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Volumn 288, Issue 11, 2013, Pages 7968-7977

Isomerase Pin1 stimulates dephosphorylation of Tau protein at cyclin-dependent kinase (Cdk5)-dependent Alzheimer phosphorylation sites

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIN-DEPENDENT KINASE; FRONTOTEMPORAL DEMENTIAS; HYPERPHOSPHORYLATION; MICROTUBULE ASSOCIATED PROTEIN; NEUROFIBRILLARY TANGLES; PHOSPHORYLATION SITES; PROTEIN PHOSPHATASE 2A; TAU HYPERPHOSPHORYLATION;

EID: 84875179717     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.433326     Document Type: Article
Times cited : (53)

References (66)
  • 1
    • 34548036227 scopus 로고    scopus 로고
    • Tau-mediated neurodegeneration in Alzheimer's disease and related disorders
    • Ballatore, C., Lee, V. M., and Trojanowski, J. Q. (2007) Tau-mediated neurodegeneration in Alzheimer's disease and related disorders. Nat. Rev. Neurosci. 8, 663-672
    • (2007) Nat. Rev. Neurosci. , vol.8 , pp. 663-672
    • Ballatore, C.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 2
    • 11144258263 scopus 로고    scopus 로고
    • Mutations causing neurodegenerative tauopathies
    • Goedert, M., and Jakes, R. (2005) Mutations causing neurodegenerative tauopathies. Biochim. Biophys. Acta 1739, 240-250
    • (2005) Biochim. Biophys. Acta , vol.1739 , pp. 240-250
    • Goedert, M.1    Jakes, R.2
  • 8
    • 61849088424 scopus 로고    scopus 로고
    • Tau phosphorylation: The therapeutic challenge for neurodegenerative disease
    • Hanger, D. P., Anderton, B. H., and Noble, W. (2009) Tau phosphorylation: the therapeutic challenge for neurodegenerative disease. Trends Mol. Med. 15, 112-119
    • (2009) Trends Mol. Med. , vol.15 , pp. 112-119
    • Hanger, D.P.1    Anderton, B.H.2    Noble, W.3
  • 10
    • 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
  • 11
    • 0031045216 scopus 로고    scopus 로고
    • Physiology and pathology of tau protein kinases in relation to Alzheimer's disease
    • Imahori, K., and Uchida, T. (1997) Physiology and pathology of tau protein kinases in relation to Alzheimer's disease. J. Biochem. 121, 179-188
    • (1997) J. Biochem. , vol.121 , pp. 179-188
    • Imahori, K.1    Uchida, T.2
  • 12
    • 33748752882 scopus 로고    scopus 로고
    • The roles of cyclin-dependent kinase 5 and glycogen synthase kinase 3 in tau hyperphosphorylation
    • Plattner, F., Angelo, M., and Giese, K. P. (2006) The roles of cyclin-dependent kinase 5 and glycogen synthase kinase 3 in tau hyperphosphorylation. J. Biol. Chem. 281, 25457-25465
    • (2006) J. Biol. Chem. , vol.281 , pp. 25457-25465
    • Plattner, F.1    Angelo, M.2    Giese, K.P.3
  • 13
    • 0026731425 scopus 로고
    • Tau protein kinase i converts normal tau protein into A68-like component of paired helical filaments
    • Ishiguro, K., Takamatsu, M., Tomizawa, K., Omori, A., Takahashi, M., Arioka, M., and Uchida, T. (1992) Tau protein kinase I converts normal tau protein into A68-like component of paired helical filaments. J. Biol. Chem. 267, 10897-10901
    • (1992) J. Biol. Chem. , vol.267 , pp. 10897-10901
    • Ishiguro, K.1    Takamatsu, M.2    Tomizawa, K.3    Omori, A.4    Takahashi, M.5    Arioka, M.6    Uchida, T.7
  • 15
    • 78650004185 scopus 로고    scopus 로고
    • Regulation and role of cyclin-dependent kinase activity in neuronal survival and death
    • Hisanaga, S., and Endo, R. (2010) Regulation and role of cyclin-dependent kinase activity in neuronal survival and death. J. Neurochem. 115, 1309-1321
    • (2010) J. Neurochem. , vol.115 , pp. 1309-1321
    • Hisanaga, S.1    Endo, R.2
  • 16
    • 0033540060 scopus 로고    scopus 로고
    • Conversion of p35 to p25 deregulates Cdk5 activity and promotes neurodegeneration
    • Patrick, G. N., Zukerberg, L., Nikolic, M., de la Monte, S., Dikkes, P., and Tsai, L. H. (1999) Conversion of p35 to p25 deregulates Cdk5 activity and promotes neurodegeneration. Nature 402, 615-622
    • (1999) Nature , vol.402 , pp. 615-622
    • Patrick, G.N.1    Zukerberg, L.2    Nikolic, M.3    De La Monte, S.4    Dikkes, P.5    Tsai, L.H.6
  • 17
    • 48249132446 scopus 로고    scopus 로고
    • Myristoylation of p39 and p35 is a determinant of cytoplasmic or nuclear localization of active cyclin-dependent kinase 5 complexes
    • Asada, A., Yamamoto, N., Gohda, M., Saito, T., Hayashi, N., and Hisanaga, S. (2008) Myristoylation of p39 and p35 is a determinant of cytoplasmic or nuclear localization of active cyclin-dependent kinase 5 complexes. J. Neurochem. 106, 1325-1336
    • (2008) J. Neurochem. , vol.106 , pp. 1325-1336
    • Asada, A.1    Yamamoto, N.2    Gohda, M.3    Saito, T.4    Hayashi, N.5    Hisanaga, S.6
  • 18
    • 84869123752 scopus 로고    scopus 로고
    • Phosphorylation of p35 and p39 by Cdk5 determines the subcellular location of the holokinase in a phosphorylation-site-specific manner
    • Asada, A., Saito, T., and Hisanaga, S. (2012) Phosphorylation of p35 and p39 by Cdk5 determines the subcellular location of the holokinase in a phosphorylation-site-specific manner. J. Cell Sci. 125, 3421-3429
    • (2012) J. Cell Sci. , vol.125 , pp. 3421-3429
    • Asada, A.1    Saito, T.2    Hisanaga, S.3
  • 19
    • 77954187920 scopus 로고    scopus 로고
    • Membrane association facilitates degradation and cleavage of the cyclin-dependent kinase 5 activators p35 and p39
    • Minegishi, S., Asada, A., Miyauchi, S., Fuchigami, T., Saito, T., and Hisanaga, S. (2010) Membrane association facilitates degradation and cleavage of the cyclin-dependent kinase 5 activators p35 and p39. Biochemistry 49, 5482-5493
    • (2010) Biochemistry , vol.49 , pp. 5482-5493
    • Minegishi, S.1    Asada, A.2    Miyauchi, S.3    Fuchigami, T.4    Saito, T.5    Hisanaga, S.6
  • 20
    • 0034595834 scopus 로고    scopus 로고
    • Calpain-dependent proteolytic cleavage of the p35 cyclin-dependent kinase 5 activator to p25
    • Kusakawa, G., Saito, T., Onuki, R., Ishiguro, K., Kishimoto, T., and Hisanaga, S. (2000) Calpain-dependent proteolytic cleavage of the p35 cyclin-dependent kinase 5 activator to p25. J. Biol. Chem. 275, 17166-17172
    • (2000) J. Biol. Chem. , vol.275 , pp. 17166-17172
    • Kusakawa, G.1    Saito, T.2    Onuki, R.3    Ishiguro, K.4    Kishimoto, T.5    Hisanaga, S.6
  • 21
    • 0034682414 scopus 로고    scopus 로고
    • Neurotoxicity induces cleavage of p35 to p25 by calpain
    • Lee, M. S., Kwon, Y. T., Li, M., Peng, J., Friedlander, R. M., and Tsai, L. H. (2000) Neurotoxicity induces cleavage of p35 to p25 by calpain. Nature 405, 360-364
    • (2000) Nature , vol.405 , pp. 360-364
    • Lee, M.S.1    Kwon, Y.T.2    Li, M.3    Peng, J.4    Friedlander, R.M.5    Tsai, L.H.6
  • 22
    • 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
  • 25
    • 11144249896 scopus 로고    scopus 로고
    • Increased tau phosphorylation on mitogen-activated protein kinase consensus sites and cognitive decline in transgenic models for Alzheimer's disease and FTDP-17: Evidence for distinct molecular processes underlying tau abnormalities
    • Lambourne, S. L., Sellers, L. A., Bush, T. G., Choudhury, S. K., Emson, P. C., Suh, Y. H., and Wilkinson, L. S. (2005) Increased tau phosphorylation on mitogen-activated protein kinase consensus sites and cognitive decline in transgenic models for Alzheimer's disease and FTDP-17: evidence for distinct molecular processes underlying tau abnormalities. Mol. Cell. Biol. 25, 278-293
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 278-293
    • Lambourne, S.L.1    Sellers, L.A.2    Bush, T.G.3    Choudhury, S.K.4    Emson, P.C.5    Suh, Y.H.6    Wilkinson, L.S.7
  • 26
    • 0033055359 scopus 로고    scopus 로고
    • Stable expression in Chinese hamster ovary cells of mutated tau genes causing frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17
    • Matsumura, N., Yamazaki, T., and Ihara, Y. (1999) Stable expression in Chinese hamster ovary cells of mutated tau genes causing frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17). Am. J. Pathol. 154, 1649-1656
    • (1999) Am. J. Pathol. , vol.154 , pp. 1649-1656
    • Matsumura, N.1    Yamazaki, T.2    Ihara, Y.3
  • 27
    • 0342368837 scopus 로고    scopus 로고
    • The FTDP-17-linked mutation R406W abolishes the interaction of phosphorylated tau with microtubules
    • Pérez, M., Lim, F., Arrasate, M., and Avila, J. (2000) The FTDP-17-linked mutation R406W abolishes the interaction of phosphorylated tau with microtubules. J. Neurochem. 74, 2583-2589
    • (2000) J. Neurochem. , vol.74 , pp. 2583-2589
    • Pérez, M.1    Lim, F.2    Arrasate, M.3    Avila, J.4
  • 28
    • 0035937481 scopus 로고    scopus 로고
    • Effects of FTDP-17 mutations on the in vitro phosphorylation of tau by glycogen synthase kinase 3β identified by mass spectrometry demonstrate certain mutations exert long-range conformational changes
    • Connell, J. W., Gibb, G. M., Betts, J. C., Blackstock, W. P., Gallo, J., Lovestone, S., Hutton, M., and Anderton, B. H. (2001) Effects of FTDP-17 mutations on the in vitro phosphorylation of tau by glycogen synthase kinase 3β identified by mass spectrometry demonstrate certain mutations exert long-range conformational changes. FEBS Lett. 493, 40-44
    • (2001) FEBS Lett , vol.493 , pp. 40-44
    • Connell, J.W.1    Gibb, G.M.2    Betts, J.C.3    Blackstock, W.P.4    Gallo, J.5    Lovestone, S.6    Hutton, M.7    Anderton, B.H.8
  • 29
    • 24744462506 scopus 로고    scopus 로고
    • Phosphorylation of FTDP-17 mutant tau by cyclin-dependent kinase 5 complexed with p35, p25, or p39
    • Sakaue, F., Saito, T., Sato, Y., Asada, A., Ishiguro, K., Hasegawa, M., and Hisanaga, S. (2005) Phosphorylation of FTDP-17 mutant tau by cyclin-dependent kinase 5 complexed with p35, p25, or p39. J. Biol. Chem. 280, 31522-31529
    • (2005) J. Biol. Chem. , vol.280 , pp. 31522-31529
    • Sakaue, F.1    Saito, T.2    Sato, Y.3    Asada, A.4    Ishiguro, K.5    Hasegawa, M.6    Hisanaga, S.7
  • 30
    • 0028902487 scopus 로고
    • Dephosphorylation of Alzheimer paired helical filaments by protein phosphatase-2A and -2B
    • Wang, J. Z., Gong, C. X, Zaidi, T., Grundke-Iqbal, I., and Iqbal, K. (1995) Dephosphorylation of Alzheimer paired helical filaments by protein phosphatase-2A and -2B. J. Biol. Chem. 270, 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
  • 31
    • 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
  • 32
    • 47849120642 scopus 로고    scopus 로고
    • Decrease of protein phosphatase 2A and its association with accumulation and hyperphosphorylation of tau in Down syndrome
    • Liang, Z., Liu, F., Iqbal, K., Grundke-Iqbal, I., Wegiel, J., and Gong, C. X. (2008) Decrease of protein phosphatase 2A and its association with accumulation and hyperphosphorylation of tau in Down syndrome. J. Alzheimers Dis. 13, 295-302
    • (2008) J. Alzheimers Dis. , vol.13 , pp. 295-302
    • Liang, Z.1    Liu, F.2    Iqbal, K.3    Grundke-Iqbal, I.4    Wegiel, J.5    Gong, C.X.6
  • 33
    • 0029416987 scopus 로고
    • Dephosphorylation of fetal-tau and paired helical filaments-tau by protein phosphatases 1 and 2A and calcineurin
    • Yamamoto, H., Hasegawa, M., Ono, T., Tashima, K., Ihara, Y., and Miyamoto, E. (1995) Dephosphorylation of fetal-tau and paired helical filaments-tau by protein phosphatases 1 and 2A and calcineurin. J. Biochem. 118, 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
  • 35
    • 84859185373 scopus 로고    scopus 로고
    • Proline isomer-specific antibodies reveal the early pathogenic tau conformation in Alzheimer's disease
    • Nakamura, K., Greenwood, A., Binder, L., Bigio, E. H., Denial, S., Nicholson, L., Zhou, X. Z., and Lu, K. P. (2012) Proline isomer-specific antibodies reveal the early pathogenic tau conformation in Alzheimer's disease. Cell 149, 232-244
    • (2012) Cell , vol.149 , pp. 232-244
    • Nakamura, K.1    Greenwood, A.2    Binder, L.3    Bigio, E.H.4    Denial, S.5    Nicholson, L.6    Zhou, X.Z.7    Lu, K.P.8
  • 36
    • 34848907217 scopus 로고    scopus 로고
    • Molecular mechanisms of the phospho-dependent prolyl cis/trans isomerase Pin1
    • Lippens, G., Landrieu, I., and Smet, C. (2007) Molecular mechanisms of the phospho-dependent prolyl cis/trans isomerase Pin1. FEBS J. 274, 5211-5222
    • (2007) FEBS J , vol.274 , pp. 5211-5222
    • Lippens, G.1    Landrieu, I.2    Smet, C.3
  • 37
    • 80053299231 scopus 로고    scopus 로고
    • Prolyl isomerase Pin1 as a molecular switch to determine the fate of phosphoproteins
    • Liou, Y. C., Zhou, X. Z., and Lu, K. P. (2011) Prolyl isomerase Pin1 as a molecular switch to determine the fate of phosphoproteins. Trends Biochem. Sci. 36, 501-514
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 501-514
    • Liou, Y.C.1    Zhou, X.Z.2    Lu, K.P.3
  • 40
    • 0033600242 scopus 로고    scopus 로고
    • The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein
    • Lu, P. J., Wulf, G., Zhou, X. Z., Davies, P., and Lu, K. P. (1999) The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein. Nature 399, 784-788
    • (1999) Nature , vol.399 , pp. 784-788
    • Lu, P.J.1    Wulf, G.2    Zhou, X.Z.3    Davies, P.4    Lu, K.P.5
  • 41
    • 1242307774 scopus 로고    scopus 로고
    • The peptidyl prolyl cis/trans-isomerase Pin1 recognizes the phospho-Thr212-Pro213 site on Tau
    • Smet, C., Sambo, A. V., Wieruszeski, J. M., Leroy, A., Landrieu, I., Buée, L., and Lippens, G. (2004) The peptidyl prolyl cis/trans-isomerase Pin1 recognizes the phospho-Thr212-Pro213 site on Tau. Biochemistry 43, 2032-2040
    • (2004) Biochemistry , vol.43 , pp. 2032-2040
    • Smet, C.1    Sambo, A.V.2    Wieruszeski, J.M.3    Leroy, A.4    Landrieu, I.5    Buée, L.6    Lippens, G.7
  • 42
    • 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
  • 44
    • 0037458625 scopus 로고    scopus 로고
    • V-1, a protein expressed transiently during murine cerebellar development, regulates actin polymerization via interaction with capping protein
    • Taoka, M., Ichimura, T., Wakamiya-Tsuruta, A., Kubota, Y., Araki, T., Obinata, T., and Isobe, T. (2003) V-1, a protein expressed transiently during murine cerebellar development, regulates actin polymerization via interaction with capping protein. J. Biol. Chem. 278, 5864-5870
    • (2003) J. Biol. Chem. , vol.278 , pp. 5864-5870
    • Taoka, M.1    Ichimura, T.2    Wakamiya-Tsuruta, A.3    Kubota, Y.4    Araki, T.5    Obinata, T.6    Isobe, T.7
  • 45
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 47
    • 77953170566 scopus 로고    scopus 로고
    • Quantitative measurement of in vivo phosphorylation states of Cdk5 activator p35 by Phos-tag SDS-PAGE
    • Hosokawa, T., Saito, T., Asada, A., Fukunaga, K., and Hisanaga, S. (2010) Quantitative measurement of in vivo phosphorylation states of Cdk5 activator p35 by Phos-tag SDS-PAGE. Mol. Cell. Proteomics. 9, 1133-1143
    • (2010) Mol. Cell. Proteomics. , vol.9 , pp. 1133-1143
    • Hosokawa, T.1    Saito, T.2    Asada, A.3    Fukunaga, K.4    Hisanaga, S.5
  • 48
    • 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
  • 51
    • 0031737206 scopus 로고    scopus 로고
    • Microtubule-stimulated phosphorylation of tau at Ser202 and Thr205 by cdk5 decreases its microtubule nucleation activity
    • Wada, Y., Ishiguro, K., Itoh, T. J., Uchida, T., Hotani, H., Saito, T., Kishimoto, T., and Hisanaga, S. (1998) Microtubule-stimulated phosphorylation of tau at Ser202 and Thr205 by cdk5 decreases its microtubule nucleation activity. J. Biochem. 124, 738-746
    • (1998) J. Biochem. , vol.124 , pp. 738-746
    • Wada, Y.1    Ishiguro, K.2    Itoh, T.J.3    Uchida, T.4    Hotani, H.5    Saito, T.6    Kishimoto, T.7    Hisanaga, S.8
  • 53
    • 33750701178 scopus 로고    scopus 로고
    • Thermodynamics of phosphopeptide binding to the human peptidyl prolyl cis/trans isomerase Pin1
    • Daum, S., Fanghänel, J., Wildemann, D., and Schiene-Fischer, C. (2006) Thermodynamics of phosphopeptide binding to the human peptidyl prolyl cis/trans isomerase Pin1. Biochemistry 45, 12125-12135
    • (2006) Biochemistry , vol.45 , pp. 12125-12135
    • Daum, S.1    Fanghänel, J.2    Wildemann, D.3    Schiene-Fischer, C.4
  • 54
    • 22744432396 scopus 로고    scopus 로고
    • Control of protein-protein interactions: Structure-based discovery of low molecular weight inhibitors of the interactions between Pin1WWdomain and phosphopeptides
    • Smet, C., Duckert, J. F., Wieruszeski, J. M., Landrieu, I., Buée, L., Lippens, G., and Déprez, B. (2005) Control of protein-protein interactions: structure-based discovery of low molecular weight inhibitors of the interactions between Pin1WWdomain and phosphopeptides. J. Med. Chem. 48, 4815-4823
    • (2005) J. Med. Chem. , vol.48 , pp. 4815-4823
    • Smet, C.1    Duckert, J.F.2    Wieruszeski, J.M.3    Landrieu, I.4    Buée, L.5    Lippens, G.6    Déprez, B.7
  • 55
    • 0028946744 scopus 로고
    • Monoclonal antibody AT8 recognises tau protein phosphorylated at both serine 202 and threonine 205
    • Goedert, M., Jakes, R., and Vanmechelen, E., (1995) Monoclonal antibody AT8 recognises tau protein phosphorylated at both serine 202 and threonine 205. Neurosci. Lett. 189, 167-169
    • (1995) Neurosci. Lett. , vol.189 , pp. 167-169
    • Goedert, M.1    Jakes, R.2    Vanmechelen, E.3
  • 56
    • 84857073309 scopus 로고    scopus 로고
    • Regulation of mitochondrial transport and inter-microtubule spacing by tau phosphorylation at the sites hyperphosphorylated in Alzheimer's disease
    • Shahpasand, K., Uemura, I., Saito, T., Asano, T., Hata, K., Shibata, K., Toyoshima, Y., Hasegawa, M., and Hisanaga, S. (2012) Regulation of mitochondrial transport and inter-microtubule spacing by tau phosphorylation at the sites hyperphosphorylated in Alzheimer's disease. J. Neurosci. 32, 2430-2441
    • (2012) J. Neurosci. , vol.32 , pp. 2430-2441
    • Shahpasand, K.1    Uemura, I.2    Saito, T.3    Asano, T.4    Hata, K.5    Shibata, K.6    Toyoshima, Y.7    Hasegawa, M.8    Hisanaga, S.9
  • 57
    • 84857476293 scopus 로고    scopus 로고
    • γ-Aminobutyric acid type A (GABAA) receptor activation modulates tau phosphorylation
    • Nykänen, N. P., Kysenius, K., Sakha, P., Tammela, P., and Huttunen, H. J. (2012) γ-Aminobutyric acid type A (GABAA) receptor activation modulates tau phosphorylation. J. Biol. Chem. 287, 6743-6752
    • (2012) J. Biol. Chem. , vol.287 , pp. 6743-6752
    • Nykänen, N.P.1    Kysenius, K.2    Sakha, P.3    Tammela, P.4    Huttunen, H.J.5
  • 59
    • 0032473350 scopus 로고    scopus 로고
    • The mitotic peptidyl-prolyl isomerase, Pin1, interacts with Cdc25 and Plx1
    • Crenshaw, D. G., Yang, J., Means, A. R., and Kornbluth, S. (1998) The mitotic peptidyl-prolyl isomerase, Pin1, interacts with Cdc25 and Plx1. EMBO J. 17, 1315-1327
    • (1998) EMBO J , vol.17 , pp. 1315-1327
    • Crenshaw, D.G.1    Yang, J.2    Means, A.R.3    Kornbluth, S.4
  • 62
    • 0032578024 scopus 로고    scopus 로고
    • Accumulation of cyclin-dependent kinase 5 (cdk5) in neurons with early stages of Alzheimer's disease neurofibrillary degeneration
    • Pei, J. J., Grundke-Iqbal, I., Iqbal, K., Bogdanovic, N., Winblad, B., and Cowburn, R. F. (1998) Accumulation of cyclin-dependent kinase 5 (cdk5) in neurons with early stages of Alzheimer's disease neurofibrillary degeneration. Brain Res. 797, 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
  • 63
    • 0032502829 scopus 로고    scopus 로고
    • Characterization of tau phosphorylation in glycogen synthase kinase-3β and cyclin dependent kinase-5 activator (p23) transfected cells
    • Michel, G., Mercken, M., Murayama, M., Noguchi, K., Ishiguro, K., Imahori, K., and Takashima, A. (1998) Characterization of tau phosphorylation in glycogen synthase kinase-3β and cyclin dependent kinase-5 activator (p23) transfected cells. Biochim Biophys. Acta 1380, 177-182
    • (1998) Biochim Biophys. Acta , vol.1380 , pp. 177-182
    • Michel, G.1    Mercken, M.2    Murayama, M.3    Noguchi, K.4    Ishiguro, K.5    Imahori, K.6    Takashima, A.7
  • 64
    • 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
  • 65
    • 0036841609 scopus 로고    scopus 로고
    • Tau assembly in inducible transfectants expressing wild-type or FTDP-17 tau
    • DeTure, M., Ko, L. W., Easson, C., and Yen, S. H. (2002) Tau assembly in inducible transfectants expressing wild-type or FTDP-17 tau. Am. J. Pathol. 161, 1711-1722
    • (2002) Am. J. Pathol. , vol.161 , pp. 1711-1722
    • Deture, M.1    Ko, L.W.2    Easson, C.3    Yen, S.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.