메뉴 건너뛰기




Volumn 21, Issue 5, 2005, Pages 403-419

Role of molecular chaperones in neurodegenerative disorders

Author keywords

Chaperone; Neurodegeneration; Protein aggregation; Senescence

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN; ANDROGEN RECEPTOR; ATAXIN 1; ATAXIN 3; CHAPERONE; GELDANAMYCIN; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 27; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 72; HEAT SHOCK PROTEIN 84; HEAT SHOCK PROTEIN 90; HUNTINGTIN; PARKIN; POLYGLUTAMINE; POLYPEPTIDE; PRION PROTEIN; PROTEASOME; RAPAMYCIN; STRESS ACTIVATED PROTEIN KINASE; SUPEROXIDE DISMUTASE; TAU PROTEIN; UBIQUITIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 23344432914     PISSN: 02656736     EISSN: None     Source Type: Journal    
DOI: 10.1080/02656730500041871     Document Type: Review
Times cited : (121)

References (129)
  • 1
    • 0037397705 scopus 로고    scopus 로고
    • Emerging ideas on the molecular basis of protein and peptide aggregation
    • Thirumalai D, Klimov DK, Dima RI. Emerging ideas on the molecular basis of protein and peptide aggregation. Curr Opin Struct Biol 2003;13:146-159.
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 146-159
    • Thirumalai, D.1    Klimov, D.K.2    Dima, R.I.3
  • 2
    • 0036052739 scopus 로고    scopus 로고
    • Ideas of order for amyloid fibril structure
    • Wetzel R. Ideas of order for amyloid fibril structure. Structure (Camb) 2002;10:1031-1036.
    • (2002) Structure (Camb.) , vol.10 , pp. 1031-1036
    • Wetzel, R.1
  • 3
    • 0037022297 scopus 로고    scopus 로고
    • Conformational Abs recognizing a generic amyloid fibril epitope
    • O'Nuallain B, Wetzel R. Conformational Abs recognizing a generic amyloid fibril epitope. Proc Natl Acad Sci (USA) 2002;99:1485-1490.
    • (2002) Proc. Natl. Acad. Sci. (USA) , vol.99 , pp. 1485-1490
    • O'Nuallain, B.1    Wetzel, R.2
  • 5
    • 0034924812 scopus 로고    scopus 로고
    • Folding of newly translated proteins in vivo: The role of molecular chaperones
    • Frydman J. Folding of newly translated proteins in vivo: the role of molecular chaperones. Annu Rev Biochem 2001;70:603-647.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 603-647
    • Frydman, J.1
  • 6
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • Goldberg AL. Protein degradation and protection against misfolded or damaged proteins. Nature 2003;426:895-899.
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 9
    • 0344466781 scopus 로고    scopus 로고
    • Characterization and dynamics of aggresome formation by a cytosolic GFP-chimera
    • Garcia-Mata R, Bebok Z, Sorscher EJ, Sztul ES. Characterization and dynamics of aggresome formation by a cytosolic GFP-chimera. J Cell Biol 1999;146:1239-1254.
    • (1999) J. Cell. Biol. , vol.146 , pp. 1239-1254
    • Garcia-Mata, R.1    Bebok, Z.2    Sorscher, E.J.3    Sztul, E.S.4
  • 10
    • 0029911025 scopus 로고    scopus 로고
    • Heat shock causes protein aggregation and reduced protein solubility at the centrosome and other cytoplasmic locations
    • Vidair CA, Huang RN, Doxsey SJ. Heat shock causes protein aggregation and reduced protein solubility at the centrosome and other cytoplasmic locations. Int J Hyperthermia 1999;12:681-695.
    • (1999) Int. J. Hyperthermia. , vol.12 , pp. 681-695
    • Vidair, C.A.1    Huang, R.N.2    Doxsey, S.J.3
  • 12
    • 0029909097 scopus 로고    scopus 로고
    • Ubiquitin-mediated proteolysis centers in Hela cells - Indication from atudies of an inhibitor of the chymotrypsin-like activity of the proteasome
    • Wojcik C, Schroeter D, Wilk S, Lamprecht J, Paweletz N. Ubiquitin-mediated proteolysis centers in Hela cells - indication from atudies of an inhibitor of the chymotrypsin-like activity of the proteasome. Eur J Cell Biol 1996;71:311-318.
    • (1996) Eur. J. Cell. Biol. , vol.71 , pp. 311-318
    • Wojcik, C.1    Schroeter, D.2    Wilk, S.3    Lamprecht, J.4    Paweletz, N.5
  • 13
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • Johnston JA, Ward CL, Kopito RR. Aggresomes: a cellular response to misfolded proteins. J Cell Biol 1998;143:1883-1898.
    • (1998) J. Cell. Biol. , vol.143 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 15
    • 0346020435 scopus 로고    scopus 로고
    • The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress
    • Kawaguchi Y, Kovacs JJ, McLaurin A, Vance JM, Ito A, Yao TP. The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress. Cell 2003;115:727-738.
    • (2003) Cell , vol.115 , pp. 727-738
    • Kawaguchi, Y.1    Kovacs, J.J.2    McLaurin, A.3    Vance, J.M.4    Ito, A.5    Yao, T.P.6
  • 16
    • 0344874551 scopus 로고    scopus 로고
    • Emerging role for autophagy in the removal of aggresomes in Schwann cells
    • Fortun J, Dunn Jr WA, Joy S, Li J, Notterpek L. Emerging role for autophagy in the removal of aggresomes in Schwann cells. J Neurosci 2003;23:10672-10680.
    • (2003) J. Neurosci. , vol.23 , pp. 10672-10680
    • Fortun, J.1    Dunn Jr., W.A.2    Joy, S.3    Li, J.4    Notterpek, L.5
  • 17
    • 0036566266 scopus 로고    scopus 로고
    • Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy
    • Ravikumar B, Duden R, Rubinsztein DC. Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy. Hum Mol Genet 2002;11:1107-1117.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1107-1117
    • Ravikumar, B.1    Duden, R.2    Rubinsztein, D.C.3
  • 18
    • 0041589248 scopus 로고    scopus 로고
    • Alpha-Synuclein is degraded by both autophagy and the proteasome
    • Epub 2003 Apr 28
    • Webb JL, Ravikumar B, Atkins J, Skepper JN, Rubinsztein DC. Alpha-Synuclein is degraded by both autophagy and the proteasome. J Biol Chem 2003;278:25009-25013. Epub 2003 Apr 28.
    • (2003) J. Biol. Chem. , vol.278 , pp. 25009-25013
    • Webb, J.L.1    Ravikumar, B.2    Atkins, J.3    Skepper, J.N.4    Rubinsztein, D.C.5
  • 20
    • 0035858883 scopus 로고    scopus 로고
    • Intracellular aggregation of polypeptides with expanded polyglutamine domain is stimulated by stress-activated kinase mekk1
    • Meriin AB, Mabuchi K, Gabai VL, Yaglom JA, Kazantsev A, Sherman MY. Intracellular aggregation of polypeptides with expanded polyglutamine domain is stimulated by stress-activated kinase mekk1. J Cell Biol 2001;153:851-864.
    • (2001) J. Cell. Biol. , vol.153 , pp. 851-864
    • Meriin, A.B.1    Mabuchi, K.2    Gabai, V.L.3    Yaglom, J.A.4    Kazantsev, A.5    Sherman, M.Y.6
  • 21
    • 0038039288 scopus 로고    scopus 로고
    • Polyglutamine protein aggregation and toxicity are linked to the cellular stress response
    • Cowan K, Diamond M, Welch W. Polyglutamine protein aggregation and toxicity are linked to the cellular stress response. Human Molec Gen 2003;12:1377-1391.
    • (2003) Human. Molec. Gen. , vol.12 , pp. 1377-1391
    • Cowan, K.1    Diamond, M.2    Welch, W.3
  • 22
    • 0034681144 scopus 로고    scopus 로고
    • Regulation of expanded polyglutamine protein aggregation and nuclear localization by the glucocorticoid receptor
    • Diamond MI, Robinson MR, Yamamoto KR. Regulation of expanded polyglutamine protein aggregation and nuclear localization by the glucocorticoid receptor. Proc Natl Acad Sci (USA) 2000;97:657-661.
    • (2000) Proc. Natl. Acad. Sci. (USA) , vol.97 , pp. 657-661
    • Diamond, M.I.1    Robinson, M.R.2    Yamamoto, K.R.3
  • 26
    • 0036678146 scopus 로고    scopus 로고
    • The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans
    • Morley JF, Brignull HR, Weyers JJ, Morimoto RI. The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans. Proc Natl Acad Sci (USA) 2002;99:10417-10422.
    • (2002) Proc. Natl. Acad. Sci. (USA) , vol.99 , pp. 10417-10422
    • Morley, J.F.1    Brignull, H.R.2    Weyers, J.J.3    Morimoto, R.I.4
  • 30
    • 0031918640 scopus 로고    scopus 로고
    • Intranuclear neuronal inclusions in Huntington's disease and dentatorubral and pallidoluysian atrophy: Correlation between the density of inclusions and IT15 CAG triplet repeat length
    • Becher MW, Kotzuk JA, Sharp AH, Davies SW, Bates GP, Price DL, Ross CA. 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 1998;4:387-397.
    • (1998) Neurobiol. Dis. , vol.4 , pp. 387-397
    • Becher, M.W.1    Kotzuk, J.A.2    Sharp, A.H.3    Davies, S.W.4    Bates, G.P.5    Price, D.L.6    Ross, C.A.7
  • 33
    • 0037461730 scopus 로고    scopus 로고
    • Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders
    • Sanchez I, Mahlke C, Yuan J. Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders. Nature 2003;421:373-379.
    • (2003) Nature , vol.421 , pp. 373-379
    • Sanchez, I.1    Mahlke, C.2    Yuan, J.3
  • 34
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • Epub 2003 Apr 09
    • Caughey B, Lansbury PT. Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu Rev Neurosci 2003;26:267-298. Epub 2003 Apr 09.
    • (2003) Annu. Rev. Neurosci. , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 35
    • 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. Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 2004;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
  • 37
    • 0038689039 scopus 로고    scopus 로고
    • Protein aggregation and the ubiquitin proteasome pathway: Gaining the UPPer hand on neurodegeneration
    • Berke SJ, Paulson HL. Protein aggregation and the ubiquitin proteasome pathway: gaining the UPPer hand on neurodegeneration. Curr Opin Genet Dev 2003;13:253-261.
    • (2003) Curr. Opin. Genet. Dev. , vol.13 , pp. 253-261
    • Berke, S.J.1    Paulson, H.L.2
  • 38
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross CA, Poirier MA. Protein aggregation and neurodegenerative disease. Nat Med 2004;10:S10-S17.
    • (2004) Nat. Med. , vol.10
    • Ross, C.A.1    Poirier, M.A.2
  • 40
    • 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. Nature Genet 1999;23:425-428.
    • (1999) Nature 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
  • 41
    • 0032945938 scopus 로고    scopus 로고
    • Polyglutamine-expanded androgen receptors form aggregates that sequester heat shock proteins, proteasome components and SRC-1, and are suppressed by the HDJ-2 chaperone
    • Stenoien DL, Cummings CJ, Adams HP, Mancini MG, Patel K, DeMartino GN, Marcelli M, Weigel NL, Mancini MA. Polyglutamine-expanded androgen receptors form aggregates that sequester heat shock proteins, proteasome components and SRC-1, and are suppressed by the HDJ-2 chaperone. Hum Mol Genet 1999;8:731-741.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 731-741
    • Stenoien, D.L.1    Cummings, C.J.2    Adams, H.P.3    Mancini, M.G.4    Patel, K.5    DeMartino, G.N.6    Marcelli, M.7    Weigel, N.L.8    Mancini, M.A.9
  • 42
    • 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
  • 43
    • 0035897405 scopus 로고    scopus 로고
    • Identities of sequestered proteins in aggregates from cells with induced polyglutamine expression
    • Suhr ST, Senut MC, Whitelegge JP, Faull YF, Cuizon DB, Gage FH. Identities of sequestered proteins in aggregates from cells with induced polyglutamine expression. J Cell Biol 2001;153:283-294.
    • (2001) J. Cell. Biol. , vol.153 , pp. 283-294
    • Suhr, S.T.1    Senut, M.C.2    Whitelegge, J.P.3    Faull, Y.F.4    Cuizon, D.B.5    Gage, F.H.6
  • 44
    • 0036848793 scopus 로고    scopus 로고
    • Purification of polyglutamine aggregates and identification of elongation factor-1alpha and heat shock protein 84 as aggregate-interacting proteins
    • Mitsui K, Nakayama H, Akagi T, Nekooki M, Ohtawa K, Takio K, Hashikawa T, Nukina N. Purification of polyglutamine aggregates and identification of elongation factor-1alpha and heat shock protein 84 as aggregate-interacting proteins. J Neurosci 2002;22:9267-9277.
    • (2002) J. Neurosci. , vol.22 , pp. 9267-9277
    • Mitsui, K.1    Nakayama, H.2    Akagi, T.3    Nekooki, M.4    Ohtawa, K.5    Takio, K.6    Hashikawa, T.7    Nukina, N.8
  • 45
    • 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
    • Epub 2004 Apr 28
    • Hay DG, Sathasivam K, Tobaben S, Stahl B, Marber M, Mestril R, Mahal A, Smith DL, Woodman B, Bates GP. 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 2004;13:1389-1405. Epub 2004 Apr 28.
    • (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
  • 46
    • 0035664213 scopus 로고    scopus 로고
    • Histological evidence of protein aggregation in mutant SOD1 transgenic mice and in amyotrophic lateral sclerosis neural tissues
    • Watanabe M, Dykes-Hoberg M, Culotta VC, Price DL, Wong PC, Rothstein JD. Histological evidence of protein aggregation in mutant SOD1 transgenic mice and in amyotrophic lateral sclerosis neural tissues. Neurobiol Dis 2001;8:933-941.
    • (2001) Neurobiol. Dis. , vol.8 , pp. 933-941
    • Watanabe, M.1    Dykes-Hoberg, M.2    Culotta, V.C.3    Price, D.L.4    Wong, P.C.5    Rothstein, J.D.6
  • 47
    • 1042266326 scopus 로고    scopus 로고
    • Aggresomes formed by alpha-synuclein and synphilin-1 are cytoprotective
    • Epub 2003 Nov 19
    • Tanaka M, Kim YM, Lee G, Junn E, Iwatsubo T, Mouradian MM. Aggresomes formed by alpha-synuclein and synphilin-1 are cytoprotective. J Biol Chem 2004;279:4625-4631. Epub 2003 Nov 19.
    • (2004) J. Biol. Chem. , vol.279 , pp. 4625-4631
    • Tanaka, M.1    Kim, Y.M.2    Lee, G.3    Junn, E.4    Iwatsubo, T.5    Mouradian, M.M.6
  • 49
    • 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, Lutz R, Lueder G, Priller J, Lehrach H, Hayer-Hartl MK, Hartl FU, Wanker EE. Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease. Hum Mol Genet 2001;10:1307-1315.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1307-1315
    • Sittler, A.1    Lutz, R.2    Lueder, G.3    Priller, J.4    Lehrach, H.5    Hayer-Hartl, M.K.6    Hartl, F.U.7    Wanker, E.E.8
  • 50
    • 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
  • 51
    • 0034708793 scopus 로고    scopus 로고
    • Chaperones Hsp70 and Hsp40 suppress aggregate formation and apoptosis in cultured neuronal cells expressing truncated androgen receptor protein with expanded polyglutamine tract
    • Kobayashi Y, Kume A, Li M, Doyu M, Hata M, Ohtsuka K, Sobue G. 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    Sobue, G.7
  • 52
    • 0033499931 scopus 로고    scopus 로고
    • Analysis of the role of heat shock protein (Hsp) molecular chaperones in polyglutamine disease
    • Chai Y, Koppenhafer SL, Bonini NM, Paulson HL. Analysis of the role of heat shock protein (Hsp) molecular chaperones in polyglutamine disease. J Neurosci 1999;19:10338-10347.
    • (1999) J. Neurosci. , vol.19 , pp. 10338-10347
    • Chai, Y.1    Koppenhafer, S.L.2    Bonini, N.M.3    Paulson, H.L.4
  • 53
    • 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. Nature Genet 1998;19:148-154.
    • (1998) Nature 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
  • 54
    • 0035930598 scopus 로고    scopus 로고
    • Chaperone suppression of cellular toxicity of huntingtin is independent of polyglutamine aggregation
    • Zhou H, Li SH, Li XJ. Chaperone suppression of cellular toxicity of huntingtin is independent of polyglutamine aggregation. J Biol Chem 2001;276:48417-48424.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48417-48424
    • Zhou, H.1    Li, S.H.2    Li, X.J.3
  • 55
    • 0034646426 scopus 로고    scopus 로고
    • Effects of heat shock, heat shock protein 40 (HDJ-2), and proteasome inhibition on protein aggregation in cellular models of Huntington's disease
    • Wyttenbach A, Carmichael J, Swartz J, Furlong RA, Narain Y, Rankin J, Rubinsztein DC. Effects of heat shock, heat shock protein 40 (HDJ-2), and proteasome inhibition on protein aggregation in cellular models of Huntington's disease. Proc Natl Acad Sci (USA) 2000;97:2898-2903.
    • (2000) Proc. Natl. Acad. Sci. (USA) , vol.97 , pp. 2898-2903
    • Wyttenbach, A.1    Carmichael, J.2    Swartz, J.3    Furlong, R.A.4    Narain, Y.5    Rankin, J.6    Rubinsztein, D.C.7
  • 56
    • 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
  • 57
    • 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
  • 59
    • 0037059040 scopus 로고    scopus 로고
    • Chaperoning brain degeneration
    • Bonini NM. Chaperoning brain degeneration. Proc Natl Acad Sci (USA) 2002. 99, Suppl 4:16407-16411.
    • (2002) Proc. Natl. Acad. Sci. (USA) , vol.99 , Issue.SUPPL. 4 , pp. 16407-16411
    • Bonini, N.M.1
  • 61
    • 0037444446 scopus 로고    scopus 로고
    • Heat shock protein 70 chaperone overexpression ameliorates phenotypes of the spinal and bulbar muscular atrophy transgenic mouse model by reducing nuclear-localized mutant androgen receptor protein
    • Adachi H, Katsuno M, Minamiyama M, Sang C, Pagoulatos G, Angelidis C, Kusakabe M, Yoshiki A, Kobayashi Y, Doyu M, Sobue G. Heat shock protein 70 chaperone overexpression ameliorates phenotypes of the spinal and bulbar muscular atrophy transgenic mouse model by reducing nuclear-localized mutant androgen receptor protein. J Neurosci 2003;23:2203-2211.
    • (2003) J. Neurosci. , vol.23 , pp. 2203-2211
    • Adachi, H.1    Katsuno, M.2    Minamiyama, M.3    Sang, C.4    Pagoulatos, G.5    Angelidis, C.6    Kusakabe, M.7    Yoshiki, A.8    Kobayashi, Y.9    Doyu, M.10    Sobue, G.11
  • 62
    • 0347928859 scopus 로고    scopus 로고
    • Overexpression of heat shock protein 70 in R6/2 Huntington's disease mice has only modest effects on disease progression
    • Hansson O, Nylandsted J, Castilho RF, Leist M, Jaattela M, Brundin P. Overexpression of heat shock protein 70 in R6/2 Huntington's disease mice has only modest effects on disease progression. Brain Res 2003;970:47-57.
    • (2003) Brain Res. , vol.970 , pp. 47-57
    • Hansson, O.1    Nylandsted, J.2    Castilho, R.F.3    Leist, M.4    Jaattela, M.5    Brundin, P.6
  • 63
    • 1242274389 scopus 로고    scopus 로고
    • Heat shock protein 70 participates in the neuroprotective response to intracellularly expressed beta-amyloid in neurons
    • Magrane J, Smith RC, Walsh K, Querfurth HW. Heat shock protein 70 participates in the neuroprotective response to intracellularly expressed beta-amyloid in neurons. J Neurosci 2004;24:1700-1706.
    • (2004) J. Neurosci. , vol.24 , pp. 1700-1706
    • Magrane, J.1    Smith, R.C.2    Walsh, K.3    Querfurth, H.W.4
  • 64
    • 0344507132 scopus 로고    scopus 로고
    • Up-regulation of protein chaperones preserves viability of cells expressing toxic Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis
    • Bruening W, Roy J, Giasson B, Figlewicz DA, Mushynski WE, Durham HD. Up-regulation of protein chaperones preserves viability of cells expressing toxic Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis. J Neurochem 1999;72:693-699.
    • (1999) J. Neurochem. , vol.72 , pp. 693-699
    • Bruening, W.1    Roy, J.2    Giasson, B.3    Figlewicz, D.A.4    Mushynski, W.E.5    Durham, H.D.6
  • 65
    • 2942620074 scopus 로고    scopus 로고
    • Hsp70 reduces alpha-synuclein aggregation and toxicity
    • Epub 2004 Mar 25
    • Klucken J, Shin Y, Masliah E, Hyman BT, McLean PJ. Hsp70 reduces alpha-synuclein aggregation and toxicity. J Biol Chem 2004;279:25497-25502. Epub 2004 Mar 25.
    • (2004) J. Biol. Chem. , vol.279 , pp. 25497-25502
    • Klucken, J.1    Shin, Y.2    Masliah, E.3    Hyman, B.T.4    McLean, P.J.5
  • 66
    • 0036468432 scopus 로고    scopus 로고
    • Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease
    • Auluck PK, Chan HY, Trojanowski JQ, Lee VM, Bonini NM. Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease. Science 2002;295:865-868.
    • (2002) Science , vol.295 , pp. 865-868
    • Auluck, P.K.1    Chan, H.Y.2    Trojanowski, J.Q.3    Lee, V.M.4    Bonini, N.M.5
  • 67
    • 0038356802 scopus 로고    scopus 로고
    • Heat shock protein-90-induced microglial clearance of exogenous amyloid-betal-42 in rat hippocampus in vivo
    • Takata K, Kitamura Y, Tsuchiya D, Kawasaki T, Taniguchi T, Shimohama S. Heat shock protein-90-induced microglial clearance of exogenous amyloid-betal-42 in rat hippocampus in vivo. Neurosci Lett 2003;344:87-90.
    • (2003) Neurosci. Lett. , vol.344 , pp. 87-90
    • Takata, K.1    Kitamura, Y.2    Tsuchiya, D.3    Kawasaki, T.4    Taniguchi, T.5    Shimohama, S.6
  • 68
    • 1642356755 scopus 로고    scopus 로고
    • HSP27 but not HSP70 has a potent protective effect against alpha-synuclein-induced cell death in mammalian neuronal cells
    • Zourlidou A, Payne Smith MD, Latchman DS. HSP27 but not HSP70 has a potent protective effect against alpha-synuclein-induced cell death in mammalian neuronal cells. J Neurochem 2004;88:1439-1448.
    • (2004) J. Neurochem. , vol.88 , pp. 1439-1448
    • Zourlidou, A.1    Payne Smith, M.D.2    Latchman, D.S.3
  • 69
    • 2342444942 scopus 로고    scopus 로고
    • Binding of tau to heat shock protein 27 leads to decreased concentration of hyperphosphorylated tau and enhanced cell survival
    • Epub 2004 Feb 12
    • Shimura H, Miura-Shimura Y, Kosik KS. Binding of tau to heat shock protein 27 leads to decreased concentration of hyperphosphorylated tau and enhanced cell survival. J Biol Chem 2004;279:17957-17962. Epub 2004 Feb 12.
    • (2004) J. Biol. Chem. , vol.279 , pp. 17957-17962
    • Shimura, H.1    Miura-Shimura, Y.2    Kosik, K.S.3
  • 70
    • 0042591262 scopus 로고    scopus 로고
    • Hsp105alpha suppresses the aggregation of truncated androgen receptor with expanded CAG repeats and cell toxicity
    • Epub 2003 Apr 24
    • Ishibara K, Yamagishi N, Saito Y, Adachi H, Kobayashi Y, Sobue G, Ohtsuka K, Hatayama T. Hsp105alpha suppresses the aggregation of truncated androgen receptor with expanded CAG repeats and cell toxicity. J Biol Chem 2003;278:25143-25150. Epub 2003 Apr 24.
    • (2003) J. Biol. Chem. , vol.278 , pp. 25143-25150
    • Ishibara, K.1    Yamagishi, N.2    Saito, Y.3    Adachi, H.4    Kobayashi, Y.5    Sobue, G.6    Ohtsuka, K.7    Hatayama, T.8
  • 71
    • 1942486792 scopus 로고    scopus 로고
    • Treatment with arimoclomol, a coinducer of heat shock proteins, delays disease progression in ALS mice
    • Epub 2004 Mar 21
    • Kieran D, Kalmar B, Dick JR, Riddoch-Contreras J, Burnstock G, Greensmith L. Treatment with arimoclomol, a coinducer of heat shock proteins, delays disease progression in ALS mice. Nat Med 2004;10:402-405. Epub 2004 Mar 21.
    • (2004) Nat. Med. , vol.10 , pp. 402-405
    • Kieran, D.1    Kalmar, B.2    Dick, J.R.3    Riddoch-Contreras, J.4    Burnstock, G.5    Greensmith, L.6
  • 74
    • 0027996115 scopus 로고
    • Protein disaggregation mediated by heat-shock protein Hsp104
    • Parsell DA, Kowal AS, Singer MA, Lindquist S. Protein disaggregation mediated by heat-shock protein Hsp104. Nature 1994;372:475-478.
    • (1994) Nature , vol.372 , pp. 475-478
    • Parsell, D.A.1    Kowal, A.S.2    Singer, M.A.3    Lindquist, S.4
  • 76
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins
    • Glover JR, Lindquist S. Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 1998;94:73-82.
    • (1998) Cell , vol.94 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 77
    • 0033598703 scopus 로고    scopus 로고
    • Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network
    • Goloubinoff P, Mogk A, Zvi AP, Tomoyasu T, Bukau B. Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Proc Natl Acad Sci (USA) 1999;96:13732-13737.
    • (1999) Proc. Natl. Acad. Sci. (USA) , vol.96 , pp. 13732-13737
    • Goloubinoff, P.1    Mogk, A.2    Zvi, A.P.3    Tomoyasu, T.4    Bukau, B.5
  • 78
    • 3042561822 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Hsp104 enhances the chaperone capacity of human cells and inhibits heat stress-induced proapoptotic signaling
    • Mosser DD, Ho S, Glover JR. Saccharomyces cerevisiae Hsp104 enhances the chaperone capacity of human cells and inhibits heat stress-induced proapoptotic signaling. Biochemistry 2004;43:8107-8115.
    • (2004) Biochemistry , vol.43 , pp. 8107-8115
    • Mosser, D.D.1    Ho, S.2    Glover, J.R.3
  • 79
    • 0035684430 scopus 로고    scopus 로고
    • CHIP is a chaperonedependent E3 ligase that ubiquitylates unfolded protein
    • Murata S, Minami Y, Minami M, Chiba T, Tanaka K. CHIP is a chaperonedependent E3 ligase that ubiquitylates unfolded protein. EMBO Rep 2001;2:1133-1138.
    • (2001) EMBO Rep. , vol.2 , pp. 1133-1138
    • Murata, S.1    Minami, Y.2    Minami, M.3    Chiba, T.4    Tanaka, K.5
  • 80
    • 0142093671 scopus 로고    scopus 로고
    • Pael receptor, endoplasmic reticulum stress, and Parkinson's disease
    • Takahashi R, Imai Y. Pael receptor, endoplasmic reticulum stress, and Parkinson's disease. J Neurol 2003;250 (Suppl 3):11125-11129.
    • (2003) J. Neurol. , vol.250 , Issue.SUPPL. 3 , pp. 11125-11129
    • Takahashi, R.1    Imai, Y.2
  • 81
    • 0036345454 scopus 로고    scopus 로고
    • CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity
    • Imai Y, Soda M, Hatakeyama S, Akagi T, Hashikawa T, Nakayama KI, Takahashi R. CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity. Mol Cell 2002;10:55-67.
    • (2002) Mol. Cell , vol.10 , pp. 55-67
    • Imai, Y.1    Soda, M.2    Hatakeyama, S.3    Akagi, T.4    Hashikawa, T.5    Nakayama, K.I.6    Takahashi, R.7
  • 82
    • 0038159253 scopus 로고    scopus 로고
    • Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function
    • Epub 2003 Apr 03
    • Tsai YC, Fishman PS, Thakor NV, Oyler GA. Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function. J Biol Chem 2003;278:22044-22055. Epub 2003 Apr 03.
    • (2003) J. Biol. Chem. , vol.278 , pp. 22044-22055
    • Tsai, Y.C.1    Fishman, P.S.2    Thakor, N.V.3    Oyler, G.A.4
  • 83
    • 1042266624 scopus 로고    scopus 로고
    • CHIP-Hsc7O complex ubiquitinates phosphorylated tau and enhances cell survival
    • Epub 2003 Nov 10
    • Shimura H, Schwartz D, Gygi SP, Kosik KS. CHIP-Hsc7O complex ubiquitinates phosphorylated tau and enhances cell survival. J Biol Chem 2004;279:4869-4876. Epub 2003 Nov 10.
    • (2004) J. Biol. Chem. , vol.279 , pp. 4869-4876
    • Shimura, H.1    Schwartz, D.2    Gygi, S.P.3    Kosik, K.S.4
  • 84
    • 5444239863 scopus 로고    scopus 로고
    • U-box protein carboxyl terminus of Hsc70-interacting protein (CHIP) mediates poly-ubiquitylation preferentially on four-repeat Tau and is involved in neurodegeneration of tauopathy
    • Hatakeyama S, Matsumoto M, Kamura T, Murayama M, Chui DH, Planel E, Takahashi R, Nakayama KI, Takashima A. U-box protein carboxyl terminus of Hsc70-interacting protein (CHIP) mediates poly-ubiquitylation preferentially on four-repeat Tau and is involved in neurodegeneration of tauopathy. J Neurochem 2004;91:299-307.
    • (2004) J. Neurochem. , vol.91 , pp. 299-307
    • Hatakeyama, S.1    Matsumoto, M.2    Kamura, T.3    Murayama, M.4    Chui, D.H.5    Planel, E.6    Takahashi, R.7    Nakayama, K.I.8    Takashima, A.9
  • 85
    • 0032582562 scopus 로고    scopus 로고
    • Role of Hsp70 in regulation of stress-kinase JNK: Implication in apoptosis and aging
    • Gabai VL, Meriin AB, Yaglom JA, Volloch VZ, Sherman MY. Role of Hsp70 in regulation of stress-kinase JNK: implication in apoptosis and aging. FEBS Lett 1998;438:1-4.
    • (1998) FEBS Lett. , vol.438 , pp. 1-4
    • Gabai, V.L.1    Meriin, A.B.2    Yaglom, J.A.3    Volloch, V.Z.4    Sherman, M.Y.5
  • 86
    • 0029347097 scopus 로고
    • Puromycin induces apoptosis of developing chick sympathetic neurons in a similar manner to NGF-deprivation
    • Sugita M, Morita T, Yonesaki T. Puromycin induces apoptosis of developing chick sympathetic neurons in a similar manner to NGF-deprivation. Zoological Sci 1995;12:419-425.
    • (1995) Zoological. Sci. , vol.12 , pp. 419-425
    • Sugita, M.1    Morita, T.2    Yonesaki, T.3
  • 88
    • 0026771452 scopus 로고
    • Induced thermotolerance to apoptosis in a human T lymphocyte cell line
    • Mosser DD, Martin LH. Induced thermotolerance to apoptosis in a human T lymphocyte cell line. J Cell Physiol 1992;151:561-570.
    • (1992) J. Cell. Physiol. , vol.151 , pp. 561-570
    • Mosser, D.D.1    Martin, L.H.2
  • 89
    • 0030739208 scopus 로고    scopus 로고
    • Role of the human heat shock protein hsp70 in protection against stress-induced apoptosis
    • Mosser DD, Caron AW, Bourget L, Denis-Larose C, Massie B. Role of the human heat shock protein hsp70 in protection against stress-induced apoptosis. Mol Cell Biol 1997;17:5317-5327.
    • (1997) Mol. Cell Biol. , vol.17 , pp. 5317-5327
    • Mosser, D.D.1    Caron, A.W.2    Bourget, L.3    Denis-Larose, C.4    Massie, B.5
  • 91
    • 0032513215 scopus 로고    scopus 로고
    • Proteasome inhibitors activate stress-kinases and induce Hsp72: Diverse effects on apoptosis
    • Meriin A, Gabai V, Yaglom J, Shiffin V, Sherman M. Proteasome inhibitors activate stress-kinases and induce Hsp72: diverse effects on apoptosis. J Biol Chem 1998;273:6373-6379.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6373-6379
    • Meriin, A.1    Gabai, V.2    Yaglom, J.3    Shiffin, V.4    Sherman, M.5
  • 92
    • 0034644522 scopus 로고    scopus 로고
    • Signal transduction by the JNK group of MAP kinases
    • Davis RJ. Signal transduction by the JNK group of MAP kinases. Cell 2000;103:239-252.
    • (2000) Cell , vol.103 , pp. 239-252
    • Davis, R.J.1
  • 93
    • 0033118607 scopus 로고    scopus 로고
    • The Jnk1 and Jnk2 protein kinases are required for regional specific apoptosis during early brain development
    • Kuan CY, Yang DD, Roy DRS, Davis RJ, Rakic P, Flavell RA. The Jnk1 and Jnk2 protein kinases are required for regional specific apoptosis during early brain development. Neuron 1999;22:667-676.
    • (1999) Neuron , vol.22 , pp. 667-676
    • Kuan, C.Y.1    Yang, D.D.2    Roy, D.R.S.3    Davis, R.J.4    Rakic, P.5    Flavell, R.A.6
  • 95
    • 0001388128 scopus 로고    scopus 로고
    • Expression of polyglutamine-expanded Huntingtin activates the SEK1-JNK pathway and induces apoptosis in a hippocampal neuronal cell line
    • Liu YF. Expression of polyglutamine-expanded Huntingtin activates the SEK1-JNK pathway and induces apoptosis in a hippocampal neuronal cell line. J Biol Chem 1998;273:28873-28877.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28873-28877
    • Liu, Y.F.1
  • 97
    • 0038269098 scopus 로고    scopus 로고
    • Polyglutamine expansion induces a protein-damaging stress connecting heat shock protein 70 to the JNK pathway
    • Epub 2003 Feb 21
    • Merienne K, Helmlinger D, Perkin GR, Devys D, Trottier Y. Polyglutamine expansion induces a protein-damaging stress connecting heat shock protein 70 to the JNK pathway. J Biol Chem 2003;278:16957-16967. Epub 2003 Feb 21.
    • (2003) J. Biol. Chem. , vol.278 , pp. 16957-16967
    • Merienne, K.1    Helmlinger, D.2    Perkin, G.R.3    Devys, D.4    Trottier, Y.5
  • 98
    • 0041816369 scopus 로고    scopus 로고
    • Kennedy's disease. Phosphorylation of the polyglutamine-expanded form of androgen receptor regulates its cleavage by caspase-3 and enhances cell death
    • LaFevre-Bernt M, Ellerby L. Kennedy's disease. Phosphorylation of the polyglutamine-expanded form of androgen receptor regulates its cleavage by caspase-3 and enhances cell death. J Biol Chem 2003;278:34918-34924.
    • (2003) J. Biol. Chem. , vol.278 , pp. 34918-34924
    • LaFevre-Bernt, M.1    Ellerby, L.2
  • 99
    • 4143112468 scopus 로고    scopus 로고
    • Expanded huntingtin activates the C-Jun N terminal kinase/C-Jun pathway prior to aggregate formation in striatal neurons in culture
    • Garcia M, Charvin D, Caboche J. Expanded huntingtin activates the C-Jun N terminal kinase/C-Jun pathway prior to aggregate formation in striatal neurons in culture. Neuroscience 2004;127:859-870.
    • (2004) Neuroscience , vol.127 , pp. 859-870
    • Garcia, M.1    Charvin, D.2    Caboche, J.3
  • 101
    • 0001583878 scopus 로고    scopus 로고
    • Activation of MLK2-mediated signaling cascades by polyglutamine-expanded huntingtin
    • Liu YF, Dorow D, Marshall J. Activation of MLK2-mediated signaling cascades by polyglutamine-expanded huntingtin. J Biol Chem 2000;275:19035-19040.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19035-19040
    • Liu, Y.F.1    Dorow, D.2    Marshall, J.3
  • 102
    • 0036606540 scopus 로고    scopus 로고
    • ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats
    • Nishitoh H, Matsuzawa A, Tobiume K, Saegusa K, Takeda K, Inoue K, Hori S, Kakizuka A, Ichijo H. ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats. Genes Dev 2002;16:1345-1355.
    • (2002) Genes Dev. , vol.16 , pp. 1345-1355
    • Nishitoh, H.1    Matsuzawa, A.2    Tobiume, K.3    Saegusa, K.4    Takeda, K.5    Inoue, K.6    Hori, S.7    Kakizuka, A.8    Ichijo, H.9
  • 103
    • 0032932192 scopus 로고    scopus 로고
    • Protein-damaging stresses activate c-Jun N-terminal kinase via inhibition of its dephosphorylation: A novel pathway controlled by HSP72
    • Meriin AB, Yaglom JA, Gabai VL, Zon L, Ganiatsas S, Mosser DD, Zen L, Sherman MY. Protein-damaging stresses activate c-Jun N-terminal kinase via inhibition of its dephosphorylation: a novel pathway controlled by HSP72. Mol Cell Biol 1999;19:2547-2555.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 2547-2555
    • Meriin, A.B.1    Yaglom, J.A.2    Gabai, V.L.3    Zon, L.4    Ganiatsas, S.5    Mosser, D.D.6    Zen, L.7    Sherman, M.Y.8
  • 104
    • 0035908997 scopus 로고    scopus 로고
    • The JNK phosphatase M3/6 is inhibited by protein-damaging stress
    • Palacios C, Collins MK, Perkins GR. The JNK phosphatase M3/6 is inhibited by protein-damaging stress. Curr Biol 2001;11:1439-1443.
    • (2001) Curr. Biol. , vol.11 , pp. 1439-1443
    • Palacios, C.1    Collins, M.K.2    Perkins, G.R.3
  • 105
    • 0037908648 scopus 로고    scopus 로고
    • Inactivation of dual specificity phosphatases is involved in the regulation of extracellular signal-regulated kinases by heat shock and hsp72
    • Yaglom J, O'Callaghan-Sunol C, Gabai V, Sherman MY. Inactivation of dual specificity phosphatases is involved in the regulation of extracellular signal-regulated kinases by heat shock and hsp72. Mol Cell Biol 2003;23:3813-3824.
    • (2003) Mol. Cell Biol. , vol.23 , pp. 3813-3824
    • Yaglom, J.1    O'Callaghan-Sunol, C.2    Gabai, V.3    Sherman, M.Y.4
  • 110
    • 0035889973 scopus 로고    scopus 로고
    • Proteasomal-dependent aggregate reversal and absence of cell death in a conditional mouse model of Huntington's disease
    • Martin-Aparicio E, Yamamoto A, Hernandez F, Hen R, Avila J, Lucas JJ. Proteasomal-dependent aggregate reversal and absence of cell death in a conditional mouse model of Huntington's disease. J Neurosci 2001;21:8772-8781.
    • (2001) J. Neurosci. , vol.21 , pp. 8772-8781
    • Martin-Aparicio, E.1    Yamamoto, A.2    Hernandez, F.3    Hen, R.4    Avila, J.5    Lucas, J.J.6
  • 111
    • 0346786308 scopus 로고    scopus 로고
    • Living forever and dying in the attempt
    • Hayflick L. Living forever and dying in the attempt. Exp Gerontol 2003;38:1231-1241.
    • (2003) Exp. Gerontol. , vol.38 , pp. 1231-1241
    • Hayflick, L.1
  • 112
    • 0033732110 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms of stress-induced premature senescence (SIPS) of human diploid fibroblasts and melanocytes
    • Toussaint O, Medrano EE, von Zglinicki T. Cellular and molecular mechanisms of stress-induced premature senescence (SIPS) of human diploid fibroblasts and melanocytes. Exp Gerontol 2000;35: 927-945.
    • (2000) Exp. Gerontol. , vol.35 , pp. 927-945
    • Toussaint, O.1    Medrano, E.E.2    von Zglinicki, T.3
  • 113
    • 0035500487 scopus 로고    scopus 로고
    • Cellular senescence as a tumor-suppressor mechanism
    • Campisi J. Cellular senescence as a tumor-suppressor mechanism. Trends Cell Biol 2001;11:S27-S31.
    • (2001) Trends Cell Biol. , vol.11
    • Campisi, J.1
  • 114
    • 2342570379 scopus 로고    scopus 로고
    • Hallmarks of senescence in carcinogenesis and cancer therapy
    • Shay JW, Roninson IB. Hallmarks of senescence in carcinogenesis and cancer therapy. Oncogene 2004;23:2919-2933.
    • (2004) Oncogene , vol.23 , pp. 2919-2933
    • Shay, J.W.1    Roninson, I.B.2
  • 115
    • 0042346327 scopus 로고    scopus 로고
    • Central role of the proteasome in senescence and survival of human fibroblasts: Induction of a senescence-like phenotype upon its inhibition and resistance to stress upon its activation
    • Epub 2003 May 07
    • Chondrogianni N, Stratford FL, Trougakos IP, Friguet B, Rivett AJ, Genes ES. Central role of the proteasome in senescence and survival of human fibroblasts: induction of a senescence-like phenotype upon its inhibition and resistance to stress upon its activation. J Biol Chem 2003;278:28026-28037. Epub 2003 May 07.
    • (2003) J. Biol. Chem. , vol.278 , pp. 28026-28037
    • Chondrogianni, N.1    Stratford, F.L.2    Trougakos, I.P.3    Friguet, B.4    Rivett, A.J.5    Genes, E.S.6
  • 116
    • 0024359486 scopus 로고
    • Attenuated induction of heat shock gene expression in aging diploid fibroblasts
    • Liu AY, Lin Z, Choi HS, Sorhage F, Li B. Attenuated induction of heat shock gene expression in aging diploid fibroblasts. J Biol Chem 1989;264:12037-12045.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12037-12045
    • Liu, A.Y.1    Lin, Z.2    Choi, H.S.3    Sorhage, F.4    Li, B.5
  • 117
    • 1842789989 scopus 로고    scopus 로고
    • Mechanisms of cellular senescence in human and mouse cells
    • Itahana K, Campisi J, Dimri GP. Mechanisms of cellular senescence in human and mouse cells. Biogerontology 2004;5:1-10.
    • (2004) Biogerontology , vol.5 , pp. 1-10
    • Itahana, K.1    Campisi, J.2    Dimri, G.P.3
  • 118
    • 0021171248 scopus 로고
    • Werner's syndrome: An underdiagnosed disorder resembling premature aging
    • Tollefsbol TO, Cohen HJ. Werner's syndrome: an underdiagnosed disorder resembling premature aging. Age 1984;7:75-88.
    • (1984) Age , vol.7 , pp. 75-88
    • Tollefsbol, T.O.1    Cohen, H.J.2
  • 119
    • 0032524563 scopus 로고    scopus 로고
    • Molecular analysis of H202-induced senescent-like growth arrest in normal human fibroblasts: P53 and Rb control G1 arrest but not cell replication
    • Chen QM, Bartholomew JC, Campisi J, Acosta M, Reagan JD, Ames BN. Molecular analysis of H202-induced senescent-like growth arrest in normal human fibroblasts: p53 and Rb control G1 arrest but not cell replication. Biochem J 1998;332:43-50.
    • (1998) Biochem. J. , vol.332 , pp. 43-50
    • Chen, Q.M.1    Bartholomew, J.C.2    Campisi, J.3    Acosta, M.4    Reagan, J.D.5    Ames, B.N.6
  • 120
    • 1842789948 scopus 로고    scopus 로고
    • Proteasome inhibition induces a senescence-like phenotype in primary human fibroblasts cultures
    • Chondrogianni N, Gonos ES. Proteasome inhibition induces a senescence-like phenotype in primary human fibroblasts cultures. Biogerontology 2004;5:55-61.
    • (2004) Biogerontology , vol.5 , pp. 55-61
    • Chondrogianni, N.1    Gonos, E.S.2
  • 121
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence NF, Sampat RM, Kopito RR. Impairment of the ubiquitin-proteasome system by protein aggregation. Science 2001;292:1552-1555.
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 122
    • 0035504960 scopus 로고    scopus 로고
    • Centrosome disorganization in fibroblast cultures derived from R6/2 Huntington's disease (HD) transgenic mice and HD patients
    • Sathasivam K, Woodman B, Mahal A, Bertaux F, Wanker EE, Shima DT, Bates GP. Centrosome disorganization in fibroblast cultures derived from R6/2 Huntington's disease (HD) transgenic mice and HD patients. Hum Mol Genet 2001;10:2425-2435.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 2425-2435
    • Sathasivam, K.1    Woodman, B.2    Mahal, A.3    Bertaux, F.4    Wanker, E.E.5    Shima, D.T.6    Bates, G.P.7
  • 123
    • 4444303263 scopus 로고    scopus 로고
    • Generalized brain and skin proteasome inhibition in Huntington's disease
    • Seo H, Sonntag KC, Isacson O. Generalized brain and skin proteasome inhibition in Huntington's disease. Ann Neurol 2004;56:319-328.
    • (2004) Ann. Neurol. , vol.56 , pp. 319-328
    • Seo, H.1    Sonntag, K.C.2    Isacson, O.3
  • 125
    • 0034131044 scopus 로고    scopus 로고
    • Impaired proteasome function in Alzheimer's disease
    • Keller JN, Hanni KB, Markesbery WR. Impaired proteasome function in Alzheimer's disease. J Neurochem 2000;75:436-439.
    • (2000) J. Neurochem. , vol.75 , pp. 436-439
    • Keller, J.N.1    Hanni, K.B.2    Markesbery, W.R.3
  • 127
    • 0037159608 scopus 로고    scopus 로고
    • Lysosomal malfunction accompanies alpha-synuclein aggregation in a progressive mouse model of Parkinson's disease
    • Meredith GE, Totterdell S, Petroske E, Santa Cruz K, Callison Jr RC, Lau YS. Lysosomal malfunction accompanies alpha-synuclein aggregation in a progressive mouse model of Parkinson's disease. Brain Res 2002;956:156-165.
    • (2002) Brain Res. , vol.956 , pp. 156-165
    • Meredith, G.E.1    Totterdell, S.2    Petroske, E.3    Santa Cruz, K.4    Callison Jr., R.C.5    Lau, Y.S.6
  • 128
    • 4644238084 scopus 로고    scopus 로고
    • Early changes in neurons of the hippocampus and neocortex in transgenic rats expressing intracellular human a-beta
    • discussion 443-449
    • Lopez EM, Bell KF, Ribeiro-da-Silva A, Cuello AC. Early changes in neurons of the hippocampus and neocortex in transgenic rats expressing intracellular human a-beta. J Alzheimers Dis 2004;6:421-31, discussion 443-449.
    • (2004) J. Alzheimers Dis. , vol.6 , pp. 421-431
    • Lopez, E.M.1    Bell, K.F.2    Ribeiro-da-Silva, A.3    Cuello, A.C.4
  • 129
    • 0037418339 scopus 로고    scopus 로고
    • Dietary restriction normalizes glucose metabolism and BDNF levels, slows disease progression, and increases survival in huntingtin mutant mice
    • Epub 2003 Feb 14
    • Duan W, Guo Z, Jiang H, Ware M, Li XJ, Mattson MP. Dietary restriction normalizes glucose metabolism and BDNF levels, slows disease progression, and increases survival in huntingtin mutant mice. Proc Natl Acad Sci (USA) 2003;100:2911-2916. Epub 2003 Feb 14.
    • (2003) Proc. Natl. Acad. Sci. (USA) , vol.100 , pp. 2911-2916
    • Duan, W.1    Guo, Z.2    Jiang, H.3    Ware, M.4    Li, X.J.5    Mattson, M.P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.