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Volumn 22, Issue 7, 2008, Pages 2357-2367

Tau isoform expression and regulation in human cortical neurons

Author keywords

Alzheimer; Cytoskeleton; Phosphatase; Phosphorylation; Tauopathy

Indexed keywords

LAMININ; PHOSPHATASE; TAU PROTEIN;

EID: 46749151737     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fj.07-096909     Document Type: Article
Times cited : (34)

References (70)
  • 2
    • 0028123071 scopus 로고
    • Alzheimer's disease: A central role for amyloid
    • Selkoe, D. J. (1994) Alzheimer's disease: a central role for amyloid. J. Neuropathol. Exp. Neurol. 53, 438-447
    • (1994) J. Neuropathol. Exp. Neurol , vol.53 , pp. 438-447
    • Selkoe, D.J.1
  • 3
    • 0025753852 scopus 로고
    • The molecular pathology of Alzheimer's disease
    • Selkoe, D. J. (1991) The molecular pathology of Alzheimer's disease. Neuron 6, 487-498
    • (1991) Neuron , vol.6 , pp. 487-498
    • Selkoe, D.J.1
  • 4
    • 0003374626 scopus 로고    scopus 로고
    • Tau protein pathology in neurodegenerative diseases
    • Spillantini, M. G., and Goedert, M. (1998) Tau protein pathology in neurodegenerative diseases. Trends Neurosci. 21, 428-433
    • (1998) Trends Neurosci , vol.21 , pp. 428-433
    • Spillantini, M.G.1    Goedert, M.2
  • 5
    • 0032191105 scopus 로고    scopus 로고
    • Filamentous nerve cell inclusions in neurodegenerative diseases
    • Goedert, M., Spillantini, M. G., and Davies, S. W. (1998) Filamentous nerve cell inclusions in neurodegenerative diseases. Current Opin. Neurobiol. 8, 619-632
    • (1998) Current Opin. Neurobiol , vol.8 , pp. 619-632
    • Goedert, M.1    Spillantini, M.G.2    Davies, S.W.3
  • 7
    • 84880185976 scopus 로고    scopus 로고
    • Discoveries of tau, abnormally hyperphosphorylated tau and others of neurofibrillary degeneration: A personal historical perspective
    • Iqbal, K., and Grundke-Iqbal, I. (2006) Discoveries of tau, abnormally hyperphosphorylated tau and others of neurofibrillary degeneration: a personal historical perspective. J. Alzheimers Dis. 9, 219-242
    • (2006) J. Alzheimers Dis , vol.9 , pp. 219-242
    • Iqbal, K.1    Grundke-Iqbal, I.2
  • 8
    • 0034509448 scopus 로고    scopus 로고
    • A very incomplete comprehensive theory of Alzheimer's disease
    • Davies, P. (2000) A very incomplete comprehensive theory of Alzheimer's disease. Ann. N. Y. Acad. Sci. 924, 8-16
    • (2000) Ann. N. Y. Acad. Sci , vol.924 , pp. 8-16
    • Davies, P.1
  • 9
    • 0009364134 scopus 로고
    • Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease
    • Kosik, K. S., Joachim, C. L., and Selkoe, D. J. (1986) Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease. Proc. Natl. Acad. Sci. U. S. A. 83, 4044-4048
    • (1986) Proc. Natl. Acad. Sci. U. S. A , vol.83 , pp. 4044-4048
    • Kosik, K.S.1    Joachim, C.L.2    Selkoe, D.J.3
  • 10
    • 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
  • 11
    • 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., and Crowther, R. A. (1989) 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, 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
  • 12
    • 0022397025 scopus 로고
    • Microtubule-associated proteins and in vitro astrocyte differentiation
    • Couchie, D., Fages, C., Bridoux, A. M., Rolland, B., Tardy, M., and Nunez, J. (1985) Microtubule-associated proteins and in vitro astrocyte differentiation. J. Cell Biol. 101, 2095-2103
    • (1985) J. Cell Biol , vol.101 , pp. 2095-2103
    • Couchie, D.1    Fages, C.2    Bridoux, A.M.3    Rolland, B.4    Tardy, M.5    Nunez, J.6
  • 13
    • 0022360337 scopus 로고
    • Cultured neurons contain a variety of microtubule-associated proteins
    • Peng, I., Binder, L. I., and Black, M. M. (1985) Cultured neurons contain a variety of microtubule-associated proteins. Brain Res. 361, 200-211
    • (1985) Brain Res , vol.361 , pp. 200-211
    • Peng, I.1    Binder, L.I.2    Black, M.M.3
  • 14
    • 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, 15-19
    • (1998) Trends Neurosci , vol.21 , pp. 15-19
    • Neve, R.L.1    Robakis, N.K.2
  • 15
    • 0033850407 scopus 로고    scopus 로고
    • Tau protein isoforms, phosphorylation and role in neurodegenerative disorders
    • Buee, L., Bussiere, T., Buee-Scherrer, V., Delacourte, A., and Hof, P. R. (2000) Tau protein isoforms, phosphorylation and role in neurodegenerative disorders. Brain Res. 33, 95-130
    • (2000) Brain Res , vol.33 , pp. 95-130
    • Buee, L.1    Bussiere, T.2    Buee-Scherrer, V.3    Delacourte, A.4    Hof, P.R.5
  • 16
    • 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., Kurnit, 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, 271-280
    • (1986) Brain Res , vol.387 , pp. 271-280
    • Neve, R.L.1    Harris, P.2    Kosik, K.S.3    Kurnit, D.M.4    Donlon, T.A.5
  • 17
    • 0002792366 scopus 로고
    • Cloning and sequencing 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 sequencing 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. U. S. A. 85, 4051-4055
    • (1988) Proc. Natl. Acad. Sci. U. S. A , vol.85 , pp. 4051-4055
    • Goedert, M.1    Wischik, C.M.2    Crowther, R.A.3    Walker, J.E.4    Klug, A.5
  • 18
    • 0026488111 scopus 로고
    • Structure and novel exons of the human tau gene
    • Andreadis, A., Brown, W. M., and Kosik, K. S. (1992) Structure and novel exons of the human tau gene. Biochemistry 31, 10626-10633
    • (1992) Biochemistry , vol.31 , pp. 10626-10633
    • Andreadis, A.1    Brown, W.M.2    Kosik, K.S.3
  • 19
    • 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, 519-526
    • (1989) Neuron , vol.3 , pp. 519-526
    • Goedert, M.1    Spillantini, M.G.2    Jakes, R.3    Rutherford, D.4    Crowther, R.A.5
  • 20
    • 0025600995 scopus 로고
    • Expression of separate isoforms of human tau protein: Correlation with the tau pattern in brain and effects on tubulin polymerization
    • Goedert, M., and Jakes, R. (1990) Expression of separate isoforms of human tau protein: correlation with the tau pattern in brain and effects on tubulin polymerization. EMBO J. 9, 4225-4230
    • (1990) EMBO J , vol.9 , pp. 4225-4230
    • Goedert, M.1    Jakes, R.2
  • 22
    • 0024641959 scopus 로고
    • Developmentally regulated expression of specific tau sequences
    • Kosik, K. S., Orecchio, L. D., Bakalis, S., and Neve, R. L. (1989) Developmentally regulated expression of specific tau sequences. Neuron 2, 1389-1397
    • (1989) Neuron , vol.2 , pp. 1389-1397
    • Kosik, K.S.1    Orecchio, L.D.2    Bakalis, S.3    Neve, R.L.4
  • 23
    • 0034624014 scopus 로고    scopus 로고
    • Structural and functional differences between 3-repeat and 4-repeat tau isoforms. Implications for normal tau function and the onset of neurodegenetative disease
    • Goode, B. L., Chau, M., Denis, P. E., and Feinstein, S. C. (2000) Structural and functional differences between 3-repeat and 4-repeat tau isoforms. Implications for normal tau function and the onset of neurodegenetative disease. J. Biol. Chem. 275, 38182-38189
    • (2000) J. Biol. Chem , vol.275 , pp. 38182-38189
    • Goode, B.L.1    Chau, M.2    Denis, P.E.3    Feinstein, S.C.4
  • 24
    • 12344323961 scopus 로고    scopus 로고
    • Tau phosphorylation in neuronal cell function and dysfunction
    • Johnson, G. V., and Stoothoff, W. H. (2004) Tau phosphorylation in neuronal cell function and dysfunction. J. Cell Sci. 117, 5721-5729
    • (2004) J. Cell Sci , vol.117 , pp. 5721-5729
    • Johnson, G.V.1    Stoothoff, W.H.2
  • 25
    • 10944227282 scopus 로고    scopus 로고
    • Tau phosphorylation: Physiological and pathological consequences
    • Stoothoff, W. H., and Johnson, G. V. (2005) Tau phosphorylation: physiological and pathological consequences. Biochim. Biophys. Acta 1739, 280-297
    • (2005) Biochim. Biophys. Acta , vol.1739 , pp. 280-297
    • Stoothoff, W.H.1    Johnson, G.V.2
  • 26
    • 0032938625 scopus 로고    scopus 로고
    • Assembly of paired helical filaments from mouse tau: Implications for the neurofibrillary pathology in transgenic mouse models for Alzheimer's disease
    • Kampers, T., Pangalos, M., Geerts, H., Wiech, H., and Mandelkow, E. (1999) Assembly of paired helical filaments from mouse tau: implications for the neurofibrillary pathology in transgenic mouse models for Alzheimer's disease. FEBS Lett. 451, 39-44
    • (1999) FEBS Lett , vol.451 , pp. 39-44
    • Kampers, T.1    Pangalos, M.2    Geerts, H.3    Wiech, H.4    Mandelkow, E.5
  • 27
    • 0034089887 scopus 로고    scopus 로고
    • Human tau filaments induce microtubule and synapse loss in an in vivo model of neurofibrillary degenerative disease
    • Hall, G. F., Chu, B., Lee, G., and Yao, J. (2000) Human tau filaments induce microtubule and synapse loss in an in vivo model of neurofibrillary degenerative disease. J. Cell Sci. 113, 1373-1387
    • (2000) J. Cell Sci , vol.113 , pp. 1373-1387
    • Hall, G.F.1    Chu, B.2    Lee, G.3    Yao, J.4
  • 28
    • 0028879127 scopus 로고
    • Tau isoform expression and phosphorylation state during differentiation of cultured neuronal cells
    • Smith, C. J., Anderton, B. H., Davis, D. R., and Gallo, J. M. (1995) Tau isoform expression and phosphorylation state during differentiation of cultured neuronal cells. FEBS Lett. 375, 243-248
    • (1995) FEBS Lett , vol.375 , pp. 243-248
    • Smith, C.J.1    Anderton, B.H.2    Davis, D.R.3    Gallo, J.M.4
  • 29
    • 33745268224 scopus 로고    scopus 로고
    • Different conformations of amyloid beta induce neurotoxicity by distinct mechanisms in human cortical neurons
    • Deshpande, A., Mina, E., Glabe, C., and Busciglio, J. (2006) Different conformations of amyloid beta induce neurotoxicity by distinct mechanisms in human cortical neurons. J. Neurosci. 26, 6011-6018
    • (2006) J. Neurosci , vol.26 , pp. 6011-6018
    • Deshpande, A.1    Mina, E.2    Glabe, C.3    Busciglio, J.4
  • 32
    • 15244350098 scopus 로고    scopus 로고
    • Increased frequency of argyrophilic grain disease in Alzheimer disease with 4R tau-specific immunohistochemistry
    • Fujino, Y., Wang, D. S., Thomas, N., Espinoza, M., Davies, P., and Dickson, D. W. (2005) Increased frequency of argyrophilic grain disease in Alzheimer disease with 4R tau-specific immunohistochemistry. J. Neuropathol. Exp. Neurol. 64, 209-214
    • (2005) J. Neuropathol. Exp. Neurol , vol.64 , pp. 209-214
    • Fujino, Y.1    Wang, D.S.2    Thomas, N.3    Espinoza, M.4    Davies, P.5    Dickson, D.W.6
  • 34
    • 0037439642 scopus 로고    scopus 로고
    • Aberrant activation of focal adhesion proteins mediates fibrillar amyloid beta-induced neuronal dystrophy
    • Grace, E. A., and Busciglio, J. (2003) Aberrant activation of focal adhesion proteins mediates fibrillar amyloid beta-induced neuronal dystrophy. J. Neurosci. 23, 493-502
    • (2003) J. Neurosci , vol.23 , pp. 493-502
    • Grace, E.A.1    Busciglio, J.2
  • 35
    • 0037103844 scopus 로고    scopus 로고
    • Expression patterns of tau mRNA isoforms correlate with susceptible lesions in progressive supranuclear palsy and corticobasal degeneration
    • Takanashi, M., Mori, H., Arima, K., Mizuno, Y., and Hattori, N. (2002) Expression patterns of tau mRNA isoforms correlate with susceptible lesions in progressive supranuclear palsy and corticobasal degeneration. Brain Res. Mol. Brain Res. 104, 210-219
    • (2002) Brain Res. Mol. Brain Res , vol.104 , pp. 210-219
    • Takanashi, M.1    Mori, H.2    Arima, K.3    Mizuno, Y.4    Hattori, N.5
  • 37
    • 0035851175 scopus 로고    scopus 로고
    • Reduced protein phosphatase 2A activity induces hyperphosphorylation and altered compartmentalization of tau in transgenic mice
    • Kins, S., Crameri, A., Evans, D. R., Hemmings, B. A., Nitsch, R. M., and Gotz, J. (2001) Reduced protein phosphatase 2A activity induces hyperphosphorylation and altered compartmentalization of tau in transgenic mice. J. Biol. Chem. 276, 38193-38200
    • (2001) J. Biol. Chem , vol.276 , pp. 38193-38200
    • Kins, S.1    Crameri, A.2    Evans, D.R.3    Hemmings, B.A.4    Nitsch, R.M.5    Gotz, J.6
  • 38
    • 0027217027 scopus 로고
    • Cantharidin, another natural toxin that inhibits the activity of serine/threonine protein phosphatases types 1 and 2A
    • Honkanen, R. E. (1993) Cantharidin, another natural toxin that inhibits the activity of serine/threonine protein phosphatases types 1 and 2A. FEBS Lett. 330, 283-286
    • (1993) FEBS Lett , vol.330 , pp. 283-286
    • Honkanen, R.E.1
  • 39
    • 22844451947 scopus 로고    scopus 로고
    • Optically active cantharidin analogues possessing selective inhibitory activity on Ser/Thr protein phosphatase 2B (calcineurin): Implications for the binding mode
    • Baba, Y., Hirukawa, N., and Sodeoka, M. (2005) Optically active cantharidin analogues possessing selective inhibitory activity on Ser/Thr protein phosphatase 2B (calcineurin): implications for the binding mode. Bioorg. Med. Chem. 13, 5164-5170
    • (2005) Bioorg. Med. Chem , vol.13 , pp. 5164-5170
    • Baba, Y.1    Hirukawa, N.2    Sodeoka, M.3
  • 40
    • 0027519717 scopus 로고
    • Protein phosphatase 2A and its [3H]cantharidin/[3H]endothall thioanhydride binding site. Inhibitor specificity of cantharidin and ATP analogues
    • Li, Y. M., Mackintosh, C., and Casida, J. E. (1993) Protein phosphatase 2A and its [3H]cantharidin/[3H]endothall thioanhydride binding site. Inhibitor specificity of cantharidin and ATP analogues. Biochem. Pharmacol. 46, 1435-1443
    • (1993) Biochem. Pharmacol , vol.46 , pp. 1435-1443
    • Li, Y.M.1    Mackintosh, C.2    Casida, J.E.3
  • 41
    • 4544337913 scopus 로고    scopus 로고
    • A CaMKII/calcineurin switch controls the direction of Ca(2+)-dependent growth cone guidance
    • Wen, Z., Guirland, C., Ming, G. L., and Zheng, J. Q. (2004) A CaMKII/calcineurin switch controls the direction of Ca(2+)-dependent growth cone guidance. Neuron 43, 835-846
    • (2004) Neuron , vol.43 , pp. 835-846
    • Wen, Z.1    Guirland, C.2    Ming, G.L.3    Zheng, J.Q.4
  • 42
    • 0026574179 scopus 로고
    • Specific inhibition of calcineurin by type II synthetic pyrethroid insecticides
    • Enan, E., and Matsumura, F. (1992) Specific inhibition of calcineurin by type II synthetic pyrethroid insecticides. Biochem. Pharmacol. 43, 1777-1784
    • (1992) Biochem. Pharmacol , vol.43 , pp. 1777-1784
    • Enan, E.1    Matsumura, F.2
  • 43
    • 0023905661 scopus 로고
    • The establishment of polarity by hippocampal neurons in culture
    • Dotti, C. G., Sullivan, C. A., and Banker, G. A. (1988) The establishment of polarity by hippocampal neurons in culture. J. Neurosci. 8, 1454-1468
    • (1988) J. Neurosci , vol.8 , pp. 1454-1468
    • Dotti, C.G.1    Sullivan, C.A.2    Banker, G.A.3
  • 44
    • 0030051269 scopus 로고    scopus 로고
    • MAP-1B/TAU functional redundancy during laminin-enhanced axonal growth
    • DiTella, M. C., Feiguin, F., Carri, N., Kosik, K. S., and Caceres, A. (1996) MAP-1B/TAU functional redundancy during laminin-enhanced axonal growth. J. Cell Sci. 109, 467-477
    • (1996) J. Cell Sci , vol.109 , pp. 467-477
    • DiTella, M.C.1    Feiguin, F.2    Carri, N.3    Kosik, K.S.4    Caceres, A.5
  • 45
    • 0033549267 scopus 로고    scopus 로고
    • Tangled areas of Alzheimer brain have upregulated levels of exon 10 containing tau mRNA
    • Yasojima, K., McGeer, E. G., and McGeer, P. L. (1999) Tangled areas of Alzheimer brain have upregulated levels of exon 10 containing tau mRNA. Brain Res. 831, 301-305
    • (1999) Brain Res , vol.831 , pp. 301-305
    • Yasojima, K.1    McGeer, E.G.2    McGeer, P.L.3
  • 46
    • 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. (1994) The phosphorylation state of tau in the developing rat brain is regulated by phosphoprotein phosphatases. J. Biol. Chem. 269, 30981-30987
    • (1994) J. Biol. Chem , vol.269 , pp. 30981-30987
    • Mawal-Dewan, M.1    Henley, J.2    Van de Voorde, A.3    Trojanowski, J.Q.4    Lee, V.M.5
  • 47
    • 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, 1201-1207
    • (1996) Neuron , vol.17 , pp. 1201-1207
    • Sontag, E.1    Nunbhakdi-Craig, V.2    Lee, G.3    Bloom, G.S.4    Mumby, M.C.5
  • 48
    • 0031913730 scopus 로고    scopus 로고
    • Activation of a PP2A-like phosphatase and dephosphorylation of tau protein characterize onset of the execution phase of apoptosis
    • Mills, J. C., Lee, V. M., and Pittman, R. N. (1998) Activation of a PP2A-like phosphatase and dephosphorylation of tau protein characterize onset of the execution phase of apoptosis. J. Cell Sci. 111, 625-636
    • (1998) J. Cell Sci , vol.111 , pp. 625-636
    • Mills, J.C.1    Lee, V.M.2    Pittman, R.N.3
  • 49
    • 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. (2001) PP2A mRNA expression is quantitatively decreased in Alzheimer's disease hippocampus. Exp. Neurol. 168, 402-412
    • (2001) Exp. Neurol , vol.168 , pp. 402-412
    • Vogelsberg-Ragaglia, V.1    Schuck, T.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 50
    • 0028986916 scopus 로고
    • β-Amyloid fibrils induce tau phosphorylation and loss of microtubule binding
    • Busciglio, J., Lorenzo, A., Yeh, J., and Yankner, B. A. (1995) β-Amyloid fibrils induce tau phosphorylation and loss of microtubule binding. Neuron 14, 879-888
    • (1995) Neuron , vol.14 , pp. 879-888
    • Busciglio, J.1    Lorenzo, A.2    Yeh, J.3    Yankner, B.A.4
  • 51
    • 27644478606 scopus 로고    scopus 로고
    • Contributions of protein phosphatases PP1, PP2A, PP2B, and PP5 to the regulation of tau phosphorylation
    • Liu, F., Grundke-Iqbal, I., Iqbal, K., and Gong, C. X. (2005) Contributions of protein phosphatases PP1, PP2A, PP2B, and PP5 to the regulation of tau phosphorylation. Euro. J. Neurosci. 22, 1942-1950
    • (2005) Euro. J. Neurosci , vol.22 , pp. 1942-1950
    • Liu, F.1    Grundke-Iqbal, I.2    Iqbal, K.3    Gong, C.X.4
  • 52
    • 0027984739 scopus 로고
    • Epitope mapping of monoclonal antibodies to the paired helical filaments of Alzheimer's disease: Identification of phosphorylation sites in tau protein
    • Goedert, M., Jakes, R., Crowther, R. A., Cohen, P., Vanmechelen, E., Vandermeeren, M., and Cras, P. (1994) Epitope mapping of monoclonal antibodies to the paired helical filaments of Alzheimer's disease: identification of phosphorylation sites in tau protein. Biochem. J. 301, 871-877
    • (1994) Biochem. J , vol.301 , pp. 871-877
    • Goedert, M.1    Jakes, R.2    Crowther, R.A.3    Cohen, P.4    Vanmechelen, E.5    Vandermeeren, M.6    Cras, P.7
  • 53
    • 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. U. S. A. 87, 5827-5831
    • (1990) Proc. Natl. Acad. Sci. U. S. A , vol.87 , pp. 5827-5831
    • Greenberg, S.G.1    Davies, P.2
  • 54
    • 0036937699 scopus 로고    scopus 로고
    • Specific tau phosphorylation sites correlate with severity of neuronal cytopathology in Alzheimer's disease
    • Augustinack, J. C., Schneider, A., Mandelkow, E. M., and Hyman, B. T. (2002) Specific tau phosphorylation sites correlate with severity of neuronal cytopathology in Alzheimer's disease. Acta Neuropathol. (Berl.) 103, 26-35
    • (2002) Acta Neuropathol. (Berl.) , vol.103 , pp. 26-35
    • Augustinack, J.C.1    Schneider, A.2    Mandelkow, E.M.3    Hyman, B.T.4
  • 55
    • 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
  • 57
    • 0041355331 scopus 로고    scopus 로고
    • Microtubule-dependent oligomerization of tau. Implications for physiological tau function and tauopathies
    • Makrides, V., Shen, T. E., Bhatia, R., Smith, B. L., Thimm, J., Lal, R., and Feinstein, S. C. (2003) Microtubule-dependent oligomerization of tau. Implications for physiological tau function and tauopathies. J. Biol. Chem. 278, 33298-33304
    • (2003) J. Biol. Chem , vol.278 , pp. 33298-33304
    • Makrides, V.1    Shen, T.E.2    Bhatia, R.3    Smith, B.L.4    Thimm, J.5    Lal, R.6    Feinstein, S.C.7
  • 58
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., and Glabe, C. G. (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300, 486-489
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6    Glabe, C.G.7
  • 60
    • 0035823577 scopus 로고    scopus 로고
    • Functional differences of tau isoforms containing 3 or 4 C-terminal repeat regions and the influence of oxidative stress
    • Utton, M. A., Gibb, G. M., Burdett, I. D., Anderton, B. H., and Vandecandelaere, A. (2001) Functional differences of tau isoforms containing 3 or 4 C-terminal repeat regions and the influence of oxidative stress. J. Biol. Chem. 276, 34288-34297
    • (2001) J. Biol. Chem , vol.276 , pp. 34288-34297
    • Utton, M.A.1    Gibb, G.M.2    Burdett, I.D.3    Anderton, B.H.4    Vandecandelaere, A.5
  • 61
    • 17144409371 scopus 로고    scopus 로고
    • Three- and four-repeat tau regulate the dynamic instability of two distinct microtubule subpopulations in qualitatively different manners. Implications for neurodegeneration
    • Levy, S. F., Leboeuf, A. C., Massie, M. R., Jordan, M. A., Wilson, L., and Feinstein, S. C. (2005) Three- and four-repeat tau regulate the dynamic instability of two distinct microtubule subpopulations in qualitatively different manners. Implications for neurodegeneration. J. Biol. Chem. 280, 13520-13528
    • (2005) J. Biol. Chem , vol.280 , pp. 13520-13528
    • Levy, S.F.1    Leboeuf, A.C.2    Massie, M.R.3    Jordan, M.A.4    Wilson, L.5    Feinstein, S.C.6
  • 63
    • 46749138015 scopus 로고    scopus 로고
    • Treat abnormal hyperphosphorylation and not aggregation of tau
    • Alonso, A., Li, B., Grundke, I., and Iqbal K. (2006) Treat abnormal hyperphosphorylation and not aggregation of tau. Alzheimers Dementia 2, S29-S30
    • (2006) Alzheimers Dementia , vol.2
    • Alonso, A.1    Li, B.2    Grundke, I.3    Iqbal, K.4
  • 64
    • 33947307791 scopus 로고    scopus 로고
    • Missorting of tau in neurons causes degeneration of synapses that can be rescued by the kinase MARK2/Par-1
    • Thies, E., and Mandelkow, E. M. (2007) Missorting of tau in neurons causes degeneration of synapses that can be rescued by the kinase MARK2/Par-1. J. Neurosci. 27, 2896-2907
    • (2007) J. Neurosci , vol.27 , pp. 2896-2907
    • Thies, E.1    Mandelkow, E.M.2
  • 65
    • 0032543684 scopus 로고    scopus 로고
    • Hutton, M, Lendon, C. L, Rizzu, P, Baker, M, Froelich, S, Houlden, H, Pickering-Brown, S, Chakraverty, S, Isaacs, A, Grover, A, Hackett, J, Adamson, J, Lincoln, S, Dickson, D, Davies, P, Petersen, R. C, Stevens, M, de Graaff, E, Wauters, E, van Baren, J, Hillebrand, M, Joosse, M, Kwon, J. M, Nowotny, P, Che, L. K, Norton, J, Morris, J. C, Reed, L. A, Trojanowski, J, Basun, H, Lannfelt, L, Neystat, M, Fahn, S, Dark, F, Tannenberg, T, Dodd, P. R, Hayward, N, Kwok, J. B, Schofield, P. R, Andreadis, A, Snowden, J, Craufurd, D, Neary, D, Owen, F, Oostra, B. A, Hardy, J, Goate, A, van Swieten, J, Mann, D, Lynch, T, and Heutink, P, 1998 Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17. Nature 393, 702-705
    • Hutton, M., Lendon, C. L., Rizzu, P., Baker, M., Froelich, S., Houlden, H., Pickering-Brown, S., Chakraverty, S., Isaacs, A., Grover, A., Hackett, J., Adamson, J., Lincoln, S., Dickson, D., Davies, P., Petersen, R. C., Stevens, M., de Graaff, E., Wauters, E., van Baren, J., Hillebrand, M., Joosse, M., Kwon, J. M., Nowotny, P., Che, L. K., Norton, J., Morris, J. C., Reed, L. A., Trojanowski, J., Basun, H., Lannfelt, L., Neystat, M., Fahn, S., Dark, F., Tannenberg, T., Dodd, P. R., Hayward, N., Kwok, J. B., Schofield, P. R., Andreadis, A., Snowden, J., Craufurd, D., Neary, D., Owen, F., Oostra, B. A., Hardy, J., Goate, A., van Swieten, J., Mann, D., Lynch, T., and Heutink, P. (1998) Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17. Nature 393, 702-705
  • 66
    • 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., Bird, T. D., and Schellenberg, G. D. (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. U. S. A. 96, 5598-5603
    • (1999) Proc. Natl. Acad. Sci. U. S. A , vol.96 , pp. 5598-5603
    • D'Souza, I.1    Poorkaj, P.2    Hong, M.3    Nochlin, D.4    Lee, V.M.5    Bird, T.D.6    Schellenberg, G.D.7
  • 67
    • 0033591225 scopus 로고    scopus 로고
    • 5′- splice site mutations in tau associated with the inherited dementia FTDP-17 affect a stem-loop structure that regulates alternative splicing of exon 10
    • Grover, A., Houlden, H., Baker, M., Adamson, J., Lewis, J., Prihar, G., Pickering-Brown, S., Duff, K., and Hutton, M. (1999) 5′- splice site mutations in tau associated with the inherited dementia FTDP-17 affect a stem-loop structure that regulates alternative splicing of exon 10. J. Biol. Chem. 274, 15134-15143
    • (1999) J. Biol. Chem , vol.274 , pp. 15134-15143
    • Grover, A.1    Houlden, H.2    Baker, M.3    Adamson, J.4    Lewis, J.5    Prihar, G.6    Pickering-Brown, S.7    Duff, K.8    Hutton, M.9
  • 68
    • 0026784416 scopus 로고
    • p42 MAP kinase phosphorylation sites in microtubule-associated protein tau are dephosphorylated by protein phosphatase 2A1. Implications for Alzheimer's disease [corrected]
    • Goedert, M., Cohen, E. S., Jakes, R., and Cohen, P. (1992) p42 MAP kinase phosphorylation sites in microtubule-associated protein tau are dephosphorylated by protein phosphatase 2A1. Implications for Alzheimer's disease [corrected]. FEBS Lett. 312, 95-99
    • (1992) FEBS Lett , vol.312 , pp. 95-99
    • Goedert, M.1    Cohen, E.S.2    Jakes, R.3    Cohen, P.4
  • 69
    • 0028885494 scopus 로고
    • Protein phosphatase 2A is the major enzyme in brain that dephosphorylates tau protein phosphorylated by proline-directed protein kinases or cyclic AMP-dependent protein kinase
    • Goedert, M., Jakes, R., Qi, Z., Wang, J. H., and Cohen, P. (1995) Protein phosphatase 2A is the major enzyme in brain that dephosphorylates tau protein phosphorylated by proline-directed protein kinases or cyclic AMP-dependent protein kinase. J. Neurochem. 65, 2804-2807
    • (1995) J. Neurochem , vol.65 , pp. 2804-2807
    • Goedert, M.1    Jakes, R.2    Qi, Z.3    Wang, J.H.4    Cohen, P.5
  • 70
    • 0032555642 scopus 로고    scopus 로고
    • Protein phosphatase 1 is targeted to microtubules by the microtubule-associated protein Tau
    • Liao, H., Li, Y., Brautigan, D. L., and Gundersen, G. G. (1998) Protein phosphatase 1 is targeted to microtubules by the microtubule-associated protein Tau. J. Biol. Chem. 273, 21901-21908
    • (1998) J. Biol. Chem , vol.273 , pp. 21901-21908
    • Liao, H.1    Li, Y.2    Brautigan, D.L.3    Gundersen, G.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.