메뉴 건너뛰기




Volumn 114, Issue 1, 2004, Pages 121-130

Caspase-cleavage of tau is an early event in Alzheimer disease tangle pathology

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; CASPASE; CYTOSKELETON PROTEIN; GLYCOGEN SYNTHASE KINASE 3BETA; TAU PROTEIN; MEMBRANE PROTEIN; PRESENILIN 1; PSEN1 PROTEIN, HUMAN;

EID: 3242749074     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI200420640     Document Type: Article
Times cited : (494)

References (80)
  • 1
    • 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. 343:461-463.
    • (1990) Nature , vol.343 , pp. 461-463
    • Caceres, A.1    Kosik, K.S.2
  • 2
    • 0032476645 scopus 로고    scopus 로고
    • Overexpression of tau protein inhibits kinesin-dependent trafficking of vesicles, mitochondria, and endoplasmic reticulum: Implications for Alzheimer's disease
    • Ebneth, A., et al. 1998. Overexpression of tau protein inhibits kinesin-dependent trafficking of vesicles, mitochondria, and endoplasmic reticulum: implications for Alzheimer's disease. J. Cell Biol. 143:777-794.
    • (1998) J. Cell Biol. , vol.143 , pp. 777-794
    • Ebneth, A.1
  • 3
    • 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. 156:1051-1063.
    • (2002) J. Cell Biol. , vol.156 , pp. 1051-1063
    • Stamer, K.1    Vogel, R.2    Thies, E.3    Mandelkow, E.4    Mandelkow, E.M.5
  • 6
    • 0023009658 scopus 로고
    • Microtubule-associated protein tau. A component of Alzheimer paired helical filaments
    • Grundke-Iqbal, I., et al. 1986. Microtubule-associated protein tau. A component of Alzheimer paired helical filaments. J. Biol. Chem. 261:6084-6089.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6084-6089
    • Grundke-Iqbal, I.1
  • 7
    • 0024044195 scopus 로고
    • Structural characterization of the core of the paired helical filament of Alzheimer disease
    • Wischik, C.M., et al. 1988. Structural characterization of the core of the paired helical filament of Alzheimer disease. Proc. Natl. Acad. Sci. U. S. A. 85:4884-4888.
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 4884-4888
    • Wischik, C.M.1
  • 8
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer-related changes
    • Braak, H., and Braak, E. 1991. Neuropathological stageing of Alzheimer-related changes. Acta Neuropathol. 82:239-259.
    • (1991) Acta Neuropathol. , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 9
    • 0030936599 scopus 로고    scopus 로고
    • Alz-50 and MC-1, a new monoclonal antibody raised to paired helical filaments, recognize conformational epitopes on recombinant tau
    • Jicha, G.A., Bowser, R., Kazam, I.G., and Davies, P. 1997. Alz-50 and MC-1, a new monoclonal antibody raised to paired helical filaments, recognize conformational epitopes on recombinant tau. J. Neurosci. Res. 48:128-132.
    • (1997) J. Neurosci. Res. , vol.48 , pp. 128-132
    • Jicha, G.A.1    Bowser, R.2    Kazam, I.G.3    Davies, P.4
  • 10
    • 0033558929 scopus 로고    scopus 로고
    • Sequence requirements for formation of conformational variants of tau similar to those found in Alzheimer's disease
    • Jicha, G.A., Berenfeld, B., and Davies, P. 1999. Sequence requirements for formation of conformational variants of tau similar to those found in Alzheimer's disease. J. Neurosci. Res. 55:713-723.
    • (1999) J. Neurosci. Res. , vol.55 , pp. 713-723
    • Jicha, G.A.1    Berenfeld, B.2    Davies, P.3
  • 11
    • 0034594482 scopus 로고    scopus 로고
    • Formation of diffuse and fibrillar tangles in aging and early Alzheimer's disease
    • Uboga, N.V., and Price, J.L. 2000. Formation of diffuse and fibrillar tangles in aging and early Alzheimer's disease. Neurobiol. Aging. 21:1-10.
    • (2000) Neurobiol. Aging , vol.21 , pp. 1-10
    • Uboga, N.V.1    Price, J.L.2
  • 12
    • 0034282067 scopus 로고    scopus 로고
    • Conformational change as one of the earliest alterations of tau in Alzheimer's disease
    • Weaver, C.L., Espinoza, M., Kress, Y., and Davies, P. 2000. Conformational change as one of the earliest alterations of tau in Alzheimer's disease. Neurobiol. Aging. 21:719-727.
    • (2000) Neurobiol. Aging , vol.21 , pp. 719-727
    • Weaver, C.L.1    Espinoza, M.2    Kress, Y.3    Davies, P.4
  • 13
    • 0028946744 scopus 로고
    • Monoclonal antibody AT8 recognises tau protein phosphorylated at both serine 202 and threonine 205
    • Goedert, M., Jakes, R., and Vanmechelen, E. 1995. Monoclonal antibody AT8 recognises tau protein phosphorylated at both serine 202 and threonine 205. Neurosci. Lett. 189:167-169.
    • (1995) Neurosci. Lett. , vol.189 , pp. 167-169
    • Goedert, M.1    Jakes, R.2    Vanmechelen, E.3
  • 14
    • 0027217679 scopus 로고
    • The abnormal phosphorylation of tau protein at Ser-202 in Alzheimer disease recapitulates phosphorylation during development
    • Goedert, M., et al. 1993. The abnormal phosphorylation of tau protein at Ser-202 in Alzheimer disease recapitulates phosphorylation during development. Proc. Natl. Acad. Sci. U. S. A. 90:5066-5070.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 5066-5070
    • Goedert, M.1
  • 15
    • 0026501888 scopus 로고
    • Hydrofluoric acid-treated tau PHF proteins display the same biochemical properties as normal tau
    • Greenberg, S.G., Davies, P., Schein, J.D., and Binder, L.I. 1992. Hydrofluoric acid-treated tau PHF proteins display the same biochemical properties as normal tau. J. Biol. Chem. 267:564-569.
    • (1992) J. Biol. Chem. , vol.267 , pp. 564-569
    • Greenberg, S.G.1    Davies, P.2    Schein, J.D.3    Binder, L.I.4
  • 16
    • 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. 3:1141-1154.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1141-1154
    • Drechsel, D.N.1    Hyman, A.A.2    Cobb, M.H.3    Kirschner, M.W.4
  • 17
    • 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., and Mandelkow, E. 1993. Phosphorylation of Ser262 strongly reduces binding of tau to microtubules: distinction between PHF-like immunoreactivity and microtubule binding. Neuron. 11:153-163.
    • (1993) Neuron , vol.11 , pp. 153-163
    • Biernat, J.1    Gustke, N.2    Drewes, G.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 18
    • 0027308924 scopus 로고
    • Abnormal tau phosphorylation at Ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding
    • Bramblett, G.T., et al. 1993. Abnormal tau phosphorylation at Ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding. Neuron. 10:1089-1099.
    • (1993) Neuron , vol.10 , pp. 1089-1099
    • Bramblett, G.T.1
  • 19
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr, J.F., Wyllie, A.H., and Currie, A.R. 1972. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br. J. Cancer. 26:239-257.
    • (1972) Br. J. Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 20
    • 0033617402 scopus 로고    scopus 로고
    • Involvement of caspases in proteolytic cleavage of Alzheimer's amyloid-beta precursor protein and amyloidogenic A beta peptide formation
    • Gervais, F.G., et al. 1999. Involvement of caspases in proteolytic cleavage of Alzheimer's amyloid-beta precursor protein and amyloidogenic A beta peptide formation. Cell. 97:395-406.
    • (1999) Cell , vol.97 , pp. 395-406
    • Gervais, F.G.1
  • 21
    • 0032747486 scopus 로고    scopus 로고
    • Activation of caspase-3 in single neurons and autophagic granules of granulovacuolar degeneration in Alzheimer's disease. Evidence for apoptotic cell death
    • Stadelmann, C., et al. 1999. Activation of caspase-3 in single neurons and autophagic granules of granulovacuolar degeneration in Alzheimer's disease. Evidence for apoptotic cell death. Am. J. Pathol. 155:1459-1466.
    • (1999) Am. J. Pathol. , vol.155 , pp. 1459-1466
    • Stadelmann, C.1
  • 23
    • 0035141757 scopus 로고    scopus 로고
    • Correlation between caspase activation and neurofibrillary tangle formation in Alzheimer's disease
    • Rohn, T.T., et al. 2001. Correlation between caspase activation and neurofibrillary tangle formation in Alzheimer's disease. Am. J. Pathol. 158:189-198.
    • (2001) Am. J. Pathol. , vol.158 , pp. 189-198
    • Rohn, T.T.1
  • 24
    • 0035917831 scopus 로고    scopus 로고
    • Activated caspase-3 expression in Alzheimer's and aged control brain: Correlation with Alzheimer pathology
    • Su, J.H., Zhao, M., Anderson, A.J., Srinivasan, A., and Cotman, C.W. 2001. Activated caspase-3 expression in Alzheimer's and aged control brain: correlation with Alzheimer pathology. Brain Res. 898:350-357.
    • (2001) Brain Res. , vol.898 , pp. 350-357
    • Su, J.H.1    Zhao, M.2    Anderson, A.J.3    Srinivasan, A.4    Cotman, C.W.5
  • 25
    • 0036968953 scopus 로고    scopus 로고
    • Caspase-9 activation and caspase cleavage of tau in the Alzheimer's disease brain
    • Rohn, T.T., et al. 2002. Caspase-9 activation and caspase cleavage of tau in the Alzheimer's disease brain. Neurobiol. Dis. 11:341-354.
    • (2002) Neurobiol. Dis. , vol.11 , pp. 341-354
    • Rohn, T.T.1
  • 26
    • 0042837889 scopus 로고    scopus 로고
    • Caspase activation in the limbic cortex of subjects with early Alzheimer's disease
    • Gastard, M.C., Troncoso, J.C., and Koliatsos, V.E. 2003. Caspase activation in the limbic cortex of subjects with early Alzheimer's disease. Ann. Neurol. 54:393-398.
    • (2003) Ann. Neurol. , vol.54 , pp. 393-398
    • Gastard, M.C.1    Troncoso, J.C.2    Koliatsos, V.E.3
  • 27
    • 0028934919 scopus 로고
    • Proteolysis of fodrin (non-erythroid spectrin) during apoptosis
    • Martin, S.J., et al. 1995. Proteolysis of fodrin (non-erythroid spectrin) during apoptosis. J. Biol. Chem. 270:6425-6428.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6425-6428
    • Martin, S.J.1
  • 28
    • 17344365975 scopus 로고    scopus 로고
    • Tau cleavage and dephosphorylation in cerebellar granule neurons undergoing apoptosis
    • Canu, N., et al. 1998. Tau cleavage and dephosphorylation in cerebellar granule neurons undergoing apoptosis. J. Neurosci. 18:7061-7074.
    • (1998) J. Neurosci. , vol.18 , pp. 7061-7074
    • Canu, N.1
  • 29
    • 0031930313 scopus 로고    scopus 로고
    • Antibody to caspase-cleaved actin detects apoptosis in differentiated neuroblastoma and plaque-associated neurons and microglia in Alzheimer's disease
    • Yang, F., et al. 1998. Antibody to caspase-cleaved actin detects apoptosis in differentiated neuroblastoma and plaque-associated neurons and microglia in Alzheimer's disease. Am. J. Pathol. 152:379-389.
    • (1998) Am. J. Pathol. , vol.152 , pp. 379-389
    • Yang, F.1
  • 30
    • 0033928035 scopus 로고    scopus 로고
    • The neuronal microtubule-associated protein tau is asubstrate for caspase-3 and an effector of apoptosis
    • Fasulo, L., et al. 2000. The neuronal microtubule-associated protein tau is asubstrate for caspase-3 and an effector of apoptosis. J. Neurochem. 75:624-633.
    • (2000) J. Neurochem. , vol.75 , pp. 624-633
    • Fasulo, L.1
  • 31
    • 0035116325 scopus 로고    scopus 로고
    • Proapoptotic effects of tau cleavage product generated by caspase-3
    • Chung, C.W., et al. 2001. Proapoptotic effects of tau cleavage product generated by caspase-3. Neurobiol. Dis. 8:162-172.
    • (2001) Neurobiol. Dis. , vol.8 , pp. 162-172
    • Chung, C.W.1
  • 32
    • 0037119943 scopus 로고    scopus 로고
    • DEDD regulates degradation of intermediate filaments during apoptosis
    • Lee, J.C., et al. 2002. DEDD regulates degradation of intermediate filaments during apoptosis. J. Cell Biol. 158:1051-1066.
    • (2002) J. Cell Biol. , vol.158 , pp. 1051-1066
    • Lee, J.C.1
  • 33
    • 0037468612 scopus 로고    scopus 로고
    • C-terminal 15 kDa fragment of cytoskeletal actin is posttranslationally N-myristoylated upon caspase-mediated cleavage and targeted to mitochondria
    • Utsumi, T., Sakurai, N., Nakano, K., and Ishisaka, R. 2003. C-terminal 15 kDa fragment of cytoskeletal actin is posttranslationally N-myristoylated upon caspase-mediated cleavage and targeted to mitochondria. FEBS Lett. 539:37-44.
    • (2003) FEBS Lett. , vol.539 , pp. 37-44
    • Utsumi, T.1    Sakurai, N.2    Nakano, K.3    Ishisaka, R.4
  • 34
    • 0041689948 scopus 로고    scopus 로고
    • Caspase cleavage of tau: Linking amyloid and neurofibrillary tangles in Alzheimer's disease
    • Gamblin, T.C., et al. 2003. Caspase cleavage of tau: linking amyloid and neurofibrillary tangles in Alzheimer's disease. Proc. Natl. Acad. Sci. U. S. A. 100:10032-10037.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 10032-10037
    • Gamblin, T.C.1
  • 35
    • 12644260802 scopus 로고    scopus 로고
    • The structural basis of monoclonal antibody Alz50's selectivity for Alzheimer's disease pathology
    • Carmel, G., Mager, E.M., Binder, L.I., and Kuret, J. 1996. The structural basis of monoclonal antibody Alz50's selectivity for Alzheimer's disease pathology. J. Biol. Chem. 271:32789-32795.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32789-32795
    • Carmel, G.1    Mager, E.M.2    Binder, L.I.3    Kuret, J.4
  • 36
    • 0024109687 scopus 로고
    • Epitopes that span the tau molecule are shared with paired helical filaments
    • Kosik, K.S., et al. 1988. Epitopes that span the tau molecule are shared with paired helical filaments. Neuron. 1:817-825.
    • (1988) Neuron , vol.1 , pp. 817-825
    • Kosik, K.S.1
  • 37
    • 0036799487 scopus 로고    scopus 로고
    • Multiple caspases are activated after traumatic brain injury: Evidence for involvement in functional outcome
    • Knoblach, S.M., et al. 2002. Multiple caspases are activated after traumatic brain injury: evidence for involvement in functional outcome. J. Neurotrauma. 19:1155-1170.
    • (2002) J. Neurotrauma , vol.19 , pp. 1155-1170
    • Knoblach, S.M.1
  • 38
    • 0034700253 scopus 로고    scopus 로고
    • Oxidative regulation of fatty acid-induced tau polymerization
    • Gamblin, T.C., King, M.E., Kuret, J., Berry, R.W., and Binder, L.I. 2000. Oxidative regulation of fatty acid-induced tau polymerization. Biochemistry. 39:14203-14210.
    • (2000) Biochemistry , vol.39 , pp. 14203-14210
    • Gamblin, T.C.1    King, M.E.2    Kuret, J.3    Berry, R.W.4    Binder, L.I.5
  • 39
    • 0037126688 scopus 로고    scopus 로고
    • Toward a unified scheme for the aggregation of tau into Alzheimer paired helical filaments
    • Barghorn, S., and Mandelkow, E. 2002. Toward a unified scheme for the aggregation of tau into Alzheimer paired helical filaments. Biochemistry. 41:14885-14896.
    • (2002) Biochemistry , vol.41 , pp. 14885-14896
    • Barghorn, S.1    Mandelkow, E.2
  • 41
    • 0028675873 scopus 로고
    • Alzheimer's disease-like phosphorylation of the microtubule-associated protein tau by glycogen synthase kinase-3 in transfecred mammalian cells
    • Lovestone, S., et al. 1994. Alzheimer's disease-like phosphorylation of the microtubule-associated protein tau by glycogen synthase kinase-3 in transfecred mammalian cells. Curr. Biol. 4:1077-1086.
    • (1994) Curr. Biol. , vol.4 , pp. 1077-1086
    • Lovestone, S.1
  • 42
    • 0027257708 scopus 로고
    • Apoptosis is induced by beta-amyloid in cultured central nervous system neurons
    • Loo, D.T., et al. 1993. Apoptosis is induced by beta-amyloid in cultured central nervous system neurons. Proc. Natl. Acad. Sci. U. S. A. 90:7951-795.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 7951-7795
    • Loo, D.T.1
  • 43
    • 0033593456 scopus 로고    scopus 로고
    • Multiple pathways of apoptosis in PC12 cells. CrmA inhibits apoptosis induced by beta-amyloid
    • Ivins, K.J., Ivins, J.K., Sharp, J.P., and Cotman, C.W. 1999. Multiple pathways of apoptosis in PC12 cells. CrmA inhibits apoptosis induced by beta-amyloid. J. Biol. Chem. 274:2107-2112.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2107-2112
    • Ivins, K.J.1    Ivins, J.K.2    Sharp, J.P.3    Cotman, C.W.4
  • 44
    • 0032726814 scopus 로고    scopus 로고
    • Neuronal apoptosis induced by beta-amyloid is mediated by caspase-8
    • Ivins, K.J., Thornton, P.L., Rohn, T.T., and Cotman, C.W. 1999. Neuronal apoptosis induced by beta-amyloid is mediated by caspase-8. Neurobiol. Dis. 6:440-449.
    • (1999) Neurobiol. Dis. , vol.6 , pp. 440-449
    • Ivins, K.J.1    Thornton, P.L.2    Rohn, T.T.3    Cotman, C.W.4
  • 45
    • 0042697305 scopus 로고    scopus 로고
    • Triple-transgenic model of Alzheimer's disease with plaques and tangles: Intracellular Abeta and synaptic dysfunction
    • Oddo, S., et al. 2003. Triple-transgenic model of Alzheimer's disease with plaques and tangles: intracellular Abeta and synaptic dysfunction. Neuron. 39:409-421.
    • (2003) Neuron , vol.39 , pp. 409-421
    • Oddo, S.1
  • 46
    • 0037826853 scopus 로고    scopus 로고
    • Inhibition of tau polymerization by its carboxy-terminal caspase cleavage fragment
    • Berry, R.W., et al. 2003. Inhibition of tau polymerization by its carboxy-terminal caspase cleavage fragment. Biochemistry. 42:8325-8331.
    • (2003) Biochemistry , vol.42 , pp. 8325-8331
    • Berry, R.W.1
  • 47
    • 0033677809 scopus 로고    scopus 로고
    • C-terminal inhibition of tau assembly in vitro and in Alzheimer's disease
    • Abraha, A., et al. 2000. C-terminal inhibition of tau assembly in vitro and in Alzheimer's disease. J. Cell Sci. 113:3737-3745.
    • (2000) J. Cell Sci. , vol.113 , pp. 3737-3745
    • Abraha, A.1
  • 48
    • 0027398169 scopus 로고
    • Molecular characterization of the minimal protease resistant tau unit of the Alzheimer's disease paired helical filament
    • Novak, M., Kabat, J., and Wischik, C.M. 1993. Molecular characterization of the minimal protease resistant tau unit of the Alzheimer's disease paired helical filament. EMBO J. 12:365-370.
    • (1993) EMBO J. , vol.12 , pp. 365-370
    • Novak, M.1    Kabat, J.2    Wischik, C.M.3
  • 49
    • 0035811050 scopus 로고    scopus 로고
    • Hyperphosphorylation induces self-assembly of tau into tangles of paired helical filaments/straight filaments
    • Alonso, A., Zaidi, T., Novak, M., Grundke-Iqbal, I., and Iqbal, K. 2001. Hyperphosphorylation induces self-assembly of tau into tangles of paired helical filaments/straight filaments. Proc. Natl. Acad. Sci. U. S. A. 98:6923-6928.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 6923-6928
    • Alonso, A.1    Zaidi, T.2    Novak, M.3    Grundke-Iqbal, I.4    Iqbal, K.5
  • 50
    • 0042889049 scopus 로고    scopus 로고
    • Neurodegeneration and defective neurotransmission in a Caenorhabditis elegans model of tauopathy
    • Kraemer, B.C., et al. 2003. Neurodegeneration and defective neurotransmission in a Caenorhabditis elegans model of tauopathy. Proc. Natl. Acad. Sci. U. S. A. 100:9980-9985.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 9980-9985
    • Kraemer, B.C.1
  • 51
    • 0035943436 scopus 로고    scopus 로고
    • Formation of neurofibrillary tangles in P3011 tau transgenic mice induced by Abeta 42 fibrils
    • Gotz, 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. 293:1491-1495.
    • (2001) Science , vol.293 , pp. 1491-1495
    • Gotz, J.1    Chen, F.2    Van Dorpe, J.3    Nitsch, R.M.4
  • 52
    • 17944382037 scopus 로고    scopus 로고
    • Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP
    • Lewis, J., et al. 2001. Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP. Science. 293:1487-1491.
    • (2001) Science , vol.293 , pp. 1487-1491
    • Lewis, J.1
  • 53
    • 0037118247 scopus 로고    scopus 로고
    • Human wild-type tau interacts with wingless pathway components and produces neurofibrillary pathology in Drosophila
    • Jackson, G.R., et al. 2002. Human wild-type tau interacts with wingless pathway components and produces neurofibrillary pathology in Drosophila. Neuron. 34:509-519.
    • (2002) Neuron , vol.34 , pp. 509-519
    • Jackson, G.R.1
  • 54
    • 0041803006 scopus 로고    scopus 로고
    • Hyperphosphorylation and aggregation of tau in mice expressing normal human tau isoforms
    • Andorfer, C., et al. 2003. Hyperphosphorylation and aggregation of tau in mice expressing normal human tau isoforms. J. Neurochem. 86:582-590.
    • (2003) J. Neurochem. , vol.86 , pp. 582-590
    • Andorfer, C.1
  • 55
    • 0035824277 scopus 로고    scopus 로고
    • Tau phosphorylation during apoptosis of human SH-SY5Y neuroblastoma cells
    • Mookherjee, P., and Johnson, G.V. 2001. Tau phosphorylation during apoptosis of human SH-SY5Y neuroblastoma cells. Brain Res. 921:31-43.
    • (2001) Brain Res. , vol.921 , pp. 31-43
    • Mookherjee, P.1    Johnson, G.V.2
  • 56
    • 0033899864 scopus 로고    scopus 로고
    • Staging of cytoskeletal and beta-amyloid changes in human isocortex reveals biphasic synaptic protein response during progression of Alzheimer's disease
    • Mukaetova-Ladinska, E.B., et al. 2000. Staging of cytoskeletal and beta-amyloid changes in human isocortex reveals biphasic synaptic protein response during progression of Alzheimer's disease. Am. J. Pathol. 157:623-636.
    • (2000) Am. J. Pathol. , vol.157 , pp. 623-636
    • Mukaetova-Ladinska, E.B.1
  • 57
    • 0033622324 scopus 로고    scopus 로고
    • Intraneuronal Abeta42 accumulation in human brain
    • Gouras, G.K., et al. 2000. Intraneuronal Abeta42 accumulation in human brain. Am. J. Pathol. 156:15-20.
    • (2000) Am. J. Pathol. , vol.156 , pp. 15-20
    • Gouras, G.K.1
  • 58
    • 0344845132 scopus 로고    scopus 로고
    • Amyloid deposition precedes tangle formation in a triple transgenic model of Alzheimer's disease
    • Oddo, S., Caccamo, A., Kitazawa, M., Tseng, B.P., and LaFerla, F.M. 2003. Amyloid deposition precedes tangle formation in a triple transgenic model of Alzheimer's disease. Neurobiol. Aging. 24:1063-1070.
    • (2003) Neurobiol. Aging , vol.24 , pp. 1063-1070
    • Oddo, S.1    Caccamo, A.2    Kitazawa, M.3    Tseng, B.P.4    LaFerla, F.M.5
  • 60
    • 0037474263 scopus 로고    scopus 로고
    • Apoptotic neuronal cell death induced by the non-fibrillar amyloid-beta peptide proceeds through an early reactive oxygen species-dependent cytoskeleton perturbation
    • Sponne, I., et al. 2003. Apoptotic neuronal cell death induced by the non-fibrillar amyloid-beta peptide proceeds through an early reactive oxygen species-dependent cytoskeleton perturbation. J. Biol. Chem. 278:3437-3445.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3437-3445
    • Sponne, I.1
  • 61
    • 0037186074 scopus 로고    scopus 로고
    • Altered metabolism of the amyloid beta precursor protein is associated with mitochondrial dysfunction in Down's syndrome
    • Busciglio, J., et al. 2002. Altered metabolism of the amyloid beta precursor protein is associated with mitochondrial dysfunction in Down's syndrome. Neuron. 33:677-688.
    • (2002) Neuron , vol.33 , pp. 677-688
    • Busciglio, J.1
  • 62
    • 0036827031 scopus 로고    scopus 로고
    • Intraneuronal Alzheimer abeta42 accumulates in multivesicular bodies and is associated with synaptic pathology
    • Takahashi, R.H., et al. 2002. Intraneuronal Alzheimer abeta42 accumulates in multivesicular bodies and is associated with synaptic pathology. Am. J. Pathol. 161:1869-1879.
    • (2002) Am. J. Pathol. , vol.161 , pp. 1869-1879
    • Takahashi, R.H.1
  • 63
    • 0035933279 scopus 로고    scopus 로고
    • Intraneuronal Abeta accumulation precedes plaque formation in beta-amyloid precursor protein and presenilin-1 double-transgenic mice
    • Wirths, O., et al. 2001. Intraneuronal Abeta accumulation precedes plaque formation in beta-amyloid precursor protein and presenilin-1 double-transgenic mice. Neurosci. Lett. 306:116-120.
    • (2001) Neurosci. Lett. , vol.306 , pp. 116-120
    • Wirths, O.1
  • 64
    • 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. 30:156-165.
    • (1991) Ann. Neurol. , vol.30 , pp. 156-165
    • McKee, A.C.1    Kosik, K.S.2    Kowall, N.W.3
  • 65
    • 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. 17:921-933.
    • (1996) Neurobiol. Aging , vol.17 , pp. 921-933
    • Cummings, B.J.1    Pike, C.J.2    Shankle, R.3    Cotman, C.W.4
  • 66
    • 0033394155 scopus 로고    scopus 로고
    • Memory and mental status correlates of modified Braak staging
    • Grober, E., et al. 1999. Memory and mental status correlates of modified Braak staging. Neurobiol. Aging. 20:573-579.
    • (1999) Neurobiol. Aging , vol.20 , pp. 573-579
    • Grober, E.1
  • 68
    • 0032487648 scopus 로고    scopus 로고
    • Amyloid beta-peptide induces apoptosis-related events in synapses and dendrites
    • Mattson, M.P., Partin, J., and Begley, J.G. 1998. Amyloid beta-peptide induces apoptosis-related events in synapses and dendrites. Brain Res. 807:167-176.
    • (1998) Brain Res. , vol.807 , pp. 167-176
    • Mattson, M.P.1    Partin, J.2    Begley, J.G.3
  • 69
    • 0037458021 scopus 로고    scopus 로고
    • Caspase 3 activation is essential for neuroprotection in preconditioning
    • McLaughlin, B., et al. 2003. Caspase 3 activation is essential for neuroprotection in preconditioning. Proc. Natl. Acad. Sci. U. S. A. 100:715-720.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 715-720
    • McLaughlin, B.1
  • 70
    • 3342980580 scopus 로고    scopus 로고
    • The kinder side of killer proteases: Caspase activation contributes to neuroprotection and CNS remodeling
    • McLaughlin, B. 2004. The kinder side of killer proteases: caspase activation contributes to neuroprotection and CNS remodeling. Apoptosis. 9:111-121.
    • (2004) Apoptosis , vol.9 , pp. 111-121
    • McLaughlin, B.1
  • 71
    • 0346218254 scopus 로고    scopus 로고
    • Atypical role of proximal caspase-8 in truncated Tau-indued neurite regression and neuron cell death
    • Chung, C.W., et al. 2003. Atypical role of proximal caspase-8 in truncated Tau-indued neurite regression and neuron cell death. Neurobiol. Dis. 14:557-566.
    • (2003) Neurobiol. Dis. , vol.14 , pp. 557-566
    • Chung, C.W.1
  • 72
    • 0037017399 scopus 로고    scopus 로고
    • Selective cytotoxicity of intracellular amyloid beta peptide1-42 through p53 and Bax in cultured primary human neurons
    • Zhang, Y., McLaughlin, R., Goodyer, C., and LeBlanc, A. 2002. Selective cytotoxicity of intracellular amyloid beta peptide1-42 through p53 and Bax in cultured primary human neurons. J. Cell Biol. 156:519-529.
    • (2002) J. Cell Biol. , vol.156 , pp. 519-529
    • Zhang, Y.1    McLaughlin, R.2    Goodyer, C.3    LeBlanc, A.4
  • 73
    • 0036869740 scopus 로고    scopus 로고
    • Caspase activation in the Alzheimer's disease brain: Tortuous and torturous
    • Rohn, T.T., Rissman, R.A., Head, E., and Cotman, C.W. 2002. Caspase activation in the Alzheimer's disease brain: tortuous and torturous. Drug News Perspect. 15:549-557.
    • (2002) Drug News Perspect. , vol.15 , pp. 549-557
    • Rohn, T.T.1    Rissman, R.A.2    Head, E.3    Cotman, C.W.4
  • 74
    • 0141960033 scopus 로고    scopus 로고
    • beta-Amyloid induces paired helical filament-like tau filaments in tissue culture
    • Ferrari, A., Hoerndli, F., Baechi, T., Nitsch, R.M., and Gotz, J. 2003. beta-Amyloid induces paired helical filament-like tau filaments in tissue culture. J. Biol. Chem. 278:40162-40168.
    • (2003) J. Biol. Chem. , vol.278 , pp. 40162-40168
    • Ferrari, A.1    Hoerndli, F.2    Baechi, T.3    Nitsch, R.M.4    Gotz, J.5
  • 75
    • 0034730759 scopus 로고    scopus 로고
    • Nonsaturable binding indicates clustering of tau on the microtubule surface in a paired helical filament-like conformation
    • Ackmann, M., Wiech, H., and Mandelkow, E. 2000. Nonsaturable binding indicates clustering of tau on the microtubule surface in a paired helical filament-like conformation. J. Biol. Chem. 275:30335-30343.
    • (2000) J. Biol. Chem. , vol.275 , pp. 30335-30343
    • Ackmann, M.1    Wiech, H.2    Mandelkow, E.3
  • 76
    • 0035067021 scopus 로고    scopus 로고
    • Inhibition of neuronal maturation in primary hippocampal neurons from tau deficient mice
    • Dawson, H.N., et al. 2001. Inhibition of neuronal maturation in primary hippocampal neurons from tau deficient mice. J. Cell Sci. 114:1179-1187.
    • (2001) J. Cell Sci. , vol.114 , pp. 1179-1187
    • Dawson, H.N.1
  • 77
    • 0036135127 scopus 로고    scopus 로고
    • Apolipoprotein E affects the central nervous system response to injury and the development of cerebral edema
    • Lynch, J.R., et al. 2002. Apolipoprotein E affects the central nervous system response to injury and the development of cerebral edema. Ann. Neurol. 51:113-117.
    • (2002) Ann. Neurol. , vol.51 , pp. 113-117
    • Lynch, J.R.1
  • 78
    • 0032988610 scopus 로고    scopus 로고
    • Mild cognitive impairment: Clinical characterization and outcome
    • Petersen, R.C., et al. 1999. Mild cognitive impairment: clinical characterization and outcome. Arch. Neurol. 56:303-308.
    • (1999) Arch. Neurol. , vol.56 , pp. 303-308
    • Petersen, R.C.1
  • 79
    • 0036685608 scopus 로고    scopus 로고
    • Transgenic mouse model of tauopathies with glial pathology and nervous system degeneration
    • Higuchi, M., et al. 2002. Transgenic mouse model of tauopathies with glial pathology and nervous system degeneration. Neuron. 35:433-446.
    • (2002) Neuron , vol.35 , pp. 433-446
    • Higuchi, M.1
  • 80
    • 0034008482 scopus 로고    scopus 로고
    • Ultrastructural evidence of fibrillar beta-amyloid associated with neuronal membranes in behaviorally characterized aged dog brains
    • Torp, R., et al. 2000. Ultrastructural evidence of fibrillar beta-amyloid associated with neuronal membranes in behaviorally characterized aged dog brains. Neuroscience. 96:495-506.
    • (2000) Neuroscience , vol.96 , pp. 495-506
    • Torp, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.