases: an investigation in Huntington's, Alzheimer's, and Pick's Diseases Exp Neurol 150 213 222 9527890
    • (1998) Exp Neurol , vol.150 , pp. 213-222
    • Singhrao, S.K.1    Thomas, P.2    Wood, J.D.3
  • 155
    • 0037379416 scopus 로고    scopus 로고
    • Homozygosity for CAG mutation in Huntington disease is associated with a more severe clinical course
    • 12615650
    • F Squitieri C Gellera M Cannella, et al. 2003 Homozygosity for CAG mutation in Huntington disease is associated with a more severe clinical course Brain 126 946 955 12615650
    • (2003) Brain , vol.126 , pp. 946-955
    • Squitieri, F.1    Gellera, C.2    Cannella, M.3
  • 156
    • 11144353613 scopus 로고    scopus 로고
    • SUMO modification of huntingtin and Huntington's Disease pathology
    • 15064418
    • JS Steffan N Agrawal J Pallos, et al. 2004 SUMO modification of huntingtin and Huntington's Disease pathology Science 304 100 104 15064418
    • (2004) Science , vol.304 , pp. 100-104
    • Steffan, J.S.1    Agrawal, N.2    Pallos, J.3
  • 157
    • 0036798685 scopus 로고    scopus 로고
    • Intranuclear ataxin1 inclusions contain both fast- and slow-exchanging components
    • 12360291
    • DL Stenoien M Mielke MA Mancini 2002 Intranuclear ataxin1 inclusions contain both fast- and slow-exchanging components Nat Cell Biol 4 806 810 12360291
    • (2002) Nat Cell Biol , vol.4 , pp. 806-810
    • Stenoien, D.L.1    Mielke, M.2    Mancini, M.A.3
  • 158
    • 33645104605 scopus 로고    scopus 로고
    • Interaction of huntingtin fragments with brain membranes; Clues to early dysfunction in Huntington's disease
    • 16405500
    • J Suopanki C Götz G Lutsch, et al. 2006 Interaction of huntingtin fragments with brain membranes; clues to early dysfunction in Huntington's disease J Neurochem 96 870 884 16405500
    • (2006) J Neurochem , vol.96 , pp. 870-884
    • Suopanki, J.1    Götz, C.2    Lutsch, G.3
  • 159
    • 38349158062 scopus 로고    scopus 로고
    • Soluble polyglutamine oligomers formed prior to inclusion body formation are cytotoxic
    • 17947294
    • T Takahashi S Kikuchi S Katada Y Nagai M Nishizawa O Onodera 2008 Soluble polyglutamine oligomers formed prior to inclusion body formation are cytotoxic Hum Mol Genet 17 345 356 17947294
    • (2008) Hum Mol Genet , vol.17 , pp. 345-356
    • Takahashi, T.1    Kikuchi, S.2    Katada, S.3    Nagai, Y.4    Nishizawa, M.5    Onodera, O.6
  • 160
    • 34548227453 scopus 로고    scopus 로고
    • Detection of polyglutamine protein oligomers in cells by fluorescence correlation spectroscopy
    • 17573338
    • Y Takahashi Y Okamoto HA Popiel, et al. 2007 Detection of polyglutamine protein oligomers in cells by fluorescence correlation spectroscopy J Biol Chem 282 24039 24048 17573338
    • (2007) J Biol Chem , vol.282 , pp. 24039-24048
    • Takahashi, Y.1    Okamoto, Y.2    Popiel, H.A.3
  • 161
    • 33749177252 scopus 로고    scopus 로고
    • The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions
    • 16980959
    • S Tam R Geller C Spiess J Frydman 2006 The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions Nat Cell Biol 8 1155 1162 16980959
    • (2006) Nat Cell Biol , vol.8 , pp. 1155-1162
    • Tam, S.1    Geller, R.2    Spiess, C.3    Frydman, J.4
  • 162
    • 0035976971 scopus 로고    scopus 로고
    • Intra- and intermolecular beta-pleated sheet formation in glutamine-repeat inserted myoglobin as a model for polyglutamine diseases
    • 11584007
    • M Tanaka I Morishima T Akagi T Hashikawa N Nukina 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 11584007
    • (2001) J Biol Chem , vol.276 , pp. 45470-45475
    • Tanaka, M.1    Morishima, I.2    Akagi, T.3    Hashikawa, T.4    Nukina, N.5
  • 163
    • 0037415751 scopus 로고    scopus 로고
    • From Alzheimer to Huntington: Why is a structural understanding so difficult?
    • 12554637
    • PA Temussi L Masino A Pastore 2003 From Alzheimer to Huntington: why is a structural understanding so difficult? EMBO J 22 355 361 12554637
    • (2003) EMBO J , vol.22 , pp. 355-361
    • Temussi, P.A.1    Masino, L.2    Pastore, A.3
  • 164
    • 64049119303 scopus 로고    scopus 로고
    • Polyglutamine disruption of the huntingtin exon 1 N terminus triggers a complex aggregation mechanism
    • 19270701
    • AK Thakur M Jayaraman R Mishra, et al. 2009 Polyglutamine disruption of the huntingtin exon 1 N terminus triggers a complex aggregation mechanism Nat Struct Mol Biol 16 380 389 19270701
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 380-389
    • Thakur, A.K.1    Jayaraman, M.2    Mishra, R.3
  • 165
    • 0037168642 scopus 로고    scopus 로고
    • Mutational analysis of the structural organization of polyglutamine aggregates
    • 12444250
    • AK Thakur R Wetzel 2002 Mutational analysis of the structural organization of polyglutamine aggregates Proc Natl Acad Sci USA 99 17014 17019 12444250
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 17014-17019
    • Thakur, A.K.1    Wetzel, R.2
  • 166
    • 1642447764 scopus 로고    scopus 로고
    • Ataxin 1, a SCA1 neurodegenerative disorder protein, is functionally linked to the silencing mediator of retinoid and thyroid hormone receptors
    • 15016912
    • C-C Tsai H-Y Kao A Mitzutani, et al. 2004 Ataxin 1, a SCA1 neurodegenerative disorder protein, is functionally linked to the silencing mediator of retinoid and thyroid hormone receptors Proc Natl Acad Sci USA 101 4047 4052 15016912
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 4047-4052
    • Tsai, C.-C.1    Kao, H.-Y.2    Mitzutani, A.3
  • 167
    • 1842766144 scopus 로고    scopus 로고
    • Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins
    • 15068806
    • P Venkatraman R Wetzel M Tanaka N Nukina AL Goldberg 2004 Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins Mol Cell 14 95 104 15068806
    • (2004) Mol Cell , vol.14 , pp. 95-104
    • Venkatraman, P.1    Wetzel, R.2    Tanaka, M.3    Nukina, N.4    Goldberg, A.L.5
  • 168
    • 68949127591 scopus 로고    scopus 로고
    • Thermodynamics of β-Sheet formation in polyglutamine
    • 19580768
    • A Vitalis N Lyle RV Pappu 2009 Thermodynamics of β-Sheet formation in polyglutamine Biophys J 97 303 311 19580768
    • (2009) Biophys J , vol.97 , pp. 303-311
    • Vitalis, A.1    Lyle, N.2    Pappu, R.V.3
  • 169
    • 54249132105 scopus 로고    scopus 로고
    • Atomistic simulations of the effects of polyglutamine chain length and solvent quality on conformational equilibria and spontaneous homodimerization
    • 18824003
    • A Vitalis X Wang RV Pappu 2008 Atomistic simulations of the effects of polyglutamine chain length and solvent quality on conformational equilibria and spontaneous homodimerization J Mol Biol 384 279 297 18824003
    • (2008) J Mol Biol , vol.384 , pp. 279-297
    • Vitalis, A.1    Wang, X.2    Pappu, R.V.3
  • 170
    • 36949012566 scopus 로고    scopus 로고
    • Huntington disease models and human neuropathology: Similarities and differences
    • 17978822
    • J Vonsattel 2008 Huntington disease models and human neuropathology: similarities and differences Acta Neuropathol 115 55 69 17978822
    • (2008) Acta Neuropathol , vol.115 , pp. 55-69
    • Vonsattel, J.1
  • 171
    • 67650745109 scopus 로고    scopus 로고
    • Loss of Hsp70 exacerbates pathogenesis but not levels of fibrillar aggregates in a mouse model of Huntington's Disease
    • 19605647
    • JL Wacker S-Y Huang AD Steele, et al. 2009 Loss of Hsp70 exacerbates pathogenesis but not levels of fibrillar aggregates in a mouse model of Huntington's Disease J Neurosci 29 9104 9114 19605647
    • (2009) J Neurosci , vol.29 , pp. 9104-9114
    • Wacker, J.L.1    Huang, S.-Y.2    Steele, A.D.3
  • 172
    • 16544383250 scopus 로고    scopus 로고
    • Hsp70 and Hsp40 attenuate formation of spherical and annular polyglutamine oligomers by partitioning monomer
    • 15543156
    • JL Wacker MH Zareie H Fong M Sarikaya PJ Muchowski 2004 Hsp70 and Hsp40 attenuate formation of spherical and annular polyglutamine oligomers by partitioning monomer Nat Struct Mol Biol 11 1215 1222 15543156
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 1215-1222
    • Wacker, J.L.1    Zareie, M.H.2    Fong, H.3    Sarikaya, M.4    Muchowski, P.J.5
  • 173
    • 15844414208 scopus 로고    scopus 로고
    • The roles of proteolysis and nuclear localisation in the toxicity of the polyglutamine diseases. A review
    • 15639797
    • R Walsh E Storey D Stefani L Kelly V Turnbull 2005 The roles of proteolysis and nuclear localisation in the toxicity of the polyglutamine diseases. A review Neurotox Res 7 43 57 15639797
    • (2005) Neurotox Res , vol.7 , pp. 43-57
    • Walsh, R.1    Storey, E.2    Stefani, D.3    Kelly, L.4    Turnbull, V.5
  • 174
    • 70349838220 scopus 로고    scopus 로고
    • Examining polyglutamine peptide length: A connection between collapsed conformations and increased aggregation
    • 19699209
    • RH Walters RM Murphy 2009 Examining polyglutamine peptide length: a connection between collapsed conformations and increased aggregation J Mol Biol 393 978 992 19699209
    • (2009) J Mol Biol , vol.393 , pp. 978-992
    • Walters, R.H.1    Murphy, R.M.2
  • 175
    • 58949099388 scopus 로고    scopus 로고
    • Effects of overexpression of Huntingtin proteins on mitochondrial integrity
    • 19039036
    • H Wang PJ Lim M Karbowski MJ Monteiro 2009 Effects of overexpression of Huntingtin proteins on mitochondrial integrity Hum Mol Genet 18 737 752 19039036
    • (2009) Hum Mol Genet , vol.18 , pp. 737-752
    • Wang, H.1    Lim, P.J.2    Karbowski, M.3    Monteiro, M.J.4
  • 176
    • 41549129945 scopus 로고    scopus 로고
    • Impaired ubiquitin-proteasome system activity in the synapses of Huntington's disease mice
    • 18362179
    • J Wang C-E Wang A Orr S Tydlacka S-H Li X-J Li 2008 Impaired ubiquitin-proteasome system activity in the synapses of Huntington's disease mice J Cell Biol 180 1177 1189 18362179
    • (2008) J Cell Biol , vol.180 , pp. 1177-1189
    • Wang, J.1    Wang, C.-E.2    Orr, A.3    Tydlacka, S.4    Li, S.-H.5    Li, X.-J.6
  • 177
    • 48749095822 scopus 로고    scopus 로고
    • Characterization of proteins associated with polyglutamine aggregates: A novel approach towards isolation of aggregates from protein conformation disorders
    • 19164926
    • Y Wang AB Meriin CE Costello MY Sherman 2007 Characterization of proteins associated with polyglutamine aggregates: a novel approach towards isolation of aggregates from protein conformation disorders Prion 1 128 135 19164926
    • (2007) Prion , vol.1 , pp. 128-135
    • Wang, Y.1    Meriin, A.B.2    Costello, C.E.3    Sherman, M.Y.4
  • 178
    • 38049139425 scopus 로고    scopus 로고
    • Sensitive biochemical aggregate detection reveals aggregation onset before symptom development in cellular and murine models of Huntington's disease
    • 17986219
    • A Weiss C Klein B Woodman, et al. 2008 Sensitive biochemical aggregate detection reveals aggregation onset before symptom development in cellular and murine models of Huntington's disease J Neurochem 104 846 858 17986219
    • (2008) J Neurochem , vol.104 , pp. 846-858
    • Weiss, A.1    Klein, C.2    Woodman, B.3
  • 179
    • 0032502715 scopus 로고    scopus 로고
    • Caspase cleavage of gene products associated with triplet expansion disorders generates truncated fragments containing the polyglutamine tract
    • 9535906
    • CL Wellington LM Ellerby AS Hackam, 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 9535906
    • (1998) J Biol Chem , vol.273 , pp. 9158-9167
    • Wellington, C.L.1    Ellerby, L.M.2    Hackam, A.S.3
  • 180
    • 12144288251 scopus 로고    scopus 로고
    • Venezuelan kindreds reveal that genetic and environmental factors modulate Huntington's disease age of onset
    • 14993615
    • NS Wexler 2004 Venezuelan kindreds reveal that genetic and environmental factors modulate Huntington's disease age of onset Proc Natl Acad Sci USA 101 3498 3503 14993615
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 3498-3503
    • Wexler, N.S.1
  • 182
    • 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
    • 19084066
    • AJ Williams TM Knutson VF Colomer Gould HL Paulson 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 19084066
    • (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
  • 183
    • 77649271684 scopus 로고    scopus 로고
    • Modulation of polyglutamine conformations and dimer formation by the N-terminus of huntingtin
    • TE Williamson A Vitalis SL Crick RV Pappu 2010 Modulation of polyglutamine conformations and dimer formation by the N-terminus of huntingtin J Mol Biol 396 1230 1295
    • (2010) J Mol Biol , vol.396 , pp. 1230-1295
    • Williamson, T.E.1    Vitalis, A.2    Crick, S.L.3    Pappu, R.V.4
  • 184
    • 0031807249 scopus 로고    scopus 로고
    • Atrophin-1, the DRPLA gene product, interacts with two families of WW domain-containing proteins
    • 9647693
    • JD Wood J Yuan RL Margolis, et al. 1998 Atrophin-1, the DRPLA gene product, interacts with two families of WW domain-containing proteins Mol Cell Neurosci 11 149 160 9647693
    • (1998) Mol Cell Neurosci , vol.11 , pp. 149-160
    • Wood, J.D.1    Yuan, J.2    Margolis, R.L.3
  • 185
    • 0035880474 scopus 로고    scopus 로고
    • Polyglutamine expansions cause decreased CRE-mediated transcription and early gene expression changes prior to cell death in an inducible cell model of Huntington's disease
    • 11532992
    • A Wyttenbach J Swartz H Kita, et al. 2001 Polyglutamine expansions cause decreased CRE-mediated transcription and early gene expression changes prior to cell death in an inducible cell model of Huntington's disease Hum Mol Genet 10 1829 1845 11532992
    • (2001) Hum Mol Genet , vol.10 , pp. 1829-1845
    • Wyttenbach, A.1    Swartz, J.2    Kita, H.3
  • 186
    • 0035149350 scopus 로고    scopus 로고
    • Interaction between neuronal intranuclear inclusions and promyelocytic leukemia protein nuclear and coiled bodies in CAG repeat diseases
    • 11696439
    • M Yamada T Sato T Shimohata, et al. 2001 Interaction between neuronal intranuclear inclusions and promyelocytic leukemia protein nuclear and coiled bodies in CAG repeat diseases Am J Pathol 159 1785 1795 11696439
    • (2001) Am J Pathol , vol.159 , pp. 1785-1795
    • Yamada, M.1    Sato, T.2    Shimohata, T.3
  • 187
    • 0034737299 scopus 로고    scopus 로고
    • Reversal of neuropathology and motor dysfunction in a conditional model of Huntington's Disease
    • 10778856
    • A Yamamoto JJ Lucas R Hen 2000 Reversal of neuropathology and motor dysfunction in a conditional model of Huntington's Disease Cell 101 57 66 10778856
    • (2000) Cell , vol.101 , pp. 57-66
    • Yamamoto, A.1    Lucas, J.J.2    Hen, R.3
  • 188
    • 0037059609 scopus 로고    scopus 로고
    • Drosophila atrophin homolog functions as a transcriptional corepressor in multiple developmental processes
    • 11792320
    • S Zhang L Xu J Lee T Xu 2002 Drosophila atrophin homolog functions as a transcriptional corepressor in multiple developmental processes Cell 108 45 56 11792320
    • (2002) Cell , vol.108 , pp. 45-56
    • Zhang, S.1    Xu, L.2    Lee, J.3    Xu, T.4
  • 189
    • 0035930598 scopus 로고    scopus 로고
    • Chaperone suppression of cellular toxicity of huntingtin is independent of polyglutamine aggregation
    • 11606565
    • H Zhou S-H Li X-J Li 2001 Chaperone suppression of cellular toxicity of huntingtin is independent of polyglutamine aggregation J Biol Chem 276 48417 48424 11606565
    • (2001) J Biol Chem , vol.276 , pp. 48417-48424
    • Zhou, H.1    Li, S.-H.2    Li, X.-J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.