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Volumn 69, Issue 1, 1997, Pages 191-198

Reactivating kinase/p38 phosphorylates τ protein in vitro

Author keywords

Alzheimer; Inflammation; p38; Paired helical filaments; Phosphorylation; Reactivating kinase; Stress;

Indexed keywords

MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN KINASE; TAU PROTEIN;

EID: 0030918416     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1997.69010191.x     Document Type: Article
Times cited : (145)

References (69)
  • 1
    • 0027757042 scopus 로고
    • Abnormal Alzheimer-like phosphorylation of tau-protein by cyclin-dependent kinases cdk2 and cdk5
    • Baumann K., Mandelkow E.-M., Biernat J., Piwnica-Worms H., and Mandelkow E. (1993) Abnormal Alzheimer-like phosphorylation of tau-protein by cyclin-dependent kinases cdk2 and cdk5. FEBS Lett. 336, 417-424.
    • (1993) FEBS Lett. , vol.336 , pp. 417-424
    • Baumann, K.1    Mandelkow, E.-M.2    Biernat, J.3    Piwnica-Worms, H.4    Mandelkow, E.5
  • 2
    • 0027338266 scopus 로고
    • 262 strongly reduces binding of tau to microtubules: Distinction between PHF-like immunoreactivity and microtubule binding
    • 262 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
  • 3
    • 0025998840 scopus 로고
    • Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates
    • Boyle W. J., van der Geer P., and Hunter T. (1991) Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates. Methods Enzymol. 201, 110-149.
    • (1991) Methods Enzymol. , vol.201 , pp. 110-149
    • Boyle, W.J.1    Van Der Geer, P.2    Hunter, T.3
  • 4
    • 0027512745 scopus 로고
    • Neurofilament monoclonal antibodies RT97 and 8D8 recognize different modified epitopes in paired helical filament-τ in Alzheimer's disease
    • Brion J.-P., Couck A.-M., Robertson J., Loviny T. L. F., and Anderton B. H. (1993a) Neurofilament monoclonal antibodies RT97 and 8D8 recognize different modified epitopes in paired helical filament-τ in Alzheimer's disease. J. Neurochem. 60, 1372-1382.
    • (1993) J. Neurochem. , vol.60 , pp. 1372-1382
    • Brion, J.-P.1    Couck, A.-M.2    Robertson, J.3    Loviny, T.L.F.4    Anderton, B.H.5
  • 5
    • 0027429479 scopus 로고
    • Developmental changes in τ phosphorylation: Fetal τ is transiently phosphorylated in a manner similar to paired helical filament-τ characteristic of Alzheimer's disease
    • Brion J.-P., Smith C., Couck A.-M., Gallo J.-M., and Anderton B. H. (1993b) Developmental changes in τ phosphorylation: fetal τ is transiently phosphorylated in a manner similar to paired helical filament-τ characteristic of Alzheimer's disease. J. Neurochem. 61, 2071-2080.
    • (1993) J. Neurochem. , vol.61 , pp. 2071-2080
    • Brion, J.-P.1    Smith, C.2    Couck, A.-M.3    Gallo, J.-M.4    Anderton, B.H.5
  • 6
    • 0028926263 scopus 로고
    • Parallel signal processing among mammalian MAPKs
    • Cano E. and Mahadevan L. C. (1995) Parallel signal processing among mammalian MAPKs. Trends Biochem. Sci. 20, 117-122.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 117-122
    • Cano, E.1    Mahadevan, L.C.2
  • 7
    • 0025217147 scopus 로고
    • Phosphate-dependent monoclonal antibodies to neurofilaments and Alzheimer neurofibrillary tangles recognize a synthetic phosphopeptide
    • Coleman M. P. and Anderton B. H. (1990) Phosphate-dependent monoclonal antibodies to neurofilaments and Alzheimer neurofibrillary tangles recognize a synthetic phosphopeptide. J. Neurochem. 54, 1548-1555.
    • (1990) J. Neurochem. , vol.54 , pp. 1548-1555
    • Coleman, M.P.1    Anderton, B.H.2
  • 8
    • 0029782176 scopus 로고    scopus 로고
    • Purification and cDNA cloning of SAPKK3, the major activator of RK/p38 in stress- and cytokine-stimulated monocytes and epithelial cells
    • Cuenda A., Alonso G., Morrice N., Jones M., Meier R., Cohen P., and Nebreda A. R. (1996) Purification and cDNA cloning of SAPKK3, the major activator of RK/p38 in stress-and cytokine-stimulated monocytes and epithelial cells. EMBO J. 15, 4156-4164.
    • (1996) EMBO J. , vol.15 , pp. 4156-4164
    • Cuenda, A.1    Alonso, G.2    Morrice, N.3    Jones, M.4    Meier, R.5    Cohen, P.6    Nebreda, A.R.7
  • 9
    • 0029123294 scopus 로고
    • The phosphorylation state of the microtubule-associated protein tau as affected by glutamate, colchicine and β-amyloid in primary rat cortical neuronal cultures
    • Davis D. R., Brion J.-P., Couck A.-M., Gallo J.-M., Hanger D. P., Ladhani K., Lewis C., Miller C. C. J., Rupniak T., Smith C., and Anderton B. H. (1995) The phosphorylation state of the microtubule-associated protein tau as affected by glutamate, colchicine and β-amyloid in primary rat cortical neuronal cultures. Biochem. J. 309, 941-949.
    • (1995) Biochem. J. , vol.309 , pp. 941-949
    • Davis, D.R.1    Brion, J.-P.2    Couck, A.-M.3    Gallo, J.-M.4    Hanger, D.P.5    Ladhani, K.6    Lewis, C.7    Miller, C.C.J.8    Rupniak, T.9    Smith, C.10    Anderton, B.H.11
  • 10
    • 0028073283 scopus 로고
    • MAPKs: New JNK expands the group
    • Davis R. J. (1994) MAPKs: new JNK expands the group. Trends Biochem. Sci. 19, 470-473.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 470-473
    • Davis, R.J.1
  • 11
    • 0028329953 scopus 로고
    • JNK1: A protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain
    • Dérijard B., Hibi M., Wu I.-H., Barrett T., Su B., Deng T., Karin M., and Davis R. J. (1994) JNK1: a protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain. Cell 76, 1025-1037.
    • (1994) Cell , vol.76 , pp. 1025-1037
    • Dérijard, B.1    Hibi, M.2    Wu, I.-H.3    Barrett, T.4    Su, B.5    Deng, T.6    Karin, M.7    Davis, R.J.8
  • 12
    • 0028969480 scopus 로고
    • Activation of the MAP kinase homologue RK requires the phosphorylation of Thr-180 and Tyr-182 and both residues are phosphorylated in chemically stressed KB cells
    • Doza Y. N., Cuenda A., Thomas G. M., Cohen P., and Nebreda A. R. (1995) Activation of the MAP kinase homologue RK requires the phosphorylation of Thr-180 and Tyr-182 and both residues are phosphorylated in chemically stressed KB cells. FEBS Lett. 364, 223-228.
    • (1995) FEBS Lett. , vol.364 , pp. 223-228
    • Doza, Y.N.1    Cuenda, A.2    Thomas, G.M.3    Cohen, P.4    Nebreda, A.R.5
  • 13
    • 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
  • 15
    • 0028015872 scopus 로고
    • Interleukin-1 activates a novel protein kinase cascade that results in the phosphorylation of hsp27
    • Freshney N. W., Rawlinson L., Guesdon F., Jones E., Cowley S., Hsuan J., and Saklatvala J. (1994) Interleukin-1 activates a novel protein kinase cascade that results in the phosphorylation of hsp27. Cell 78, 1039-1049.
    • (1994) Cell , vol.78 , pp. 1039-1049
    • Freshney, N.W.1    Rawlinson, L.2    Guesdon, F.3    Jones, E.4    Cowley, S.5    Hsuan, J.6    Saklatvala, J.7
  • 16
    • 0028173238 scopus 로고
    • τ phosphorylation in human, primate, and rat brain: Evidence that a pool of τ is highly phosphorylated in vivo and is rapidly dephosphorylated in vitro
    • Carver T. D., Harris K. A., Lehman R. A. W., Lee V. M.-Y., Trojanowski J. Q., and Billingsley M. L. (1994) τ phosphorylation in human, primate, and rat brain: evidence that a pool of τ is highly phosphorylated in vivo and is rapidly dephosphorylated in vitro. J. Neurochem. 63, 2279-2287.
    • (1994) J. Neurochem. , vol.63 , pp. 2279-2287
    • Carver, T.D.1    Harris, K.A.2    Lehman, R.A.W.3    Lee, V.M.-Y.4    Trojanowski, J.Q.5    Billingsley, M.L.6
  • 17
    • 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
  • 18
    • 0026595846 scopus 로고
    • Tau proteins of Alzheimer paired helical filaments: Abnormal phosphorylation of all six brain isoforms
    • Goedert M., Spillantini M. G., Cairns N. J., and Crowther R. A. (1992) Tau proteins of Alzheimer paired helical filaments: abnormal phosphorylation of all six brain isoforms. Neuron 8, 159-168.
    • (1992) Neuron , vol.8 , pp. 159-168
    • Goedert, M.1    Spillantini, M.G.2    Cairns, N.J.3    Crowther, R.A.4
  • 20
    • 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
  • 21
    • 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, 167-170.
    • (1995) Neurosci. Lett. , vol.189 , pp. 167-170
    • Goedert, M.1    Jakes, R.2    Vanmechelen, E.3
  • 22
    • 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
  • 24
    • 0027333557 scopus 로고
    • Cellular processing of beta-amyloid precursor protein and the genesis of amyloid beta-peptide
    • Haass C. and Selkoe D. J. (1993) Cellular processing of beta-amyloid precursor protein and the genesis of amyloid beta-peptide. Cell 75, 1039-1042.
    • (1993) Cell , vol.75 , pp. 1039-1042
    • Haass, C.1    Selkoe, D.J.2
  • 25
    • 0027936755 scopus 로고
    • A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells
    • Han J., Lee J.-D., Bibbs L., and Ulevitch R. J. (1994) A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells. Science 265, 808-811.
    • (1994) Science , vol.265 , pp. 808-811
    • Han, J.1    Lee, J.-D.2    Bibbs, L.3    Ulevitch, R.J.4
  • 26
    • 0026487365 scopus 로고
    • Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: Generation of paired helical filament epitopes and neuronal localisation of the kinase
    • Hanger D. P., Hughes K., Woodgett J. R., Brion J.-P., and Anderton B. H. (1992) Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: generation of paired helical filament epitopes and neuronal localisation of the kinase. Neurosci. Lett. 147, 58-62.
    • (1992) Neurosci. Lett. , vol.147 , pp. 58-62
    • Hanger, D.P.1    Hughes, K.2    Woodgett, J.R.3    Brion, J.-P.4    Anderton, B.H.5
  • 28
    • 0029879046 scopus 로고    scopus 로고
    • Characterization of mAb AP422, a novel phosphorylation-dependent monoclonal antibody against tau protein
    • Hasegawa M., Jakes R., Crowther R. A., Lee V. M. Y., Ihara Y., and Goedert M. (1996) Characterization of mAb AP422, a novel phosphorylation-dependent monoclonal antibody against tau protein. FEBS Lett 384, 25-30.
    • (1996) FEBS Lett , vol.384 , pp. 25-30
    • Hasegawa, M.1    Jakes, R.2    Crowther, R.A.3    Lee, V.M.Y.4    Ihara, Y.5    Goedert, M.6
  • 29
    • 0029873980 scopus 로고    scopus 로고
    • Inhibition of p38 mitogen-activated protein kinase by insulin in cultured fetal neurons
    • Heidenreich K. A. and Kummer J. L. (1996) Inhibition of p38 mitogen-activated protein kinase by insulin in cultured fetal neurons. J. Biol. Chem. 271, 9891-9894.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9891-9894
    • Heidenreich, K.A.1    Kummer, J.L.2
  • 30
    • 0027423418 scopus 로고
    • Identification of an oncoprotein- and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain
    • Hibi M., Lin A., Smeal T., Minden A., and Karin M. (1993) Identification of an oncoprotein-and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain. Genes Dev. 7, 2135-2148.
    • (1993) Genes Dev. , vol.7 , pp. 2135-2148
    • Hibi, M.1    Lin, A.2    Smeal, T.3    Minden, A.4    Karin, M.5
  • 31
    • 0026580539 scopus 로고
    • Baculovirus-mediated expression and characterisation of rat glycogen synthase kinase-3 beta, the mammalian homologue of the Drosophila melanogaster zeste-white 3sgg homeotic gene product
    • Hughes K., Pulverer B. J., Theocharous P., and Woodgett J. R. (1992) Baculovirus-mediated expression and characterisation of rat glycogen synthase kinase-3 beta, the mammalian homologue of the Drosophila melanogaster zeste-white 3sgg homeotic gene product. Eur. J. Biochem. 203, 305-311.
    • (1992) Eur. J. Biochem. , vol.203 , pp. 305-311
    • Hughes, K.1    Pulverer, B.J.2    Theocharous, P.3    Woodgett, J.R.4
  • 32
    • 0023675999 scopus 로고
    • A novel tubulin-dependent protein kinase forming a paired helical filament epitope on tau
    • Ishiguro K., Ihara Y., Uchida T., and Imahori K. (1988) A novel tubulin-dependent protein kinase forming a paired helical filament epitope on tau. J. Biochem. (Tokyo) 104, 319-321.
    • (1988) J. Biochem. (Tokyo) , vol.104 , pp. 319-321
    • Ishiguro, K.1    Ihara, Y.2    Uchida, T.3    Imahori, K.4
  • 33
    • 0026619472 scopus 로고
    • Phosphorylation sites on tau by tau protein kinase I, a bovine derived kinase generating an epitope of paired helical filaments
    • Ishiguro K., Omori A., Takamatsu M., Sato K., Arioka M., Uchida T., and Imahori K. (1992a) Phosphorylation sites on tau by tau protein kinase I, a bovine derived kinase generating an epitope of paired helical filaments. Neurosci. Lett. 148, 202-206.
    • (1992) Neurosci. Lett. , vol.148 , pp. 202-206
    • Ishiguro, K.1    Omori, A.2    Takamatsu, M.3    Sato, K.4    Arioka, M.5    Uchida, T.6    Imahori, K.7
  • 35
    • 0027255817 scopus 로고
    • Glycogen synthase kinase 3β is identical to tau protein kinase I generating several epitopes of paired helical filaments
    • Ishiguro K., Shiratsuchi A., Sato S., Omori A., Arioka M., Kobayashi S., Uchida T., and Imahori K. (1993) Glycogen synthase kinase 3β is identical to tau protein kinase I generating several epitopes of paired helical filaments. FEBS Lett. 325, 167-172.
    • (1993) FEBS Lett. , vol.325 , pp. 167-172
    • Ishiguro, K.1    Shiratsuchi, A.2    Sato, S.3    Omori, A.4    Arioka, M.5    Kobayashi, S.6    Uchida, T.7    Imahori, K.8
  • 36
    • 0028207389 scopus 로고
    • Identification of the 23 kDa subunit of tau protein kinase II as a putative activator of cdk5 in bovine brain
    • Ishiguro K., Kobayashi S., Omori A., Takamatsu M., Yonekura S., Anzai K., Imahori K., and Uchida T. (1994) Identification of the 23 kDa subunit of tau protein kinase II as a putative activator of cdk5 in bovine brain. FEBS Lett. 342, 203-208.
    • (1994) FEBS Lett. , vol.342 , pp. 203-208
    • Ishiguro, K.1    Kobayashi, S.2    Omori, A.3    Takamatsu, M.4    Yonekura, S.5    Anzai, K.6    Imahori, K.7    Uchida, T.8
  • 37
    • 0029982565 scopus 로고    scopus 로고
    • Characterization of the structure and function of a new mitogen-activated protein kinase (p38β)
    • Jiang Y., Chen C. H., Li Z. J., Guo W., Gegner J. A., Lin S. C., and Han J. H. (1996) Characterization of the structure and function of a new mitogen-activated protein kinase (p38β). J. Biol. Chem. 271, 17920-17926.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17920-17926
    • Jiang, Y.1    Chen, C.H.2    Li, Z.J.3    Guo, W.4    Gegner, J.A.5    Lin, S.C.6    Han, J.H.7
  • 38
    • 0027426029 scopus 로고
    • A cdc2-related kinase PSSA-LRE/cdk5 is homologous with the 30 kDa subunit of tau protein kinase II, a proline-directed protein kinase associated with microtubule
    • Kobayashi S., Ishiguro K., Omori A., Takamatsu M., Arioka M., Imahori K., and Uchida T. (1993) A cdc2-related kinase PSSA-LRE/cdk5 is homologous with the 30 kDa subunit of tau protein kinase II, a proline-directed protein kinase associated with microtubule. FEBS Lett. 335, 171-175.
    • (1993) FEBS Lett. , vol.335 , pp. 171-175
    • Kobayashi, S.1    Ishiguro, K.2    Omori, A.3    Takamatsu, M.4    Arioka, M.5    Imahori, K.6    Uchida, T.7
  • 39
    • 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
  • 40
    • 0029744885 scopus 로고    scopus 로고
    • Sounding the alarm: Protein kinase cascades activated by stress and inflammation
    • Kyriakis J. M. and Avruch J. (1996) Sounding the alarm: protein kinase cascades activated by stress and inflammation. J. Biol. Chem. 271, 24313-24316.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24313-24316
    • Kyriakis, J.M.1    Avruch, J.2
  • 42
    • 0029556015 scopus 로고
    • The stress-activated protein kinases - A novel ERK subfamily responsive to cellular stress and inflammatory cytokines
    • Kyriakis J. M., Woodgett J. R., and Avruch J. (1995) The stress-activated protein kinases - A novel ERK subfamily responsive to cellular stress and inflammatory cytokines. Ann. NY Acad. Sci. 766, 303-319.
    • (1995) Ann. NY Acad. Sci. , vol.766 , pp. 303-319
    • Kyriakis, J.M.1    Woodgett, J.R.2    Avruch, J.3
  • 43
    • 0026694067 scopus 로고
    • Implication of brain cdc2 and MAP2 kinases in the phosphorylation of tau protein in Alzheimer's disease
    • Ledesma M. D., Correas I., Avila J., and Diaz Nido J. (1992) Implication of brain cdc2 and MAP2 kinases in the phosphorylation of tau protein in Alzheimer's disease. FEBS Lett. 308, 218-224.
    • (1992) FEBS Lett. , vol.308 , pp. 218-224
    • Ledesma, M.D.1    Correas, I.2    Avila, J.3    Diaz Nido, J.4
  • 45
    • 0029034251 scopus 로고
    • ATF-2 contains a phosphorylation-dependent transcriptional activation domain
    • Livingstone C., Patel G., and Jones N. (1995) ATF-2 contains a phosphorylation-dependent transcriptional activation domain. EMBO J. 14, 1785-1797.
    • (1995) EMBO J. , vol.14 , pp. 1785-1797
    • Livingstone, C.1    Patel, G.2    Jones, N.3
  • 46
    • 0030937952 scopus 로고    scopus 로고
    • The phosphorylation of tau: A critical stage in neurodevelopment and neurodegenerative processes
    • Lovestone S. and Reynolds C. H. (1997) The phosphorylation of tau: a critical stage in neurodevelopment and neurodegenerative processes. Neuroscience 78, 309-324.
    • (1997) Neuroscience , vol.78 , pp. 309-324
    • Lovestone, S.1    Reynolds, C.H.2
  • 49
    • 0030155860 scopus 로고    scopus 로고
    • Amyloid β-peptide and oxidative cellular injury in Alzheimer's disease
    • Mark R. J., Blanc E. M., and Mattson M. P. (1996) Amyloid β-peptide and oxidative cellular injury in Alzheimer's disease. Mol. Neurobiol. 12, 211-224.
    • (1996) Mol. Neurobiol. , vol.12 , pp. 211-224
    • Mark, R.J.1    Blanc, E.M.2    Mattson, M.P.3
  • 50
    • 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
    • Matsuo E. S., Shin R.-W., Billingsley M. L., Van DeVoorde A., O'Connor M., Trojanowski J. Q., and Lee V. M.-Y. (1994) Biopsy-derived adult human brain tau is phosphorylated at many of the same sites as Alzheimer's disease paired helical filament tau. Neuron 13, 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
  • 51
    • 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.-Y. (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.-Y.5
  • 52
    • 0029610011 scopus 로고
    • The inflammatory response system of brain: Implications for therapy of Alzheimer and other neurodegenerative diseases
    • McGeer P. L. and McGeer E. G. (1995) The inflammatory response system of brain: implications for therapy of Alzheimer and other neurodegenerative diseases. Brain Res. Rev. 21, 195-218.
    • (1995) Brain Res. Rev. , vol.21 , pp. 195-218
    • McGeer, P.L.1    McGeer, E.G.2
  • 53
    • 0029811901 scopus 로고    scopus 로고
    • Arthritis and anti-inflammatory agents as possible protective factors for Alzheimer's disease: A review of 17 epidemiologic studies
    • McGeer P. L., Schulzer M., and McGeer E. G. (1996) Arthritis and anti-inflammatory agents as possible protective factors for Alzheimer's disease: a review of 17 epidemiologic studies. Neurology 47, 425-432.
    • (1996) Neurology , vol.47 , pp. 425-432
    • McGeer, P.L.1    Schulzer, M.2    McGeer, E.G.3
  • 54
    • 0028984151 scopus 로고
    • 3F12 kinase: A novel MAP kinase expressed in a subset of neurons in the human nervous system
    • 3F12 kinase: a novel MAP kinase expressed in a subset of neurons in the human nervous system. Neuron 14, 67-78.
    • (1995) Neuron , vol.14 , pp. 67-78
    • Mohit, A.A.1    Martin, J.H.2    Miller, C.A.3
  • 56
    • 0027990436 scopus 로고
    • PHF-tau from Alzheimer's brain comprises four species on SDS-PAGE which can be mimicked by in vitro phosphorylation of human brain tau by glycogen synthase kinase-3β
    • Mulot S. F. C., Hughes K., Woodgett J. R., Anderton B. H., and Hanger D. P. (1994) PHF-tau from Alzheimer's brain comprises four species on SDS-PAGE which can be mimicked by in vitro phosphorylation of human brain tau by glycogen synthase kinase-3β. FEBS Lett. 349, 359-364.
    • (1994) FEBS Lett. , vol.349 , pp. 359-364
    • Mulot, S.F.C.1    Hughes, K.2    Woodgett, J.R.3    Anderton, B.H.4    Hanger, D.P.5
  • 57
    • 0028935270 scopus 로고
    • Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine
    • Raingeaud J., Gupta S., Rogers J. S., Dickens M., Han J., Ulevitch R. J., and Davis R. J. (1995) Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine. J. Biol. Chem. 270, 7420-7426.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7420-7426
    • Raingeaud, J.1    Gupta, S.2    Rogers, J.S.3    Dickens, M.4    Han, J.5    Ulevitch, R.J.6    Davis, R.J.7
  • 58
    • 0030943263 scopus 로고    scopus 로고
    • Stress-activated protein/c-Jun N-terminal kinase phosphorylates τ protein
    • Reynolds C. H., Utton M. A., Gibb G. M., Yates A., and Anderton B. H. (1997) Stress-activated protein/c-Jun N-terminal kinase phosphorylates τ protein. J. Neurochem. 68, 1736-1744.
    • (1997) J. Neurochem. , vol.68 , pp. 1736-1744
    • Reynolds, C.H.1    Utton, M.A.2    Gibb, G.M.3    Yates, A.4    Anderton, B.H.5
  • 60
    • 0028022750 scopus 로고
    • A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase-2 and phosphorylation of the small heat shock proteins
    • Rouse J., Cohen P., Trigon S., Morange M., Alonso-Llamazares A., Zamanillo D., Hunt T., and Nebreda A. R. (1994) A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase-2 and phosphorylation of the small heat shock proteins. Cell 78, 1027-1037.
    • (1994) Cell , vol.78 , pp. 1027-1037
    • Rouse, J.1    Cohen, P.2    Trigon, S.3    Morange, M.4    Alonso-Llamazares, A.5    Zamanillo, D.6    Hunt, T.7    Nebreda, A.R.8
  • 63
    • 0028000717 scopus 로고
    • Dorothy Russell Memorial Lecture: The molecular pathology of Alzheimer's disease: are we any closer to understanding the neurodegenerative process?
    • Smith C. and Anderton B. H. (1994) Dorothy Russell Memorial Lecture: The molecular pathology of Alzheimer's disease: are we any closer to understanding the neurodegenerative process? Neuropathol. Appl. Neurobiol. 20, 322-338.
    • (1994) Neuropathol. Appl. Neurobiol. , vol.20 , pp. 322-338
    • Smith, C.1    Anderton, B.H.2
  • 64
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith D. B. and Johnson K. S. (1988) Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene 67, 31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 67
    • 0028880006 scopus 로고
    • Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis
    • Xia Z. G., Dickens M., Raingeaud J., Davis R. J., and Greenberg M. E. (1995) Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis. Science 270, 1326-1331.
    • (1995) Science , vol.270 , pp. 1326-1331
    • Xia, Z.G.1    Dickens, M.2    Raingeaud, J.3    Davis, R.J.4    Greenberg, M.E.5
  • 68
    • 0025909275 scopus 로고
    • Identification and characterization of the ATP. Mg-dependent protein phosphatase activator (FA) as a microtubule protein kinase in the brain
    • Yang S. D., Yu J. S., and Lai Y. G. (1991) Identification and characterization of the ATP. Mg-dependent protein phosphatase activator (FA) as a microtubule protein kinase in the brain. J. Protein Chem. 10, 171-181.
    • (1991) J. Protein Chem. , vol.10 , pp. 171-181
    • Yang, S.D.1    Yu, J.S.2    Lai, Y.G.3
  • 69
    • 0028818395 scopus 로고
    • Mxi2, a mitogen-activated protein kinase that recognizes and phosphorylates Max protein
    • Zervos A. S., Faccio L., Gatto J. P., Kyriakis J. M., and Brent R. (1995) Mxi2, a mitogen-activated protein kinase that recognizes and phosphorylates Max protein. Proc. Natl. Acad. Sci. USA 92, 10531-10534.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10531-10534
    • Zervos, A.S.1    Faccio, L.2    Gatto, J.P.3    Kyriakis, J.M.4    Brent, R.5


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