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Volumn 2, Issue 2, 2002, Pages 131-150

Tau and axonopathy in neurodegenerative disorders

Author keywords

Alzheimer's disease; Axonal transport microtubules; Tau; Tauopathies

Indexed keywords

MICROTUBULE ASSOCIATED PROTEIN; PHOSPHOPROTEIN PHOSPHATASE; PROTEIN KINASE; TAU PROTEIN;

EID: 0036052388     PISSN: 15351084     EISSN: None     Source Type: Journal    
DOI: 10.1385/NMM:2:2:131     Document Type: Review
Times cited : (126)

References (225)
  • 1
    • 12944268979 scopus 로고    scopus 로고
    • Hyperphosphorylated tau and neurofilament and cytoskeletal disruptions in mice overexpressing human p25, an activator of cdk5
    • Ahlijanian M. K., Barrezueta N. X., Williams R. D., Jakowski A., Kowsz K. P., et al. (2000) Hyperphosphorylated tau and neurofilament and cytoskeletal disruptions in mice overexpressing human p25, an activator of cdk5. Proc. Natl. Acad. Sci. USA 97(6), 2910-2915.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , Issue.6 , pp. 2910-2915
    • Ahlijanian, M.K.1    Barrezueta, N.X.2    Williams, R.D.3    Jakowski, A.4    Kowsz, K.P.5
  • 2
    • 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(43), 10,626-10,633.
    • (1992) Biochemistry , vol.31 , Issue.43 , pp. 10626-10633
    • Andreadis, A.1    Brown, W.M.2    Kosik, K.S.3
  • 3
    • 0345561533 scopus 로고    scopus 로고
    • Polymerization of tau peptides into fibrillar structures. The effect of FTDP-17 mutations
    • Arrasate M., Perez M., Armas-Portela R., and Avila J. (1999) Polymerization of tau peptides into fibrillar structures. The effect of FTDP-17 mutations. FEBS Lett. 446(1), 199-202.
    • (1999) FEBS Lett. , vol.446 , Issue.1 , pp. 199-202
    • Arrasate, M.1    Perez, M.2    Armas-Portela, R.3    Avila, J.4
  • 4
    • 0026740795 scopus 로고
    • Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease
    • Arriagada P. V., Growdon J. H., Hedley-Whyte E. T., and Hyman B. T. (1992) Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease. Neurology 42(3 Pt 1), 631-639.
    • (1992) Neurology , vol.42 , Issue.3 PART 1 , pp. 631-639
    • Arriagada, P.V.1    Growdon, J.H.2    Hedley-Whyte, E.T.3    Hyman, B.T.4
  • 5
    • 0028840239 scopus 로고
    • Paired helical filament tau (PHFtau) in Niemann-Pick type C disease is similar to PHFtau in Alzheimer's disease
    • Auer I. A., Schmidt M. L., Lee V. M.-Y., et al. (1995) Paired helical filament tau (PHFtau) in Niemann-Pick type C disease is similar to PHFtau in Alzheimer's disease. Acta Neuropathol. (Berl) 90, 547-551.
    • (1995) Acta Neuropathol. (Berl) , vol.90 , pp. 547-551
    • Auer, I.A.1    Schmidt, M.L.2    Lee, V.M.-Y.3
  • 6
    • 0342419162 scopus 로고
    • Polarity orientation of microtubules in hippocampal neurons: Uniformity in the axon and nonuniformity in the dendrite
    • Baas P. W., Deitch J. S., Black M. M., and Banker G. A. (1988) Polarity orientation of microtubules in hippocampal neurons: uniformity in the axon and nonuniformity in the dendrite. Proc. Natl. Acad. Sci. USA 85(21), 8335-8339.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , Issue.21 , pp. 8335-8339
    • Baas, P.W.1    Deitch, J.S.2    Black, M.M.3    Banker, G.A.4
  • 7
    • 0023192282 scopus 로고
    • Neurofibrillary tangles in Alzheimer's disease and progressive supranuclear palsy: Antigenic similarities and differences. Micortubule-associated protein tau antigenicity is prominent in all types of tangles
    • Bancher C., Lassmann H., Budka H., et al. (1987) Neurofibrillary tangles in Alzheimer's disease and progressive supranuclear palsy: antigenic similarities and differences. Micortubule-associated protein tau antigenicity is prominent in all types of tangles. Acta Neuropathol. (Berl) 74, 39-46.
    • (1987) Acta Neuropathol. (Berl) , vol.74 , pp. 39-46
    • Bancher, C.1    Lassmann, H.2    Budka, H.3
  • 8
    • 0024587074 scopus 로고
    • Accumulation of abnormally phosphorylated tau precedes the formation of neurofibrillary tangles in Alzheimer's disease
    • Bancher C., Brunner C., Lassmann H., Budka H., Jellinger K., Wiche G., et al. (1989) Accumulation of abnormally phosphorylated tau precedes the formation of neurofibrillary tangles in Alzheimer's disease. Brain Res. 477(1-2), 90-99.
    • (1989) Brain Res. , vol.477 , Issue.1-2 , pp. 90-99
    • Bancher, C.1    Brunner, C.2    Lassmann, H.3    Budka, H.4    Jellinger, K.5    Wiche, G.6
  • 9
    • 0027451311 scopus 로고
    • Neuropathological staging of Alzheimer lesions and intellectual status in Alzheimer's and Parkinson's disease patients
    • Bancher C., Braak H., Fischer P., and Jellinger K. A. (1993) Neuropathological staging of Alzheimer lesions and intellectual status in Alzheimer's and Parkinson's disease patients. Neurosci. Lett. 162(1-2), 179-182.
    • (1993) Neurosci. Lett. , vol.162 , Issue.1-2 , pp. 179-182
    • Bancher, C.1    Braak, H.2    Fischer, P.3    Jellinger, K.A.4
  • 10
    • 0029877684 scopus 로고    scopus 로고
    • Correlations between mental state and quantitative neuropathology in the Vienna Longitudinal Study on Dementia
    • Bancher C., Jellinger K., Lassmann H., Fischer P., and Leblhuber F. (1996) Correlations between mental state and quantitative neuropathology in the Vienna Longitudinal Study on Dementia. Eur. Arch. Psychiatry Clin. Neurosci. 246(3), 137-146.
    • (1996) Eur. Arch. Psychiatry Clin. Neurosci. , vol.246 , Issue.3 , pp. 137-146
    • Bancher, C.1    Jellinger, K.2    Lassmann, H.3    Fischer, P.4    Leblhuber, F.5
  • 11
    • 0034718571 scopus 로고    scopus 로고
    • Structure, microtubule interactions, and paired helical filament aggregation by tau mutants of frontotemporal dementias
    • Barghorn S., Zheng-Fischhöfer Q., Ackmann M., Biernat J., von Bergen M., et al. (2000) Structure, microtubule interactions, and paired helical filament aggregation by tau mutants of frontotemporal dementias. Biochemistry 39(38), 11,714-11,721.
    • (2000) Biochemistry , vol.39 , Issue.38 , pp. 11714-11721
    • Barghorn, S.1    Zheng-Fischhöfer, Q.2    Ackmann, M.3    Biernat, J.4    Von Bergen, M.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(36), 17,577-17,583.
    • (1987) J. Biol. Chem. , vol.262 , Issue.36 , pp. 17577-17583
    • Baudier, J.1    Cole, R.D.2
  • 13
    • 0027757042 scopus 로고
    • Abnormal Alzheimer-like phosphorylation of tau-protein by cyclin-dependent kinases cdk2 and cdk5
    • Baumann K., Mandelkow E. M., Biernat J., Piwnica-Worms H., and Mandelkow E. (1993) Abnormal Alzheimer-like phosphorylation of tau-protein by cyclin-dependent kinases cdk2 and cdk5. FEBS Lett. 336(3), 417-424.
    • (1993) FEBS Lett. , vol.336 , Issue.3 , pp. 417-424
    • Baumann, K.1    Mandelkow, E.M.2    Biernat, J.3    Piwnica-Worms, H.4    Mandelkow, E.5
  • 14
    • 0021270695 scopus 로고
    • Light and electron microscopic studies of the distribution of microtubule-associated protein 2 in rat brain: A difference between dendritic and axonal cytoskeletons
    • Bernhardt R. and Matus A. (1984) Light and electron microscopic studies of the distribution of microtubule-associated protein 2 in rat brain: a difference between dendritic and axonal cytoskeletons. J. Comp. Neurol. 226(2), 203-221.
    • (1984) J. Comp. Neurol. , vol.226 , Issue.2 , pp. 203-221
    • Bernhardt, R.1    Matus, A.2
  • 15
    • 0027338266 scopus 로고
    • Phosphorylation of Ser262 strongly reduces binding of tau to microtubules: Distinction between PHF-like immuno-reactivity and microtubule binding
    • Biernat J., Gustke N., Drewes G., Mandelkow E. M., and Mandelkow E. (1993) Phosphorylation of Ser262 strongly reduces binding of tau to microtubules: distinction between PHF-like immuno-reactivity and microtubule binding. Neuron 11(1), 153-163.
    • (1993) Neuron , vol.11 , Issue.1 , pp. 153-163
    • Biernat, J.1    Gustke, N.2    Drewes, G.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 16
    • 0031007546 scopus 로고    scopus 로고
    • Regulated phosphorylation and dephosphorylation of tau protein: Effects on microtubule interaction, intracellular trafficking and neurodegeneration
    • Billingsley M. L. and Kincaid R. L. (1997) Regulated phosphorylation and dephosphorylation of tau protein: effects on microtubule interaction, intracellular trafficking and neurodegeneration. Biochem J. 323 (Pt 3), 577-591.
    • (1997) Biochem J. , vol.323 , Issue.PART 3 , pp. 577-591
    • Billingsley, M.L.1    Kincaid, R.L.2
  • 17
    • 0022365608 scopus 로고
    • The distribution of tau in the mammalian central nervous system
    • Binder L. I., Frankfurter A., and Rebhun L. I. (1985) The distribution of tau in the mammalian central nervous system. J. Cell Biol. 101(4), 1371-1378.
    • (1985) J. Cell Biol. , vol.101 , Issue.4 , pp. 1371-1378
    • Binder, L.I.1    Frankfurter, A.2    Rebhun, L.I.3
  • 18
    • 0030669037 scopus 로고    scopus 로고
    • Relationships between regional neuronal loss and neurofibrillary changes in the hippocampal formation and duration and severity of Alzheimer disease
    • Bobinski M., Wegiel J., Tarnawski M., Bobinski M., Reisberg B., de Leon M. J., et al. (1997) Relationships between regional neuronal loss and neurofibrillary changes in the hippocampal formation and duration and severity of Alzheimer disease. J. Neuropathol. Exp. Neurol. 56(4), 414-420.
    • (1997) J. Neuropathol. Exp. Neurol. , vol.56 , Issue.4 , pp. 414-420
    • Bobinski, M.1    Wegiel, J.2    Tarnawski, M.3    Bobinski, M.4    Reisberg, B.5    De Leon, M.J.6
  • 19
    • 0023111344 scopus 로고
    • Argyrophilic grains: Characteristic pathology of cerebral cortex in cases of adult onset dementia without Alzheimer changes
    • Braak H. and Braak E. (1987) Argyrophilic grains: characteristic pathology of cerebral cortex in cases of adult onset dementia without Alzheimer changes. Neurosci. Lett. 76, 124-127.
    • (1987) Neurosci. Lett. , vol.76 , pp. 124-127
    • Braak, H.1    Braak, E.2
  • 20
    • 0029013727 scopus 로고
    • Staging of Alzheimer's disease-related neurofibrillary changes
    • discussion 278-284
    • Braak H. and Braak E. (1992) Staging of Alzheimer's disease-related neurofibrillary changes. Neurobiol. Aging 16(3), 271-278, discussion 278-284.
    • (1992) Neurobiol. Aging , vol.16 , Issue.3 , pp. 271-278
    • Braak, H.1    Braak, E.2
  • 21
    • 0028362458 scopus 로고
    • A sequence of cytoskeleton changes related to the formation of neurofibrillary tangles and neuropil threads
    • Braak E., Braak H., and Mandelkow E. M. (1994) A sequence of cytoskeleton changes related to the formation of neurofibrillary tangles and neuropil threads. Acta Neuropathol. (Berl) 87(6), 554-567.
    • (1994) Acta Neuropathol. (Berl) , vol.87 , Issue.6 , pp. 554-567
    • Braak, E.1    Braak, H.2    Mandelkow, E.M.3
  • 22
    • 0033198039 scopus 로고    scopus 로고
    • Formation of compact myelin is required for maturation of the axonal cytoskeleton
    • Brady S. T., Witt A. S., Kirkpatrick L. L., de Waegh S. M., Readhead C., Tu P. H., et al. (1999) Formation of compact myelin is required for maturation of the axonal cytoskeleton. J. Neurosci. 19(17), 7278-7288.
    • (1999) J. Neurosci. , vol.19 , Issue.17 , pp. 7278-7288
    • Brady, S.T.1    Witt, A.S.2    Kirkpatrick, L.L.3    De Waegh, S.M.4    Readhead, C.5    Tu, P.H.6
  • 23
    • 0027308924 scopus 로고
    • Abnormal tau phosphorylation at Ser396 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 Ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding. Neuron 10(6), 1089-1099.
    • (1993) Neuron , vol.10 , Issue.6 , 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
  • 24
    • 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(5), 1327-1340.
    • (1995) J. Cell Biol. , vol.131 , Issue.5 , pp. 1327-1340
    • Brandt, R.1    Leger, J.2    Lee, G.3
  • 25
    • 0023929799 scopus 로고
    • Both adult and juvenile tau microtubule-associated proteins are axon specific in the developing and adult rat cerebellum
    • Brion J. P., Guilleminot J., Couchie D., Flament D. J., and Nunez J. (1988) Both adult and juvenile tau microtubule-associated proteins are axon specific in the developing and adult rat cerebellum. Neuroscience 25(1), 139-146.
    • (1988) Neuroscience , vol.25 , Issue.1 , pp. 139-146
    • Brion, J.P.1    Guilleminot, J.2    Couchie, D.3    Flament, D.J.4    Nunez, J.5
  • 26
    • 0345580607 scopus 로고    scopus 로고
    • Transgenic expression of the shortest human tau affects its compartmentalization and its phosphorylation as in the pretangle stage of Alzheimer's disease
    • Brion J. P., Tremp G., and Octave J. N. (1999) Transgenic expression of the shortest human tau affects its compartmentalization and its phosphorylation as in the pretangle stage of Alzheimer's disease. Am. J. Pathol. 154(1), 255-270.
    • (1999) Am. J. Pathol. , vol.154 , Issue.1 , pp. 255-270
    • Brion, J.P.1    Tremp, G.2    Octave, J.N.3
  • 28
    • 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., et al. (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
  • 29
    • 0033059975 scopus 로고    scopus 로고
    • Frontotemporal dementia and corticobasal degeneration in a family with a P301S mutation in tau
    • Bugiani O., Murrell J. R., Giaccone G., Hasegawa M., Ghigo G., et al. (1999) Frontotemporal dementia and corticobasal degeneration in a family with a P301S mutation in tau. J. Neuropathol. Exp. Neurol. 58(6), 667-677.
    • (1999) J. Neuropathol. Exp. Neurol. , vol.58 , Issue.6 , pp. 667-677
    • Bugiani, O.1    Murrell, J.R.2    Giaccone, G.3    Hasegawa, M.4    Ghigo, G.5
  • 30
    • 1942470734 scopus 로고
    • Polarity of axoplasmic microtubules in the olfactory nerve of the frog
    • Burton P. R. and Paige J. L. (1981) Polarity of axoplasmic microtubules in the olfactory nerve of the frog. Proc. Natl. Acad. Sci. USA 78(5), 3269-3273.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , Issue.5 , pp. 3269-3273
    • Burton, P.R.1    Paige, J.L.2
  • 31
    • 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(3), 717-730.
    • (1991) J. Cell Biol. , vol.115 , Issue.3 , pp. 717-730
    • Butner, K.A.1    Kirschner, M.W.2
  • 32
    • 0025098891 scopus 로고
    • Inhibition of neurite polarity by tau antisense oligonucleotides in primary cerebellar neurons
    • Caceres A. and Kosik K. S. (1990) Inhibition of neurite polarity by tau antisense oligonucleotides in primary cerebellar neurons. Nature 343(6257), 461-463.
    • (1990) Nature , vol.343 , Issue.6257 , pp. 461-463
    • Caceres, A.1    Kosik, K.S.2
  • 33
    • 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(6), 1515-1123.
    • (1991) J. Neurosci. , vol.11 , Issue.6 , pp. 1515-1123
    • Caceres, A.1    Potrebic, S.2    Kosik, K.S.3
  • 34
    • 0026729767 scopus 로고
    • Projection domains of MAP2 and tau determine spacings between microtubules in dendrites and axons
    • Chen J., Kanai Y., Cowan N. J., and Hirokawa N.(1992) Projection domains of MAP2 and tau determine spacings between microtubules in dendrites and axons. Nature 360(6405), 674-677.
    • (1992) Nature , vol.360 , Issue.6405 , pp. 674-677
    • Chen, J.1    Kanai, Y.2    Cowan, N.J.3    Hirokawa, N.4
  • 35
    • 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. Neurol. 55(5), 499-508.
    • (1996) J. Neuropathol. Exp. Neurol. , vol.55 , Issue.5 , pp. 499-508
    • Chin, S.S.-M.1    Goldman, J.E.2
  • 36
    • 0032573083 scopus 로고    scopus 로고
    • Pathogenic implications of mutations in the tau gene in pallido-ponto-nigral degeneration and related neurodegenerative disorders linked to chromosome 17
    • Clark L. N., Poorkaj P., Wszolek Z., Geschwind D. H., Nasreddine Z. S., et al. (1998) Pathogenic implications of mutations in the tau gene in pallido-ponto-nigral degeneration and related neurodegenerative disorders linked to chromosome 17. Proc. Natl. Acad. Sci. USA 95(22), 13,103-13,107.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , Issue.22 , pp. 13103-13107
    • Clark, L.N.1    Poorkaj, P.2    Wszolek, Z.3    Geschwind, D.H.4    Nasreddine, Z.S.5
  • 37
    • 0017649032 scopus 로고
    • Purification of tau, a microtubule-associated protein that induces assembly of micro-tubules from purified tubulin
    • Cleveland D. W., Hwo S.-Y., and Kirschner M. W. (1977) Purification of tau, a microtubule-associated protein that induces assembly of micro-tubules from purified tubulin. J. Mol. Biol. 116(2), 207-225.
    • (1977) J. Mol. Biol. , vol.116 , Issue.2 , pp. 207-225
    • Cleveland, D.W.1    Hwo, S.-Y.2    Kirschner, M.W.3
  • 38
    • 0027194791 scopus 로고
    • Gene dose of apolipoprotein E type 4 allele and the risk of Alzheimer's disease in late onset families
    • Corder E. H., Saunders A. M., Strittmatter W. J., Schmechel D. E., Gaskell P. C., Small G. W., et al. (1993) Gene dose of apolipoprotein E type 4 allele and the risk of Alzheimer's disease in late onset families. Science 261(5123), 921-923.
    • (1993) Science , vol.261 , Issue.5123 , pp. 921-923
    • Corder, E.H.1    Saunders, A.M.2    Strittmatter, W.J.3    Schmechel, D.E.4    Gaskell, P.C.5    Small, G.W.6
  • 40
    • 0028972701 scopus 로고
    • Image analysis of beta-amyloid load in Alzheimer's disease and relation to dementia severity
    • Cummings B. J. and Cotman C. W. (1995) Image analysis of beta-amyloid load in Alzheimer's disease and relation to dementia severity. Lancet 346(8989), 1524-1528.
    • (1995) Lancet , vol.346 , Issue.8989 , pp. 1524-1528
    • Cummings, B.J.1    Cotman, C.W.2
  • 41
    • 0030464914 scopus 로고    scopus 로고
    • Beta-amyloid deposition and other measures of neuropathology predict cognitive status in Alzheimer's disease
    • Cummings B. J., Pike C. J., Shankle R., and Cotman C. W. (1996) Beta-amyloid deposition and other measures of neuropathology predict cognitive status in Alzheimer's disease. Neurobiol. Aging 17(6), 921-933.
    • (1996) Neurobiol. Aging , vol.17 , Issue.6 , pp. 921-933
    • Cummings, B.J.1    Pike, C.J.2    Shankle, R.3    Cotman, C.W.4
  • 42
    • 0035067021 scopus 로고    scopus 로고
    • Inhibition of neuronal maturation in primary hippocampal neurons from tau deficient mice
    • Dawson H. N., Ferreira A., Eyster M. V., Ghoshal N., Binder L. I., and Vitek M. P. (2001) Inhibition of neuronal maturation in primary hippocampal neurons from tau deficient mice. J. Cell Sci. 114(Pt 6), 1179-1187.
    • (2001) J. Cell Sci. , vol.114 , Issue.PART 6 , pp. 1179-1187
    • Dawson, H.N.1    Ferreira, A.2    Eyster, M.V.3    Ghoshal, N.4    Binder, L.I.5    Vitek, M.P.6
  • 43
    • 0021270292 scopus 로고
    • Distribution of microtubule-associated protein 2 in the nervous system of the rat studied by immunofluorescence
    • De Camilli P., Miller P. E., Navone F., Theurkauf W. E., and Vallee R. B. (1984) Distribution of microtubule-associated protein 2 in the nervous system of the rat studied by immunofluorescence. Neuroscience 11(4), 817-846.
    • (1984) Neuroscience , vol.11 , Issue.4 , pp. 817-846
    • De Camilli, P.1    Miller, P.E.2    Navone, F.3    Theurkauf, W.E.4    Vallee, R.B.5
  • 44
    • 0026580004 scopus 로고
    • Local modulation of neurofilament phosphorylation, axonal caliber, and slow axonal transport by myelinating Schwann cells
    • de Waegh S. M., Lee V. M.-Y., and Brady S. T. (1992) Local modulation of neurofilament phosphorylation, axonal caliber, and slow axonal transport by myelinating Schwann cells. Cell 68, 451-463.
    • (1992) Cell , vol.68 , pp. 451-463
    • De Waegh, S.M.1    Lee, V.M.-Y.2    Brady, S.T.3
  • 45
    • 0026512066 scopus 로고
    • Identification of normal and pathological aging in prospectively studied nondemented elderly humans
    • Dickson D. W., Crystal H. A., Mattiace L. A., Masur D. M., Blau A. D., Davies P., et al. (1992) Identification of normal and pathological aging in prospectively studied nondemented elderly humans. Neurobiol. Aging 13(1), 179-189.
    • (1992) Neurobiol. Aging , vol.13 , Issue.1 , pp. 179-189
    • Dickson, D.W.1    Crystal, H.A.2    Mattiace, L.A.3    Masur, D.M.4    Blau, A.D.5    Davies, P.6
  • 46
    • 0029657947 scopus 로고    scopus 로고
    • Cytoskeletal pathology in non-Alzheimer degenerative dementia: New lesions in diffuse Lewy body disease, Pick's disease, and corticobasal degeneration
    • Dickson D. W., Feany M. B., Yen S. H., Mattiace L. A., and Davies P. (1996) Cytoskeletal pathology in non-Alzheimer degenerative dementia: new lesions in diffuse Lewy body disease, Pick's disease, and corticobasal degeneration. J. Neural. Transm. Suppl. 47, 31-46.
    • (1996) J. Neural. Transm. , Issue.SUPPL. 47 , pp. 31-46
    • Dickson, D.W.1    Feany, M.B.2    Yen, S.H.3    Mattiace, L.A.4    Davies, P.5
  • 47
    • 0031901513 scopus 로고    scopus 로고
    • Pick's disease: A modern approach
    • Dickson D. W. (1998) Pick's disease: a modern approach. Brain Pathol. 8(2), 339-354.
    • (1998) Brain Pathol. , vol.8 , Issue.2 , pp. 339-354
    • Dickson, D.W.1
  • 48
    • 0027058857 scopus 로고
    • Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau
    • Drechsel D. N., Hyman A. A., Cobb M. H., and Kirschner M. W. (1992) Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau. Mol. Biol. Cell 3(10), 1141-1154.
    • (1992) Mol. Biol. Cell , vol.3 , Issue.10 , pp. 1141-1154
    • Drechsel, D.N.1    Hyman, A.A.2    Cobb, M.H.3    Kirschner, M.W.4
  • 49
    • 0026549985 scopus 로고
    • Mitogen activated protein (MAP) kinase transforms tau protein into an Alzheimer-like state
    • Drewes G., Lichtenberg-Kraag B., Doring F., Mandelkow E. M., Biernat J., Goris J., et al. (1992) Mitogen activated protein (MAP) kinase transforms tau protein into an Alzheimer-like state. EMBO J. 11(6), 2131-2138.
    • (1992) EMBO J. , vol.11 , Issue.6 , pp. 2131-2138
    • Drewes, G.1    Lichtenberg-Kraag, B.2    Doring, F.3    Mandelkow, E.M.4    Biernat, J.5    Goris, J.6
  • 50
    • 0027753055 scopus 로고
    • Dephosphorylation of tau protein and Alzheimer paired helical filaments by calcineurin and phosphatase-2A
    • Drewes G., Mandelkow E. M., Baumann K., Goris J., Merlevede W., and Mandelkow E. (1993) Dephosphorylation of tau protein and Alzheimer paired helical filaments by calcineurin and phosphatase-2A. FEBS Lett. 336(3), 425-432.
    • (1993) FEBS Lett. , vol.336 , Issue.3 , pp. 425-432
    • Drewes, G.1    Mandelkow, E.M.2    Baumann, K.3    Goris, J.4    Merlevede, W.5    Mandelkow, E.6
  • 51
    • 0030969575 scopus 로고    scopus 로고
    • MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption
    • Drewes G., Ebneth A., Preuss U., Mandelkow E. M., and Mandelkow E. (1997) MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption. Cell 89(2), 297-308.
    • (1997) Cell , vol.89 , Issue.2 , pp. 297-308
    • Drewes, G.1    Ebneth, A.2    Preuss, U.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 52
    • 0033545946 scopus 로고    scopus 로고
    • Missense and silent tau gene mutations cause frontotemporal dementia with parkinsonism-chromosome 17 type, by affecting multiple alternative RNA splicing regulatory elements
    • D'Souza I., Poorkaj P., Hong M., Nochlin D., Lee V. M.-Y., et al. (1999) Missense and silent tau gene mutations cause frontotemporal dementia with parkinsonism-chromosome 17 type, by affecting multiple alternative RNA splicing regulatory elements. Proc. Natl. Acad. Sci. USA 96(10), 5598-5603.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , Issue.10 , pp. 5598-5603
    • D'Souza, I.1    Poorkaj, P.2    Hong, M.3    Nochlin, D.4    Lee, V.M.-Y.5
  • 53
    • 0034016093 scopus 로고    scopus 로고
    • Characterization of pathology in transgenic mice over-expressing human genomic and cDNA tau transgenes
    • Duff K., Knight H., Refolo L. M., Sanders S., Yu X., Picciano M., et al. (2000) Characterization of pathology in transgenic mice over-expressing human genomic and cDNA tau transgenes. Neurobiol Dis. 7(2), 87-98.
    • (2000) Neurobiol Dis. , vol.7 , Issue.2 , pp. 87-98
    • Duff, K.1    Knight, H.2    Refolo, L.M.3    Sanders, S.4    Yu, X.5    Picciano, M.6
  • 54
    • 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. Pathol. 146(6), 1388-1396.
    • (1995) Am. J. Pathol. , vol.146 , Issue.6 , pp. 1388-1396
    • Feany, M.B.1    Dickson, D.W.2
  • 55
    • 0030049067 scopus 로고    scopus 로고
    • Neuropathologic overlap of progressive supra-nuclear palsy, Pick's disease and corticobasal degeneration
    • Feany M. B., Mattiace L. A., and Dickson D. W. (1996) Neuropathologic overlap of progressive supra-nuclear palsy, Pick's disease and corticobasal degeneration. J. Neuropathol. Exp. Neurol. 55(1), 53-67.
    • (1996) J. Neuropathol. Exp. Neurol. , vol.55 , Issue.1 , pp. 53-67
    • Feany, M.B.1    Mattiace, L.A.2    Dickson, D.W.3
  • 56
    • 0025857173 scopus 로고
    • Abnormal tau proteins in progressive supranuclear palsy: Similarities and differences with the neurofibrillary degeneration of the Alzheimer type
    • Flament S., Delacourte A., Verny M., et al. (1991) Abnormal tau proteins in progressive supranuclear palsy: similarities and differences with the neurofibrillary degeneration of the Alzheimer type. Acta Neuropathol. (Berl) 81, 591-596.
    • (1991) Acta Neuropathol. (Berl) , vol.81 , pp. 591-596
    • Flament, S.1    Delacourte, A.2    Verny, M.3
  • 57
    • 0034469810 scopus 로고    scopus 로고
    • New insights into genetic and molecular mechanisms of brain degeneration in tauopathies
    • Forman M. S., Lee V. M.-Y., and Trojanowski J. Q. (2000) New insights into genetic and molecular mechanisms of brain degeneration in tauopathies. J. Chem. Neuroanat. 20(3-4), 225-244.
    • (2000) J. Chem. Neuroanat. , vol.20 , Issue.3-4 , pp. 225-244
    • Forman, M.S.1    Lee, V.M.-Y.2    Trojanowski, J.Q.3
  • 58
    • 0036088014 scopus 로고    scopus 로고
    • Signature tau neuropathology in gray and white matter of corticobasal degeneration
    • Forman M. S., Zhukareva V., Bergeron C., Chin S. S., Grossman M., Clark C., et al. (2002) Signature tau neuropathology in gray and white matter of corticobasal degeneration. Am. J. Pathol. 160(6), 2045-2053.
    • (2002) Am. J. Pathol. , vol.160 , Issue.6 , pp. 2045-2053
    • Forman, M.S.1    Zhukareva, V.2    Bergeron, C.3    Chin, S.S.4    Grossman, M.5    Clark, C.6
  • 59
    • 0030977392 scopus 로고    scopus 로고
    • Frontotemporal dementia and parkinsonism linked to chromosome 17: A consensus conference. Conference participants
    • Foster N. L., Wilhelmsen K., Sima A. A., et al. (1997) Frontotemporal dementia and parkinsonism linked to chromosome 17: a consensus conference. Conference participants. Ann. Neurol. 41, 706-715.
    • (1997) Ann. Neurol. , vol.41 , pp. 706-715
    • Foster, N.L.1    Wilhelmsen, K.2    Sima, A.A.3
  • 60
    • 0034705192 scopus 로고    scopus 로고
    • In vitro polymerization of tau protein monitored by laser light scattering: Method and application to the study of FTDP-17 mutants
    • Gamblin T. C., King M. E., Dawson H., Vitek M. P., Kuret J., et al. (2000) In vitro polymerization of tau protein monitored by laser light scattering: method and application to the study of FTDP-17 mutants. Biochemistry 39(20), 6136-6144.
    • (2000) Biochemistry , vol.39 , Issue.20 , pp. 6136-6144
    • Gamblin, T.C.1    King, M.E.2    Dawson, H.3    Vitek, M.P.4    Kuret, J.5
  • 61
    • 0028985574 scopus 로고
    • Alzheimer-type neuropathology in transgenic mice overexpressing V717F beta-amyloid precursor protein
    • Games D., Adams D., Alessandrini R., Barbour R., Berthelette P., et al. (1995) Alzheimer-type neuropathology in transgenic mice overexpressing V717F beta-amyloid precursor protein. Nature 373(6514), 523-527.
    • (1995) Nature , vol.373 , Issue.6514 , pp. 523-527
    • Games, D.1    Adams, D.2    Alessandrini, R.3    Barbour, R.4    Berthelette, P.5
  • 63
    • 0002792366 scopus 로고
    • Cloning and swquencing of the cDNA encoding a core protein of the paired helical filament of alzheimer disease: Identification as the microtubule-associated protein tau
    • Goedert M., Wischik C. M., Crowther R. A., Walker J. E., and Klug A. (1988) Cloning and swquencing of the cDNA encoding a core protein of the paired helical filament of alzheimer disease: identification as the microtubule-associated protein tau. Proc. Natl. Acad. Sci. USA 85(11), 4051-4055.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , Issue.11 , pp. 4051-4055
    • Goedert, M.1    Wischik, C.M.2    Crowther, R.A.3    Walker, J.E.4    Klug, A.5
  • 64
    • 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. (1989) Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease. Neuron 3(4), 519-526.
    • (1989) Neuron , vol.3 , Issue.4 , pp. 519-526
    • Goedert, M.1    Spillantini, M.G.2    Jakes, R.3    Rutherford, D.4    Crowther, R.A.5
  • 65
    • 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(13), 4225-4230.
    • (1990) EMBO J. , vol.9 , Issue.13 , pp. 4225-4230
    • Goedert, M.1    Jakes, R.2
  • 66
    • 0026784416 scopus 로고
    • p42 MAP kinase phosphorylation sites in microtubule-associated protein tau are dephosphorylated by protein phosphatase 2A1. Implications for Alzheimer's disease
    • Goedert M., Cohen E. S., Jakes R., and Cohen P. (1992a) p42 MAP kinase phosphorylation sites in microtubule-associated protein tau are dephosphorylated by protein phosphatase 2A1. Implications for Alzheimer's disease. FEBS Lett. 312(1), 95-99.
    • (1992) FEBS Lett. , vol.312 , Issue.1 , pp. 95-99
    • Goedert, M.1    Cohen, E.S.2    Jakes, R.3    Cohen, P.4
  • 67
    • 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. (1992b) Tau proteins of Alzheimer paired helical filaments: abnormal phosphorylation of all six brain isoforms. Neuron 8(1), 159-168.
    • (1992) Neuron , vol.8 , Issue.1 , pp. 159-168
    • Goedert, M.1    Spillantini, M.G.2    Cairns, N.J.3    Crowther, R.A.4
  • 68
    • 0027217679 scopus 로고
    • The abnormal phosphorylation of tau protein at Ser-202 in Alzheimer disease recapitulates phosphorylation during development
    • Goedert M., Jakes R., Crowther R. A., Six J., Lubke U., Vandermeeren M., et al. (1993) The abnormal phosphorylation of tau protein at Ser-202 in Alzheimer disease recapitulates phosphorylation during development. Proc. Natl. Acad. Sci. USA 90(11), 5066-5070.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , Issue.11 , pp. 5066-5070
    • Goedert, M.1    Jakes, R.2    Crowther, R.A.3    Six, J.4    Lubke, U.5    Vandermeeren, M.6
  • 70
    • 0029907548 scopus 로고    scopus 로고
    • Assembly of microtubule-associated protein tau into Alzheimer-like filaments induce by sulphated glycosamino-glycans
    • Goedert M., Jakes R., Spillantini M. G., Hasegawa M., Smith M. J., and Crowther R. A. (1996) Assembly of microtubule-associated protein tau into Alzheimer-like filaments induce by sulphated glycosamino-glycans. Nature 383(6600), 550-553.
    • (1996) Nature , vol.383 , Issue.6600 , pp. 550-553
    • Goedert, M.1    Jakes, R.2    Spillantini, M.G.3    Hasegawa, M.4    Smith, M.J.5    Crowther, R.A.6
  • 71
    • 0030963035 scopus 로고    scopus 로고
    • Phosphorylation of microtubule-associated protein tau by stress-activated protein kinases
    • Goedert M., Hasegawa M., Jakes R., Lawler S., Cuenda A., and Cohen P. (1997a) Phosphorylation of microtubule-associated protein tau by stress-activated protein kinases. FEBS Lett. 409(1), 57-62.
    • (1997) FEBS Lett. , vol.409 , Issue.1 , pp. 57-62
    • Goedert, M.1    Hasegawa, M.2    Jakes, R.3    Lawler, S.4    Cuenda, A.5    Cohen, P.6
  • 73
    • 0032919462 scopus 로고    scopus 로고
    • Effects of frontotemporal dementia FTDP-17 mutations on heparin-induced assembly of tau filaments
    • Goedert M., Jakes R., and Crowther R. A. (1999) Effects of frontotemporal dementia FTDP-17 mutations on heparin-induced assembly of tau filaments. FEBS Lett. 450(3), 306-311.
    • (1999) FEBS Lett. , vol.450 , Issue.3 , pp. 306-311
    • Goedert, M.1    Jakes, R.2    Crowther, R.A.3
  • 74
    • 0029979798 scopus 로고    scopus 로고
    • Profound loss of layer II entorhinal cortex neurons occurs in very mild Alzheimer's disease
    • Gomez-Isla T., Price J. L., McKeel D. W. Jr., Morris J. C., Growdon J. H., and Hyman B. T. (1996) Profound loss of layer II entorhinal cortex neurons occurs in very mild Alzheimer's disease. J. Neurosci. 16(14), 4491-4500.
    • (1996) J. Neurosci. , vol.16 , Issue.14 , pp. 4491-4500
    • Gomez-Isla, T.1    Price, J.L.2    McKeel D.W., Jr.3    Morris, J.C.4    Growdon, J.H.5    Hyman, B.T.6
  • 75
    • 0028175215 scopus 로고
    • Identification of a novel microtubule binding and assembly domain in the developmentally regulated interrepeat region of tau
    • Goode B. L. and Feinstein S. C. (1994) Identification of a novel microtubule binding and assembly domain in the developmentally regulated interrepeat region of tau. J. Cell Biol. 124(5), 769-782.
    • (1994) J. Cell Biol. , vol.124 , Issue.5 , pp. 769-782
    • Goode, B.L.1    Feinstein, S.C.2
  • 76
    • 0028965635 scopus 로고
    • Somatodendritic localization and hyperphosphorylation of tau protein in transgenic mice expressing the longest human brain tau isoform
    • Götz J., Probst A., Spillantini M. G., Schafer T., Jakes R., et al. (1995) Somatodendritic localization and hyperphosphorylation of tau protein in transgenic mice expressing the longest human brain tau isoform. EMBO J. 14(7), 1304-1313.
    • (1995) EMBO J. , vol.14 , Issue.7 , pp. 1304-1313
    • Götz, J.1    Probst, A.2    Spillantini, M.G.3    Schafer, T.4    Jakes, R.5
  • 77
    • 0035943436 scopus 로고    scopus 로고
    • Formation of neurofibrillary tangles in P3011 tau transgenic mice induced by Abeta 42 fibrils
    • Götz J., Chen F., van Dorpe J., and Nitsch R. M. (2001) Formation of neurofibrillary tangles in P3011 tau transgenic mice induced by Abeta 42 fibrils. Science 293(5534), 1491-1495.
    • (2001) Science , vol.293 , Issue.5534 , pp. 1491-1495
    • Götz, J.1    Chen, F.2    Van Dorpe, J.3    Nitsch, R.M.4
  • 78
    • 0025292866 scopus 로고
    • A preparation of Alzheimer paired helical filaments that displays distinct tau proteins by polyacrylamide gel electrophoresis
    • Greenberg S. G. and Davies P. (1990) A preparation of Alzheimer paired helical filaments that displays distinct tau proteins by polyacrylamide gel electrophoresis. Proc. Natl. Acad. Sci. USA 87(15), 5827-5831.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , Issue.15 , pp. 5827-5831
    • Greenberg, S.G.1    Davies, P.2
  • 79
    • 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(1), 564-569.
    • (1992) J. Biol. Chem. , vol.267 , Issue.1 , pp. 564-569
    • Greenberg, S.G.1    Davies, P.2    Schein, J.D.3    Binder, L.I.4
  • 80
    • 0022744803 scopus 로고
    • Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology
    • Grundke-Iqbal I., Iqbal K., Tung Y. C., Quinlan M., Wisniewski H. M., and Binder L. I. (1986) Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology. Proc. Natl. Acad. Sci. USA 83(13), 4913-4917.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , Issue.13 , pp. 4913-4917
    • Grundke-Iqbal, I.1    Iqbal, K.2    Tung, Y.C.3    Quinlan, M.4    Wisniewski, H.M.5    Binder, L.I.6
  • 81
    • 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., Goedert M., et al. (1992) The Alzheimer-like phosphorylation of tau protein reduces microtubule binding and involves Ser-Pro and Thr-Pro motifs. FEBS Lett. 307(2), 199-205.
    • (1992) FEBS Lett. , vol.307 , Issue.2 , pp. 199-205
    • Gustke, N.1    Steiner, B.2    Mandelkow, E.M.3    Biernat, J.4    Meyer, H.E.5    Goedert, M.6
  • 82
    • 0024461007 scopus 로고
    • Tau protein becomes long and stiff upon phosphorylation: Correlation between paracrystalline structure and degree of phosphorylation
    • Hagestedt T., Lichtenberg B., Wille H., Mandelkow E. M., and Mandelkow E. (1989) Tau protein becomes long and stiff upon phosphorylation: correlation between paracrystalline structure and degree of phosphorylation. J. Cell Biol. 109(4 Pt 1), 1643-1651.
    • (1989) J. Cell Biol. , vol.109 , Issue.4 PART 1 , pp. 1643-1651
    • Hagestedt, T.1    Lichtenberg, B.2    Wille, H.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 83
    • 0026487365 scopus 로고
    • Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: Generation of paired helical filament epitopes and neuronal localisation of the kinase
    • Hanger D. P., Hughes K., Woodgett J. R., Brion J. P., and Anderton B. H. (1992) Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: generation of paired helical filament epitopes and neuronal localisation of the kinase. Neurosci. Lett. 147(1), 58-62.
    • (1992) Neurosci. Lett. , vol.147 , Issue.1 , pp. 58-62
    • Hanger, D.P.1    Hughes, K.2    Woodgett, J.R.3    Brion, J.P.4    Anderton, B.H.5
  • 84
    • 0028301455 scopus 로고
    • Altered microtubule organization in small-calibre axons of mice lacking tau protein
    • Harada A., Oguchi K., Okabe S., Kuno J., Terada S., Ohshima T., et al. (1994) Altered microtubule organization in small-calibre axons of mice lacking tau protein. Nature 369(6480), 488-491.
    • (1994) Nature , vol.369 , Issue.6480 , pp. 488-491
    • Harada, A.1    Oguchi, K.2    Okabe, S.3    Kuno, J.4    Terada, S.5    Ohshima, T.6
  • 85
    • 0027404098 scopus 로고
    • Okadaic acid induces hyperphosphorylated forms of tau protein in human brain slices
    • Harris K. A., Oyler G. A., Doolittle G. M., Vincent I., Lehman R. A., Kincaid R. L., et al. (1993) Okadaic acid induces hyperphosphorylated forms of tau protein in human brain slices. Ann. Neurol. 33 (1), 77-87.
    • (1993) Ann. Neurol. , vol.33 , Issue.1 , pp. 77-87
    • Harris, K.A.1    Oyler, G.A.2    Doolittle, G.M.3    Vincent, I.4    Lehman, R.A.5    Kincaid, R.L.6
  • 86
    • 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. FEBS Lett. 384(1), 25-30.
    • (1996) FEBS Lett. , vol.384 , Issue.1 , pp. 25-30
    • Hasegawa, M.1    Jakes, R.2    Crowther, R.A.3    Lee, V.M.-Y.4    Ihara, Y.5    Goedert, M.6
  • 87
    • 0031439109 scopus 로고    scopus 로고
    • Alzheimer-like changes in microtubule-associated protein tau induced by sulfated glycosaminoglycans. Inhibition of microtubule binding, stimulation of phosphorylation, and filament assembly depend on the degree of sulfation
    • Hasegawa M., Crowther R. A., Jakes R., and Goedert M. (1997) Alzheimer-like changes in microtubule-associated protein tau induced by sulfated glycosaminoglycans. Inhibition of microtubule binding, stimulation of phosphorylation, and filament assembly depend on the degree of sulfation. J. Biol. Chem. 272(52), 33,118-33,124.
    • (1997) J. Biol. Chem. , vol.272 , Issue.52 , pp. 33118-33124
    • Hasegawa, M.1    Crowther, R.A.2    Jakes, R.3    Goedert, M.4
  • 88
    • 0032561415 scopus 로고    scopus 로고
    • Tau proteins with FTDP-17 mutations have a reduced ability to promote microtubule assembly
    • Hasegawa M., Smith M. J., and Goedert M. (1998) Tau proteins with FTDP-17 mutations have a reduced ability to promote microtubule assembly. FEBS Lett. 437(3), 207-210.
    • (1998) FEBS Lett. , vol.437 , Issue.3 , pp. 207-210
    • Hasegawa, M.1    Smith, M.J.2    Goedert, M.3
  • 89
    • 0033060662 scopus 로고    scopus 로고
    • FTDP-17 mutations N279K and S305N in tau produce increased splicing of exon 10
    • Hasegawa M., Smith M. J., Iijima M., Tabira T., and Goedert M. (1999) FTDP-17 mutations N279K and S305N in tau produce increased splicing of exon 10. FEBS Lett. 443(2), 93-96.
    • (1999) FEBS Lett. , vol.443 , Issue.2 , pp. 93-96
    • Hasegawa, M.1    Smith, M.J.2    Iijima, M.3    Tabira, T.4    Goedert, M.5
  • 90
    • 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., et al. (1994) Preliminary NINDS neuropathologic criteria for Steele-Richardson-Olszewski syndrome (progressive supranuclear palsy). Neurology 44(11), 2015-2019.
    • (1994) Neurology , vol.44 , Issue.11 , pp. 2015-2019
    • Hauw, J.J.1    Daniel, S.E.2    Dickson, D.3    Horoupian, D.S.4    Jellinger, K.5
  • 91
    • 0019781474 scopus 로고
    • Polarity orientation of axonal microtubules
    • Heidemann S. R., Landers J. M., and Hamborg M. A. (1981) Polarity orientation of axonal microtubules. J. Cell Biol. 91(3 Pt 1), 661-665.
    • (1981) J. Cell Biol. , vol.91 , Issue.3 PART 1 , pp. 661-665
    • Heidemann, S.R.1    Landers, J.M.2    Hamborg, M.A.3
  • 92
    • 0041862939 scopus 로고    scopus 로고
    • Tau protein and tauopathy
    • (Davis K. L., Charney D., Coyle J., and Nemeroff C. N., eds.), Lippincott Williams & Wilkins, Baltimore, MD
    • Higuchi M., Trojanowski J. Q., and Lee V. M.-Y. (2002) Tau protein and tauopathy, in Neuropsychopharmacology: The Fifth Generation of Progress (Davis K. L., Charney D., Coyle J., and Nemeroff C. N., eds.), Lippincott Williams & Wilkins, Baltimore, MD, pp. 1339-1353.
    • (2002) Neuropsychopharmacology: The Fifth Generation of Progress , pp. 1339-1353
    • Higuchi, M.1    Trojanowski, J.Q.2    Lee, V.M.-Y.3
  • 93
    • 0024507707 scopus 로고
    • Tau consists of a set of proteins with repeated C-terminal microtubule-binding domains and variable N-terminal domains
    • Himmler A., Drechsel D., Kirschner M. W., and Martin D. W. Jr. (1989) Tau consists of a set of proteins with repeated C-terminal microtubule-binding domains and variable N-terminal domains. Mol. Cell Biol. 9(4), 1381-1388.
    • (1989) Mol. Cell Biol. , vol.9 , Issue.4 , pp. 1381-1388
    • Himmler, A.1    Drechsel, D.2    Kirschner, M.W.3    Martin D.W., Jr.4
  • 94
    • 0000035923 scopus 로고
    • Parkinsonism dementia complex in endemic disease on the island of Guam - Pathologic features
    • Hirano A., Malamud N., and Kurland L. T. (1961) Parkinsonism dementia complex in endemic disease on the island of Guam - pathologic features. Brain 84, 662.
    • (1961) Brain , vol.84 , pp. 662
    • Hirano, A.1    Malamud, N.2    Kurland, L.T.3
  • 95
    • 0030028366 scopus 로고    scopus 로고
    • Selective stabilization of tau in axons and microtubule-associated protein 2C in cell bodies and dendrites contributes to polarized localization of cytoskeletal proteins in mature neurons
    • Hirokawa N., Funakoshi T., Sato-Harada R., 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(4), 667-679.
    • (1996) J. Cell Biol. , vol.132 , Issue.4 , pp. 667-679
    • Hirokawa, N.1    Funakoshi, T.2    Sato-Harada, R.3    Kanai, Y.4
  • 96
    • 0028039176 scopus 로고
    • Amyotrophic lateral sclerosis/parkinsonism dementia complex of Guam: Quantitative neuropathology, immunohistochemical analysis of neuronal vulnerability, and comparison with related neurodegenerative disorders
    • Hof P. R., Nimchinsky E. A., Buée-Scherrer V., et al. (1994) Amyotrophic lateral sclerosis/parkinsonism dementia complex of Guam: quantitative neuropathology, immunohistochemical analysis of neuronal vulnerability, and comparison with related neurodegenerative disorders. Acta Neuropathol. (Berl) 88, 397-404.
    • (1994) Acta Neuropathol. (Berl) , vol.88 , pp. 397-404
    • Hof, P.R.1    Nimchinsky, E.A.2    Buée-Scherrer, V.3
  • 97
    • 0030750558 scopus 로고    scopus 로고
    • Unique Alzheimer's disease paired helical filament specific epitopes involve double phosphorylation at specific sites
    • Hoffmann R., Lee V. M.-Y., Leight S., Varga I., and Otvos L. Jr. (1997) Unique Alzheimer's disease paired helical filament specific epitopes involve double phosphorylation at specific sites. Biochemistry 36(26), 8114-8124.
    • (1997) Biochemistry , vol.36 , Issue.26 , pp. 8114-8124
    • Hoffmann, R.1    Lee, V.M.-Y.2    Leight, S.3    Varga, I.4    Otvos L., Jr.5
  • 98
    • 0030748390 scopus 로고    scopus 로고
    • Insulin and insulin-like growth factor-1 regulate tau phosphorylation in cultured human neurons
    • Hong M. and Lee V. M.-Y. (1997) Insulin and insulin-like growth factor-1 regulate tau phosphorylation in cultured human neurons. J. Biol. Chem. 272(31), 19,547-19,553.
    • (1997) J. Biol. Chem. , vol.272 , Issue.31 , pp. 19547-19553
    • Hong, M.1    Lee, V.M.-Y.2
  • 99
    • 0030868557 scopus 로고    scopus 로고
    • Lithium reduces tau phosphorylation by inhibition of glycogen synthase kinase-3
    • Hong M., Chen D. C., Klein P. S., and Lee V. M.-Y. (1997) Lithium reduces tau phosphorylation by inhibition of glycogen synthase kinase-3. J. Biol. Chem. 272(40), 25,326-25,332.
    • (1997) J. Biol. Chem. , vol.272 , Issue.40 , pp. 25326-25332
    • Hong, M.1    Chen, D.C.2    Klein, P.S.3    Lee, V.M.-Y.4
  • 100
    • 0032484089 scopus 로고    scopus 로고
    • Mutation-specific functional impairments in distinct tau isoforms of hereditary FTDP-17
    • Hong M., Zhukareva V., Vogelsberg-Ragaglia V., Wszolek Z., Reed L., Miller B. I., et al. (1998) Mutation-specific functional impairments in distinct tau isoforms of hereditary FTDP-17. Science 282(5395), 1914-1917.
    • (1998) Science , vol.282 , Issue.5395 , pp. 1914-1917
    • Hong, M.1    Zhukareva, V.2    Vogelsberg-Ragaglia, V.3    Wszolek, Z.4    Reed, L.5    Miller, B.I.6
  • 101
    • 0028922244 scopus 로고
    • Evidence for cdk5 as a major activity phosphorylating tau protein in porcine brain extract
    • Hosoi T., Uchiyama M., Okumura E., Saito T., Ishiguro K., Uchida T., et al. (1995) Evidence for cdk5 as a major activity phosphorylating tau protein in porcine brain extract. J. Biochem. (Tokyo) 117(4), 741-749.
    • (1995) J. Biochem. (Tokyo) , vol.117 , Issue.4 , pp. 741-749
    • Hosoi, T.1    Uchiyama, M.2    Okumura, E.3    Saito, T.4    Ishiguro, K.5    Uchida, T.6
  • 102
    • 0029742199 scopus 로고    scopus 로고
    • Correlative memory deficits, Aβ elevation, and amyloid plaques in transgenic mice
    • Hsiao K., Chapman P., Nilsen S., Eckman C., Harigaya Y., et al. (1996) Correlative memory deficits, Aβ elevation, and amyloid plaques in transgenic mice. Science 274(5284), 99-102.
    • (1996) Science , vol.274 , Issue.5284 , pp. 99-102
    • Hsiao, K.1    Chapman, P.2    Nilsen, S.3    Eckman, C.4    Harigaya, Y.5
  • 103
    • 0032543684 scopus 로고    scopus 로고
    • Association of missense and 5′-spilice-site mutations in tau with the inherited dementia FTDP-17
    • Hutton M., Lendon C. I., Rizzu P., Baker M., Froelich S., et al. (1998) Association of missense and 5′-spilice-site mutations in tau with the inherited dementia FTDP-17. Nature 393(6686), 702-705.
    • (1998) Nature , vol.393 , Issue.6686 , pp. 702-705
    • Hutton, M.1    Lendon, C.I.2    Rizzu, P.3    Baker, M.4    Froelich, S.5
  • 104
    • 0002931170 scopus 로고
    • Quantitative neuropathology in Alzheimer's disease: Neuronal loss in high-order association cortex parallels dementia
    • (Iqbal K., Mortimer J. A., Winblad B., and Wisniewski H. M., eds.), Wiley, New York, NY
    • Hyman B. T., West H. L., Gomez-Isla T., and Mui S. (1995) Quantitative neuropathology in Alzheimer's disease: Neuronal loss in high-order association cortex parallels dementia. In Research Advances in Alzheimer's Disease and Related Disorders (Iqbal K., Mortimer J. A., Winblad B., and Wisniewski H. M., eds.), Wiley, New York, NY, pp. 453-460.
    • (1995) Research Advances in Alzheimer's Disease and Related Disorders , pp. 453-460
    • Hyman, B.T.1    West, H.L.2    Gomez-Isla, T.3    Mui, S.4
  • 105
    • 0033602013 scopus 로고    scopus 로고
    • A distinct familial presenile dementia with a novel missense mutation in the tau gene
    • Iijima M., Tabira T., Poorkaj P., Schellenberg G. D., Trojanowski J. Q., et al. (1999) A distinct familial presenile dementia with a novel missense mutation in the tau gene. NeuroReport 10(3), 497-501.
    • (1999) NeuroReport , vol.10 , Issue.3 , pp. 497-501
    • Iijima, M.1    Tabira, T.2    Poorkaj, P.3    Schellenberg, G.D.4    Trojanowski, J.Q.5
  • 106
    • 0033969771 scopus 로고    scopus 로고
    • Muscle weakness, hyperactivity, and impairment in fear conditioning in tau-deficient mice
    • Ikegami S., Harada A., and Hirokawa N. (2000) Muscle weakness, hyperactivity, and impairment in fear conditioning in tau-deficient mice. Neurosci Lett. 279(3), 129-132.
    • (2000) Neurosci Lett. , vol.279 , Issue.3 , pp. 129-132
    • Ikegami, S.1    Harada, A.2    Hirokawa, N.3
  • 107
  • 108
    • 0033230886 scopus 로고    scopus 로고
    • Age-dependent emergence and progression of a tauopathy in transgenic mice over-expressing the shortest human tau isoform
    • Ishihara T., Hong M., Zhang B., Nakagawa Y., Lee M. K., et al. (1999) Age-dependent emergence and progression of a tauopathy in transgenic mice over-expressing the shortest human tau isoform. Neuron 24(3), 751-762.
    • (1999) Neuron , vol.24 , Issue.3 , pp. 751-762
    • Ishihara, T.1    Hong, M.2    Zhang, B.3    Nakagawa, Y.4    Lee, M.K.5
  • 109
    • 0035134081 scopus 로고    scopus 로고
    • Age dependent induction of congophilic neurofibrillary inclusions in tau transgenic mice
    • Ishihara T., Zhang B., Higuchi M., Yashiyama Y., Trojanowski J. Q., and Lee V. M.-Y. (2001) Age dependent induction of congophilic neurofibrillary inclusions in tau transgenic mice. Am. J. Pathol. 158(2), 555-562.
    • (2001) Am. J. Pathol. , vol.158 , Issue.2 , pp. 555-562
    • Ishihara, T.1    Zhang, B.2    Higuchi, M.3    Yashiyama, Y.4    Trojanowski, J.Q.5    Lee, V.M.-Y.6
  • 110
    • 0035882526 scopus 로고    scopus 로고
    • Attenuated neurodegenerative disease phenotype in tau transgenic mouse lacking neurofilaments
    • Ishihara T., Higuchi M., Zhang B., Yoshiyama Y., Hong M., Trojanowski J. Q., et al. (2001) Attenuated neurodegenerative disease phenotype in tau transgenic mouse lacking neurofilaments. J. Neurosci. 21(16), 6026-6035.
    • (2001) J. Neurosci. , vol.21 , Issue.16 , pp. 6026-6035
    • Ishihara, T.1    Higuchi, M.2    Zhang, B.3    Yoshiyama, Y.4    Hong, M.5    Trojanowski, J.Q.6
  • 111
    • 0024431202 scopus 로고
    • A case of adult-onset dementia with argyrophilic grains
    • Itagaki S., McGeer P. L., Akiyama H., et al. (1989) A case of adult-onset dementia with argyrophilic grains. Ann. Neurol. 26, 685-689.
    • (1989) Ann. Neurol. , vol.26 , pp. 685-689
    • Itagaki, S.1    McGeer, P.L.2    Akiyama, H.3
  • 112
    • 0027978991 scopus 로고
    • Neuronal and glial tau-positive inclusions in diverse neurologic diseases share common phosphorylation characteristics
    • Iwatsubo T., Hasegawa M., and Ihara Y. (1994) Neuronal and glial tau-positive inclusions in diverse neurologic diseases share common phosphorylation characteristics. Acta Neuropathol. 88(2), 129-136.
    • (1994) Acta Neuropathol. , vol.88 , Issue.2 , pp. 129-136
    • Iwatsubo, T.1    Hasegawa, M.2    Ihara, Y.3
  • 113
    • 0030590911 scopus 로고    scopus 로고
    • RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments
    • Kampers T., Friedhoff P., Biernat J., Mandelkow E. M., and Mandelkow E. (1996) RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments. FEBS Lett. 399(3), 344-349.
    • (1996) FEBS Lett. , vol.399 , Issue.3 , pp. 344-349
    • Kampers, T.1    Friedhoff, P.2    Biernat, J.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 114
    • 0026711059 scopus 로고
    • Fetal-type phosphorylation of the tau in paired helical filaments
    • Kanemaru K., Takio K., Miura R., Titani K., and Ihara Y. (1992) Fetal-type phosphorylation of the tau in paired helical filaments. J. Neurochem. 58(5), 1667-1675.
    • (1992) J. Neurochem. , vol.58 , Issue.5 , pp. 1667-1675
    • Kanemaru, K.1    Takio, K.2    Miura, R.3    Titani, K.4    Ihara, Y.5
  • 115
    • 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, 192-194.
    • (1963) Nature , vol.197 , pp. 192-194
    • Kidd, M.1
  • 116
    • 0035313624 scopus 로고    scopus 로고
    • Changes in microtubule stability and density in myelin-deficient shiverer mouse CNS axons
    • Kirkpatrick L. L., Witt A. S., Payne H. R., Shine H. D., and Brady S. T. (2001) Changes in microtubule stability and density in myelin-deficient shiverer mouse CNS axons. J. Neurosci. 21(7), 2288-2297.
    • (2001) J. Neurosci. , vol.21 , Issue.7 , pp. 2288-2297
    • Kirkpatrick, L.L.1    Witt, A.S.2    Payne, H.R.3    Shine, H.D.4    Brady, S.T.5
  • 117
    • 0027426029 scopus 로고
    • A cdc2-related kinase PSSALRE/cdk5 is homologous with the 30 kDa subunit of tau protein kinase II, a proline-directed protein kinase associated with microtubule
    • Kobayashi S., Ishiguro K., Omori A., Takamatsu M., Arioka M., Imahori K., et al. (1993) A cdc2-related kinase PSSALRE/cdk5 is homologous with the 30 kDa subunit of tau protein kinase II, a proline-directed protein kinase associated with microtubule. FEBS Lett. 335(2), 171-175.
    • (1993) FEBS Lett. , vol.335 , Issue.2 , pp. 171-175
    • Kobayashi, S.1    Ishiguro, K.2    Omori, A.3    Takamatsu, M.4    Arioka, M.5    Imahori, K.6
  • 118
    • 0031655746 scopus 로고    scopus 로고
    • Astrocytic plaques and tufts of abnormal fibers do not coexist in corticobasal degeneration and progressive supranuclear palsy
    • Komori T., Arai N., Oda M., Nakayama H., Mori H., Yagishita S., et al. (1998) Astrocytic plaques and tufts of abnormal fibers do not coexist in corticobasal degeneration and progressive supranuclear palsy. Acta Neuropathol. (Berl) 96(4), 401-408.
    • (1998) Acta Neuropathol. (Berl) , vol.96 , Issue.4 , pp. 401-408
    • Komori, T.1    Arai, N.2    Oda, M.3    Nakayama, H.4    Mori, H.5    Yagishita, S.6
  • 119
    • 0032886469 scopus 로고    scopus 로고
    • Tau-positive glial inclusions in progressive supranuclear palsy, corticobasal degeneration and Pick's disease
    • Komori T. (1999) Tau-positive glial inclusions in progressive supranuclear palsy, corticobasal degeneration and Pick's disease. Brain Pathol. 9(4), 663-679.
    • (1999) Brain Pathol. , vol.9 , Issue.4 , pp. 663-679
    • Komori, T.1
  • 120
    • 0024109663 scopus 로고
    • The carboxyl third of tau is tightly bound to paired helical filaments
    • Kondo J., Honda T., Mori H., Hamada Y., Miura R., Ogawara M., et al. (1988) The carboxyl third of tau is tightly bound to paired helical filaments. Neuron 1(9), 827-834.
    • (1988) Neuron , vol.1 , Issue.9 , pp. 827-834
    • Kondo, J.1    Honda, T.2    Mori, H.3    Hamada, Y.4    Miura, R.5    Ogawara, M.6
  • 121
    • 0024109687 scopus 로고
    • Epitopes that span the tau molecule are shared with paired helical filaments
    • Kosik K. S., Orecchio L. D., Binder L., Trojanowski J. Q., Lee V. M.-Y., and Lee G. (1988) Epitopes that span the tau molecule are shared with paired helical filaments. Neuron 1(9), 817-825.
    • (1988) Neuron , vol.1 , Issue.9 , pp. 817-825
    • Kosik, K.S.1    Orecchio, L.D.2    Binder, L.3    Trojanowski, J.Q.4    Lee, V.M.-Y.5    Lee, G.6
  • 122
    • 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(4), 1389-1397.
    • (1989) Neuron , vol.2 , Issue.4 , pp. 1389-1397
    • Kosik, K.S.1    Orecchio, L.D.2    Bakalis, S.3    Neve, R.L.4
  • 123
    • 0023626638 scopus 로고
    • Axonal disruption and aberrant localization of tau protein characterize the neuropil pathology of Alzheimer's disease
    • Kowall N. W. and Kosik K. S. (1987) Axonal disruption and aberrant localization of tau protein characterize the neuropil pathology of Alzheimer's disease. Ann. Neurol. 22(5), 639-643.
    • (1987) Ann. Neurol. , vol.22 , Issue.5 , pp. 639-643
    • Kowall, N.W.1    Kosik, K.S.2
  • 124
    • 0028091523 scopus 로고
    • Ultrastructure and biochemical composition of paired helical filaments in corticobasal degeneration
    • Ksiezak-Reding H., Morgan K., Mattiace L. A., et al. (1994) Ultrastructure and biochemical composition of paired helical filaments in corticobasal degeneration. Am. J. Pathol. 145, 1496-1508.
    • (1994) Am. J. Pathol. , vol.145 , pp. 1496-1508
    • Ksiezak-Reding, H.1    Morgan, K.2    Mattiace, L.A.3
  • 125
    • 0023905288 scopus 로고
    • The primary structure and heterogeneity of tau protein from mouse brain
    • Lee G., Cowan N., and Kirschner M. W. (1988) The primary structure and heterogeneity of tau protein from mouse brain. Science 239 (4837), 285-288.
    • (1988) Science , vol.239 , Issue.4837 , pp. 285-288
    • Lee, G.1    Cowan, N.2    Kirschner, M.W.3
  • 126
    • 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(6), 1615-1624.
    • (1989) Neuron , vol.2 , Issue.6 , pp. 1615-1624
    • Lee, G.1    Neve, R.L.2    Kosik, K.S.3
  • 127
    • 0025904444 scopus 로고
    • A68: A major subunit of paired helical filaments and derivatized forms of normal Tau
    • Lee V. M.-Y., Balin B. J., Otvos L. Jr., and Trojanowski J. Q. (1991) A68: a major subunit of paired helical filaments and derivatized forms of normal Tau. Science 251(4994), 675-678.
    • (1991) Science , vol.251 , Issue.4994 , pp. 675-678
    • Lee, V.M.-Y.1    Balin, B.J.2    Otvos L., Jr.3    Trojanowski, J.Q.4
  • 129
    • 0033798031 scopus 로고    scopus 로고
    • Paullones are potent inhibitors of glycogen synthase kinase-3beta and cyclin-dependent kinase 5/p25
    • Leost M., Schultz C., Link A., Wu Y. Z., Biernat J., Mandelkow E. M., et al. (2000) Paullones are potent inhibitors of glycogen synthase kinase-3beta and cyclin-dependent kinase 5/p25. Eur. J. Biochem. 267(19), 5983-5994.
    • (2000) Eur. J. Biochem. , vol.267 , Issue.19 , pp. 5983-5994
    • Leost, M.1    Schultz, C.2    Link, A.3    Wu, Y.Z.4    Biernat, J.5    Mandelkow, E.M.6
  • 130
    • 0034426011 scopus 로고    scopus 로고
    • Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein
    • Lewis J., McGowan E., Rockwood J., Melrose H., Nacharaju P., et al. (2000) Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein. Nat. Genet. 25(4), 402-405.
    • (2000) Nat. Genet. , vol.25 , Issue.4 , pp. 402-405
    • Lewis, J.1    McGowan, E.2    Rockwood, J.3    Melrose, H.4    Nacharaju, P.5
  • 131
    • 17944382037 scopus 로고    scopus 로고
    • Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP
    • Lewis J., Dickson D. W., Lin W. L., Chisholm L., Corral A., Jones G., et al. (2001) Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP. Science 293(5534), 1487-1491.
    • (2001) Science , vol.293 , Issue.5534 , pp. 1487-1491
    • Lewis, J.1    Dickson, D.W.2    Lin, W.L.3    Chisholm, L.4    Corral, A.5    Jones, G.6
  • 132
    • 0031887227 scopus 로고    scopus 로고
    • Cognitive, neuroimaging, and pathological studies in a patient with Pick's disease
    • Lieberman A. P., Trojanowski J. Q., Lee V. M.-Y., et al. (1998) Cognitive, neuroimaging, and pathological studies in a patient with Pick's disease. Ann. Neurol. 43, 259-265.
    • (1998) Ann. Neurol. , vol.43 , pp. 259-265
    • Lieberman, A.P.1    Trojanowski, J.Q.2    Lee, V.M.-Y.3
  • 133
    • 0021338217 scopus 로고    scopus 로고
    • Phosphorylation affects the ability of tau protein to promote microtubule assembly
    • Lindwall G. and Cole R. D. (19) Phosphorylation affects the ability of tau protein to promote microtubule assembly. J. Biol. Chem. 259(8), 5301-5305.
    • J. Biol. Chem. , vol.259 , Issue.8 , pp. 5301-5305
    • Lindwall, G.1    Cole, R.D.2
  • 134
    • 0026597280 scopus 로고
    • Phosphorylation by cAMP-dependent protein kinase inhibits the degradation of tau by calpain
    • Litersky J. M. and Johnson G. V. (1992) Phosphorylation by cAMP-dependent protein kinase inhibits the degradation of tau by calpain. J. Biol. Chem. 267(3), 1563-1568.
    • (1992) J. Biol. Chem. , vol.267 , Issue.3 , pp. 1563-1568
    • Litersky, J.M.1    Johnson, G.V.2
  • 135
    • 0027195313 scopus 로고
    • Subcellular localization of tau mRNA in differentiating neuronal cell culture: Implications for neuronal polarity
    • Litman P., Barg J., Rindzoonski L., and Ginzburg I. (1993) Subcellular localization of tau mRNA in differentiating neuronal cell culture: implications for neuronal polarity. Neuron 10(4), 627-638.
    • (1993) Neuron , vol.10 , Issue.4 , pp. 627-638
    • Litman, P.1    Barg, J.2    Rindzoonski, L.3    Ginzburg, I.4
  • 136
    • 8944226575 scopus 로고    scopus 로고
    • Clinical research criteria for the diagnosis of progressive supranuclear palsy (Steele-Richardson-Olszewski syndrome): Report of the NINDS-SPSP international workshop
    • Litvan I., Agid Y., Calne D., Campbell G., Dubois B., et al. (1996) Clinical research criteria for the diagnosis of progressive supranuclear palsy (Steele-Richardson-Olszewski syndrome): report of the NINDS-SPSP international workshop. Neurology 47(1), 1-9.
    • (1996) Neurology , vol.47 , Issue.1 , pp. 1-9
    • Litvan, I.1    Agid, Y.2    Calne, D.3    Campbell, G.4    Dubois, B.5
  • 137
    • 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. Sci. USA 92(22), 10,369-10,373.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , Issue.22 , pp. 10369-10373
    • LoPresti, P.1    Szuchet, S.2    Papasozomenos, S.C.3    Zinkowski, R.P.4    Binder, L.I.5
  • 138
    • 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 188, 119-129.
    • (1995) Brain , vol.188 , pp. 119-129
    • Love, S.1    Bridges, L.R.2    Case, C.P.3
  • 139
    • 0030714092 scopus 로고    scopus 로고
    • Elevated 4-hydroxy-nonenal in ventricular fluid in Alzheimer's disease
    • Lovell M. A., Ehmann W. D., Mattson M. P., and Markesbery W. R. (1997) Elevated 4-hydroxy-nonenal in ventricular fluid in Alzheimer's disease. Neurobiol. Aging 18, 457-461.
    • (1997) Neurobiol. Aging , vol.18 , pp. 457-461
    • Lovell, M.A.1    Ehmann, W.D.2    Mattson, M.P.3    Markesbery, W.R.4
  • 140
    • 0029994754 scopus 로고    scopus 로고
    • Phosphorylation of tau by glycogen synthase kinase-3 beta in intact mammalian cells: The effects on the organization and stability of microtubules
    • Lovestone S., Hartley C. L., Pearce J., and Anderton B. H. (1996) Phosphorylation of tau by glycogen synthase kinase-3 beta in intact mammalian cells: the effects on the organization and stability of microtubules. Neuroscience 73(4), 1145-1157.
    • (1996) Neuroscience , vol.73 , Issue.4 , pp. 1145-1157
    • Lovestone, S.1    Hartley, C.L.2    Pearce, J.3    Anderton, B.H.4
  • 141
    • 0033561207 scopus 로고    scopus 로고
    • Lithium reduces tau phosphorylation: Effects in living cells and in neurons at therapeutic concentrations
    • Lovestone S., Davis D. R., Webster M. T., Kaech S., Brion J. P., Matus A., et al. (1999) Lithium reduces tau phosphorylation: effects in living cells and in neurons at therapeutic concentrations. Biol. Psychiatry 45(8), 995-1003.
    • (1999) Biol. Psychiatry , vol.45 , Issue.8 , pp. 995-1003
    • Lovestone, S.1    Davis, D.R.2    Webster, M.T.3    Kaech, S.4    Brion, J.P.5    Matus, A.6
  • 142
    • 0026619584 scopus 로고
    • Glycogen synthase kinase-3 and the Alzheimer-like state of microtubule-associated protein tau
    • Mandelkow E. M., Drewes G., Biernat J., Gustke N., Van Lint J., Vandenheede J. R., et al. (1992) Glycogen synthase kinase-3 and the Alzheimer-like state of microtubule-associated protein tau. FEBS Lett. 314(3), 315-321.
    • (1992) FEBS Lett. , vol.314 , Issue.3 , pp. 315-321
    • Mandelkow, E.M.1    Drewes, G.2    Biernat, J.3    Gustke, N.4    Van Lint, J.5    Vandenheede, J.R.6
  • 143
    • 0025331812 scopus 로고
    • Spinal cord neurofibrillary tangles of Guamanian amyotrophic lateral sclerosis and parkinsonism-dementia complex: An immunohistochemical study
    • Matsumoto S., Hirano A., and Goto S. (1990) Spinal cord neurofibrillary tangles of Guamanian amyotrophic lateral sclerosis and parkinsonism-dementia complex: an immunohistochemical study. Neurology 40, 975-979.
    • (1990) Neurology , vol.40 , pp. 975-979
    • Matsumoto, S.1    Hirano, A.2    Goto, S.3
  • 144
    • 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., Van deVoorde A., O'Connor M., Trojanowski J. Q., et al. (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(4), 989-1002.
    • (1994) Neuron , vol.13 , Issue.4 , pp. 989-1002
    • Matsuo, E.S.1    Shin, R.W.2    Billingsley, M.L.3    Van deVoorde, A.4    O'Connor, M.5    Trojanowski, J.Q.6
  • 145
    • 0025273543 scopus 로고
    • Antigenic changes similar to those seen in neurofibrillary tangles are elicited by glutamate and Ca2+ influx in cultured hippocampal neurons
    • Mattson M. P. (1990) Antigenic changes similar to those seen in neurofibrillary tangles are elicited by glutamate and Ca2+ influx in cultured hippocampal neurons. Neuron 4, 105-117.
    • (1990) Neuron , vol.4 , pp. 105-117
    • Mattson, M.P.1
  • 146
    • 0030779677 scopus 로고    scopus 로고
    • Cellular actions of beta-amyloid precursor protein and its soluble and fibrillogenic derivatives
    • Mattson M. P. (1997) Cellular actions of beta-amyloid precursor protein and its soluble and fibrillogenic derivatives. Physiol. Rev. 77, 1081-1132.
    • (1997) Physiol. Rev. , vol.77 , pp. 1081-1132
    • Mattson, M.P.1
  • 147
    • 0030797336 scopus 로고    scopus 로고
    • 4-Hydroxynonenal, a product of lipid peroxidation, inhibits dephosphorylation of the microtubule-associated protein tau
    • Mattson M. P., Fu W., Waeg G., and Uchida K. (1997) 4-Hydroxynonenal, a product of lipid peroxidation, inhibits dephosphorylation of the microtubule-associated protein tau. Neuroreport 8, 2275-2281.
    • (1997) Neuroreport , vol.8 , pp. 2275-2281
    • Mattson, M.P.1    Fu, W.2    Waeg, G.3    Uchida, K.4
  • 148
    • 0028172239 scopus 로고
    • The phosphorylation state of tau in the developing rat brain is regulated by phosphoprotein phosphatases
    • Mawal-Dewan M., Henley J., Van de Voorde 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(49), 30,981-30,987.
    • (1994) J. Biol. Chem. , vol.269 , Issue.49 , pp. 30981-30987
    • Mawal-Dewan, M.1    Henley, J.2    Van de Voorde, A.3    Trojanowski, J.Q.4    Lee, V.M.-Y.5
  • 149
    • 0029823961 scopus 로고    scopus 로고
    • Identification of phosphorylation sites in PHF-TAU from patients with Guam amyotrophic lateral sclerosis/ parkinsonism-dementia complex
    • Mawal-Dewan M., Schmidt M. L., Balin B., Perl D. P., Lee V. M.-Y., and Trojanowski J. Q. (1996) Identification of phosphorylation sites in PHF-TAU from patients with Guam amyotrophic lateral sclerosis/ parkinsonism-dementia complex. J. Neuropathol. Exp. Neurol. 55(10), 1051-1059.
    • (1996) J. Neuropathol. Exp. Neurol. , vol.55 , Issue.10 , pp. 1051-1059
    • Mawal-Dewan, M.1    Schmidt, M.L.2    Balin, B.3    Perl, D.P.4    Lee, V.M.-Y.5    Trojanowski, J.Q.6
  • 150
    • 0025773225 scopus 로고
    • Neuritic pathology and dementia in Alzheimer's disease
    • McKee A. C., Kosik K. S., and Kowall N. W. (1991) Neuritic pathology and dementia in Alzheimer's disease. Ann. Neurol. 30(2), 156-165.
    • (1991) Ann. Neurol. , vol.30 , Issue.2 , pp. 156-165
    • McKee, A.C.1    Kosik, K.S.2    Kowall, N.W.3
  • 151
    • 0034764622 scopus 로고    scopus 로고
    • Clinical and pathological diagnosis of frontotemporal dementia: Report of the Work Group on Frontotemporal Dementia and Pick's Disease
    • Work Group on Frontotemporal Dementia and Pick's Disease
    • McKhann G. M., Albert M. S., Grossman M., Miller B., Dickson D., and Trojanowski J. Q. (2001) Work Group on Frontotemporal Dementia and Pick's Disease. Clinical and pathological diagnosis of frontotemporal dementia: report of the Work Group on Frontotemporal Dementia and Pick's Disease. Arch. Neurol. 58(11), 1803-1809.
    • (2001) Arch. Neurol. , vol.58 , Issue.11 , pp. 1803-1809
    • McKhann, G.M.1    Albert, M.S.2    Grossman, M.3    Miller, B.4    Dickson, D.5    Trojanowski, J.Q.6
  • 152
    • 0028266611 scopus 로고
    • Association of measles virus with neurofibrillary tangles in subacute sclerosing panencephalitis: A combined in situ hybridization and immunocytochemical investigation
    • McQuaid S., Allen 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. Neurobiol. 20, 103-110.
    • (1994) Neuropathol. Appl. Neurobiol. , vol.20 , pp. 103-110
    • McQuaid, S.1    Allen, I.V.2    McMahon, J.3    Kirk, J.4
  • 153
    • 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(12), 8259-8267.
    • (1995) J. Neurosci. , vol.15 , Issue.12 , pp. 8259-8267
    • Mercken, M.1    Fischer, I.2    Kosik, K.S.3    Nixon, R.A.4
  • 154
    • 0029039987 scopus 로고
    • Differential sensitivity to proteolysis by brain calpain of adult human tau, fetal human tau and PHF-tau
    • Mercken M., Grynspan F., and Nixon R. A. (1995) Differential sensitivity to proteolysis by brain calpain of adult human tau, fetal human tau and PHF-tau. FEBS Lett. 368(1), 10-14.
    • (1995) FEBS Lett. , vol.368 , Issue.1 , pp. 10-14
    • Mercken, M.1    Grynspan, F.2    Nixon, R.A.3
  • 155
    • 0030813929 scopus 로고    scopus 로고
    • Selective destruction of stable microtubules and axons by inhibitors of protein serine/threonine phosphatases in cultured human neurons
    • Merrick S. E., Trojanowski J. Q., and Lee V. M.-Y. (1997) Selective destruction of stable microtubules and axons by inhibitors of protein serine/threonine phosphatases in cultured human neurons. J. Neurosci. 17(15), 5726-5737.
    • (1997) J. Neurosci. , vol.17 , Issue.15 , pp. 5726-5737
    • Merrick, S.E.1    Trojanowski, J.Q.2    Lee, V.M.-Y.3
  • 157
    • 0027936091 scopus 로고
    • Corticobasal degeneration: A disease with widespread appearance of abnormal tau and neurofibrillary tangles, and its relation to progressive supranuclear palsy
    • Mori H., Nishimura M., Namba Y., and Oda M. (1994) Corticobasal degeneration: a disease with widespread appearance of abnormal tau and neurofibrillary tangles, and its relation to progressive supranuclear palsy. Acta Neuropathol. (Berl) 88, 113-121.
    • (1994) Acta Neuropathol. (Berl) , vol.88 , pp. 113-121
    • Mori, H.1    Nishimura, M.2    Namba, Y.3    Oda, M.4
  • 159
    • 0031567583 scopus 로고    scopus 로고
    • Lithium inhibits Alzheimer's disease-like tau protein phosphorylation in neurons
    • Munoz-Montano J. R., Moreno F. J., Avila J., and Diaz-Nido J. (1997) Lithium inhibits Alzheimer's disease-like tau protein phosphorylation in neurons. FEBS Lett. 411(2-3), 183-188.
    • (1997) FEBS Lett. , vol.411 , Issue.2-3 , pp. 183-188
    • Munoz-Montano, J.R.1    Moreno, F.J.2    Avila, J.3    Diaz-Nido, J.4
  • 160
    • 0025273951 scopus 로고
    • Immunocytochemical and ultrastructural studies of Pick's disease
    • Murayama S., Mori H., Ihara Y., and Tomonaga M. (1990) Immunocytochemical and ultrastructural studies of Pick's disease. Ann. Neurol. 27, 394-405.
    • (1990) Ann. Neurol. , vol.27 , pp. 394-405
    • Murayama, S.1    Mori, H.2    Ihara, Y.3    Tomonaga, M.4
  • 161
    • 0032763203 scopus 로고    scopus 로고
    • Tau gene mutation G389R causes a tauopathy with abundant Pick body-like inclusions and axonal deposits
    • Murrell J. R., Spillantini M. G., Zolo P., Guazzelli M., Smith M. J., et al. (1999) Tau gene mutation G389R causes a tauopathy with abundant Pick body-like inclusions and axonal deposits. J. Neuropathol. Exp. Neurol. 58(12), 1207-1226.
    • (1999) J. Neuropathol. Exp. Neurol. , vol.58 , Issue.12 , pp. 1207-1226
    • Murrell, J.R.1    Spillantini, M.G.2    Zolo, P.3    Guazzelli, M.4    Smith, M.J.5
  • 162
    • 0033011181 scopus 로고    scopus 로고
    • Accelerated filament formation from tau protein with specific FTDP-17 missense mutations
    • Nacharaju P., Lewis J., Easson C., Yen S., Hackett J., et al. (1999) Accelerated filament formation from tau protein with specific FTDP-17 missense mutations. FEBS Lett. 447(2-3), 195-199.
    • (1999) FEBS Lett. , vol.447 , Issue.2-3 , pp. 195-199
    • Nacharaju, P.1    Lewis, J.2    Easson, C.3    Yen, S.4    Hackett, J.5
  • 163
    • 0016367146 scopus 로고
    • Microtubule densities and total numbers in selected axons of the crayfish abdominal nerve cord
    • Nadelhaft I. (1974) Microtubule densities and total numbers in selected axons of the crayfish abdominal nerve cord. J. Neurocytol. 3(1), 73-86.
    • (1974) J. Neurocytol. , vol.3 , Issue.1 , pp. 73-86
    • Nadelhaft, I.1
  • 164
    • 0022827447 scopus 로고
    • Identification of cDNA clones for the human microtubule-associated protein tau and chromosomal localization of the genes for tau and microtubule-associated protein 2
    • Neve R. L., Harris P., Kosik K. S., Kurmit D. M., and Donlon T. A. (1986) Identification of cDNA clones for the human microtubule-associated protein tau and chromosomal localization of the genes for tau and microtubule-associated protein 2. Brain Res. 387(3), 271-280.
    • (1986) Brain Res. , vol.387 , Issue.3 , pp. 271-280
    • Neve, R.L.1    Harris, P.2    Kosik, K.S.3    Kurmit, D.M.4    Donlon, T.A.5
  • 165
    • 0006325405 scopus 로고    scopus 로고
    • Alzheimer's disease: A re-examination of the amyloid hypothesis
    • Neve R. L. and Robakis N. K. (1998) Alzheimer's disease: a re-examination of the amyloid hypothesis. Trends Neurosci. 21(1), 15-19.
    • (1998) Trends Neurosci. , vol.21 , Issue.1 , pp. 15-19
    • Neve, R.L.1    Robakis, N.K.2
  • 166
    • 0026700385 scopus 로고
    • Glial fibrillary tangles with straight tubules in the brains of patients with progressive supranuclear palsy
    • Nishimura M., Namba Y., Ikeda K., and Oda M. (1992) Glial fibrillary tangles with straight tubules in the brains of patients with progressive supranuclear palsy. Neurosci. Lett. 143(1-2), 35-38.
    • (1992) Neurosci. Lett. , vol.143 , Issue.1-2 , pp. 35-38
    • Nishimura, M.1    Namba, Y.2    Ikeda, K.3    Oda, M.4
  • 167
    • 0024354716 scopus 로고
    • Rapid turnover of microtubule-associated protein MAP2 in the axon revealed by microinjection of biotinylated MAP2 into cultured neurons
    • Okabe S. and Hirokawa N. (1989) Rapid turnover of microtubule-associated protein MAP2 in the axon revealed by microinjection of biotinylated MAP2 into cultured neurons. Proc. Natl. Acad. Sci. USA 86(11), 4127-4131.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , Issue.11 , pp. 4127-4131
    • Okabe, S.1    Hirokawa, N.2
  • 168
    • 0033540060 scopus 로고    scopus 로고
    • Conversion of p35 to p25 deregulates Cdk5 activity and promotes neurodegeneration
    • Patrick G. N., Zukerberg L., Nikolic M., de la Monte S., Dikkes P., and Tsai L. H. (1999) Conversion of p35 to p25 deregulates Cdk5 activity and promotes neurodegeneration. Nature 402(6762), 615-622.
    • (1999) Nature , vol.402 , Issue.6762 , pp. 615-622
    • Patrick, G.N.1    Zukerberg, L.2    Nikolic, M.3    De la Monte, S.4    Dikkes, P.5    Tsai, L.H.6
  • 169
    • 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. (Berl) 81, 89-94.
    • (1990) Acta Neuropathol. (Berl) , vol.81 , pp. 89-94
    • Paulus, W.1    Selim, M.2
  • 170
    • 0029796168 scopus 로고    scopus 로고
    • Polymerization of tau into filaments in the presence of heparin: The minimal sequence required for tau-tau interaction
    • Perez M., Valpuesta J. M., Medina M., Montejo G., and Avila J. (1996) Polymerization of tau into filaments in the presence of heparin: the minimal sequence required for tau-tau interaction. J. Neurochem. 67(3), 1183-1190.
    • (1996) J. Neurochem. , vol.67 , Issue.3 , pp. 1183-1190
    • Perez, M.1    Valpuesta, J.M.2    Medina, M.3    Montejo, G.4    Avila, J.5
  • 171
    • 0023175260 scopus 로고
    • Filaments of Pick's bodies contain altered cytoskeletal elements
    • Perry G., Stwart D., Friedman R., et al. (1987) Filaments of Pick's bodies contain altered cytoskeletal elements. Am. J. Pathol. 127, 559-568.
    • (1987) Am. J. Pathol. , vol.127 , pp. 559-568
    • Perry, G.1    Stwart, D.2    Friedman, R.3
  • 172
    • 0033669232 scopus 로고    scopus 로고
    • Pick's disease is associated with mutations in the tau gene
    • Pickering-Brown S., Baker M., Yen S. H., Liu W. K., Hasegawa M., et al. (2000) Pick's disease is associated with mutations in the tau gene. Ann. Neurol. 48(5), 806-808.
    • (2000) Ann. Neurol. , vol.48 , Issue.5 , pp. 806-808
    • Pickering-Brown, S.1    Baker, M.2    Yen, S.H.3    Liu, W.K.4    Hasegawa, M.5
  • 173
    • 0022976136 scopus 로고
    • Filamentous aggregates in Pick's disease, progressive supranuclear palsy, and Alzheimer's disease share antigenic determinants with microtubule-associated protein, tau
    • Pollock N. J., Mirra S. S., Binder L. I., Hansen L. A., and Wood J. G. (1986) Filamentous aggregates in Pick's disease, progressive supranuclear palsy, and Alzheimer's disease share antigenic determinants with microtubule-associated protein, tau. Lancet 2(8517), 1211.
    • (1986) Lancet , vol.2 , Issue.8517 , pp. 1211
    • Pollock, N.J.1    Mirra, S.S.2    Binder, L.I.3    Hansen, L.A.4    Wood, J.G.5
  • 174
    • 14444284106 scopus 로고    scopus 로고
    • Tau is a candidate gene for chromosome 17 frontotemporal dementia
    • Poorkaj P., Bird T. D., Wijsman E., Nemens E., Garruto R. M., et al. (1998) Tau is a candidate gene for chromosome 17 frontotemporal dementia. Ann. Neurol. 43(6), 815-825.
    • (1998) Ann. Neurol. , vol.43 , Issue.6 , pp. 815-825
    • Poorkaj, P.1    Bird, T.D.2    Wijsman, E.3    Nemens, E.4    Garruto, R.M.5
  • 175
    • 0029850476 scopus 로고    scopus 로고
    • Pick's disease: Hyperphosphorylated tau protein segregates to the somatoaxonal compartment
    • Probst A., Tolnay M., Langui D., Goedert M., and Spillantini M. G. (1996) Pick's disease: hyperphosphorylated tau protein segregates to the somatoaxonal compartment. Acta Neuropathol. (Berl) 92, 588-596.
    • (1996) Acta Neuropathol. (Berl) , vol.92 , pp. 588-596
    • Probst, A.1    Tolnay, M.2    Langui, D.3    Goedert, M.4    Spillantini, M.G.5
  • 176
    • 0342803685 scopus 로고    scopus 로고
    • Axonopathy and amyotrophy in mice transgenic for human four-repeat tau protein
    • Probst A., Götz J., Wiederhold K. H., Tolnay M., Mistl C., et al. (2000) Axonopathy and amyotrophy in mice transgenic for human four-repeat tau protein. Acta Neuropathol. 99(5), 469-481.
    • (2000) Acta Neuropathol. , vol.99 , Issue.5 , pp. 469-481
    • Probst, A.1    Götz, J.2    Wiederhold, K.H.3    Tolnay, M.4    Mistl, C.5
  • 177
    • 0000146080 scopus 로고
    • Differential expression of distinct microtubule-associated proteins during brain development
    • Reiderer B. and Matus A. (1985) Differential expression of distinct microtubule-associated proteins during brain development. Proc. Natl. Acad. Sci. USA 82(17), 6006-6009.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , Issue.17 , pp. 6006-6009
    • Reiderer, B.1    Matus, A.2
  • 178
    • 0030943263 scopus 로고    scopus 로고
    • Stress-activated protein kinase/c-jun N-terminal kinase phosphorylates tau protein
    • Reynolds C. H., Utton M. A., Gibb G. M., Yates A., and Anderton B. H. (1997) Stress-activated protein kinase/c-jun N-terminal kinase phosphorylates tau protein. J. Neurochem. 68(4), 1736-1744.
    • (1997) J. Neurochem. , vol.68 , Issue.4 , pp. 1736-1744
    • Reynolds, C.H.1    Utton, M.A.2    Gibb, G.M.3    Yates, A.4    Anderton, B.H.5
  • 180
    • 0033070197 scopus 로고    scopus 로고
    • High prevalence of mutations in the microtubule-associated protein tau in a population study of frontotemporal dementia in the Netherlands
    • Rizzu P., Van Swieten J. C., Joosse M., Hasegawa M., Stevens M., et al. (1999) High prevalence of mutations in the microtubule-associated protein tau in a population study of frontotemporal dementia in the Netherlands. Am. J. Hum. Genet. 64(2), 414-421.
    • (1999) Am. J. Hum. Genet. , vol.64 , Issue.2 , pp. 414-421
    • Rizzu, P.1    Van Swieten, J.C.2    Joosse, M.3    Hasegawa, M.4    Stevens, M.5
  • 181
    • 0029971280 scopus 로고    scopus 로고
    • Neurofibrillary tangles in progressive supranuclear palsy contain the same tau epitopes identified in Alzheimer's disease PHF-tau
    • Schmidt M. L., Huang R., Martin J. A., et al. (1996) Neurofibrillary tangles in progressive supranuclear palsy contain the same tau epitopes identified in Alzheimer's disease PHF-tau. J. Neuropathol. Exp. Neurol. 55, 534-539.
    • (1996) J. Neuropathol. Exp. Neurol. , vol.55 , pp. 534-539
    • Schmidt, M.L.1    Huang, R.2    Martin, J.A.3
  • 182
    • 0034766790 scopus 로고    scopus 로고
    • Spinal cord neurofibrillary pathology in Alzheimer disease and Guam Parkinsonism-dementia complex
    • Schmidt M. L., Zhukareva V., Perl D. P., Sheridan S. K., Schuck T., Lee V. M.-Y., et al. (2001) Spinal cord neurofibrillary pathology in Alzheimer disease and Guam Parkinsonism-dementia complex. J. Neuropathol. Exp. Neurol. 60(11), 1075-1086.
    • (2001) J. Neuropathol. Exp. Neurol. , vol.60 , Issue.11 , pp. 1075-1086
    • Schmidt, M.L.1    Zhukareva, V.2    Perl, D.P.3    Sheridan, S.K.4    Schuck, T.5    Lee, V.M.-Y.6
  • 183
    • 0033596946 scopus 로고    scopus 로고
    • Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments
    • Schneider A., Biernat J., von Bergen M., Mandelkow E., and Mandelkow E. M. (1999) Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments. Biochemistry 38(12), 3549-3558.
    • (1999) Biochemistry , vol.38 , Issue.12 , pp. 3549-3558
    • Schneider, A.1    Biernat, J.2    Von Bergen, M.3    Mandelkow, E.4    Mandelkow, E.M.5
  • 184
    • 0024589232 scopus 로고
    • Immunocytochemical characterization of neurofibrillary tangles in amyotrophic lateral sclerosis and parkinsonism-dementia of Guam
    • Shankar S. K., Yanagihara R., Garruto R. M., Grundke-Iqbal I., Kosik K. S., and Gajdusek D. C. (1989) Immunocytochemical characterization of neurofibrillary tangles in amyotrophic lateral sclerosis and parkinsonism-dementia of Guam. Ann. Neurol. 25, 146-151.
    • (1989) Ann. Neurol. , vol.25 , pp. 146-151
    • Shankar, S.K.1    Yanagihara, R.2    Garruto, R.M.3    Grundke-Iqbal, I.4    Kosik, K.S.5    Gajdusek, D.C.6
  • 185
    • 0025786986 scopus 로고
    • Hydrated autoclave pretreatment enhances tau immunoreactivity in formalin-fixed normal and alzheimer's disease brain tissues
    • Shin R. W., Iwaki T., Kitamoto T., and Tateishi J. (1991) Hydrated autoclave pretreatment enhances tau immunoreactivity in formalin-fixed normal and alzheimer's disease brain tissues. Lab. Investig. 64(5), 693-702.
    • (1991) Lab. Investig. , vol.64 , Issue.5 , pp. 693-702
    • Shin, R.W.1    Iwaki, T.2    Kitamoto, T.3    Tateishi, J.4
  • 186
    • 0025223441 scopus 로고
    • Early accumulation of heparin sulfate in neurons and in the beta-amyloid protein-containing lesions of Alzheimer's disease and Down's syndrome
    • Snow A. D., Mar H., Nochlin D., Sekiguchi R. T., Kimata K., Koike Y., et al. (1990) Early accumulation of heparin sulfate in neurons and in the beta-amyloid protein-containing lesions of Alzheimer's disease and Down's syndrome. Am. J. Pathol. 137(5), 1253-1270.
    • (1990) Am. J. Pathol. , vol.137 , Issue.5 , pp. 1253-1270
    • Snow, A.D.1    Mar, H.2    Nochlin, D.3    Sekiguchi, R.T.4    Kimata, K.5    Koike, Y.6
  • 187
    • 0028924295 scopus 로고
    • A novel pool of protein phosphatase 2A is associated with microtubules and is regulated during the cell cycle
    • Sontag E., Nunbhakdi-Craig 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(6), 1131-1144.
    • (1995) J. Cell Biol. , vol.128 , Issue.6 , pp. 1131-1144
    • Sontag, E.1    Nunbhakdi-Craig, V.2    Bloom, G.S.3    Mumby, M.C.4
  • 188
    • 0030461275 scopus 로고    scopus 로고
    • Regulation of the phosphorylation state and microtubule-binding activity of Tau by protein phosphatase 2A
    • Sontag E., Nunbhakdi-Craig V., Lee G., Bloom G. S., and Mumby M. C. (1996) Regulation of the phosphorylation state and microtubule-binding activity of Tau by protein phosphatase 2A. Neuron 17(6), 1201-1207.
    • (1996) Neuron , vol.17 , Issue.6 , pp. 1201-1207
    • Sontag, E.1    Nunbhakdi-Craig, V.2    Lee, G.3    Bloom, G.S.4    Mumby, M.C.5
  • 190
    • 0033663879 scopus 로고    scopus 로고
    • A novel tau mutation (N296N) in familial dementia with swollen achromatic neurons and corticobasal inclusion bodies
    • Spillantini M. G., Yoshida H., Rizzini C., Lantos P. L., Khan N., et al. (2000) A novel tau mutation (N296N) in familial dementia with swollen achromatic neurons and corticobasal inclusion bodies. Ann. Neurol. 48(6), 939-943.
    • (2000) Ann. Neurol. , vol.48 , Issue.6 , pp. 939-943
    • Spillantini, M.G.1    Yoshida, H.2    Rizzini, C.3    Lantos, P.L.4    Khan, N.5
  • 191
    • 0032786370 scopus 로고    scopus 로고
    • Prominent axonopathy in the brain and spinal cord of transgenic mice overexpressing four-repeat human tau protein
    • Spittaels K., Van den Haute C., Van Dorpe J., Bruynseels K., Vandezande K., et al. (1999) Prominent axonopathy in the brain and spinal cord of transgenic mice overexpressing four-repeat human tau protein. Am. J. Pathol. 155(6), 2153-2165.
    • (1999) Am. J. Pathol. , vol.155 , Issue.6 , pp. 2153-2165
    • Spittaels, K.1    Van den Haute, C.2    Van Dorpe, J.3    Bruynseels, K.4    Vandezande, K.5
  • 192
    • 0034731461 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3beta phosphorylates protein tau and rescues the axonopathy in the central nervous system of human four-repeat tau transgenic mice
    • Spittaels K., Van den Haute C., Van Dorpe J., Geerts H., Mercken M., Bruynseels K., et al. (2000) Glycogen synthase kinase-3beta phosphorylates protein tau and rescues the axonopathy in the central nervous system of human four-repeat tau transgenic mice. J. Biol. Chem. 275(52), 41,340-41,349.
    • (2000) J. Biol. Chem. , vol.275 , Issue.52 , pp. 41340-41349
    • Spittaels, K.1    Van den Haute, C.2    Van Dorpe, J.3    Geerts, H.4    Mercken, M.5    Bruynseels, K.6
  • 193
    • 0037128935 scopus 로고    scopus 로고
    • Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress
    • Stamer K., Vogel R., Thies E., Mandelkow E., and Mandelkow E. M. (2002) Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress. J. Cell Biol. 156 (6), 1051-1063.
    • (2002) J. Cell Biol. , vol.156 , Issue.6 , pp. 1051-1063
    • Stamer, K.1    Vogel, R.2    Thies, E.3    Mandelkow, E.4    Mandelkow, E.M.5
  • 194
    • 0034093228 scopus 로고    scopus 로고
    • Progressive supranuclear palsy pathology caused by a novel silent mutation in exon 10 of the tau gene: Expansion of the disease phenotype caused by tau gene mutations
    • Stanford P. M., Halliday G. M., Brooks W. S., Kwok J. B., Storey C. E., et al. (2000) Progressive supranuclear palsy pathology caused by a novel silent mutation in exon 10 of the tau gene: expansion of the disease phenotype caused by tau gene mutations. Brain 123(5), 880-893.
    • (2000) Brain , vol.123 , Issue.5 , pp. 880-893
    • Stanford, P.M.1    Halliday, G.M.2    Brooks, W.S.3    Kwok, J.B.4    Storey, C.E.5
  • 195
    • 0028131169 scopus 로고
    • Stress exacerbates neuron loss and cytoskeletal pathology in the hippocampus
    • Stein-Behrens B., Mattson M. P., Chang I., Yeh M., and Sapolsky R. (1994) Stress exacerbates neuron loss and cytoskeletal pathology in the hippocampus. J. Neurosci. 14, 5373-5380.
    • (1994) J. Neurosci. , vol.14 , pp. 5373-5380
    • Stein-Behrens, B.1    Mattson, M.P.2    Chang, I.3    Yeh, M.4    Sapolsky, R.5
  • 196
    • 0028035306 scopus 로고
    • Isoform-specific interactions of apolipoprotein E with microtubule-associated protein tau: Implications for Alzheimer disease
    • Strittmatter W. J., Saunders A. M., Goedert M., Weisgraber K. H., Dong L. M., Jakes R, et al. (1994) Isoform-specific interactions of apolipoprotein E with microtubule-associated protein tau: implications for Alzheimer disease. Proc. Natl. Acad. Sci. USA 91(23), 11,183-11,186.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , Issue.23 , pp. 11183-11186
    • Strittmatter, W.J.1    Saunders, A.M.2    Goedert, M.3    Weisgraber, K.H.4    Dong, L.M.5    Jakes, R.6
  • 197
    • 0011444914 scopus 로고    scopus 로고
    • Two amyloid precursor protein transgenic mouse models with Alzheimer disease-like pathology
    • Sturchler-Pierrat C., Abramowski D., Duke M., Wiederhold K. H., Mistl C., et al. (1997) Two amyloid precursor protein transgenic mouse models with Alzheimer disease-like pathology. Proc. Natl. Acad. Sci. USA 94(24), 13,287-13,292.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , Issue.24 , pp. 13287-13292
    • Sturchler-Pierrat, C.1    Abramowski, D.2    Duke, M.3    Wiederhold, K.H.4    Mistl, C.5
  • 199
    • 0032717803 scopus 로고    scopus 로고
    • Lithium inhibits neurite growth and tau protein kinaseI/glycogen synthase kinase-3beta-dependent phosphorylation of juvenile tau in cultured hippocampal neurons
    • Takahashi M., Yasutake K., and Tomizawa K. (1999) Lithium inhibits neurite growth and tau protein kinaseI/glycogen synthase kinase-3beta-dependent phosphorylation of juvenile tau in cultured hippocampal neurons. J. Neurochem. 73(5), 2073-2083.
    • (1999) J. Neurochem. , vol.73 , Issue.5 , pp. 2073-2083
    • Takahashi, M.1    Yasutake, K.2    Tomizawa, K.3
  • 200
    • 0034605045 scopus 로고    scopus 로고
    • Defects in axonal elongation and neuronal migration in mice with disrupted tau and map1b genes
    • Takei Y., Teng J., Harada A., and Hirokawa N. (2000) Defects in axonal elongation and neuronal migration in mice with disrupted tau and map1b genes. J. Cell Biol. 150(5), 989-1000.
    • (2000) J. Cell Biol. , vol.150 , Issue.5 , pp. 989-1000
    • Takei, Y.1    Teng, J.2    Harada, A.3    Hirokawa, N.4
  • 201
    • 0036138044 scopus 로고    scopus 로고
    • Neurodegeneration with tau accumulation in a transgenic mouse expressing V337M human tau
    • Tanemura K., Murayama M., Akagi T., Hashikawa T., Tominaga T., Ichikawa M., et al. (2002) Neurodegeneration with tau accumulation in a transgenic mouse expressing V337M human tau. J. Neurosci. 22(1), 133-141.
    • (2002) J. Neurosci. , vol.22 , Issue.1 , pp. 133-141
    • Tanemura, K.1    Murayama, M.2    Akagi, T.3    Hashikawa, T.4    Tominaga, T.5    Ichikawa, M.6
  • 202
    • 0033694470 scopus 로고    scopus 로고
    • Prominent axonopathy and disruption of axonal transport in transgenic mice expressing human apolipoprotein E4 in neurons of brain and spinal cord
    • Tesseur I., Van Dorpe J., Bruynseels K., Bronfman F., Sciot R., Van Lommel A., et al. (2000) Prominent axonopathy and disruption of axonal transport in transgenic mice expressing human apolipoprotein E4 in neurons of brain and spinal cord. Am. J. Pathol. 157(5), 1495-1510.
    • (2000) Am. J. Pathol. , vol.157 , Issue.5 , pp. 1495-1510
    • Tesseur, I.1    Van Dorpe, J.2    Bruynseels, K.3    Bronfman, F.4    Sciot, R.5    Van Lommel, A.6
  • 203
    • 0032460625 scopus 로고    scopus 로고
    • Progression of neurofibrillary changes and PHF-tau in end-stage Alzheimer's disease is different from plaque and cortical microglial pathology
    • Thal D. R., Arendt T., Waldmann G., Holzer M., Zedlick D., Rub U., et al. (1998) Progression of neurofibrillary changes and PHF-tau in end-stage Alzheimer's disease is different from plaque and cortical microglial pathology. Neurobiol. Aging 19(6), 517-525.
    • (1998) Neurobiol. Aging , vol.19 , Issue.6 , pp. 517-525
    • Thal, D.R.1    Arendt, T.2    Waldmann, G.3    Holzer, M.4    Zedlick, D.5    Rub, U.6
  • 204
    • 0034070445 scopus 로고    scopus 로고
    • Alzheimer-related taupathology in the perforant path target zone and in the hippocampal stratum oriens and radiatum correlates with onset and degree of dementia
    • Thal D. R., Holzer M., Rub U., Waldmann G., Gunzel S., Zedlick D., et al. (2000) Alzheimer-related taupathology in the perforant path target zone and in the hippocampal stratum oriens and radiatum correlates with onset and degree of dementia. Exp. Neurol. 163(1), 98-110.
    • (2000) Exp. Neurol. , vol.163 , Issue.1 , pp. 98-110
    • Thal, D.R.1    Holzer, M.2    Rub, U.3    Waldmann, G.4    Gunzel, S.5    Zedlick, D.6
  • 205
    • 0028820411 scopus 로고
    • Domains of tau protein, differential phosphorylation, and dynamic instability of microtubules
    • Trinczek B., Biernat J., Baumann K., Mandelkow E. M., and Mandelkow E. (1995) Domains of tau protein, differential phosphorylation, and dynamic instability of microtubules. Mol. Biol. Cell 6(12), 1887-1902.
    • (1995) Mol. Biol. Cell , vol.6 , Issue.12 , pp. 1887-1902
    • Trinczek, B.1    Biernat, J.2    Baumann, K.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 206
    • 0024529404 scopus 로고
    • Distribution of tau proteins in the normal human central and peripheral nervous system
    • Trojanowski J. Q., Schuck T., Schmidt M. L., and Lee V. M.-Y. (1989) Distribution of tau proteins in the normal human central and peripheral nervous system. J. Histochem. Cytochem. 37(2), 209-215.
    • (1989) J. Histochem. Cytochem. , vol.37 , Issue.2 , pp. 209-215
    • Trojanowski, J.Q.1    Schuck, T.2    Schmidt, M.L.3    Lee, V.M.-Y.4
  • 207
    • 0024395055 scopus 로고
    • Distribution of phosphate-independent MAP2 epitopes revealed with monoclonal antibodies in microwave-denatured human nervous system tissues
    • Trojanowski J. Q., Schuck T., Schmidt M. L., and Lee V. M.-Y. (1989) Distribution of phosphate-independent MAP2 epitopes revealed with monoclonal antibodies in microwave-denatured human nervous system tissues. J. Neurosci. Methods 29(2), 171-180.
    • (1989) J. Neurosci. Methods , vol.29 , Issue.2 , pp. 171-180
    • Trojanowski, J.Q.1    Schuck, T.2    Schmidt, M.L.3    Lee, V.M.-Y.4
  • 208
    • 0027978170 scopus 로고    scopus 로고
    • p35 is a neural-specific regulatory subunit of cyclin-dependent kinase 5
    • Tsai L. H., Delalle I., Caviness V. S. Jr., Chae T., and Harlow E. (19) p35 is a neural-specific regulatory subunit of cyclin-dependent kinase 5. Nature 371(6496), 419-423.
    • Nature , vol.371 , Issue.6496 , pp. 419-423
    • Tsai, L.H.1    Delalle, I.2    Caviness V.S., Jr.3    Chae, T.4    Harlow, E.5
  • 209
    • 0028023051 scopus 로고
    • Demonstration of neurofibrillary tangles and neuropil thread-like structures in spinal cord white matter in parkinsonism-dementia complex on Guam and in Guamanian amyotrophic lateral sclerosis
    • Umahara T., Hirano A., Kato S., et al. (1994) Demonstration of neurofibrillary tangles and neuropil thread-like structures in spinal cord white matter in parkinsonism-dementia complex on Guam and in Guamanian amyotrophic lateral sclerosis. Acta Neuropathol. (Berl) 88, 180-184.
    • (1994) Acta Neuropathol. (Berl) , vol.88 , pp. 180-184
    • Umahara, T.1    Hirano, A.2    Kato, S.3
  • 211
    • 0023806825 scopus 로고
    • Phylogenetic conservation of brain microtubule-associated proteins MAP2 and tau
    • Viereck C., Tucker R. P., Binder L. I., and Matus A. (1990) Phylogenetic conservation of brain microtubule-associated proteins MAP2 and tau. Neuroscience 26(3), 893-904.
    • (1990) Neuroscience , vol.26 , Issue.3 , pp. 893-904
    • Viereck, C.1    Tucker, R.P.2    Binder, L.I.3    Matus, A.4
  • 212
    • 0033638377 scopus 로고    scopus 로고
    • Distinct FTDP-17 missense mutations in tau produce tau aggregates and other phathological phenotypes in transfected CHO cells
    • Vogelsberg-Ragaglia V., Bruce J., Richter-Lansberg C., Zhang B., Hong M., et al. (2000) Distinct FTDP-17 missense mutations in tau produce tau aggregates and other phathological phenotypes in transfected CHO cells. Mol. Biol. Cell 11(12), 4093-4104.
    • (2000) Mol. Biol. Cell , vol.11 , Issue.12 , pp. 4093-4104
    • Vogelsberg-Ragaglia, V.1    Bruce, J.2    Richter-Lansberg, C.3    Zhang, B.4    Hong, M.5
  • 213
    • 0035075793 scopus 로고    scopus 로고
    • PP2A mRNA expression is quantitatively decreased in Alzheimer's disease hippocampus
    • Vogelsberg-Ragaglia V., Schuck T., Trojanowski J. Q., and Lee V. M.-Y. (2001) PP2A mRNA expression is quantitatively decreased in Alzheimer's disease hippocampus. Exp. Neurol. 168(2), 402-412.
    • (2001) Exp. Neurol. , vol.168 , Issue.2 , pp. 402-412
    • Vogelsberg-Ragaglia, V.1    Schuck, T.2    Trojanowski, J.Q.3    Lee, V.M.-Y.4
  • 214
    • 0028246505 scopus 로고
    • Corticobasal degeneration: Etiopathological significance of the cytoskeletal alterations
    • Wakabayashi K., Oyanagi K., Makifuchi T., et al. (1994) Corticobasal degeneration: etiopathological significance of the cytoskeletal alterations. Acta Neuropathol. (Berl) 87, 545-553.
    • (1994) Acta Neuropathol. (Berl) , vol.87 , pp. 545-553
    • Wakabayashi, K.1    Oyanagi, K.2    Makifuchi, T.3
  • 217
    • 0028073692 scopus 로고
    • Localization of disnhibition-dementia-parkinsonism-amyotrophy complex to 17q21-22
    • Wilhelmsen K. C., Lynch T., Pavlou E., et al. (1994) Localization of disnhibition-dementia-parkinsonism-amyotrophy complex to 17q21-22. Am. J. Hum. Gen. 55, 1159-1165.
    • (1994) Am. J. Hum. Gen. , vol.55 , pp. 1159-1165
    • Wilhelmsen, K.C.1    Lynch, T.2    Pavlou, E.3
  • 218
    • 0030923223 scopus 로고    scopus 로고
    • Free fatty acids simulate the polymerization of tau and amyloid beta peptides. In vitro evidence for a common effector of pathogenesis in Alzheimer's disease
    • Wilson D. M. and Binder L. I. (1997) Free fatty acids simulate the polymerization of tau and amyloid beta peptides. In vitro evidence for a common effector of pathogenesis in Alzheimer's disease. Am. J. Pathol. 150(6), 2181-2195.
    • (1997) Am. J. Pathol. , vol.150 , Issue.6 , pp. 2181-2195
    • Wilson, D.M.1    Binder, L.I.2
  • 219
    • 0003986552 scopus 로고
    • Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease
    • Wischik C. M., Novak M., Thogersen H. C., Edwards P. C., Runswick M. J., Jakes R., et al. (1988) Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease. Proc. Natl. Acad. Sci. USA 85(12), 4506-4510.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , Issue.12 , pp. 4506-4510
    • Wischik, C.M.1    Novak, M.2    Thogersen, H.C.3    Edwards, P.C.4    Runswick, M.J.5    Jakes, R.6
  • 220
    • 0025286104 scopus 로고
    • Molecular cloning and expression of glycogen synthase kinase-3/factorA
    • Woodgett J. R. (1990) Molecular cloning and expression of glycogen synthase kinase-3/factorA. EMBO J. 9(8), 2431-2438.
    • (1990) EMBO J. , vol.9 , Issue.8 , pp. 2431-2438
    • Woodgett, J.R.1
  • 221
    • 0026543843 scopus 로고
    • Appearance of paired nucleated, Tau-positive glia in patients with progressive supranuclear palsy brain tissue
    • Yamada T., McGeer P. L., and McGeer E. G. (1992) Appearance of paired nucleated, Tau-positive glia in patients with progressive supranuclear palsy brain tissue. Neurosci. Lett. 135(1), 99-102.
    • (1992) Neurosci. Lett. , vol.135 , Issue.1 , pp. 99-102
    • Yamada, T.1    McGeer, P.L.2    McGeer, E.G.3
  • 222
    • 0028004473 scopus 로고
    • Astrocytic straight tubules in the brain of a patient with Pick's disease
    • Yamazaki M., Nakano I., Imazu O., Kaieda R., and Terashi A. (1994) Astrocytic straight tubules in the brain of a patient with Pick's disease. Acta Neuropathol. (Berl) 88(6), 587-591.
    • (1994) Acta Neuropathol. (Berl) , vol.88 , Issue.6 , pp. 587-591
    • Yamazaki, M.1    Nakano, I.2    Imazu, O.3    Kaieda, R.4    Terashi, A.5
  • 223
    • 0034074542 scopus 로고    scopus 로고
    • A novel mutation at posititon +12 in the intron following exon 10 of the tau gene in familial frontotemporal dementia (FTD-Kumamoto)
    • Yasuda M., Takamatsu J., D'Souza I., Crowther R. A., Kawamata T., et al. (2000) A novel mutation at posititon +12 in the intron following exon 10 of the tau gene in familial frontotemporal dementia (FTD-Kumamoto). Ann. Neurol. 47(4), 422-429.
    • (2000) Ann. Neurol. , vol.47 , Issue.4 , pp. 422-429
    • Yasuda, M.1    Takamatsu, J.2    D'Souza, I.3    Crowther, R.A.4    Kawamata, T.5
  • 224
    • 0027237861 scopus 로고
    • Tau in paired helical filaments is functionally distinct from fetal tau: Assembly incompetence of paired helical filamenttau
    • Yoshida H. and Ihara Y. (1993) Tau in paired helical filaments is functionally distinct from fetal tau: assembly incompetence of paired helical filamenttau. J. Neurochem. 61(3), 1183-1186.
    • (1993) J. Neurochem. , vol.61 , Issue.3 , pp. 1183-1186
    • Yoshida, H.1    Ihara, Y.2
  • 225
    • 0032521599 scopus 로고    scopus 로고
    • Sequential phosphorylation of Tau by glycogen synthase kinase-3beta and protein kinase A at Thr212 and Ser214 generates the Alzheimer-specific epitope of antibody AT100 and requires a paired-helical-filament-like conformation
    • Zheng-Fischhofer Q., Biernat J., Mandelkow E. M., Illenberger S., Godemann R., and Mandelkow E. (1998) Sequential phosphorylation of Tau by glycogen synthase kinase-3beta and protein kinase A at Thr212 and Ser214 generates the Alzheimer-specific epitope of antibody AT100 and requires a paired-helical-filament-like conformation. Eur. J. Biochem. 252(3), 542-552.
    • (1998) Eur. J. Biochem. , vol.252 , Issue.3 , pp. 542-552
    • Zheng-Fischhofer, Q.1    Biernat, J.2    Mandelkow, E.M.3    Illenberger, S.4    Godemann, R.5    Mandelkow, E.6


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