메뉴 건너뛰기




Volumn 112, Issue 4, 2005, Pages 547-555

Microtubule-associated protein tau is a substrate of ATP/Mg 2+-dependent proteasome protease system

Author keywords

Alzheimer's disease; ATP; Proteasome; Tau; Ubiquitin

Indexed keywords

ADENOSINE TRIPHOSPHATE; BRAIN EXTRACT; DODECYL SULFATE SODIUM; EPITOPE; LACTACYSTIN; MAGNESIUM CHLORIDE; PROTEASOME; TAU PROTEIN;

EID: 17644416738     PISSN: 03009564     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00702-004-0196-x     Document Type: Article
Times cited : (63)

References (25)
  • 1
    • 0031030057 scopus 로고    scopus 로고
    • Processive degradation of proteins and other catalytic properties of the proteasome from Thermoplasma acidophilum
    • Akopian TN, Kisselev AF, Goldberg AL (1997) Processive degradation of proteins and other catalytic properties of the proteasome from Thermoplasma acidophilum. J Biol Chem 272: 1791-1798
    • (1997) J Biol Chem , vol.272 , pp. 1791-1798
    • Akopian, T.N.1    Kisselev, A.F.2    Goldberg, A.L.3
  • 2
    • 0029037696 scopus 로고
    • Bovine and human tau, highly homologous but less crossreactive: Implications for Alzheimer disease
    • Alonso Adel C, Grundke-Iqbal I, Iqbal K (1995) Bovine and human tau, highly homologous but less crossreactive: implications for Alzheimer disease. Brain Res Mol Brain Res 31(1-2): 194-200
    • (1995) Brain Res Mol Brain Res , vol.31 , Issue.1-2 , pp. 194-200
    • Alonso Adel, C.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 3
    • 0034680902 scopus 로고    scopus 로고
    • Role of protein phosphatase-2A and -1 in the regulation of GSK-3, cdk5 and cdc2 and the phosphorylation of tau in rat forebrain
    • Bennecib M, Gong CX, Grundke-Iqbal I, Iqbal K (2000) Role of protein phosphatase-2A and -1 in the regulation of GSK-3, cdk5 and cdc2 and the phosphorylation of tau in rat forebrain. FEBS Lett 485: 87-93
    • (2000) FEBS Lett , vol.485 , pp. 87-93
    • Bennecib, M.1    Gong, C.X.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 4
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer-related changes
    • Braak H, Braak E (1991) Neuropathological stageing of Alzheimer-related changes. Acta Neuropathol 82: 239-259
    • (1991) Acta Neuropathol , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 7
    • 0034528413 scopus 로고    scopus 로고
    • Tau gene mutations in frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17). Their relevance for understanding the neurodegenerative process
    • Goedert M, Ghetti B, Spillantini MG (2000) Tau gene mutations in frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17). Their relevance for understanding the neurodegenerative process. Ann NY Acad Sci 920: 74-78
    • (2000) Ann NY Acad Sci , vol.920 , pp. 74-78
    • Goedert, M.1    Ghetti, B.2    Spillantini, M.G.3
  • 9
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • Goldberg AL (2003) Protein degradation and protection against misfolded or damaged proteins. Nature 426: 895-899
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 12
    • 0032543684 scopus 로고    scopus 로고
    • Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17
    • Hutton M, Lendon CL, Rizzu P, et al. (1998) Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17. Nature 393: 702-705
    • (1998) Nature , vol.393 , pp. 702-705
    • Hutton, M.1    Lendon, C.L.2    Rizzu, P.3
  • 14
    • 0037381710 scopus 로고    scopus 로고
    • Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer's disease
    • Keck S, Nitsch R, Grune T, Ullrich O (2003) Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer's disease. J Neurochem 85: 115-122
    • (2003) J Neurochem , vol.85 , pp. 115-122
    • Keck, S.1    Nitsch, R.2    Grune, T.3    Ullrich, O.4
  • 15
    • 0034131044 scopus 로고    scopus 로고
    • Impaired proteasome function in Alzheimer's disease
    • Keller JN, Hanni KB, Markesbery WR (2000) Impaired proteasome function in Alzheimer's disease. J Neurochem 75: 436-439
    • (2000) J Neurochem , vol.75 , pp. 436-439
    • Keller, J.N.1    Hanni, K.B.2    Markesbery, W.R.3
  • 16
    • 0028013249 scopus 로고
    • Alzheimer disease: Correlation of cerebro-spinal fluid and brain ubiquitin levels
    • Kudo T, Iqbal K, Ravid R, Swaab DF, Grundke-Iqbal I (1994) Alzheimer disease: correlation of cerebro-spinal fluid and brain ubiquitin levels. Brain Res 639: 1-7
    • (1994) Brain Res , vol.639 , pp. 1-7
    • Kudo, T.1    Iqbal, K.2    Ravid, R.3    Swaab, D.F.4    Grundke-Iqbal, I.5
  • 18
    • 0037383052 scopus 로고    scopus 로고
    • Relationship between beta-amyloid degradation and the 26S proteasome in neural cells
    • Lopez Salon M, Pasquini L, Besio Moreno M, Pasquini JM, Soto E (2003) Relationship between beta-amyloid degradation and the 26S proteasome in neural cells. Exp Neurol 180: 131-143
    • (2003) Exp Neurol , vol.180 , pp. 131-143
    • Lopez Salon, M.1    Pasquini, L.2    Besio Moreno, M.3    Pasquini, J.M.4    Soto, E.5
  • 19
    • 0023140474 scopus 로고
    • Ubiquitin is a component of paired helical filaments in Alzheimer's disease
    • Mori H, Kondo J, Ihara Y (1987) Ubiquitin is a component of paired helical filaments in Alzheimer's disease. Science 235: 1641-1644
    • (1987) Science , vol.235 , pp. 1641-1644
    • Mori, H.1    Kondo, J.2    Ihara, Y.3
  • 20
    • 0027193036 scopus 로고
    • Ubiquitin is conjugated with amino-terminally processed tau in paired helical filaments
    • Morishima-Kawashima M, Hasegawa M, Takio K, Suzuki M, Titani K, Ihara Y (1993) Ubiquitin is conjugated with amino-terminally processed tau in paired helical filaments. Neuron 10: 1151-1160
    • (1993) Neuron , vol.10 , pp. 1151-1160
    • Morishima-Kawashima, M.1    Hasegawa, M.2    Takio, K.3    Suzuki, M.4    Titani, K.5    Ihara, Y.6
  • 21
    • 1042266624 scopus 로고    scopus 로고
    • CHIP-Hsc70 complex ubiquitinates phosphorylated Tau and enhances cell survival
    • Shimura H, Schwartz D, Gygi SP, Kosik KS (2004) CHIP-Hsc70 complex ubiquitinates phosphorylated Tau and enhances cell survival. J Biol Chem 279: 4869-4887
    • (2004) J Biol Chem , vol.279 , pp. 4869-4887
    • Shimura, H.1    Schwartz, D.2    Gygi, S.P.3    Kosik, K.S.4
  • 23
    • 0032146362 scopus 로고    scopus 로고
    • Mutations in RNA: A first example of molecular misreading in Alzheimer's disease
    • van Leeuwen FW, Burbach JP, Hol EM (1998) Mutations in RNA: a first example of molecular misreading in Alzheimer's disease. Trends Neurosci 21: 331-335
    • (1998) Trends Neurosci , vol.21 , pp. 331-335
    • Van Leeuwen, F.W.1    Burbach, J.P.2    Hol, E.M.3
  • 25
    • 0030867774 scopus 로고    scopus 로고
    • The ubiquitin system
    • Varshavsky A (1997) The ubiquitin system. Trends Biochem Sci 22: 383-387
    • (1997) Trends Biochem Sci , vol.22 , pp. 383-387
    • Varshavsky, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.