메뉴 건너뛰기




Volumn 83, Issue 5, 2005, Pages 343-352

A novel therapeutic strategy for polyglutamine diseases by stabilizing aggregation-prone proteins with small molecules

Author keywords

Amyloid; Huntington disease; Polyglutamine; Trehalose

Indexed keywords

ANTIOXIDANT; ARYLBUTYRIC ACID DERIVATIVE; ASPARTYLGLUTAMYLVALYLASPARTYL FLUORMETHYL KETONE; ATAXIN 1; ATAXIN 3; BENZYLOXYCARBONYLVALYLALANYLASPARTYL FLUOROMETHYL KETONE; BN 82451; BUTYRIC ACID; CYCLODEXTRIN; CYSTAMINE; DICHLOROACETIC ACID; DISACCHARIDE; HISTONE DEACETYLASE INHIBITOR; HUNTINGTIN; LITHIUM CHLORIDE; MINOCYCLINE; MITHRAMYCIN; MUTANT PROTEIN; MYOGLOBIN; PEPTIDE; POLYGLUTAMINE; PROTEIN INHIBITOR; RAPAMYCIN DERIVATIVE; REMACEMIDE; TAUROURSODEOXYCHOLIC ACID; THIOCTIC ACID; TREHALOSE; UNCLASSIFIED DRUG; VORINOSTAT; AMYLOID;

EID: 23044445857     PISSN: 09462716     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00109-004-0632-2     Document Type: Review
Times cited : (77)

References (93)
  • 1
    • 0034094873 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegeneration
    • Zoghbi HY, Orr HT (2000) Glutamine repeats and neurodegeneration. Annu Rev Neurosci 23:217-247
    • (2000) Annu Rev Neurosci , vol.23 , pp. 217-247
    • Zoghbi, H.Y.1    Orr, H.T.2
  • 3
    • 84993912315 scopus 로고
    • Increased apoptosis and early embryonic lethality in mice nullizygous for the Huntington's disease gene homologue
    • Zeitlin S, Liu JP, Chapman DL, Papaioannou VE, Efstratiadis A (1995) Increased apoptosis and early embryonic lethality in mice nullizygous for the Huntington's disease gene homologue. Nat Genet 11:155-163
    • (1995) Nat Genet , vol.11 , pp. 155-163
    • Zeitlin, S.1    Liu, J.P.2    Chapman, D.L.3    Papaioannou, V.E.4    Efstratiadis, A.5
  • 7
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DiFiglia M, Sapp E, Chase KO, Davies SW, Bates GP, Vonsattel JP, Aronin N (1997) Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 277:1990-1993
    • (1997) Science , vol.277 , pp. 1990-1993
    • DiFiglia, M.1    Sapp, E.2    Chase, K.O.3    Davies, S.W.4    Bates, G.P.5    Vonsattel, J.P.6    Aronin, N.7
  • 8
    • 0031680014 scopus 로고    scopus 로고
    • A cellular model that recapitulates major pathogenic steps of Huntington's disease
    • Lunkes A, Mandel JL (1998) A cellular model that recapitulates major pathogenic steps of Huntington's disease. Hum Mol Genet 7:1355-1361
    • (1998) Hum Mol Genet , vol.7 , pp. 1355-1361
    • Lunkes, A.1    Mandel, J.L.2
  • 10
    • 0141891215 scopus 로고    scopus 로고
    • Pathogenesis of polyglutamine disorders: Aggregation revisited
    • Michalik A, Van Broeckhoven C (2003) Pathogenesis of polyglutamine disorders: aggregation revisited. Hum Mol Genet 12:R173-R186
    • (2003) Hum Mol Genet , vol.12
    • Michalik, A.1    Van Broeckhoven, C.2
  • 11
    • 0035031779 scopus 로고    scopus 로고
    • Polyglutamine and CBP: Fatal attraction?
    • Mccampbell A, Fischbeck KH (2001) Polyglutamine and CBP: fatal attraction? Nat Med 7:528-530
    • (2001) Nat Med , vol.7 , pp. 528-530
    • Mccampbell, A.1    Fischbeck, K.H.2
  • 13
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross CA, Poirier MA (2004) Protein aggregation and neurodegenerative disease. Nat Med 10[Suppl]:S10-S17
    • (2004) Nat Med , vol.10 , Issue.SUPPL.
    • Ross, C.A.1    Poirier, M.A.2
  • 14
    • 0038701684 scopus 로고    scopus 로고
    • Huntingtin aggregation and toxicity in Huntington's disease
    • Bates G (2003) Huntingtin aggregation and toxicity in Huntington's disease. Lancet 361:1642-1644
    • (2003) Lancet , vol.361 , pp. 1642-1644
    • Bates, G.1
  • 16
    • 0035964955 scopus 로고    scopus 로고
    • Trans-suppression of misfolding in an amyloid disease
    • Hammarstrom P, Schneider F, Kelly JW (2001) Trans-suppression of misfolding in an amyloid disease. Science 293:2459-2462
    • (2001) Science , vol.293 , pp. 2459-2462
    • Hammarstrom, P.1    Schneider, F.2    Kelly, J.W.3
  • 17
    • 0037473750 scopus 로고    scopus 로고
    • Prevention of transthyretin amyloid disease by changing protein misfolding energetics
    • Hammarstrom P, Wiseman RL, Powers ET, Kelly JW (2003) Prevention of transthyretin amyloid disease by changing protein misfolding energetics. Science 299:713-716
    • (2003) Science , vol.299 , pp. 713-716
    • Hammarstrom, P.1    Wiseman, R.L.2    Powers, E.T.3    Kelly, J.W.4
  • 18
    • 0346727128 scopus 로고    scopus 로고
    • Therapeutic approaches to protein-misfolding diseases
    • Cohen FE, Kelly JW (2003) Therapeutic approaches to protein-misfolding diseases. Nature 426:905-909
    • (2003) Nature , vol.426 , pp. 905-909
    • Cohen, F.E.1    Kelly, J.W.2
  • 19
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson CM (2003) Protein folding and misfolding. Nature 426:884-890
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 22
    • 0037461730 scopus 로고    scopus 로고
    • Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders
    • Sanchez I, Mahlke C, Yuan J (2003) Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders. Nature 421:373-379
    • (2003) Nature , vol.421 , pp. 373-379
    • Sanchez, I.1    Mahlke, C.2    Yuan, J.3
  • 23
    • 0031838352 scopus 로고    scopus 로고
    • Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1
    • Cummings CJ, Mancini MA, Antalffy B, DeFranco DB, Orr HT, Zoghbi HY (1998) Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1. Nat Genet 19:148-154
    • (1998) Nat Genet , vol.19 , pp. 148-154
    • Cummings, C.J.1    Mancini, M.A.2    Antalffy, B.3    DeFranco, D.B.4    Orr, H.T.5    Zoghbi, H.Y.6
  • 24
    • 0034641589 scopus 로고    scopus 로고
    • Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: Their role in suppression of aggregation and cellular toxicity
    • Jana NR, Tanaka M, Wang GH, Nukina N (2000) Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: their role in suppression of aggregation and cellular toxicity. Hum Mol Genet 9:2009-2018
    • (2000) Hum Mol Genet , vol.9 , pp. 2009-2018
    • Jana, N.R.1    Tanaka, M.2    Wang, G.H.3    Nukina, N.4
  • 29
    • 4744349602 scopus 로고    scopus 로고
    • Increased expression of p62 in expanded polyglutamine-expressing cells and its association with polyglutamine inclusions
    • Nagaoka U, Kim K, Jana NR, Doi H, Maruyama M, Mitsui K, Oyama F, Nukina N (2004) Increased expression of p62 in expanded polyglutamine-expressing cells and its association with polyglutamine inclusions. J Neurochem 91:57-68
    • (2004) J Neurochem , vol.91 , pp. 57-68
    • Nagaoka, U.1    Kim, K.2    Jana, N.R.3    Doi, H.4    Maruyama, M.5    Mitsui, K.6    Oyama, F.7    Nukina, N.8
  • 30
    • 3342879140 scopus 로고    scopus 로고
    • Identification of ubiquitin-interacting proteins in purified polyglutamine aggregates
    • Doi H, Mitsui K, Kurosawa M, Machida Y, Kuroiwa Y, Nukina N (2004) Identification of ubiquitin-interacting proteins in purified polyglutamine aggregates. FEBS Lett 571:171-176
    • (2004) FEBS Lett , vol.571 , pp. 171-176
    • Doi, H.1    Mitsui, K.2    Kurosawa, M.3    Machida, Y.4    Kuroiwa, Y.5    Nukina, N.6
  • 31
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • Caughey B, Lansbury PT (2003) Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu Rev Neurosci 26:267-298
    • (2003) Annu Rev Neurosci , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 32
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
    • Stefani M, Dobson CM (2003) Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J Mol Med 81:678-699
    • (2003) J Mol Med , vol.81 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 33
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • Arrasate M, Mitra S, Schweitzer ES, Segal MR, Finkbeiner S (2004) Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 431:805-810
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 34
    • 0037174879 scopus 로고    scopus 로고
    • Huntingtin spheroids and protofibrils as precursors in polyglutamine fibrilization
    • Poirier MA, Li H, Macosko J, Cai S, Amzel M, Ross CA (2002) Huntingtin spheroids and protofibrils as precursors in polyglutamine fibrilization. J Biol Chem 277:41032-41037
    • (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
  • 35
    • 0141668882 scopus 로고    scopus 로고
    • Expansion of polyglutamine induces the formation of quasi-aggregate in the early stage of protein fibrillization
    • Tanaka M, Machida Y, Nishikawa Y, Akagi T, Hashikawa T, Fujisawa T, Nukina N (2003) Expansion of polyglutamine induces the formation of quasi-aggregate in the early stage of protein fibrillization. J Biol Chem 278:34717-34724
    • (2003) J Biol Chem , vol.278 , pp. 34717-34724
    • Tanaka, M.1    Machida, Y.2    Nishikawa, Y.3    Akagi, T.4    Hashikawa, T.5    Fujisawa, T.6    Nukina, N.7
  • 36
    • 0345701297 scopus 로고    scopus 로고
    • Oligomeric and polymeric aggregates formed by proteins containing expanded polyglutamine
    • Iuchi S, Hoffner G, Verbeke P, Djian P, Green H (2003) Oligomeric and polymeric aggregates formed by proteins containing expanded polyglutamine. Proc Natl Acad Sci U S A 100:2409-2414
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 2409-2414
    • Iuchi, S.1    Hoffner, G.2    Verbeke, P.3    Djian, P.4    Green, H.5
  • 38
    • 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, Sarikaya M, Muchowski PJ (2004) Hsp70 and Hsp40 attenuate formation of spherical and annular polyglutamine oligomers by partitioning monomer. Nat Struct Mol Biol 11:1215-1222
    • (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
  • 49
    • 0036677435 scopus 로고    scopus 로고
    • Tauroursodeoxycholic acid, a bile acid, is neuroprotective in a transgenic animal model of Huntington's disease
    • Keene CD, Rodrigues CM, Eich T, Chhabra MS, Steer CJ, Low WC (2002) Tauroursodeoxycholic acid, a bile acid, is neuroprotective in a transgenic animal model of Huntington's disease. Proc Natl Acad Sci U S A 99:10671-10676
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 10671-10676
    • Keene, C.D.1    Rodrigues, C.M.2    Eich, T.3    Chhabra, M.S.4    Steer, C.J.5    Low, W.C.6
  • 50
    • 0034660457 scopus 로고    scopus 로고
    • Neuroprotective effects of creatine in a transgenic mouse model of Huntington's disease
    • Ferrante RJ (2000) Neuroprotective effects of creatine in a transgenic mouse model of Huntington's disease. J Neurosci 20:4389-4397
    • (2000) J Neurosci , vol.20 , pp. 4389-4397
    • Ferrante, R.J.1
  • 52
    • 0038115294 scopus 로고    scopus 로고
    • Creatine therapy provides neuroprotection after onset of clinical symptoms in Huntington's disease transgenic mice
    • Dedeoglu A, Kubilus JK, Yang L, Ferrante KL, Hersch SM, Beal MF, Ferrante RJ (2003) Creatine therapy provides neuroprotection after onset of clinical symptoms in Huntington's disease transgenic mice. J Neurochem 85:1359-1367
    • (2003) J Neurochem , vol.85 , pp. 1359-1367
    • Dedeoglu, A.1    Kubilus, J.K.2    Yang, L.3    Ferrante, K.L.4    Hersch, S.M.5    Beal, M.F.6    Ferrante, R.J.7
  • 54
    • 0035960544 scopus 로고    scopus 로고
    • Coenzyme Q10 and remacemide hydrochloride ameliorate motor deficits in a Huntington's disease transgenic mouse model
    • Schilling G, Coonfield ML, Ross CA, Borchelt DR (2001) Coenzyme Q10 and remacemide hydrochloride ameliorate motor deficits in a Huntington's disease transgenic mouse model. Neurosci Lett 315:149-153
    • (2001) Neurosci Lett , vol.315 , pp. 149-153
    • Schilling, G.1    Coonfield, M.L.2    Ross, C.A.3    Borchelt, D.R.4
  • 57
    • 0042666901 scopus 로고    scopus 로고
    • Chronic lithium chloride treatment has variable effects on motor behaviour and survival of mice transgenic for the Huntington's disease mutation
    • Wood NI, Morton AJ (2003) Chronic lithium chloride treatment has variable effects on motor behaviour and survival of mice transgenic for the Huntington's disease mutation. Brain Res Bull 61:375-383
    • (2003) Brain Res Bull , vol.61 , pp. 375-383
    • Wood, N.I.1    Morton, A.J.2
  • 58
    • 0035968856 scopus 로고    scopus 로고
    • Lipoic acid improves survival in transgenic mouse models of Huntington's disease
    • Andreassen OA, Ferrante RJ, Dedeoglu A, Beal MF (2001) Lipoic acid improves survival in transgenic mouse models of Huntington's disease. Neuroreport 12:3371-3373
    • (2001) Neuroreport , vol.12 , pp. 3371-3373
    • Andreassen, O.A.1    Ferrante, R.J.2    Dedeoglu, A.3    Beal, M.F.4
  • 59
    • 0037971143 scopus 로고    scopus 로고
    • Increased survival and neuroprotective effects of BN82451 in a transgenic mouse model of Huntington's disease
    • Klivenyi P, Ferrante RJ, Gardian G, Browne S, Chabrier PE, Beal MF (2003) Increased survival and neuroprotective effects of BN82451 in a transgenic mouse model of Huntington's disease. J Neurochem 86:267-272
    • (2003) J Neurochem , vol.86 , pp. 267-272
    • Klivenyi, P.1    Ferrante, R.J.2    Gardian, G.3    Browne, S.4    Chabrier, P.E.5    Beal, M.F.6
  • 63
    • 0036172346 scopus 로고    scopus 로고
    • Prolonged survival and decreased abnormal movements in transgenic model of Huntington disease, with administration of the transglutaminase inhibitor cystamine
    • Karpuj MV, Becher MW, Springer JE, Chabas D, Youssef S, Pedotti R, Mitchell D, Steinman L (2002) Prolonged survival and decreased abnormal movements in transgenic model of Huntington disease, with administration of the transglutaminase inhibitor cystamine. Nat Med 8:143-149
    • (2002) Nat Med , vol.8 , pp. 143-149
    • Karpuj, M.V.1    Becher, M.W.2    Springer, J.E.3    Chabas, D.4    Youssef, S.5    Pedotti, R.6    Mitchell, D.7    Steinman, L.8
  • 65
    • 0035047651 scopus 로고    scopus 로고
    • Therapeutic opportunities in polyglutamine disease
    • Hughes RE, Olson JM (2001) Therapeutic opportunities in polyglutamine disease. Nat Med 7:419-423
    • (2001) Nat Med , vol.7 , pp. 419-423
    • Hughes, R.E.1    Olson, J.M.2
  • 67
    • 0032776447 scopus 로고    scopus 로고
    • Peptide models for inherited neurodegenerative disorders: Conformation and aggregation properties of long polyglutamine peptides with and without interruptions
    • Sharma D, Sharma S, Pasha S, Brahmachari SK (1999) Peptide models for inherited neurodegenerative disorders: conformation and aggregation properties of long polyglutamine peptides with and without interruptions. FEBS Lett 456:181-185
    • (1999) FEBS Lett , vol.456 , pp. 181-185
    • Sharma, D.1    Sharma, S.2    Pasha, S.3    Brahmachari, S.K.4
  • 68
    • 0035084096 scopus 로고    scopus 로고
    • Solubilization and disaggregation of polyglutamine peptides
    • Chen S, Wetzel R (2001) Solubilization and disaggregation of polyglutamine peptides. Protein Sci 10:887-891
    • (2001) Protein Sci , vol.10 , pp. 887-891
    • Chen, S.1    Wetzel, R.2
  • 69
    • 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 (2001) An expanded glutamine repeat destabilizes native ataxin-3 structure and mediates formation of parallel beta-fibrils. Proc Natl Acad Sci U S A 98:11955-11960
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 11955-11960
    • Bevivino, A.E.1    Loll, P.J.2
  • 71
    • 0029059477 scopus 로고
    • Incorporation of glutamine repeats makes protein oligomerize: Implications for neurodegenerative diseases
    • Stott K, Blackburn JM, Butler PJ, Perutz M (1995) Incorporation of glutamine repeats makes protein oligomerize: implications for neurodegenerative diseases. Proc Natl Acad Sci U S A 92:6509-6513
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 6509-6513
    • Stott, K.1    Blackburn, J.M.2    Butler, P.J.3    Perutz, M.4
  • 73
    • 0035976971 scopus 로고    scopus 로고
    • Intra-and intermolecular β-pleated sheet formation in glutamine-repeat inserted myoglobin as a model for polyglutamine diseases
    • Tanaka M, Morishima I, Akagi T, Hashikawa T, Nukina N (2001) Intra-and intermolecular β-pleated sheet formation in glutamine-repeat inserted myoglobin as a model for polyglutamine diseases. J Biol Chem 276:45470-45475
    • (2001) J Biol Chem , vol.276 , pp. 45470-45475
    • Tanaka, M.1    Morishima, I.2    Akagi, T.3    Hashikawa, T.4    Nukina, N.5
  • 74
    • 0037072274 scopus 로고    scopus 로고
    • The effects of aggregation-inducing motifs on amyloid formation of model proteins related to neurodegenerative diseases
    • Tanaka M, Machida Y, Nishikawa Y, Akagi T, Morishima I, Hashikawa T, Fujisawa T, Nukina N (2002) The effects of aggregation-inducing motifs on amyloid formation of model proteins related to neurodegenerative diseases. Biochemistry 41:10277-10286
    • (2002) Biochemistry , vol.41 , pp. 10277-10286
    • Tanaka, M.1    Machida, Y.2    Nishikawa, Y.3    Akagi, T.4    Morishima, I.5    Hashikawa, T.6    Fujisawa, T.7    Nukina, N.8
  • 76
    • 0032039542 scopus 로고    scopus 로고
    • Multiple effects of trehalose on protein folding in vitro and in vivo
    • Singer MA, Lindquist S (1998) Multiple effects of trehalose on protein folding in vitro and in vivo. Mol Cell 1:639-648
    • (1998) Mol Cell , vol.1 , pp. 639-648
    • Singer, M.A.1    Lindquist, S.2
  • 80
    • 1242353099 scopus 로고    scopus 로고
    • A screen for drugs that protect against the cytotoxicity of polyglutamine-expanded androgen receptor
    • Piccioni F, Roman BR, Fischbeck KH, Taylor JP (2004) A screen for drugs that protect against the cytotoxicity of polyglutamine-expanded androgen receptor. Hum Mol Genet 13:437-446
    • (2004) Hum Mol Genet , vol.13 , pp. 437-446
    • Piccioni, F.1    Roman, B.R.2    Fischbeck, K.H.3    Taylor, J.P.4
  • 81
    • 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, Kaddis FG, Hutton JC, Freed CR (1999) Mice transgenic for an expanded CAG repeat in the Huntington's disease gene develop diabetes. Diabetes 48:649-651
    • (1999) Diabetes , vol.48 , pp. 649-651
    • Hurlbert, M.S.1    Zhou, W.2    Wasmeier, C.3    Kaddis, F.G.4    Hutton, J.C.5    Freed, C.R.6
  • 82
    • 0021927818 scopus 로고
    • Diabetes mellitus in Huntington's disease
    • Farrer A (1985) Diabetes mellitus in Huntington's disease. Clin Genet 27:62-67
    • (1985) Clin Genet , vol.27 , pp. 62-67
    • Farrer, A.1
  • 85
    • 0037096376 scopus 로고    scopus 로고
    • Calpain activation in Huntington's disease
    • Gafni J, Ellerby LM (2002) Calpain activation in Huntington's disease. J Neurosci 22:4842-4849
    • (2002) J Neurosci , vol.22 , pp. 4842-4849
    • Gafni, J.1    Ellerby, L.M.2
  • 86
    • 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, Wang Y, Cuiffo B, Kegel KB, Qin ZH, Aronin N, DiFiglia M (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 U S A 98:12784-12789
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 12784-12789
    • Kim, Y.J.1    Yi, Y.2    Sapp, E.3    Wang, Y.4    Cuiffo, B.5    Kegel, K.B.6    Qin, Z.H.7    Aronin, N.8    DiFiglia, M.9
  • 87
  • 88
    • 9144264986 scopus 로고    scopus 로고
    • Polyglutamine expansion in ataxin-3 does not affect protein stability: Implications for misfolding and disease
    • Chow MK, Ellisdon AM, Cabrita LD, Bottomley SP (2004) Polyglutamine expansion in ataxin-3 does not affect protein stability: implications for misfolding and disease. J Biol Chem 279:47643-47651
    • (2004) J Biol Chem , vol.279 , pp. 47643-47651
    • Chow, M.K.1    Ellisdon, A.M.2    Cabrita, L.D.3    Bottomley, S.P.4
  • 89
    • 0036850529 scopus 로고    scopus 로고
    • Aggregated polyglutamine peptides delivered to nuclei are toxic to mammalian cells
    • Yang W, Dunlap JR, Andrews RB, Wetzel R (2002) Aggregated polyglutamine peptides delivered to nuclei are toxic to mammalian cells. Hum Mol Genet 11:2905-2917
    • (2002) Hum Mol Genet , vol.11 , pp. 2905-2917
    • Yang, W.1    Dunlap, J.R.2    Andrews, R.B.3    Wetzel, R.4
  • 90
    • 0035363805 scopus 로고    scopus 로고
    • Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease
    • Sittler A, Lurz R, Lueder G, Priller J, Lehrach H, Hayer-Hartl MK, Hartl FU, Wanker EE (2001) Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease. Hum Mol Genet 10: 1307-1315
    • (2001) Hum Mol Genet , vol.10 , pp. 1307-1315
    • Sittler, A.1    Lurz, R.2    Lueder, G.3    Priller, J.4    Lehrach, H.5    Hayer-Hartl, M.K.6    Hartl, F.U.7    Wanker, E.E.8
  • 91
    • 3242695184 scopus 로고    scopus 로고
    • Progressive decrease in chaperone protein levels in a mouse model of Huntington's disease and induction of stress proteins as a therapeutic approach
    • Hay DG, Sathasivam K, Tobaben S, Stahl B, Marber M, Mestril R, Mahal A, Smith DL, Woodman B, Bates GP (2004) Progressive decrease in chaperone protein levels in a mouse model of Huntington's disease and induction of stress proteins as a therapeutic approach. Hum Mol Genet 13:1389-1405
    • (2004) Hum Mol Genet , vol.13 , pp. 1389-1405
    • Hay, D.G.1    Sathasivam, K.2    Tobaben, S.3    Stahl, B.4    Marber, M.5    Mestril, R.6    Mahal, A.7    Smith, D.L.8    Woodman, B.9    Bates, G.P.10
  • 92
    • 0036852712 scopus 로고    scopus 로고
    • Pharmacological prevention of Parkinson disease in Drosophila
    • Auluck PK, Bonini NM (2002) Pharmacological prevention of Parkinson disease in Drosophila. Nat Med 8:1185-1186
    • (2002) Nat Med , vol.8 , pp. 1185-1186
    • Auluck, P.K.1    Bonini, N.M.2
  • 93
    • 4344569643 scopus 로고    scopus 로고
    • Geldanamycin induces Hsp70 and prevents alpha-synuclein aggregation and toxicity in vitro
    • McLean PJ, Klucken J, Shin Y, Hyman BT (2004) Geldanamycin induces Hsp70 and prevents alpha-synuclein aggregation and toxicity in vitro. Biochem Biophys Res Commun 321:665-669
    • (2004) Biochem Biophys Res Commun , vol.321 , pp. 665-669
    • McLean, P.J.1    Klucken, J.2    Shin, Y.3    Hyman, B.T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.