메뉴 건너뛰기




Volumn 154, Issue 1, 1999, Pages 255-270

Transgenic expression of the shortest human tau affects its compartmentalization and its phosphorylation as in the pretangle stage of Alzheimer's disease

Author keywords

[No Author keywords available]

Indexed keywords

MICROTUBULE ASSOCIATED PROTEIN; TAU PROTEIN;

EID: 0345580607     PISSN: 00029440     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0002-9440(10)65272-8     Document Type: Article
Times cited : (174)

References (76)
  • 2
    • 0030905501 scopus 로고    scopus 로고
    • Normal and pathological tau proteins as factors for microtubule assembly
    • Delacourte A, Buée L: Normal and pathological tau proteins as factors for microtubule assembly. Int Rev Cytol 1997, 171:167-224
    • (1997) Int Rev Cytol , vol.171 , pp. 167-224
    • Delacourte, A.1    Buée, L.2
  • 3
    • 0021338217 scopus 로고
    • Phosphorylation affects the ability of tau protein to promote microtubule assembly
    • Lindwall G, Cole RD: Phosphorylation affects the ability of tau protein to promote microtubule assembly. J Biol Chem 1984, 259:5301-5306
    • (1984) J Biol Chem , vol.259 , pp. 5301-5306
    • Lindwall, G.1    Cole, R.D.2
  • 5
    • 0029994754 scopus 로고    scopus 로고
    • Phosphorylation of tau by glycogen synthase kinase-3β in intact mammalian cells: The effects on the organization and stability of microtubules
    • Lovestone S, Hartley CL, Pearce J, Anderton BH: Phosphorylation of tau by glycogen synthase kinase-3β in intact mammalian cells: the effects on the organization and stability of microtubules. Neuroscience 1996, 73:1145-1157
    • (1996) Neuroscience , vol.73 , pp. 1145-1157
    • Lovestone, S.1    Hartley, C.L.2    Pearce, J.3    Anderton, B.H.4
  • 6
    • 0022365608 scopus 로고
    • The distribution of tau in the mammalian central nervous system
    • Binder LI, Frankfurter A, Rebhun I: The distribution of tau in the mammalian central nervous system. J Cell Biol 1985, 101:1371-1378
    • (1985) J Cell Biol , vol.101 , pp. 1371-1378
    • Binder, L.I.1    Frankfurter, A.2    Rebhun, I.3
  • 7
    • 0023929799 scopus 로고
    • Both adult and juvenile tau microtubule-associated proteins are axon specific in the developing and adult rat cerebellum
    • Brion JP, Guilleminot J, Couchie D, Nunez J: Both adult and juvenile tau microtubule-associated proteins are axon specific in the developing and adult rat cerebellum. Neuroscience 1988, 25:139-146
    • (1988) Neuroscience , vol.25 , pp. 139-146
    • Brion, J.P.1    Guilleminot, J.2    Couchie, D.3    Nunez, J.4
  • 8
    • 0027195313 scopus 로고
    • Subcellular localization of tau mRNA in differentiating neuronal cell culture: Implications for neuronal polarity
    • Litman P, Barg J, Rindzoonski L, Ginzburg I: Subcellular localization of tau mRNA in differentiating neuronal cell culture: implications for neuronal polarity. Neuron 1993, 10:627-638
    • (1993) Neuron , vol.10 , pp. 627-638
    • Litman, P.1    Barg, J.2    Rindzoonski, L.3    Ginzburg, I.4
  • 9
    • 0028838142 scopus 로고
    • Sorting mechanisms of tau and MAP2 in neurons: Suppressed axonal transit of MAP2 and locally regulated microtubule binding
    • Kanai Y, Hirokawa N: Sorting mechanisms of tau and MAP2 in neurons: suppressed axonal transit of MAP2 and locally regulated microtubule binding. Neuron 1995, 14:421-432
    • (1995) Neuron , vol.14 , pp. 421-432
    • Kanai, Y.1    Hirokawa, N.2
  • 10
    • 0030028366 scopus 로고    scopus 로고
    • Selective stabilization of tau in axons and microtubule-associated protein 2C in cell bodies and dendrites contributes to polarized localization of cytoskeletal proteins in mature neurons
    • Hirokawa N, Funakoshi T, Sato-Harada R, Kanai Y: Selective stabilization of tau in axons and microtubule-associated protein 2C in cell bodies and dendrites contributes to polarized localization of cytoskeletal proteins in mature neurons. J Cell Biol 1996, 132:667-679
    • (1996) J Cell Biol , vol.132 , pp. 667-679
    • Hirokawa, N.1    Funakoshi, T.2    Sato-Harada, R.3    Kanai, Y.4
  • 11
    • 0028914641 scopus 로고
    • Cis-acting signals and trans-acting proteins are involved in tau mRNA targeting into neurites of differentiating neuronal cells
    • Behar L, Marx R, Sadot E, Barg J, Ginzburg I: cis-acting signals and trans-acting proteins are involved in tau mRNA targeting into neurites of differentiating neuronal cells. Int J Dev Neurosci 1995, 13:113-127
    • (1995) Int J Dev Neurosci , vol.13 , pp. 113-127
    • Behar, L.1    Marx, R.2    Sadot, E.3    Barg, J.4    Ginzburg, I.5
  • 12
    • 0023911326 scopus 로고
    • Light and electron microscope localization of the microtubule-associated tau protein in rat brain
    • Migheli A, Butler M, Brown K, Shelanski ML: Light and electron microscope localization of the microtubule-associated tau protein in rat brain. J Neurosci 1988, 8:1846-1851
    • (1988) J Neurosci , vol.8 , pp. 1846-1851
    • Migheli, A.1    Butler, M.2    Brown, K.3    Shelanski, M.L.4
  • 14
    • 0029790283 scopus 로고    scopus 로고
    • Neurodegenerative disorders with extensive tau pathology: A comparative study and review
    • Feany MB, Dickson DW: Neurodegenerative disorders with extensive tau pathology: a comparative study and review. Ann Neurol 1996, 40:139-148
    • (1996) Ann Neurol , vol.40 , pp. 139-148
    • Feany, M.B.1    Dickson, D.W.2
  • 15
    • 0022257253 scopus 로고
    • Mise en évidence immunologique de la protéine tau au niveau des lésions de dégénérescence neurofibrillaire de la maladie d'Alzheimer
    • Brion JP, Passareiro H, Nunez J, Flament-Durand J: Mise en évidence immunologique de la protéine tau au niveau des lésions de dégénérescence neurofibrillaire de la maladie d'Alzheimer. Arch Biol (Brux) 1985, 95:229-235
    • (1985) Arch Biol (Brux) , vol.95 , pp. 229-235
    • Brion, J.P.1    Passareiro, H.2    Nunez, J.3    Flament-Durand, J.4
  • 16
    • 0022980104 scopus 로고
    • Alzheimer's disease: Tau proteins, the promoting factors of microtubule assembly, are major components of paired helical filaments
    • Delacourte A, Defossez A: Alzheimer's disease: tau proteins, the promoting factors of microtubule assembly, are major components of paired helical filaments. J Neurol Sci 1986, 76:173-186
    • (1986) J Neurol Sci , vol.76 , pp. 173-186
    • Delacourte, A.1    Defossez, A.2
  • 18
    • 0009364134 scopus 로고
    • The microtubule-associated protein, tau, is a major antigenic component of paired helical filaments in Alzheimer's disease
    • Kosik KS, Joachim CL, Selkoe DJ: The microtubule-associated protein, tau, is a major antigenic component of paired helical filaments in Alzheimer's disease. Proc Natl Acad Sci USA 1986, 83:4044-4048
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 4044-4048
    • Kosik, K.S.1    Joachim, C.L.2    Selkoe, D.J.3
  • 20
    • 0040415446 scopus 로고    scopus 로고
    • Tau protein, and the neurofibrillary pathology of Alzheimer's disease
    • Edited by W Wasco, RE Tanzi. Totowa, New Jersey, Humana Press Inc
    • Goedert M, Trojanowski JQ, Lee VMY: Tau protein, and the neurofibrillary pathology of Alzheimer's disease. Molecular Mechanisms of Dementia. Edited by W Wasco, RE Tanzi. Totowa, New Jersey, Humana Press Inc, 1997, pp 199-218
    • (1997) Molecular Mechanisms of Dementia , pp. 199-218
    • Goedert, M.1    Trojanowski, J.Q.2    Lee, V.M.Y.3
  • 25
    • 0028362458 scopus 로고
    • A sequence of cytoskeleton changes related to the formation of neurofibrillary tangles and neuropil threads
    • Braak E, Braak H, Mandelkow E-M: A sequence of cytoskeleton changes related to the formation of neurofibrillary tangles and neuropil threads. Acta Neuropathol (Berl) 1994, 87:554-567
    • (1994) Acta Neuropathol (Berl) , vol.87 , pp. 554-567
    • Braak, E.1    Braak, H.2    Mandelkow, E.-M.3
  • 28
    • 0023277545 scopus 로고
    • Single step method of RNA isolation by acid guanidium thiocyanate-phenol-chloroform extraction
    • Chromczynski P, Sacchi N: Single step method of RNA isolation by acid guanidium thiocyanate-phenol-chloroform extraction. Anal Biochem 1987, 162:156-159
    • (1987) Anal Biochem , vol.162 , pp. 156-159
    • Chromczynski, P.1    Sacchi, N.2
  • 29
    • 0027984739 scopus 로고
    • Epitope mapping of monoclonal antibodies to the paired helical filaments of Alzheimer's disease: Identification of phosphorylation sites in tau protein
    • Goedert M, Jakes R, Crowther RA, Cohen P, Vanmechelen E, Vandermeeren M, Cras P: Epitope mapping of monoclonal antibodies to the paired helical filaments of Alzheimer's disease: identification of phosphorylation sites in tau protein. Biochem J 1994, 301:871-877
    • (1994) Biochem J , vol.301 , pp. 871-877
    • Goedert, M.1    Jakes, R.2    Crowther, R.A.3    Cohen, P.4    Vanmechelen, E.5    Vandermeeren, M.6    Cras, P.7
  • 30
    • 0026097837 scopus 로고
    • Tau in Alzheimer neurofibrillary tangles: N- and C-terminal regions are differentially associated with paired helical filaments and the location of a putative abnormal phosphorylation site
    • Brion JP, Hanger DP, Bruce MT, Couck AM, Flament-Durand J, Anderton BH: Tau in Alzheimer neurofibrillary tangles: N- and C-terminal regions are differentially associated with paired helical filaments and the location of a putative abnormal phosphorylation site. Biochem J 1991, 273:127-133
    • (1991) Biochem J , vol.273 , pp. 127-133
    • Brion, J.P.1    Hanger, D.P.2    Bruce, M.T.3    Couck, A.M.4    Flament-Durand, J.5    Anderton, B.H.6
  • 31
    • 0028946744 scopus 로고
    • Monoclonal antibody AT8 recognises tau protein phosphorylated at both serine 202 and threonine 205
    • Goedert M, Jakes R, Vanmechelen E: Monoclonal antibody AT8 recognises tau protein phosphorylated at both serine 202 and threonine 205. Neurosci Lett 1995, 189:167-170
    • (1995) Neurosci Lett , vol.189 , pp. 167-170
    • Goedert, M.1    Jakes, R.2    Vanmechelen, E.3
  • 32
    • 0030750558 scopus 로고    scopus 로고
    • Unique Alzheimer's disease paired helical filament specific epitopes involve double phosphorylation at specific sites
    • Hoffmann R, Lee VMY, Leight S, Varga I, Otvos L Jr.: Unique Alzheimer's disease paired helical filament specific epitopes involve double phosphorylation at specific sites. Biochemistry 1997, 36:8114-8124
    • (1997) Biochemistry , vol.36 , pp. 8114-8124
    • Hoffmann, R.1    Lee, V.M.Y.2    Leight, S.3    Varga, I.4    Otvos L., Jr.5
  • 33
    • 0028593606 scopus 로고
    • Monoclonal antibody PHF-1 recognizes tau protein phosphorylated at serine residues 396 and 404
    • Otvos L,Jr., Feiner L, Lang E, Szendrei GI, Goedert M, Lee VM-Y: Monoclonal antibody PHF-1 recognizes tau protein phosphorylated at serine residues 396 and 404. J Neurosci Res 1994, 39:669-673
    • (1994) J Neurosci Res , vol.39 , pp. 669-673
    • Otvos L., Jr.1    Feiner, L.2    Lang, E.3    Szendrei, G.I.4    Goedert, M.5    Lee, V.M.-Y.6
  • 36
    • 0029879046 scopus 로고    scopus 로고
    • Characterization of mAb AP422, a novel phosphorylation-dependent monoclonal antibody against tau protein
    • Hasegawa M, Jakes R, Crowther RA, Lee VMY, Ihara Y, Goedert M: Characterization of mAb AP422, a novel phosphorylation-dependent monoclonal antibody against tau protein. FEBS Lett 1996, 384:25-30
    • (1996) FEBS Lett , vol.384 , pp. 25-30
    • Hasegawa, M.1    Jakes, R.2    Crowther, R.A.3    Lee, V.M.Y.4    Ihara, Y.5    Goedert, M.6
  • 37
    • 0030783142 scopus 로고    scopus 로고
    • A conformation-, and phosphorylation-dependent antibody recognizing the paired helical filaments of Alzheimer's disease
    • Jicha GA, Lane E, Vincent I, Otvos L Jr, Hoffmann R, Davies P: A conformation-, and phosphorylation-dependent antibody recognizing the paired helical filaments of Alzheimer's disease. J Neurochem 1997, 69:2087-2095
    • (1997) J Neurochem , vol.69 , pp. 2087-2095
    • Jicha, G.A.1    Lane, E.2    Vincent, I.3    Otvos L., Jr.4    Hoffmann, R.5    Davies, P.6
  • 38
    • 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
  • 39
    • 0030936599 scopus 로고    scopus 로고
    • Alz-50 and MC-1, a new monoclonal antibody raised to paired helical filaments, recognize conformational epitopes on recombinant tau
    • Jicha GA, Bowser R, Kazam IG, Davies P: Alz-50 and MC-1, a new monoclonal antibody raised to paired helical filaments, recognize conformational epitopes on recombinant tau. J Neurosci Res 1997, 48:128-132
    • (1997) J Neurosci Res , vol.48 , pp. 128-132
    • Jicha, G.A.1    Bowser, R.2    Kazam, I.G.3    Davies, P.4
  • 41
    • 0026058252 scopus 로고
    • Synaptophysin and chromogranin A immunoreactivities in senile plaques of Alzheimer's disease
    • Brion JP, Couck AM, Bruce M, Anderton BH, Flament-Durand J: Synaptophysin and chromogranin A immunoreactivities in senile plaques of Alzheimer's disease. Brain Res 1991, 539:143-150
    • (1991) Brain Res , vol.539 , pp. 143-150
    • Brion, J.P.1    Couck, A.M.2    Bruce, M.3    Anderton, B.H.4    Flament-Durand, J.5
  • 43
    • 0024415926 scopus 로고
    • A ubiquitous mammalian expression vector, pHMG, based on a housekeeping gene promoter
    • Gautier C, Mehtali M, Lathe R: A ubiquitous mammalian expression vector, pHMG, based on a housekeeping gene promoter. Nucleic Acids Res 1989, 17:8389
    • (1989) Nucleic Acids Res , vol.17 , pp. 8389
    • Gautier, C.1    Mehtali, M.2    Lathe, R.3
  • 45
    • 0023905288 scopus 로고
    • The primary structure and heterogeneity of tau protein from mouse brain
    • Lee G, Cowan N, Kirschner M: The primary structure and heterogeneity of tau protein from mouse brain. Science 1988, 239:285-288
    • (1988) Science , vol.239 , pp. 285-288
    • Lee, G.1    Cowan, N.2    Kirschner, M.3
  • 46
    • 0028965635 scopus 로고
    • Somatodendritic localization and hyperphosphorylation of tau protein in transgenic mice expressing the longest human brain tau isoform
    • Götz J, Probst A, Spillantini MG, Schäfer T, Jakes R, Bürki K, Goedert M: Somatodendritic localization and hyperphosphorylation of tau protein in transgenic mice expressing the longest human brain tau isoform. EMBO J 1995, 14:1304-1313
    • (1995) EMBO J , vol.14 , pp. 1304-1313
    • Götz, J.1    Probst, A.2    Spillantini, M.G.3    Schäfer, T.4    Jakes, R.5    Bürki, K.6    Goedert, M.7
  • 47
    • 0026495920 scopus 로고
    • Heterogeneity of Tau proteins during mouse brain development and differentiation of cultured neurons
    • Larcher JC, Boucher D, Ginzburg I, Gros F, Denoulet P: Heterogeneity of Tau proteins during mouse brain development and differentiation of cultured neurons. Dev Biol 1992, 154:195-204
    • (1992) Dev Biol , vol.154 , pp. 195-204
    • Larcher, J.C.1    Boucher, D.2    Ginzburg, I.3    Gros, F.4    Denoulet, P.5
  • 48
    • 0026786976 scopus 로고
    • Expression and phosphorylation of a three-repeat isoform of tau in transfected non-neuronal cells
    • Gallo J-M, Hanger DP, Twist EC, Kosik KS, Anderton BH: Expression and phosphorylation of a three-repeat isoform of tau in transfected non-neuronal cells. Biochem J 1992, 286:399-404
    • (1992) Biochem J , vol.286 , pp. 399-404
    • Gallo, J.-M.1    Hanger, D.P.2    Twist, E.C.3    Kosik, K.S.4    Anderton, B.H.5
  • 49
    • 0029018840 scopus 로고
    • The role of tau phosphorylation in transfected COS-1 cells
    • Medina M, De Garcini EM, Avila J: The role of tau phosphorylation in transfected COS-1 cells. Mol Cell Biochem 1995, 148:79-88
    • (1995) Mol Cell Biochem , vol.148 , pp. 79-88
    • Medina, M.1    De Garcini, E.M.2    Avila, J.3
  • 50
    • 0026487365 scopus 로고
    • Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: Generation of paired helical filaments epitopes and neuronal localization of the kinase
    • Hanger DP, Hughes K, Woodgett JR, Brion JP, Anderton BH: Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: generation of paired helical filaments epitopes and neuronal localization of the kinase. Neurosci Lett 1992, 147:58-62
    • (1992) Neurosci Lett , vol.147 , pp. 58-62
    • Hanger, D.P.1    Hughes, K.2    Woodgett, J.R.3    Brion, J.P.4    Anderton, B.H.5
  • 52
    • 0025856776 scopus 로고
    • A serine/threonine proline kinase activity is included in the tau protein kinase fraction forming a paired helical filament epitope
    • Ishiguro K, Omori A, Sato K, Tomizawa K, Imahori K, Uchida T: A serine/threonine proline kinase activity is included in the tau protein kinase fraction forming a paired helical filament epitope. Neurosci Lett 1991, 128:195-198
    • (1991) Neurosci Lett , vol.128 , pp. 195-198
    • Ishiguro, K.1    Omori, A.2    Sato, K.3    Tomizawa, K.4    Imahori, K.5    Uchida, T.6
  • 53
    • 0028143773 scopus 로고
    • Distribution of the phosphorylated microtubule-associated protein tau in developing cortical neurons
    • Brion JP, Octave JN, Couck AM: Distribution of the phosphorylated microtubule-associated protein tau in developing cortical neurons. Neuroscience 1994, 63:895-909
    • (1994) Neuroscience , vol.63 , pp. 895-909
    • Brion, J.P.1    Octave, J.N.2    Couck, A.M.3
  • 54
    • 0024438227 scopus 로고
    • Expression of multiple tau isoforms and microtubule bundle formation in fibroblasts translected with a single tau cDNA
    • Kanai Y, Takemura R, Oshima T, Mori H, Ihara Y, Yanagisawa M, Masaki T, Kirokawa N: Expression of multiple tau isoforms and microtubule bundle formation in fibroblasts translected with a single tau cDNA. J Cell Biol 1989, 109:1173-1184
    • (1989) J Cell Biol , vol.109 , pp. 1173-1184
    • Kanai, Y.1    Takemura, R.2    Oshima, T.3    Mori, H.4    Ihara, Y.5    Yanagisawa, M.6    Masaki, T.7    Kirokawa, N.8
  • 55
    • 0025785076 scopus 로고
    • Identification of 3- and 4-repeat tau isoforms within the PHF in Alzheimer's disease
    • Jakes R, Novak M, Davison M, Wischik CM: Identification of 3- and 4-repeat tau isoforms within the PHF in Alzheimer's disease. EMBO J 1991, 10:2725-2729
    • (1991) EMBO J , vol.10 , pp. 2725-2729
    • Jakes, R.1    Novak, M.2    Davison, M.3    Wischik, C.M.4
  • 56
    • 0024523426 scopus 로고
    • A distinct form of tau is selectively incorporated into Alzheimer's paired helical filaments
    • Mori H, Hamada Y, Kawaguchi M, Honda T, Kondo J, Ihara Y: A distinct form of tau is selectively incorporated into Alzheimer's paired helical filaments. Biochem Biophys Res Commun 1989, 159: 1221-1226
    • (1989) Biochem Biophys Res Commun , vol.159 , pp. 1221-1226
    • Mori, H.1    Hamada, Y.2    Kawaguchi, M.3    Honda, T.4    Kondo, J.5    Ihara, Y.6
  • 57
    • 0026501888 scopus 로고
    • Hydrofluoric acid-treated τ-phf proteins display the same biochemical properties as normal τ
    • Greenberg SG, Davies P, Schein JD, Binder LI: Hydrofluoric acid-treated τ-phf proteins display the same biochemical properties as normal τ. J Biol Chem 1992, 267:564-569
    • (1992) J Biol Chem , vol.267 , pp. 564-569
    • Greenberg, S.G.1    Davies, P.2    Schein, J.D.3    Binder, L.I.4
  • 58
    • 0030838124 scopus 로고    scopus 로고
    • Identification of microtubule-associated protein tau isoforms in Alzheimer's paired helical filaments
    • McLaughlin L, Zemlan FP. Dean GE: Identification of microtubule-associated protein tau isoforms in Alzheimer's paired helical filaments. Brain Res Bull 1997, 43:501-508
    • (1997) Brain Res Bull , vol.43 , pp. 501-508
    • McLaughlin, L.1    Zemlan, F.P.2    Dean, G.E.3
  • 59
    • 0026755755 scopus 로고
    • Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro
    • Wille H, Drewes G, Biernat J, Mandelkow E-M, Mandelkow E: Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro. J Cell Biol 1992, 118:573-584
    • (1992) J Cell Biol , vol.118 , pp. 573-584
    • Wille, H.1    Drewes, G.2    Biernat, J.3    Mandelkow, E.-M.4    Mandelkow, E.5
  • 60
    • 0029907548 scopus 로고    scopus 로고
    • Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans
    • Goedert M, Jakes R, Spillantini MG, Hasegawa M, Smith MJ, Crowther RA: Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans. Nature 1996, 383:550-553
    • (1996) Nature , vol.383 , pp. 550-553
    • Goedert, M.1    Jakes, R.2    Spillantini, M.G.3    Hasegawa, M.4    Smith, M.J.5    Crowther, R.A.6
  • 61
    • 0030590911 scopus 로고    scopus 로고
    • RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments
    • Kampers T, Friedhoff P, Biernat J, Mandelkow EM: RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments. FEBS Lett 1996, 399:344-349
    • (1996) FEBS Lett , vol.399 , pp. 344-349
    • Kampers, T.1    Friedhoff, P.2    Biernat, J.3    Mandelkow, E.M.4
  • 62
    • 0026787130 scopus 로고
    • Protein sequence and mass spectrometric analyses of tau in the Alzheimer's disease brain
    • Hasegawa M, Morishima-Kawashima M, Takio K, Suzuki M, Titani K, Ihara Y: Protein sequence and mass spectrometric analyses of tau in the Alzheimer's disease brain. J Biol Chem 1992, 267:17047-17054
    • (1992) J Biol Chem , vol.267 , pp. 17047-17054
    • Hasegawa, M.1    Morishima-Kawashima, M.2    Takio, K.3    Suzuki, M.4    Titani, K.5    Ihara, Y.6
  • 63
    • 0027338266 scopus 로고
    • 262 strongly reduces binding of tau to microtubules: Distinction between PHF-like immunoreactivity and microtubule binding
    • 262 strongly reduces binding of tau to microtubules: distinction between PHF-like immunoreactivity and microtubule binding. Neuron 1993, 11:153-163
    • (1993) Neuron , vol.11 , pp. 153-163
    • Biernat, J.1    Gustke, N.2    Drewes, G.3    Mandelkow, E.-M.4    Mandelkow, E.5
  • 64
    • 0027945346 scopus 로고
    • Biopsy-derived adult human brain tau is phosphorylated at many of the same sites as Alzheimer's disease paired helical filament tau
    • Matsuo ES, Shin R-W, Billingsley ML, Van DeVoorde A, O'Connor M, Trojanowski JQ, Lee VM-Y: Biopsy-derived adult human brain tau is phosphorylated at many of the same sites as Alzheimer's disease paired helical filament tau. Neuron 1994, 13:989-1002
    • (1994) Neuron , vol.13 , pp. 989-1002
    • Matsuo, E.S.1    Shin, R.-W.2    Billingsley, M.L.3    Van DeVoorde, A.4    O'Connor, M.5    Trojanowski, J.Q.6    Lee, V.M.-Y.7
  • 66
    • 0026700385 scopus 로고
    • Glial fibrillary tangles with straight tubules in the brains of patients with progressive supranuclear palsy
    • Nishimura M, Namba Y, Ikeda K, Oda M: Glial fibrillary tangles with straight tubules in the brains of patients with progressive supranuclear palsy. Neurosci Lett 1992, 143:35-38
    • (1992) Neurosci Lett , vol.143 , pp. 35-38
    • Nishimura, M.1    Namba, Y.2    Ikeda, K.3    Oda, M.4
  • 67
    • 0029057678 scopus 로고
    • Paired helical filaments and straight tubules in astrocytes: An electron microscopic study in dementia of the Alzheimer type
    • Yamazaki M, Nakano I, Imazu O, Terashi A: Paired helical filaments and straight tubules in astrocytes: an electron microscopic study in dementia of the Alzheimer type. Acta Neuropathol (Berlin) 1995, 90:31-36
    • (1995) Acta Neuropathol (Berlin) , vol.90 , pp. 31-36
    • Yamazaki, M.1    Nakano, I.2    Imazu, O.3    Terashi, A.4
  • 68
    • 0030887854 scopus 로고    scopus 로고
    • Familial multiple system tauopathy with presenile dementia: A disease with abundant neuronal and glial tau filaments
    • Spillantini MG, Goedert M, Crowther RA, Murrell JR, Farlow MR, Ghetti B: Familial multiple system tauopathy with presenile dementia: a disease with abundant neuronal and glial tau filaments. Proc Natl Acad Sci USA 1997, 94:4113-4118
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4113-4118
    • Spillantini, M.G.1    Goedert, M.2    Crowther, R.A.3    Murrell, J.R.4    Farlow, M.R.5    Ghetti, B.6
  • 69
    • 0024592795 scopus 로고
    • Tau protein immunoreactivity in dementia of the Alzheimer type: II. Electron microscopy and pathogenetic implications
    • Papasozomenos SC: Tau protein immunoreactivity in dementia of the Alzheimer type: II. Electron microscopy and pathogenetic implications. Lab Invest 1989, 60:375-389
    • (1989) Lab Invest , vol.60 , pp. 375-389
    • Papasozomenos, S.C.1
  • 70
    • 0029058568 scopus 로고
    • Ultrastructure of neurofibrillary tangles in the cerebral cortex of sheep
    • Nelson PT, Saper CB: Ultrastructure of neurofibrillary tangles in the cerebral cortex of sheep. Neurobiol Aging 1995, 16:315-323
    • (1995) Neurobiol Aging , vol.16 , pp. 315-323
    • Nelson, P.T.1    Saper, C.B.2
  • 71
    • 0030894830 scopus 로고    scopus 로고
    • Human tau becomes phosphorylated and forms filamentous deposits when overexpressed in lamprey central neurons in situ
    • Hall GF, Yao J, Lee G: Human tau becomes phosphorylated and forms filamentous deposits when overexpressed in lamprey central neurons in situ. Proc Natl Acad Sci USA 1997, 94:4733-4738
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4733-4738
    • Hall, G.F.1    Yao, J.2    Lee, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.