메뉴 건너뛰기




Volumn 4, Issue 10, 2013, Pages

Suppression of polyglutamine protein toxicity by co-expression of a heat-shock protein 40 and a heat-shock protein 110

Author keywords

APG 1; HCS70ab; HSP110; HSP40; Neurodegeneration; PolyQ

Indexed keywords

ADENOSINE TRIPHOSPHATASE; HEAT SHOCK COGNATE PROTEIN 70; HEAT SHOCK COGNATE PROTEIN 70CB; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 110; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 90; POLYGLUTAMINE; PROTEIN DNAJ; PROTEIN DNAJ 1; UNCLASSIFIED DRUG;

EID: 84887473021     PISSN: None     EISSN: 20414889     Source Type: Journal    
DOI: 10.1038/cddis.2013.351     Document Type: Article
Times cited : (60)

References (57)
  • 2
    • 25844487226 scopus 로고    scopus 로고
    • Diseases of unstable repeat expansion: Mechanisms and common principles
    • Gatchel JR, Zoghbi HY. Diseases of unstable repeat expansion: Mechanisms and common principles. Nat Rev Genet 2005; 6: 743-755.
    • (2005) Nat Rev Genet , vol.6 , pp. 743-755
    • Gatchel, J.R.1    Zoghbi, H.Y.2
  • 3
    • 11144243412 scopus 로고    scopus 로고
    • Modulation of neurodegeneration by molecular chaperones
    • Muchowski PJ, Wacker JL. Modulation of neurodegeneration by molecular chaperones. Nat Rev Neurosci 2005; 6: 11-22.
    • (2005) Nat Rev Neurosci , vol.6 , pp. 11-22
    • Muchowski, P.J.1    Wacker, J.L.2
  • 4
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl FU, Bracher A, Hayer-Hartl M. Molecular chaperones in protein folding and proteostasis. Nature 2011; 475: 324-332.
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 5
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • Bukau B, Weissman J, Horwich A. Molecular chaperones and protein quality control. Cell 2006; 125: 443-451.
    • (2006) Cell , vol.125 , pp. 443-451
    • Bukau, B.1    Weissman, J.2    Horwich, A.3
  • 7
    • 27144524290 scopus 로고    scopus 로고
    • Active HSF1 significantly suppresses polyglutamine aggregate formation in cellular and mouse models
    • Fujimoto M, Takaki E, Hayashi T, Kitaura Y, Tanaka Y, Inouye S et al. Active HSF1 significantly suppresses polyglutamine aggregate formation in cellular and mouse models. J Biol Chem 2005; 280: 34908-34916.
    • (2005) J Biol Chem , vol.280 , pp. 34908-34916
    • Fujimoto, M.1    Takaki, E.2    Hayashi, T.3    Kitaura, Y.4    Tanaka, Y.5    Inouye, S.6
  • 8
    • 77958449033 scopus 로고    scopus 로고
    • Heat shock factor 1 ameliorates proteotoxicity in cooperation with the transcription factor NFAT
    • Hayashida N, Fujimoto M, Tan K, Prakasam R, Shinkawa T, Li L et al. Heat shock factor 1 ameliorates proteotoxicity in cooperation with the transcription factor NFAT. EMBO J 2010; 29: 3459-3469.
    • (2010) EMBO J , vol.29 , pp. 3459-3469
    • Hayashida, N.1    Fujimoto, M.2    Tan, K.3    Prakasam, R.4    Shinkawa, T.5    Li, L.6
  • 9
    • 77954947810 scopus 로고    scopus 로고
    • The HSP70 chaperone machinery J proteins as drivers of functional specificity
    • Kampinga HH, Craig EA. The HSP70 chaperone machinery: J proteins as drivers of functional specificity. Nat Rev Mol Cell Biol 2010; 11: 579-592.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 579-592
    • Kampinga, H.H.1    Craig, E.A.2
  • 11
    • 0034629073 scopus 로고    scopus 로고
    • Genetic suppression of polyglutamine toxicity in Drosophila
    • Kazemi-Esfarjani P, Benzer S. Genetic suppression of polyglutamine toxicity in Drosophila. Science 2000; 287: 1837-1840.
    • (2000) Science , vol.287 , pp. 1837-1840
    • Kazemi-Esfarjani, P.1    Benzer, S.2
  • 12
    • 35949001344 scopus 로고    scopus 로고
    • Genome-wide screen for modifiers of ataxin-3 neurodegeneration in Drosophila
    • Bilen J, Bonini NM. Genome-wide screen for modifiers of ataxin-3 neurodegeneration in Drosophila. PLoS Genet 2007; 3: 1950-1964.
    • (2007) PLoS Genet , vol.3 , pp. 1950-1964
    • Bilen, J.1    Bonini, N.M.2
  • 13
    • 0037205425 scopus 로고    scopus 로고
    • Characterization of a brain-enriched chaperone, MRJ, that inhibits Huntingtin aggregation and toxicity independently
    • Chuang JZ, Zhou H, Zhu M, Li SH, Li XJ, Sung CH. Characterization of a brain-enriched chaperone, MRJ, that inhibits Huntingtin aggregation and toxicity independently. J Biol Chem 2002; 277: 19831-19838.
    • (2002) J Biol Chem , vol.277 , pp. 19831-19838
    • Chuang, J.Z.1    Zhou, H.2    Zhu, M.3    Li, S.H.4    Li, X.J.5    Sung, C.H.6
  • 14
    • 34548608465 scopus 로고    scopus 로고
    • Modulation of polyglutamine inclusion formation by the Hsp70 chaperone machine
    • Rujano MA, Kampinga HH, Salomons FA. Modulation of polyglutamine inclusion formation by the Hsp70 chaperone machine. Exp Cell Res 2007; 313: 3568-3578.
    • (2007) Exp Cell Res , vol.313 , pp. 3568-3578
    • Rujano, M.A.1    Kampinga, H.H.2    Salomons, F.A.3
  • 15
    • 75949094261 scopus 로고    scopus 로고
    • A DNAJB chaperone subfamily with HDAC-dependent activities suppresses toxic protein aggregation
    • Hageman J, Rujano MA, van Waarde MA, Kakkar V, Dirks RP, Govorukhina N et al. A DNAJB chaperone subfamily with HDAC-dependent activities suppresses toxic protein aggregation. Mol Cell 2010; 7: 355-369.
    • (2010) Mol Cell , vol.7 , pp. 355-369
    • Hageman, J.1    Rujano, M.A.2    Van Waarde, M.A.3    Kakkar, V.4    Dirks, R.P.5    Govorukhina, N.6
  • 16
    • 0034708793 scopus 로고    scopus 로고
    • Chaperones Hsp70 and Hsp40 suppress aggregate formation and apoptosis in cultured neuronal cells expressing truncated androgen receptor protein with expanded polyglutamine tract
    • Kobayashi Y, Kume A, Li M, Doyu M, Hata M, Ohtsuka K et al. Chaperones Hsp70 and Hsp40 suppress aggregate formation and apoptosis in cultured neuronal cells expressing truncated androgen receptor protein with expanded polyglutamine tract. J Biol Chem 2000; 275: 8772-8778.
    • (2000) J Biol Chem , vol.275 , pp. 8772-8778
    • Kobayashi, Y.1    Kume, A.2    Li, M.3    Doyu, M.4    Hata, M.5    Ohtsuka, K.6
  • 17
    • 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 G, Nukina N. 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 2000; 9: 2009-2018.
    • (2000) Hum Mol Genet , vol.9 , pp. 2009-2018
    • Jana, N.R.1    Tanaka, M.2    Wang, G.3    Nukina, N.4
  • 18
    • 0001133526 scopus 로고    scopus 로고
    • Hsp110 protects heat-denatured proteins and confers cellular thermoresistance
    • Oh HJ, Chen X, Subjeck Jr. Hsp110 protects heat-denatured proteins and confers cellular thermoresistance. J Biol Chem 1997; 272: 31636-31640.
    • (1997) J Biol Chem , vol.272 , pp. 31636-31640
    • Oh, H.J.1    Chen, X.2    Subjeck, J.R.3
  • 19
    • 0036678054 scopus 로고    scopus 로고
    • Overexpression of yeast Hsp110 homolog Sse1p suppresses ydj1-151 thermosensitivity and restores Hsp90-dependent activity
    • Goeckeler JL, Stephens A, Lee P, Caplan AJ, Brodsky JL. Overexpression of yeast Hsp110 homolog Sse1p suppresses ydj1-151 thermosensitivity and restores Hsp90-dependent activity. Mol Biol Cell 2002; 13: 2760-2770.
    • (2002) Mol Biol Cell , vol.13 , pp. 2760-2770
    • Goeckeler, J.L.1    Stephens, A.2    Lee, P.3    Caplan, A.J.4    Brodsky, J.L.5
  • 20
    • 2542435778 scopus 로고    scopus 로고
    • The function of the yeast molecular chaperone Sse1 is mechanistically distinct from the closely related hsp70 family
    • Shaner L, Trott A, Goeckeler JL, Brodsky JL, Morano KA. The function of the yeast molecular chaperone Sse1 is mechanistically distinct from the closely related hsp70 family. J Biol Chem 2004; 279: 21992-22001.
    • (2004) J Biol Chem , vol.279 , pp. 21992-22001
    • Shaner, L.1    Trott, A.2    Goeckeler, J.L.3    Brodsky, J.L.4    Morano, K.A.5
  • 21
    • 29244432181 scopus 로고    scopus 로고
    • Hsp110 cooperates with different cytosolic HSP70 systems in a pathway for de novo folding
    • Yam AY, Albanese V, Lin HT, Frydman J. Hsp110 cooperates with different cytosolic HSP70 systems in a pathway for de novo folding. J Biol Chem 2005; 280: 41252-41261.
    • (2005) J Biol Chem , vol.280 , pp. 41252-41261
    • Yam, A.Y.1    Albanese, V.2    Lin, H.T.3    Frydman, J.4
  • 22
    • 29244467709 scopus 로고    scopus 로고
    • The yeast Hsp110 Sse1 functionally interacts with the Hsp70 chaperones Ssa and Ssb
    • Shaner L, Wegele H, Buchner J, Morano KA. The yeast Hsp110 Sse1 functionally interacts with the Hsp70 chaperones Ssa and Ssb. J Biol Chem 2005; 280: 41262-41269.
    • (2005) J Biol Chem , vol.280 , pp. 41262-41269
    • Shaner, L.1    Wegele, H.2    Buchner, J.3    Morano, K.A.4
  • 23
    • 33745749328 scopus 로고    scopus 로고
    • Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor
    • Raviol H, Sadlish H, Rodriguez F, Mayer M.P, Bukau B. Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor. EMBO J 2006; 25: 2510-2518.
    • (2006) EMBO J , vol.25 , pp. 2510-2518
    • Raviol, H.1    Sadlish, H.2    Rodriguez, F.3    Mayer, M.P.4    Bukau, B.5
  • 24
    • 33745762927 scopus 로고    scopus 로고
    • Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s
    • Dragovic Z, Broadley SA, Shomura Y, Bracher A, Hartl FU. Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s. EMBO J 2006; 25: 2519-2528.
    • (2006) EMBO J , vol.25 , pp. 2519-2528
    • Dragovic, Z.1    Broadley, S.A.2    Shomura, Y.3    Bracher, A.4    Hartl, F.U.5
  • 25
    • 60849126687 scopus 로고    scopus 로고
    • Progressive aggregation despite chaperone associations of a mutant SOD1-YFP in transgenic mice that develop ALS
    • Wang J, Farr GW, Zeiss CJ, Rodriguez-Gil DJ, Wilson JH, Furtak K et al. Progressive aggregation despite chaperone associations of a mutant SOD1-YFP in transgenic mice that develop ALS. Proc Natl Acad Sci USA 2009; 106: 1392-1397.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 1392-1397
    • Wang, J.1    Farr, G.W.2    Zeiss, C.J.3    Rodriguez-Gil, D.J.4    Wilson, J.H.5    Furtak, K.6
  • 26
    • 34547893834 scopus 로고    scopus 로고
    • Heat-shock protein 105 interacts with and suppresses aggregation of mutant Cu/Zn superoxide dismutase: Clues to a possible strategy for treating ALS
    • Yamashita H, Kawamata J, Okawa K, Kanki R, Nakamizo T, Hatayama T et al. Heat-shock protein 105 interacts with and suppresses aggregation of mutant Cu/Zn superoxide dismutase: Clues to a possible strategy for treating ALS. J Neurochem 2007; 102: 1497-1505.
    • (2007) J Neurochem , vol.102 , pp. 1497-1505
    • Yamashita, H.1    Kawamata, J.2    Okawa, K.3    Kanki, R.4    Nakamizo, T.5    Hatayama, T.6
  • 27
    • 84861749562 scopus 로고    scopus 로고
    • Human heat shock protein 105/110 kDa (Hsp105/110) regulates biogenesis and quality control of misfolded cystic fibrosis transmembrane conductance regulator at multiple levels
    • Saxena A, Banasavadi-Siddegowda YK, Fan Y, Bhattacharya S, Roy G, Giovannucci DR et al. Human heat shock protein 105/110 kDa (Hsp105/110) regulates biogenesis and quality control of misfolded cystic fibrosis transmembrane conductance regulator at multiple levels. J Biol Chem 2012; 287: 19158-19170.
    • (2012) J Biol Chem , vol.287 , pp. 19158-19170
    • Saxena, A.1    Banasavadi-Siddegowda, Y.K.2    Fan, Y.3    Bhattacharya, S.4    Roy, G.5    Giovannucci, D.R.6
  • 28
    • 77956672926 scopus 로고    scopus 로고
    • Loss of Hsp110 leads to age-dependent tau hyperphosphorylation and early accumulation of insoluble amyloid beta
    • Eroglu B, Moskophidis D, Mivechi NF. Loss of Hsp110 leads to age-dependent tau hyperphosphorylation and early accumulation of insoluble amyloid beta. Mol Cell Biol 2010; 30: 4626-4643.
    • (2010) Mol Cell Biol , vol.30 , pp. 4626-4643
    • Eroglu, B.1    Moskophidis, D.2    Mivechi, N.F.3
  • 29
    • 84870159570 scopus 로고    scopus 로고
    • Probing mechanisms that underlie human neurodegenerative disease in Drosophila
    • Jaiswal M, Sandoval H, Zhang K, Bayat V, Bellen HJ. Probing mechanisms that underlie human neurodegenerative disease in Drosophila. Annu Rev Genet 2012; 46: 371-396.
    • (2012) Annu Rev Genet , vol.46 , pp. 371-396
    • Jaiswal, M.1    Sandoval, H.2    Zhang, K.3    Bayat, V.4    Bellen, H.J.5
  • 30
    • 80052451891 scopus 로고    scopus 로고
    • Modeling human trinucleotide repeat diseases in Drosophila
    • Yu Z, Bonini NM. Modeling human trinucleotide repeat diseases in Drosophila. Int Rev Neurobiol 2011; 99: 191-212.
    • (2011) Int Rev Neurobiol , vol.99 , pp. 191-212
    • Yu, Z.1    Bonini, N.M.2
  • 31
    • 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. Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1. Nat Genet 1998; 19: 148-154.
    • (1998) Nat Genet , vol.19 , pp. 148-154
    • Cummings, C.J.1    Mancini, M.A.2    Antalffy, B.3    De Franco, D.B.4    Orr, H.T.5    Zoghbi, H.Y.6
  • 32
    • 46849116411 scopus 로고    scopus 로고
    • Structural and functional diversities between members of the human HSPB, HSPH, HSPA, and DNAJ chaperone families
    • Vos MJ, Hageman J, Carra S, Kampinga HH. Structural and functional diversities between members of the human HSPB, HSPH, HSPA, and DNAJ chaperone families. Biochemistry 2008; 47: 7001-7011.
    • (2008) Biochemistry , vol.47 , pp. 7001-7011
    • Vos, M.J.1    Hageman, J.2    Carra, S.3    Kampinga, H.H.4
  • 33
    • 0032727617 scopus 로고    scopus 로고
    • Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70
    • Warrick JM, Chan HY, Gray-Board GL, Chai Y, Paulson HL, Bonini NM. Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70. Nat Genet 1999; 23: 425-428.
    • (1999) Nat Genet , vol.23 , pp. 425-428
    • Warrick, J.M.1    Chan, H.Y.2    Gray-Board, G.L.3    Chai, Y.4    Paulson, H.L.5    Bonini, N.M.6
  • 34
    • 0034703863 scopus 로고    scopus 로고
    • Mechanisms of chaperone suppression of polyglutamine disease: Selectivity, synergy and modulation of protein solubility in Drosophila
    • Chan HY, Warrick JM, Gray-Board GL, Paulson HL, Bonini NM. Mechanisms of chaperone suppression of polyglutamine disease: Selectivity, synergy and modulation of protein solubility in Drosophila. Hum Mol Genet 2000; 9: 2811-2820.
    • (2000) Hum Mol Genet , vol.9 , pp. 2811-2820
    • Chan, H.Y.1    Warrick, J.M.2    Gray-Board, G.L.3    Paulson, H.L.4    Bonini, N.M.5
  • 35
    • 0027160708 scopus 로고
    • Targeted gene expression as a means of altering cell fates and generating dominant phenotypes
    • Brand AH, Perrimon N. Targeted gene expression as a means of altering cell fates and generating dominant phenotypes. Development 1993; 118: 401-415.
    • (1993) Development , vol.118 , pp. 401-415
    • Brand, A.H.1    Perrimon, N.2
  • 36
    • 10844264219 scopus 로고    scopus 로고
    • Genomic deletions of the Drosophila melanogaster Hsp70 genes
    • Gong WJ, Golic KG. Genomic deletions of the Drosophila melanogaster Hsp70 genes. Genetics 2004; 168: 1467-1476.
    • (2004) Genetics , vol.168 , pp. 1467-1476
    • Gong, W.J.1    Golic, K.G.2
  • 37
    • 33750015475 scopus 로고    scopus 로고
    • A Drosophila ortholog of the human MRJ modulates polyglutamine toxicity and aggregation
    • Fayazi Z, Ghosh S, Marion S, Bao X, Shero M, Kazemi-Esfarjani P. A Drosophila ortholog of the human MRJ modulates polyglutamine toxicity and aggregation. Neurobiol Dis 2006; 24: 226-244.
    • (2006) Neurobiol Dis , vol.24 , pp. 226-244
    • Fayazi, Z.1    Ghosh, S.2    Marion, S.3    Bao, X.4    Shero, M.5    Kazemi-Esfarjani, P.6
  • 39
    • 77955870526 scopus 로고    scopus 로고
    • A genomewide RNA interference screen for modifiers of aggregates formation by mutant Huntingtin in Drosophila
    • Zhang S, Binari R, Zhou R, Perrimon N. A genomewide RNA interference screen for modifiers of aggregates formation by mutant Huntingtin in Drosophila. Genetics 2009; 184: 1165-1179.
    • (2009) Genetics , vol.184 , pp. 1165-1179
    • Zhang, S.1    Binari, R.2    Zhou, R.3    Perrimon, N.4
  • 40
    • 0032168160 scopus 로고    scopus 로고
    • Polyglutamineexpanded human huntingtin transgenes induce degeneration of Drosophila photoreceptor neurons
    • Jackson GR, Salecker I, Dong X, Yao X, Arnheim N, Faber PW et al. Polyglutamineexpanded human huntingtin transgenes induce degeneration of Drosophila photoreceptor neurons. Neuron 1998; 21: 633-642.
    • (1998) Neuron , vol.21 , pp. 633-642
    • Jackson, G.R.1    Salecker, I.2    Dong, X.3    Yao, X.4    Arnheim, N.5    Faber, P.W.6
  • 41
    • 67649219195 scopus 로고    scopus 로고
    • Computational analysis of the human HSPH/HSPA/DNAJ family and cloning of a human HSPH/HSPA/DNAJ expression library
    • Hageman J, Kampinga HH. Computational analysis of the human HSPH/HSPA/DNAJ family and cloning of a human HSPH/HSPA/DNAJ expression library. Cell Stress Chaperones 2009; 14: 1-21.
    • (2009) Cell Stress Chaperones , vol.14 , pp. 1-21
    • Hageman, J.1    Kampinga, H.H.2
  • 43
    • 0031017476 scopus 로고    scopus 로고
    • A novel hsp110-related gene, apg-1, that is abundantly expressed in the testis responds to a low temperature heat shock rather than the traditional elevated temperatures
    • Kaneko Y, Nishiyama H, Nonoguchi K, Higashitsuji H, Kishishita M, Fujita J. A novel hsp110-related gene, apg-1, that is abundantly expressed in the testis responds to a low temperature heat shock rather than the traditional elevated temperatures. J Biol Chem 1997; 272: 2640-2645.
    • (1997) J Biol Chem , vol.272 , pp. 2640-2645
    • Kaneko, Y.1    Nishiyama, H.2    Nonoguchi, K.3    Higashitsuji, H.4    Kishishita, M.5    Fujita, J.6
  • 44
    • 0029564092 scopus 로고
    • Cloning and expression of murine high molecular mass heat shock proteins, HSP105
    • Yasuda K, Nakai A, Hatayama T, Nagata K. Cloning and expression of murine high molecular mass heat shock proteins, HSP105. J Biol Chem 1995; 270: 29718-29723.
    • (1995) J Biol Chem , vol.270 , pp. 29718-29723
    • Yasuda, K.1    Nakai, A.2    Hatayama, T.3    Nagata, K.4
  • 45
    • 77956407962 scopus 로고    scopus 로고
    • Levels of DNAJB family members (HSP40) correlate with disease onset in patients with spinocerebellar ataxia type 3
    • Zijlstra MP, Rujano MA, Van Waarde MA, Vis E, Brunt ER, Kampinga HH. Levels of DNAJB family members (HSP40) correlate with disease onset in patients with spinocerebellar ataxia type 3. Eur J Neurosci 2010; 32: 760-770.
    • (2010) Eur J Neurosci , vol.32 , pp. 760-770
    • Zijlstra, M.P.1    Rujano, M.A.2    Van Waarde, M.A.3    Vis, E.4    Brunt, E.R.5    Kampinga, H.H.6
  • 46
    • 34249286265 scopus 로고    scopus 로고
    • Hsp40 molecules that target to the ubiquitin-proteasome system decrease inclusion formation in models of polyglutamine disease
    • Howarth JL, Kelly S, Keasey MP, Glover CP, Lee YB, Mitrophanous K et al. Hsp40 molecules that target to the ubiquitin-proteasome system decrease inclusion formation in models of polyglutamine disease. Mol Ther 2007; 15: 1100-1105.
    • (2007) Mol Ther , vol.15 , pp. 1100-1105
    • Howarth, J.L.1    Kelly, S.2    Keasey, M.P.3    Glover, C.P.4    Lee, Y.B.5    Mitrophanous, K.6
  • 47
    • 0036501074 scopus 로고    scopus 로고
    • Molecular chaperones enhance the degradation of expanded polyglutamine repeat androgen receptor in a cellular model of spinal and bulbar muscular atrophy
    • Bailey CK, Andriola IF, Kampinga HH, Merry DE. Molecular chaperones enhance the degradation of expanded polyglutamine repeat androgen receptor in a cellular model of spinal and bulbar muscular atrophy. Hum Mol Genet 2002; 11: 515-523.
    • (2002) Hum Mol Genet , vol.11 , pp. 515-523
    • Bailey, C.K.1    Andriola, I.F.2    Kampinga, H.H.3    Merry, D.E.4
  • 48
    • 46149116088 scopus 로고    scopus 로고
    • Hsp110 chaperones regulate prion formation and propagation in S. Cerevisiae by two discrete activities
    • Sadlish H, Rampelt H, Shorter J, Wegrzyn RD, Andreasson C, Lindquist S et al. Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities. PLoS One 2008; 3: E1763.
    • (2008) PLoS One , vol.3
    • Sadlish, H.1    Rampelt, H.2    Shorter, J.3    Wegrzyn, R.D.4    Andreasson, C.5    Lindquist, S.6
  • 49
    • 36349015924 scopus 로고    scopus 로고
    • The Hsp110 molecular chaperone stabilizes apolipoprotein B from endoplasmic reticulum-Associated degradation (ERAD)
    • Hrizo SL, Gusarova V, Habiel DM, Goeckeler JL, Fisher EA, Brodsky JL. The Hsp110 molecular chaperone stabilizes apolipoprotein B from endoplasmic reticulum-Associated degradation (ERAD). J Biol Chem 2007; 282: 32665-32675.
    • (2007) J Biol Chem , vol.282 , pp. 32665-32675
    • Hrizo, S.L.1    Gusarova, V.2    Habiel, D.M.3    Goeckeler, J.L.4    Fisher, E.A.5    Brodsky, J.L.6
  • 50
    • 66849143696 scopus 로고    scopus 로고
    • Converging concepts of protein folding in vitro and in vivo
    • Hartl FU, Hayer-Hartl M. Converging concepts of protein folding in vitro and in vivo. Nat Struct Mol Biol 2009; 16: 574-581.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 574-581
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 51
    • 80054699747 scopus 로고    scopus 로고
    • The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system
    • Shorter J. The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system. PLoS One 2011; 6: E26319.
    • (2011) PLoS One , vol.6
    • Shorter, J.1
  • 53
    • 21244489544 scopus 로고    scopus 로고
    • HspB8, a small heat shock protein mutated in human neuromuscular disorders, has in vivo chaperone activity in cultured cells
    • Carra S, Sivilotti M, Chavez Zobel AT, Lambert H, Landry J. HspB8, a small heat shock protein mutated in human neuromuscular disorders, has in vivo chaperone activity in cultured cells. Hum Mol Genet 2005; 14: 1659-1669.
    • (2005) Hum Mol Genet , vol.14 , pp. 1659-1669
    • Carra, S.1    Sivilotti, M.2    Chavez Zobel, A.T.3    Lambert, H.4    Landry, J.5
  • 54
    • 0042591262 scopus 로고    scopus 로고
    • Hsp105alpha suppresses the aggregation of truncated androgen receptor with expanded CAG repeats and cell toxicity
    • Ishihara K, Yamagishi N, Saito Y, Adachi H, Kobayashi Y, Sobue G et al. Hsp105alpha suppresses the aggregation of truncated androgen receptor with expanded CAG repeats and cell toxicity. J Biol Chem 2003; 278: 25143-25150.
    • (2003) J Biol Chem , vol.278 , pp. 25143-25150
    • Ishihara, K.1    Yamagishi, N.2    Saito, Y.3    Adachi, H.4    Kobayashi, Y.5    Sobue, G.6
  • 55
    • 69949180640 scopus 로고    scopus 로고
    • TOR-mediated autophagy regulates cell death in Drosophila neurodegenerative disease
    • Wang T, Lao U, Edgar BA. TOR-mediated autophagy regulates cell death in Drosophila neurodegenerative disease. J Cell Biol 2009; 186: 703-711.
    • (2009) J Cell Biol , vol.186 , pp. 703-711
    • Wang, T.1    Lao, U.2    Edgar, B.A.3
  • 56
    • 84864605572 scopus 로고    scopus 로고
    • LST8 regulates cell growth via targetof-rapamycin complex 2 (TORC2)
    • Wang T, Blumhagen R, Lao U, Kuo Y, Edgar BA. LST8 regulates cell growth via targetof-rapamycin complex 2 (TORC2). Mol Cell Biol 2012; 32: 2203-2213.
    • (2012) Mol Cell Biol , vol.32 , pp. 2203-2213
    • Wang, T.1    Blumhagen, R.2    Lao, U.3    Kuo, Y.4    Edgar, B.A.5
  • 57
    • 0035254534 scopus 로고    scopus 로고
    • Modulation of Drosophila heat shock transcription factor activity by the molecular chaperone DROJ1
    • Marchler G, Wu C. Modulation of Drosophila heat shock transcription factor activity by the molecular chaperone DROJ1. EMBO J 2001; 20: 499-509.
    • (2001) EMBO J , vol.20 , pp. 499-509
    • Marchler, G.1    Wu, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.