메뉴 건너뛰기




Volumn 321, Issue 3, 2004, Pages 665-669

Geldanamycin induces Hsp70 and prevents α-synuclein aggregation and toxicity in vitro

Author keywords

Aggregation; Heat shock protein; Lewy body; Parkinson's disease; Protein folding

Indexed keywords

ALPHA SYNUCLEIN; GELDANAMYCIN; HEAT SHOCK PROTEIN 70;

EID: 4344569643     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.07.021     Document Type: Article
Times cited : (161)

References (18)
  • 1
    • 0034703863 scopus 로고    scopus 로고
    • Mechanisms of chaperone suppression of polyglutamine disease: Selectivity, synergy and modulation of protein solubility in Drosophila
    • H.Y. Chan, J.M. Warrick, G.L. Gray-Board, H.L. Paulson, and N.M. Bonini Mechanisms of chaperone suppression of polyglutamine disease: selectivity, synergy and modulation of protein solubility in Drosophila Hum. Mol. Genet. 9 2000 2811 2820
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2811-2820
    • Chan, H.Y.1    Warrick, J.M.2    Gray-Board, G.L.3    Paulson4    Bonini, N.M.H.L.5
  • 2
    • 0031838352 scopus 로고    scopus 로고
    • Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1
    • C.J. Cummings, M.A. Mancini, B. Antalffy, D.B. Defranco, H.T. Orr, and H.Y. Zoghbi Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1 Nat. Genet. 19 1998 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    Orr5    Zoghbi, H.Y.H.T.6
  • 3
    • 0036468432 scopus 로고    scopus 로고
    • Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson’s disease
    • P.K. Auluck, H.Y. Chan, J.Q. Trojanowski, V.M. Lee, and N.M. Bonini Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson’s disease Science 295 2002 865 868
    • (2002) Science , vol.295 , pp. 865-868
    • Auluck, P.K.1    Chan, H.Y.2    Trojanowski, J.Q.3    Lee4    Bonini, N.M.V.M.5
  • 4
    • 0031944830 scopus 로고    scopus 로고
    • Nigral and cortical Lewy bodies and dystrophic nigral neurites in Parkinson’s disease and cortical Lewy body disease contain alpha-synuclein immunoreactivity
    • M.C. Irizarry, W. Growdon, T. Gomez-Isla, K. Newell, J.M. George, D.F. Clayton, and B.T. Hyman Nigral and cortical Lewy bodies and dystrophic nigral neurites in Parkinson’s disease and cortical Lewy body disease contain alpha-synuclein immunoreactivity J. Neuropathol. Exp. Neurol. 57 1998 334 337
    • (1998) J. Neuropathol. Exp. Neurol. , vol.57 , pp. 334-337
    • Irizarry, M.C.1    Growdon, W.2    Gomez-Isla, T.3    Newell, K.4    George, J.M.5    Clayton6    Hyman, B.T.D.F.7
  • 8
    • 0035363805 scopus 로고    scopus 로고
    • Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington’s disease
    • A. Sittler, R. Lurz, G. Lueder, J. Priller, M.K. Hayer-Hartl, F.U. Hartl, H. Lehrach, and E.R. Wanker Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntingtonâ €™s disease Human. Mol. Genet. 10 2001 1307 1315
    • (2001) Human. Mol. Genet. , vol.10 , pp. 1307-1315
    • Sittler, A.1    Lurz, R.2    Lueder, G.3    Priller, J.4    Hayer-Hartl, M.K.5    Hartl, F.U.6    Lehrach7    Wanker, E.R.H.8
  • 9
    • 0036852712 scopus 로고    scopus 로고
    • Pharmacological prevention of parkinson disease in Drosophila
    • P.K. Auluck, and N.M. Bonini Pharmacological prevention of parkinson disease in Drosophila Nat. Med. 8 2002 1185 1186
    • (2002) Nat. Med. , vol.8 , pp. 1185-1186
    • Auluck1    Bonini, N.M.P.K.2
  • 11
    • 0035859226 scopus 로고    scopus 로고
    • α-Synuclein-enhanced green fluorescent protein fusion proteins form proteasomal sensitive inclusions in primary neurons
    • P.J. McLean, H. Kawamata, and B.T. Hyman α-Synuclein- enhanced green fluorescent protein fusion proteins form proteasomal sensitive inclusions in primary neurons Neuroscience 104 2001 901 912
    • (2001) Neuroscience , vol.104 , pp. 901-912
    • McLean, P.J.1    Kawamata2    Hyman, B.T.H.3
  • 12
    • 0034708767 scopus 로고    scopus 로고
    • Membrane association and protein conformation of alpha-synuclein in intact neurons. Effect of Parkinson’s disease-linked mutations
    • P.J. McLean, H. Kawamata, S. Ribich, and B.T. Hyman Membrane association and protein conformation of alpha-synuclein in intact neurons. Effect of Parkinson’s disease-linked mutations J. Biol. Chem. 275 2000 8812 8816
    • (2000) J. Biol. Chem. , vol.275 , pp. 8812-8816
    • McLean, P.J.1    Kawamata, H.2    Ribich3    Hyman, B.T.S.4
  • 14
    • 0034996655 scopus 로고    scopus 로고
    • Interaction of α-synuclein and synphilin-1: Effect of Parkinson’s disease associated mutations
    • H. Kawamata, P.J. McLean, N. Sharma, and B.T. Hyman Interaction of α-synuclein and synphilin-1: effect of Parkinson†™s disease associated mutations J. Neurochem. 77 2001 929 934
    • (2001) J. Neurochem. , vol.77 , pp. 929-934
    • Kawamata, H.1    McLean, P.J.2    Sharma3    Hyman, B.T.N.4
  • 16
    • 0023931333 scopus 로고
    • Lewy bodies are ubiquitinated. A light and electron microscopic immunocytochemical study
    • S. Kuzuhara, H. Mori, N. Izumiyama, M. Yoshimura, and Y. Ihara Lewy bodies are ubiquitinated. A light and electron microscopic immunocytochemical study Acta. Neuropathol. (Berl.) 75 1988 345 353
    • (1988) Acta. Neuropathol. (Berl.) , vol.75 , pp. 345-353
    • Kuzuhara, S.1    Mori, H.2    Izumiyama, N.3    Yoshimura4    Ihara, Y.M.5
  • 17
    • 0038386274 scopus 로고    scopus 로고
    • Zeroing in on the pathogenic form of alpha-synuclein and its mechanism of neurotoxicity in Parkinson’s disease
    • M.J. Volles, and P.T. Lansbury Jr. Zeroing in on the pathogenic form of alpha-synuclein and its mechanism of neurotoxicity in Parkinson†™s disease Biochemistry 42 2003 7871 7878
    • (2003) Biochemistry , vol.42 , pp. 7871-7878
    • Lansbury P.T., Jr.1    Volles, M.J.2
  • 18
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • B. Caughey, and P.T. Lansbury Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders Annu. Rev. Neurosci. 26 2003 267 298
    • (2003) Annu. Rev. Neurosci. , vol.26 , pp. 267-298
    • Caughey1    Lansbury, P.T.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.