메뉴 건너뛰기




Volumn 2006, Issue , 2006, Pages

Tau phosphorylation, aggregation, and cell toxicity

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN; ATAXIN 1; ATAXIN 3; HUNTINGTIN; NEUROFILAMENT PROTEIN; PRION PROTEIN; TAU PROTEIN;

EID: 33646083011     PISSN: 11107243     EISSN: 11107251     Source Type: Journal    
DOI: 10.1155/JBB/2006/74539     Document Type: Review
Times cited : (51)

References (57)
  • 1
    • 0035902194 scopus 로고    scopus 로고
    • Shattuck lecture - Neurodegenerative diseases and prions
    • 11357156
    • S B Prusiner Shattuck lecture - neurodegenerative diseases and prions. The New England Journal of Medicine 344 2001 20 1516 1526 11357156
    • (2001) The New England Journal of Medicine , vol.344 , Issue.20 , pp. 1516-1526
    • Prusiner, S.B.1
  • 2
    • 0037018932 scopus 로고    scopus 로고
    • Alpha-helix structure in Alzheimer's disease aggregates of tau-protein
    • 12033949
    • M Sadqi F Hernández U Pan Alpha-helix structure in Alzheimer's disease aggregates of tau-protein. Biochemistry 41 2002 22 7150 7155 12033949
    • (2002) Biochemistry , vol.41 , Issue.22 , pp. 7150-7155
    • Sadqi, M.1    Hernández, F.2    Pan, U.3
  • 3
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • 15483602
    • M Arrasate S Mitra E S Schweitzer M R Segal S Finkbeiner Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 431 2004 7010 805 810 15483602
    • (2004) Nature , vol.431 , Issue.7010 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 4
    • 21544465581 scopus 로고    scopus 로고
    • An alternative interpretation of the amyloid Abeta hypothesis with regard to the pathogenesis of Alzheimer's disease
    • 15967987
    • V T Marchesi An alternative interpretation of the amyloid Abeta hypothesis with regard to the pathogenesis of Alzheimer's disease. Proceedings of the National Academy of Sciences of the United States of America 102 2005 26 9093 9098 15967987
    • (2005) Proceedings of the National Academy of Sciences of the United States of America , vol.102 , Issue.26 , pp. 9093-9098
    • Marchesi, V.T.1
  • 5
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • 11375494
    • N F Bence R M Sampat R R Kopito Impairment of the ubiquitin-proteasome system by protein aggregation. Science 292 2001 5521 1552 1555 11375494
    • (2001) Science , vol.292 , Issue.5521 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 7
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • 15272267
    • C A Ross M A Poirier Protein aggregation and neurodegenerative disease. Nature Medicine 10 2004 suppl S10 S17 15272267
    • (2004) Nature Medicine , vol.10
    • Ross, C.A.1    Poirier, M.A.2
  • 8
    • 1642289188 scopus 로고    scopus 로고
    • Role of tau protein in both physiological and pathological conditions
    • 15044677
    • J Avila J J Lucas M Pérez F Hernández Role of tau protein in both physiological and pathological conditions. Physiological Reviews 84 2004 2 361 384 15044677
    • (2004) Physiological Reviews , vol.84 , Issue.2 , pp. 361-384
    • Avila, J.1    Lucas, J.J.2    Pérez, M.3    Hernández, F.4
  • 9
    • 0026799198 scopus 로고
    • The microtubule binding repeats of tau protein assemble into filaments like those found in Alzheimer's disease
    • 1505683
    • R A Crowther O F Olesen R Jakes M Goedert The microtubule binding repeats of tau protein assemble into filaments like those found in Alzheimer's disease. FEBS Letters 309 1992 2 199 202 1505683
    • (1992) FEBS Letters , vol.309 , Issue.2 , pp. 199-202
    • Crowther, R.A.1    Olesen, O.F.2    Jakes, R.3    Goedert, M.4
  • 10
    • 0022917474 scopus 로고
    • Self assembly of microtubule associated protein tau into filaments resembling those found in Alzheimer disease
    • 3099793
    • E Montejo de Garcini L Serrano J Avila Self assembly of microtubule associated protein tau into filaments resembling those found in Alzheimer disease. Biochemical and Biophysical Research Communications 141 1986 2 790 796 3099793
    • (1986) Biochemical and Biophysical Research Communications , vol.141 , Issue.2 , pp. 790-796
    • Montejo De Garcini, E.1    Serrano, L.2    Avila, J.3
  • 11
    • 0029796168 scopus 로고    scopus 로고
    • Polymerization of tau into filaments in the presence of heparin: The minimal sequence required for tau-tau interaction
    • 8752125
    • M Pérez J M Valpuesta M Medina E Montejo de Garcini J Avila Polymerization of tau into filaments in the presence of heparin: the minimal sequence required for tau-tau interaction. Journal of Neurochemistry 67 1996 3 1183 1190 8752125
    • (1996) Journal of Neurochemistry , vol.67 , Issue.3 , pp. 1183-1190
    • Pérez, M.1    Valpuesta, J.M.2    Medina, M.3    Montejo De Garcini, E.4    Avila, J.5
  • 12
    • 0026755755 scopus 로고
    • Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro
    • 1639844
    • H Wille G Drewes J Biernat E M Mandelkow E Mandelkow Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro. The Journal of Cell Biology 118 1992 3 573 584 1639844
    • (1992) The Journal of Cell Biology , vol.118 , Issue.3 , pp. 573-584
    • Wille, H.1    Drewes, G.2    Biernat, J.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 14
    • 20444486153 scopus 로고    scopus 로고
    • TATA-binding protein in neurodegenerative disease
    • 15916858
    • W M van Roon-Mom S J Reid R L Faull R G Snell TATA-binding protein in neurodegenerative disease. Neuroscience 133 2005 4 863 872 15916858
    • (2005) Neuroscience , vol.133 , Issue.4 , pp. 863-872
    • Van Roon-Mom, W.M.1    Reid, S.J.2    Faull, R.L.3    Snell, R.G.4
  • 16
    • 24144440041 scopus 로고    scopus 로고
    • In vivo evidence of CHIP up-regulation attenuating tau aggregation
    • 16111477
    • N Sahara M Murayama T Mizoroki In vivo evidence of CHIP up-regulation attenuating tau aggregation. Journal of Neurochemistry 94 2005 5 1254 1263 16111477
    • (2005) Journal of Neurochemistry , vol.94 , Issue.5 , pp. 1254-1263
    • Sahara, N.1    Murayama, M.2    Mizoroki, T.3
  • 18
    • 1042266624 scopus 로고    scopus 로고
    • CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival
    • 14612456
    • H Shimura D Schwartz S P Gygi K S Kosik CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival. The Journal of Biological Chemistry 279 2004 6 4869 4876 14612456
    • (2004) The Journal of Biological Chemistry , vol.279 , Issue.6 , pp. 4869-4876
    • Shimura, H.1    Schwartz, D.2    Gygi, S.P.3    Kosik, K.S.4
  • 19
    • 4444370179 scopus 로고    scopus 로고
    • How does parkin ligate ubiquitin to Parkinson's disease?
    • 15229644
    • P J Kahle C Haass How does parkin ligate ubiquitin to Parkinson's disease? EMBO Reports 5 2004 7 681 685 15229644
    • (2004) EMBO Reports , vol.5 , Issue.7 , pp. 681-685
    • Kahle, P.J.1    Haass, C.2
  • 20
  • 21
    • 0037465354 scopus 로고    scopus 로고
    • Tau polymerization: Role of the amino terminus
    • 12590615
    • T C Gamblin R W Berry L I Binder Tau polymerization: role of the amino terminus. Biochemistry 42 2003 7 2252 2257 12590615
    • (2003) Biochemistry , vol.42 , Issue.7 , pp. 2252-2257
    • Gamblin, T.C.1    Berry, R.W.2    Binder, L.I.3
  • 22
    • 0347594304 scopus 로고    scopus 로고
    • Modeling tau polymerization in vitro: A review and synthesis
    • 14690409
    • T C Gamblin R W Berry L I Binder Modeling tau polymerization in vitro: a review and synthesis. Biochemistry 42 2003 51 15009 15017 14690409
    • (2003) Biochemistry , vol.42 , Issue.51 , pp. 15009-15017
    • Gamblin, T.C.1    Berry, R.W.2    Binder, L.I.3
  • 23
    • 0034705192 scopus 로고    scopus 로고
    • In vitro polymerization of tau protein monitored by laser light scattering: Method and application to the study of FTDP-17 mutants
    • 10821687
    • T C Gamblin M E King H Dawson In vitro polymerization of tau protein monitored by laser light scattering: method and application to the study of FTDP-17 mutants. Biochemistry 39 2000 20 6136 6144 10821687
    • (2000) Biochemistry , vol.39 , Issue.20 , pp. 6136-6144
    • Gamblin, T.C.1    King, M.E.2    Dawson, H.3
  • 24
    • 0034700253 scopus 로고    scopus 로고
    • Oxidative regulation of fatty acid-induced tau polymerization
    • 11087369
    • T C Gamblin M E King J Kuret R W Berry L I Binder Oxidative regulation of fatty acid-induced tau polymerization. Biochemistry 39 2000 46 14203 14210 11087369
    • (2000) Biochemistry , vol.39 , Issue.46 , pp. 14203-14210
    • Gamblin, T.C.1    King, M.E.2    Kuret, J.3    Berry, R.W.4    Binder, L.I.5
  • 26
    • 0028065142 scopus 로고
    • Analysis of microtubule-associated protein tau glycation in paired helical filaments
    • 8063802
    • M D Ledesma P Bonay C Colaço J Avila Analysis of microtubule-associated protein tau glycation in paired helical filaments. The Journal of Biological Chemistry 269 1994 34 21614 21619 8063802
    • (1994) The Journal of Biological Chemistry , vol.269 , Issue.34 , pp. 21614-21619
    • Ledesma, M.D.1    Bonay, P.2    Colaço, C.3    Avila, J.4
  • 28
    • 0343831898 scopus 로고    scopus 로고
    • In vitro assembly of tau protein: Mapping the regions involved in filament formation
    • 11352733
    • M Pérez M Arrasate E Montejo de Garcini V Munoz J Avila In vitro assembly of tau protein: mapping the regions involved in filament formation. Biochemistry 40 2001 20 5983 5991 11352733
    • (2001) Biochemistry , vol.40 , Issue.20 , pp. 5983-5991
    • Pérez, M.1    Arrasate, M.2    Montejo De Garcini, E.3    Munoz, V.4    Avila, J.5
  • 29
    • 12144289142 scopus 로고    scopus 로고
    • Quinones facilitate the self-assembly of the phosphorylated tubulin binding region of tau into fibrillar polymers
    • 15005624
    • I Santa-María F Hernández C P Martin J Avila F J Moreno Quinones facilitate the self-assembly of the phosphorylated tubulin binding region of tau into fibrillar polymers. Biochemistry 43 2004 10 2888 2897 15005624
    • (2004) Biochemistry , vol.43 , Issue.10 , pp. 2888-2897
    • Santa-María, I.1    Hernández, F.2    Martin, C.P.3    Avila, J.4    Moreno, F.J.5
  • 30
  • 31
    • 0242720372 scopus 로고    scopus 로고
    • Chronic lithium treatment decreases mutant tau protein aggregation in a transgenic mouse model
    • 14624025
    • M Pérez F Hernández F Lim J Diaz-Nido J Avila Chronic lithium treatment decreases mutant tau protein aggregation in a transgenic mouse model. Journal of Alzheimer's Disease 5 2003 4 301 308 14624025
    • (2003) Journal of Alzheimer's Disease , vol.5 , Issue.4 , pp. 301-308
    • Pérez, M.1    Hernández, F.2    Lim, F.3    Diaz-Nido, J.4    Avila, J.5
  • 33
    • 23844434232 scopus 로고    scopus 로고
    • Untangling memory deficits
    • 16079873
    • K Duff E Planel Untangling memory deficits. Nature Medicine 11 2005 8 826 827 16079873
    • (2005) Nature Medicine , vol.11 , Issue.8 , pp. 826-827
    • Duff, K.1    Planel, E.2
  • 35
    • 1242337344 scopus 로고    scopus 로고
    • Zeta 14-3-3 protein favours the formation of human tau fibrillar polymers
    • 15036595
    • F Hernández R Cuadros J Avila Zeta 14-3-3 protein favours the formation of human tau fibrillar polymers. Neuroscience Letters 357 2004 2 143 146 15036595
    • (2004) Neuroscience Letters , vol.357 , Issue.2 , pp. 143-146
    • Hernández, F.1    Cuadros, R.2    Avila, J.3
  • 37
    • 0033600242 scopus 로고    scopus 로고
    • The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein
    • 10391244
    • P J Lu G Wulf X Z Zhou P Davies K P Lu The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein. Nature 399 1999 6738 784 788 10391244
    • (1999) Nature , vol.399 , Issue.6738 , pp. 784-788
    • Lu, P.J.1    Wulf, G.2    Zhou, X.Z.3    Davies, P.4    Lu, K.P.5
  • 38
    • 24144434063 scopus 로고    scopus 로고
    • DNA sequence variations in the prolyl isomerase Pin1 gene and Alzheimer's disease
    • 16095818
    • M Poli L B Gatta R Dominici DNA sequence variations in the prolyl isomerase Pin1 gene and Alzheimer's disease. Neuroscience Letters 389 2005 2 66 70 16095818
    • (2005) Neuroscience Letters , vol.389 , Issue.2 , pp. 66-70
    • Poli, M.1    Gatta, L.B.2    Dominici, R.3
  • 40
    • 10944256690 scopus 로고    scopus 로고
    • Inability of tau to properly regulate neuronal microtubule dynamics: A loss-of-function mechanism by which tau might mediate neuronal cell death
    • 15615645
    • S C Feinstein L Wilson Inability of tau to properly regulate neuronal microtubule dynamics: a loss-of-function mechanism by which tau might mediate neuronal cell death. Biochimica et Biophysica Acta 1739 2005 2-3 268 279 15615645
    • (2005) Biochimica et Biophysica Acta , vol.1739 , Issue.2-3 , pp. 268-279
    • Feinstein, S.C.1    Wilson, L.2
  • 41
    • 0033788787 scopus 로고    scopus 로고
    • Reduced binding of protein phosphatase 2A to tau protein with frontotemporal dementia and parkinsonism linked to chromosome 17 mutations
    • 11032905
    • M Goedert S Satumtira R Jakes Reduced binding of protein phosphatase 2A to tau protein with frontotemporal dementia and parkinsonism linked to chromosome 17 mutations. Journal of Neurochemistry 75 2000 5 2155 2162 11032905
    • (2000) Journal of Neurochemistry , vol.75 , Issue.5 , pp. 2155-2162
    • Goedert, M.1    Satumtira, S.2    Jakes, R.3
  • 42
    • 10944241542 scopus 로고    scopus 로고
    • Tau alteration and neuronal degeneration in tauopathies: Mechanisms and models
    • 15615650
    • R Brandt M Hundelt N Shahani Tau alteration and neuronal degeneration in tauopathies: mechanisms and models. Biochimica et Biophysica Acta 1739 2005 2-3 331 354 15615650
    • (2005) Biochimica et Biophysica Acta , vol.1739 , Issue.2-3 , pp. 331-354
    • Brandt, R.1    Hundelt, M.2    Shahani, N.3
  • 43
    • 20044367108 scopus 로고    scopus 로고
    • Cell-cycle reentry and cell death in transgenic mice expressing nonmutant human tau isoforms
    • 15930395
    • C Andorfer C M Acker Y Kress P R Hof K Duff P Davies Cell-cycle reentry and cell death in transgenic mice expressing nonmutant human tau isoforms. The Journal of Neuroscience 25 2005 22 5446 5454 15930395
    • (2005) The Journal of Neuroscience , vol.25 , Issue.22 , pp. 5446-5454
    • Andorfer, C.1    Acker, C.M.2    Kress, Y.3    Hof, P.R.4    Duff, K.5    Davies, P.6
  • 44
    • 17044435830 scopus 로고    scopus 로고
    • Tau phosphorylation in Alzheimer's disease: Pathogen or protector?
    • 15823754
    • H G Lee G Perry P I Moreira Tau phosphorylation in Alzheimer's disease: pathogen or protector? Trends in Molecular Medicine 11 2005 4 164 169 15823754
    • (2005) Trends in Molecular Medicine , vol.11 , Issue.4 , pp. 164-169
    • Lee, H.G.1    Perry, G.2    Moreira, P.I.3
  • 45
    • 0026740795 scopus 로고
    • Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease
    • 1549228
    • P V Arriagada J H Growdon E T Hedley-Whyte B T Hyman Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease. Neurology 42 1992 3 pt 1 631 639 1549228
    • (1992) Neurology , vol.42 , Issue.31 , pp. 631-639
    • Arriagada, P.V.1    Growdon, J.H.2    Hedley-Whyte, E.T.3    Hyman, B.T.4
  • 46
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer-related changes
    • 1759558
    • H Braak E Braak Neuropathological stageing of Alzheimer-related changes. Acta Neuropathologica (Berl) 82 1991 4 239 259 1759558
    • (1991) Acta Neuropathologica (Berl) , vol.82 , Issue.4 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 48
    • 0028918383 scopus 로고
    • Extracellular neurofibrillary tangles reflect neuronal loss and provide further evidence of extensive protein cross-linking in Alzheimer disease
    • 7610759
    • P Cras M A Smith P L Richey S L Siedlak P Mulvihill G Perry Extracellular neurofibrillary tangles reflect neuronal loss and provide further evidence of extensive protein cross-linking in Alzheimer disease. Acta Neuropathologica (Berl) 89 1995 4 291 295 7610759
    • (1995) Acta Neuropathologica (Berl) , vol.89 , Issue.4 , pp. 291-295
    • Cras, P.1    Smith, M.A.2    Richey, P.L.3    Siedlak, S.L.4    Mulvihill, P.5    Perry, G.6
  • 49
    • 0028864025 scopus 로고
    • Neurons, intracellular and extracellular neurofibrillary tangles in subdivisions of the hippocampal cortex in normal ageing and Alzheimer's disease
    • 8584267
    • Y Fukutani K Kobayashi I Nakamura K Watanabe K Isaki N J Cairns Neurons, intracellular and extracellular neurofibrillary tangles in subdivisions of the hippocampal cortex in normal ageing and Alzheimer's disease. Neuroscience Letters 200 1995 1 57 60 8584267
    • (1995) Neuroscience Letters , vol.200 , Issue.1 , pp. 57-60
    • Fukutani, Y.1    Kobayashi, K.2    Nakamura, I.3    Watanabe, K.4    Isaki, K.5    Cairns, N.J.6
  • 50
    • 0024804051 scopus 로고
    • Neurofibrillary degeneration and neuronal loss in Alzheimer's disease
    • 2628782
    • W Bondareff C Q Mountjoy M Roth D L Hauser Neurofibrillary degeneration and neuronal loss in Alzheimer's disease. Neurobiology of Aging 10 1989 6 709 715 2628782
    • (1989) Neurobiology of Aging , vol.10 , Issue.6 , pp. 709-715
    • Bondareff, W.1    Mountjoy, C.Q.2    Roth, M.3    Hauser, D.L.4
  • 51
    • 0033614777 scopus 로고    scopus 로고
    • Filamentous nerve cell inclusions in neurodegenerative diseases: Tauopathies and alpha-synucleinopathies
    • 10434313
    • M Goedert Filamentous nerve cell inclusions in neurodegenerative diseases: tauopathies and alpha-synucleinopathies. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences 354 1999 1386 1101 1118 10434313
    • (1999) Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences , vol.354 , Issue.1386 , pp. 1101-1118
    • Goedert, M.1
  • 53
    • 22344438508 scopus 로고    scopus 로고
    • Tau suppression in a neurodegenerative mouse model improves memory function
    • 16020737
    • K Santacruz J Lewis T Spires Tau suppression in a neurodegenerative mouse model improves memory function. Science 309 2005 5733 476 481 16020737
    • (2005) Science , vol.309 , Issue.5733 , pp. 476-481
    • Santacruz, K.1    Lewis, J.2    Spires, T.3
  • 54
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • 12704221
    • B Caughey P T Lansbury Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annual Review of Neuroscience 26 2003 267 298 12704221
    • (2003) Annual Review of Neuroscience , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 55
    • 0032897924 scopus 로고    scopus 로고
    • A clinical pathological comparison of three families with frontotemporal dementia and identical mutations in the tau gene (P301L)
    • 10219785
    • T D Bird D Nochlin P Poorkaj A clinical pathological comparison of three families with frontotemporal dementia and identical mutations in the tau gene (P301L). Brain 122 1999 pt 4 741 756 10219785
    • (1999) Brain , vol.122 , Issue.4 , pp. 741-756
    • Bird, T.D.1    Nochlin, D.2    Poorkaj, P.3
  • 56
    • 0032894121 scopus 로고    scopus 로고
    • The biochemical pathway of neurofibrillary degeneration in aging and Alzheimer's disease
    • 10214737
    • A Delacourte J P David N Sergeant The biochemical pathway of neurofibrillary degeneration in aging and Alzheimer's disease. Neurology 52 1999 6 1158 1165 10214737
    • (1999) Neurology , vol.52 , Issue.6 , pp. 1158-1165
    • Delacourte, A.1    David, J.P.2    Sergeant, N.3
  • 57
    • 0344653664 scopus 로고    scopus 로고
    • Neuronal loss correlates with but exceeds neurofibrillary tangles in Alzheimer's disease
    • 9005861
    • T Gomez-Isla R Hollister H West Neuronal loss correlates with but exceeds neurofibrillary tangles in Alzheimer's disease. Annals of Neurology 41 1997 1 17 24 9005861
    • (1997) Annals of Neurology , vol.41 , Issue.1 , pp. 17-24
    • Gomez-Isla, T.1    Hollister, R.2    West, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.