메뉴 건너뛰기




Volumn 161, Issue 5, 2002, Pages 1711-1722

Tau Assembly in inducible transfectants expressing wild-type or FTDP-17 tau

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; SODIUM CHLORIDE; TAU PROTEIN; TYLOXAPOL;

EID: 0036841609     PISSN: 00029440     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0002-9440(10)64448-3     Document Type: Article
Times cited : (58)

References (41)
  • 1
    • 0034081234 scopus 로고    scopus 로고
    • Tau gene mutations in frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17)
    • Spillantini MG, Van Swieten JC, Goedert M: Tau gene mutations in frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17). Neurogenetics 2000, 2:193-205
    • (2000) Neurogenetics , vol.2 , pp. 193-205
    • Spillantini, M.G.1    Van Swieten, J.C.2    Goedert, M.3
  • 2
    • 0034640005 scopus 로고    scopus 로고
    • Untangling tau-related dementia
    • Heutink P: Untangling tau-related dementia. Hum Mol Genet 2000, 9:979-986
    • (2000) Hum Mol Genet , vol.9 , pp. 979-986
    • Heutink, P.1
  • 8
    • 0035808361 scopus 로고    scopus 로고
    • Tau filament formation in transgenic mice expressing P301L tau
    • Gotz J, Chen F, Barmettler R, Nitsch RM: Tau filament formation in transgenic mice expressing P301L tau. J Biol Chem 2000, 276:529-534
    • (2000) J Biol Chem , vol.276 , pp. 529-534
    • Gotz, J.1    Chen, F.2    Barmettler, R.3    Nitsch, R.M.4
  • 12
    • 0035254160 scopus 로고    scopus 로고
    • Mutated tau binds less avidly to microtubules than wildtype tau in living cells
    • Nagiec EW, Sampson KE, Abraham I: Mutated tau binds less avidly to microtubules than wildtype tau in living cells. J Neurosci Res 2001, 63:268-275
    • (2001) J Neurosci Res , vol.63 , pp. 268-275
    • Nagiec, E.W.1    Sampson, K.E.2    Abraham, I.3
  • 13
    • 0033011181 scopus 로고    scopus 로고
    • Accelerated filament formation from tau protein with specific FTDP-17 missense mutations
    • Nacharaju P, Lewis J, Easson C, Yen S, Hackett J, Hutton M, Yen SH: Accelerated filament formation from tau protein with specific FTDP-17 missense mutations. FEBS Lett 1999, 447:195-199
    • (1999) FEBS Lett , vol.447 , pp. 195-199
    • Nacharaju, P.1    Lewis, J.2    Easson, C.3    Yen, S.4    Hackett, J.5    Hutton, M.6    Yen, S.H.7
  • 14
    • 0032919462 scopus 로고    scopus 로고
    • Effects of frontotemporal dementia FTDP-17 mutations on heparin-induced assembly of tau filaments
    • Goedert M, Jakes R, Crowther RA: Effects of frontotemporal dementia FTDP-17 mutations on heparin-induced assembly of tau filaments. FEBS Lett 1999, 450:306-311
    • (1999) FEBS Lett , vol.450 , pp. 306-311
    • Goedert, M.1    Jakes, R.2    Crowther, R.A.3
  • 15
    • 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
    • Gamblin TC, King ME, Dawson H, Vitek MP, Kuret J, Berry RW, Binder LI: In vitro polymerization of tau protein monitored by laser light scattering: Method and application to the study of FTDP-17 mutants. Biochemistry 2000, 39:6136-6144
    • (2000) Biochemistry , vol.39 , pp. 6136-6144
    • Gamblin, T.C.1    King, M.E.2    Dawson, H.3    Vitek, M.P.4    Kuret, J.5    Berry, R.W.6    Binder, L.I.7
  • 17
    • 0029999787 scopus 로고    scopus 로고
    • Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules
    • Alonso AC, Grundke-Iqbal, Iqbal K: Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules. Nat Med 1996, 2:783-787
    • (1996) Nat Med , vol.2 , pp. 783-787
    • Alonso, A.C.1    Grundke-Iqbal2    Iqbal, K.3
  • 18
    • 0031012497 scopus 로고    scopus 로고
    • Abnormal phosphorylation of tau and the mechanism of Alzheimer neurofibrillary degeneration: Sequestration of microtubule-associated proteins 1 and 2 and the disassembly of microtubules by the abnormal tau
    • Alonso A, Grundke-Iqbal I, Barra HS, Iqbal K: Abnormal phosphorylation of tau and the mechanism of Alzheimer neurofibrillary degeneration: Sequestration of microtubule-associated proteins 1 and 2 and the disassembly of microtubules by the abnormal tau. Proc Nat Acad Sci USA 1997, 94:298-303
    • (1997) Proc Nat Acad Sci USA , vol.94 , pp. 298-303
    • Alonso, A.1    Grundke-Iqbal, I.2    Barra, H.S.3    Iqbal, K.4
  • 19
    • 0035937481 scopus 로고    scopus 로고
    • Effects of FTDP-17 mutations on the in vitro phosphorylation of tau by glycogen synthase kinase 3beta identified by mass spectrometry demonstrate certain mutations exert long-range conformational changes
    • Connell JW, Gibb GM, Betts JC, Blackstock WP, Gallo J, Lovestone S, Hutton M, Anderton BH: Effects of FTDP-17 mutations on the in vitro phosphorylation of tau by glycogen synthase kinase 3beta identified by mass spectrometry demonstrate certain mutations exert long-range conformational changes. FEBS Lett 2001, 493:40-44
    • (2001) FEBS Lett , vol.493 , pp. 40-44
    • Connell, J.W.1    Gibb, G.M.2    Betts, J.C.3    Blackstock, W.P.4    Gallo, J.5    Lovestone, S.6    Hutton, M.7    Anderton, B.H.8
  • 21
    • 0342368837 scopus 로고    scopus 로고
    • The FTDP-17-linked mutation R406W abolishes the interaction of phosphorylated tau with microtubules
    • Perez M, Lim F, Arrasate M, Avila J: The FTDP-17-linked mutation R406W abolishes the interaction of phosphorylated tau with microtubules. J Neurochem 2000, 74:2583-2589
    • (2000) J Neurochem , vol.74 , pp. 2583-2589
    • Perez, M.1    Lim, F.2    Arrasate, M.3    Avila, J.4
  • 22
    • 0034193290 scopus 로고    scopus 로고
    • Missense point mutations of tau to segregate with FTDP-17 exhibit site-specific effects on microtubule structure in COS cells: A novel action of R406W mutation
    • Sahara N, Tomiyama T, Mor HJ: Missense point mutations of tau to segregate with FTDP-17 exhibit site-specific effects on microtubule structure in COS cells: A novel action of R406W mutation. J Neurosci Res 2000, 60:380-387
    • (2000) J Neurosci Res , vol.60 , pp. 380-387
    • Sahara, N.1    Tomiyama, T.2    Mor, H.J.3
  • 23
    • 0032782662 scopus 로고    scopus 로고
    • Abnormal microtubule packing in processes of SF9 cells expressing the FTDP-17 V337M tau mutation
    • Frappier T, Liang NS, Brown K, Leung CL, Lynch T, Liem RK, Shelanski ML: Abnormal microtubule packing in processes of SF9 cells expressing the FTDP-17 V337M tau mutation. FEBS Lett 1999, 455: 262-266
    • (1999) FEBS Lett , vol.455 , pp. 262-266
    • Frappier, T.1    Liang, N.S.2    Brown, K.3    Leung, C.L.4    Lynch, T.5    Liem, R.K.6    Shelanski, M.L.7
  • 24
    • 0033055359 scopus 로고    scopus 로고
    • Stable expression in Chinese hamster ovary cells of mutated tau genes causing frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17)
    • Matsumura N, Yamazaki T, Ihara Y: Stable expression in Chinese hamster ovary cells of mutated tau genes causing frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17). Am J Pathol 1999, 154:1649-1656
    • (1999) Am J Pathol , vol.154 , pp. 1649-1656
    • Matsumura, N.1    Yamazaki, T.2    Ihara, Y.3
  • 25
    • 0036118882 scopus 로고    scopus 로고
    • Formation of aberrant phosphotau fibrillar polymers in neural cultured cells
    • Perez M, Hernandez F. Gomez-Ramos A, Smith M, Perry G, Avila J: Formation of aberrant phosphotau fibrillar polymers in neural cultured cells. FEBS Lett 2002, 269:1484-1489
    • (2002) FEBS Lett , vol.269 , pp. 1484-1489
    • Perez, M.1    Hernandez, F.2    Gomez-Ramos, A.3    Smith, M.4    Perry, G.5    Avila, J.6
  • 26
    • 0032833626 scopus 로고    scopus 로고
    • Neuropathologic differentiation of progressive supranuclear palsy and corticobasal degeneration
    • Dickson DW: Neuropathologic differentiation of progressive supranuclear palsy and corticobasal degeneration. J Neurol 1999, 246:6-15
    • (1999) J Neurol , vol.246 , pp. 6-15
    • Dickson, D.W.1
  • 27
    • 0030774852 scopus 로고    scopus 로고
    • Degradation of tau by lysosomal enzyme cathepsin D: Implication for Alzheimer neurofibrillary degeneration
    • Kenessey A, Nacharaju P, Ko LW, Yen SH: Degradation of tau by lysosomal enzyme cathepsin D: implication for Alzheimer neurofibrillary degeneration J Neurochem 1997, 69:2026-2038
    • (1997) J Neurochem , vol.69 , pp. 2026-2038
    • Kenessey, A.1    Nacharaju, P.2    Ko, L.W.3    Yen, S.H.4
  • 28
    • 0019365666 scopus 로고
    • Antibodies to neurofilament glial filament and fibroblast intermediate filament proteins to different cell types of the nervous system
    • Yen SH, Fields KL: Antibodies to neurofilament glial filament and fibroblast intermediate filament proteins to different cell types of the nervous system. J Cell Biol 1981, 88:115-126
    • (1981) J Cell Biol , vol.88 , pp. 115-126
    • Yen, S.H.1    Fields, K.L.2
  • 29
    • 0029114196 scopus 로고
    • Oxidation of cysteine-322 in the repeat domain of microtubule-associated protein tau controls the in vitro assembly of paired helical filaments
    • Schweers O, Mandelkow EM, Biernat J, Mandelkow E: Oxidation of cysteine-322 in the repeat domain of microtubule-associated protein tau controls the in vitro assembly of paired helical filaments. Proc Natl Acad Sci USA 1995, 92:8463-8467
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8463-8467
    • Schweers, O.1    Mandelkow, E.M.2    Biernat, J.3    Mandelkow, E.4
  • 31
  • 34
    • 0033558929 scopus 로고    scopus 로고
    • Sequence requirements for formation of conformational variants of tau similar to those found in Alzheimer's disease
    • Jicha GA, Berenfeld B, Davies P: Sequence requirements for formation of conformational variants of tau similar to those found in Alzheimer's disease. J Neurosci Res 1999, 55:713-723
    • (1999) J Neurosci Res , vol.55 , pp. 713-723
    • Jicha, G.A.1    Berenfeld, B.2    Davies, P.3
  • 35
    • 0034254722 scopus 로고    scopus 로고
    • Role of phosphorylation in the conformation of tau peptides implicated in Alzheimer's disease
    • Daly NL, Hoffmann R, Otvos Jr L, Craik DJ: Role of phosphorylation in the conformation of tau peptides implicated in Alzheimer's disease. Biochemistry 2000, 39:9039-9046
    • (2000) Biochemistry , vol.39 , pp. 9039-9046
    • Daly, N.L.1    Hoffmann, R.2    Otvos L., Jr.3    Craik, D.J.4
  • 36
    • 12644260802 scopus 로고    scopus 로고
    • The structural basis of monoclonal antibody Alz50's selectivity for Alzheimer's disease pathology
    • Carmel G, Mager EM, Binder LI, Kuret J: The structural basis of monoclonal antibody Alz50's selectivity for Alzheimer's disease pathology. J Biol Chem 1996, 271:32789-32795
    • (1996) J Biol Chem , vol.271 , pp. 32789-32795
    • Carmel, G.1    Mager, E.M.2    Binder, L.I.3    Kuret, J.4
  • 37
  • 39
    • 0032561415 scopus 로고    scopus 로고
    • FTDP-17 mutations N279K and S305N in tau produce increased splicing of exon 10
    • Hasegawa M, Smith MJ, Goedert M: FTDP-17 mutations N279K and S305N in tau produce increased splicing of exon 10. FEBS Lett 1998, 437:207-210
    • (1998) FEBS Lett , vol.437 , pp. 207-210
    • Hasegawa, M.1    Smith, M.J.2    Goedert, M.3
  • 41
    • 0035181835 scopus 로고    scopus 로고
    • Competition for microtubule-binding with dual expression of tau missense and splice isoforms
    • Lu M, Kosik KS: Competition for microtubule-binding with dual expression of tau missense and splice isoforms. Mol Biol Cell 2001, 12:171-184
    • (2001) Mol Biol Cell , vol.12 , pp. 171-184
    • Lu, M.1    Kosik, K.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.