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Volumn 1252, Issue C, 2003, Pages 383-393

Heat shock proteins reduce aggregation and facilitate degradation of tau protein

Author keywords

Aggregation; Alzheimer's disease; Degradation; Heat shock proteins; Tau

Indexed keywords


EID: 42249112110     PISSN: 05315131     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0531-5131(03)00077-3     Document Type: Article
Times cited : (5)

References (18)
  • 1
    • 0033600274 scopus 로고    scopus 로고
    • Translating cell biology into therapeutic advances in Alzheimer's disease
    • D.J Selkoe Translating cell biology into therapeutic advances in Alzheimer's disease Nature 399 1999 A23 A31
    • (1999) Nature , vol.399 , pp. A23-A31
    • Selkoe, D.J1
  • 5
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • F.U Hartl Molecular chaperones in cellular protein folding Nature 381 1996 571 579
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U1
  • 6
    • 0035451646 scopus 로고    scopus 로고
    • Unfolding the role of chaperones and chaperonins in human disease
    • A.M Slavotinek L.G Biesecker Unfolding the role of chaperones and chaperonins in human disease Trends Genet. 17 2001 528 535
    • (2001) Trends Genet. , vol.17 , pp. 528-535
    • Slavotinek, A.M1    Biesecker, L.G2
  • 8
    • 0034662915 scopus 로고    scopus 로고
    • Bacterial and yeast chaperones reduce both aggregate formation and cell death in mammalian cell models of Huntington's disease
    • J Carmichael J Chatellier A Woolfson C Milstein A.R Fersht D.C Rubinsztein Bacterial and yeast chaperones reduce both aggregate formation and cell death in mammalian cell models of Huntington's disease Proc. Natl. Acad. Sci. U. S. A. 97 2000 9701 9705
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 9701-9705
    • Carmichael, J1    Chatellier, J2    Woolfson, A3    Milstein, C4    Fersht, A.R5    Rubinsztein, D.C6
  • 9
    • 0032727617 scopus 로고    scopus 로고
    • Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70
    • J.M Warrick H.Y Chan G.L Gray-Board Y Chai H.L Paulson N.M Bonini Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70 Nat. Genet. 23 1999 425 428
    • (1999) Nat. Genet. , vol.23 , pp. 425-428
    • Warrick, J.M1    Chan, H.Y2    Gray-Board, G.L3    Chai, Y4    Paulson, H.L5    Bonini, N.M6
  • 10
    • 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 H Lehrach M.K Hayer-Hartl F.U Hartl E.E Wanker Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease Hum. Mol. Genet. 10 2001 1307 1315
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1307-1315
    • Sittler, A1    Lurz, R2    Lueder, G3    Priller, J4    Lehrach, H5    Hayer-Hartl, M.K6    Hartl, F.U7    Wanker, E.E8
  • 11
    • 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 N.M Bonini Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease Science 295 2001 865 868
    • (2001) Science , vol.295 , pp. 865-868
    • Auluck, P.K1    Chan, H.Y2    Trojanowski, J.Q3    Lee, V.M4    Bonini, N.M5
  • 14
    • 0028785525 scopus 로고
    • Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain
    • R Brandt J Leger G Lee Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain J. Cell Biol. 131 1995 1327 1340
    • (1995) J. Cell Biol. , vol.131 , pp. 1327-1340
    • Brandt, R1    Leger, J2    Lee, G3
  • 15
    • 0035942736 scopus 로고    scopus 로고
    • Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells
    • S.M Elbashir J Harborth W Lendeckel A Yalcin K Weber T Tuschl Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells Nature 411 2001 494 498
    • (2001) Nature , vol.411 , pp. 494-498
    • Elbashir, S.M1    Harborth, J2    Lendeckel, W3    Yalcin, A4    Weber, K5    Tuschl, T6
  • 16
    • 0030913980 scopus 로고    scopus 로고
    • The ‘jaws’ model of tau-microtubule interaction examined in CHO cells
    • U Preuss J Biernat E.M Mandelkow E Mandelkow The ‘jaws’ model of tau-microtubule interaction examined in CHO cells J. Cell Sci. 110 1997 789 800
    • (1997) J. Cell Sci. , vol.110 , pp. 789-800
    • Preuss, U1    Biernat, J2    Mandelkow, E.M3    Mandelkow, E4
  • 17
    • 0027199869 scopus 로고
    • Prohormone processing in the trans-Golgi network: endoproteolytic cleavage of prosomatostatin and formation of nascent secretory vesicles in permeabilized cells
    • H Xu D Shields Prohormone processing in the trans -Golgi network: endoproteolytic cleavage of prosomatostatin and formation of nascent secretory vesicles in permeabilized cells J. Cell Biol. 122 1993 1169 1184
    • (1993) J. Cell Biol. , vol.122 , pp. 1169-1184
    • Xu, H1    Shields, D2
  • 18
    • 0032555685 scopus 로고    scopus 로고
    • Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1
    • J Zou Y Guo T Guettouche D.F Smith R Voellmy Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1 Cell 94 1998 471 480
    • (1998) Cell , vol.94 , pp. 471-480
    • Zou, J1    Guo, Y2    Guettouche, T3    Smith, D.F4    Voellmy, R5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.