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Volumn 90, Issue 4, 2004, Pages 829-838

Phosphorylated p38MAPK specific antibodies cross-react with sarkosyl-insoluble hyperphosphorylated tau proteins

Author keywords

Active p38 mitogen activated protein kinase; Cross reactivity; Sarkosyl insoluble tau; Tauopathies

Indexed keywords

ANTIBODY; BRAIN EXTRACT; MITOGEN ACTIVATED PROTEIN KINASE P38; TAU PROTEIN;

EID: 4143121059     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2004.02558.x     Document Type: Article
Times cited : (13)

References (55)
  • 1
    • 0036850725 scopus 로고    scopus 로고
    • Abundant tau filaments and nonapoptotic neurodegeneration in transgenic mice expressing human P301S tau protein
    • Allen B., Ingram E., Takao M. et al. (2002) Abundant tau filaments and nonapoptotic neurodegeneration in transgenic mice expressing human P301S tau protein. J. Neurosci. 2, 9340-9351.
    • (2002) J. Neurosci. , vol.2 , pp. 9340-9351
    • Allen, B.1    Ingram, E.2    Takao, M.3
  • 3
    • 0030458524 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3 alteration in Alzheimer's disease is related to neurofibrillary tangle formation
    • Baum L., Hansen L., Masliah E. and Saitoh T. (1996) Glycogen synthase kinase 3 alteration in Alzheimer's disease is related to neurofibrillary tangle formation. Mol. Chem. Neuropathol. 29, 253-261.
    • (1996) Mol. Chem. Neuropathol. , vol.29 , pp. 253-261
    • Baum, L.1    Hansen, L.2    Masliah, E.3    Saitoh, T.4
  • 5
    • 0037181485 scopus 로고    scopus 로고
    • Phosphorylation of microtubule-associated protein tau by stress-activated protein kinases in intact cells
    • Buee-Scherrer V. and Goedert M. (2002) Phosphorylation of microtubule-associated protein tau by stress-activated protein kinases in intact cells. FEBS Lett. 515, 151-154.
    • (2002) FEBS Lett. , vol.515 , pp. 151-154
    • Buee-Scherrer, V.1    Goedert, M.2
  • 6
    • 0033758105 scopus 로고    scopus 로고
    • Microtubule-affinity-regulating kinase (MARK) is tightly associated with neurofibrillary tangles in Alzheimer brain: A fluorescence resonance energy transfer study
    • Chin J. Y., Knowles R. B., Schneider A., Drewes G., Mandelkow E. M. and Hyman B. T. (2000) Microtubule-affinity-regulating kinase (MARK) is tightly associated with neurofibrillary tangles in Alzheimer brain: a fluorescence resonance energy transfer study. J. Neuropathol. Exp. Neurol. 1, 966-971.
    • (2000) J. Neuropathol. Exp. Neurol. , vol.1 , pp. 966-971
    • Chin, J.Y.1    Knowles, R.B.2    Schneider, A.3    Drewes, G.4    Mandelkow, E.M.5    Hyman, B.T.6
  • 7
    • 0345405447 scopus 로고    scopus 로고
    • Aberrant Cdk5 Activation by p25 triggers pathological events leading to neurodegeneration and neurofibrillary tangles
    • Cruz J. C., Tseng H.-C., Goldman J. A., Shih H. and Tsai L.-H. (2003) Aberrant Cdk5 Activation by p25 triggers pathological events leading to neurodegeneration and neurofibrillary tangles. Neuron 40, 471-483.
    • (2003) Neuron , vol.40 , pp. 471-483
    • Cruz, J.C.1    Tseng, H.-C.2    Goldman, J.A.3    Shih, H.4    Tsai, L.-H.5
  • 8
    • 0022239478 scopus 로고
    • Monoclonal antibodies to Alzheimer neurofibrillary tangles. 2. Demonstration of a common antigenic determinant between ANT and neurofibrillary degeneration in progressive supranuclear palsy
    • Dickson D. W., Kress Y., Crowe A. and Yen S.-H. (1985) Monoclonal antibodies to Alzheimer neurofibrillary tangles. 2. Demonstration of a common antigenic determinant between ANT and neurofibrillary degeneration in progressive supranuclear palsy. Am. J. Pathol. 120, 292-303.
    • (1985) Am. J. Pathol. , vol.120 , pp. 292-303
    • Dickson, D.W.1    Kress, Y.2    Crowe, A.3    Yen, S.-H.4
  • 9
    • 0035094403 scopus 로고    scopus 로고
    • Phosphorylated map kinase (ERK1, ERK2) expression is associated with early tau deposition in neurons and glial cells, but not with increased nuclear DNA vulnerability and cell death, in Alzheimer's disease, Pick's disease, progressive supranuclear palsy, and corticobasal degeneration
    • Ferrer I., Blanco R., Carmona M. et al. (2001a) Phosphorylated map kinase (ERK1, ERK2) expression is associated with early tau deposition in neurons and glial cells, but not with increased nuclear DNA vulnerability and cell death, in Alzheimer's disease, Pick's disease, progressive supranuclear palsy, and corticobasal degeneration. Brain Pathol. 11, 144-158.
    • (2001) Brain Pathol. , vol.11 , pp. 144-158
    • Ferrer, I.1    Blanco, R.2    Carmona, M.3
  • 10
    • 0035659377 scopus 로고    scopus 로고
    • Phosphorylated mitogen-activated protein kinase (MAPK/ERK-P), protein kinase of 38 kDa (p38-P), stress-activated protein kinase (SAPK/JNK-P), and calcium/calmodulin-dependent kinase II (CaM kinase II) are differentially expressed in tau deposits in neurons and glial cells in tauopathies
    • Ferrer I., Blanco R., Carmona M. and Puig B. (2001b) Phosphorylated mitogen-activated protein kinase (MAPK/ERK-P), protein kinase of 38 kDa (p38-P), stress-activated protein kinase (SAPK/JNK-P), and calcium/calmodulin-dependent kinase II (CaM kinase II) are differentially expressed in tau deposits in neurons and glial cells in tauopathies. J. Neural Transmission 108, 1397-1415.
    • (2001) J. Neural Transmission , vol.108 , pp. 1397-1415
    • Ferrer, I.1    Blanco, R.2    Carmona, M.3    Puig, B.4
  • 11
    • 0037246583 scopus 로고    scopus 로고
    • Phosphorylated protein kinases associated with neuronal and glial tau deposits in argyrophilic grain disease
    • Ferrer I., Barrachina M., Tolnay M., Rey M. J., Vidal N., Carmona M., Blanco R. and Puig B. (2003) Phosphorylated protein kinases associated with neuronal and glial tau deposits in argyrophilic grain disease. Brain Pathol. 13, 62-78.
    • (2003) Brain Pathol. , vol.13 , pp. 62-78
    • Ferrer, I.1    Barrachina, M.2    Tolnay, M.3    Rey, M.J.4    Vidal, N.5    Carmona, M.6    Blanco, R.7    Puig, B.8
  • 12
    • 0032516493 scopus 로고    scopus 로고
    • Rapid assembly of Alzheimer-like paired helical filaments from microtubule-associated protein tau monitored by fluorescence in solution
    • Friedhoff P., Schneider A., Mandelkow E. M. and Mandelkow E. (1998) Rapid assembly of Alzheimer-like paired helical filaments from microtubule-associated protein tau monitored by fluorescence in solution. Biochemistry. 37, 10223-10230.
    • (1998) Biochemistry , vol.37 , pp. 10223-10230
    • Friedhoff, P.1    Schneider, A.2    Mandelkow, E.M.3    Mandelkow, E.4
  • 13
    • 0036434880 scopus 로고    scopus 로고
    • Tau conformational changes correspond to impairments of episodic memory in mild cognitive impairment and Alzheimer's disease
    • Ghoshal N., Garcia-Sierra F., Wuu J., Leurgans S., Bennet D. A., Berry R. W. and Binder L. I. (2002) Tau conformational changes correspond to impairments of episodic memory in mild cognitive impairment and Alzheimer's disease. Exp. Neurol. 177, 475-493.
    • (2002) Exp. Neurol. , vol.177 , pp. 475-493
    • Ghoshal, N.1    Garcia-Sierra, F.2    Wuu, J.3    Leurgans, S.4    Bennet, D.A.5    Berry, R.W.6    Binder, L.I.7
  • 14
    • 0029907548 scopus 로고    scopus 로고
    • Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans
    • Goedert M., Jakes R., Spillantini M., Hasegawa M., Smith M. J. and Crowther R. A. (1996) Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans. Nature 383, 550-553.
    • (1996) Nature , vol.383 , pp. 550-553
    • Goedert, M.1    Jakes, R.2    Spillantini, M.3    Hasegawa, M.4    Smith, M.J.5    Crowther, R.A.6
  • 15
    • 0030963035 scopus 로고    scopus 로고
    • Phosphorylation of microtubule-associated protein tau by stress-activated protein kinases
    • Goedert M., Hasegawa M., Jakes R., Lawler S., Cuenda A. and and- Cohen P. (1997) Phosphorylation of microtubule-associated protein tau by stress-activated protein kinases. FEBS Lett. 409, 57-62.
    • (1997) FEBS Lett. , vol.409 , pp. 57-62
    • Goedert, M.1    Hasegawa, M.2    Jakes, R.3    Lawler, S.4    Cuenda, A.5    Cohen, P.6
  • 17
    • 0033043939 scopus 로고    scopus 로고
    • p38 kinase is activated in the Alzheimer's disease brain
    • Hensley K., Floyd R. A., Zheng N.-Y. et al. (1999) p38 kinase is activated in the Alzheimer's disease brain. J. Neurochem. 72, 2053-2058.
    • (1999) J. Neurochem. , vol.72 , pp. 2053-2058
    • Hensley, K.1    Floyd, R.A.2    Zheng, N.-Y.3
  • 18
    • 17044461433 scopus 로고    scopus 로고
    • The endogenous and cell cycle-dependent phosphorylation of tau protein in living cells: Implications for Alzheimer's disease
    • Illenberger S., Zheng-Fischhofer Q., Preuss U. et al. (1998) The endogenous and cell cycle-dependent phosphorylation of tau protein in living cells: implications for Alzheimer's disease. Mol Biol. Cell 9, 1495-1512.
    • (1998) Mol Biol. Cell , vol.9 , pp. 1495-1512
    • Illenberger, S.1    Zheng-Fischhofer, Q.2    Preuss, U.3
  • 19
    • 0029618170 scopus 로고
    • Analysis of phosphorylation of tau with antibodies specific for phosphorylation sites
    • Ishiguro K., Sato K., Takamatsu M., Park J., Uchida T. and Imahori K. (1995) Analysis of phosphorylation of tau with antibodies specific for phosphorylation sites. Neurosci. Lett. 202, 81-84.
    • (1995) Neurosci. Lett. , vol.202 , pp. 81-84
    • Ishiguro, K.1    Sato, K.2    Takamatsu, M.3    Park, J.4    Uchida, T.5    Imahori, K.6
  • 20
    • 0042425738 scopus 로고    scopus 로고
    • Co-localzation of glycogen synthase kinase-3 with neurofibrillary tangles and granulovacuolar degeneration in transgenic mice
    • Ishizawa T., Sahara N., Ishiguro K., Kersh J., McGowan E., Lewis J., Hutton M., Dickson D. W. and Yen S.-H. (2003) Co-localzation of glycogen synthase kinase-3 with neurofibrillary tangles and granulovacuolar degeneration in transgenic mice. Am. J. Pathol. 163, 1057-1067.
    • (2003) Am. J. Pathol. , vol.163 , pp. 1057-1067
    • Ishizawa, T.1    Sahara, N.2    Ishiguro, K.3    Kersh, J.4    McGowan, E.5    Lewis, J.6    Hutton, M.7    Dickson, D.W.8    Yen, S.-H.9
  • 21
    • 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
  • 22
    • 0030590911 scopus 로고    scopus 로고
    • RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments
    • Kampers T., Friedhoff P., Biemat J., Mandelkow E. E. and Mandelkow E. (1996) RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments. FEBS Lett. 399, 344-349.
    • (1996) FEBS Lett. , vol.399 , pp. 344-349
    • Kampers, T.1    Friedhoff, P.2    Biemat, J.3    Mandelkow, E.E.4    Mandelkow, E.5
  • 23
    • 0030774852 scopus 로고    scopus 로고
    • Degradation of tau by lysosomal enzyme cathepsin D: Implication for Alzheimer neurofibrillary degeneration
    • Kenessey A., Nacharaju P., Ko L. and Yen S.-H. (1997) Degradation of tau by lysosomal enzyme cathepsin D: implication for Alzheimer neurofibrillary degeneration. J. Neurochem. 69, 2026-2038.
    • (1997) J. Neurochem. , vol.69 , pp. 2026-2038
    • Kenessey, A.1    Nacharaju, P.2    Ko, L.3    Yen, S.-H.4
  • 24
    • 0344505849 scopus 로고    scopus 로고
    • Tau interacts with src-family non-receptor tyrosine kinases
    • Lee G., Newman S. T., Gard D. L., Band H. and Panchamoorthy G. (1998) Tau interacts with src-family non-receptor tyrosine kinases. J. Cell Sci. 111, 3167-3177.
    • (1998) J. Cell Sci. , vol.111 , pp. 3167-3177
    • Lee, G.1    Newman, S.T.2    Gard, D.L.3    Band, H.4    Panchamoorthy, G.5
  • 25
    • 12144288564 scopus 로고    scopus 로고
    • Phosphorylation of tau by Fyn: Implication for Alzheimer's disease
    • Lee G., Thangavel R., Sharma V. M. et al. (2004) Phosphorylation of tau by Fyn: Implication for Alzheimer's disease. J. Neurosci. 24, 2304-2312.
    • (2004) J. Neurosci. , vol.24 , pp. 2304-2312
    • Lee, G.1    Thangavel, R.2    Sharma, V.M.3
  • 27
    • 0034426011 scopus 로고    scopus 로고
    • Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein
    • Lewis J., McGowan E., Rockwood J. et al. (2000) Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein. Nat. Genet. 25, 402-405.
    • (2000) Nat. Genet. , vol.25 , pp. 402-405
    • Lewis, J.1    McGowan, E.2    Rockwood, J.3
  • 28
    • 17944382037 scopus 로고    scopus 로고
    • Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP
    • Lewis J., Dickson D. W., Lin W. L. 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    Dickson, D.W.2    Lin, W.L.3
  • 29
    • 0028878537 scopus 로고
    • Detection of a Cdc2-related kinase associated with Alzheimer paired helical filaments
    • Liu W. K., Williams R. T., Hall F. L., Dickson D. W. and Yen S.-H. (1995) Detection of a Cdc2-related kinase associated with Alzheimer paired helical filaments. Am. J. Pathol. 146, 228-238.
    • (1995) Am. J. Pathol. , vol.146 , pp. 228-238
    • Liu, W.K.1    Williams, R.T.2    Hall, F.L.3    Dickson, D.W.4    Yen, S.-H.5
  • 30
    • 0038689162 scopus 로고    scopus 로고
    • Cdk5 is a key factor in tau aggregation and tangle formation in vivo
    • Noble W., Olm V., Takata K. et al. (2003) Cdk5 is a key factor in tau aggregation and tangle formation in vivo. Neuron 38, 555-565.
    • (2003) Neuron , vol.38 , pp. 555-565
    • Noble, W.1    Olm, V.2    Takata, K.3
  • 32
    • 0032850599 scopus 로고    scopus 로고
    • Distribution of active glycogen synthase kinase 3β (GSK-3β) in brains' staged for Alzheimer's disease neurofibrillary changes
    • Pei J. J., Braak E., Braak H., Grundke-Iqbal I., Iqbal K., Winblad B. and Cowburn R. F. (1999) Distribution of active glycogen synthase kinase 3β (GSK-3β) in brains' staged for Alzheimer's disease neurofibrillary changes. J. Neuropathol. Exp. Neurol. 58, 1010-1019.
    • (1999) J. Neuropathol. Exp. Neurol. , vol.58 , pp. 1010-1019
    • Pei, J.J.1    Braak, E.2    Braak, H.3    Grundke-Iqbal, I.4    Iqbal, K.5    Winblad, B.6    Cowburn, R.F.7
  • 33
    • 0035087703 scopus 로고    scopus 로고
    • Localization of active forms of C-jun kinase (JNK) and p38 kinase in Alzheimer's disease brains at different stages of neurofibrillary degeneration
    • Pei J. J., Braak E., Braak H., Grundke-Iqbal I., Iqbal K., Winblad B. and Cowburn R. F. (2001) Localization of active forms of C-jun kinase (JNK) and p38 kinase in Alzheimer's disease brains at different stages of neurofibrillary degeneration. J. Alzheimer's Disease 3, 41-48.
    • (2001) J. Alzheimer's Disease , vol.3 , pp. 41-48
    • Pei, J.J.1    Braak, E.2    Braak, H.3    Grundke-Iqbal, I.4    Iqbal, K.5    Winblad, B.6    Cowburn, R.F.7
  • 34
    • 0029796168 scopus 로고    scopus 로고
    • Polymerization of tau into filaments in the presence of heparin: The minimal sequence required for tau-tau interaction
    • Perez M., Valpuesta J. M., Medina M., Montejo de Garcini E. and Avila J. (1996) Polymerization of tau into filaments in the presence of heparin: the minimal sequence required for tau-tau interaction. J. Neurochem. 67, 1183-1190.
    • (1996) J. Neurochem. , vol.67 , pp. 1183-1190
    • Perez, M.1    Valpuesta, J.M.2    Medina, M.3    Montejo De Garcini, E.4    Avila, J.5
  • 35
    • 0036660263 scopus 로고    scopus 로고
    • Role of GSK-3β in Alzheimer's disease pathology
    • Planel E. and Sun X. and. Takashima A. (2002) Role of GSK-3β in Alzheimer's disease pathology. Drug Dev Res. 56, 491-510.
    • (2002) Drug Dev. Res. , vol.56 , pp. 491-510
    • Planel, E.1    Sun, X.2    Takashima, A.3
  • 36
    • 0034067992 scopus 로고    scopus 로고
    • Phosphorylation sites on tau identified by nanoelectrospray mass sprectroscopy: Differences in vitro between the mitogen-activated protein kinases ERK2, c-Jun N-terminal kinase and P38, and glycogen synthase kinase 3β
    • Reynolds C. H., Betts J. C., Blackstock W. P., Nebreda A. R. and Adnerton B. H. (2000) Phosphorylation sites on tau identified by nanoelectrospray mass sprectroscopy: differences in vitro between the mitogen-activated protein kinases ERK2, c-Jun N-terminal kinase and P38, and glycogen synthase kinase 3β. J. Neurochem. 74, 1587-1595.
    • (2000) J. Neurochem. , vol.74 , pp. 1587-1595
    • Reynolds, C.H.1    Betts, J.C.2    Blackstock, W.P.3    Nebreda, A.R.4    Adnerton, B.H.5
  • 37
    • 0036904519 scopus 로고    scopus 로고
    • Assembly of tau in transgenic animals expressing P301L tau: Alteration of phosphorylation and solubility
    • Sahara N., Lewis J., DeTure M., McGowan E., Dickson D. W., Hutton M. and Yen S.-H. (2002) Assembly of tau in transgenic animals expressing P301L tau: alteration of phosphorylation and solubility. J. Neurochem. 83, 1498-1508.
    • (2002) J. Neurochem. , vol.83 , pp. 1498-1508
    • Sahara, N.1    Lewis, J.2    DeTure, M.3    McGowan, E.4    Dickson, D.W.5    Hutton, M.6    Yen, S.-H.7
  • 38
    • 0036580703 scopus 로고    scopus 로고
    • Activation of c-Jun N-terminal kinase and p38 in an Alzheimer's disease model is associated with amyloid deposition
    • Savage M. J., Lin Y. G., Ciallebella J. R., Flood D. G. and Scott R. W. (2002) Activation of c-Jun N-terminal kinase and p38 in an Alzheimer's disease model is associated with amyloid deposition. J. Neurosci. 22, 3376-3385.
    • (2002) J. Neurosci. , vol.22 , pp. 3376-3385
    • Savage, M.J.1    Lin, Y.G.2    Ciallebella, J.R.3    Flood, D.G.4    Scott, R.W.5
  • 39
    • 0033596946 scopus 로고    scopus 로고
    • Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments
    • Schneider A., Biernat J., von Bergen M., Mandelkow E. and Mandelkow E. M. (1999) Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments. Biochemistry 38, 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
  • 40
    • 0034622242 scopus 로고    scopus 로고
    • Casein kinase I delta is associated with pathological accumulation of tau in several neurodegenerative diseases
    • Schwab C., DeMaggio A. J., Ghoshal N., Binder L. I., Kuret J. and McGeer P. L. (2000) Casein kinase I delta is associated with pathological accumulation of tau in several neurodegenerative diseases. Neurobiol. Aging 21, 503-510.
    • (2000) Neurobiol. Aging , vol.21 , pp. 503-510
    • Schwab, C.1    DeMaggio, A.J.2    Ghoshal, N.3    Binder, L.I.4    Kuret, J.5    McGeer, P.L.6
  • 41
    • 0031727983 scopus 로고    scopus 로고
    • Ser-262 in human recombinant tau protein is a markedly more favorable site for phosphorylation by CaMKII than PKA or PhK
    • Sironi J. J., Yen S.-H., Gondal J. A., Wu O., Grundke-Iqbal I. and Iqbal K. (1998) Ser-262 in human recombinant tau protein is a markedly more favorable site for phosphorylation by CaMKII than PKA or PhK. FEBS Lett. 436, 471-475.
    • (1998) FEBS Lett. , vol.436 , pp. 471-475
    • Sironi, J.J.1    Yen, S.-H.2    Gondal, J.A.3    Wu, O.4    Grundke-Iqbal, I.5    Iqbal, K.6
  • 42
    • 0036193799 scopus 로고    scopus 로고
    • Comparative analysis of an improved thioflavin-S stain, Gallyas silver stain, and immunohistochemistry for neurofibrillary tangle demonstration on the same sections
    • Sun A., Nguyen X. V. and Bing G. (2002) Comparative analysis of an improved thioflavin-S stain, Gallyas silver stain, and immunohistochemistry for neurofibrillary tangle demonstration on the same sections. J. Histochem. Cytochem. 50, 463-472.
    • (2002) J. Histochem. Cytochem. , vol.50 , pp. 463-472
    • Sun, A.1    Nguyen, X.V.2    Bing, G.3
  • 43
    • 0141672049 scopus 로고    scopus 로고
    • p38 MAP kinase is activated at early stages in Alzheimer's disease brain
    • Sun A., Liu M., Nguyen X. V. and Bing G. (2003) p38 MAP kinase is activated at early stages in Alzheimer's disease brain. Exp. Neurol. 183, 394-405.
    • (2003) Exp. Neurol. , vol.183 , pp. 394-405
    • Sun, A.1    Liu, M.2    Nguyen, X.V.3    Bing, G.4
  • 44
    • 0035971151 scopus 로고    scopus 로고
    • Phosphorylation of tau is regulated by PKN
    • Taniguchi T., Kawamata T., Mukai H. et al. (2001) Phosphorylation of tau is regulated by PKN. J. Biol. Chem. 276, 10025-10031.
    • (2001) J. Biol. Chem. , vol.276 , pp. 10025-10031
    • Taniguchi, T.1    Kawamata, T.2    Mukai, H.3
  • 46
    • 0034741928 scopus 로고    scopus 로고
    • Brain Aβ amyloidosis in APPsw mice induces accumulation of presenilin-1 and tau
    • Tomidokoro Y., Harigaya Y., Matsubara E. et al. (2001) Brain Aβ amyloidosis in APPsw mice induces accumulation of presenilin-1 and tau. J. Pathol. 194, 500-506.
    • (2001) J. Pathol. , vol.194 , pp. 500-506
    • Tomidokoro, Y.1    Harigaya, Y.2    Matsubara, E.3
  • 47
    • 0038383029 scopus 로고    scopus 로고
    • Persistent activation of p38 mitogen-activated protein kinase in a mouse model of familial amyotrophic lateral sclerosis correlates with disease progression
    • Tortarolo M., Veglianese P., Calvaresi N., Botturi A., Rossi C., Giorgini A., Migheli A. and Bendotti C. (2003) Persistent activation of p38 mitogen-activated protein kinase in a mouse model of familial amyotrophic lateral sclerosis correlates with disease progression. Mol. Cell Neurosci. 23, 180-192.
    • (2003) Mol. Cell Neurosci. , vol.23 , pp. 180-192
    • Tortarolo, M.1    Veglianese, P.2    Calvaresi, N.3    Botturi, A.4    Rossi, C.5    Giorgini, A.6    Migheli, A.7    Bendotti, C.8
  • 48
    • 0031006939 scopus 로고    scopus 로고
    • Aberrant expression of mitotic cdc2/cyclin B1 kinase in degenerating neurons of Alzheimer's disease brain
    • Vincent I., Jicha G. and Rosado M. and. Dickson D. W. (1997) Aberrant expression of mitotic cdc2/cyclin B1 kinase in degenerating neurons of Alzheimer's disease brain. J. Neurosci. 17, 3588-3598.
    • (1997) J. Neurosci. , vol.17 , pp. 3588-3598
    • Vincent, I.1    Jicha, G.2    Rosado, M.3    Dickson, D.W.4
  • 49
    • 0036138048 scopus 로고    scopus 로고
    • Rapid tyrosine phosphorylation of neuronal proteins including tau and focal adhesion kinase in response to amyloid-β peptide exposure: Involvement of Src family protein kinases
    • Willamson R., Scales T., Clark B. R. et al. (2002) Rapid tyrosine phosphorylation of neuronal proteins including tau and focal adhesion kinase in response to amyloid-β peptide exposure: involvement of Src family protein kinases. J. Neurosci. 22, 10-20.
    • (2002) J. Neurosci. , vol.22 , pp. 10-20
    • Willamson, R.1    Scales, T.2    Clark, B.R.3
  • 50
    • 0030923223 scopus 로고    scopus 로고
    • Free fatty acids stimulate the polymerization of tau and amyloid β peptides. In vitro evidence for a common effector of pathogenesis in Alzheimer's disease
    • Wilson D. M. and Binder L. I. (1997) Free fatty acids stimulate the polymerization of tau and amyloid β peptides. In vitro evidence for a common effector of pathogenesis in Alzheimer's disease. Am. J. Pathol. 150, 2181-2195.
    • (1997) Am. J. Pathol. , vol.150 , pp. 2181-2195
    • Wilson, D.M.1    Binder, L.I.2
  • 51
    • 0029737421 scopus 로고    scopus 로고
    • Preferential labeling of Alzheimer neurofibrillary tangles with antisera for tau protein kinase (TPK) I/glycogen synthase kinase-3β and cyclin-dependent kinase 5, a component of TPK II
    • Yamaguchi H., Ishiguro K., Uchida T., Takashima A. and Lemere C. A. and. Imahori K. (1996) Preferential labeling of Alzheimer neurofibrillary tangles with antisera for tau protein kinase (TPK) I/glycogen synthase kinase-3β and cyclin-dependent kinase 5, a component of TPK II. Acta Neuropathol. 1, 232-241.
    • (1996) Acta Neuropathol. , vol.1 , pp. 232-241
    • Yamaguchi, H.1    Ishiguro, K.2    Uchida, T.3    Takashima, A.4    Lemere, C.A.5    Imahori, K.6
  • 52
    • 0028170044 scopus 로고
    • Protein kinase FA/glycogen synthase kinase-3 α after heparin potentiation phosphorylates tau on sites abnormally phosphorylated in Alzheimer's disease brain
    • Yang S. D. Yu J. S., Shiah S. G. and Huang J. J. (1994) Protein kinase FA/glycogen synthase kinase-3 α after heparin potentiation phosphorylates tau on sites abnormally phosphorylated in Alzheimer's disease brain. J. Neurochem. 63, 1416-1425.
    • (1994) J. Neurochem. , vol.63 , pp. 1416-1425
    • Yang, S.D.1    Yu, J.S.2    Shiah, S.G.3    Huang, J.J.4
  • 53
    • 0022200969 scopus 로고
    • Monoclonal antibodies to Alzheimer neurofibrillary tangles. 1. Identification of polypeptides
    • Yen S.-H., Crowe A. and Dickson D. W. (1985) Monoclonal antibodies to Alzheimer neurofibrillary tangles. 1. Identification of polypeptides. Am. J. Pathol. 120, 282-291.
    • (1985) Am. J. Pathol. , vol.120 , pp. 282-291
    • Yen, S.-H.1    Crowe, A.2    Dickson, D.W.3
  • 54
    • 0033782845 scopus 로고    scopus 로고
    • Activation of p38 kinase links tau phosphorylation, oxidative stress, and cell cycle-related events in Alzheimer's disease
    • Zhu X., Rottkamp C. A., Boux H., Takeda A., Perry G. and Smith M. A. (2000) Activation of p38 kinase links tau phosphorylation, oxidative stress, and cell cycle-related events in Alzheimer's disease. J. Neutopathol. Exp. Neurol. 59, 880-888.
    • (2000) J. Neutopathol. Exp. Neurol. , vol.59 , pp. 880-888
    • Zhu, X.1    Rottkamp, C.A.2    Boux, H.3    Takeda, A.4    Perry, G.5    Smith, M.A.6
  • 55
    • 0035142804 scopus 로고    scopus 로고
    • Activation and redistribution of c-jun N-terminal kinase/stress activated protein kinase in degenerating neurons in Alzheimer's disease
    • Zhu X., Raina A. K., Rottkamp C. A., Aliev G., Perry G., Boux H. and Smith M. A. (2001) Activation and redistribution of c-jun N-terminal kinase/stress activated protein kinase in degenerating neurons in Alzheimer's disease. J. Neurochem. 76, 435-441.
    • (2001) J. Neurochem. , vol.76 , pp. 435-441
    • Zhu, X.1    Raina, A.K.2    Rottkamp, C.A.3    Aliev, G.4    Perry, G.5    Boux, H.6    Smith, M.A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.