메뉴 건너뛰기




Volumn 856, Issue 1-2, 2000, Pages 163-175

Conformation of paired helical filaments blocks dephosphorylation of epitopes shared with fetal tau except Ser199/202 and Ser202/Thr2055

Author keywords

Alzheimer's disease; Formic acid; Paired helical filament; Phosphatase; Tau protein

Indexed keywords

ALKALINE PHOSPHATASE; EPITOPE; PHOSPHATASE; TAU PROTEIN;

EID: 0033963038     PISSN: 00068993     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-8993(99)02391-4     Document Type: Article
Times cited : (33)

References (65)
  • 3
    • 0027308924 scopus 로고
    • Abnormal tau phosphorylation at Ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding
    • G.T. Bramblett, M. Goedert, R. Jakes, S.E. Merrick, J.Q. Trojanowski, V.M.-Y. Lee, 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.-Y.6
  • 4
    • 12644260802 scopus 로고    scopus 로고
    • The structural basis of monoclonal antibody Alz50s selectivity for Alzheimer's disease pathology
    • G. Carmel, E.M. Mager, L.I. Binder, J. Kuret, The structural basis of monoclonal antibody Alz50s selectivity for Alzheimer's disease pathology, J. Biol. Chem. 271 (1996) 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
  • 5
    • 0017758306 scopus 로고
    • Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly
    • D.W. Cleveland, S.-Y. Hwo, M.W. Kirschner, Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly, J. Mol. Biol. 116 (1977) 227-247.
    • (1977) J. Mol. Biol. , vol.116 , pp. 227-247
    • Cleveland, D.W.1    Hwo, S.-Y.2    Kirschner, M.W.3
  • 6
    • 0024348594 scopus 로고
    • The repeat region of microtubule-associated protein tau forms part of the core of the paired helical filament of Alzheimer's disease
    • T. Crowther, M. Goedert, C.M. Wischik, The repeat region of microtubule-associated protein tau forms part of the core of the paired helical filament of Alzheimer's disease (Review), Ann. Med. 21 (1989) 127-132.
    • (1989) Ann. Med. , vol.21 , pp. 127-132
    • Crowther, T.1    Goedert, M.2    Wischik, C.M.3
  • 7
    • 0028121105 scopus 로고
    • Assembly of Alzheimer-like filaments from full-length tau protein
    • R.A. Crowther, O.F. Olesen, M.J. Smith, R. Jakes, M. Goedert, Assembly of Alzheimer-like filaments from full-length tau protein, FEBS Lett. 337 (1994) 135-138.
    • (1994) FEBS Lett. , vol.337 , pp. 135-138
    • Crowther, R.A.1    Olesen, O.F.2    Smith, M.J.3    Jakes, R.4    Goedert, M.5
  • 8
    • 0027753055 scopus 로고
    • Dephosphorylation of tau protein and Alzheimer paired helical filaments by calcineurin and phosphatase2A
    • G. Drewes, E.-M. Mandelkow, K. Baumann, J. Goris, W. Merlevede, E. Mandelkow, Dephosphorylation of tau protein and Alzheimer paired helical filaments by calcineurin and phosphatase2A, FEBS Lett. 336 (1993) 425-432.
    • (1993) FEBS Lett. , vol.336 , pp. 425-432
    • Drewes, G.1    Mandelkow, E.-M.2    Baumann, K.3    Goris, J.4    Merlevede, W.5    Mandelkow, E.6
  • 11
    • 0027984739 scopus 로고
    • Epitope mapping of monoclonal antibodies to the paired helical filaments of Alzheimer's disease: Identification of phosphorylation sites in tau protein
    • M. Goedert, R. Jakes, R.A. Crowther, P. Cohen, E. Vanmechelen, M. Vandermeeren, P. Cras, 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
  • 12
    • 0028946744 scopus 로고
    • Monoclonal antibody AT8 recognises tau protein phosphorylated at both serine 202 and threonine 205, Neurosci
    • M. Goedert, R. Jakes, E. Vanmechelen, Monoclonal antibody AT8 recognises tau protein phosphorylated at both serine 202 and threonine 205, Neurosci. Lett. 189 (1995) 167-169.
    • (1995) Lett. , vol.189 , pp. 167-169
    • Goedert, M.1    Jakes, R.2    Vanmechelen, E.3
  • 13
    • 0026595846 scopus 로고
    • Tau proteins of Alzheimer paired helical filaments: Abnormal phosphorylation of all six brain isoforms
    • M. Goedert, M.G. Spillantini, N.J. Cairns, R.A. Crowther, 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
  • 14
    • 0024745894 scopus 로고
    • Multiple isoforms of human microtubule-associated protein tau: Sequences and localization in neurofibrillary tangles of Alzheimer's disease
    • M. Goedert, M.G. Spillantini, R. Jakes, D. Rutherford, R.A. Crowther, Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease, Neuron 3 (1989) 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
  • 15
    • 0028064431 scopus 로고
    • Dephosphorylation of Alzheimer's disease abnormally phosphorylated tau by protein phosphatase-2A
    • C.X. Gong, I. Grundke-Iqbal, K. Iqbal, Dephosphorylation of Alzheimer's disease abnormally phosphorylated tau by protein phosphatase-2A, Neuroscience 61 (1994) 765-772.
    • (1994) Neuroscience , vol.61 , pp. 765-772
    • Gong, C.X.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 16
    • 0029113874 scopus 로고
    • Phosphatase activity toward abnormally phosphorylated tau: Decrease in Alzheimer disease brain
    • C.X. Gong, S. Shaikh, J.-Z. Wang, T. Zaidi, I. Grundke-Iqbal, K. Iqbal, Phosphatase activity toward abnormally phosphorylated tau: decrease in Alzheimer disease brain, J. Neurochem. 65 (1995) 732-738.
    • (1995) J. Neurochem. , vol.65 , pp. 732-738
    • Gong, C.X.1    Shaikh, S.2    Wang, J.-Z.3    Zaidi, T.4    Grundke-Iqbal, I.5    Iqbal, K.6
  • 18
    • 0024461007 scopus 로고
    • Tau protein becomes long and stiff upon phosphorylation: Correlation between paracrystalline structure and degree of phosphorylation
    • T. Hagestedt, B. Lichtenberg, H. Wille, E.-M. Mandelkow, E. Mandelkow, Tau protein becomes long and stiff upon phosphorylation: correlation between paracrystalline structure and degree of phosphorylation, J. Cell Biol. 109 (1989) 1643-1651.
    • (1989) J. Cell Biol. , vol.109 , pp. 1643-1651
    • Hagestedt, T.1    Lichtenberg, B.2    Wille, H.3    Mandelkow, E.-M.4    Mandelkow, E.5
  • 19
    • 0031439109 scopus 로고    scopus 로고
    • Alzheimer-like changes in microtubule-associated protein Tau induced by sulfated glycosaminoglycans. Inhibition of microtubule binding, stimulation of phosphorylation, and filament assembly depend on the degree of sulfation
    • M. Hasegawa, R.A. Crowther, R. Jakes, M. Goedert, Alzheimer-like changes in microtubule-associated protein Tau induced by sulfated glycosaminoglycans. Inhibition of microtubule binding, stimulation of phosphorylation, and filament assembly depend on the degree of sulfation, J. Biol. Chem. 272 (1997) 33118-33124.
    • (1997) J. Biol. Chem. , vol.272 , pp. 33118-33124
    • Hasegawa, M.1    Crowther, R.A.2    Jakes, R.3    Goedert, M.4
  • 20
  • 21
    • 0028361538 scopus 로고
    • Alzheimer paired helical filaments. Restoration of the biological activity by dephosphorylation
    • K. Iqbal, T. Zaidi, C. Bancher, I. Grundke-Iqbal, Alzheimer paired helical filaments. Restoration of the biological activity by dephosphorylation, FEBS Lett. 349 (1994) 104-108.
    • (1994) FEBS Lett. , vol.349 , pp. 104-108
    • Iqbal, K.1    Zaidi, T.2    Bancher, C.3    Grundke-Iqbal, I.4
  • 22
    • 0027372016 scopus 로고
    • The extent of phosphorylation of fetal tau is comparable to that of PHF-tau from Alzheimer paired helical filaments
    • A. Kenessey, S.H. Yen, The extent of phosphorylation of fetal tau is comparable to that of PHF-tau from Alzheimer paired helical filaments, Brain Res. 629 (1993) 40-46.
    • (1993) Brain Res. , vol.629 , pp. 40-46
    • Kenessey S.h Yen, A.1
  • 23
    • 0027361281 scopus 로고
    • Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease
    • E. Kopke, Y.C. Tung, S. Shaikh, A.C. Alonso, K. Iqbal, I. Grundke-Iqbal, Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease, J. Biol. Chem. 268 (1993) 24374-24384.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24374-24384
    • Kopke, E.1    Tung, Y.C.2    Shaikh, S.3    Alonso, A.C.4    Iqbal, K.5    Grundke-Iqbal, I.6
  • 25
    • 0023899370 scopus 로고
    • Immunochemical and biochemical characterization of tau proteins in normal and Alzheimer's disease brains with Alz 50 and Tau-1
    • H. Ksiezak-Reding, L.I. Binder, S.-H. Yen, Immunochemical and biochemical characterization of tau proteins in normal and Alzheimer's disease brains with Alz 50 and Tau-1, J. Biol. Chem. 263 (1988) 7948-7953.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7948-7953
    • Ksiezak-Reding, H.1    Binder, L.I.2    Yen, S.-H.3
  • 26
    • 0026676007 scopus 로고
    • Phosphate analysis and dephosphorylation of modified tau associated with paired helical filaments
    • H. Ksiezak-Reding, W.K. Liu, S.H. Yen, Phosphate analysis and dephosphorylation of modified tau associated with paired helical filaments, Brain Res. 597 (1992) 209-212.
    • (1992) Brain Res. , vol.597 , pp. 209-212
    • Ksiezak-Reding, H.1    Liu, W.K.2    Yen, S.H.3
  • 27
    • 0028242639 scopus 로고
    • Tau immunoreactivity and SDS solubility of two populations of paired helical filaments that differ in morphology
    • H. Ksiezak-Reding, K. Morgan, D.W. Dickson, Tau immunoreactivity and SDS solubility of two populations of paired helical filaments that differ in morphology, Brain Res. 649 (1994) 185-196.
    • (1994) Brain Res. , vol.649 , pp. 185-196
    • Ksiezak-Reding, H.1    Morgan, K.2    Dickson, D.W.3
  • 28
    • 0028877178 scopus 로고
    • Binding of Alz 50 depends on Phe8 in tau synthetic peptides and varies between native and denatured tau proteins
    • H. Ksiezak-Reding, R. Leibowitz, R. Bowser, P. Davies, Binding of Alz 50 depends on Phe8 in tau synthetic peptides and varies between native and denatured tau proteins, Brain Res. 697 (1995) 63-75.
    • (1995) Brain Res. , vol.697 , pp. 63-75
    • Ksiezak-Reding, H.1    Leibowitz, R.2    Bowser, R.3    Davies, P.4
  • 29
    • 0028297078 scopus 로고
    • Mass and physical dimensions of two distinct populations of paired helical filaments
    • H. Ksiezak-Reding, J.S. Wall, Mass and physical dimensions of two distinct populations of paired helical filaments, Neurobiol. Aging 15 (1994) 11-19.
    • (1994) Neurobiol. Aging , vol.15 , pp. 11-19
    • Ksiezak-Reding, H.1    Wall, J.S.2
  • 30
    • 0030723127 scopus 로고    scopus 로고
    • Casein kinase 1 is tightly associated with paired helical filaments isolated from Alzheimer's disease brain
    • J. Kuret, G.S. Johnson, D. Cha, E.R. Christenson, A.J. DeMaggio, M.F. Hoekstra, Casein kinase 1 is tightly associated with paired helical filaments isolated from Alzheimer's disease brain, J. Neurochem. 69 (1997) 2506-2515.
    • (1997) J. Neurochem. , vol.69 , pp. 2506-2515
    • Kuret, J.1    Johnson, G.S.2    Cha, D.3    Christenson, E.R.4    DeMaggio, A.J.5    Hoekstra, M.F.6
  • 31
    • 0032555642 scopus 로고    scopus 로고
    • Protein phosphatase 1 is targeted to microtubules by the microtubule-associated protein tau
    • H. Liao, Y. Li, D.L. Brautigan, G.G. Gundersen, Protein phosphatase 1 is targeted to microtubules by the microtubule-associated protein tau, J. Biol. Chem. 273 (1998) 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
  • 32
    • 0023695297 scopus 로고
    • Structure and elasticity of microtubule-associated protein tau
    • B. Lichtenberg, E.-M. Mandelkow, T. Hagestedt, E. Mandelkow, Structure and elasticity of microtubule-associated protein tau, Nature 334 (1988) 359-362.
    • (1988) Nature , vol.334 , pp. 359-362
    • Lichtenberg, B.1    Mandelkow, E.-M.2    Hagestedt, T.3    Mandelkow, E.4
  • 33
    • 0021171445 scopus 로고
    • The purification of tau protein and the occurrence of two phosphorylation states of tau in brain
    • G. Lindwall, R.D. Cole, The purification of tau protein and the occurrence of two phosphorylation states of tau in brain, J. Biol. Chem. 259 (1984) 12241-12245.
    • (1984) J. Biol. Chem. , vol.259 , pp. 12241-12245
    • Lindwall, G.1    Cole, R.D.2
  • 34
    • 0025719441 scopus 로고
    • Abnormal proteins from Alzheimer's disease brain. Purification and amino acid analysis
    • W.-K. Liu, H. Ksiezak-Reding, S.H. Yen, Abnormal proteins from Alzheimer's disease brain. Purification and amino acid analysis, J. Biol. Chem. 266 (1991) 21723-21727.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21723-21727
    • Liu, W.-K.1    Ksiezak-Reding, H.2    Yen, S.H.3
  • 35
    • 0028878537 scopus 로고
    • Detection of a cdc2-related kinase with Alzheimer paired helical filaments
    • W.-K. Liu, R. Williams, F.L. Hall, D.W. Dickson, S.H. Yen, Detection of a cdc2-related kinase with Alzheimer paired helical filaments, Am. J. Pathol. 146 (1995) 228-238.
    • (1995) Am. J. Pathol. , vol.146 , pp. 228-238
    • Liu, W.-K.1    Williams, R.2    Hall, F.L.3    Dickson, D.W.4    Yen, S.H.5
  • 36
    • 0030937952 scopus 로고    scopus 로고
    • The phosphorylation of tau: A critical stage in neurodevelopment and neurodegenerative processes
    • S. Lovestone, C.H. Reynolds, The phosphorylation of tau: a critical stage in neurodevelopment and neurodegenerative processes, Neuroscience 78 (1997) 309-324.
    • (1997) Neuroscience , vol.78 , pp. 309-324
    • Lovestone, S.1    Reynolds, C.H.2
  • 38
    • 0027945346 scopus 로고
    • Biopsy-derived adult human brain tau is phosphorylated at many of the same sites as Alzheimer's disease paired helical filament tau
    • E.S. Matsuo, R.-W. Shin, M.L. Billingsley, A. Van deVoorde, M. O'Connor, J.Q. Trojanowski, V.M.-Y. Lee, Biopsy-derived adult human brain tau is phosphorylated at many of the same sites as Alzheimer's disease paired helical filament tau, Neuron 13 (1994) 989-1002.
    • (1994) Neuron , vol.13 , pp. 989-1002
    • Matsuo, E.S.1    Shin, R.-W.2    Billingsley, M.L.3    Van DeVoorde, A.4    O'Connor, M.5    Trojanowski, J.Q.6    Lee, V.M.-Y.7
  • 39
    • 0029039987 scopus 로고
    • Differential sensitivity to proteolysis by brain calpain of adult human tau, fetal human tau and PHF-tau
    • M. Mercken, F. Grynspan, R.A. Nixon, Differential sensitivity to proteolysis by brain calpain of adult human tau, fetal human tau and PHF-tau, FEBS Lett. 368 (1995) 10-14.
    • (1995) FEBS Lett. , vol.368 , pp. 10-14
    • Mercken, M.1    Grynspan, F.2    Nixon, R.A.3
  • 42
    • 0028593606 scopus 로고
    • Monoclonal antibody PHF-1 recognizes tau protein phosphorylated at serine residues 396-404
    • L. Otvos, L. Feiner, E. Lang, G.I. Szendrei, M. Goedert, V.M.-Y. Lee, Monoclonal antibody PHF-1 recognizes tau protein phosphorylated at serine residues 396-404, J. Neurosci. 39 (1994) 669-673.
    • (1994) J. Neurosci. , vol.39 , pp. 669-673
    • Otvos, L.1    Feiner, L.2    Lang, E.3    Szendrei, G.I.4    Goedert, M.5    Lee, V.M.-Y.6
  • 43
    • 0027978340 scopus 로고
    • Expression of protein phosphatases (PP-1, PP-2A, PP-2B and FTP-1B) and protein kinases (MAP kinase and P34cdc2) in the hippocampus of patients with Alzheimer disease and normal aged individuals
    • J.J. Pei, E. Sersen, K. Iqbal, I. Grundke-Iqbal, Expression of protein phosphatases (PP-1, PP-2A, PP-2B and FTP-1B) and protein kinases (MAP kinase and P34cdc2) in the hippocampus of patients with Alzheimer disease and normal aged individuals, Brain Res. 655 (1994) 70-76.
    • (1994) Brain Res. , vol.655 , pp. 70-76
    • Pei, J.J.1    Sersen, E.2    Iqbal, K.3    Grundke-Iqbal, I.4
  • 44
    • 0031911959 scopus 로고    scopus 로고
    • Subcellular localization of protein phosphatases and abnormally phosphorylated tau in the temporal cortex from Alzheimer's disease and control brains
    • J.J. Pei, C.X. Gong, K. Iqbal, I. Grundke-Iqbal, Q.L. Wu, B. Winblad, R.F. Cowburn, Subcellular localization of protein phosphatases and abnormally phosphorylated tau in the temporal cortex from Alzheimer's disease and control brains, J. Neural Transm. 105 (1998) 69-83.
    • (1998) J. Neural Transm. , vol.105 , pp. 69-83
    • Pei, J.J.1    Gong, C.X.2    Iqbal, K.3    Grundke-Iqbal, I.4    Wu, Q.L.5    Winblad, B.6    Cowburn, R.F.7
  • 45
    • 0032578024 scopus 로고    scopus 로고
    • Accumulation of cyclin-dependent kinase 5 (cdk5) in neurons with early stages of Alzheimer's disease neurofibrillary degeneration
    • J.J. Pei, I. Grundke-Iqbal, K. Iqbal, N. Bogdanovic, B. Winblad, R. F Cowburn, Accumulation of cyclin-dependent kinase 5 (cdk5) in neurons with early stages of Alzheimer's disease neurofibrillary degeneration, Brain Res. 797 (1998) 267-277.
    • (1998) Brain Res. , vol.797 , pp. 267-277
    • Pei, J.J.1    Grundke-Iqbal, I.2    Iqbal, K.3    Bogdanovic, N.4    Winblad, B.5    Cowburn, R.F.6
  • 46
    • 0026696360 scopus 로고
    • Mitogen-activated protein kinases: Versatile transducers for cell signaling (Review)
    • S.L. Pelech, J.S. Sanghera, Mitogen-activated protein kinases: versatile transducers for cell signaling (Review), Trends Biochem. Sci. 17 (1992) 233-238.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 233-238
    • Pelech, S.L.1    Sanghera, J.S.2
  • 47
    • 77956917564 scopus 로고
    • E. coli alkaline phosphatase
    • P.D. Boyer (Ed.), Academic Press, Orlando
    • T.W. Reid, I.B. Wilson, E. coli alkaline phosphatase, in: P.D. Boyer (Ed.), The Ezymes, Vol. 4, Academic Press, Orlando, (1971) 373-415.
    • (1971) The Ezymes , vol.4 , pp. 373-415
    • Reid, T.W.1    Wilson, I.B.2
  • 48
    • 0030022195 scopus 로고    scopus 로고
    • Quantitative image analysis of temporal changes in tau and neurofilament proteins during the course of acute experimental neurofibrillary degeneration; non-phosphorylated epitopes precede phosphorylation
    • J. Savory, Y. Huang, M.M. Herman, M.R. Wills, Quantitative image analysis of temporal changes in tau and neurofilament proteins during the course of acute experimental neurofibrillary degeneration; non-phosphorylated epitopes precede phosphorylation, Brain Res. 707 (1996) 272-281.
    • (1996) Brain Res. , vol.707 , pp. 272-281
    • Savory, J.1    Huang, Y.2    Herman, M.M.3    Wills, M.R.4
  • 49
    • 0033596946 scopus 로고    scopus 로고
    • Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments
    • A. Schneider, J. Biernat, M. von Bergen, E. Mandelkow, E.M. Mandelkow, Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments, Biochemistry 38 (1999) 3549-3558.
    • (1999) Biochemistry , vol.38 , pp. 3549-3558
    • Schneider, A.1    Biernat, J.2    Von Bergen, M.3    Mandelkow, E.4    Mandelkow, E.M.5
  • 50
    • 0028170411 scopus 로고
    • Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for β-structure
    • O. Schweers, E. Schonbrunn-Hanebeck, A. Marx, E. Mandelkow, Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for β-structure, J. Biol. Chem. 269 (1994) 24290-24297.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24290-24297
    • Schweers, O.1    Schonbrunn-Hanebeck, E.2    Marx, A.3    Mandelkow, E.4
  • 52
    • 0030461275 scopus 로고    scopus 로고
    • Regulation of the phosphorylation state and microtubule-binding activity of tau by protein phosphatase 2A
    • E. Sontag, V. Nunbhakdi-Craig, G. Lee, G.S. Bloom, M.C. Mumby, Regulation of the phosphorylation state and microtubule-binding activity of tau by protein phosphatase 2A, Neuron 17 (1996) 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
  • 53
    • 0033520355 scopus 로고    scopus 로고
    • Molecular interactions among protein phosphatase 2A, tau, and microtubules. Implications for the regulation of tau phosphorylation and the development of tauopathies
    • E. Sontag, V. Nunbhakdi-Craig, G. Lee, R. Brandt, C. Kamibayashi, J. Kuret, C.L. White, M.C. Mumby, G.S. Bloom, Molecular interactions among protein phosphatase 2A, tau, and microtubules. Implications for the regulation of tau phosphorylation and the development of tauopathies, J. Biol. Chem. 274 (1999) 25490-25498.
    • (1999) J. Biol. Chem. , vol.274 , pp. 25490-25498
    • Sontag, E.1    Nunbhakdi-Craig, V.2    Lee, G.3    Brandt, R.4    Kamibayashi, C.5    Kuret, J.6    White, C.L.7    Mumby, M.C.8    Bloom, G.S.9
  • 54
    • 0029569152 scopus 로고
    • Phosphorylation of paired helical filament tau in Alzheimer's disease neurofibrillary lesions: Focusing on phosphatases
    • J.Q. Trojanowski, V.M.-Y. Lee, Phosphorylation of paired helical filament tau in Alzheimer's disease neurofibrillary lesions: focusing on phosphatases, FASEB J. 9 (1995) 1570-1576.
    • (1995) FASEB J. , vol.9 , pp. 1570-1576
    • Trojanowski, J.Q.1    Lee, V.M.-Y.2
  • 55
    • 0027284385 scopus 로고
    • Localization of the mitogen activated protein kinase ERK2 in Alzheimer's disease neurofibrillary tangles and senile plaque neuntes
    • J.Q. Trojanowski, M. Mawal-Dewan, M.L. Schmidt, J. Martin, V.M.-Y. Lee, Localization of the mitogen activated protein kinase ERK2 in Alzheimer's disease neurofibrillary tangles and senile plaque neuntes, Brain Res. 618 (1993) 333-337.
    • (1993) Brain Res. , vol.618 , pp. 333-337
    • Trojanowski, J.Q.1    Mawal-Dewan, M.2    Schmidt, M.L.3    Martin, J.4    Lee, V.M.-Y.5
  • 56
    • 0026521716 scopus 로고
    • A protein kinase associated with paired helical filaments in Alzheimer's disease
    • I. Vincent, P. Davies, A protein kinase associated with paired helical filaments in Alzheimer's disease, Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 2878-2882.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 2878-2882
    • Vincent, I.1    Davies, P.2
  • 57
    • 0031006939 scopus 로고    scopus 로고
    • Aberrant expression of mitotic cdc2/cyclin B1 kinase in degenerating neurons of Alzheimer's disease brain
    • I. Vincent, G. Jicha, M. Rosado, D.W. Dickson, Aberrant expression of mitotic cdc2/cyclin B1 kinase in degenerating neurons of Alzheimer's disease brain, J. Neurosci. 17 (1997) 3588-3598.
    • (1997) J. Neurosci. , vol.17 , pp. 3588-3598
    • Vincent, I.1    Jicha, G.2    Rosado, M.3    Dickson, D.W.4
  • 58
    • 0031685160 scopus 로고    scopus 로고
    • Mitotic phosphoepitopes precede paired helical filaments in Alzheimer's disease
    • I. Vincent, J.H. Zheng, D.W. Dickson, Y. Kress, P. Davies, Mitotic phosphoepitopes precede paired helical filaments in Alzheimer's disease, Neurobiol. Aging 19 (1998) 287-296.
    • (1998) Neurobiol. Aging , vol.19 , pp. 287-296
    • Vincent, I.1    Zheng, J.H.2    Dickson, D.W.3    Kress, Y.4    Davies, P.5
  • 59
    • 0028902487 scopus 로고
    • Dephosphorylation of Alzheimer paired helical filaments by protein phosphatase-2A and -2B
    • J.Z. Wang, C.X. Gong, T. Zaidi, I. Grundke-Iqbal, K. Iqbal, Dephosphorylation of Alzheimer paired helical filaments by protein phosphatase-2A and -2B, J. Biol. Chem. 270 (1995) 4854-4860.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4854-4860
    • Wang, J.Z.1    Gong, C.X.2    Zaidi, T.3    Grundke-Iqbal, I.4    Iqbal, K.5
  • 60
    • 0029995590 scopus 로고    scopus 로고
    • Restoration of biological activity of Alzheimer abnormally phosphorylated tau by dephospho-rylation with protein phosphatase-2A, -2B and -1
    • J.Z. Wang, I. Grundke-Iqbal, K. Iqbal, Restoration of biological activity of Alzheimer abnormally phosphorylated tau by dephospho-rylation with protein phosphatase-2A, -2B and -1, Brain Res. Mol. Brain Res. 38 (1996) 200-208.
    • (1996) Brain Res. Mol. Brain Res. , vol.38 , pp. 200-208
    • Wang, J.Z.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 61
    • 0029416987 scopus 로고
    • Dephosphorylation of fetal tau and paired helical filaments-tau by protein phosphatases 1 and 2A and calcineurin
    • H. Yamamoto, M. Hasegawa, T. Ono, K. Tashima, Y. Ihara, E. Miyamoto, Dephosphorylation of fetal tau and paired helical filaments-tau by protein phosphatases 1 and 2A and calcineurin, J. Biochem. 118 (1995) 1224-1231.
    • (1995) J. Biochem. , vol.118 , pp. 1224-1231
    • Yamamoto, H.1    Hasegawa, M.2    Ono, T.3    Tashima, K.4    Ihara, Y.5    Miyamoto, E.6
  • 62
    • 0028785672 scopus 로고
    • Calpain-induced proteolysis of normal human tau and tau associated with paired helical filaments
    • L.-S. Yang, H. Ksiezak-Reding, Calpain-induced proteolysis of normal human tau and tau associated with paired helical filaments, Eur. J. Biochem. 233 (1995) 9-17.
    • (1995) Eur. J. Biochem. , vol.233 , pp. 9-17
    • Yang, L.-S.1    Ksiezak-Reding, H.2
  • 63
    • 0030923581 scopus 로고    scopus 로고
    • Tau released from paired helical filaments with formic acid or guanidine is susceptible to calpain-mediated proteolysis
    • L.-S. Yang, W. Gordon-Krajcer, H. Ksiezak-Reding, Tau released from paired helical filaments with formic acid or guanidine is susceptible to calpain-mediated proteolysis, J. Neurochem. 69 (1997) 1548-1558.
    • (1997) J. Neurochem. , vol.69 , pp. 1548-1558
    • Yang, L.-S.1    Gordon-Krajcer, W.2    Ksiezak-Reding, H.3
  • 64
    • 0027237861 scopus 로고
    • Tau in paired helical filaments is functionally distinct from fetal tau: Assembly incompetence of paired helical filament-tau
    • H. Yoshida, Y. Ihara, 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
  • 65
    • 0032521599 scopus 로고    scopus 로고
    • Sequential phosphorylation of Tau by glycogen synthase kinase-3beta and protein kinase a at Thr212 and Ser214 generates the Alzheimer-specific epitope of antibody AT100 and requires a paired-helical-filament-like conformation
    • Q. Zheng-Fischhofer, J. Biernat, E.-M. Mandelkow, S. Illenberger, R. Godemann, E. Mandelkow, Sequential phosphorylation of Tau by glycogen synthase kinase-3beta and protein kinase A at Thr212 and Ser214 generates the Alzheimer-specific epitope of antibody AT100 and requires a paired-helical-filament-like conformation, Eur. J. Biochem. 252 (1998) 542-552.
    • (1998) Eur. J. Biochem. , vol.252 , pp. 542-552
    • Zheng-Fischhofer, Q.1    Biernat, J.2    Mandelkow, E.-M.3    Illenberger, S.4    Godemann, R.5    Mandelkow, E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.