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Volumn 171, Issue , 1997, Pages 167-224

Normal and pathological Tau proteins as factors for microtubule assembly

Author keywords

Alzheimer's disease; Corticobasal degeneration; MAPs; Microtubules; Neurofibrillary degeneration; PHF; Phosphorylation; Pick disease; Tau proteins

Indexed keywords

MICROTUBULE ASSOCIATED PROTEIN; PHOSPHATASE; PROTEIN KINASE; TAU PROTEIN; TUBULIN; UBIQUITIN;

EID: 0030905501     PISSN: 00747696     EISSN: None     Source Type: Book Series    
DOI: 10.1016/s0074-7696(08)62588-7     Document Type: Review
Times cited : (111)

References (268)
  • 1
    • 0021681351 scopus 로고
    • Microtubule-associated proteins connect microtubules and neurofilaments in vitro
    • Aamodt, E. J., and Williams, R. C, Jr. (1984). Microtubule-associated proteins connect microtubules and neurofilaments in vitro. Biochemistry 23, 6023-6031.
    • (1984) Biochemistry , vol.23 , pp. 6023-6031
    • Aamodt, E.J.1    Williams Jr., R.C.2
  • 2
    • 0344296880 scopus 로고
    • Unusual argyrophilic glial cells in progressive supranuclear palsy
    • Abe, H., Yagishita, S., and Amano, N. (1994). Unusual argyrophilic glial cells in progressive supranuclear palsy. Neiirodegeneration 3, 85-90.
    • (1994) Neiirodegeneration , vol.3 , pp. 85-90
    • Abe, H.1    Yagishita, S.2    Amano, N.3
  • 4
    • 0028227962 scopus 로고
    • Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer's disease
    • Alonso, A. D., Zaidi, T., Grundke-Iqbal, I., and Iqbal, K. (1994). Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer's disease. Proc. Nail. Acad. Sei. USA 91, 5562-5566.
    • (1994) Proc. Nail. Acad. Sei. USA , vol.91 , pp. 5562-5566
    • Alonso, A.D.1    Zaidi, T.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 5
    • 0026488111 scopus 로고
    • Structure and novel exons of the human-Tau gene
    • Andreadis, A., Brown, W. M., and Kosik, K. S. (1992). Structure and novel exons of the human-Tau gene. Biochemistry 31, 10626-10633.
    • (1992) Biochemistry , vol.31 , pp. 10626-10633
    • Andreadis, A.1    Brown, W.M.2    Kosik, K.S.3
  • 6
    • 0029078383 scopus 로고
    • Relative exon affinities and suboptimal splice site signals lead to non-equivalence of two cassette exon
    • Andreadis, A., Broderick, J. A., and Kosik, K. S. (1995). Relative exon affinities and suboptimal splice site signals lead to non-equivalence of two cassette exon. Nucleic Acids Res. 23,3585-3593.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 3585-3593
    • Andreadis, A.1    Broderick, J.A.2    Kosik, K.S.3
  • 8
    • 0029066704 scopus 로고
    • Increased expression and subcellular translocation of the mitogen activated protein kinase kinase and mitogen-activated protein kinase in Alzheimer's disease
    • Arendt, T., Holzer, M., Grossmann, A., Zedlick, D., and Bruckner, M. K. (1995). Increased expression and subcellular translocation of the mitogen activated protein kinase kinase and mitogen-activated protein kinase in Alzheimer's disease. Acta Psychiatr. Scand. 68, 5-18.
    • (1995) Acta Psychiatr. Scand. , vol.68 , pp. 5-18
    • Arendt, T.1    Holzer, M.2    Grossmann, A.3    Zedlick, D.4    Bruckner, M.K.5
  • 10
    • 0028246491 scopus 로고
    • Twisted tubulofilaments of inclusion body myositis muscle resemble paired helical filaments of Alzheimer brain and contain hyperphosphorylated tau
    • Askanas, V., Engel, W. K., Bilak, M., Alvarez, R. B., and Selkoe, D. J. (1994). Twisted tubulofilaments of inclusion body myositis muscle resemble paired helical filaments of Alzheimer brain and contain hyperphosphorylated tau. Am. J. Palhol. 144, 177-187.
    • (1994) Am. J. Palhol. , vol.144 , pp. 177-187
    • Askanas, V.1    Engel, W.K.2    Bilak, M.3    Alvarez, R.B.4    Selkoe, D.J.5
  • 12
    • 0023630392 scopus 로고
    • Phosphorylation of Tau proteins to a state like that in Alzheimer's brain is catalyzed by a calcium/calmodulin-dependent kinase and modulated by phospholipids
    • Baudier, J., and Cole, R. D (1987). Phosphorylation of Tau proteins to a state like that in Alzheimer's brain is catalyzed by a calcium/calmodulin-dependent kinase and modulated by phospholipids. J. BioL Chem. 262, 17577-17583.
    • (1987) J. BioL Chem. , vol.262 , pp. 17577-17583
    • Baudier, J.1    Cole, R.D.2
  • 13
    • 0028879044 scopus 로고
    • Overexpressed Tau protein in cultured cells is phosphorylated without formation of PHF: Implication of phosphoprotein phosphatase involvement
    • Baum, L., Seger, R., Woodgett, J. R., Kawabata, S., Maruyama, K., Koyama, M., Silver, J., and Saitoh, T. (1995). Overexpressed Tau protein in cultured cells is phosphorylated without formation of PHF: Implication of phosphoprotein phosphatase involvement. Mol. Brain Res. 34, 1-17.
    • (1995) Mol. Brain Res. , vol.34 , pp. 1-17
    • Baum, L.1    Seger, R.2    Woodgett, J.R.3    Kawabata, S.4    Maruyama, K.5    Koyama, M.6    Silver, J.7    Saitoh, T.8
  • 14
    • 0027757042 scopus 로고
    • Abnormal Alzheimer-like phosphorylation of Tau-protein by cyclin-dependent kinases cdk2 and cdk5
    • Baumann, K., Mandelkow, E. M., Biernat, J., et al. (1993). Abnormal Alzheimer-like phosphorylation of Tau-protein by cyclin-dependent kinases cdk2 and cdk5. FEES Lett. 336,417-424.
    • (1993) FEES Lett. , vol.336 , pp. 417-424
    • Baumann, K.1    Mandelkow, E.M.2    Biernat, J.3
  • 15
    • 0028914641 scopus 로고
    • Tau mRNA targeting into neuntes of differentiating neuronal cells
    • Behar, L., Marx, R., Sadot, E., Barg, J., and Ginzburg, I. (1995). cis-acting signals and transacting proteins are involved in Tau mRNA targeting into neuntes of differentiating neuronal cells. Int. J. Dev. Neurosd. 13, 113-127.
    • (1995) Int. J. Dev. Neurosd. , vol.13 , pp. 113-127
    • Behar, L.1    Marx, R.2    Sadot, E.3    Barg, J.4    Ginzburg, I.5
  • 16
    • 0029032732 scopus 로고
    • Apolipoprotein E immunoreactivity within neurofibrillary tangles: Relationship to Tau and PHF in Alzheimer's disease
    • Benzing, W. C., and Mufson, E. J. (1995). Apolipoprotein E immunoreactivity within neurofibrillary tangles: Relationship to Tau and PHF in Alzheimer's disease. Exp. Neural. 132, 162-171.
    • (1995) Exp. Neural. , vol.132 , pp. 162-171
    • Benzing, W.C.1    Mufson, E.J.2
  • 17
    • 0027338266 scopus 로고
    • Phosphorylation of ser(262) strongly reduces binding of Tau-protein to microtubules-Distinction between PHF-like immunoreactivity and microtubule binding
    • Biernat, J., Gustke, N., Drewes, G., Mandelkow, E. M., and Mandelkow, E. (1993). Phosphorylation of ser(262) strongly reduces binding of Tau-protein to microtubules-Distinction between PHF-like immunoreactivity and microtubule binding. Neuron 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
  • 18
    • 0022365608 scopus 로고
    • The distribution of Tau in the mammalian central nervous system
    • Binder, L. I., Frankfurter, A., and Rebhun, L. (1985). The distribution of Tau in the mammalian central nervous system. J. Cell Biol. 101, 1371-1378.
    • (1985) J. Cell Biol. , vol.101 , pp. 1371-1378
    • Binder, L.I.1    Frankfurter, A.2    Rebhun, L.3
  • 19
  • 20
    • 0028110393 scopus 로고
    • Polyglutamylation of tubulin as a progressive regulator of in vitro interaction between the microtubule-associated protein Tau and tubulin
    • Boucher, D., Larcher, J. C., Gros, F., and Denoulet, P. (1994). Polyglutamylation of tubulin as a progressive regulator of in vitro interaction between the microtubule-associated protein Tau and tubulin. Biochemistry 33, 12471-12477.
    • (1994) Biochemistry , vol.33 , pp. 12471-12477
    • Boucher, D.1    Larcher, J.C.2    Gros, F.3    Denoulet, P.4
  • 21
    • 0028213511 scopus 로고
    • Regional distribution of neurofibrillary tangles and senile plaques in the cerebral cortex of elderly patients - A quantitative evaluation of a one-year-autopsy population from a geriatric hospital
    • Bouras, C, Hof, P. R., Giannakopoulos, P., Michel, J. P., and Morrison, J. H. (1994). Regional distribution of neurofibrillary tangles and senile plaques in the cerebral cortex of elderly patients - A quantitative evaluation of a one-year-autopsy population from a geriatric hospital. Cerebral Cortex 4, 138-150.
    • (1994) Cerebral Cortex , vol.4 , pp. 138-150
    • Bouras, C.1    Hof, P.R.2    Giannakopoulos, P.3    Michel, J.P.4    Morrison, J.H.5
  • 22
    • 0028982504 scopus 로고
    • Distribution of Big Tau in the central nervous system of the adult and developing rat
    • Boyne, L. J., Tessler, A., Murray, M., and Fischer, I. (1995). Distribution of Big Tau in the central nervous system of the adult and developing rat. J. Camp. Neural. 358, 279-293.
    • (1995) J. Camp. Neural. , vol.358 , pp. 279-293
    • Boyne, L.J.1    Tessler, A.2    Murray, M.3    Fischer, I.4
  • 23
    • 0023912552 scopus 로고
    • Neuropil threads occur in dendrites of tangle-bearing nerve cells
    • Braak, H., and Braak, E. (1988). Neuropil threads occur in dendrites of tangle-bearing nerve cells. Neuropathol. Appl. Neural. 14, 39-43.
    • (1988) Neuropathol. Appl. Neural. , vol.14 , pp. 39-43
    • Braak, H.1    Braak, E.2
  • 24
    • 0022595501 scopus 로고
    • Occurrence of neuropils threads in the senile human brain and in Alzheimer's disease
    • Braak, H., and Braak, E., Grundke-Iqbal, I., and Iqbal, K. (1988). Occurrence of neuropils threads in the senile human brain and in Alzheimer's disease. A 3rd location of paired helical filaments outside of neurofibrillary tangles and neuritic plaques. Neurosd. Lett. 65, 351-355.
    • (1988) A , vol.65 , pp. 351-355
    • Braak, H.1    Braak, E.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 25
    • 0029013727 scopus 로고
    • Staging of Alzheimer's disease-related neurofibrillary changes
    • Braak, H., and Braak, E. (1995). Staging of Alzheimer's disease-related neurofibrillary changes. Neurobiol. Aging 16, 271-278.
    • (1995) Neurobiol. Aging , vol.16 , pp. 271-278
    • Braak, H.1    Braak, E.2
  • 26
    • 0028210962 scopus 로고
    • Abnormally phosphorylated Tau protein related to the formation of neurofibrillary tangles and neuropil threads in the cerebral cortex of sheep and goat
    • Braak, H., Braak, E., and Strothjohann, M. (1994). Abnormally phosphorylated Tau protein related to the formation of neurofibrillary tangles and neuropil threads in the cerebral cortex of sheep and goat. Neurosd. Lett. 171,1-4.
    • (1994) Neurosd. Lett. , vol.171 , pp. 1-4
    • Braak, H.1    Braak, E.2    Strothjohann, M.3
  • 27
    • 0029040690 scopus 로고
    • Presence of Tau in isolated nuclei from human brain
    • Brady, R. M., Zinkowski, R. P., and Binder, L. I. (1995). Presence of Tau in isolated nuclei from human brain. Neurobiol. Aging 16, 479-486.
    • (1995) Neurobiol. Aging , vol.16 , pp. 479-486
    • Brady, R.M.1    Zinkowski, R.P.2    Binder, L.I.3
  • 28
    • 0027308924 scopus 로고
    • Abnormal Tau-phosphorylation at ser(396) in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding
    • Bramblett, G. T., Goedert, M., Jakes, R., Merrick, S. E., Trojanowski, J. Q., and Lee, V. M. Y. (1993). Abnormal Tau-phosphorylation at ser(396) in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding. Neuron 10,1089-1099.
    • (1993) Neuron , vol.10 , pp. 1089-1099
    • Bramblett, G.T.1    Goedert, M.2    Jakes, R.3    Merrick, S.E.4    Trojanowski, J.Q.5    Lee, V.M.Y.6
  • 29
    • 0028785525 scopus 로고
    • Interaction of Tau with the neural plasma membrane mediated by tau's amino-terminal projection domain
    • Brandt, R., Leger, J., and Lee, G. (1995). Interaction of Tau with the neural plasma membrane mediated by tau's amino-terminal projection domain. J. Cell Biol. 131,1327-1340.
    • (1995) J. Cell Biol. , vol.131 , pp. 1327-1340
    • Brandt, R.1    Leger, J.2    Lee, G.3
  • 30
    • 0022257253 scopus 로고
    • Immunological detection of Tau protein in neurofibrillary tangles of Alzheimer's disease
    • Brion, J. P., Passareiro, H., Nunez, J., and Flament-Durand, J. (1985). Immunological detection of Tau protein in neurofibrillary tangles of Alzheimer's disease. Arch. Biol. 95, 229-235.
    • (1985) Arch. Biol. , vol.95 , pp. 229-235
    • Brion, J.P.1    Passareiro, H.2    Nunez, J.3    Flament-Durand, J.4
  • 31
    • 5244352593 scopus 로고
    • Recent findings in Pick's disease
    • Brion, S., and Mikol, J. (1973). Recent findings in Pick's disease. Prog. Neuropathol. 2, 421.
    • (1973) Prog. Neuropathol. , vol.2 , pp. 421
    • Brion, S.1    Mikol, J.2
  • 34
    • 33645880213 scopus 로고
    • Tau pathology in neurodegenerative disorders: Biochemical analysis
    • Buée-Scherrer, V., Buée, L., Vermersch, P., et al. (1994). Tau pathology in neurodegenerative disorders: Biochemical analysis. Soc. Neurosci. Abstr. 20,1647.
    • (1994) Soc. Neurosci. Abstr. , vol.20 , pp. 1647
    • Buée-Scherrer, V.1    Buée, L.2    Vermersch, P.3
  • 35
    • 0028957084 scopus 로고
    • Neurofibrillary degeneration in amyotrophic lateral sclerosis/ parkinsonism-dementia complex of Guam-Immunochemical characterization of Tau proteins
    • Buée-Scherrer, V., Buée, L., Hof, P. R., Leveugle, B., Gilles, C, Loerzel, A. J., Perl, D. P., and Delacourte, A. (1995). Neurofibrillary degeneration in amyotrophic lateral sclerosis/ parkinsonism-dementia complex of Guam-Immunochemical characterization of Tau proteins. Am. J. Pathol. 146, 924-932.
    • (1995) Am. J. Pathol. , vol.146 , pp. 924-932
    • Buée-Scherrer, V.1    Buée, L.2    Hof, P.R.3    Leveugle, B.4    Gilles, C.5    Loerzel, A.J.6    Perl, D.P.7    Delacourte, A.8
  • 38
    • 33645880533 scopus 로고    scopus 로고
    • Pathological tau proteins in postencephalitic parkinsonism: Similarities and differences with Alzheimer's disease and other neurode-generative disorders
    • Buée-Scherrer, V., Buée, L., Perl, D. P., et al. (1996c). Pathological tau proteins in postencephalitic parkinsonism: Similarities and differences with Alzheimer's disease and other neurode-generative disorders. Submitted for publication.
    • (1996) Submitted for Publication.
    • Buée-Scherrer, V.1    Buée, L.2    Perl, D.P.3
  • 40
    • 0028986916 scopus 로고
    • Amyloid fibrils induce Tau phosphorylation and loss of microtubule binding
    • Busciglio, J., Lorenzo, A., Yeh, J., and Yanker, B. A. (1995). beta Amyloid fibrils induce Tau phosphorylation and loss of microtubule binding. Neuron 14, 879-888.
    • (1995) Neuron , vol.14 , pp. 879-888
    • Busciglio, J.1    Lorenzo, A.2    Yeh, J.3    Yanker, B.A.4
  • 41
    • 0026046950 scopus 로고
    • Tau-protein binds to microtubules through a flexible array of distributed weak sites
    • Butner, K. A., and Kirschner, M. W. (1991). Tau-protein binds to microtubules through a flexible array of distributed weak sites. J. Cell. Biol. 115, 717-730.
    • (1991) J. Cell. Biol. , vol.115 , pp. 717-730
    • Butner, K.A.1    Kirschner, M.W.2
  • 42
    • 0026584805 scopus 로고
    • Detection of an unstable fragment of DNA specific to individuals with myotonic dystrophy
    • Buxton, J., Shelbourne, P., and Davies, J. (1992). Detection of an unstable fragment of DNA specific to individuals with myotonic dystrophy. Nature 355, 547-548.
    • (1992) Nature , vol.355 , pp. 547-548
    • Buxton, J.1    Shelbourne, P.2    Davies, J.3
  • 43
    • 0025098891 scopus 로고
    • Inhibition of neunte polarity by tau antisense oligonucleotides in primary cerebellar neurons
    • Caceres, A., and Kosik, K. S. (1990). Inhibition of neunte polarity by tau antisense oligonucleotides in primary cerebellar neurons. Nature 343, 461-463.
    • (1990) Nature , vol.343 , pp. 461-463
    • Caceres, A.1    Kosik, K.S.2
  • 44
    • 0026001490 scopus 로고
    • The effect of tau-antisense oligonucleotides on neurite formation of cultured cerebellar macroneurons
    • Caceres, A., Potrebic, S., and Kosik, K. S. (1991). The effect of tau-antisense oligonucleotides on neurite formation of cultured cerebellar macroneurons. J. Neurosci. 11, 1515-1523.
    • (1991) J. Neurosci. , vol.11 , pp. 1515-1523
    • Caceres, A.1    Potrebic, S.2    Kosik, K.S.3
  • 45
    • 85030287183 scopus 로고    scopus 로고
    • Phosphorylated Ser 422, a specific Alzheimer epitope, is expressed by SKNSH-SY5Y cells after okadaic acid
    • in press.
    • Caillet-Boudin, M. L., and Delacourte, A. (1996). Phosphorylated Ser 422, a specific Alzheimer epitope, is expressed by SKNSH-SY5Y cells after okadaic acid. Neuroreport 8, in press.
    • (1996) Neuroreport , vol.8
    • Caillet-Boudin, M.L.1    Delacourte, A.2
  • 46
    • 0021240088 scopus 로고
    • Interaction between microtubule-associated protein Tau and spectrin
    • Carlier, M. F., Simon, C., Cassoly, R., and Pradel, L. A. (1984). Interaction between microtubule-associated protein Tau and spectrin. Biochimie. 664,305-311.
    • (1984) Biochimie. , vol.664 , pp. 305-311
    • Carlier, M.F.1    Simon, C.2    Cassoly, R.3    Pradel, L.A.4
  • 47
    • 0028938832 scopus 로고
    • Differential expression of alternatively spliced forms of MAP4: A repertoire of structurally different microtubulebinding domains
    • Chapin, S. J., Lue, C. M., Yu, M. T., and Bulinski, J. C. (1995). Differential expression of alternatively spliced forms of MAP4: A repertoire of structurally different microtubulebinding domains. Biochemistry 34,2289-2301.
    • (1995) Biochemistry , vol.34 , pp. 2289-2301
    • Chapin, S.J.1    Lue, C.M.2    Yu, M.T.3    Bulinski, J.C.4
  • 48
    • 0029879877 scopus 로고    scopus 로고
    • Glial inclusions in CNS degenerative diseases
    • Chin, S. S. M., and Goldman, J. E. (1996). Glial inclusions in CNS degenerative diseases. J. Neuropathol. Exp. Neural. 55, 499-508.
    • (1996) J. Neuropathol. Exp. Neural. , vol.55 , pp. 499-508
    • Chin, S.S.M.1    Goldman, J.E.2
  • 49
    • 0024792262 scopus 로고
    • Protein phosphatases come of age
    • Cohen, P., and Cohen, P. T. W. (1989). Protein phosphatases come of age. J. Biol. Chem. 264, 21435-21438.
    • (1989) J. Biol. Chem. , vol.264 , pp. 21435-21438
    • Cohen, P.1    Cohen, P.T.W.2
  • 50
    • 0025335664 scopus 로고
    • The tubulin-binding sequence of brain microtubule-associated proteins, Tau and MAP2, is also involved in actin binding
    • Correas, I., Padilla, R., and Avila, J. (1990). The tubulin-binding sequence of brain microtubule-associated proteins, Tau and MAP2, is also involved in actin binding. Biochem. J. 269,61-64.
    • (1990) Biochem. J. , vol.269 , pp. 61-64
    • Correas, I.1    Padilla, R.2    Avila, J.3
  • 51
    • 0021242668 scopus 로고
    • Subcortical dementia: Review of an emerging concept
    • Cummings, J. L., and Benson, D. F. (1984). Subcortical dementia: review of an emerging concept. Arch. Neural. 41, 874-879.
    • (1984) Arch. Neural. , vol.41 , pp. 874-879
    • Cummings, J.L.1    Benson, D.F.2
  • 52
    • 0028040462 scopus 로고
    • Pathological Tau proteins of Alzheimer's disease as a biochemical marker of neurofibrillary degeneration
    • Delacourte, A. (1994). Pathological Tau proteins of Alzheimer's disease as a biochemical marker of neurofibrillary degeneration. Biomed. Pharmacother. 48,287-295.
    • (1994) Biomed. Pharmacother. , vol.48 , pp. 287-295
    • Delacourte, A.1
  • 53
    • 0022980104 scopus 로고
    • Alzheimer's disease: Tau proteins, the promoting factors of microtubule assembly, are major components of paired helical filaments
    • Delacourte, A., and Défossez, A. (1986). Alzheimer's disease: Tau proteins, the promoting factors of microtubule assembly, are major components of paired helical filaments. J. Neural. Sei. 76, 173-186.
    • (1986) J. Neural. Sei. , vol.76 , pp. 173-186
    • Delacourte, A.1    Défossez, A.2
  • 54
    • 0025284610 scopus 로고
    • Pathological proteins Tau 64 and 69 are specifically expressed in the somatodendritic domain of the degenerating cortical neurons during Alzheimer's disease: Demonstration with a panel of antibodies against Tau proteins
    • Delacourte, A., Flament, S., Dibe, E. M., Hublau, P., Sablonniere, B., Hemon, B., Scherrer, V., and Défossez, A. (1990). Pathological proteins Tau 64 and 69 are specifically expressed in the somatodendritic domain of the degenerating cortical neurons during Alzheimer's disease: Demonstration with a panel of antibodies against Tau proteins. Acta Neuropathol. 80,111-117.
    • (1990) Acta Neuropathol. , vol.80 , pp. 111-117
    • Delacourte, A.1    Flament, S.2    Dibe, E.M.3    Hublau, P.4    Sablonniere, B.5    Hemon, B.6    Scherrer, V.7    Défossez, A.8
  • 56
    • 0029770683 scopus 로고    scopus 로고
    • Ptl-1, a gene whose products are homologous to the tau microtubule-associated proteins
    • Dermott, J. B., Aamodt, S., and Aamodt, E. (1996) ptl-1, a gene whose products are homologous to the tau microtubule-associated proteins. Biochemistry 35, 9415-9423.
    • (1996) Biochemistry , vol.35 , pp. 9415-9423
    • Dermott, J.B.1    Aamodt, S.2    Aamodt, E.3
  • 57
    • 0029018830 scopus 로고
    • Tau protein is altered by focal cerebral ischaemia in the rat: An immunohistochemical and immunoblotting study
    • Dewar, D., and Dawson, D. (1995). Tau protein is altered by focal cerebral ischaemia in the rat: An immunohistochemical and immunoblotting study. Brain Res. 684, 70-78.
    • (1995) Brain Res. , vol.684 , pp. 70-78
    • Dewar, D.1    Dawson, D.2
  • 58
    • 0028275310 scopus 로고
    • Cerebral ischemia induces alterations in Tau and ubiquitin proteins
    • Dewar, D., Graham, D. I., Teasdale, G. M., and McCulloch, J. (1994). Cerebral ischemia induces alterations in Tau and ubiquitin proteins. Dementia 5,168-173.
    • (1994) Dementia , vol.5 , pp. 168-173
    • Dewar, D.1    Graham, D.I.2    Teasdale, G.M.3    McCulloch, J.4
  • 59
    • 0030051269 scopus 로고    scopus 로고
    • Map-1B/Tau functional redundancy during laminin-enhanced axonal growth
    • Ditella, M. C, Feiguin, F., Carri, N., Kosik, K. S., and Caceres, A. (1996). Map-1B/Tau functional redundancy during laminin-enhanced axonal growth. J. Cell Sd. 109, 467-477.
    • (1996) J. Cell Sd. , vol.109 , pp. 467-477
    • Ditella, M.C.1    Feiguin, F.2    Carri, N.3    Kosik, K.S.4    Caceres, A.5
  • 60
    • 0027328373 scopus 로고
    • Glycosylation of mammalian neurofilaments-Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides-L and poIypeptides-M
    • Dong, D. L. Y., Xu, Z. S., Chevier, M. R., Cotter, R. J., Cleveland, D. W., and Hart, G. W. (1993). Glycosylation of mammalian neurofilaments-Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides-L and poIypeptides-M. J. Biol. Chem. 268, 16679-16687.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16679-16687
    • Dong, D.L.Y.1    Xu, Z.S.2    Chevier, M.R.3    Cotter, R.J.4    Cleveland, D.W.5    Hart, G.W.6
  • 61
    • 0026267223 scopus 로고
    • Intracellular organization of hippocampal neurons during the development of neuronal polarity
    • Dotti, C. G., and Banker, G. (1991). Intracellular organization of hippocampal neurons during the development of neuronal polarity. J. Cell. Sei. Suppl. 15, 75-84.
    • (1991) J. Cell. Sei. Suppl. , vol.15 , pp. 75-84
    • Dotti, C.G.1    Banker, G.2
  • 62
    • 0023627237 scopus 로고
    • The expression and distribution of the microtubule-associated proteins Tau and microtubule-associated protein 2 in hippocampal neurons in the rat in situ and in cell culture
    • Dotti, C. G., Banker, G., and Binder, L. I. (1987). The expression and distribution of the microtubule-associated proteins Tau and microtubule-associated protein 2 in hippocampal neurons in the rat in situ and in cell culture. Neuroscience 23,121-130.
    • (1987) Neuroscience , vol.23 , pp. 121-130
    • Dotti, C.G.1    Banker, G.2    Binder, L.I.3
  • 63
    • 0026549985 scopus 로고
    • Mitogen activated protein (MAP) kinase transforms Tau-protein into an Alzheimer-like state
    • Drewes, G., Lichtenbergkraag, B., Doring, F., Mandelkow, E. M., Biernat, J., and Gori, X. (1992). Mitogen activated protein (MAP) kinase transforms Tau-protein into an Alzheimer-like state. EMBO J. 11, 2131-2138.
    • (1992) EMBO J. , vol.11 , pp. 2131-2138
    • Drewes, G.1    Lichtenbergkraag, B.2    Doring, F.3    Mandelkow, E.M.4    Biernat, J.5    Gori, X.6
  • 64
    • 0028937631 scopus 로고
    • Microtubule-associated protein microtubule affinity-regulating kinase (p110(mark))-A novel protein kinase that regulates tau-microtubule interactions and dynamic instability by phosphorylation at the Alzheimer-specific site serine 262
    • Drewes, G., Trinczek, B., Illenberger, S., Biernat, J., Schmittulms, G., Meyer, H. E., Mandelkow, E. M., and Mandelkow, E. (1995). Microtubule-associated protein microtubule affinity-regulating kinase (p110(mark))-A novel protein kinase that regulates tau-microtubule interactions and dynamic instability by phosphorylation at the Alzheimer-specific site serine 262. J. Biol. Chem. 270, 7679-7688.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7679-7688
    • Drewes, G.1    Trinczek, B.2    Illenberger, S.3    Biernat, J.4    Schmittulms, G.5    Meyer, H.E.6    Mandelkow, E.M.7    Mandelkow, E.8
  • 65
    • 0022896901 scopus 로고
    • Tau protein function in living cells
    • Drubin, D. G., and Kirschner, M. W. (1986). Tau protein function in living cells. J. Cell. Biol. 103, 2738-2746.
    • (1986) J. Cell. Biol. , vol.103 , pp. 2738-2746
    • Drubin, D.G.1    Kirschner, M.W.2
  • 66
    • 0023937193 scopus 로고
    • Regulation of microtubule protein levels during cellular morphogenesis in nerve growth factor-treated PC12 cells
    • Drubin, D. G., Kobayashi, S., Kellogg, D., and Kirschner, M. W. (1988). Regulation of microtubule protein levels during cellular morphogenesis in nerve growth factor-treated PC12 cells. J. Cell Biol. 106, 1583-1591.
    • (1988) J. Cell Biol. , vol.106 , pp. 1583-1591
    • Drubin, D.G.1    Kobayashi, S.2    Kellogg, D.3    Kirschner, M.W.4
  • 67
    • 0028886016 scopus 로고
    • Postnatal changes in Ser/Thr protein phosphatases and their association with microtubules
    • Dudek, S. M., and Johnson, G. V. W. (1995). Postnatal changes in Ser/Thr protein phosphatases and their association with microtubules. Dev. Brain Res. 90, 54-61.
    • (1995) Dev. Brain Res. , vol.90 , pp. 54-61
    • Dudek, S.M.1    Johnson, G.V.W.2
  • 68
    • 0028982522 scopus 로고
    • Shift from fetal-type to Alzheimer-type phosphorylated Tau proteins in SKNSH-SY 5Y cells treated with okadaic acid
    • Dupont-Wallois, L., Sautiere, P. E., Cocquerelle, C., Bailleul, B., Delacourte, A., and Caillet-Boudin, M. L. (1995). Shift from fetal-type to Alzheimer-type phosphorylated Tau proteins in SKNSH-SY 5Y cells treated with okadaic acid. FEBS Lett. 357, 197-201.
    • (1995) FEBS Lett. , vol.357 , pp. 197-201
    • Dupont-Wallois, L.1    Sautiere, P.E.2    Cocquerelle, C.3    Bailleul, B.4    Delacourte, A.5    Caillet-Boudin, M.L.6
  • 69
    • 0004028961 scopus 로고
    • Springer-Verlag, Berlin/New York
    • Dustin, P. (1984). "Microtubules." Springer-Verlag, Berlin/New York.
    • (1984) Microtubules
    • Dustin, P.1
  • 70
    • 0029062956 scopus 로고
    • Widespread cytoskeletal pathology characterizes corticobasal degeneration
    • Feany, M. B., and Dickson, D. W. (1995). Widespread cytoskeletal pathology characterizes corticobasal degeneration. Am. J. Palhol. 146, 1388-1396.
    • (1995) Am. J. Palhol. , vol.146 , pp. 1388-1396
    • Feany, M.B.1    Dickson, D.W.2
  • 71
    • 0029041149 scopus 로고
    • Epitope expression and hyperphosphorylation of Tau protein in corticobasal degeneration: Differentiation from progressive supranuclear palsy
    • Feany, M. B., Ksiezak-Reding, H., Liu, W. K., Vincent, I., Yen, S. H. C, and Dickson, D. W. (1995b). Epitope expression and hyperphosphorylation of Tau protein in corticobasal degeneration: Differentiation from progressive supranuclear palsy. Acta Neuropathol. 90, 37-43.
    • (1995) Acta Neuropathol. , vol.90 , pp. 37-43
    • Feany, M.B.1    Ksiezak-Reding, H.2    Liu, W.K.3    Vincent, I.4    Yen, S.H.C.5    Dickson, D.W.6
  • 72
    • 0030049067 scopus 로고    scopus 로고
    • Neuropathologic overlap of progressive supranuclear palsy, Pick's disease and corticobasal degeneration
    • Feany, M. B., Mattiace, L. A., and Dickson, D. W. (1996). Neuropathologic overlap of progressive supranuclear palsy, Pick's disease and corticobasal degeneration. J. Neuropathol. Exp. Neurol. 55, 53-67.
    • (1996) J. Neuropathol. Exp. Neurol. , vol.55 , pp. 53-67
    • Feany, M.B.1    Mattiace, L.A.2    Dickson, D.W.3
  • 73
    • 0024417670 scopus 로고
    • The expression of acetylated microtubules during axonal and dendritic growth in cerebellar macroneurons which develop in vitro
    • Ferreira, A., and Caceres, A. (1989). The expression of acetylated microtubules during axonal and dendritic growth in cerebellar macroneurons which develop in vitro. Dev. Brain Res. 49, 205-213.
    • (1989) Dev. Brain Res. , vol.49 , pp. 205-213
    • Ferreira, A.1    Caceres, A.2
  • 74
    • 0024468551 scopus 로고
    • Characterization of two pathological tau-protein variants in Alzheimer brain cortices
    • Flament, S., Delacourte, A., Hemon, B., and Defossez, A. (1989). Characterization of two pathological tau-protein variants in Alzheimer brain cortices. J. Neural. Sei. 92, 133-141.
    • (1989) J. Neural. Sei. , vol.92 , pp. 133-141
    • Flament, S.1    Delacourte, A.2    Hemon, B.3    Defossez, A.4
  • 77
    • 0029072567 scopus 로고
    • Modulation of the phosphorylation state of Tau in situ: The roles of calcium and cyclic AMP
    • Fleming, L. M., and Johnson, G. V. M. (1995). Modulation of the phosphorylation state of Tau in situ: The roles of calcium and cyclic AMP. Biochem. J. 309, 41-47.
    • (1995) Biochem. J. , vol.309 , pp. 41-47
    • Fleming, L.M.1    Johnson, G.V.M.2
  • 78
    • 0026076318 scopus 로고
    • Pacific paradigms of environmentally-induced neurological disorders: Clinical, epidemiological and molecular perspectives
    • Garruto, R. M. (1991). Pacific paradigms of environmentally-induced neurological disorders: Clinical, epidemiological and molecular perspectives. Neurotoxicology 12, 347-378.
    • (1991) Neurotoxicology , vol.12 , pp. 347-378
    • Garruto, R.M.1
  • 79
    • 0028173238 scopus 로고
    • Tau phosphorylation in human, primate, and rat brain: Evidence that a pool of Tau is highly phosphorylated in vivo and is rapidly dephosphorylated in vitro
    • Carver, T. D., Harris, K. A., Lehman, R. A. \V., Lee, V. M. Y., Trojanowski, J. Q., and Billingsley, M. L. (1994). Tau phosphorylation in human, primate, and rat brain: Evidence that a pool of Tau is highly phosphorylated in vivo and is rapidly dephosphorylated in vitro. J. Neurochem. 63. 2279-2287.
    • (1994) J. Neurochem. , vol.63 , pp. 2279-2287
    • Carver, T.D.1    Harris, K.A.2    Lehman, R.A.V.3    Lee, V.M.Y.4    Trojanowski, J.Q.5    Billingsley, M.L.6
  • 80
    • 0029874980 scopus 로고    scopus 로고
    • Microtubule assembly competence analysis of freshly-biopsied human tau, dephosphorylated tau, and Alzheimer tau
    • Garver, T. D., Lehman, R. A. W., and Billingsley, M. L. (1996). Microtubule assembly competence analysis of freshly-biopsied human tau, dephosphorylated tau, and Alzheimer tau. J. Neiirosci. Res. 44, 12-20.
    • (1996) J. Neiirosci. Res. , vol.44 , pp. 12-20
    • Garver, T.D.1    Lehman, R.A.W.2    Billingsley, M.L.3
  • 81
    • 0027264771 scopus 로고
    • Expression of high molecular weight Tau in the central and peripheral nervous systems
    • Georgieff, I. S., Liem, R. K. H., Couchie, D., Mavilia, C, Nunez, J., and Shelanski, M. (1993). Expression of high molecular weight Tau in the central and peripheral nervous systems. J. Cell Sei. 105, 729-737.
    • (1993) J. Cell Sei. , vol.105 , pp. 729-737
    • Georgieff, I.S.1    Liem, R.K.H.2    Couchie, D.3    Mavilia, C.4    Nunez, J.5    Shelanski, M.6
  • 82
    • 51849178459 scopus 로고
    • Uber eigernartige hereditar-familiare Erkrankung des Zentralnervensystems
    • Gerstmann, J., Sträussler, E., and Schienker, I. (1936). Uber eigernartige hereditar-familiare Erkrankung des Zentralnervensystems. Z. Neural. 154, 736-762.
    • (1936) Z. Neural. , vol.154 , pp. 736-762
    • Gerstmann, J.1    Sträussler, E.2    Schienker, I.3
  • 86
    • 0028884524 scopus 로고
    • Regional distribution of neurofibrillary tangles and senile plaques in the cerebral cortex of very old patients
    • Giannakopoulos, P., Hof, P. R., Giannakopoulos, A. S., Herrmann, F. R., Michel, J. P., and Bouras, C. (1995a). Regional distribution of neurofibrillary tangles and senile plaques in the cerebral cortex of very old patients. Arch. Neural. 52, 1150-1159.
    • (1995) Arch. Neural. , vol.52 , pp. 1150-1159
    • Giannakopoulos, P.1    Hof, P.R.2    Giannakopoulos, A.S.3    Herrmann, F.R.4    Michel, J.P.5    Bouras, C.6
  • 87
    • 0029633769 scopus 로고
    • Age versus ageing as a cause of dementia
    • Giannakopoulos, P., Hof, P. R., and Bouras, C. (1995b). Age versus ageing as a cause of dementia. Lancet 346, 1486-1487.
    • (1995) Lancet , vol.346 , pp. 1486-1487
    • Giannakopoulos, P.1    Hof, P.R.2    Bouras, C.3
  • 88
    • 0025600995 scopus 로고
    • Expression of separate isoforms of human Tau protein: Correlation with the Tau pattern in brain and effects on tubulin polymerization
    • Goedert, M., and Jakes, R. (1990). Expression of separate isoforms of human Tau protein: Correlation with the Tau pattern in brain and effects on tubulin polymerization. EMBO J. 9, 4225-4230.
    • (1990) EMBO J. , vol.9 , pp. 4225-4230
    • Goedert, M.1    Jakes, R.2
  • 89
    • 0024387161 scopus 로고
    • Cloning and sequencing of the cDNA encoding an isoform of microtubule-associated protein tau containing 4 tandem repeats-Differential expression of tau protein messenger RNAs in human brain
    • Goedert, M., Spillantini, M. G., Potier, M. C., Ulrich, J., and Crowther, R. A. (1989a). Cloning and sequencing of the cDNA encoding an isoform of microtubule-associated protein tau containing 4 tandem repeats-Differential expression of tau protein messenger RNAs in human brain. EMBO J. 8, 393-399.
    • (1989) EMBO J. , vol.8 , pp. 393-399
    • Goedert, M.1    Spillantini, M.G.2    Potier, M.C.3    Ulrich, J.4    Crowther, R.A.5
  • 90
    • 0024745894 scopus 로고
    • Multiple isoforms of human microtubule-associated protein tau: Sequences and localization in neurofibrillary tangles of Alzheimer's disease
    • Goedert, M., Spillantini, M. G., Jakes, R., Rutherford, D., and Crowther, R. A. (19895). Multiple isoforms of human microtubule-associated protein tau: Sequences and localization in neurofibrillary tangles of Alzheimer's disease. Neuron 3, 519-526.
    • (1989) Neuron , vol.3 , pp. 519-526
    • Goedert, M.1    Spillantini, M.G.2    Jakes, R.3    Rutherford, D.4    Crowther, R.A.5
  • 91
    • 0026595846 scopus 로고
    • Tau-proteins of Alzheimer paired helical filaments-Abnormal phosphorylation of all six brain isoforms
    • Goedert, M., Spillantini, M. G., Cairns, N. J., and Crowther, R. A. (1992). Tau-proteins of Alzheimer paired helical filaments-Abnormal phosphorylation of all six brain isoforms. Neuron 8, 159-168.
    • (1992) Neuron , vol.8 , pp. 159-168
    • Goedert, M.1    Spillantini, M.G.2    Cairns, N.J.3    Crowther, R.A.4
  • 92
    • 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, R. A., Cohen, P., Vanmechelen, E., Vandermeeren, M., and Cras, P. (1994). Epitope mapping of monoclonal antibodies to the paired helical filaments of Alzheimer's disease: Identification of phosphorylation sites in Tau protein. Biochem. J. 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
  • 93
    • 0028946744 scopus 로고
    • Monoclonal antibody AT8 recognizes Tau protein phosphorylated at both serine 202 and threonine 205
    • Goedert, M., Jakes, R., and Vanmechelen, E. (1995). Monoclonal antibody AT8 recognizes Tau protein phosphorylated at both serine 202 and threonine 205. Neurosci. Lett. 189,167-170.
    • (1995) Neurosci. Lett. , vol.189 , pp. 167-170
    • Goedert, M.1    Jakes, R.2    Vanmechelen, E.3
  • 94
    • 0029113874 scopus 로고
    • Phosphatase activity toward abnormally phosphorylated tau: Decrease in Alzheimer disease brain
    • Gong, C. X., Shaikh, S., Wang, J. Z., Zaidi, T., Grundke-Iqbal, I., and Iqbal, K. (1995). Phosphatase activity toward abnormally phosphorylated tau: Decrease in Alzheimer disease brain. J. Neurocliem. 65, 732-738.
    • (1995) J. Neurocliem. , vol.65 , pp. 732-738
    • Gong, C.X.1    Shaikh, S.2    Wang, J.Z.3    Zaidi, T.4    Grundke-Iqbal, I.5    Iqbal, K.6
  • 95
    • 0028175215 scopus 로고
    • Identification of a novel microtubule binding and assembly domain in the developmentally regulated Inter-Repeat region of tau
    • Goode, B. L., and Feinstein, S. C. (1994). Identification of a novel microtubule binding and assembly domain in the developmentally regulated Inter-Repeat region of tau. J. Cell Biol. 124, 769-782.
    • (1994) J. Cell Biol. , vol.124 , pp. 769-782
    • Goode, B.L.1    Feinstein, S.C.2
  • 96
    • 0021842984 scopus 로고
    • Dephosphorylation of microtubule-associated protein 2, Tau factor, and tubulin by calcineurin
    • Goto, S., Yamamoto, H., Fukunaga, K., Iwasa, T., Matsukado, Y., and Miyamoto, E. (1985). Dephosphorylation of microtubule-associated protein 2, Tau factor, and tubulin by calcineurin. J. Neurochem. 451, 276-283.
    • (1985) J. Neurochem. , vol.451 , pp. 276-283
    • Goto, S.1    Yamamoto, H.2    Fukunaga, K.3    Iwasa, T.4    Matsukado, Y.5    Miyamoto, E.6
  • 97
    • 0028965635 scopus 로고
    • Somatodendritic localization and hyperphosphorylation of Tau protein in transgenic mice expressing the longest human brain Tau isoform
    • Gotz, J., Probst, A., Spillantini, M. G., Schafer, T., Jakes, R., Burki, K., and Goedert, M. (1995). Somatodendritic localization and hyperphosphorylation of Tau protein in transgenic mice expressing the longest human brain Tau isoform. EMBO J. 14,1304-1313.
    • (1995) EMBO J. , vol.14 , pp. 1304-1313
    • Gotz, J.1    Probst, A.2    Spillantini, M.G.3    Schafer, T.4    Jakes, R.5    Burki, K.6    Goedert, M.7
  • 98
    • 0026501888 scopus 로고
    • Hydrofluoric acid-treated tau-PHF proteins display the same biochemical properties as normal tau
    • Greenberg, S. G., Davies, P. Schein, J. D., and Binder, L. I. (1992). Hydrofluoric acid-treated tau-PHF proteins display the same biochemical properties as normal tau. J. Biol. Chem. 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
  • 99
    • 0029161154 scopus 로고
    • Localization and in situ phosphorylation state of nuclear tau
    • Greenwood, J. A., and Johnson, G. V. W. (1995). Localization and in situ phosphorylation state of nuclear tau. Exp. Cell Res. 220, 332-337.
    • (1995) Exp. Cell Res. , vol.220 , pp. 332-337
    • Greenwood, J.A.1    Johnson, G.V.W.2
  • 100
    • 0028049937 scopus 로고
    • Casein kinase II preferentially phosphorylates human Tau isoforms containing an aminoterminal insert-Identification of threonine 39 as the primary phosphate acceptor
    • Greenwood, J. A., Scott, C. W., Spreen, R. C, Caputo, C. B., and Johnson, G. V. W. (1994). Casein kinase II preferentially phosphorylates human Tau isoforms containing an aminoterminal insert-Identification of threonine 39 as the primary phosphate acceptor. J. Biol. Chem. 269, 4373-4380.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4373-4380
    • Greenwood, J.A.1    Scott, C.W.2    Spreen, R.C.3    Caputo, C.B.4    Johnson, G.V.W.5
  • 101
    • 0018129689 scopus 로고
    • Evidence for actin filament-microtubule interaction mediated by microtubule-associated proteins
    • Griffith, L. M., and Pollard, T. D. (1978). Evidence for actin filament-microtubule interaction mediated by microtubule-associated proteins. J. Cell Biol. 78, 958-965.
    • (1978) J. Cell Biol. , vol.78 , pp. 958-965
    • Griffith, L.M.1    Pollard, T.D.2
  • 102
    • 0022744803 scopus 로고
    • Abnormal phosphorylation of the Map Tau in Alzheimer cytoskeletal pathology
    • Grundke-Iqbal, I., Iqbal, K., Tung, Y. C., et al. (1986). Abnormal phosphorylation of the Map Tau in Alzheimer cytoskeletal pathology. Proc. Natl. Acad. Sei. USA 83, 4913-4917.
    • (1986) Proc. Natl. Acad. Sei. USA , vol.83 , pp. 4913-4917
    • Grundke-Iqbal, I.1    Iqbal, K.2    Tung, Y.C.3
  • 103
    • 0027272449 scopus 로고
    • Clinical picture of frontal lobe degeneration of non-Alzheimer type
    • Gustafson, L. (1993). Clinical picture of frontal lobe degeneration of non-Alzheimer type. Dementia 4, 143-148.
    • (1993) Dementia , vol.4 , pp. 143-148
    • Gustafson, L.1
  • 104
    • 0026683725 scopus 로고
    • The Alzheimer-like phosphorylation of tau-protein reduces microtubule binding and involves Ser-Pro and Thr-Pro motifs
    • Gustke, N., Steiner, B., Mandelkow, E. M., Biernat, J., Meyer, H. E., and Goedert, M. (1992). The Alzheimer-like phosphorylation of tau-protein reduces microtubule binding and involves Ser-Pro and Thr-Pro motifs. FEES Lett. 307, 199-205.
    • (1992) FEES Lett. , vol.307 , pp. 199-205
    • Gustke, N.1    Steiner, B.2    Mandelkow, E.M.3    Biernat, J.4    Meyer, H.E.5    Goedert, M.6
  • 105
    • 0028027088 scopus 로고
    • Domains of Tau protein and interactions with microtubules
    • Gustke, N., Trinczek, B., Mandelkow, E. M., and Mandelkow, E. (1994). Domains of Tau protein and interactions with microtubules. Biochemistry 33, 9511-9522.
    • (1994) Biochemistry , vol.33 , pp. 9511-9522
    • Gustke, N.1    Trinczek, B.2    Mandelkow, E.M.3    Mandelkow, E.4
  • 106
    • 0024461007 scopus 로고
    • Tau protein becomes long and stiff upon phosphorylation: Correlation between paracrystalline structure and degree of phosphorylation
    • Hagestedt, G., Lichtenberg, B., Wille, H., Mandelkow, E. M., and Mandelkow, M. (1989). Tau protein becomes long and stiff upon phosphorylation: Correlation between paracrystalline structure and degree of phosphorylation. J. Cell Biol. 109, 1643-1651.
    • (1989) J. Cell Biol. , vol.109 , pp. 1643-1651
    • Hagestedt, G.1    Lichtenberg, B.2    Wille, H.3    Mandelkow, E.M.4    Mandelkow, M.5
  • 107
    • 0018416633 scopus 로고
    • Dementia in Parkinson's disease: A neuropathologic study
    • Hakim, A. M., and Mathieson, G. (1979). Dementia in Parkinson's disease: A neuropathologic study. Neurology 29, 1204-1214.
    • (1979) Neurology , vol.29 , pp. 1204-1214
    • Hakim, A.M.1    Mathieson, G.2
  • 109
    • 0024533584 scopus 로고
    • Alz-50 Immunoreactivity in the neonatal rat - Changes in development and co-distribution with Map-2 immunoreactivity
    • Hamre, K. M., Hyman, B. T., Goodlett, C. R., West, J. R., and Vanhoesen, G. W. (1989). Alz-50 Immunoreactivity in the neonatal rat - Changes in development and co-distribution with Map-2 immunoreactivity. Neurosd. Lett. 98, 264-271.
    • (1989) Neurosd. Lett. , vol.98 , pp. 264-271
    • Hamre, K.M.1    Hyman, B.T.2    Goodlett, C.R.3    West, J.R.4    Vanhoesen, G.W.5
  • 110
    • 0026487365 scopus 로고
    • Glycogen synthase kinase-3 induces alzheimers disease-like phosphorylation of Tau-generation of paired helical filament epitopes and neuronal localisation of the kinase
    • Hanger, O.P., Hughes, K., Woodgett, J. R., Brion, J. P., and Anderton, B. H. (1992). Glycogen synthase kinase-3 induces alzheimers disease-like phosphorylation of Tau-generation of paired helical filament epitopes and neuronal localisation of the kinase. Neurosci. Lett. 147, 58-62.
    • (1992) Neurosci. Lett. , vol.147 , pp. 58-62
    • Hanger, O.P.1    Hughes, K.2    Woodgett, J.R.3    Brion, J.P.4    Anderton, B.H.5
  • 112
    • 0026546599 scopus 로고
    • An anatomical cascade hypothesis for Alzheimer's disease
    • Hardy, J. (1992). An anatomical cascade hypothesis for Alzheimer's disease. Trends Neurosci. 15, 200-201.
    • (1992) Trends Neurosci. , vol.15 , pp. 200-201
    • Hardy, J.1
  • 114
    • 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., and Ihara, Y. (1992). Protein sequence and mass spectrometric analyses of Tau in the Alzheimer's disease brain. J. Biol. Chem. 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
  • 115
    • 0027155834 scopus 로고
    • Characterization of 2 distinct monoclonal antibodies to paired helical filaments-Further evidence for fetal-type phosphorylation of the Tau in paired helical filaments
    • Hasegawa, M., Watanabe, A., Takio, K., Suzuki, M., Arai, T., Titani, K., and Ihara, Y. (1993). Characterization of 2 distinct monoclonal antibodies to paired helical filaments-Further evidence for fetal-type phosphorylation of the Tau in paired helical filaments. J. Neurochem. 60,2068-2077.
    • (1993) J. Neurochem. , vol.60 , pp. 2068-2077
    • Hasegawa, M.1    Watanabe, A.2    Takio, K.3    Suzuki, M.4    Arai, T.5    Titani, K.6    Ihara, Y.7
  • 116
    • 0029879046 scopus 로고    scopus 로고
    • Characterization of mAb AP422, a novel phosphorylation-dependent monoclonal antibody against Tau protein
    • Hasegawa, M., Jakes, R., Crowther, R. A., Lee, V. M. Y., Ihara, Y., and Goedert, M. (1996). Characterization of mAb AP422, a novel phosphorylation-dependent monoclonal antibody against Tau protein. FEES Lett. 384, 25-30.
    • (1996) FEES 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
  • 117
    • 0025093199 scopus 로고
    • Constant neurofibrillary changes in the neocortex in progressive supranuclear palsy-Basic differences with Alzheimer's disease and aging
    • Hauw, J. J., Verny, M., Delaere, P., Cervera, P., He, Y., and Duyckaerts, C. (1990). Constant neurofibrillary changes in the neocortex in progressive supranuclear palsy-Basic differences with Alzheimer's disease and aging. Neurosci. Lett. 119, 182-186.
    • (1990) Neurosci. Lett. , vol.119 , pp. 182-186
    • Hauw, J.J.1    Verny, M.2    Delaere, P.3    Cervera, P.4    He, Y.5    Duyckaerts, C.6
  • 118
    • 0028092015 scopus 로고
    • Preliminary NINDS neuropathologic criteria for Steele-Richardson-Olszewski syndrome (progressive supranuclear palsy)
    • Hauw, J. J., Daniel, S. E., Dickson, D., Horoupian, D. S., Jellinger, K., Lantos, P. L., Mckee, A., Tabaton, M., and Litvan, I. (1994). Preliminary NINDS neuropathologic criteria for Steele-Richardson-Olszewski syndrome (progressive supranuclear palsy). Neurology 44, 2015-2019.
    • (1994) Neurology , vol.44 , pp. 2015-2019
    • Hauw, J.J.1    Daniel, S.E.2    Dickson, D.3    Horoupian, D.S.4    Jellinger, K.5    Lantos, P.L.6    Mckee, A.7    Tabaton, M.8    Litvan, I.9
  • 119
    • 0028785529 scopus 로고
    • Subpopulations of Tau interact with microtubules and actin filaments in various cell types
    • Henriquez, J. P., Cross, D., Vial, C, and Maccioni, R. B. (1995). Subpopulations of Tau interact with microtubules and actin filaments in various cell types. Cell Biochem. Fund. 13, 239-250.
    • (1995) Cell Biochem. Fund. , vol.13 , pp. 239-250
    • Henriquez, J.P.1    Cross, D.2    Vial, C.3    Maccioni, R.B.4
  • 120
    • 0029064572 scopus 로고
    • Early Alzheimer disease-like histopathology increases in frequency with age in mice transgenic for beta-APP751
    • Higgins, L. S. Rodems, J. M., Catalano, R., Quon, D., and Cordell, B. (1995). Early Alzheimer disease-like histopathology increases in frequency with age in mice transgenic for beta-APP751. Proc. Natl. Acad. Sei. USA 92, 4402-4406.
    • (1995) Proc. Natl. Acad. Sei. USA , vol.92 , pp. 4402-4406
    • Higgins, L.S.1    Rodems, J.M.2    Catalano, R.3    Quon, D.4    Cordell, B.5
  • 121
    • 0024498630 scopus 로고
    • Structure of the bovine tau-gene-Alternatively spliced transcripts generate a protein family
    • Himmler, A. (1989). Structure of the bovine tau-gene-Alternatively spliced transcripts generate a protein family. Mol. Cell Biol. 9, 1389-1396.
    • (1989) Mol. Cell Biol. , vol.9 , pp. 1389-1396
    • Himmler, A.1
  • 122
    • 73049132762 scopus 로고
    • Parkinsonism-dementia complex, and endemic disease on the island of Guam: I. Clinical features
    • Hirano, A., Kurland, L. T., Krooth, R. S., and Lessel, S. (1961). Parkinsonism-dementia complex, and endemic disease on the island of Guam: I. Clinical features. Brain 84,642-661.
    • (1961) Brain , vol.84 , pp. 642-661
    • Hirano, A.1    Kurland, L.T.2    Krooth, R.S.3    Lessel, S.4
  • 123
    • 0014276827 scopus 로고
    • The fine structure of some intraganglionic alterations. Neurofibrillary tangles, granulovacuolar bodies and "rod-like" structures as seen in Guam amyotrophic lateral sclerosis and Parkinson's dementia complex
    • Hirano, A., Dembitzer, H. M., and Kurland, L. Y. (1968). The fine structure of some intraganglionic alterations. Neurofibrillary tangles, granulovacuolar bodies and "rod-like" structures as seen in Guam amyotrophic lateral sclerosis and Parkinson's dementia complex. J. Neuropathol. Exp. Neural. 67, 167-182.
    • (1968) J. Neuropathol. Exp. Neural. , vol.67 , pp. 167-182
    • Hirano, A.1    Dembitzer, H.M.2    Kurland, L.Y.3
  • 124
    • 0024094998 scopus 로고
    • Tau proteins: The molecular structure and mode of binding on microtubules
    • Hirokawa, N., Shiomura, Y., and Okabe, S. (1988). Tau proteins: The molecular structure and mode of binding on microtubules. J. Cell Biol. 107, 1449-1459.
    • (1988) J. Cell Biol. , vol.107 , pp. 1449-1459
    • Hirokawa, N.1    Shiomura, Y.2    Okabe, S.3
  • 125
    • 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., Satoharada, R., and Kanai, Y. (1996). 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. 132,667-679.
    • (1996) J. Cell Biol. , vol.132 , pp. 667-679
    • Hirokawa, N.1    Funakoshi, T.2    Satoharada, R.3    Kanai, Y.4
  • 126
    • 0002377794 scopus 로고
    • The cellular basis of cortical disconnection in Alzheimer's disease and related dementing conditions
    • R. D. Terry, R. Katzman, and K. L. Bick, Eds., Raven Press, New York
    • Hof, P. R., and Morrison, J. H. (1994). The cellular basis of cortical disconnection in Alzheimer's disease and related dementing conditions. In "Alzheimer's Disease" (R. D. Terry, R. Katzman, and K. L. Bick, Eds.), pp. 197-229. Raven Press, New York.
    • (1994) Alzheimer's Disease , pp. 197-229
    • Hof, P.R.1    Morrison, J.H.2
  • 127
    • 0025955171 scopus 로고
    • Neurofibrillary tangle distribution in the cerebral cortex of Parkinsonism-dementia cases from Guam - Differences with Alzheimer's disease
    • Hof, P. R., Perl, D. P., Loerzel, A. J., and Morrison, J. H. (1991). Neurofibrillary tangle distribution in the cerebral cortex of Parkinsonism-dementia cases from Guam - Differences with Alzheimer's disease. Brain Res. 564, 306-313.
    • (1991) Brain Res. , vol.564 , pp. 306-313
    • Hof, P.R.1    Perl, D.P.2    Loerzel, A.J.3    Morrison, J.H.4
  • 128
    • 0026454256 scopus 로고
    • Differential distribution of neurofibrillary tangles in the cerebral cortex of Dementia Pugilistica and Alzheimer's disease cases
    • Hof, P. R., Bouras, C, Buée, L., Delacourte, A., Perl, D. P., and Morrison, J. H. (1992a). Differential distribution of neurofibrillary tangles in the cerebral cortex of Dementia Pugilistica and Alzheimer's disease cases. Acta Neuropathol. 85, 23-30.
    • (1992) Acta Neuropathol. , vol.85 , pp. 23-30
    • Hof, P.R.1    Bouras, C.2    Buée, L.3    Delacourte, A.4    Perl, D.P.5    Morrison, J.H.6
  • 131
    • 0028011866 scopus 로고
    • Quantitative neuropathologic analysis of picks disease cases - Cortical distribution of pick bodies and coexistence with alzheimers disease
    • Hof, P. R., Bouras, C, Perl, D. P., and Morrison, J. H. (1994b). Quantitative neuropathologic analysis of picks disease cases - Cortical distribution of pick bodies and coexistence with alzheimers disease. Acta Neuropathol. 87,115-124.
    • (1994) Acta Neuropathol. , vol.87 , pp. 115-124
    • Hof, P.R.1    Bouras, C.2    Perl, D.P.3    Morrison, J.H.4
  • 132
    • 0028948391 scopus 로고
    • Age-related distribution of neuropathologic changes in the cerebral cortex of patients with Down's syndrome: Quantitative regional analysis and comparison with Alzheimer's disease
    • Hof, P. R., Bouras, C., Perl, D. P., Sparks, D. L., Mehta, N., and Morrison, J. H. (1995). Age-related distribution of neuropathologic changes in the cerebral cortex of patients with Down's syndrome: Quantitative regional analysis and comparison with Alzheimer's disease. Arch. Neural. 52, 379-391.
    • (1995) Arch. Neural. , vol.52 , pp. 379-391
    • Hof, P.R.1    Bouras, C.2    Perl, D.P.3    Sparks, D.L.4    Mehta, N.5    Morrison, J.H.6
  • 134
    • 0028276575 scopus 로고
    • Extracellular signal regulated kinases-Localization of protein and mRNA in the human hippocampal formation in Alzheimer's disease
    • Hyman, B. T., Elvhage, T. E., and Reiter, J. (1994). Extracellular signal regulated kinases-Localization of protein and mRNA in the human hippocampal formation in Alzheimer's disease. Am. J. Pathol. 144, 565-572.
    • (1994) Am. J. Pathol. , vol.144 , pp. 565-572
    • Hyman, B.T.1    Elvhage, T.E.2    Reiter, J.3
  • 135
    • 0022724941 scopus 로고
    • Phosphorylated tau protein is integrated into paired helical filaments in Alzheimer's disease
    • Ihara, Y., Nukina, N., Miura, R., and Ogawara, M. (1986). Phosphorylated tau protein is integrated into paired helical filaments in Alzheimer's disease. J. Biochem. (Tokyo) 99,1807-1810.
    • (1986) J. Biochem. (Tokyo) , vol.99 , pp. 1807-1810
    • Ihara, Y.1    Nukina, N.2    Miura, R.3    Ogawara, M.4
  • 136
    • 0027500717 scopus 로고
    • Anti-tau-positive glial fibrillary tangles in the brain of postencephalitic parkinsonism of economo type
    • Ikeda, K., Akiyama, H., Kondo, H., and Ikeda, K. (1993). Anti-tau-positive glial fibrillary tangles in the brain of postencephalitic parkinsonism of economo type. Neurosci. Lett. 162,176-178.
    • (1993) Neurosci. Lett. , vol.162 , pp. 176-178
    • Ikeda, K.1    Akiyama, H.2    Kondo, H.3    Ikeda, K.4
  • 137
    • 0029062279 scopus 로고
    • Numerous glial fibrillary tangles in oligondendroglia in cases of subacute sclerosing panencephalitis with neurofibrillary tangles
    • Ikeda, K., Akiyama, H., Kondo, H., Arai, T., Arai, N., and Yagishita, S. (1995). Numerous glial fibrillary tangles in oligondendroglia in cases of subacute sclerosing panencephalitis with neurofibrillary tangles. Neurosci. Lett. 194, 133-135.
    • (1995) Neurosci. Lett. , vol.194 , pp. 133-135
    • Ikeda, K.1    Akiyama, H.2    Kondo, H.3    Arai, T.4    Arai, N.5    Yagishita, S.6
  • 138
    • 0020565637 scopus 로고
    • Protein phosphatases: Properties and role in cellular regulation
    • Ingebristen, T. S., and Cohen, P. (1983). Protein phosphatases: Properties and role in cellular regulation. Science 221, 331-338.
    • (1983) Science , vol.221 , pp. 331-338
    • Ingebristen, T.S.1    Cohen, P.2
  • 139
    • 85030283251 scopus 로고    scopus 로고
    • Tau in fibroblasts with and without the Swedish APP 670/671 mutation
    • Ingelson, M., and Lannfelt, L. (1996). Tau in fibroblasts with and without the Swedish APP 670/671 mutation. Neurobiol. Aging 17 (Suppl. 4), S101.
    • (1996) Neurobiol. Aging , vol.17 , Issue.4 SUPPL.
    • Ingelson, M.1    Lannfelt, L.2
  • 140
    • 0029008731 scopus 로고
    • Alzheimer abnormally phosphorylated tau is more hyperphosphorylated than the fetal tau abd causes the disruption of microtubules
    • Iqbal, K., and Grundke-Iqbal, I. (1995). Alzheimer abnormally phosphorylated tau is more hyperphosphorylated than the fetal tau abd causes the disruption of microtubules. Neurobiol. Aging 16, 375-379.
    • (1995) Neurobiol. Aging , vol.16 , pp. 375-379
    • Iqbal, K.1    Grundke-Iqbal, I.2
  • 141
    • 0019521760 scopus 로고
    • Distribution and ultrastructure of Alzheimer's neurofibrillary tangles in postencephalitic Parkinsonism of Economo type
    • Ishii, T., and Nakamura, Y. (1981). Distribution and ultrastructure of Alzheimer's neurofibrillary tangles in postencephalitic Parkinsonism of Economo type. Acta Neuropathol. 55,59-62.
    • (1981) Acta Neuropathol. , vol.55 , pp. 59-62
    • Ishii, T.1    Nakamura, Y.2
  • 142
    • 0028883086 scopus 로고
    • Myotonie dystrophy: Correlation of clinical symptoms with the size of the CTG trinucleotide repeat
    • Jaspert, A., Fahsold, R., Grehl, H., and Claus, D. (1995). Myotonie dystrophy: Correlation of clinical symptoms with the size of the CTG trinucleotide repeat. J. Neural. 242, 99-104.
    • (1995) J. Neural. , vol.242 , pp. 99-104
    • Jaspert, A.1    Fahsold, R.2    Grehl, H.3    Claus, D.4
  • 143
    • 0023635030 scopus 로고
    • Tau antisera recognize neurofibrillary tangles in a range of neurodegenerative disorders
    • Joachim, C. L., Morris, J. H., Kosik, K. S., and Selkoe, D. J. (1987). Tau antisera recognize neurofibrillary tangles in a range of neurodegenerative disorders. Ann. Neural. 22,514-520.
    • (1987) Ann. Neural. , vol.22 , pp. 514-520
    • Joachim, C.L.1    Morris, J.H.2    Kosik, K.S.3    Selkoe, D.J.4
  • 144
    • 0026563915 scopus 로고
    • Differential phosphorylation of Tau by cyclic AMP-dependent protein kinase and Ca-2+/calmodulin-dependent protein kinase-II - Metabolic and functional consequences
    • Johnson, G. V. W. (1992). Differential phosphorylation of Tau by cyclic AMP-dependent protein kinase and Ca-2+/calmodulin-dependent protein kinase-II - Metabolic and functional consequences. J. Neurochem. 59, 2056-2062.
    • (1992) J. Neurochem. , vol.59 , pp. 2056-2062
    • Johnson, G.V.W.1
  • 145
    • 0024438227 scopus 로고
    • Expression of multiple tau isoforms and microtubule bundle formation in fibroblasts transfected with a single tau cDNA
    • Kanai, Y., Takemura, R., Oshima, T., Mori, H., Ihara, Y., Yanagisawa, M., Masaki, T., and Hirokawa, N. (1989). Expression of multiple tau isoforms and microtubule bundle formation in fibroblasts transfected with a single tau cDNA. J. Cell Biol. 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    Hirokawa, N.8
  • 146
    • 0026758380 scopus 로고
    • Microtubule bundling by Tau proteins in vivo: Analysis of functional domains
    • Kanai, J., Chen, J., and Hirokawa, N. (1992). Microtubule bundling by Tau proteins in vivo: Analysis of functional domains. EMBO J. 11, 3953-3961.
    • (1992) EMBO J. , vol.11 , pp. 3953-3961
    • Kanai, J.1    Chen, J.2    Hirokawa, N.3
  • 147
    • 37049048544 scopus 로고
    • Paired helical filaments in electron microscopy of Alzheimer's disease
    • Kidd, M. (1963). Paired helical filaments in electron microscopy of Alzheimer's disease. Nature 197, 192-193.
    • (1963) Nature , vol.197 , pp. 192-193
    • Kidd, M.1
  • 148
    • 0025736188 scopus 로고
    • Presenile appearance of abundant Alzheimer's neurofibrillary tangles without senile plaques in the brain in myotonic dystrophy
    • Kiuchi, A., Otsuka, N., Namba, Y., Nakano, I., and Tomonaga, M. (1991). Presenile appearance of abundant Alzheimer's neurofibrillary tangles without senile plaques in the brain in myotonic dystrophy. Acta Neuropathol. 82, 1-5.
    • (1991) Acta Neuropathol. , vol.82 , pp. 1-5
    • Kiuchi, A.1    Otsuka, N.2    Namba, Y.3    Nakano, I.4    Tomonaga, M.5
  • 149
  • 150
    • 0029053634 scopus 로고
    • Rapid reversible phosphorylation of rat brain Tau proteins in response to cold water stress
    • Korneyev, A., Binder, L., and Bernardis, J. (1995). Rapid reversible phosphorylation of rat brain Tau proteins in response to cold water stress. Neurosci. Lett. 191, 19-22.
    • (1995) Neurosci. Lett. , vol.191 , pp. 19-22
    • Korneyev, A.1    Binder, L.2    Bernardis, J.3
  • 151
    • 0024641959 scopus 로고
    • Developmentally regulated expression of specific tau sequences
    • Kosik, K. S., Orecchio, L. D., Bakalis, S., and Neve, R. L. (1989). Developmentally regulated expression of specific tau sequences. Neuron 2, 1389-1397.
    • (1989) Neuron , vol.2 , pp. 1389-1397
    • Kosik, K.S.1    Orecchio, L.D.2    Bakalis, S.3    Neve, R.L.4
  • 153
    • 0028065142 scopus 로고
    • Analysis of microtubule-associated protein Tau glycation in paired helical filaments
    • Ledesma, M. D., Bonay, P., Colaco, C, and Avila, J. (1994). Analysis of microtubule-associated protein Tau glycation in paired helical filaments. J. Biol. Chem. 269,21614-21619.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21614-21619
    • Ledesma, M.D.1    Bonay, P.2    Colaco, C.3    Avila, J.4
  • 154
    • 0029133373 scopus 로고
    • Tau protein from Alzheimer's disease patients is glycated at its tubulin-binding domain
    • Ledesma, M. D., Bonay, P., and Avila, J. (1995). Tau protein from Alzheimer's disease patients is glycated at its tubulin-binding domain. J. Neurochem. 65, 1658-1664.
    • (1995) J. Neurochem. , vol.65 , pp. 1658-1664
    • Ledesma, M.D.1    Bonay, P.2    Avila, J.3
  • 155
    • 0026704256 scopus 로고
    • Expression of tau protein in non-neuronal cells-Microtubule binding and stabilization
    • Lee, G., and Rook, S. L. (1992). Expression of tau protein in non-neuronal cells-Microtubule binding and stabilization. J. Cell Sei. 102, 227-237.
    • (1992) J. Cell Sei. , vol.102 , pp. 227-237
    • Lee, G.1    Rook, S.L.2
  • 156
    • 0023905288 scopus 로고
    • The primary structure and heterogeneity of Tau protein from mouse brain
    • Lee, G., Cowan, N., and Kirschner, M. (1988). The primary structure and heterogeneity of Tau protein from mouse brain. Science 239, 285-289.
    • (1988) Science , vol.239 , pp. 285-289
    • Lee, G.1    Cowan, N.2    Kirschner, M.3
  • 157
    • 0024675418 scopus 로고
    • The microtubule binding domain of tau protein
    • Lee, G., Neve, R. L., and Kosik, K. S. (1989). The microtubule binding domain of tau protein. Neuron 2,1615-1624.
    • (1989) Neuron , vol.2 , pp. 1615-1624
    • Lee, G.1    Neve, R.L.2    Kosik, K.S.3
  • 158
    • 0024574386 scopus 로고
    • Dystrophie peptidergic neuntes in senile plaques of Alzheimers disease hippocampus precede formation of paired helical filaments
    • Lenders, M. B., Peers, M. C., Tramu, G., Delacourte, A., Defossez, A., Petit, H., and Mazzuca, M. (1989). Dystrophie peptidergic neuntes in senile plaques of Alzheimers disease hippocampus precede formation of paired helical filaments. Brain Res. 481, 344-349.
    • (1989) Brain Res. , vol.481 , pp. 344-349
    • Lenders, M.B.1    Peers, M.C.2    Tramu, G.3    Delacourte, A.4    Defossez, A.5    Petit, H.6    Mazzuca, M.7
  • 159
    • 0020365611 scopus 로고
    • Interactions between neurofilaments and microtubule-associated proteins: A possible mechanism for intraorganellar bridging
    • Leterrier, J. F., Liem, R. K., and Shelanski, M. L. (1982). Interactions between neurofilaments and microtubule-associated proteins: A possible mechanism for intraorganellar bridging. J. Cell Biol. 95, 982-986.
    • (1982) J. Cell Biol. , vol.95 , pp. 982-986
    • Leterrier, J.F.1    Liem, R.K.2    Shelanski, M.L.3
  • 160
    • 0021338217 scopus 로고
    • Phosphorylation affects the ability of Tau protein to promote microtubule assembly
    • Lindwall, G., and Cole, R. D. (1984). Phosphorylation affects the ability of Tau protein to promote microtubule assembly. J. Biol. Chem. 255, 5301-5305.
    • (1984) J. Biol. Chem. , vol.255 , pp. 5301-5305
    • Lindwall, G.1    Cole, R.D.2
  • 161
    • 0026597280 scopus 로고
    • Phosphorylation by cAMP-dependent protein kinase inhibits the degradation of tau by calpain
    • Litersky, J. M., and Johnson, G. V. W. (1992). Phosphorylation by cAMP-dependent protein kinase inhibits the degradation of tau by calpain. J. Biol. Chem. 267, 1563-1568.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1563-1568
    • Litersky, J.M.1    Johnson, G.V.W.2
  • 162
    • 0028878537 scopus 로고
    • Detection of a Cdc2-related kinase associated with Alzheimer paired helical filaments
    • Liu, W. K., Williams, R. T., Hall, F. L., Dickson, D. W., and Yen, S. H. (1995). Detection of a Cdc2-related kinase associated with Alzheimer paired helical filaments. Am. J. Pathol. 146, 228-238.
    • (1995) Am. J. Pathol. , vol.146 , pp. 228-238
    • Liu, W.K.1    Williams, R.T.2    Hall, F.L.3    Dickson, D.W.4    Yen, S.H.5
  • 163
    • 0028287275 scopus 로고
    • Interaction of tubulin and microtubule proteins with vanadate oligomers
    • Lobert, S., Isern, N., Hennington, B. S., and Correia, J. J. (1994). Interaction of tubulin and microtubule proteins with vanadate oligomers. Biochemistry 33, 6244-6252.
    • (1994) Biochemistry , vol.33 , pp. 6244-6252
    • Lobert, S.1    Isern, N.2    Hennington, B.S.3    Correia, J.J.4
  • 164
    • 0028853922 scopus 로고
    • Functional implications for the microtubule-associated protein tau: Localization in oligodendrocytes
    • Lopresti, P. Szuchet, S., Papasozomenos, S. C., Zinkowski, R. P., and Binder, L. I. (1995). Functional implications for the microtubule-associated protein tau: Localization in oligodendrocytes. Proc. Natl. Acad. Sei. USA 92, 10369-10373.
    • (1995) Proc. Natl. Acad. Sei. USA , vol.92 , pp. 10369-10373
    • Lopresti, P.1    Szuchet, S.2    Papasozomenos, S.C.3    Zinkowski, R.P.4    Binder, L.I.5
  • 165
    • 0028929548 scopus 로고
    • Neurofibrillary tangles in Niemann-Pick disease type C
    • Love, S., Bridges, L. R., and Case, C. P. (1995). Neurofibrillary tangles in Niemann-Pick disease type C. Brain 118,119-129.
    • (1995) Brain , vol.118 , pp. 119-129
    • Love, S.1    Bridges, L.R.2    Case, C.P.3
  • 166
    • 0029589683 scopus 로고
    • Ultrastructure and immunoreactivity of dystrophic axons indicate a different pathogenesis of Hallervorden-Spatz disease and infantile neuroaxonal dystrophy
    • Malandrini, A., Cavallaro, T., Fabrizi, G. M., Berti, G., Salvestroni, R., Salvadori, C., and Guazzi, G. C. (1995). Ultrastructure and immunoreactivity of dystrophic axons indicate a different pathogenesis of Hallervorden-Spatz disease and infantile neuroaxonal dystrophy. Virchows Archiv. A 427, 415-421.
    • (1995) Virchows Archiv. A , vol.427 , pp. 415-421
    • Malandrini, A.1    Cavallaro, T.2    Fabrizi, G.M.3    Berti, G.4    Salvestroni, R.5    Salvadori, C.6    Guazzi, G.C.7
  • 168
    • 0028998409 scopus 로고
    • The rnicrotubule cytoskeleton and the development of neuronal polarity
    • Mandell, J. W., and Banker, G. A. (1995). The rnicrotubule cytoskeleton and the development of neuronal polarity. Neuwbiol. Aging 16,229-237.
    • (1995) Neuwbiol. Aging , vol.16 , pp. 229-237
    • Mandell, J.W.1    Banker, G.A.2
  • 170
    • 0028989637 scopus 로고
    • Alzheimer's-associated phospho-Tau epitope in human neuroblastoma cell cultures: Up-regulation by fibronectin and laminin
    • Martin, H., Lambert, M. P., Barber, K., Hinton, S., and Klein, W. L. (1995). Alzheimer's-associated phospho-Tau epitope in human neuroblastoma cell cultures: Up-regulation by fibronectin and laminin. Neuroscience 66, 769-779.
    • (1995) Neuroscience , vol.66 , pp. 769-779
    • Martin, H.1    Lambert, M.P.2    Barber, K.3    Hinton, S.4    Klein, W.L.5
  • 171
    • 0027955864 scopus 로고
    • Kinesin and Tau bind to distinct sites on microtubules
    • Marya, P. K., Syed, Z., Fraylich, P. E., and Eagles, P. A. M. (1994). Kinesin and Tau bind to distinct sites on microtubules. J. Cell Sei. 107, 339-344.
    • (1994) J. Cell Sei. , vol.107 , pp. 339-344
    • Marya, P.K.1    Syed, Z.2    Fraylich, P.E.3    Eagles, P.A.M.4
  • 172
    • 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, E. S., Shin, R. W., Billingsley, M. L., Vandevoorde, A., O'connor, M., Trojanowski, J. Q., and Lee, V. M. Y. (1994). Biopsy-derived adult human brain Tau is phosphorylated at many of the same sites as Alzheimer's disease paired helical filament tau. Neuron 13,989-1002.
    • (1994) Neuron , vol.13 , pp. 989-1002
    • Matsuo, E.S.1    Shin, R.W.2    Billingsley, M.L.3    Vandevoorde, A.4    O'Connor, M.5    Trojanowski, J.Q.6    Lee, V.M.Y.7
  • 173
    • 0028082066 scopus 로고
    • Stiff microtubules and neuronal morphology
    • Matus, A. (1994). Stiff microtubules and neuronal morphology. Trends Neurosci. 17,19-22.
    • (1994) Trends Neurosci. , vol.17 , pp. 19-22
    • Matus, A.1
  • 174
    • 0028172239 scopus 로고
    • The phosphorylation state of Tau in the developing rat brain is regulated by phosphoprotein phosphatases
    • Mawal-Dewan, M., Henley, J., Vandevoorde, A., Trojanowski, J. Q., and Lee, V. M. Y. (1994). The phosphorylation state of Tau in the developing rat brain is regulated by phosphoprotein phosphatases. J. Biol. Chem. 269, 30981-30987.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30981-30987
    • Mawal-Dewan, M.1    Henley, J.2    Vandevoorde, A.3    Trojanowski, J.Q.4    Lee, V.M.Y.5
  • 176
    • 0028266611 scopus 로고
    • Association of measles virus with neurofibrillary tangles in subacute sclerosing panencephalitis - A combined in situ hybridization and immunocytochemical investigation
    • McQuaid, S., Alien, I. V., Mcmahon, J., and Kirk, J. (1994). Association of measles virus with neurofibrillary tangles in subacute sclerosing panencephalitis - A combined in situ hybridization and immunocytochemical investigation. Neuropathol. Appl. Neural. 20, 103-110.
    • (1994) Neuropathol. Appl. Neural. , vol.20 , pp. 103-110
    • McQuaid, S.1    Alien, I.V.2    Mcmahon, J.3    Kirk, J.4
  • 177
    • 0028207977 scopus 로고
    • Molecular motors and cell motility in the brain
    • Mercer, J. A., Albanesi, J. P., and Brady, S. T. (1994). Molecular motors and cell motility in the brain. Brain Pathol. 4, 167-179.
    • (1994) Brain Pathol. , vol.4 , pp. 167-179
    • Mercer, J.A.1    Albanesi, J.P.2    Brady, S.T.3
  • 178
    • 0026758096 scopus 로고
    • Monoclonal antibodies with selective specificity for Alzheimer Tau are directed against phosphatase-sensitive epitopes
    • Mercken, M., Vandermeeren, M., Lubke, U., Six, J., Boons, J., and Vandevoorde, A. (1992). Monoclonal antibodies with selective specificity for Alzheimer Tau are directed against phosphatase-sensitive epitopes. Acta Neuropathol. 84,265-272.
    • (1992) Acta Neuropathol. , vol.84 , pp. 265-272
    • Mercken, M.1    Vandermeeren, M.2    Lubke, U.3    Six, J.4    Boons, J.5    Vandevoorde, A.6
  • 179
    • 0029588380 scopus 로고
    • Three distinct axonal transport rates for tau, tubulin, and other microtubule-associated proteins: Evidence for dynamic interactions of Tau with microtubules in vivo
    • Mercken, M. Fischer, I., Kosik, K. S., and Nixon, R. A. (1995). Three distinct axonal transport rates for tau, tubulin, and other microtubule-associated proteins: Evidence for dynamic interactions of Tau with microtubules in vivo. J. Neurosci. 15, 8259-8267.
    • (1995) J. Neurosci. , vol.15 , pp. 8259-8267
    • Mercken, M.1    Fischer, I.2    Kosik, K.S.3    Nixon, R.A.4
  • 180
    • 0029669963 scopus 로고    scopus 로고
    • Site-specific dephosphorylation of tau protein at Ser(202)/Thr(205) in response to microtubule depolymerization in cultured human neurons involves protein phosphatase 2A
    • Merrick, S. E., Demoise, D. C., and Lee, V. M. Y. (1996). Site-specific dephosphorylation of tau protein at Ser(202)/Thr(205) in response to microtubule depolymerization in cultured human neurons involves protein phosphatase 2A. J. Biol. Chem. 271, 5589-5594.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5589-5594
    • Merrick, S.E.1    Demoise, D.C.2    Lee, V.M.Y.3
  • 181
    • 0028930433 scopus 로고
    • Pancreatic Tau related maps: Biochemical and immunofluorescence analysis in a tumoral cell line
    • Michalik, L., Neuville, P., Vanier, M. T., and Launay, J. F. (1995). Pancreatic Tau related maps: Biochemical and immunofluorescence analysis in a tumoral cell line. Mol. Cell Biochem. 143, 107-112.
    • (1995) Mol. Cell Biochem. , vol.143 , pp. 107-112
    • Michalik, L.1    Neuville, P.2    Vanier, M.T.3    Launay, J.F.4
  • 182
    • 0024327615 scopus 로고
    • Development of Alzheimer neurofibrillary changes in two autopsy cases of myotonic dystrophy
    • Mitake, S., Inagaki, T., Niimi, T., Shirai, T., Yamamoto, M. (1989). Development of Alzheimer neurofibrillary changes in two autopsy cases of myotonic dystrophy. Clin. Neurol. (Tokyo) 29, 488-492.
    • (1989) Clin. Neurol. (Tokyo) , vol.29 , pp. 488-492
    • Mitake, S.1    Inagaki, T.2    Niimi, T.3    Shirai, T.4    Yamamoto, M.5
  • 183
    • 0022347937 scopus 로고
    • Substructure of 20-nm filaments of progressive supranuclear palsy
    • Montpetit, V., Clapin, D. F., and Guberman, A. (1985). Substructure of 20-nm filaments of progressive supranuclear palsy. Acta Neuropathol. 68, 311-318.
    • (1985) Acta Neuropathol. , vol.68 , pp. 311-318
    • Montpetit, V.1    Clapin, D.F.2    Guberman, A.3
  • 184
    • 0023140474 scopus 로고
    • Ubiquitin is a component of paired helical filaments in Alzheimer's disease
    • Mori, H., Kondo, J., and 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
  • 185
    • 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., and 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
  • 188
    • 0028785002 scopus 로고
    • Tau protein immunoreactivity in muscle fibers with rimmed vacuoles differs from that in regenerating muscle fibers
    • Murakami, N., Ishiguro, K., Ihara, Y., Nonaka, L, Sugita, H., and Imahori, K. (1995). Tau protein immunoreactivity in muscle fibers with rimmed vacuoles differs from that in regenerating muscle fibers. Acta Neuropalhol. 90, 467-471.
    • (1995) Acta Neuropalhol. , vol.90 , pp. 467-471
    • Murakami, N.1    Ishiguro, K.2    Ihara, Y.3    Nonaka, L.4    Sugita, H.5    Imahori, K.6
  • 189
    • 0029058568 scopus 로고
    • Ultrastructure of neurofibrillary tangles in the cerebral cortex of sheep
    • Nelson, P. T., and Safer, C. B. (1995). Ultrastructure of neurofibrillary tangles in the cerebral cortex of sheep. Neurobiol. Aging. 16, 315-323.
    • (1995) Neurobiol. Aging. , vol.16 , pp. 315-323
    • Nelson, P.T.1    Safer, C.B.2
  • 190
    • 0029161127 scopus 로고
    • In situ localization with digoxigenin-labelled probes of tau-related mRNAs in the rat pancreas
    • Neuville, P., Vanier, M. T., Michalik, L., and Launay, J. F. (1995). In situ localization with digoxigenin-labelled probes of tau-related mRNAs in the rat pancreas. Histochem. J. 27, 565-574.
    • (1995) Histochem. J. , vol.27 , pp. 565-574
    • Neuville, P.1    Vanier, M.T.2    Michalik, L.3    Launay, J.F.4
  • 191
    • 0022827447 scopus 로고
    • Identification of cDNA clones for the human microtubule-associated protein Tau and chromosmal location of genes for Tau and microtubule-associated protein 2
    • Neve, R. L., Harris, P., Kosik, K., Kurnit, D. M., and Donlon, A. (1986). Identification of cDNA clones for the human microtubule-associated protein Tau and chromosmal location of genes for Tau and microtubule-associated protein 2. Mol Brain Res I, 271-280.
    • (1986) Mol Brain Res I , pp. 271-280
    • Neve, R.L.1    Harris, P.2    Kosik, K.3    Kurnit, D.M.4    Donlon, A.5
  • 192
    • 0025828989 scopus 로고
    • Tau-related protein present in paired helical filaments has a decreased tubulin binding capacity as compared with microtubule-associated protein tau
    • Nieto, A., Correas, I., Lopezotin, C, and Avila, J. (1991). Tau-related protein present in paired helical filaments has a decreased tubulin binding capacity as compared with microtubule-associated protein tau. Biochim. Biophys. Acta 1096, 197-204.
    • (1991) Biochim. Biophys. Acta , vol.1096 , pp. 197-204
    • Nieto, A.1    Correas, I.2    Lopezotin, C.3    Avila, J.4
  • 193
    • 0029071320 scopus 로고
    • Immunocytochemical characterization of glial fibrillary tangles in Alzheimer's disease brain
    • Nishimura, M., Tomimoto, H., Suenaga, T., Namba, Y., Ikeda, K., Akiguchi, I., and Kimura, J. (1995). Immunocytochemical characterization of glial fibrillary tangles in Alzheimer's disease brain. Am. J. Pathol. 146,1052-1058.
    • (1995) Am. J. Pathol. , vol.146 , pp. 1052-1058
    • Nishimura, M.1    Tomimoto, H.2    Suenaga, T.3    Namba, Y.4    Ikeda, K.5    Akiguchi, I.6    Kimura, J.7
  • 194
    • 0028937904 scopus 로고
    • Expression of tau-like microtubule-associated proteins in calcitonin-producing cells
    • Nishiyama, I., Oota, T., and Ogiso, M. (1995). Expression of tau-like microtubule-associated proteins in calcitonin-producing cells. Biomed. Res. 16, 59-62.
    • (1995) Biomed. Res. , vol.16 , pp. 59-62
    • Nishiyama, I.1    Oota, T.2    Ogiso, M.3
  • 195
    • 0023270888 scopus 로고
    • Neuropathological changes of the brain in myotonic dystrophy. Some new observations
    • Ono, S., Inoue, K., Mannen, T., Kanda, F., Jinnai, K., and Takahashi, K. (1987). Neuropathological changes of the brain in myotonic dystrophy. Some new observations. J. Neural. Sei. 81, 301-320.
    • (1987) J. Neural. Sei. , vol.81 , pp. 301-320
    • Ono, S.1    Inoue, K.2    Mannen, T.3    Kanda, F.4    Jinnai, K.5    Takahashi, K.6
  • 197
    • 0028593606 scopus 로고
    • Monoclonal antibody PHF-1 recognizes Tau protein phosphorylated at serine residues 396 and 404
    • Otvos, L., Feiner, L., Lang, E., Szendrei, G. I., Goedert, M., and Lee, V. M. Y. (1994). Monoclonal antibody PHF-1 recognizes Tau protein phosphorylated at serine residues 396 and 404. J. Neurosd. Res. 39, 669-673.
    • (1994) J. Neurosd. Res. , vol.39 , pp. 669-673
    • Otvos, L.1    Feiner, L.2    Lang, E.3    Szendrei, G.I.4    Goedert, M.5    Lee, V.M.Y.6
  • 198
    • 85030283761 scopus 로고    scopus 로고
    • Nonneuronal tau, transient upregulation and subsequent accumulation of big Tau and small Tau in chloroquine neuropathy
    • [Abstract 759]
    • Oyama, F., Gu, Y., Murakami, N., Nonaka, I., and Ihara, Y. (1996). Nonneuronal tau, transient upregulation and subsequent accumulation of big Tau and small Tau in chloroquine neuropathy. Neurobiol. Aging 17(Suppl. 4), S188. [Abstract 759]
    • (1996) Neurobiol. Aging , vol.17 , Issue.4 SUPPL.
    • Oyama, F.1    Gu, Y.2    Murakami, N.3    Nonaka, I.4    Ihara, Y.5
  • 199
    • 0028696957 scopus 로고
    • Topographic investigation of brain atrophy in Parkinsonism dementia complex of Guam: A comparison with Alzheimer's disease and progressive supranuclear palsy
    • Oyanagi, K., Makifushi, T., Ohtoh, T., Ikuta, F., Chen, K. M., Chase, T. N., and Gajdusek, D. C. (1994). Topographic investigation of brain atrophy in Parkinsonism dementia complex of Guam: A comparison with Alzheimer's disease and progressive supranuclear palsy. Neurodegeneration 3, 301-304.
    • (1994) Neurodegeneration , vol.3 , pp. 301-304
    • Oyanagi, K.1    Makifushi, T.2    Ohtoh, T.3    Ikuta, F.4    Chen, K.M.5    Chase, T.N.6    Gajdusek, D.C.7
  • 200
    • 0029098802 scopus 로고
    • Kinetic stabilization of microtubule dynamics at steady state by Tau and microtubule-binding domains of tau
    • Panda, D., Goode, B. L., Feinstein, S. C., and Wilson, L. (1995). Kinetic stabilization of microtubule dynamics at steady state by Tau and microtubule-binding domains of tau. Biochemistry 34, 11117-11127.
    • (1995) Biochemistry , vol.34 , pp. 11117-11127
    • Panda, D.1    Goode, B.L.2    Feinstein, S.C.3    Wilson, L.4
  • 201
    • 0030065109 scopus 로고    scopus 로고
    • Heat shock induces rapid dephosphorylation of Tau in both female and male rats followed by hyperphosphorylation only in female rats: Implications for Alzheimer's disease
    • Papasozomenos, S. C. (1996). Heat shock induces rapid dephosphorylation of Tau in both female and male rats followed by hyperphosphorylation only in female rats: Implications for Alzheimer's disease. J. Neurochem. 66,1140-1149.
    • (1996) J. Neurochem. , vol.66 , pp. 1140-1149
    • Papasozomenos, S.C.1
  • 202
    • 0023907603 scopus 로고
    • Alzheimer's disease: Study of the distribution of paired helical filaments tau proteins in the human central nervous system
    • Parent, M., Delacourte, A., Défossez, A., Hémon, B., Han, K-K., and Petit, H. (1988). Alzheimer's disease: Study of the distribution of paired helical filaments tau proteins in the human central nervous system. C. R. Acad. Sei. 306, 391-397.
    • (1988) C. R. Acad. Sei. , vol.306 , pp. 391-397
    • Parent, M.1    Delacourte, A.2    Défossez, A.3    Hémon, B.4    Han, K.-K.5    Petit, H.6
  • 203
    • 0025184284 scopus 로고
    • Corticonigral degeneration with neuronal achromasia and basal neurofibrillary tangles
    • Paulus, W., and Selim, M. (1990). Corticonigral degeneration with neuronal achromasia and basal neurofibrillary tangles. Acta Neuropathol. 81, 89-94.
    • (1990) Acta Neuropathol. , vol.81 , pp. 89-94
    • Paulus, W.1    Selim, M.2
  • 204
    • 0028922172 scopus 로고
    • Neuropsychological pattern of striatonigral degeneration: Comparison with Parkinson's disease and progressive supranuclear palsy
    • Pillon, B., Gouiderkhouja, N., Deweer, B., Vidailhet, M., Malapani, C, Dubois, B., and Agid, Y. (1995). Neuropsychological pattern of striatonigral degeneration: Comparison with Parkinson's disease and progressive supranuclear palsy. J. Neural. Neurosurg. Ps. 58,174-179.
    • (1995) J. Neural. Neurosurg. Ps. , vol.58 , pp. 174-179
    • Pillon, B.1    Gouiderkhouja, N.2    Deweer, B.3    Vidailhet, M.4    Malapani, C.5    Dubois, B.6    Agid, Y.7
  • 205
    • 0029043272 scopus 로고
    • Inhibition of glutamate-induced neurotoxicity by a Tau antisense oligonucleotide in primary culture of rat cerebellar granule cells
    • Pizzi, M., Valerio, A., Arrighi, V., Galli, P., Belloni, M., Ribola, M., Alberici, A., Spano, P., and Memo, M. (1995). Inhibition of glutamate-induced neurotoxicity by a Tau antisense oligonucleotide in primary culture of rat cerebellar granule cells. Eur. Neurosci. 7,1603-1613.
    • (1995) Eur. Neurosci. , vol.7 , pp. 1603-1613
    • Pizzi, M.1    Valerio, A.2    Arrighi, V.3    Galli, P.4    Belloni, M.5    Ribola, M.6    Alberici, A.7    Spano, P.8    Memo, M.9
  • 206
    • 0029618124 scopus 로고
    • Apolipoprotein E, synaptic plasticity and Alzheimer's disease
    • Poirier, J., Minnich, A., and Davignon, J. (1995). Apolipoprotein E, synaptic plasticity and Alzheimer's disease. Ann. Med. 27, 663-670.
    • (1995) Ann. Med. , vol.27 , pp. 663-670
    • Poirier, J.1    Minnich, A.2    Davignon, J.3
  • 207
    • 0020607502 scopus 로고
    • Phosphorylation of microtubule-associated proteins regulates their interaction with actin filaments
    • Pollard, T. D. (1983). Phosphorylation of microtubule-associated proteins regulates their interaction with actin filaments. J. Biol. Chem. 258, 7064-7067.
    • (1983) J. Biol. Chem. , vol.258 , pp. 7064-7067
    • Pollard, T.D.1
  • 208
    • 0027509787 scopus 로고
    • Phosphorylated Tau epitope of Alzheimer's disease is coupled to axon development in the avian central nervous system
    • Pope, W., Enam, S. A., Bawa, N., Miller, B. E., Ghanbari, H. A., and Klein, W. L. (1993). Phosphorylated Tau epitope of Alzheimer's disease is coupled to axon development in the avian central nervous system. Exp. Neural. 120, 106-113.
    • (1993) Exp. Neural. , vol.120 , pp. 106-113
    • Pope, W.1    Enam, S.A.2    Bawa, N.3    Miller, B.E.4    Ghanbari, H.A.5    Klein, W.L.6
  • 209
    • 0030049915 scopus 로고    scopus 로고
    • Filament heterogeneity within the dystrophic neurites of senile plaques suggests blockage of fast axonal transport in Alzheimer's disease
    • Praprotnik, D., Smith, M. A., Richey, P. L., Vinters, H. V., and Perry, G. (1996). Filament heterogeneity within the dystrophic neurites of senile plaques suggests blockage of fast axonal transport in Alzheimer's disease. Acta Neuropathol. 91, 226-235.
    • (1996) Acta Neuropathol. , vol.91 , pp. 226-235
    • Praprotnik, D.1    Smith, M.A.2    Richey, P.L.3    Vinters, H.V.4    Perry, G.5
  • 210
    • 0028861792 scopus 로고
    • Complementary distribution of Tau proteins in different phosphorylation states within growing axons
    • Rebhan, M., Vacun, G., and Rosner, H. (1995). Complementary distribution of Tau proteins in different phosphorylation states within growing axons. Neuroreport 6, 429-432.
    • (1995) Neuroreport , vol.6 , pp. 429-432
    • Rebhan, M.1    Vacun, G.2    Rosner, H.3
  • 211
    • 0025327761 scopus 로고
    • Interaction of microtubules and microtubule-associated proteins (MAPs) with rat brain mitochondria
    • Rendeon, A. D., Jung, D., and Jancsik, V. (1990). Interaction of microtubules and microtubule-associated proteins (MAPs) with rat brain mitochondria. Biochem. J. 269, 555-556.
    • (1990) Biochem. J. , vol.269 , pp. 555-556
    • Rendeon, A.D.1    Jung, D.2    Jancsik, V.3
  • 212
    • 0029026860 scopus 로고
    • Association of mitogen-activated protein kinase with the microtubule cytoskeleton
    • Reszka, A. A., Seger, R., Diltz, C. D., Krebs, E. G., and Fischer, E. H. (1995). Association of mitogen-activated protein kinase with the microtubule cytoskeleton. Proc. Natl. Acad. Sei. USA 92, 8881-8885.
    • (1995) Proc. Natl. Acad. Sei. USA , vol.92 , pp. 8881-8885
    • Reszka, A.A.1    Seger, R.2    Diltz, C.D.3    Krebs, E.G.4    Fischer, E.H.5
  • 213
    • 0010436038 scopus 로고
    • Degenerative diseases of the central nervous system
    • R. L. Davis and D. M. Robertson, Eds., Williams & Wilkins, Baltimore.
    • Rewcastle, N. B. (1991). Degenerative diseases of the central nervous system. In "Textbook of Neuropathology, second edition" (R. L. Davis and D. M. Robertson, Eds.), pp. 903-961. Williams & Wilkins, Baltimore.
    • (1991) Textbook of Neuropathology, Second Edition , pp. 903-961
    • Rewcastle, N.B.1
  • 214
    • 0027359507 scopus 로고
    • Differential distribution of Tau proteins in developing cat cerebellum
    • Riederer, B. M., and Binder, L. I. (1994). Differential distribution of Tau proteins in developing cat cerebellum. Brain Res. Bull. 33, 155-161.
    • (1994) Brain Res. Bull. , vol.33 , pp. 155-161
    • Riederer, B.M.1    Binder, L.I.2
  • 215
    • 0027947563 scopus 로고
    • Corticobasal degeneration: A clinical study of 36 cases
    • Rinne, J. O., Lee, M. S., Thompson, P. D., and Marsden, C. D. (1994). Corticobasal degeneration: A clinical study of 36 cases. Brain 117,1183-1196.
    • (1994) Brain , vol.117 , pp. 1183-1196
    • Rinne, J.O.1    Lee, M.S.2    Thompson, P.D.3    Marsden, C.D.4
  • 216
    • 0029156358 scopus 로고
    • Developmental expression of Tau proteins in the chicken and rat brain: Rapid down-regulation of a paired helical filament epitope in the rat cerebral cortex coincides with the transition from immature to adult Tau isoforms
    • Rosner, H., Rebhan, M., Vacun, G., and Vanmechelen, E. (1995). Developmental expression of Tau proteins in the chicken and rat brain: Rapid down-regulation of a paired helical filament epitope in the rat cerebral cortex coincides with the transition from immature to adult Tau isoforms. Int. J. Dev. Neurosci. 13, 607-617.
    • (1995) Int. J. Dev. Neurosci. , vol.13 , pp. 607-617
    • Rosner, H.1    Rebhan, M.2    Vacun, G.3    Vanmechelen, E.4
  • 217
    • 0029933181 scopus 로고    scopus 로고
    • Identification of a Tau promoter region mediating tissue-specific-regulated expression in PC12 cells
    • Sadot, E., Heicklenklein, A., Barg, J., Behar, L., Ginzburg, I., and Fisher, A. (1996a). Identification of a Tau promoter region mediating tissue-specific-regulated expression in PC12 cells. J. Mol. Biol. 256, 805-812.
    • (1996) J. Mol. Biol. , vol.256 , pp. 805-812
    • Sadot, E.1    Heicklenklein, A.2    Barg, J.3    Behar, L.4    Ginzburg, I.5    Fisher, A.6
  • 218
    • 0029670637 scopus 로고    scopus 로고
    • Activation of m(1) muscarinic acetylcholine receptor regulates Tau phosphorylation in transfected PC12 cells
    • Sadot, E., Gunvitz, D. B., Lazarovici, P., and Ginzburg, I. (1996b). Activation of m(1) muscarinic acetylcholine receptor regulates Tau phosphorylation in transfected PC12 cells. J. Neurochem. 66, 877-880.
    • (1996) J. Neurochem. , vol.66 , pp. 877-880
    • Sadot, E.1    Gunvitz, D.B.2    Lazarovici, P.3    Ginzburg, I.4
  • 219
    • 0028865376 scopus 로고
    • In situ dephosphorylation of Tau by protein phosphatase 2A and 2B in fetal rat primary cultured neurons
    • Saito, T., Ishiguro, K., Uchida, T., Miyamoto, E., Kishimoto, T., and Hisanaga, S. (1995). In situ dephosphorylation of Tau by protein phosphatase 2A and 2B in fetal rat primary cultured neurons. FEES Lett. 376, 238-242.
    • (1995) FEES Lett. , vol.376 , pp. 238-242
    • Saito, T.1    Ishiguro, K.2    Uchida, T.3    Miyamoto, E.4    Kishimoto, T.5    Hisanaga, S.6
  • 220
    • 0028887946 scopus 로고
    • Stabilization and bundling of subtilisin-treated microtubules induced by microtubule associated proteins
    • Saoudi, Y., Paintrand, I., Multigner, L., and Job, D. (1995). Stabilization and bundling of subtilisin-treated microtubules induced by microtubule associated proteins. J. Cell Sci. 108, 357-367.
    • (1995) J. Cell Sci. , vol.108 , pp. 357-367
    • Saoudi, Y.1    Paintrand, I.2    Multigner, L.3    Job, D.4
  • 221
    • 0019421552 scopus 로고
    • Microtubule-associated proteins (MAPs) and the organization of actin filaments in vitro
    • Sattilaro, R. F., Dentier, W. L.; and LeChuyse, E. L. (1981). Microtubule-associated proteins (MAPs) and the organization of actin filaments in vitro. J. Cell Biol. 90, 467-473.
    • (1981) J. Cell Biol. , vol.90 , pp. 467-473
    • Sattilaro, R.F.1    Dentier, W.L.2    Lechuyse, E.L.3
  • 222
    • 0002090729 scopus 로고
    • Detection of Alzheimer-type Tau proteins in okadaic acid-treated Sknsh-Sy 5Y neuroblastoma cells
    • Sautière, P. E., Caillet-Boudin, M. L., Wattez, A., and Delacourte, A. (1994). Detection of Alzheimer-type Tau proteins in okadaic acid-treated Sknsh-Sy 5Y neuroblastoma cells. Neurodegeneration 3, 53-60.
    • (1994) Neurodegeneration , vol.3 , pp. 53-60
    • Sautière, P.E.1    Caillet-Boudin, M.L.2    Wattez, A.3    Delacourte, A.4
  • 223
    • 0028097327 scopus 로고
    • Molecular diversity at the carboxyl terminus of human and rat Tau
    • Sawa, A., Oyama, F., Matsushita, M., et al. (1994). Molecular diversity at the carboxyl terminus of human and rat Tau. Mol. Brain Res. 27, 111-117.
    • (1994) Mol. Brain Res. , vol.27 , pp. 111-117
    • Sawa, A.1    Oyama, F.2    Matsushita, M.3
  • 224
    • 0028174753 scopus 로고
    • Extensive network of PHF tau-rich dystrophic neuntes permeates neocortex and nearly all neuritic and diffuse amyloid plaques in Alzheimer disease
    • Schmidt, M. L., Didario, A. G., Lee, V. M. Y., and Trojanowski, J. Q. (1994). Extensive network of PHF tau-rich dystrophic neuntes permeates neocortex and nearly all neuritic and diffuse amyloid plaques in Alzheimer disease. FEBS Lett. 344, 69-73.
    • (1994) FEBS Lett. , vol.344 , pp. 69-73
    • Schmidt, M.L.1    Didario, A.G.2    Lee, V.M.Y.3    Trojanowski, J.Q.4
  • 227
    • 0027936669 scopus 로고
    • Diverse distribution and function of fibrous microtubule-associated proteins in the nervous system
    • Schoenfeld, T. A., and Obar, R. A. (1994). Diverse distribution and function of fibrous microtubule-associated proteins in the nervous system. Int. Rev. Cytol. 151, 67-137.
    • (1994) Int. Rev. Cytol. , vol.151 , pp. 67-137
    • Schoenfeld, T.A.1    Obar, R.A.2
  • 228
    • 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, E. M., Biernat, J., and Mandelkow, E. (1995). Oxidation of cysteine-322 in the repeat domain of microtubule-associated protein Tau controls the in vitro assembly of paired helical filaments. Proc. Nail. Acad. Sei USA 92, 8463-8467.
    • (1995) Proc. Nail. Acad. Sei USA , vol.92 , pp. 8463-8467
    • Schweers, O.1    Mandelkow, E.M.2    Biernat, J.3    Mandelkow, E.4
  • 229
    • 0028803726 scopus 로고
    • Isoelectric point differentiates PHF-Tau from biopsy-derived human brain Tau proteins
    • Sergeant, N., Bussiere, T., Vermersch, P.., Lejeune, J. P., and Delacourte, A. (1995). Isoelectric point differentiates PHF-Tau from biopsy-derived human brain Tau proteins. Neuroreport 6, 2217-2220.
    • (1995) Neuroreport , vol.6 , pp. 2217-2220
    • Sergeant, N.1    Bussiere, T.2    Vermersch, P.3    Lejeune, J.P.4    Delacourte, A.5
  • 231
    • 0030033901 scopus 로고    scopus 로고
    • Changes in phosphorylation of Tau during ischemia and reperfusion in the rabbit spinal cord
    • Shackelford, D. A., and Nelson, K. E. (1996). Changes in phosphorylation of Tau during ischemia and reperfusion in the rabbit spinal cord. J. Neurochem. 66, 286-295.
    • (1996) J. Neurochem. , vol.66 , pp. 286-295
    • Shackelford, D.A.1    Nelson, K.E.2
  • 232
    • 0024589232 scopus 로고
    • Immunocytochemical characterization of neurofibrillary tangles in amyotrophic lateral sclerosis and Parkinsonism-Dementia of Guam
    • Shankar, S. K., Yanagihara, R. M., Garruto, I., Grundke-Iqbal, K. S., Kosik, D. C, and Gajdusek, C. (1989). Immunocytochemical characterization of neurofibrillary tangles in amyotrophic lateral sclerosis and Parkinsonism-Dementia of Guam. Ann. Neural. 25, 146-151.
    • (1989) Ann. Neural. , vol.25 , pp. 146-151
    • Shankar, S.K.1    Yanagihara, R.M.2    Garruto, I.3    Grundke-Iqbal, K.S.4    Kosik, D.C.5    Gajdusek, C.6
  • 233
    • 0030046767 scopus 로고    scopus 로고
    • Phosphatase inhibition in human neuroblastoma cells alters Tau antigenicity and renders it incompetent to associate with exogenous microtubules
    • Shea, T. B., and Fischer, I. (1996). Phosphatase inhibition in human neuroblastoma cells alters Tau antigenicity and renders it incompetent to associate with exogenous microtubules. FEBS Lett. 380, 63-67.
    • (1996) FEBS Lett. , vol.380 , pp. 63-67
    • Shea, T.B.1    Fischer, I.2
  • 234
    • 0026693034 scopus 로고
    • Microtubule-associated protein tau is required for axonal neurite elaboration by neuroblastoma cells
    • Shea, T. B., Beermann, M. L., Nixon, R. A., and Fischer, I. (1992). Microtubule-associated protein tau is required for axonal neurite elaboration by neuroblastoma cells. J. Neurosci. Res. 32, 363-374.
    • (1992) J. Neurosci. Res. , vol.32 , pp. 363-374
    • Shea, T.B.1    Beermann, M.L.2    Nixon, R.A.3    Fischer, I.4
  • 235
    • 0028848032 scopus 로고
    • Amino acid phosphatase activity of alkaline phosphatase-A possible role of protein phosphatase
    • Shinozaki, T., Watanabe, H., Arita, S., and Chigira, M. (1995). Amino acid phosphatase activity of alkaline phosphatase-A possible role of protein phosphatase. Eur. J. Biochem. 227, 367-371.
    • (1995) Eur. J. Biochem. , vol.227 , pp. 367-371
    • Shinozaki, T.1    Watanabe, H.2    Arita, S.3    Chigira, M.4
  • 236
    • 0030067749 scopus 로고    scopus 로고
    • Non-proline-dependent protein kinases phosphorylate several sites found in Tau from Alzheimer disease brain
    • Singh, T. J., Zaidi, T., Grundke-Iqbal., and Iqbal, K. (1996). Non-proline-dependent protein kinases phosphorylate several sites found in Tau from Alzheimer disease brain. Mol. Cell. Biochem. 154, 143-151.
    • (1996) Mol. Cell. Biochem. , vol.154 , pp. 143-151
    • Singh, T.J.1    Zaidi, T.2    Grundke-Iqbal3    Iqbal, K.4
  • 239
    • 0028918921 scopus 로고
    • Tau protein kinase I/GSK-3 beta/kinase F-A in heparin phosphorylates Tau on Ser(199), Thr(231), Ser(235), Ser(262) Ser(369), and Ser(400) sites phosphorylated in Alzheimer disease brain
    • Song, J. S., and Yang, S. D. (1995). Tau protein kinase I/GSK-3 beta/kinase F-A in heparin phosphorylates Tau on Ser(199), Thr(231), Ser(235), Ser(262) Ser(369), and Ser(400) sites phosphorylated in Alzheimer disease brain. J. Protein Client. 14, 95-105.
    • (1995) J. Protein Client. , vol.14 , pp. 95-105
    • Song, J.S.1    Yang, S.D.2
  • 240
    • 0028924295 scopus 로고
    • A novel pool of protein phosphatase 2A is associated with microtubules and is regulated during the cell cycle
    • Sontag, E., Nunbhakdicraig, V., Bloom, G. S., and Mumby, M. C. (1995). A novel pool of protein phosphatase 2A is associated with microtubules and is regulated during the cell cycle. J. Cell Biol. 128, 1131-1144.
    • (1995) J. Cell Biol. , vol.128 , pp. 1131-1144
    • Sontag, E.1    Nunbhakdicraig, V.2    Bloom, G.S.3    Mumby, M.C.4
  • 241
    • 17344377502 scopus 로고    scopus 로고
    • Dephosphorylation studies of SKNSH-Sy 5Y cell Tau proteins by endogenous phosphatase activity
    • Soulié, C, Lepagnol, J., Delacourte, A., and Caillet-Boudin M. L. (1996). Dephosphorylation studies of SKNSH-Sy 5Y cell Tau proteins by endogenous phosphatase activity. Neurosci. Lett. 206,189-192.
    • (1996) Neurosci. Lett. , vol.206 , pp. 189-192
    • Soulié, C.1    Lepagnol, J.2    Delacourte, A.3    Caillet-Boudin, M.L.4
  • 242
    • 0028981873 scopus 로고
    • Glycogen synthase kinase-3 beta phosphorylates Tau protein at multiple sites in intact cells
    • Sperber, B. R., Leight, S., Goedert, M., and Lee, V. M. Y. (1995). Glycogen synthase kinase-3 beta phosphorylates Tau protein at multiple sites in intact cells. Neurosd. Lett. 197,149-153.
    • (1995) Neurosd. Lett. , vol.197 , pp. 149-153
    • Sperber, B.R.1    Leight, S.2    Goedert, M.3    Lee, V.M.Y.4
  • 243
    • 0030000867 scopus 로고    scopus 로고
    • Comparison of the neurofibrillary pathology in Alzheimer's disease and familial presenile dementia with tangles
    • Spillantini, M. G., Crowther, R. A., and Goedert, M. (1996). Comparison of the neurofibrillary pathology in Alzheimer's disease and familial presenile dementia with tangles. Acta Neuropathol. 92, 42-48.
    • (1996) Acta Neuropathol. , vol.92 , pp. 42-48
    • Spillantini, M.G.1    Crowther, R.A.2    Goedert, M.3
  • 244
    • 75549116708 scopus 로고
    • Progressive supranuclear palsy. A heterogeneous degeneration involving brain stem, basal ganglia and cerebellum with vertical gaze and pseudobulbar palsy, nuchal dystonia and dementia
    • Steele, J. C., Richardson, J. C., and Olzewski, J. (1964). Progressive supranuclear palsy. A heterogeneous degeneration involving brain stem, basal ganglia and cerebellum with vertical gaze and pseudobulbar palsy, nuchal dystonia and dementia. Arch. Neural. 10, 333-359.
    • (1964) Arch. Neural. , vol.10 , pp. 333-359
    • Steele, J.C.1    Richardson, J.C.2    Olzewski, J.3
  • 246
    • 0030044463 scopus 로고    scopus 로고
    • Exposure of rat hippocampal neurons to amyloid beta peptide (25-35) induces the inactivation of phosphatidyl inositol-3 kinase and the activation of Tau protein kinase I glycogen synthase kinase-3 beta
    • Takashima, A., Noguchi, K., Michel, G., Mercken, M., Hoshi, M., Ishiguro, K., and Imahori, K. (1996). Exposure of rat hippocampal neurons to amyloid beta peptide (25-35) induces the inactivation of phosphatidyl inositol-3 kinase and the activation of Tau protein kinase I glycogen synthase kinase-3 beta. Neurosd. Lett. 203, 33-36.
    • (1996) Neurosd. Lett. , vol.203 , pp. 33-36
    • Takashima, A.1    Noguchi, K.2    Michel, G.3    Mercken, M.4    Hoshi, M.5    Ishiguro, K.6    Imahori, K.7
  • 249
    • 0015738782 scopus 로고
    • Ultrastructure of neurofibrillary tangles in Steele-Richardson-Olszewski syndrome
    • Tellez-Nagel, I., and Wisniewski, H. M. (1973). Ultrastructure of neurofibrillary tangles in Steele-Richardson-Olszewski syndrome. Arch. Neural. 29, 324-327.
    • (1973) Arch. Neural. , vol.29 , pp. 324-327
    • Tellez-Nagel, I.1    Wisniewski, H.M.2
  • 250
    • 0017581518 scopus 로고
    • Ultrastructure of neurofibrillary tangles in progressive supranuclear palsy
    • Tomonaga, M. (1977). Ultrastructure of neurofibrillary tangles in progressive supranuclear palsy. Acta Neuropathol. 37, 177-181.
    • (1977) Acta Neuropathol. , vol.37 , pp. 177-181
    • Tomonaga, M.1
  • 252
    • 0026409455 scopus 로고
    • Clinical aspects of Niemann-Pick type C disease in the adult
    • Turpin, J. C, Masson, M., and Baumann, N. (1991). Clinical aspects of Niemann-Pick type C disease in the adult. Dev. Neurosd. 13, 304-306.
    • (1991) Dev. Neurosd. , vol.13 , pp. 304-306
    • Turpin, J.C.1    Masson, M.2    Baumann, N.3
  • 253
    • 0027309539 scopus 로고
    • The phosphatase inhibitor okadaic acid induces a phosphorylated paired helical filament Tau-Epitope in human LA-N-5 neuroblastoma cells
    • Vandermeeren, M., Lubke, U., Six, J., and Cras, P. (1993). The phosphatase inhibitor okadaic acid induces a phosphorylated paired helical filament Tau-Epitope in human LA-N-5 neuroblastoma cells. Neurosd. Lett. 153, 57-60.
    • (1993) Neurosd. Lett. , vol.153 , pp. 57-60
    • Vandermeeren, M.1    Lubke, U.2    Six, J.3    Cras, P.4
  • 254
    • 0026756330 scopus 로고
    • Presence of abnormally phosphorylated Tau proteins in the entorhinal cortex of aged Non-Demented subjects
    • Vermersch, P., Frigard, B., David, J. P., Fallet-Bianco, C., and Delacourte, A. (1992). Presence of abnormally phosphorylated Tau proteins in the entorhinal cortex of aged Non-Demented subjects. Neurosd. Lett. 144, 143-146.
    • (1992) Neurosd. Lett. , vol.144 , pp. 143-146
    • Vermersch, P.1    Frigard, B.2    David, J.P.3    Fallet-Bianco, C.4    Delacourte, A.5
  • 255
    • 0027178388 scopus 로고
    • Dementia in Parkinson's disease-Biochemical evidence for cortical involvement using the immunodetection of abnormal Tau-Proteins
    • Vermersch, P., Delacourte, A., Javoy-Agid, F., Hauw, J. J., and Agid, Y. (1993). Dementia in Parkinson's disease-Biochemical evidence for cortical involvement using the immunodetection of abnormal Tau-Proteins. Ann. Neural. 33, 445-450.
    • (1993) Ann. Neural. , vol.33 , pp. 445-450
    • Vermersch, P.1    Delacourte, A.2    Javoy-Agid, F.3    Hauw, J.J.4    Agid, Y.5
  • 256
    • 0028283573 scopus 로고
    • Biochemical mapping of neurofibrillary degeneration in a case of progressive supranuclear palsy: Evidence for general cortical involvement
    • Vermersch, P., Robitaille, Y., Bernier, L., Wattez, A., Gauvreau, D., and Delacourte, A. (1994). Biochemical mapping of neurofibrillary degeneration in a case of progressive supranuclear palsy: Evidence for general cortical involvement. Acta Neuropathol. 87, 572-577.
    • (1994) Acta Neuropathol. , vol.87 , pp. 572-577
    • Vermersch, P.1    Robitaille, Y.2    Bernier, L.3    Wattez, A.4    Gauvreau, D.5    Delacourte, A.6
  • 260
    • 0030062245 scopus 로고    scopus 로고
    • Mitotic mechanisms in Alzheimer's disease?
    • Vincent, I., Rosado, M., and Davies, P. (1996). Mitotic mechanisms in Alzheimer's disease? J. Cell Biol. 132, 413-425.
    • (1996) J. Cell Biol. , vol.132 , pp. 413-425
    • Vincent, I.1    Rosado, M.2    Davies, P.3
  • 261
  • 264
    • 0026543843 scopus 로고
    • Appearance of paired nucleated, taupositive glia in progressive supranuclear palsy brain tissue
    • Yamada, T., McGeer, P. L., and McGeer, E. G. (1992). Appearance of paired nucleated, taupositive glia in progressive supranuclear palsy brain tissue. Neurosci. Lett. 135, 99-102.
    • (1992) Neurosci. Lett. , vol.135 , pp. 99-102
    • Yamada, T.1    McGeer, P.L.2    McGeer, E.G.3
  • 265
    • 0023933407 scopus 로고
    • Dephosphorylation of microtubule proteins by brain protein phosphatases 1 and 2A, and its effect on microtubule assembly
    • Yamamoto, H., Saitoh, Y., Fukunaga, K., Nishimura, H., and Miyamoto, E. (1988). Dephosphorylation of microtubule proteins by brain protein phosphatases 1 and 2A, and its effect on microtubule assembly. J. Neurochem. 50, 1614-1623.
    • (1988) J. Neurochem. , vol.50 , pp. 1614-1623
    • Yamamoto, H.1    Saitoh, Y.2    Fukunaga, K.3    Nishimura, H.4    Miyamoto, E.5
  • 266
    • 0029416987 scopus 로고
    • Dephosphorylation of fetal-Tau and paired helical filaments-Tau by protein phosphatases 1 and 2A and calcineurin
    • Yamamoto, H., Hasegawa, M., Ono, T., Tashima, K., Ihara, Y., and Miyamoto, E. (1995). Dephosphorylation of fetal-Tau and paired helical filaments-Tau by protein phosphatases 1 and 2A and calcineurin. J. Biochem. 118, 1224-1231.
    • (1995) J. Biochem. , vol.118 , pp. 1224-1231
    • Yamamoto, H.1    Hasegawa, M.2    Ono, T.3    Tashima, K.4    Ihara, Y.5    Miyamoto, E.6
  • 267
    • 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., Kaieda, R., and Terashi, A. (1995). Paired helical filaments and straight tubules in astrocytes: An electron microscopic study in dementia of the Alzheimer type. Acta Neuropathol. 90, 31-36.
    • (1995) Acta Neuropathol. , vol.90 , pp. 31-36
    • Yamazaki, M.1    Nakano, I.2    Imazu, O.3    Kaieda, R.4    Terashi, A.5
  • 268
    • 0029076397 scopus 로고
    • Nonenzymatically glycated Tau in Alzheimer's disease induces neuronal ozidant stress resulting in cytokine gene expression and release of amyloid beta-peptide
    • Yan, S. D., Yan, S. F., Chen, X., Fu, J., Chen, M., Kuppusamy, P., Smith, M. A., Perry, G., Godman, G. C., Nawroth, P., Zweiter, J. L., and Stern, D. (1995). Nonenzymatically glycated Tau in Alzheimer's disease induces neuronal ozidant stress resulting in cytokine gene expression and release of amyloid beta-peptide. Nature Med. 1, 693-699.
    • (1995) Nature Med. , vol.1 , pp. 693-699
    • Yan, S.D.1    Yan, S.F.2    Chen, X.3    Fu, J.4    Chen, M.5    Kuppusamy, P.6    Smith, M.A.7    Perry, G.8    Godman, G.C.9    Nawroth, P.10    Zweiter, J.L.11    Stern, D.12


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