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Volumn 107, Issue 1, 1998, Pages 143-158

Developmental regulation and PKC dependence of Alzheimer's-type tau phosphorylations in cultured fetal rat hippocampal neurons

Author keywords

Alzheimer's disease; Microtubule associated proteins; Neuronal culture; PHF 1; Phosphorylation; Tau 1

Indexed keywords

PROTEIN KINASE C; TAU PROTEIN;

EID: 0032540311     PISSN: 01653806     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0165-3806(98)00019-4     Document Type: Article
Times cited : (7)

References (120)
  • 1
    • 0025734065 scopus 로고
    • TPA-induced activation of MAP kinase
    • Adams P.D., Parker P.J. TPA-induced activation of MAP kinase. FEBS Lett. 290:1991;77-82.
    • (1991) FEBS Lett. , vol.290 , pp. 77-82
    • Adams, P.D.1    Parker, P.J.2
  • 2
    • 0026679852 scopus 로고
    • Perisomatic sprouts immunoreactive for nerve growth factor receptor and neurofibrillary degeneration affect different neuronal populations in the basal nucleus in patients with Alzheimer's disease
    • Arendt T., Bruckner M.K. Perisomatic sprouts immunoreactive for nerve growth factor receptor and neurofibrillary degeneration affect different neuronal populations in the basal nucleus in patients with Alzheimer's disease. Neurosci. Lett. 148:1992;63-66.
    • (1992) Neurosci. Lett. , vol.148 , pp. 63-66
    • Arendt, T.1    Bruckner, M.K.2
  • 3
    • 0024805885 scopus 로고
    • Changes in microtubule polarity orientation during the development of hippocampal neurons in culture
    • Baas P.W., Black M.M., Banker G.A. Changes in microtubule polarity orientation during the development of hippocampal neurons in culture. J. Cell Biol. 109:1989;3085-3094.
    • (1989) J. Cell Biol. , vol.109 , pp. 3085-3094
    • Baas, P.W.1    Black, M.M.2    Banker, G.A.3
  • 4
    • 0025788253 scopus 로고
    • Processes induced by tau expression in sf9 cells have an axon-like microtubule organization
    • Baas P.W., Pienkowski T.P., Kosik K.S. Processes induced by tau expression in sf9 cells have an axon-like microtubule organization. J. Cell Biol. 115:1991;1333-1344.
    • (1991) J. Cell Biol. , vol.115 , pp. 1333-1344
    • Baas, P.W.1    Pienkowski, T.P.2    Kosik, K.S.3
  • 5
    • 0017350927 scopus 로고
    • Rat hippocampal neurons in dispersed cell culture
    • Banker G.A., Cowan M. Rat hippocampal neurons in dispersed cell culture. Brain Res. 126:1977;397-425.
    • (1977) Brain Res. , vol.126 , pp. 397-425
    • Banker, G.A.1    Cowan, M.2
  • 6
    • 0021629684 scopus 로고
    • An electron microscopic study of the development of axons and dendrites by hippocampal neurons in culture: I. Cells which develop without intercellular contacts
    • Bartlett W.P., Banker G.A. An electron microscopic study of the development of axons and dendrites by hippocampal neurons in culture: I. Cells which develop without intercellular contacts. J. Neurosci. 4:1984;1944-1953.
    • (1984) J. Neurosci. , vol.4 , pp. 1944-1953
    • Bartlett, W.P.1    Banker, G.A.2
  • 7
    • 0021603138 scopus 로고
    • An electron microscopic study of the development of axons and dendrites by hippocampal neurons in culture: II. Synaptic relationships
    • Bartlett W.P., Banker G.A. An electron microscopic study of the development of axons and dendrites by hippocampal neurons in culture: II. Synaptic relationships. J. Neurosci. 4:1984;1954-1965.
    • (1984) J. Neurosci. , vol.4 , pp. 1954-1965
    • Bartlett, W.P.1    Banker, G.A.2
  • 8
    • 0027338266 scopus 로고
    • Phosphorylation of Ser262 strongly reduces binding of tau to microtubules: Distinction between PHF-like immunoreactivity and microtubule binding
    • Biernat J., Gustke N., Drewes G., Mandelkow E.M., Mandelkow E. Phosphorylation of Ser262 strongly reduces binding of tau to microtubules: distinction between PHF-like immunoreactivity and microtubule binding. Neuron. 11:1993;153-163.
    • (1993) Neuron , vol.11 , pp. 153-163
    • Biernat, J.1    Gustke, N.2    Drewes, G.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 9
    • 0022365608 scopus 로고
    • The distribution of tau in the mammalian central nervous system
    • Binder L.I., Frankfurter A., Rebhun L.I. The distribution of tau in the mammalian central nervous system. J. Cell Biol. 101:1985;1371-1378.
    • (1985) J. Cell Biol. , vol.101 , pp. 1371-1378
    • Binder, L.I.1    Frankfurter, A.2    Rebhun, L.I.3
  • 10
    • 0029040690 scopus 로고
    • Presence of tau in isolated nuclei from human brain
    • Brady R.M., Zinkowski R.P., Binder L.I. Presence of tau in isolated nuclei from human brain. Neurobiol. Aging. 16:1995;479-486.
    • (1995) Neurobiol. Aging , vol.16 , pp. 479-486
    • Brady, R.M.1    Zinkowski, R.P.2    Binder, L.I.3
  • 11
    • 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., Lee V.M. Abnormal tau phosphorylation at ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding. Neuron. 10:1993;1089-1099.
    • (1993) Neuron , vol.10 , pp. 1089-1099
    • Bramblett, G.T.1    Goedert, M.2    Jakes, R.3    Merrick, S.E.4    Trojanowski, J.Q.5    Lee, V.M.6
  • 12
    • 0026578425 scopus 로고
    • Regions with abundant neurofibrillary pathology in human brain exhibit a selective reduction in levels of binding-competent tau and accumulation of abnormal tau-isoforms (A68 proteins)
    • Bramblett G.T., Trojanowski J.Q., Lee V.M. Regions with abundant neurofibrillary pathology in human brain exhibit a selective reduction in levels of binding-competent tau and accumulation of abnormal tau-isoforms (A68 proteins). Lab. Invest. 66:1992;212-222.
    • (1992) Lab. Invest. , vol.66 , pp. 212-222
    • Bramblett, G.T.1    Trojanowski, J.Q.2    Lee, V.M.3
  • 13
    • 0027406644 scopus 로고
    • Functional organization of microtubule-associated protein tau: Identification of regions which affect microtubule growth, nucleation, and bundle formation in vitro
    • Brandt R., Lee G. Functional organization of microtubule-associated protein tau: identification of regions which affect microtubule growth, nucleation, and bundle formation in vitro. J. Biol. Chem. 268:1993;3414-3419.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3414-3419
    • Brandt, R.1    Lee, G.2
  • 14
    • 0027429479 scopus 로고
    • Developmental changes in tau phosphorylation: Fetal tau is transiently phosphorylated in a manner similar to paired helical filament-tau characteristic of Alzheimer's disease
    • Brion J.-P., Smith C., Couck A.-M., Gallo J.-M., Anderton B.H. Developmental changes in tau phosphorylation: fetal tau is transiently phosphorylated in a manner similar to paired helical filament-tau characteristic of Alzheimer's disease. J. Neurochem. 61:1993;2071-2080.
    • (1993) J. Neurochem. , vol.61 , pp. 2071-2080
    • Brion, J.-P.1    Smith, C.2    Couck, A.-M.3    Gallo, J.-M.4    Anderton, B.H.5
  • 15
    • 0028986916 scopus 로고
    • Beta-amyloid fibrils induce tau phosphorylation and loss of microtubule binding
    • Busciglio J., Lorenzo A., Yeh J., Yankner B.A. Beta-amyloid fibrils induce tau phosphorylation and loss of microtubule binding. Neuron. 14:1995;879-888.
    • (1995) Neuron , vol.14 , pp. 879-888
    • Busciglio, J.1    Lorenzo, A.2    Yeh, J.3    Yankner, B.A.4
  • 16
    • 0026046950 scopus 로고
    • Tau protein binds to microtubules through a flexible array of distributed weak sites
    • Butner K.A., Kirschner M.W. Tau protein binds to microtubules through a flexible array of distributed weak sites. J. Cell Biol. 115:1991;717-730.
    • (1991) J. Cell Biol. , vol.115 , pp. 717-730
    • Butner, K.A.1    Kirschner, M.W.2
  • 17
    • 0025250329 scopus 로고
    • Inhibition of cGMP-dependent protein kinase by (Rp)-guanosine 3′,5′-monophosphorothioates
    • Butt E., Bemmelen M.v., Fischer L., Walter U., Jastorff B. Inhibition of cGMP-dependent protein kinase by (Rp)-guanosine 3′,5′-monophosphorothioates. FEBS Lett. 263:1990;47-50.
    • (1990) FEBS Lett. , vol.263 , pp. 47-50
    • Butt, E.1    Bemmelen, M.V.2    Fischer, L.3    Walter, U.4    Jastorff, B.5
  • 18
    • 0022641260 scopus 로고
    • Immunocytochemical localization of tubulin and microtubule-associated protein 2 during the development of hippocampal neurons in culture
    • Caceres A., Banker G.A., Binder L.I. Immunocytochemical localization of tubulin and microtubule-associated protein 2 during the development of hippocampal neurons in culture. J. Neurosci. 6:1986;714-722.
    • (1986) J. Neurosci. , vol.6 , pp. 714-722
    • Caceres, A.1    Banker, G.A.2    Binder, L.I.3
  • 19
    • 0026001490 scopus 로고
    • The effect of tau antisense oligonucleotides on neurite formation of cultured cerebellar macroneurons
    • Caceres A., Potrebic S., Kosik K.S. The effect of tau antisense oligonucleotides on neurite formation of cultured cerebellar macroneurons. J. Neurosci. 11:1991;1515-1523.
    • (1991) J. Neurosci. , vol.11 , pp. 1515-1523
    • Caceres, A.1    Potrebic, S.2    Kosik, K.S.3
  • 20
    • 0027990854 scopus 로고
    • Evidence that protein kinase C activities involved in regulating neurite growth are localized to distal neurites
    • Campenot R.B., Draker D.D., Senger D.L. Evidence that protein kinase C activities involved in regulating neurite growth are localized to distal neurites. J. Neurochem. 63:1994;868-878.
    • (1994) J. Neurochem. , vol.63 , pp. 868-878
    • Campenot, R.B.1    Draker, D.D.2    Senger, D.L.3
  • 21
    • 0026019071 scopus 로고
    • Characterization and differential distribution of the three major human protein kinase C isozymes (PKC alpha, PKC beta, and PKC gamma) of the central nervous system in normal and Alzheimer's disease brains
    • Clark E.A., Leach K.L., Trojanowski J.Q., Lee V.M.-Y. Characterization and differential distribution of the three major human protein kinase C isozymes (PKC alpha, PKC beta, and PKC gamma) of the central nervous system in normal and Alzheimer's disease brains. Lab. Invest. 64:1991;35-44.
    • (1991) Lab. Invest. , vol.64 , pp. 35-44
    • Clark, E.A.1    Leach, K.L.2    Trojanowski, J.Q.3    Lee, V.M.-Y.4
  • 22
    • 0017649032 scopus 로고
    • Purification of tau, a microtubule-associated protein that induces assembly of microtubules from purified tubulin
    • Cleveland D.W., Hwo S.Y., Kirschner M.W. Purification of tau, a microtubule-associated protein that induces assembly of microtubules from purified tubulin. J. Mol. Biol. 116:1977;207-225.
    • (1977) J. Mol. Biol. , vol.116 , pp. 207-225
    • Cleveland, D.W.1    Hwo, S.Y.2    Kirschner, M.W.3
  • 25
    • 0028973143 scopus 로고
    • Hyperphosphorylation of tau and filopodial retraction following microinjection of protein kinase C catalytic subunits
    • Cressman C.M., Shea T.B. Hyperphosphorylation of tau and filopodial retraction following microinjection of protein kinase C catalytic subunits. J. Neurosci. Res. 42:1995;648-656.
    • (1995) J. Neurosci. Res. , vol.42 , pp. 648-656
    • Cressman, C.M.1    Shea, T.B.2
  • 26
    • 0022435132 scopus 로고
    • Image reconstruction of the Alzheimer paired helical filament
    • Crowther R.A., Wischik C.M. Image reconstruction of the Alzheimer paired helical filament. EMBO J. 4:1985;3661-3665.
    • (1985) EMBO J. , vol.4 , pp. 3661-3665
    • Crowther, R.A.1    Wischik, C.M.2
  • 27
    • 0027442407 scopus 로고
    • An electron microscopic analysis of hippocampal neurons developing in culture: Early stages in the emergence of polarity
    • Deitch J.S., Banker G.A. An electron microscopic analysis of hippocampal neurons developing in culture: early stages in the emergence of polarity. J. Neurosci. 13:1993;4301-4315.
    • (1993) J. Neurosci. , vol.13 , pp. 4301-4315
    • Deitch, J.S.1    Banker, G.A.2
  • 28
    • 0028082161 scopus 로고
    • Protein kinase C - A question of specificity
    • Dekker L.V., Parker P.J. Protein kinase C - a question of specificity. Trends Biochem. Sci. 19:1994;73-77.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 73-77
    • Dekker, L.V.1    Parker, P.J.2
  • 29
    • 0025365945 scopus 로고
    • Probing the cyclic nucleotide binding sites of cAMP-dependent protein kinases I and II with analogs of adenosine 3′,5′-cyclic phosphorothioates
    • Dostmann W.R.G., Taylor S.S., Genieser H.-G., Jastorff B., Doskeland S.O., Ogreld K. Probing the cyclic nucleotide binding sites of cAMP-dependent protein kinases I and II with analogs of adenosine 3′,5′-cyclic phosphorothioates. J. Biol. Chem. 265:1990;10484-10491.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10484-10491
    • Dostmann, W.R.G.1    Taylor, S.S.2    Genieser, H.-G.3    Jastorff, B.4    Doskeland, S.O.5    Ogreld, K.6
  • 30
    • 0027058857 scopus 로고
    • Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau
    • Dreschel D.N., Hyman A.A., Cobb M.H., Kirschner M.W. Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau. Mol. Biol. Cell. 3:1992;1141-1154.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1141-1154
    • Dreschel, D.N.1    Hyman, A.A.2    Cobb, M.H.3    Kirschner, M.W.4
  • 32
    • 0023937193 scopus 로고
    • Regulation of microtubule protein levels during cellular morphogenesis in nerve growth factor-treated PC 12 cells
    • Drubin D., Kobayashi S., Kellogg D., Kirschner M. Regulation of microtubule protein levels during cellular morphogenesis in nerve growth factor-treated PC 12 cells. J. Cell Biol. 106:1988;1583-1591.
    • (1988) J. Cell Biol. , vol.106 , pp. 1583-1591
    • Drubin, D.1    Kobayashi, S.2    Kellogg, D.3    Kirschner, M.4
  • 33
    • 0022557162 scopus 로고
    • Association of tau protein with microtubules in living cells
    • Drubin D., Kobayashi S., Kirschner M. Association of tau protein with microtubules in living cells. Ann. New York Acad. Sci. 466:1986;257-268.
    • (1986) Ann. New York Acad. Sci. , vol.466 , pp. 257-268
    • Drubin, D.1    Kobayashi, S.2    Kirschner, M.3
  • 34
    • 0021334090 scopus 로고
    • Studies on the expression of the microtubule-associated protein, tau, during mouse brain development, with newly isolated complementary DNA probes
    • Drubin D.G., Caput D., Kirschner M.W. Studies on the expression of the microtubule-associated protein, tau, during mouse brain development, with newly isolated complementary DNA probes. J. Cell Biol. 98:1984;1090-1097.
    • (1984) J. Cell Biol. , vol.98 , pp. 1090-1097
    • Drubin, D.G.1    Caput, D.2    Kirschner, M.W.3
  • 35
    • 0027132379 scopus 로고
    • 3H]-PIP2 hydrolysis in Alzheimer's disease
    • 3H]-PIP2 hydrolysis in Alzheimer's disease. Life Sci. 53:1993;439-444.
    • (1993) Life Sci. , vol.53 , pp. 439-444
    • Ferrari-Dileo, G.1    Flynn, D.D.2
  • 36
    • 0024433060 scopus 로고
    • Microtubule formation and neurite growth in cerebellar macroneurons which develop in vitro: Evidence for the involvement of the microtubule-associated proteins, MAP-1a, HMW-MAP 2 and tau
    • Ferreira A., Busciglio J., Caceres A. Microtubule formation and neurite growth in cerebellar macroneurons which develop in vitro: evidence for the involvement of the microtubule-associated proteins, MAP-1a, HMW-MAP 2 and tau. Dev. Brain Res. 49:1989;215-228.
    • (1989) Dev. Brain Res. , vol.49 , pp. 215-228
    • Ferreira, A.1    Busciglio, J.2    Caceres, A.3
  • 37
    • 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., Jakes R. Expression of separate isoforms of human tau protein: correlation with the tau pattern in brain and effects on tubulin polymerization. EMBO J. 9:1990;4225-4230.
    • (1990) EMBO J. , vol.9 , pp. 4225-4230
    • Goedert, M.1    Jakes, R.2
  • 38
    • 0027984739 scopus 로고
    • Epitope mapping of monoclonal antibodies to the paired helical filaments of Alzheimer's disease: Identification of phosphorylation sites in tau protein
    • Goedert M., Jakes R., Crowther R.A., Cohen P., Vanmechelen E., Vandermeeren M., Cras P. Epitope mapping of monoclonal antibodies to the paired helical filaments of Alzheimer's disease: identification of phosphorylation sites in tau protein. Biochem. J. 301:1994;871-877.
    • (1994) Biochem. J. , vol.301 , pp. 871-877
    • Goedert, M.1    Jakes, R.2    Crowther, R.A.3    Cohen, P.4    Vanmechelen, E.5    Vandermeeren, M.6    Cras, P.7
  • 40
    • 0028946744 scopus 로고
    • Monoclonal antibody AT8 recognizes tau protein phosphorylated at both serine 202 and threonine 205
    • Goedert M., Jakes R., Vanmechelen E. Monoclonal antibody AT8 recognizes tau protein phosphorylated at both serine 202 and threonine 205. Neurosci. Lett. 189:1995;167-170.
    • (1995) Neurosci. Lett. , vol.189 , pp. 167-170
    • Goedert, M.1    Jakes, R.2    Vanmechelen, E.3
  • 41
    • 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., Crowther R.A. Tau proteins of Alzheimer paired helical filaments: abnormal phosphorylation of all six brain isoforms. Neuron. 8:1992;159-168.
    • (1992) Neuron , vol.8 , pp. 159-168
    • Goedert, M.1    Spillantini, M.G.2    Cairns, N.J.3    Crowther, R.A.4
  • 42
    • 0024387161 scopus 로고
    • Cloning and sequencing of the cDNA encoding an isoform of microtubule-associated protein tau containing four tandem repeats: Differential expression of tau protein mRNAs in human brain
    • Goedert M., Spillantini M.G., Potier M.C., Ulrich J., Crowther R.A. Cloning and sequencing of the cDNA encoding an isoform of microtubule-associated protein tau containing four tandem repeats: differential expression of tau protein mRNAs in human brain. EMBO J. 8:1989;393-399.
    • (1989) EMBO J. , vol.8 , pp. 393-399
    • Goedert, M.1    Spillantini, M.G.2    Potier, M.C.3    Ulrich, J.4    Crowther, R.A.5
  • 43
    • 0025028911 scopus 로고
    • Microtubule-associated-protein kinase (MAP) kinase activated by nerve growth factor and epidermal growth factor in PC12 cells. Identity with the mitogen activated MAP kinase of fibroblastic cells
    • Gotoh Y., Nishida E., Yamashita T., Hoshi M., Kawashima M. Microtubule-associated-protein kinase (MAP) kinase activated by nerve growth factor and epidermal growth factor in PC12 cells. Identity with the mitogen activated MAP kinase of fibroblastic cells. Eur. J. Biochem. 193:1990;661-669.
    • (1990) Eur. J. Biochem. , vol.193 , pp. 661-669
    • Gotoh, Y.1    Nishida, E.2    Yamashita, T.3    Hoshi, M.4    Kawashima, M.5
  • 44
    • 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., Binder L.I. Hydrofluoric acid-treated tau PHF proteins display the same biochemical properties as normal tau. J. Biol. Chem. 267:1992;564-569.
    • (1992) J. Biol. Chem. , vol.267 , pp. 564-569
    • Greenberg, S.G.1    Davies, P.2    Schein, J.D.3    Binder, L.I.4
  • 48
    • 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., David W., Martin J. Tau consists of a set of proteins with repeated C-terminal microtubule-binding domains and variable N-terminal domains. Mol. Cell. Biol. 9:1989;1381-1388.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 1381-1388
    • Himmler, A.1    Drechsel, D.2    Kirschner, M.W.3    David, W.4    Martin, J.5
  • 49
    • 0024094998 scopus 로고
    • Tau proteins: The molecular structure and mode of binding on microtubules
    • Hirokawa N., Shiomura Y., Okabe S. Tau proteins: the molecular structure and mode of binding on microtubules. J. Cell Biol. 107:1988;1449-1459.
    • (1988) J. Cell Biol. , vol.107 , pp. 1449-1459
    • Hirokawa, N.1    Shiomura, Y.2    Okabe, S.3
  • 51
    • 0023708239 scopus 로고
    • Massive somatodendritic sprouting of cortical neurons in Alzheimer's disease
    • Ihara Y. Massive somatodendritic sprouting of cortical neurons in Alzheimer's disease. Brain Res. 459:1988;138-144.
    • (1988) Brain Res. , vol.459 , pp. 138-144
    • Ihara, Y.1
  • 52
    • 0025785076 scopus 로고
    • Identification of 3- And 4-repeat tau isoforms within the PHF in Alzheimer's disease
    • Jakes R., Novak M., Davison M., Wischik C.M. Identification of 3- and 4-repeat tau isoforms within the PHF in Alzheimer's disease. EMBO J. 10:1991;2725-2729.
    • (1991) EMBO J. , vol.10 , pp. 2725-2729
    • Jakes, R.1    Novak, M.2    Davison, M.3    Wischik, C.M.4
  • 53
    • 0028343627 scopus 로고
    • Impaired phosphoinositide hydrolysis in Alzheimer's disease brain
    • Jope R.S., Song L., Li X., Powers R. Impaired phosphoinositide hydrolysis in Alzheimer's disease brain. Neurobiol. Aging. 15:1994;221-226.
    • (1994) Neurobiol. Aging , vol.15 , pp. 221-226
    • Jope, R.S.1    Song, L.2    Li, X.3    Powers, R.4
  • 54
    • 0028838142 scopus 로고
    • Sorting mechanisms of tau and MAP 2 in neurons: Suppressed axonal transit of MAP 2 and locally regulated microtubule binding
    • Kanai Y., Hirokawa N. Sorting mechanisms of tau and MAP 2 in neurons: suppressed axonal transit of MAP 2 and locally regulated microtubule binding. Neuron. 14:1995;421-432.
    • (1995) Neuron , vol.14 , pp. 421-432
    • Kanai, Y.1    Hirokawa, N.2
  • 55
    • 0026711059 scopus 로고
    • Fetal-type phosphorylation of the tau in paired helical filaments
    • Kanemaru K., Takio K., Miura R., Titani K., Ihara Y. Fetal-type phosphorylation of the tau in paired helical filaments. J. Neurochem. 58:1992;1667-1675.
    • (1992) J. Neurochem. , vol.58 , pp. 1667-1675
    • Kanemaru, K.1    Takio, K.2    Miura, R.3    Titani, K.4    Ihara, Y.5
  • 56
    • 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., Ihara Y. The carboxyl third of tau is tightly bound to paired helical filaments. Neuron. 1:1988;827-834.
    • (1988) Neuron , vol.1 , pp. 827-834
    • Kondo, J.1    Honda, T.2    Mori, H.3    Hamada, Y.4    Miura, R.5    Ogawara, M.6    Ihara, Y.7
  • 57
    • 0026539331 scopus 로고
    • Alzheimer's disease: A cell biological perspective
    • Kosik K.S. Alzheimer's disease: a cell biological perspective. Science. 256:1992;780-783.
    • (1992) Science , vol.256 , pp. 780-783
    • Kosik, K.S.1
  • 58
    • 0026309310 scopus 로고
    • Tau protein and the establishment of an axonal morphology
    • Kosik K.S., Caceres A. Tau protein and the establishment of an axonal morphology. J. Cell Sci. S15:1991;69-74.
    • (1991) J. Cell Sci. , vol.15 , pp. 69-74
    • Kosik, K.S.1    Caceres, A.2
  • 59
    • 0023434104 scopus 로고
    • MAP 2 and tau segregate into dendritic and axonal domains after the elaboration of morphologically distinct neurites: An immunocytochemical study of cultured rat cerebrum
    • Kosik K.S., Finch E.A. MAP 2 and tau segregate into dendritic and axonal domains after the elaboration of morphologically distinct neurites: an immunocytochemical study of cultured rat cerebrum. J. Neurosci. 7:1987;3142-3153.
    • (1987) J. Neurosci. , vol.7 , pp. 3142-3153
    • Kosik, K.S.1    Finch, E.A.2
  • 60
    • 0024641959 scopus 로고
    • Developmentally regulated expression of specific tau sequences
    • Kosik K.S., Orecchio L.D., Bakalis S., Neve R.L. Developmentally regulated expression of specific tau sequences. Neuron. 2:1989;1389-1397.
    • (1989) Neuron , vol.2 , pp. 1389-1397
    • Kosik, K.S.1    Orecchio, L.D.2    Bakalis, S.3    Neve, R.L.4
  • 61
    • 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., Lee G. Epitopes that span the tau molecule are shared with paired helical filaments. Neuron. 1:1988;817-825.
    • (1988) Neuron , vol.1 , pp. 817-825
    • Kosik, K.S.1    Orecchio, L.D.2    Binder, L.3    Trojanowski, J.Q.4    Lee, V.M.5    Lee, G.6
  • 62
    • 0025852163 scopus 로고
    • Structural stability of paired helical filaments requires microtubule-binding domains of tau: A model for self-association
    • Ksiezak-Reding H., Yen S.-Y. Structural stability of paired helical filaments requires microtubule-binding domains of tau: a model for self-association. Neuron. 6:1991;717-728.
    • (1991) Neuron , vol.6 , pp. 717-728
    • Ksiezak-Reding, H.1    Yen, S.-Y.2
  • 63
    • 0026611728 scopus 로고
    • Immunological and conformational characteristics of a phosphorylated immunodominant epitope on the paired helical filaments found in Alzheimer's disease
    • Lang E., Szendrei G.I., Lee V.M., Otvos L.J. Immunological and conformational characteristics of a phosphorylated immunodominant epitope on the paired helical filaments found in Alzheimer's disease. Biochem. Biophys. Res. Commun. 187:1992;783-790.
    • (1992) Biochem. Biophys. Res. Commun. , vol.187 , pp. 783-790
    • Lang, E.1    Szendrei, G.I.2    Lee, V.M.3    Otvos, L.J.4
  • 64
    • 0024675418 scopus 로고
    • The microtubule binding domain of tau protein
    • Lee G., Neve R.L., Kosik K.S. The microtubule binding domain of tau protein. Neuron. 2:1989;1615-1624.
    • (1989) Neuron , vol.2 , pp. 1615-1624
    • Lee, G.1    Neve, R.L.2    Kosik, K.S.3
  • 65
    • 0027254107 scopus 로고
    • Tau proteins are abnormally expressed in olfactory epithelium of Alzheimer patients and developmentally regulated in human fetal spinal cord
    • Lee J.H., Goedert M., Hill W.D., Lee V.M.-Y., Trojanowski J.Q. Tau proteins are abnormally expressed in olfactory epithelium of Alzheimer patients and developmentally regulated in human fetal spinal cord. Exp. Neurol. 121:1993;93-105.
    • (1993) Exp. Neurol. , vol.121 , pp. 93-105
    • Lee, J.H.1    Goedert, M.2    Hill, W.D.3    Lee, V.M.-Y.4    Trojanowski, J.Q.5
  • 66
    • 0025904444 scopus 로고
    • A68: A major subunit of paired helical filaments and derivatized forms of normal tau
    • Lee V.M., Balin B.J., Otvos L. Jr., Trojanowski J.Q. A68: a major subunit of paired helical filaments and derivatized forms of normal tau. Science. 251:1991;675-678.
    • (1991) Science , vol.251 , pp. 675-678
    • Lee, V.M.1    Balin, B.J.2    Otvos L., Jr.3    Trojanowski, J.Q.4
  • 67
    • 0026941497 scopus 로고
    • The disordered neuronal cytoskeleton in Alzheimer's disease
    • Lee V.M., Trojanowski J.Q. The disordered neuronal cytoskeleton in Alzheimer's disease. Curr. Opin. Neurobiol. 2:1992;653-656.
    • (1992) Curr. Opin. Neurobiol. , vol.2 , pp. 653-656
    • Lee, V.M.1    Trojanowski, J.Q.2
  • 68
    • 0021338217 scopus 로고
    • Phosphorylation affects the ability of tau protein to promote microtubule assembly
    • Lindwall G., Cole R.D. Phosphorylation affects the ability of tau protein to promote microtubule assembly. J. Biol. Chem. 259:1984;5301-5305.
    • (1984) J. Biol. Chem. , vol.259 , pp. 5301-5305
    • Lindwall, G.1    Cole, R.D.2
  • 69
    • 0026612668 scopus 로고
    • Pp42/44 MAP kinase is a component of the neurogenic pathway utilized by nerve growth factor in PC12 cells
    • Lloyd E.D., Wooten M.W. pp42/44 MAP kinase is a component of the neurogenic pathway utilized by nerve growth factor in PC12 cells. J. Neurochem. 59:1992;1099-1109.
    • (1992) J. Neurochem. , vol.59 , pp. 1099-1109
    • Lloyd, E.D.1    Wooten, M.W.2
  • 70
    • 0027453202 scopus 로고
    • Functional studies of Alzheimer's disease tau protein
    • Lu Q., Wood J.G. Functional studies of Alzheimer's disease tau protein. J. Neurosci. 13:1993;508-515.
    • (1993) J. Neurosci. , vol.13 , pp. 508-515
    • Lu, Q.1    Wood, J.G.2
  • 71
    • 0023833753 scopus 로고
    • Immunochemical evidence that three protein kinase C isozymes increase in abundance during HL-60 differentiation induced by dimethyl sulfoxide and retinoic acid
    • Makowske M., Ballester R., Cayre Y., Rosen O.M. Immunochemical evidence that three protein kinase C isozymes increase in abundance during HL-60 differentiation induced by dimethyl sulfoxide and retinoic acid. J. Biol. Chem. 263:1988;3402-3410.
    • (1988) J. Biol. Chem. , vol.263 , pp. 3402-3410
    • Makowske, M.1    Ballester, R.2    Cayre, Y.3    Rosen, O.M.4
  • 72
    • 0028998409 scopus 로고
    • The microtubule cytoskeleton and the development of neuronal polarity
    • Mandell J.W., Banker G.A. The microtubule cytoskeleton and the development of neuronal polarity. Neurobiol. Aging. 16:1995;229-238.
    • (1995) Neurobiol. Aging , vol.16 , pp. 229-238
    • Mandell, J.W.1    Banker, G.A.2
  • 73
    • 0028989637 scopus 로고
    • Alzheimer's-associated phospho-tau epitope in human neuroblastoma cell cultures: Up-regulation by fibronectin and laminin
    • Martin H., Lambert M.P., Barber K., Hinton S., Klein W.L. Alzheimer's-associated phospho-tau epitope in human neuroblastoma cell cultures: up-regulation by fibronectin and laminin. Neuroscience. 66:1995;769-779.
    • (1995) Neuroscience , vol.66 , pp. 769-779
    • Martin, H.1    Lambert, M.P.2    Barber, K.3    Hinton, S.4    Klein, W.L.5
  • 77
    • 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., Lee V.M. The phosphorylation state of tau in the developing rat brain is regulated by phosphoprotein phosphatases. J. Biol. Chem. 269:1994;30981-30987.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30981-30987
    • Mawal-Dewan, M.1    Henley, J.2    Van De Voorde, A.3    Trojanowski, J.Q.4    Lee, V.M.5
  • 78
    • 0024455082 scopus 로고
    • Microtubular reorganization and dendritic growth response in Alzheimer's disease
    • McKee A.C., Kowall N.W., Kosik K.S. Microtubular reorganization and dendritic growth response in Alzheimer's disease. Ann. Neurol. 26:1989;652-659.
    • (1989) Ann. Neurol. , vol.26 , pp. 652-659
    • McKee, A.C.1    Kowall, N.W.2    Kosik, K.S.3
  • 79
    • 0027322890 scopus 로고
    • Alzheimer disease: Depiction of increased cerebral myo-inositol with proton MR spectroscopy
    • Miller B.L., Moats R.A., Shonk T., Ernst T., Woolley S., Ross B.D. Alzheimer disease: depiction of increased cerebral myo-inositol with proton MR spectroscopy. Radiology. 187:1993;433-437.
    • (1993) Radiology , vol.187 , pp. 433-437
    • Miller, B.L.1    Moats, R.A.2    Shonk, T.3    Ernst, T.4    Woolley, S.5    Ross, B.D.6
  • 82
    • 0022827447 scopus 로고
    • Identification of cDNA clones for the human microtubule-associated protein tau and chromosomal localization of the genes for L tau and microtubule-associated protein 2
    • Neve R.L., Harris P., Kosik K.S., Kurnit D.M., Donlon T.A. Identification of cDNA clones for the human microtubule-associated protein tau and chromosomal localization of the genes for L tau and microtubule-associated protein 2. Mol. Brain Res. 1:1986;271-280.
    • (1986) Mol. Brain Res. , vol.1 , pp. 271-280
    • Neve, R.L.1    Harris, P.2    Kosik, K.S.3    Kurnit, D.M.4    Donlon, T.A.5
  • 83
    • 0024565678 scopus 로고
    • Studies and prospectives of the protein kinase C family for cellular regulation
    • Nishizuka Y. Studies and prospectives of the protein kinase C family for cellular regulation. Cancer. 63:1989;1892-1903.
    • (1989) Cancer , vol.63 , pp. 1892-1903
    • Nishizuka, Y.1
  • 84
    • 0010553282 scopus 로고
    • Synaptosomal protein kinase C subspecies: B. Down-regulation promoted by phorbol ester and its effect on evoked norepinephrine release
    • Oda T., Shearman M.S., Nishizuka Y. Synaptosomal protein kinase C subspecies: B. Down-regulation promoted by phorbol ester and its effect on evoked norepinephrine release. J. Neurosci. 10:1991;2113-2124.
    • (1991) J. Neurosci. , vol.10 , pp. 2113-2124
    • Oda, T.1    Shearman, M.S.2    Nishizuka, Y.3
  • 85
    • 0025687398 scopus 로고
    • Curly fibers are tau-positive strands in the pre- And post-synaptic neurites, consisting of paired helical filaments: Observations by the freeze-etch and replica method
    • Ohtsubo K., Izumiyama N., Kuzuhara S., Mori H., Shimada H. Curly fibers are tau-positive strands in the pre- and post-synaptic neurites, consisting of paired helical filaments: observations by the freeze-etch and replica method. Acta Neuropathol. 81:1990;111-115.
    • (1990) Acta Neuropathol. , vol.81 , pp. 111-115
    • Ohtsubo, K.1    Izumiyama, N.2    Kuzuhara, S.3    Mori, H.4    Shimada, H.5
  • 86
    • 0024561445 scopus 로고
    • Tau protein immunoreactivity in dementia of the Alzheimer type: I. Morphology, evolution, distribution, and pathogenic implications
    • Papasozomenos S.C. Tau protein immunoreactivity in dementia of the Alzheimer type: I. Morphology, evolution, distribution, and pathogenic implications. Lab. Invest. 60:1989;123-137.
    • (1989) Lab. Invest. , vol.60 , pp. 123-137
    • Papasozomenos, S.C.1
  • 87
    • 0024592795 scopus 로고
    • Tau protein immunoreactivity in dementia of the Alzheimer type: II. Electron microscopy and pathogenic implications
    • Papasozomenos S.C. Tau protein immunoreactivity in dementia of the Alzheimer type: II. Electron microscopy and pathogenic implications. Lab. Invest. 60:1989;375-389.
    • (1989) Lab. Invest. , vol.60 , pp. 375-389
    • Papasozomenos, S.C.1
  • 88
    • 0026336497 scopus 로고
    • Domain interactions in protein kinase C
    • Pears C.J., Parker P.J. Domain interactions in protein kinase C. J. Cell Sci. 100:1991;683-686.
    • (1991) J. Cell Sci. , vol.100 , pp. 683-686
    • Pears, C.J.1    Parker, P.J.2
  • 89
    • 0024956444 scopus 로고
    • Molecular insights into Alzheimer's disease
    • Pettegrew J.W. Molecular insights into Alzheimer's disease. Ann. New York Acad. Sci. 568:1989;5-28.
    • (1989) Ann. New York Acad. Sci. , vol.568 , pp. 5-28
    • Pettegrew, J.W.1
  • 90
    • 0027509787 scopus 로고
    • Phosphorylated tau epitope of Alzheimer's disease is coupled to axon development in the avian central nervous system
    • Pope W., Enam S.A., Bawa N., Miller B.E., Ghanbari H.A., Klein W.L. Phosphorylated tau epitope of Alzheimer's disease is coupled to axon development in the avian central nervous system. Exp. Neurol. 120:1993;106-113.
    • (1993) Exp. Neurol. , vol.120 , pp. 106-113
    • Pope, W.1    Enam, S.A.2    Bawa, N.3    Miller, B.E.4    Ghanbari, H.A.5    Klein, W.L.6
  • 91
    • 0020541135 scopus 로고
    • Neuritic plaques in senile dementia of Alzheimer's type: A Golgi analysis in the hippocampal region
    • Probst A., Baler V., Bron B., Ulrich J. Neuritic plaques in senile dementia of Alzheimer's type: a Golgi analysis in the hippocampal region. Brain Res. 268:1983;249-254.
    • (1983) Brain Res. , vol.268 , pp. 249-254
    • Probst, A.1    Baler, V.2    Bron, B.3    Ulrich, J.4
  • 92
    • 0027359507 scopus 로고
    • Differential distribution of tau proteins in developing cat cerebellum
    • Riederer B.M., Binder L.I. Differential distribution of tau proteins in developing cat cerebellum. Brain Res. Bull. 33:1994;155-161.
    • (1994) Brain Res. Bull. , vol.33 , pp. 155-161
    • Riederer, B.M.1    Binder, L.I.2
  • 93
    • 0021288161 scopus 로고
    • 2+-sensitive, phospholipid-dependent protein kinase activity in phorbol ester-treated 3T3 cells
    • 2+-sensitive, phospholipid-dependent protein kinase activity in phorbol ester-treated 3T3 cells. Biochem. Biophys. Res. Commun. 120:1984;1053-1059.
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 1053-1059
    • Rodriguez-Pena, A.1    Rozengurt, E.2
  • 94
    • 0031015699 scopus 로고    scopus 로고
    • Differential expression of PKC isoforms in hippocampal neuronal cultures: Modifications after basic FGF treatment
    • Roisin M.P., Barbin G. Differential expression of PKC isoforms in hippocampal neuronal cultures: modifications after basic FGF treatment. Neurochem. Int. 30:1997;261-270.
    • (1997) Neurochem. Int. , vol.30 , pp. 261-270
    • Roisin, M.P.1    Barbin, G.2
  • 96
    • 0027194957 scopus 로고
    • Continuity of neuropil threads with tangle-bearing and tangle-free neurons in Alzheimer's disease cortex
    • Schmidt M.L., Murray J.M., Trojanowski J.Q. Continuity of neuropil threads with tangle-bearing and tangle-free neurons in Alzheimer's disease cortex. Mol. Chem. Neuropathol. 18:1993;299-311.
    • (1993) Mol. Chem. Neuropathol. , vol.18 , pp. 299-311
    • Schmidt, M.L.1    Murray, J.M.2    Trojanowski, J.Q.3
  • 97
    • 0021022465 scopus 로고
    • Rat hippocampal neurons in culture: Responses to electrical and chemical stimuli
    • Segal M. Rat hippocampal neurons in culture: responses to electrical and chemical stimuli. J. Neurophysiol. 50:1983;1249-1264.
    • (1983) J. Neurophysiol. , vol.50 , pp. 1249-1264
    • Segal, M.1
  • 99
    • 0029874834 scopus 로고    scopus 로고
    • Calcium influx into human neuroblastoma cells induces ALZ-50 immunoreactivity: Involvement of calpain-mediated hydrolysis of protein kinase C
    • Shea T.B., Spencer M.J., Beerman M.L., Cressman C.M., Nixon R.A. Calcium influx into human neuroblastoma cells induces ALZ-50 immunoreactivity: involvement of calpain-mediated hydrolysis of protein kinase C. J. Neurochem. 66:1996;1539-1549.
    • (1996) J. Neurochem. , vol.66 , pp. 1539-1549
    • Shea, T.B.1    Spencer, M.J.2    Beerman, M.L.3    Cressman, C.M.4    Nixon, R.A.5
  • 100
    • 0018193920 scopus 로고
    • Dendritic sprouting in Alzheimer's presenile dementia
    • Sheibel A.B., Tomiyasu U. Dendritic sprouting in Alzheimer's presenile dementia. Exp. Neurol. 60:1978;1-8.
    • (1978) Exp. Neurol. , vol.60 , pp. 1-8
    • Sheibel, A.B.1    Tomiyasu, U.2
  • 101
    • 0026597750 scopus 로고
    • Phosphatidylinositol-specific phospholipase C activity in the postmortem human brain: No alteration in Alzheimer's disease
    • Shimohama S., Fujimoto S., Taniguchi T., Kimura J. Phosphatidylinositol-specific phospholipase C activity in the postmortem human brain: no alteration in Alzheimer's disease. Brain Res. 579:1992;347-349.
    • (1992) Brain Res. , vol.579 , pp. 347-349
    • Shimohama, S.1    Fujimoto, S.2    Taniguchi, T.3    Kimura, J.4
  • 102
    • 0027265320 scopus 로고
    • Assessment of protein kinase C isozymes by two-site enzyme immunoassay in human brains and changes in Alzheimer's disease
    • Shimohama S., Narita M., Matsushima H., Kimura J., Kameyama M., Hagiwara M., Hidaka H., Taniguchi T. Assessment of protein kinase C isozymes by two-site enzyme immunoassay in human brains and changes in Alzheimer's disease. Neurology. 43:1993;1407-1413.
    • (1993) Neurology , vol.43 , pp. 1407-1413
    • Shimohama, S.1    Narita, M.2    Matsushima, H.3    Kimura, J.4    Kameyama, M.5    Hagiwara, M.6    Hidaka, H.7    Taniguchi, T.8
  • 104
    • 0026539580 scopus 로고
    • Massive accumulation of modified tau and severe depletion of normal tau characterize the cerebral cortex and white matter of Alzheimer's disease
    • Shin R.-W., Iwaki T., Kitamoto T., Sato Y., Tateishi J. Massive accumulation of modified tau and severe depletion of normal tau characterize the cerebral cortex and white matter of Alzheimer's disease. Am. J. Pathol. 140:1992;937-945.
    • (1992) Am. J. Pathol. , vol.140 , pp. 937-945
    • Shin, R.-W.1    Iwaki, T.2    Kitamoto, T.3    Sato, Y.4    Tateishi, J.5
  • 105
    • 0023521088 scopus 로고
    • Reduced phosphoinositide concentrations in anterior temporal cortex of Alzheimer-diseased brain
    • Stokes C.E., Hawthorne J.N. Reduced phosphoinositide concentrations in anterior temporal cortex of Alzheimer-diseased brain. J. Neurochem. 48:1987;1018-1021.
    • (1987) J. Neurochem. , vol.48 , pp. 1018-1021
    • Stokes, C.E.1    Hawthorne, J.N.2
  • 106
    • 0027388775 scopus 로고
    • Recognition of the minimal epitope of monoclonal antibody Tau 1 depends upon the presence of a phosphate group but not its location
    • Szendrei G.I., Lee V.M., Otvos L. Jr. Recognition of the minimal epitope of monoclonal antibody Tau 1 depends upon the presence of a phosphate group but not its location. J. Neurosci. Res. 34:1993;243-249.
    • (1993) J. Neurosci. Res. , vol.34 , pp. 243-249
    • Szendrei, G.I.1    Lee, V.M.2    Otvos L., Jr.3
  • 108
    • 0025768292 scopus 로고
    • The axonal origin of a subpopulation of dystrophic neurites in Alzheimer's disease
    • Tourtellotte W.G., Van Hoesen G.W. The axonal origin of a subpopulation of dystrophic neurites in Alzheimer's disease. Neurosci. Lett. 129:1991;11-16.
    • (1991) Neurosci. Lett. , vol.129 , pp. 11-16
    • Tourtellotte, W.G.1    Van Hoesen, G.W.2
  • 109
    • 0027479150 scopus 로고
    • Altered tau and neurofilament proteins in neurodegenerative diseases: Diagnostic implications for Alzheimer's disease and Lewy body dementias
    • Trojanowski J., Schmidt M., Shin R.-W., Bramblett G., Rao D., Lee V. Altered tau and neurofilament proteins in neurodegenerative diseases: diagnostic implications for Alzheimer's disease and Lewy body dementias. Brain Pathol. 3:1993;45-54.
    • (1993) Brain Pathol. , vol.3 , pp. 45-54
    • Trojanowski, J.1    Schmidt, M.2    Shin, R.-W.3    Bramblett, G.4    Rao, D.5    Lee, V.6
  • 110
    • 0024529404 scopus 로고
    • Distribution of tau proteins in the normal human central and peripheral nervous system
    • Trojanowski J.Q., Schuck T., Schmidt M.L., Lee V.M.-Y. Distribution of tau proteins in the normal human central and peripheral nervous system. J. Histochem. Cytochem. 37:1989;209-215.
    • (1989) J. Histochem. Cytochem. , vol.37 , pp. 209-215
    • Trojanowski, J.Q.1    Schuck, T.2    Schmidt, M.L.3    Lee, V.M.-Y.4
  • 111
    • 0027971374 scopus 로고    scopus 로고
    • Regulation of mitogen-activated protein kinase activation by protein kinase A and C in a cell-free system
    • VanRenterghem B., Browning M.D., Maller J.L. Regulation of mitogen-activated protein kinase activation by protein kinase A and C in a cell-free system. J. Biol. Chem. 269:1996;24666-24672.
    • (1996) J. Biol. Chem. , vol.269 , pp. 24666-24672
    • Vanrenterghem, B.1    Browning, M.D.2    Maller, J.L.3
  • 112
    • 0023901864 scopus 로고
    • Mitogen-stimulated tyrosine phosphorylation of a 42-kDa cellular protein: Evidence for a protein kinase-C requirement
    • Vila J., Weber M.J. Mitogen-stimulated tyrosine phosphorylation of a 42-kDa cellular protein: evidence for a protein kinase-C requirement. J. Cell. Physiol. 135:1988;285-292.
    • (1988) J. Cell. Physiol. , vol.135 , pp. 285-292
    • Vila, J.1    Weber, M.J.2
  • 113
    • 0028339544 scopus 로고
    • Attenuated protein kinase C activity and translocation in Alzheimer's disease brain
    • Wang H., Pisano M.R., Friedman E. Attenuated protein kinase C activity and translocation in Alzheimer's disease brain. Neurobiol. Aging. 15:1994;293-298.
    • (1994) Neurobiol. Aging , vol.15 , pp. 293-298
    • Wang, H.1    Pisano, M.R.2    Friedman, E.3
  • 114
    • 0027469909 scopus 로고
    • A novel tau transcript in cultured human neuroblastoma cells expressing nuclear tau
    • Wang Y., Loomis P.A., Zinkowski R.P., Binder L.I. A novel tau transcript in cultured human neuroblastoma cells expressing nuclear tau. J. Cell Biol. 121:1993;257-267.
    • (1993) J. Cell Biol. , vol.121 , pp. 257-267
    • Wang, Y.1    Loomis, P.A.2    Zinkowski, R.P.3    Binder, L.I.4
  • 116
    • 0023120470 scopus 로고
    • High resolution of paired helical filaments in Alzheimer's disease
    • Wen G.Y., Wisniewski H.M. High resolution of paired helical filaments in Alzheimer's disease. J. Electron Microsc. 5:1987;347-355.
    • (1987) J. Electron Microsc. , vol.5 , pp. 347-355
    • Wen, G.Y.1    Wisniewski, H.M.2
  • 117
    • 0026755755 scopus 로고
    • Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro
    • Wille H., Drewes G., Biernat J., Mandelkow E.M., Mandelkow E. Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro. J. Cell Biol. 118:1992;573-584.
    • (1992) J. Cell Biol. , vol.118 , pp. 573-584
    • Wille, H.1    Drewes, G.2    Biernat, J.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 118
    • 0023766803 scopus 로고
    • Reexpression of a developmentally regulated antigen in Down syndrome and Alzheimer disease
    • Wolozin B., Scicutella A., Davies P. Reexpression of a developmentally regulated antigen in Down syndrome and Alzheimer disease. Proc. Natl. Acad. Sci. U.S.A. 85:1988;6202-6206.
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 6202-6206
    • Wolozin, B.1    Scicutella, A.2    Davies, P.3
  • 119
    • 0027237861 scopus 로고
    • Tau in paired helical filaments is functionally distinct from fetal tau: Assembly incompetence of paired helical filament-tau
    • Yoshida H., Ihara Y. Tau in paired helical filaments is functionally distinct from fetal tau: assembly incompetence of paired helical filament-tau. J. Neurochem. 61:1993;1183-1186.
    • (1993) J. Neurochem. , vol.61 , pp. 1183-1186
    • Yoshida, H.1    Ihara, Y.2


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