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Volumn 22, Issue 9, 2008, Pages 3224-3233

Overexpression of Dyrk1A contributes to neurofibrillary degeneration in Down syndrome

Author keywords

GSK 3 ; Hyperphosphorylation; Tau; Trisomy 21

Indexed keywords

GLYCOGEN SYNTHASE KINASE 3BETA; TAU PROTEIN;

EID: 51349109221     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fj.07-104539     Document Type: Article
Times cited : (207)

References (61)
  • 1
    • 0021956826 scopus 로고
    • Occurrence of neuropathological changes and dementia of Alzheimer's disease in Down's syndrome
    • Wisniewski, K. E., Wisniewski, H. M., and Wen, G. Y. (1985) Occurrence of neuropathological changes and dementia of Alzheimer's disease in Down's syndrome. Ann. Neurol. 17, 278-282
    • (1985) Ann. Neurol , vol.17 , pp. 278-282
    • Wisniewski, K.E.1    Wisniewski, H.M.2    Wen, G.Y.3
  • 2
    • 7444231620 scopus 로고    scopus 로고
    • A chromosome 21 critical region does not cause specific Down syndrome phenotypes
    • Olson, L. E., Richtsmeier, J. T., Leszl, J., and Reeves, R. H. (2004) A chromosome 21 critical region does not cause specific Down syndrome phenotypes. Science 306, 687-690
    • (2004) Science , vol.306 , pp. 687-690
    • Olson, L.E.1    Richtsmeier, J.T.2    Leszl, J.3    Reeves, R.H.4
  • 3
    • 0023009658 scopus 로고
    • Microtubule-associated protein tau. A component of Alzheimer paired helical filaments
    • Grundke-Iqbal, I., Iqbal, K., Quinlan, M., Tung, Y. C., Zaidi, M. S., and Wisniewski, H. M. (1986) Microtubule-associated protein tau. A component of Alzheimer paired helical filaments. J. Biol. Chem. 261, 6084-6089
    • (1986) J. Biol. Chem , vol.261 , pp. 6084-6089
    • Grundke-Iqbal, I.1    Iqbal, K.2    Quinlan, M.3    Tung, Y.C.4    Zaidi, M.S.5    Wisniewski, H.M.6
  • 4
    • 33646020719 scopus 로고    scopus 로고
    • Gong, C.-X., Liu, F., and Iqbal, K. (2006) Dysregulation of protein phosphorylation/dephosphorylation in Alzheimer's disease: a therapeutic target. J. Biomed. Biotech. 31825, 1-11
    • Gong, C.-X., Liu, F., and Iqbal, K. (2006) Dysregulation of protein phosphorylation/dephosphorylation in Alzheimer's disease: a therapeutic target. J. Biomed. Biotech. 31825, 1-11
  • 5
    • 0026740795 scopus 로고
    • Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease
    • Arriagada, P. V., Growdon, J. H., Hedley-Whyte, E. T., and Hyman, B. T. (1992) Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease. Neurology 42, 631-639
    • (1992) Neurology , vol.42 , pp. 631-639
    • Arriagada, P.V.1    Growdon, J.H.2    Hedley-Whyte, E.T.3    Hyman, B.T.4
  • 6
    • 0036224457 scopus 로고    scopus 로고
    • Alzheimer's neurofibrillary pathology and the spectrum of cognitive function: Findings from the Nun Study
    • Riley, K. P., Snowdon, D. A., and Markesbery, W. R. (2002) Alzheimer's neurofibrillary pathology and the spectrum of cognitive function: findings from the Nun Study. Ann. Neurol. 51, 567-577
    • (2002) Ann. Neurol , vol.51 , pp. 567-577
    • Riley, K.P.1    Snowdon, D.A.2    Markesbery, W.R.3
  • 7
    • 0031806441 scopus 로고    scopus 로고
    • Population-based study of the prevalence and presentation of dementia in adults with Down's syndrome
    • Holland, A. J., Hon, J., Huppert, F. A., Stevens, F., and Watson, P. (1998) Population-based study of the prevalence and presentation of dementia in adults with Down's syndrome. Br. J. Psychiatry 172, 493-498
    • (1998) Br. J. Psychiatry , vol.172 , pp. 493-498
    • Holland, A.J.1    Hon, J.2    Huppert, F.A.3    Stevens, F.4    Watson, P.5
  • 8
    • 10144260033 scopus 로고    scopus 로고
    • Human minibrain homologue (MNBH/DYRK1): Characterization, alternative splicing, differential tissue expression, and overexpression in Down syndrome
    • Guimerá, J., Casas, C., Pucharcos, C., Solans, A., Domenech, A., Planas, A. M., Ashley, J., Lovett, M., Estivill, X., and Pritchard, M. A. (1996) Human minibrain homologue (MNBH/DYRK1): characterization, alternative splicing, differential tissue expression, and overexpression in Down syndrome. Hum. Mol. Genet. 5, 1305-1310
    • (1996) Hum. Mol. Genet , vol.5 , pp. 1305-1310
    • Guimerá, J.1    Casas, C.2    Pucharcos, C.3    Solans, A.4    Domenech, A.5    Planas, A.M.6    Ashley, J.7    Lovett, M.8    Estivill, X.9    Pritchard, M.A.10
  • 13
    • 0035340295 scopus 로고    scopus 로고
    • The kinase DYRK phosphorylates protein-synthesis initiation factor eIF2Bepsilon at Ser539 and the microtubule-associated protein tau at Thr212: Potential role for DYRK as a glycogen synthase kinase 3-priming kinase
    • Woods, Y. L., Cohen, P., Becker, W., Jakes, R., Goedert, M., Wang, X., and Proud, C. G. (2001) The kinase DYRK phosphorylates protein-synthesis initiation factor eIF2Bepsilon at Ser539 and the microtubule-associated protein tau at Thr212: potential role for DYRK as a glycogen synthase kinase 3-priming kinase. Biochem. J. 355, 609-615
    • (2001) Biochem. J , vol.355 , pp. 609-615
    • Woods, Y.L.1    Cohen, P.2    Becker, W.3    Jakes, R.4    Goedert, M.5    Wang, X.6    Proud, C.G.7
  • 14
    • 0037124086 scopus 로고    scopus 로고
    • Dynamin is a minibrain kinase/dual specificity Yak1-related kinase 1A substrate
    • Chen-Hwang, M. C., Chen, H. R., Elzinga, M., and Hwang, Y. W. (2002) Dynamin is a minibrain kinase/dual specificity Yak1-related kinase 1A substrate. J. Biol. Chem. 277, 17597-17604
    • (2002) J. Biol. Chem , vol.277 , pp. 17597-17604
    • Chen-Hwang, M.C.1    Chen, H.R.2    Elzinga, M.3    Hwang, Y.W.4
  • 15
    • 27644478606 scopus 로고    scopus 로고
    • Contributions of various protein phosphatases in the regulation of phosphorylation of tau protein
    • Liu, F., Grundke-Iqbal, I., Iqbal, K., and Gong, C.-X. (2005) Contributions of various protein phosphatases in the regulation of phosphorylation of tau protein. Eur. J. Neurosci. 22, 1942-1950
    • (2005) Eur. J. Neurosci , vol.22 , pp. 1942-1950
    • Liu, F.1    Grundke-Iqbal, I.2    Iqbal, K.3    Gong, C.-X.4
  • 16
    • 0028970204 scopus 로고
    • Reconstitution of neuronal Cdc2-like kinase from bacteria-expressed Cdk5 and an active fragment of the brain-specific activator. Kinase activation in the absence of Cdk5 phosphorylation
    • Qi, Z., Huang, Q. Q., Lee, K. Y., Lew, J., and Wang, J. H. (1995) Reconstitution of neuronal Cdc2-like kinase from bacteria-expressed Cdk5 and an active fragment of the brain-specific activator. Kinase activation in the absence of Cdk5 phosphorylation. J. Biol. Chem. 270, 10847-10854
    • (1995) J. Biol. Chem , vol.270 , pp. 10847-10854
    • Qi, Z.1    Huang, Q.Q.2    Lee, K.Y.3    Lew, J.4    Wang, J.H.5
  • 18
    • 0033169066 scopus 로고    scopus 로고
    • Dynamic regulation of expression and phosphorylation of tau by fibroblast growth factor-2 in neural progenitor cells from adult rat hippocampus
    • Tatebayashi, Y., Iqbal, K., and Grundke-Iqbal, I. (1999) Dynamic regulation of expression and phosphorylation of tau by fibroblast growth factor-2 in neural progenitor cells from adult rat hippocampus. J. Neurosci. 19, 5245-5254
    • (1999) J. Neurosci , vol.19 , pp. 5245-5254
    • Tatebayashi, Y.1    Iqbal, K.2    Grundke-Iqbal, I.3
  • 19
    • 0037049240 scopus 로고    scopus 로고
    • Aberrant glycosylation modulates phosphorylation of tau by protein kinase A and dephosphorylation of tau by protein phosphatase 2A and 5
    • Liu, F., Zaidi, T., Iqbal, K., Grundke-Iqbal, I., and Gong, C.-X. (2002) Aberrant glycosylation modulates phosphorylation of tau by protein kinase A and dephosphorylation of tau by protein phosphatase 2A and 5. Neuroscience 115, 829-837
    • (2002) Neuroscience , vol.115 , pp. 829-837
    • Liu, F.1    Zaidi, T.2    Iqbal, K.3    Grundke-Iqbal, I.4    Gong, C.-X.5
  • 20
    • 0028227962 scopus 로고
    • Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease
    • Alonso, A. del C., Zaidi, T., Grundke-Iqbal, I., and Iqbal, K. (1994) Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease. Proc. Natl. Acad. Sci. U. S. A. 91, 5562-5566
    • (1994) Proc. Natl. Acad. Sci. U. S. A , vol.91 , pp. 5562-5566
    • Alonso, A.D.C.1    Zaidi, T.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 21
    • 3543054595 scopus 로고    scopus 로고
    • Mnbk/Dyrk1A phosphorylation regulates the interaction of dynamin 1 with SH3 domain-containing proteins
    • Huang, Y,. Chen-Hwang, M. C., Dolios, G., Murakami, N., Padovan, J. C., Wang, R., and Hwang, Y. W. (2004) Mnbk/Dyrk1A phosphorylation regulates the interaction of dynamin 1 with SH3 domain-containing proteins. Biochemistry 43, 10173-10185
    • (2004) Biochemistry , vol.43 , pp. 10173-10185
    • Huang, Y.1    Chen-Hwang, M.C.2    Dolios, G.3    Murakami, N.4    Padovan, J.C.5    Wang, R.6    Hwang, Y.W.7
  • 22
    • 0037392942 scopus 로고    scopus 로고
    • The specificities of protein kinase inhibitors: An update
    • Bain, J., McLauchlan, H., Elliott, M., and Cohen, P. (2003) The specificities of protein kinase inhibitors: an update. Biochem. J. 371, 199-204
    • (2003) Biochem. J , vol.371 , pp. 199-204
    • Bain, J.1    McLauchlan, H.2    Elliott, M.3    Cohen, P.4
  • 23
    • 0032987650 scopus 로고    scopus 로고
    • Phosphorylation of tau protein by recombinant GSK-3beta: Pronounced phosphorylation at select Ser/Thr-Pro motifs but no phosphorylation at Ser262 in the repeat domain
    • Godemann, R., Biernat, J., Mandelkow, E., and Mandelkow, E. M. (1999) Phosphorylation of tau protein by recombinant GSK-3beta: pronounced phosphorylation at select Ser/Thr-Pro motifs but no phosphorylation at Ser262 in the repeat domain. FEBS Lett. 454, 157-164
    • (1999) FEBS Lett , vol.454 , pp. 157-164
    • Godemann, R.1    Biernat, J.2    Mandelkow, E.3    Mandelkow, E.M.4
  • 24
    • 0347785492 scopus 로고    scopus 로고
    • Truncation of CDK5 activator p35 induces intensive phosphorylation of Ser202/Thr205 of human tau
    • Hashiguchi, M., Saito, T., Hisanaga, S., and Hashiguchi, T. (2002) Truncation of CDK5 activator p35 induces intensive phosphorylation of Ser202/Thr205 of human tau. J. Biol. Chem. 277, 44525-44530
    • (2002) J. Biol. Chem , vol.277 , pp. 44525-44530
    • Hashiguchi, M.1    Saito, T.2    Hisanaga, S.3    Hashiguchi, T.4
  • 25
    • 0026694783 scopus 로고
    • Brain levels of microtubule-associated protein tau are elevated in Alzheimer's disease: A radioimmuno-slot-blot assay for nanograms of the protein
    • Khatoon, S., Grundke-Iqbal, I., and Iqbal, K. (1992) Brain levels of microtubule-associated protein tau are elevated in Alzheimer's disease: a radioimmuno-slot-blot assay for nanograms of the protein. J. Neurochem. 59, 750-753
    • (1992) J. Neurochem , vol.59 , pp. 750-753
    • Khatoon, S.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 26
    • 36949040819 scopus 로고    scopus 로고
    • Site-specific effects of tau phosphorylation on its microtubule assembly activity and self-aggregation
    • Liu, F., Li, B., Tung, E. J, Grundke-Iqbal, I., Iqbal, K., and Gong, C. X. (2007) Site-specific effects of tau phosphorylation on its microtubule assembly activity and self-aggregation. Eur. J. Neurosci. 26, 3429-3436
    • (2007) Eur. J. Neurosci , vol.26 , pp. 3429-3436
    • Liu, F.1    Li, B.2    Tung, E.J.3    Grundke-Iqbal, I.4    Iqbal, K.5    Gong, C.X.6
  • 27
    • 0034723403 scopus 로고    scopus 로고
    • Specificity determinants of substrate recognition by the protein kinase DYRK1A
    • Himpel, S., Tegge, W., Frank, R., Leder, S., Joost, H. G., and Becker, W. (2000) Specificity determinants of substrate recognition by the protein kinase DYRK1A. J. Biol. Chem. 275, 2431-2438
    • (2000) J. Biol. Chem , vol.275 , pp. 2431-2438
    • Himpel, S.1    Tegge, W.2    Frank, R.3    Leder, S.4    Joost, H.G.5    Becker, W.6
  • 28
    • 33645531727 scopus 로고    scopus 로고
    • The protein kinase DYRK1A phosphorylates the splicing factor SF3b1/SAP155 at Thr434, a novel in vivo phosphorylation site
    • De Graaf, K., Czajkowska, H., Rottmann, S., Packman, L. C., Lilischkis, R., Luscher, B., and Becker, W. (2006) The protein kinase DYRK1A phosphorylates the splicing factor SF3b1/SAP155 at Thr434, a novel in vivo phosphorylation site. BMC Biochem. 7, 7
    • (2006) BMC Biochem , vol.7 , pp. 7
    • De Graaf, K.1    Czajkowska, H.2    Rottmann, S.3    Packman, L.C.4    Lilischkis, R.5    Luscher, B.6    Becker, W.7
  • 31
    • 0037414833 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3beta phosphorylates tau at both primed and unprimed sites. Differential impact on microtubule binding
    • Cho, J. H., and Johnson, G. V. (2003) Glycogen synthase kinase 3beta phosphorylates tau at both primed and unprimed sites. Differential impact on microtubule binding. J. Biol. Chem. 278, 187-193
    • (2003) J. Biol. Chem , vol.278 , pp. 187-193
    • Cho, J.H.1    Johnson, G.V.2
  • 33
    • 0027308924 scopus 로고
    • Abnormal tau phosphorylation at Ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding
    • Bramblett, G. T., Goedert, M., Jakes, R., Merrick, S. E., Trojanowski, J. Q., and Lee, V. M. (1993) Abnormal tau phosphorylation at Ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding. Neuron 10, 089-1099
    • (1993) Neuron , vol.10 , pp. 089-1099
    • Bramblett, G.T.1    Goedert, M.2    Jakes, R.3    Merrick, S.E.4    Trojanowski, J.Q.5    Lee, V.M.6
  • 34
    • 0027237861 scopus 로고
    • τ in paired helical filaments is functionally distinct from fetal τ: Assembly incompetence of paired helical filament-τ
    • Yoshida, H., and Ihara, Y. (1993) τ in paired helical filaments is functionally distinct from fetal τ: assembly incompetence of paired helical filament-τ. J. Neurochem. 61, 1183-1186
    • (1993) J. Neurochem , vol.61 , pp. 1183-1186
    • Yoshida, H.1    Ihara, Y.2
  • 35
    • 0035811050 scopus 로고    scopus 로고
    • Hyperphosphorylation induces self-assembly of tau into tangles of paired helical filaments/straight filaments
    • Alonso, A. del C., Zaidi, T., Novak, M., Grundke-Iqbal, I., and Iqbal, K. (2001) Hyperphosphorylation induces self-assembly of tau into tangles of paired helical filaments/straight filaments. Proc. Natl. Acad. Sci. U. S. A. 98, 6923-6928
    • (2001) Proc. Natl. Acad. Sci. U. S. A , vol.98 , pp. 6923-6928
    • Alonso, A.D.C.1    Zaidi, T.2    Novak, M.3    Grundke-Iqbal, I.4    Iqbal, K.5
  • 36
    • 0036118882 scopus 로고    scopus 로고
    • Formation of aberrant phosphotau fibrillar polymers in neural cultured cells
    • Perez, M., Hernandez, F., Gomez-Ramos, A., Smith, M., Perry, G., and Avila, J. (2002) Formation of aberrant phosphotau fibrillar polymers in neural cultured cells. Eur. J. Biochem. 269, 1484-1489
    • (2002) Eur. J. Biochem , vol.269 , pp. 1484-1489
    • Perez, M.1    Hernandez, F.2    Gomez-Ramos, A.3    Smith, M.4    Perry, G.5    Avila, J.6
  • 39
    • 0033135902 scopus 로고    scopus 로고
    • Human minibrain homologue (MNBH/DYRK1): Characterization, alternative splicing, differential tissue expression, and overexpression in Down syndrome
    • Guimerá, J., Casas, C., Estivill, X., and Pritchard, M. (1999) Human minibrain homologue (MNBH/DYRK1): characterization, alternative splicing, differential tissue expression, and overexpression in Down syndrome. Genomics 57, 407-418
    • (1999) Genomics , vol.57 , pp. 407-418
    • Guimerá, J.1    Casas, C.2    Estivill, X.3    Pritchard, M.4
  • 41
    • 0032475973 scopus 로고    scopus 로고
    • Sequence characteristics, subcellular localization, and substrate specificity of DYRK-related kinases, a novel family of dual specificity protein kinases
    • Becker, W., Weber, Y., Wetzel, K., Eirmbter, K., Tejedor, F. J., and Joost, H. G. (1998) Sequence characteristics, subcellular localization, and substrate specificity of DYRK-related kinases, a novel family of dual specificity protein kinases. J. Biol. Chem. 273, 25893-25902
    • (1998) J. Biol. Chem , vol.273 , pp. 25893-25902
    • Becker, W.1    Weber, Y.2    Wetzel, K.3    Eirmbter, K.4    Tejedor, F.J.5    Joost, H.G.6
  • 42
    • 0038391317 scopus 로고    scopus 로고
    • Expression patterns and subcellular localization of the Down syndrome candidate protein MNB/DYRK1A suggest a role in late neuronal differentiation
    • Hämmerle, B., Carnicero, A., Elizalde, C., Ceron, J., Martinez, S., and Tejedor, F. J. (2003) Expression patterns and subcellular localization of the Down syndrome candidate protein MNB/DYRK1A suggest a role in late neuronal differentiation. Eur. J. Neurosci. 17, 2277-2286
    • (2003) Eur. J. Neurosci , vol.17 , pp. 2277-2286
    • Hämmerle, B.1    Carnicero, A.2    Elizalde, C.3    Ceron, J.4    Martinez, S.5    Tejedor, F.J.6
  • 43
    • 26944433068 scopus 로고    scopus 로고
    • Ferrer, I., Barrachina, M., Puig, B., Martinez, de Lagran. M., Marti, E., Avila, J., and Dierssen, M. (2005) Constitutive Dyrk1A is abnormally expressed in Alzheimer disease, Down syndrome, Pick disease, and related transgenic models. Neurobiol. Dis. 20, 392-400
    • Ferrer, I., Barrachina, M., Puig, B., Martinez, de Lagran. M., Marti, E., Avila, J., and Dierssen, M. (2005) Constitutive Dyrk1A is abnormally expressed in Alzheimer disease, Down syndrome, Pick disease, and related transgenic models. Neurobiol. Dis. 20, 392-400
  • 46
    • 33747700331 scopus 로고    scopus 로고
    • Phosphorylation of amphiphysin 1 by Mnb/Dyrk1A, a kinase implicated in Down syndrome
    • Murakami, N., Xie, W., Lu, R. C., Chen-Hwang, M. C., Wieraszko, A., and Hwang, Y. W. (2006) Phosphorylation of amphiphysin 1 by Mnb/Dyrk1A, a kinase implicated in Down syndrome. J. Biol. Chem. 281, 23712-23724
    • (2006) J. Biol. Chem , vol.281 , pp. 23712-23724
    • Murakami, N.1    Xie, W.2    Lu, R.C.3    Chen-Hwang, M.C.4    Wieraszko, A.5    Hwang, Y.W.6
  • 47
    • 34548669115 scopus 로고    scopus 로고
    • Dyrk1A overexpression in immortalized hippocampal cells produces the neuropathological features of Down syndrome
    • Park, J., Yang, E. J., Yoon, J. H., and Chung, K. C. (2007) Dyrk1A overexpression in immortalized hippocampal cells produces the neuropathological features of Down syndrome. Mol. Cell. Neurosci. 36, 270-279
    • (2007) Mol. Cell. Neurosci , vol.36 , pp. 270-279
    • Park, J.1    Yang, E.J.2    Yoon, J.H.3    Chung, K.C.4
  • 48
    • 13944276825 scopus 로고    scopus 로고
    • Twenty years of the Alzheimer's disease amyloid hypothesis: A genetic perspective
    • Tanzi, R. E., and Bertram, L. (2005) Twenty years of the Alzheimer's disease amyloid hypothesis: a genetic perspective. Cell 120, 545-555
    • (2005) Cell , vol.120 , pp. 545-555
    • Tanzi, R.E.1    Bertram, L.2
  • 49
    • 39749196069 scopus 로고    scopus 로고
    • Dual-specificity tyrosine(Y)-phosphorylation regulated kinase 1A-mediated phosphorylation of amyloid precursor protein: Evidence for a functional link between Down syndrome and Alzheimer's disease
    • Ryoo, S. R., Cho, H. J., Lee, H. W., Jeong, H. K., Radnaabazar, C., Kim, Y. S., Kim, M. J., Son, M. Y., Seo, H., Chung, S. H., and Song, W. J. (2008) Dual-specificity tyrosine(Y)-phosphorylation regulated kinase 1A-mediated phosphorylation of amyloid precursor protein: evidence for a functional link between Down syndrome and Alzheimer's disease. J. Neurochem. 104, 1333-1344
    • (2008) J. Neurochem , vol.104 , pp. 1333-1344
    • Ryoo, S.R.1    Cho, H.J.2    Lee, H.W.3    Jeong, H.K.4    Radnaabazar, C.5    Kim, Y.S.6    Kim, M.J.7    Son, M.Y.8    Seo, H.9    Chung, S.H.10    Song, W.J.11
  • 51
    • 33747425620 scopus 로고    scopus 로고
    • GSK-3 is essential in the pathogenesis of Alzheimer's disease
    • Takashima, A. (2006) GSK-3 is essential in the pathogenesis of Alzheimer's disease. J. Alzheimers Dis. 9, 309-317
    • (2006) J. Alzheimers Dis , vol.9 , pp. 309-317
    • Takashima, A.1
  • 52
    • 36148942761 scopus 로고    scopus 로고
    • GSK-3 inhibitors for Alzheimer's disease
    • Avila, J., and Hernandez, F. (2007) GSK-3 inhibitors for Alzheimer's disease. Expert Rev. Neurother. 7, 1527-1533
    • (2007) Expert Rev. Neurother , vol.7 , pp. 1527-1533
    • Avila, J.1    Hernandez, F.2
  • 54
    • 1942469505 scopus 로고    scopus 로고
    • Casein kinase 1delta phosphorylates tau and disrupts its binding to microtubules
    • Li, G., Yin, H., Kuret, J. (2004) Casein kinase 1delta phosphorylates tau and disrupts its binding to microtubules. J. Biol. Chem. 279, 15938-15945
    • (2004) J. Biol. Chem , vol.279 , pp. 15938-15945
    • Li, G.1    Yin, H.2    Kuret, J.3
  • 55
    • 33646234697 scopus 로고    scopus 로고
    • Casein kinase-1 isoforms differentially associate with neurofibrillary and granulovacuolar degeneration lesions
    • Kannanayakal, T. J., Tao, H., Vandre, D. D., and Kuret, J. (2006) Casein kinase-1 isoforms differentially associate with neurofibrillary and granulovacuolar degeneration lesions. Acta Neuropathol. 111, 413-421
    • (2006) Acta Neuropathol , vol.111 , pp. 413-421
    • Kannanayakal, T.J.1    Tao, H.2    Vandre, D.D.3    Kuret, J.4
  • 56
    • 38349050020 scopus 로고    scopus 로고
    • Casein kinase 1 alpha associates with the tau-bearing lesions of inclusion body myositis
    • Kannanayakal, T. J., Mendell, J. R., and Kuret, J. (2008) Casein kinase 1 alpha associates with the tau-bearing lesions of inclusion body myositis. Neurosci. Lett. 431, 141-145
    • (2008) Neurosci. Lett , vol.431 , pp. 141-145
    • Kannanayakal, T.J.1    Mendell, J.R.2    Kuret, J.3
  • 57
    • 29144484163 scopus 로고    scopus 로고
    • Multiple roles of the DSCR1 (Adapt78 or RCAN1) gene and its protein product calcipressin 1 (or RCAN1) in disease
    • Harris, C. D., Ermak, G., and Davies, K. J. A. (2005) Multiple roles of the DSCR1 (Adapt78 or RCAN1) gene and its protein product calcipressin 1 (or RCAN1) in disease. Cell. Mol. Life Sci. 62, 2477-2486
    • (2005) Cell. Mol. Life Sci , vol.62 , pp. 2477-2486
    • Harris, C.D.1    Ermak, G.2    Davies, K.J.A.3
  • 58
    • 0028044722 scopus 로고
    • Alzheimer disease abnormally phosphorylated tau is dephosphorylated by brain protein phosphatase 2B
    • Gong, C.-X., Singh, T. J., Grundke-Iqbal, I., and Iqbal, K. (1994) Alzheimer disease abnormally phosphorylated tau is dephosphorylated by brain protein phosphatase 2B. J. Neurochem. 62, 803-806
    • (1994) J. Neurochem , vol.62 , pp. 803-806
    • Gong, C.-X.1    Singh, T.J.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 59
    • 27644478606 scopus 로고    scopus 로고
    • Contributions of various protein phosphatases in the regulation of phosphorylation of tau protein
    • Liu, F., Grundke-Iqbal, I., Iqbal, K., Gong, C.-X. (2005) Contributions of various protein phosphatases in the regulation of phosphorylation of tau protein. Eur. J. Neurosci. 22, 1942-1950
    • (2005) Eur. J. Neurosci , vol.22 , pp. 1942-1950
    • Liu, F.1    Grundke-Iqbal, I.2    Iqbal, K.3    Gong, C.-X.4
  • 60
    • 0034088846 scopus 로고    scopus 로고
    • Phosphorylation of microtubule-associated protein tau is regulated by protein phosphatase 2A: Implication for neurofibrillary degeneration in Alzheimer disease
    • Gong, C.-X., Lidsky, T., Wegiel, J., Wisniewski, H. M., Grandke-Iqbal, I., and Iqbal, K. (2000) Phosphorylation of microtubule-associated protein tau is regulated by protein phosphatase 2A: implication for neurofibrillary degeneration in Alzheimer disease. J. Biol. Chem. 275, 5535-5544
    • (2000) J. Biol. Chem , vol.275 , pp. 5535-5544
    • Gong, C.-X.1    Lidsky, T.2    Wegiel, J.3    Wisniewski, H.M.4    Grandke-Iqbal, I.5    Iqbal, K.6
  • 61
    • 33646258512 scopus 로고    scopus 로고
    • RCAN1 (DSCR1 or Adapt78) stimulates expression of GSK-3β
    • Ermak, G., Harris, C. D., Battocchio, D., Davies, K. J. A. (2006) RCAN1 (DSCR1 or Adapt78) stimulates expression of GSK-3β. FEBS J. 273, 2100-2109
    • (2006) FEBS J , vol.273 , pp. 2100-2109
    • Ermak, G.1    Harris, C.D.2    Battocchio, D.3    Davies, K.J.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.