메뉴 건너뛰기




Volumn 7, Issue MAY, 2014, Pages

GSK-3β, a pivotal kinase in Alzheimer disease

Author keywords

Alzheimer disease; GSK 3 ; Kinase; Neurodegeneration; Tau proteins

Indexed keywords

AMYLOID BETA PROTEIN; BETA CATENIN; BETA SECRETASE; GLYCOGEN SYNTHASE KINASE 3BETA; INTERLEUKIN 10; INTERLEUKIN 1BETA; INTERLEUKIN 6; MICROTUBULE ASSOCIATED PROTEIN; SOMATOMEDIN C; TAU PROTEIN; TUMOR NECROSIS FACTOR;

EID: 84901417472     PISSN: 16625099     EISSN: None     Source Type: Journal    
DOI: 10.3389/fnmol.2014.00046     Document Type: Review
Times cited : (470)

References (169)
  • 1
  • 2
    • 84858225391 scopus 로고    scopus 로고
    • Alzheimer's disease facts and figures
    • Alzheimer's Association. (2012), doi: 10.1016/j.jalz.2012.02.001
    • Alzheimer's Association. (2012). 2012 Alzheimer's disease facts and figures. Alzheimers Dement. 8, 131-168. doi: 10.1016/j.jalz.2012.02.001
    • (2012) Alzheimers Dement , vol.8 , pp. 131-168
  • 3
    • 0348108123 scopus 로고    scopus 로고
    • Synaptic plasticity and cell cycle activation in neurons are alter-native effector pathways: The 'Dr. Jekyll and Mr. Hyde concept' of Alzheimer's disease or the yin and yang of neuroplasticity
    • doi: 10.1016/j.pneurobio.2003.09.007
    • Arendt, T. (2003). Synaptic plasticity and cell cycle activation in neurons are alter-native effector pathways: the 'Dr. Jekyll and Mr. Hyde concept' of Alzheimer's disease or the yin and yang of neuroplasticity. Prog. Neurobiol. 71, 83-248. doi: 10.1016/j.pneurobio.2003.09.007
    • (2003) Prog. Neurobiol , vol.71 , pp. 83-248
    • Arendt, T.1
  • 4
    • 67349213205 scopus 로고    scopus 로고
    • Synaptic degeneration in Alzheimer's disease
    • doi: 10.1007/s00401-009-0536-x
    • Arendt, T. (2009). Synaptic degeneration in Alzheimer's disease. Acta Neuropathol. 118, 167-179. doi: 10.1007/s00401-009-0536-x
    • (2009) Acta Neuropathol , vol.118 , pp. 167-179
    • Arendt, T.1
  • 5
    • 0030454478 scopus 로고    scopus 로고
    • Expression of the cyclin-dependent kinase inhibitor p16 in Alzheimer's disease
    • doi: 10.1097/00001756-199611250-00050
    • Arendt, T., Rodel, L., Gartner, U., and Holzer, M. (1996). Expression of the cyclin-dependent kinase inhibitor p16 in Alzheimer's disease. Neuroreport 7, 3047-3049. doi: 10.1097/00001756-199611250-00050
    • (1996) Neuroreport , vol.7 , pp. 3047-3049
    • Arendt, T.1    Rodel, L.2    Gartner, U.3    Holzer, M.4
  • 6
    • 0036937699 scopus 로고    scopus 로고
    • Spe-cific tau phosphorylation sites correlate with severity of neuronal cytopathology inAlzheimer'sdisease
    • doi: 10.1007/s004010100423
    • Augustinack, J. C., Schneider, A., Mandelkow, E. M., and Hyman, B. T. (2002). Spe-cific tau phosphorylation sites correlate with severity of neuronal cytopathology inAlzheimer'sdisease. ActaNeuropathol. 103, 26-35. doi: 10.1007/s004010100423
    • (2002) ActaNeuropathol , vol.103 , pp. 26-35
    • Augustinack, J.C.1    Schneider, A.2    Mandelkow, E.M.3    Hyman, B.T.4
  • 7
    • 84872351818 scopus 로고    scopus 로고
    • Inhibition of glycogen synthase kinase-3 ameliorates beta-amyloid pathologyand restores lysosomal acidification and mammalian target of rapamycin activity in the Alzheimer disease mouse model: In vivo and in vitro studies
    • doi: 10.1074/jbc.M112.409250
    • Avrahami, L., Farfara, D., Shaham-Kol, M., Vassar, R., Frenkel, D., and Eldar-Finkelman, H. (2013). Inhibition of glycogen synthase kinase-3 ameliorates beta-amyloid pathologyand restores lysosomal acidification and mammalian target of rapamycin activity in the Alzheimer disease mouse model: in vivo and in vitro studies. J. Biol. Chem. 288, 1295-1306. doi: 10.1074/jbc.M112.409250
    • (2013) J. Biol. Chem , vol.288 , pp. 1295-1306
    • Avrahami, L.1    Farfara, D.2    Shaham-Kol, M.3    Vassar, R.4    Frenkel, D.5    Eldar-Finkelman, H.6
  • 8
    • 0037337293 scopus 로고    scopus 로고
    • White matter structural integrity in healthy aging adults and patients with Alzheimer disease: A magnetic resonance imaging study
    • doi: 10.1001/archneur.60.3.393
    • Bartzokis, G., Cummings, J. L., Sultzer, D., Henderson, V. W., Nuechterlein, K. H., and Mintz, J. (2003). White matter structural integrity in healthy aging adults and patients with Alzheimer disease: a magnetic resonance imaging study. Arch. Neurol. 60, 393-398. doi: 10.1001/archneur.60.3.393
    • (2003) Arch. Neurol , vol.60 , pp. 393-398
    • Bartzokis, G.1    Cummings, J.L.2    Sultzer, D.3    Henderson, V.W.4    Nuechterlein, K.H.5    Mintz, J.6
  • 9
    • 42949176249 scopus 로고    scopus 로고
    • Synapse elimination accompanies functional plasticity in hippocampal neurons
    • doi: 10.1073/pnas.0800027105
    • Bastrikova, N., Gardner, G. A., Reece, J. M., Jeromin, A., and Dudek, S. M. (2008). Synapse elimination accompanies functional plasticity in hippocampal neurons. Proc. Natl. Acad. Sci. U.S.A. 105, 3123-3127. doi: 10.1073/pnas.0800027105
    • (2008) Proc. Natl. Acad. Sci. U.S.A , vol.105 , pp. 3123-3127
    • Bastrikova, N.1    Gardner, G.A.2    Reece, J.M.3    Jeromin, A.4    Dudek, S.M.5
  • 10
    • 33748299477 scopus 로고    scopus 로고
    • The paradoxical pro-and anti-apoptotic actions of GSK3 in the intrinsic and extrinsic apoptosis signaling pathways
    • doi: 10.1016/j.pneurobio.2006.07.006
    • Beurel, E., and Jope, R. S. (2006). The paradoxical pro-and anti-apoptotic actions of GSK3 in the intrinsic and extrinsic apoptosis signaling pathways. Prog. Neurobiol. 79, 173-189. doi: 10.1016/j.pneurobio.2006.07.006
    • (2006) Prog. Neurobiol , vol.79 , pp. 173-189
    • Beurel, E.1    Jope, R.S.2
  • 11
    • 0242664588 scopus 로고    scopus 로고
    • Structural insights and biological effects of glycogen synthase kinase 3-specific inhibitor AR-A014418
    • doi: 10.1074/jbc.M306268200
    • Bhat, R., Xue, Y., Berg, S., Hellberg, S., Ormo, M., Nilsson, Y., et al. (2003). Structural insights and biological effects of glycogen synthase kinase 3-specific inhibitor AR-A014418. J. Biol. Chem. 278, 45937-45945. doi: 10.1074/jbc.M306268200
    • (2003) J. Biol. Chem , vol.278 , pp. 45937-45945
    • Bhat, R.1    Xue, Y.2    Berg, S.3    Hellberg, S.4    Ormo, M.5    Nilsson, Y.6
  • 12
    • 67651165504 scopus 로고    scopus 로고
    • Dendritic spine dynam-ics
    • doi: 10.1146/annurev.physiol.010908. 163140
    • Bhatt, D. H., Zhang, S., and Gan, W. B. (2009). Dendritic spine dynam-ics. Annu. Rev. Physiol. 71, 261-282. doi: 10.1146/annurev.physiol.010908. 163140
    • (2009) Annu. Rev. Physiol , vol.71 , pp. 261-282
    • Bhatt, D.H.1    Zhang, S.2    Gan, W.B.3
  • 13
    • 0034677804 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3beta facilitates staurosporine-and heat shock-induced apoptosis. Protection bylithium
    • doi: 10.1074/jbc.275.11.7583
    • Bijur, G. N., De Sarno, P., and Jope, R. S. (2000). Glycogen synthase kinase-3beta facilitates staurosporine-and heat shock-induced apoptosis. Protection bylithium. J. Biol. Chem. 275, 7583-7590. doi: 10.1074/jbc.275.11.7583
    • (2000) J. Biol. Chem , vol.275 , pp. 7583-7590
    • Bijur, G.N.1    de Sarno, P.2    Jope, R.S.3
  • 14
    • 0031007546 scopus 로고    scopus 로고
    • Regulatedphosphorylationand dephos-phorylation of tau protein: Effects on microtubule interaction, intracellular trafficking and neurodegeneration
    • Billingsley, M. L., and Kincaid, R. L. (1997). Regulatedphosphorylationand dephos-phorylation of tau protein: effects on microtubule interaction, intracellular trafficking and neurodegeneration. Biochem. J. 323(Pt 3), 577-591.
    • (1997) Biochem. J , vol.323 , Issue.PART 3 , pp. 577-591
    • Billingsley, M.L.1    Kincaid, R.L.2
  • 15
    • 33847198925 scopus 로고    scopus 로고
    • Young and excitable: New neurons in memory networks
    • doi: 10.1038/nn0307-273
    • Bischofberger, J. (2007). Young and excitable: new neurons in memory networks. Nat. Neurosci. 10, 273-275. doi: 10.1038/nn0307-273
    • (2007) Nat. Neurosci , vol.10 , pp. 273-275
    • Bischofberger, J.1
  • 16
    • 33746310315 scopus 로고    scopus 로고
    • Alzheimer's disease
    • doi: 10.1016/S0140-6736(06)69113-7
    • Blennow, K., de Leon, M. J., and Zetterberg, H. (2006). Alzheimer's disease. Lancet 368, 387-403. doi: 10.1016/S0140-6736(06)69113-7
    • (2006) Lancet , vol.368 , pp. 387-403
    • Blennow, K.1    de Leon, M.J.2    Zetterberg, H.3
  • 18
    • 49149098525 scopus 로고    scopus 로고
    • Tau aggregates: Toxic, inert, or protective species?
    • Bretteville, A., and Planel, E. (2008). Tau aggregates: toxic, inert, or protective species? J.Alzheimers Dis. 14, 431-436.
    • (2008) J.Alzheimers Dis , vol.14 , pp. 431-436
    • Bretteville, A.1    Planel, E.2
  • 19
    • 0032402095 scopus 로고    scopus 로고
    • Alzheimer amyloid protein precursor in the rat hippocampus: Transport and processing through the perforant path
    • Buxbaum, J. D., Thinakaran, G., Koliatsos, V., O'Callahan, J., Slunt, H. H., Price, D. L., et al. (1998). Alzheimer amyloid protein precursor in the rat hippocampus: transport and processing through the perforant path. J. Neurosci. 18, 9629-9637.
    • (1998) J. Neurosci , vol.18 , pp. 9629-9637
    • Buxbaum, J.D.1    Thinakaran, G.2    Koliatsos, V.3    O'Callahan, J.4    Slunt, H.H.5    Price, D.L.6
  • 20
    • 34250818767 scopus 로고    scopus 로고
    • Lithium reduces tau phosphorylation but not A beta or working memory deficits in a trans-genic model with both plaques and tangles
    • doi: 10.2353/ajpath.2007.061178
    • Caccamo, A., Oddo, S., Tran, L. X., and LaFerla, F. M. (2007). Lithium reduces tau phosphorylation but not A beta or working memory deficits in a trans-genic model with both plaques and tangles. Am. J. Pathol. 170, 1669-1675. doi: 10.2353/ajpath.2007.061178
    • (2007) Am. J. Pathol , vol.170 , pp. 1669-1675
    • Caccamo, A.1    Oddo, S.2    Tran, L.X.3    Laferla, F.M.4
  • 21
    • 0035112647 scopus 로고    scopus 로고
    • BACE1 is the major beta-secretase for generation of Abeta peptides by neurons
    • doi: 10.1038/85064
    • Cai, H., Wang, Y., McCarthy, D., Wen, H., Borchelt, D. R., Price, D. L., et al. (2001). BACE1 is the major beta-secretase for generation of Abeta peptides by neurons. Nat. Neurosci. 4, 233-234. doi: 10.1038/85064
    • (2001) Nat. Neurosci , vol.4 , pp. 233-234
    • Cai, H.1    Wang, Y.2    McCarthy, D.3    Wen, H.4    Borchelt, D.R.5    Price, D.L.6
  • 22
    • 84865415419 scopus 로고    scopus 로고
    • Roles of glycogen synthase kinase 3 in Alzheimer's disease
    • doi: 10.2174/156720512802455386
    • Cai, Z., Zhao, Y., and Zhao, B. (2012). Roles of glycogen synthase kinase 3 in Alzheimer's disease. Curr. Alzheimer Res. 9, 864-879. doi: 10.2174/156720512802455386
    • (2012) Curr. Alzheimer Res , vol.9 , pp. 864-879
    • Cai, Z.1    Zhao, Y.2    Zhao, B.3
  • 23
    • 0033776383 scopus 로고    scopus 로고
    • Selective small molecule inhibitors of glycogen synthase kinase-3 modulate glycogen metabolism and gene transcription
    • doi: 10.1016/S1074-5521(00)00025-9
    • Coghlan, M. P., Culbert, A. A., Cross, D. A., Corcoran, S. L., Yates, J. W., Pearce, N. J., et al. (2000). Selective small molecule inhibitors of glycogen synthase kinase-3 modulate glycogen metabolism and gene transcription. Chem. Biol. 7, 793-803. doi: 10.1016/S1074-5521(00)00025-9
    • (2000) Chem. Biol , vol.7 , pp. 793-803
    • Coghlan, M.P.1    Culbert, A.A.2    Cross, D.A.3    Corcoran, S.L.4    Yates, J.W.5    Pearce, N.J.6
  • 24
    • 0345276572 scopus 로고    scopus 로고
    • Synaptic slaughter in Alzheimer's disease
    • doi: 10.1016/j.neurobiolaging.2003.09.001
    • Coleman, P. D., and Yao, P. J. (2003). Synaptic slaughter in Alzheimer's disease. Neurobiol.Aging 24, 1023-1027. doi: 10.1016/j.neurobiolaging.2003.09.001
    • (2003) Neurobiol.Aging , vol.24 , pp. 1023-1027
    • Coleman, P.D.1    Yao, P.J.2
  • 25
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
    • doi: 10.1038/378785a0
    • Cross, D.A., Alessi, D. R., Cohen, P., Andjelkovich, M., andHemmings, B.A. (1995). Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature 378, 785-789. doi: 10.1038/378785a0
    • (1995) Nature , vol.378 , pp. 785-789
    • Cross, D.A.1    Alessi, D.R.2    Cohen, P.3    Andjelkovich, M.4    Andhemmings, B.A.5
  • 26
    • 0037100392 scopus 로고    scopus 로고
    • The B cell antigen receptor reg-ulates the transcriptional activator beta-catenin via protein kinase C-mediated inhibition of glycogen synthase kinase-3
    • doi: 10.4049/jimmunol.169.2.758
    • Christian, S. L., Sims, P. V., and Gold, M. R. (2002). The B cell antigen receptor reg-ulates the transcriptional activator beta-catenin via protein kinase C-mediated inhibition of glycogen synthase kinase-3. J. Immunol. 169, 758-769. doi: 10.4049/jimmunol.169.2.758
    • (2002) J. Immunol , vol.169 , pp. 758-769
    • Christian, S.L.1    Sims, P.V.2    Gold, M.R.3
  • 27
    • 14544267623 scopus 로고    scopus 로고
    • 14-3-3 Protein mediates phosphorylation of microtubule-associated pro-tein tau by serum-and glucocorticoid-induced protein kinase 1
    • Chun, J., Kwon, T., Lee, E. J., Kim, C. H., Han, Y. S., Hong, S. K., et al. 14-3-3 Protein mediates phosphorylation of microtubule-associated pro-tein tau by serum-and glucocorticoid-induced protein kinase 1. Mol. Cells 18, 360-368.
    • Mol. Cells , vol.18 , pp. 360-368
    • Chun, J.1    Kwon, T.2    Lee, E.J.3    Kim, C.H.4    Han, Y.S.5    Hong, S.K.6
  • 28
    • 0030809128 scopus 로고    scopus 로고
    • Block of LTP in rat hippocampus in vivo by beta-amyloid precursor protein fragments
    • doi: 10.1097/00001756-199710200-00006
    • Cullen, W. K., Suh, Y. H., Anwyl, R., and Rowan, M. J. (1997). Block of LTP in rat hippocampus in vivo by beta-amyloid precursor protein fragments. Neuroreport 8, 3213-3217. doi: 10.1097/00001756-199710200-00006
    • (1997) Neuroreport , vol.8 , pp. 3213-3217
    • Cullen, W.K.1    Suh, Y.H.2    Anwyl, R.3    Rowan, M.J.4
  • 29
    • 0037220599 scopus 로고    scopus 로고
    • Activation of Wnt signaling rescues neurodegeneration and behavioral impairments induced by beta-amyloid fibrils
    • doi: 10.1038/sj.mp.4001208
    • De Ferrari, G. V., Chacon, M. A., Barria, M. I., Garrido, J. L., Godoy, J. A., Olivares, G., et al. (2003). Activation of Wnt signaling rescues neurodegeneration and behavioral impairments induced by beta-amyloid fibrils. Mol. Psychiatry 8, 195-208. doi: 10.1038/sj.mp.4001208
    • (2003) Mol. Psychiatry , vol.8 , pp. 195-208
    • de Ferrari, G.V.1    Chacon, M.A.2    Barria, M.I.3    Garrido, J.L.4    Godoy, J.A.5    Olivares, G.6
  • 30
    • 84872470005 scopus 로고    scopus 로고
    • Treatment of Alzheimer's disease with the GSK-3 inhibitor tideglusib: A pilot study
    • doi: 10.3233/JAD-2012-120805
    • delSer, T., Steinwachs, K. C., Gertz, H. J., Andres, M.V., Gomez-Carrillo, B., Medina, M., et al. (2013). Treatment of Alzheimer's disease with the GSK-3 inhibitor tideglusib: a pilot study. J. Alzheimers Dis. 33, 205-215. doi: 10.3233/JAD-2012-120805
    • (2013) J. Alzheimers Dis , vol.33 , pp. 205-215
    • Delser, T.1    Steinwachs, K.C.2    Gertz, H.J.3    Andres, M.V.4    Gomez-Carrillo, B.5    Medina, M.6
  • 31
    • 84889596911 scopus 로고    scopus 로고
    • beta-amyloid impairs the regulation of N-methyl-D-aspartate recep-tors by glycogen synthase kinase 3
    • doi: 10.1016/j.neurobiolaging.2013.08.031
    • Deng, Y., Xiong, Z., Chen, P., Wei, J., Chen, S. S., and Yan, Z. (2014). beta-amyloid impairs the regulation of N-methyl-D-aspartate recep-tors by glycogen synthase kinase 3. Neurobiol. Aging 35, 449-459. doi: 10.1016/j.neurobiolaging.2013.08.031
    • (2014) Neurobiol. Aging , vol.35 , pp. 449-459
    • Deng, Y.1    Xiong, Z.2    Chen, P.3    Wei, J.4    Chen, S.S.5    Yan, Z.6
  • 32
    • 67649819365 scopus 로고    scopus 로고
    • GSK3beta, a centre-staged kinase in neuropsychiatric disorders, modu-lates long term memory by inhibitory phosphorylation at serine-9
    • doi: 10.1016/j.nbd.2009.04.003
    • Dewachter, I., Ris, L., Jaworski, T., Seymour, C. M., Kremer, A., Borghgraef, P., et al. (2009). GSK3beta, a centre-staged kinase in neuropsychiatric disorders, modu-lates long term memory by inhibitory phosphorylation at serine-9. Neurobiol. Dis. 35, 193-200. doi: 10.1016/j.nbd.2009.04.003
    • (2009) Neurobiol. Dis , vol.35 , pp. 193-200
    • Dewachter, I.1    Ris, L.2    Jaworski, T.3    Seymour, C.M.4    Kremer, A.5    Borghgraef, P.6
  • 33
    • 0026451030 scopus 로고
    • Immunocytochemistry of neurofibrillary tangles with antibodies to sub-regions of tau protein: Identification of hidden and cleaved tau epitopes and a new phosphorylation site
    • doi: 10.1007/BF00227736
    • Dickson, D. W., Ksiezak-Reding, H., Liu, W. K., Davies, P., Crowe, A., andYen, S. H. (1992). Immunocytochemistry of neurofibrillary tangles with antibodies to sub-regions of tau protein: identification of hidden and cleaved tau epitopes and a new phosphorylation site. Acta Neuropathol. 84, 596-605. doi: 10.1007/BF00227736
    • (1992) Acta Neuropathol , vol.84 , pp. 596-605
    • Dickson, D.W.1    Ksiezak-Reding, H.2    Liu, W.K.3    Davies, P.4    Crowe, A.5    Andyen, S.H.6
  • 34
    • 77953718220 scopus 로고    scopus 로고
    • Indirubin-3;-monoxime rescues spa-tial memory deficits and attenuates beta-amyloid-associated neuropathology in a mouse model of Alzheimer's disease
    • doi: 10.1016/j.nbd.2010.03.022
    • Ding, Y., Qiao, A., and Fan, G. H. (2010). Indirubin-3;-monoxime rescues spa-tial memory deficits and attenuates beta-amyloid-associated neuropathology in a mouse model of Alzheimer's disease. Neurobiol. Dis. 39, 156-168. doi: 10.1016/j.nbd.2010.03.022
    • (2010) Neurobiol. Dis , vol.39 , pp. 156-168
    • Ding, Y.1    Qiao, A.2    Fan, G.H.3
  • 35
    • 34250744600 scopus 로고    scopus 로고
    • Role of glycogen synthase kinase-3 in cell fate and epithelial-mesenchymal transitions
    • doi: 10.1159/000101306
    • Doble, B. W., and Woodgett, J. R. (2007). Role of glycogen synthase kinase-3 in cell fate and epithelial-mesenchymal transitions. Cells Tissues Organs 185, 73-84. doi: 10.1159/000101306
    • (2007) Cells Tissues Organs , vol.185 , pp. 73-84
    • Doble, B.W.1    Woodgett, J.R.2
  • 36
    • 77954904485 scopus 로고    scopus 로고
    • A kinesin signaling complex mediates the ability of GSK-3beta to affect mood-associated behaviors
    • doi: 10.1073/pnas.0913138107
    • Du, J., Wei, Y., Liu, L., Wang, Y., Khairova, R., Blumenthal, R., et al. (2010). A kinesin signaling complex mediates the ability of GSK-3beta to affect mood-associated behaviors. Proc. Natl. Acad. Sci. U.S.A. 107, 11573-11578. doi: 10.1073/pnas.0913138107
    • (2010) Proc. Natl. Acad. Sci. U.S.A , vol.107 , pp. 11573-11578
    • Du, J.1    Wei, Y.2    Liu, L.3    Wang, Y.4    Khairova, R.5    Blumenthal, R.6
  • 37
    • 78049449082 scopus 로고    scopus 로고
    • Involvement of the p75(NTR) signaling pathway in persistent synap-tic suppression coupled with synapse elimination following repeated long-term depression induction
    • doi: 10.1002/jnr.22505
    • Egashira, Y., Tanaka, T., Soni, P., Sakuragi, S., Tominaga-Yoshino, K., and Ogura, A. (2010). Involvement of the p75(NTR) signaling pathway in persistent synap-tic suppression coupled with synapse elimination following repeated long-term depression induction. J. Neurosci. Res. 88, 3433-3446. doi: 10.1002/jnr.22505
    • (2010) J. Neurosci. Res , vol.88 , pp. 3433-3446
    • Egashira, Y.1    Tanaka, T.2    Soni, P.3    Sakuragi, S.4    Tominaga-Yoshino, K.5    Ogura, A.6
  • 38
    • 0019026208 scopus 로고
    • Glycogen synthase kinase-3 from rabbit skelet al muscle. Separation from cyclic-AMP-dependent protein kinase and phosphorylase kinase
    • doi: 10.1111/j.1432-1033.1980.tb06059.x
    • Embi, N., Rylatt, D. B., and Cohen, P. (1980). Glycogen synthase kinase-3 from rabbit skelet al muscle. Separation from cyclic-AMP-dependent protein kinase and phosphorylase kinase. Eur. J. Biochem. 107, 519-527. doi: 10.1111/j.1432-1033.1980.tb06059.x
    • (1980) Eur. J. Biochem , vol.107 , pp. 519-527
    • Embi, N.1    Rylatt, D.B.2    Cohen, P.3
  • 39
    • 33646922314 scopus 로고    scopus 로고
    • Full reversal of Alzheimer's disease-like phenotype in a mouse model with conditional over-expression of glycogen synthase kinase-3
    • doi: 10.1523/JNEUROSCI.0604-06.2006
    • Engel, T., Hernandez, F., Avila, J., and Lucas, J. J. (2006). Full reversal of Alzheimer's disease-like phenotype in a mouse model with conditional over-expression of glycogen synthase kinase-3. J. Neurosci. 26, 5083-5090. doi: 10.1523/JNEUROSCI.0604-06.2006
    • (2006) J. Neurosci , vol.26 , pp. 5083-5090
    • Engel, T.1    Hernandez, F.2    Avila, J.3    Lucas, J.J.4
  • 40
    • 12944250922 scopus 로고    scopus 로고
    • Phosphorylation and inactivation of glycogen synthase kinase 3 by protein kinase A
    • doi: 10.1073/pnas.220413597
    • Fang, X., Yu, S. X., Lu, Y., Bast, R. C., Woodgett, J. R. Jr., and Mills, G. B. (2000). Phosphorylation and inactivation of glycogen synthase kinase 3 by protein kinase A. Proc. Natl. Acad. Sci. U.S.A. 97, 11960-11965. doi: 10.1073/pnas.220413597
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 11960-11965
    • Fang, X.1    Yu, S.X.2    Lu, Y.3    Bast, R.C.4    Woodgett Jr., J.R.5    Mills, G.B.6
  • 41
    • 0141960033 scopus 로고    scopus 로고
    • beta-Amyloid induces paired helical filament-like tau filaments in tissue culture
    • doi: 10.1074/jbc.M308243200
    • Ferrari, A., Hoerndli, F., Baechi, T., Nitsch, R. M., and Gotz, J. (2003). beta-Amyloid induces paired helical filament-like tau filaments in tissue culture. J. Biol. Chem. 278, 40162-40168. doi: 10.1074/jbc.M308243200
    • (2003) J. Biol. Chem , vol.278 , pp. 40162-40168
    • Ferrari, A.1    Hoerndli, F.2    Baechi, T.3    Nitsch, R.M.4    Gotz, J.5
  • 42
    • 78650904823 scopus 로고    scopus 로고
    • Lithium improves hippocampal neurogenesis, neuropathology and cognitive functions in APP mutant mice
    • doi: 10.1371/jour-nal.pone.0014382
    • Fiorentini, A., Rosi, M. C., Grossi, C., Luccarini, I., and Casamenti, F. (2010). Lithium improves hippocampal neurogenesis, neuropathology and cognitive functions in APP mutant mice. PLoS ONE 5:e14382. doi: 10.1371/jour-nal.pone.0014382
    • (2010) PLoS ONE , vol.5
    • Fiorentini, A.1    Rosi, M.C.2    Grossi, C.3    Luccarini, I.4    Casamenti, F.5
  • 43
    • 34447626493 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3: A key regulator of cellularfate
    • doi: 10.1007/s00018-007-7045-7
    • Forde, J. E., and Dale, T. C. (2007). Glycogen synthase kinase 3: a key regulator of cellularfate. Cell. Mol. LifeSci. 64, 1930-1944. doi: 10.1007/s00018-007-7045-7
    • (2007) Cell. Mol. LifeSci , vol.64 , pp. 1930-1944
    • Forde, J.E.1    Dale, T.C.2
  • 44
    • 84860553281 scopus 로고    scopus 로고
    • Does lithium preventAlzheimer's disease?
    • doi: 10.2165/11599180-000000000-00000
    • Forlenza, O. V., de Paula, V. J., Machado-Vieira, R., Diniz, B. S., and Gattaz, W. F. (2012). Does lithium preventAlzheimer's disease? DrugsAging 29, 335-342. doi: 10.2165/11599180-000000000-00000
    • (2012) DrugsAging , vol.29 , pp. 335-342
    • Forlenza, O.V.1    de Paula, V.J.2    Machado-Vieira, R.3    Diniz, B.S.4    Gattaz, W.F.5
  • 45
    • 79955546563 scopus 로고    scopus 로고
    • Disease-modifying properties of long-term lithium treatment for amnestic mildcognitiveimpairment:Randomisedcontrolledtrial
    • doi: 10.1192/bjp.bp.110.080044
    • Forlenza, O. V., Diniz, B. S., Radanovic, M., Santos, F. S., Talib, L. L., and Gattaz, W. F. (2011). Disease-modifying properties of long-term lithium treatment for amnestic mildcognitiveimpairment:randomisedcontrolledtrial. Br. J. Psychiatry 198, 351-356. doi: 10.1192/bjp.bp.110.080044
    • (2011) Br. J. Psychiatry , vol.198 , pp. 351-356
    • Forlenza, O.V.1    Diniz, B.S.2    Radanovic, M.3    Santos, F.S.4    Talib, L.L.5    Gattaz, W.F.6
  • 46
    • 0035907390 scopus 로고    scopus 로고
    • Akt participation in the Wnt signaling pathway through Dishevelled
    • doi: 10.1074/jbc.C000880200
    • Fukumoto, S., Hsieh, C. M., Maemura, K., Layne, M. D., Yet, S. F., Lee, K. H., et al. (2001). Akt participation in the Wnt signaling pathway through Dishevelled. J. Biol. Chem. 276, 17479-17483. doi: 10.1074/jbc.C000880200
    • (2001) J. Biol. Chem , vol.276 , pp. 17479-17483
    • Fukumoto, S.1    Hsieh, C.M.2    Maemura, K.3    Layne, M.D.4    Yet, S.F.5    Lee, K.H.6
  • 47
    • 80455129781 scopus 로고    scopus 로고
    • Different susceptibilityto neurodegeneration of dorsal andventral hip-pocampal dentate gyrus: A study with transgenic mice overexpressing GSK3beta
    • doi: 10.1371/journal.pone.0027262
    • Fuster-Matanzo, A., Llorens-Martin, M., de Barreda, E. G., Avila, J., and Hernandez, F. (2011). Different susceptibilityto neurodegeneration of dorsal andventral hip-pocampal dentate gyrus: a study with transgenic mice overexpressing GSK3beta. PLoS ONE 6:e27262. doi: 10.1371/journal.pone.0027262
    • (2011) PLoS ONE , vol.6
    • Fuster-Matanzo, A.1    Llorens-Martin, M.2    de Barreda, E.G.3    Avila, J.4    Hernandez, F.5
  • 50
    • 70450235497 scopus 로고    scopus 로고
    • Alzheimer's disease-like pathological features in transgenic mice expressing the APP intracellular domain
    • doi: 10.1073/pnas.0907652106
    • Ghosal, K., Vogt, D. L., Liang, M., Shen, Y., Lamb, B. T., and Pimplikar, S. W. (2009). Alzheimer's disease-like pathological features in transgenic mice expressing the APP intracellular domain. Proc. Natl. Acad. Sci. U.S.A. 106, 18367-18372. doi: 10.1073/pnas.0907652106
    • (2009) Proc. Natl. Acad. Sci. U.S.A , vol.106 , pp. 18367-18372
    • Ghosal, K.1    Vogt, D.L.2    Liang, M.3    Shen, Y.4    Lamb, B.T.5    Pimplikar, S.W.6
  • 51
    • 0032987650 scopus 로고    scopus 로고
    • Phospho-rylation of tau protein by recombinant GSK-3beta: Pronounced phosphorylation at select Ser/Thr-Pro motifs but no phosphorylation at Ser262 in the repeat domain
    • doi: 10.1016/S0014-5793(99)00741-3
    • Godemann, R., Biernat, J., Mandelkow, E., and Mandelkow, E. M. (1999). Phospho-rylation of tau protein by recombinant GSK-3beta: pronounced phosphorylation at select Ser/Thr-Pro motifs but no phosphorylation at Ser262 in the repeat domain. FEBSLett. 454, 157-164. doi: 10.1016/S0014-5793(99)00741-3
    • (1999) FEBSLett , vol.454 , pp. 157-164
    • Godemann, R.1    Biernat, J.2    Mandelkow, E.3    Mandelkow, E.M.4
  • 52
    • 75949107662 scopus 로고    scopus 로고
    • Tau-knockout mice show reduced GSK3-induced hippocampal degeneration and learning deficits
    • doi: 10.1016/j.nbd.2009.11.017
    • Gomez de Barreda, E., Perez, M., Gomez Ramos, P., de Cristobal, J., Martin-Maestro, P., Moran, A., et al. (2010). Tau-knockout mice show reduced GSK3-induced hippocampal degeneration and learning deficits. Neurobiol. Dis. 37, 622-629. doi: 10.1016/j.nbd.2009.11.017
    • (2010) Neurobiol. Dis , vol.37 , pp. 622-629
    • Gomez de Barreda, E.1    Perez, M.2    Gomez Ramos, P.3    de Cristobal, J.4    Martin-Maestro, P.5    Moran, A.6
  • 53
    • 34250019938 scopus 로고    scopus 로고
    • Neuronal apoptosis and reversible motor deficit in dominant-negative GSK-3 conditional transgenic mice
    • doi: 10.1038/sj.emboj.7601725
    • Gomez-Sintes, R., Hernandez, F., Bortolozzi, A., Artigas, F., Avila, J. J., Zaratin, P., et al. (2007). Neuronal apoptosis and reversible motor deficit in dominant-negative GSK-3 conditional transgenic mice. EMBO J. 26, 2743-2754. doi: 10.1038/sj.emboj.7601725
    • (2007) EMBO J , vol.26 , pp. 2743-2754
    • Gomez-Sintes, R.1    Hernandez, F.2    Bortolozzi, A.3    Artigas, F.4    Avila, J.J.5    Zaratin, P.6
  • 54
    • 84859333048 scopus 로고    scopus 로고
    • GSK-3 mouse models to studyneuronal apoptosis and neurodegeneration
    • doi: 10.3389/fnmol.2011.00045
    • Gomez-Sintes, R., Hernandez, F., Lucas, J. J., and Avila, J. (2011). GSK-3 mouse models to studyneuronal apoptosis and neurodegeneration. Front. Mol. Neurosci. 4:45. doi: 10.3389/fnmol.2011.00045
    • (2011) Front. Mol. Neurosci , vol.4 , pp. 45
    • Gomez-Sintes, R.1    Hernandez, F.2    Lucas, J.J.3    Avila, J.4
  • 55
    • 65949119740 scopus 로고    scopus 로고
    • Calpain-mediated truncation of GSK-3 in post-mortem brain samples
    • doi: 10.1002/jnr.21932
    • Goni-Oliver, P., Avila, J., and Hernandez, F. (2009). Calpain-mediated truncation of GSK-3 in post-mortem brain samples. J. Neurosci. Res. 87, 1156-1161. doi: 10.1002/jnr.21932
    • (2009) J. Neurosci. Res , vol.87 , pp. 1156-1161
    • Goni-Oliver, P.1    Avila, J.2    Hernandez, F.3
  • 56
    • 34547929974 scopus 로고    scopus 로고
    • N-terminal cleavage of GSK-3 bycalpain: Anewform of GSK-3 regulation
    • doi: 10.1074/jbc.M702793200
    • Goni-Oliver, P., Lucas, J. J., Avila, J., and Hernandez, F. (2007). N-terminal cleavage of GSK-3 bycalpain: anewform of GSK-3 regulation. J. Biol. Chem. 282, 22406-22413. doi: 10.1074/jbc.M702793200
    • (2007) J. Biol. Chem , vol.282 , pp. 22406-22413
    • Goni-Oliver, P.1    Lucas, J.J.2    Avila, J.3    Hernandez, F.4
  • 57
    • 0028965635 scopus 로고    scopus 로고
    • Somatodendritic localization and hyperphosphorylation of tau protein in transgenic mice expressing the longest human brain tau isoform
    • Gotz, J., Probst, A., Spillantini, M. G., Schafer, T., Jakes, R., Burki, K., et al. Somatodendritic localization and hyperphosphorylation of tau protein in transgenic mice expressing the longest human brain tau isoform. EMBO J. 14, 1304-1313.
    • EMBO J , vol.14 , pp. 1304-1313
    • Gotz, J.1    Probst, A.2    Spillantini, M.G.3    Schafer, T.4    Jakes, R.5    Burki, K.6
  • 58
    • 34548191034 scopus 로고    scopus 로고
    • H. Novel phosphorylation sites in tau from Alzheimer brain support a role for casein kinase 1 in disease pathogenesis. J. Biol
    • doi: 10.1074/jbc.M703269200
    • Hanger, D. P., Byers, H. L., Wray, S., Leung, K. Y., Saxton, M. J., Seereeram, A., et al. H. Novel phosphorylation sites in tau from Alzheimer brain support a role for casein kinase 1 in disease pathogenesis. J. Biol. Chem. 282, 23645-23654. doi: 10.1074/jbc.M703269200
    • Chem , vol.282 , pp. 23645-23654
    • Hanger, D.P.1    Byers, H.L.2    Wray, S.3    Leung, K.Y.4    Saxton, M.J.5    Seereeram, A.6
  • 59
    • 84871710082 scopus 로고    scopus 로고
    • Kinase-kinase interaction and mod-ulation of tau phosphorylation
    • doi: 10.1016/B978-0-12-405210-9.00004-7
    • Hashiguchi, M., and Hashiguchi, T. (2013). Kinase-kinase interaction and mod-ulation of tau phosphorylation. Int. Rev. Cell Mol. Biol. 300, 121-160. doi: 10.1016/B978-0-12-405210-9.00004-7
    • (2013) Int. Rev. Cell Mol. Biol , vol.300 , pp. 121-160
    • Hashiguchi, M.1    Hashiguchi, T.2
  • 60
    • 0035209308 scopus 로고    scopus 로고
    • Annual incidence of Alzheimer disease in the United States projected to theyears 2000 through 2050. AlzheimerDis
    • doi: 10.1097/00002093-200110000-00002
    • Hebert, L. E., Beckett, L.A., Scherr, P.A., and Evans, D.A. (2001).Annual incidence of Alzheimer disease in the United States projected to theyears 2000 through 2050. AlzheimerDis. Assoc. Disord. 15, 169-173. doi: 10.1097/00002093-200110000-00002
    • (2001) Assoc. Disord , vol.15 , pp. 169-173
    • Hebert, L.E.1    Beckett, L.A.2    Scherr, P.A.3    Evans, D.A.4
  • 61
    • 1642363745 scopus 로고    scopus 로고
    • Spatial learning deficit in transgenic mice that conditionally over-express GSK-3beta in the brain but do not form tau filaments
    • doi: 10.1046/j.1471-4159.2002.01269.x
    • Hernandez, F., Borrell, J., Guaza, C., Avila, J., and Lucas, J. J. (2002). Spatial learning deficit in transgenic mice that conditionally over-express GSK-3beta in the brain but do not form tau filaments. J. Neurochem. 83, 1529-1533. doi: 10.1046/j.1471-4159.2002.01269.x
    • (2002) J. Neurochem , vol.83 , pp. 1529-1533
    • Hernandez, F.1    Borrell, J.2    Guaza, C.3    Avila, J.4    Lucas, J.J.5
  • 62
    • 0036260892 scopus 로고    scopus 로고
    • Increased expression of the amyloid precursor beta-secretase in Alzheimer's disease
    • doi: 10.1002/ana.10208
    • Holsinger, R. M., McLean, C. A., Beyreuther, K., Masters, C. L., and Evin, G. (2002). Increased expression of the amyloid precursor beta-secretase in Alzheimer's disease. Ann. Neurol. 51, 783-786. doi: 10.1002/ana.10208
    • (2002) Ann. Neurol , vol.51 , pp. 783-786
    • Holsinger, R.M.1    McLean, C.A.2    Beyreuther, K.3    Masters, C.L.4    Evin, G.5
  • 63
    • 33846259727 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 inhibition is integral to long-term potentiation
    • doi: 10.1111/j.1460-9568.2006.05245.x
    • Hooper, C., Markevich, V., Plattner, F., Killick, R., Schofield, E., Engel, T., et al. (2007). Glycogen synthase kinase-3 inhibition is integral to long-term potentiation. Eur. J. Neurosci. 25, 81-86. doi: 10.1111/j.1460-9568.2006.05245.x
    • (2007) Eur. J. Neurosci , vol.25 , pp. 81-86
    • Hooper, C.1    Markevich, V.2    Plattner, F.3    Killick, R.4    Schofield, E.5    Engel, T.6
  • 64
    • 9244245733 scopus 로고    scopus 로고
    • Regulation of mitochondrial pyruvate dehydrogenase activitybytau pro-tein kinase I/glycogen synthase kinase 3beta in brain. Proc. Natl. Acad. Sci
    • doi: 10.1073/pnas.93.7.2719
    • Hoshi, M., Takashima, A., Noguchi, K., Murayama, M., Sato, M., Kondo, S., et al. Regulation of mitochondrial pyruvate dehydrogenase activitybytau pro-tein kinase I/glycogen synthase kinase 3beta in brain. Proc. Natl. Acad. Sci. U.S.A. 93, 2719-2723. doi: 10.1073/pnas.93.7.2719
    • U.S.A , vol.93 , pp. 2719-2723
    • Hoshi, M.1    Takashima, A.2    Noguchi, K.3    Murayama, M.4    Sato, M.5    Kondo, S.6
  • 65
    • 84861325478 scopus 로고    scopus 로고
    • Selectively silencing GSK-3 isoforms reduces plaques and tangles in mouse models of Alzheimer's disease
    • doi: 10.1523/JNEUR0SCI.0889-12.2012
    • Hurtado, D. E., Molina-Porcel, L., Carroll, J. C., Macdonald, C., Aboagye, A. K., Trojanowski, J. Q., et al. (2012). Selectively silencing GSK-3 isoforms reduces plaques and tangles in mouse models of Alzheimer's disease. J. Neurosci. 32, 7392-7402. doi: 10.1523/JNEUR0SCI.0889-12.2012
    • (2012) J. Neurosci , vol.32 , pp. 7392-7402
    • Hurtado, D.E.1    Molina-Porcel, L.2    Carroll, J.C.3    Macdonald, C.4    Aboagye, A.K.5    Trojanowski, J.Q.6
  • 66
    • 17044461433 scopus 로고    scopus 로고
    • The endogenous and cell cycle-dependent phosphorylation of tau protein in living cells: Implications for Alzheimer's disease
    • doi: 10.1091/mbc.9.6.1495
    • Illenberger, S., Zheng-Fischhofer, Q., Preuss, U., Stamer, K., Baumann, K., Trinczek, B., 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. doi: 10.1091/mbc.9.6.1495
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1495-1512
    • Illenberger, S.1    Zheng-Fischhofer, Q.2    Preuss, U.3    Stamer, K.4    Baumann, K.5    Trinczek, B.6
  • 67
    • 0029162513 scopus 로고
    • Evidence for silent synapses: Implications for the expression of LTP
    • doi: 10.1016/0896-6273(95)90046-2
    • Isaac, J. T., Nicoll, R. A., and Malenka, R. C. (1995). Evidence for silent synapses: implications for the expression of LTP. Neuron 15, 427-434. doi: 10.1016/0896-6273(95)90046-2
    • (1995) Neuron , vol.15 , pp. 427-434
    • Isaac, J.T.1    Nicoll, R.A.2    Malenka, R.C.3
  • 68
    • 33745567523 scopus 로고    scopus 로고
    • Role of MAP1B in axonal retrograde transport of mitochondria
    • doi: 10.1042/BJ20060205
    • Jimenez-Mateos, E. M., Gonzalez-Billault, C., Dawson, H. N., Vitek, M. P., and Avila, J. (2006). Role of MAP1B in axonal retrograde transport of mitochondria. Biochem. J. 397, 53-59. doi: 10.1042/BJ20060205
    • (2006) Biochem. J , vol.397 , pp. 53-59
    • Jimenez-Mateos, E.M.1    Gonzalez-Billault, C.2    Dawson, H.N.3    Vitek, M.P.4    Avila, J.5
  • 69
    • 33644756798 scopus 로고    scopus 로고
    • Cumulative activation of Akt and consequent inhibition of glycogen synthase kinase-3 by brain-derived neurotrophic factor and insulin-like growth factor-1 in cultured hippocam-pal neurons
    • doi: 10.1124/jpet.105. 094433
    • Johnson-Farley, N. N., Travkina, T., and Cowen, D. S. (2006). Cumulative activation of Akt and consequent inhibition of glycogen synthase kinase-3 by brain-derived neurotrophic factor and insulin-like growth factor-1 in cultured hippocam-pal neurons. J. Pharmacol. Exp. Ther. 316, 1062-1069. doi: 10.1124/jpet.105. 094433
    • (2006) J. Pharmacol. Exp. Ther , vol.316 , pp. 1062-1069
    • Johnson-Farley, N.N.1    Travkina, T.2    Cowen, D.S.3
  • 70
    • 0042379932 scopus 로고    scopus 로고
    • Lithium and GSK-3: One inhibitor, two inhibitory actions, multiple outcomes
    • doi: 10.1016/S0165-6147(03)00206-2
    • Jope, R. S. (2003). Lithium and GSK-3: one inhibitor, two inhibitory actions, multiple outcomes. Trends Pharmacol. Sci. 24, 441-443. doi: 10.1016/S0165-6147(03)00206-2
    • (2003) Trends Pharmacol. Sci , vol.24 , pp. 441-443
    • Jope, R.S.1
  • 71
    • 84856745255 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 in the etiology and treatment of mood disorders
    • doi: 10.3389/fnmol.2011.00016
    • Jope, R. S. (2011). Glycogen synthase kinase-3 in the etiology and treatment of mood disorders. Front. Mol. Neurosci. 4:16. doi: 10.3389/fnmol.2011.00016
    • (2011) Front. Mol. Neurosci , vol.4 , pp. 16
    • Jope, R.S.1
  • 72
    • 33947597084 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 (GSK3): Inflammation, diseases, and therapeutics
    • doi: 10.1007/s11064-006-9128-5
    • Jope, R. S., Yuskaitis, C. J., and Beurel, E. (2007). Glycogen synthase kinase-3 (GSK3): inflammation, diseases, and therapeutics. Neurochem. Res. 32, 577-595. doi: 10.1007/s11064-006-9128-5
    • (2007) Neurochem. Res , vol.32 , pp. 577-595
    • Jope, R.S.1    Yuskaitis, C.J.2    Beurel, E.3
  • 73
    • 1842420631 scopus 로고    scopus 로고
    • Rapid antidepressive-like activity of specific glycogen synthase kinase-3 inhibitor and its effect on beta-catenin in mouse hippocampus
    • doi: 10.1016/j.biopsych.2004.01.008
    • Kaidanovich-Beilin, O., Milman, A., Weizman, A., Pick, C. G., and Eldar-Finkelman, G. (2004). Rapid antidepressive-like activity of specific glycogen synthase kinase-3 inhibitor and its effect on beta-catenin in mouse hippocampus. Biol. Psychiatry 55, 781-784. doi: 10.1016/j.biopsych.2004.01.008
    • (2004) Biol. Psychiatry , vol.55 , pp. 781-784
    • Kaidanovich-Beilin, O.1    Milman, A.2    Weizman, A.3    Pick, C.G.4    Eldar-Finkelman, G.5
  • 74
    • 0023105114 scopus 로고
    • The precursor of Alzheimer's disease amyloid A4 pro-tein resembles a cell-surface receptor
    • doi: 10.1038/ 325733a0
    • Kang, J., Lemaire, H. G., Unterbeck, A., Salbaum, J. M., Masters, C. L., Grzeschik, K. H., et al. (1987). The precursor of Alzheimer's disease amyloid A4 pro-tein resembles a cell-surface receptor. Nature 325, 733-736. doi: 10.1038/ 325733a0
    • (1987) Nature , vol.325 , pp. 733-736
    • Kang, J.1    Lemaire, H.G.2    Unterbeck, A.3    Salbaum, J.M.4    Masters, C.L.5    Grzeschik, K.H.6
  • 75
    • 3343024236 scopus 로고    scopus 로고
    • Evolutionary constraints associated with functional specificity of the CMGC protein kinases MAPK, CDK, GSK, SRPK, DYRK, and CK2alpha
    • doi: 10.1110/ps.04637904
    • Kannan, N., and Neuwald, A. F. (2004). Evolutionary constraints associated with functional specificity of the CMGC protein kinases MAPK, CDK, GSK, SRPK, DYRK, and CK2alpha. Protein Sci. 13, 2059-2077. doi: 10.1110/ps.04637904
    • (2004) Protein Sci , vol.13 , pp. 2059-2077
    • Kannan, N.1    Neuwald, A.F.2
  • 76
    • 0032080116 scopus 로고    scopus 로고
    • Experience-induced neurogenesis in the senescent dentate gyrus
    • Kempermann, G., Kuhn, H. G., and Gage, F. H. (1998). Experience-induced neurogenesis in the senescent dentate gyrus. J. Neurosci. 18, 3206-3212.
    • (1998) J. Neurosci , vol.18 , pp. 3206-3212
    • Kempermann, G.1    Kuhn, H.G.2    Gage, F.H.3
  • 77
    • 75249102415 scopus 로고    scopus 로고
    • Does lithium protect against dementia?
    • doi: 10.1111/j.1399-5618.2009.00788.x
    • Kessing, L. V., Forman, J. L., andAndersen, P. K. (2010). Does lithium protect against dementia? BipolarDisord. 12, 87-94. doi: 10.1111/j.1399-5618.2009.00788.x
    • (2010) BipolarDisord , vol.12 , pp. 87-94
    • Kessing, L.V.1    Forman, J.L.2    Andandersen, P.K.3
  • 78
    • 56149105343 scopus 로고    scopus 로고
    • I. GSK-3beta is required for memory reconsolidation in adult brain
    • doi: 10.1371/journal.pone.0003540
    • Kimura, T., Yamashita, S., Nakao, S., Park, J. M., Murayama, M., Mizoroki, T., et al. I. GSK-3beta is required for memory reconsolidation in adult brain. PLoS ONE 3:e3540. doi: 10.1371/journal.pone.0003540
    • PLoS ONE , vol.3
    • Kimura, T.1    Yamashita, S.2    Nakao, S.3    Park, J.M.4    Murayama, M.5    Mizoroki, T.6
  • 79
    • 84890552198 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 inhibitors: Rescuers of cognitive impairments
    • doi: 10.1016/j.pharmthera.2013.07.010
    • King, M. K., Pardo, M., Cheng, Y., Downey, K., Jope, R. S., and Beurel, E. (2014). Glycogen synthase kinase-3 inhibitors: rescuers of cognitive impairments. Pharmacol. Ther. 141, 1-12. doi: 10.1016/j.pharmthera.2013.07.010
    • (2014) Pharmacol. Ther , vol.141 , pp. 1-12
    • King, M.K.1    Pardo, M.2    Cheng, Y.3    Downey, K.4    Jope, R.S.5    Beurel, E.6
  • 80
    • 0029776032 scopus 로고    scopus 로고
    • A molecular mechanism for the effect of lithium on development
    • doi: 10.1073/pnas.93.16.8455
    • Klein, P. S., and Melton, D. A. (1996). A molecular mechanism for the effect of lithium on development. Proc. Natl. Acad. Sci. U.S.A. 93, 8455-8459. doi: 10.1073/pnas.93.16.8455
    • (1996) Proc. Natl. Acad. Sci. U.S.A , vol.93 , pp. 8455-8459
    • Klein, P.S.1    Melton, D.A.2
  • 81
    • 77952475340 scopus 로고    scopus 로고
    • Murine features of neurogenesis in the human hippocampus across the lifespan from 0 to 100 years
    • doi: 10.1371/journal.pone.0008809
    • Knoth, R., Singec, I., Ditter, M., Pantazis, G., Capetian, P., Meyer, R. P., et al. (2010). Murine features of neurogenesis in the human hippocampus across the lifespan from 0 to 100 years. PLoS ONE 5:e8809. doi: 10.1371/journal.pone.0008809
    • (2010) PLoS ONE , vol.5
    • Knoth, R.1    Singec, I.2    Ditter, M.3    Pantazis, G.4    Capetian, P.5    Meyer, R.P.6
  • 82
    • 37349109154 scopus 로고    scopus 로고
    • Amyloid-beta-induced neurotoxicity is reduced by inhibition of glycogen synthase kinase-3
    • doi: 10.1016/j.brainres.2007.10.064
    • Koh, S. H., Noh, M.Y., and Kim, S. H. (2008). Amyloid-beta-induced neurotoxicity is reduced by inhibition of glycogen synthase kinase-3. Brain Res. 1188, 254-262. doi: 10.1016/j.brainres.2007.10.064
    • (2008) Brain Res , vol.1188 , pp. 254-262
    • Koh, S.H.1    Noh, M.Y.2    Kim, S.H.3
  • 83
    • 0033569653 scopus 로고    scopus 로고
    • Membrane-anchoredmet alloproteaseMDC9 hasan alpha-secretase activity responsible for processing the amyloid precursor protein
    • doi: 10.1042/0264-6021:3430371
    • Koike, H., Tomioka, S., Sorimachi, H., Saido, T. C., Maruyama, K., Okuyama, A., et al. (1999). Membrane-anchoredmet alloproteaseMDC9 hasan alpha-secretase activity responsible for processing the amyloid precursor protein. Biochem. J. 343(Pt 2), 371-375. doi: 10.1042/0264-6021:3430371
    • (1999) Biochem. J , vol.343 , Issue.PART 2 , pp. 371-375
    • Koike, H.1    Tomioka, S.2    Sorimachi, H.3    Saido, T.C.4    Maruyama, K.5    Okuyama, A.6
  • 84
    • 11844300395 scopus 로고    scopus 로고
    • Soluble Abeta oligomers ultrastructurally localize to cell processes and might be related to synaptic dysfunction in Alzheimer's disease brain
    • doi: 10.1016/j.brainres.2004.10.041
    • Kokubo, H., Kayed, R., Glabe, C. G., and Yamaguchi, H. (2005). Soluble Abeta oligomers ultrastructurally localize to cell processes and might be related to synaptic dysfunction in Alzheimer's disease brain. Brain Res. 1031, 222-228. doi: 10.1016/j.brainres.2004.10.041
    • (2005) Brain Res , vol.1031 , pp. 222-228
    • Kokubo, H.1    Kayed, R.2    Glabe, C.G.3    Yamaguchi, H.4
  • 85
    • 0035808457 scopus 로고    scopus 로고
    • Indirubins inhibit glycogen synthase kinase-3 beta and CDK5/p25, two protein kinases involved in abnormal tau phosphorylation in Alzheimer's disease. A property common to most cyclin-dependent kinase inhibitors?
    • doi: 10.1074/jbc.M002466200
    • Leclerc, S., Garnier, M., Hoessel, R., Marko, D., Bibb, J. A., Snyder, G. L., et al. (2001). Indirubins inhibit glycogen synthase kinase-3 beta and CDK5/p25, two protein kinases involved in abnormal tau phosphorylation in Alzheimer's disease. A property common to most cyclin-dependent kinase inhibitors? J. Biol. Chem. 276, 251-260. doi: 10.1074/jbc.M002466200
    • (2001) J. Biol. Chem , vol.276 , pp. 251-260
    • Leclerc, S.1    Garnier, M.2    Hoessel, R.3    Marko, D.4    Bibb, J.A.5    Snyder, G.L.6
  • 86
    • 0033798031 scopus 로고    scopus 로고
    • Paullones are potent inhibitors of glycogen synthase kinase-3beta and cyclin-dependent kinase 5/p25
    • doi: 10.1046/j.1432-1327.2000.01673.x
    • Leost, M., Schultz, C., Link, A.,Wu Y. Z., Biernat, J., Mandelkow, E. M., et al. (2000). Paullones are potent inhibitors of glycogen synthase kinase-3beta and cyclin-dependent kinase 5/p25. Eur. J. Biochem. 267, 5983-5994. doi: 10.1046/j.1432-1327.2000.01673.x
    • (2000) Eur. J. Biochem , vol.267 , pp. 5983-5994
    • Leost, M.1    Schultz, C.2    Link, A.3    Wu, Y.Z.4    Biernat, J.5    Mandelkow, E.M.6
  • 87
    • 33846129434 scopus 로고    scopus 로고
    • Increased level of active GSK-3beta in Alzheimer's disease and accumulation in argyrophilic grains and in neurones at different stages of neurofibrillary degeneration
    • doi: 10.1111/j.1365-2990.2006.00795.x
    • Leroy, K., Yilmaz, Z., and Brion, J. P. (2007). Increased level of active GSK-3beta in Alzheimer's disease and accumulation in argyrophilic grains and in neurones at different stages of neurofibrillary degeneration. Neuropathol. Appl. Neurobiol. 33, 43-55. doi: 10.1111/j.1365-2990.2006.00795.x
    • (2007) Neuropathol. Appl. Neurobiol , vol.33 , pp. 43-55
    • Leroy, K.1    Yilmaz, Z.2    Brion, J.P.3
  • 88
    • 65549090537 scopus 로고    scopus 로고
    • J. Increase of BDNF serum concentration in lithium treated patients with earlyAlzheimer's disease. J
    • doi: 10.3233/JAD-2009-1004
    • Leyhe, T., Eschweiler, G. W., Stransky, E., Gasser, T., Annas, P., Basun, H., et al. J. Increase of BDNF serum concentration in lithium treated patients with earlyAlzheimer's disease. J. AlzheimersDis. 16, 649-656. doi: 10.3233/JAD-2009-1004
    • AlzheimersDis , vol.16 , pp. 649-656
    • Leyhe, T.1    Eschweiler, G.W.2    Stransky, E.3    Gasser, T.4    Annas, P.5    Basun, H.6
  • 89
    • 33644849088 scopus 로고    scopus 로고
    • Cyclin-dependent protein kinase 5 primes microtubule-associated protein tau site-specifically for glycogen synthase kinase 3beta
    • doi: 10.1021/bi051635j
    • Li, T., Hawkes, C., Qureshi, H. Y., Kar, S., and Paudel, H. K. (2006). Cyclin-dependent protein kinase 5 primes microtubule-associated protein tau site-specifically for glycogen synthase kinase 3beta. Biochemistry 45, 3134-3145. doi: 10.1021/bi051635j
    • (2006) Biochemistry , vol.45 , pp. 3134-3145
    • Li, T.1    Hawkes, C.2    Qureshi, H.Y.3    Kar, S.4    Paudel, H.K.5
  • 90
    • 33644870413 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3beta phosphorylates Alzheimer's disease-specific Ser396 of microtubule-associated protein tau by a sequential mechanism
    • doi: 10.1021/bi051634r
    • Li, T., and Paudel, H. K. (2006). Glycogen synthase kinase 3beta phosphorylates Alzheimer's disease-specific Ser396 of microtubule-associated protein tau by a sequential mechanism. Biochemistry 45, 3125-3133. doi: 10.1021/bi051634r
    • (2006) Biochemistry , vol.45 , pp. 3125-3133
    • Li, T.1    Paudel, H.K.2
  • 91
    • 0029018512 scopus 로고
    • Activation of postsynapticallysilent synapses during pairing-induced LTP in CA1 region of hippocampal slice
    • doi: 10.1038/375400a0
    • Liao, D., Hessler, N.A., and Malinow, R. (1995).Activation of postsynapticallysilent synapses during pairing-induced LTP in CA1 region of hippocampal slice. Nature 375, 400-404. doi: 10.1038/375400a0
    • (1995) Nature , vol.375 , pp. 400-404
    • Liao, D.1    Hessler, N.A.2    Malinow, R.3
  • 92
    • 78149410463 scopus 로고    scopus 로고
    • Sevoflurane impairs memory consolidation in rats, possibly through inhibiting phosphory-lation of glycogen synthase kinase-3beta in the hippocampus
    • doi: 10.1016/j.nlm.2010.08.011
    • Liu, X. S., Xue, Q. S., Zeng, Q. W., Li, Q., Liu, J., Feng, X. M., et al. (2010). Sevoflurane impairs memory consolidation in rats, possibly through inhibiting phosphory-lation of glycogen synthase kinase-3beta in the hippocampus. Neurobiol. Learn. Mem. 94, 461-467. doi: 10.1016/j.nlm.2010.08.011
    • (2010) Neurobiol. Learn. Mem , vol.94 , pp. 461-467
    • Liu, X.S.1    Xue, Q.S.2    Zeng, Q.W.3    Li, Q.4    Liu, J.5    Feng, X.M.6
  • 93
    • 84875416121 scopus 로고    scopus 로고
    • GSK-3beta overexpression causes reversible alterations on post-synaptic densities and dendritic morphology of hippocampal granule neurons in vivo
    • doi: 10.1038/mp.2013.4
    • Llorens-Martin, M., Fuster-Matanzo, A., Teixeira, C. M., Jurado-Arjona, J., Ulloa, F., et al. (2013). GSK-3beta overexpression causes reversible alterations on post-synaptic densities and dendritic morphology of hippocampal granule neurons in vivo. Mol. Psychiatry 18, 451-460. doi: 10.1038/mp.2013.4
    • (2013) Mol. Psychiatry , vol.18 , pp. 451-460
    • Llorens-Martin, M.1    Fuster-Matanzo, A.2    Teixeira, C.M.3    Jurado-Arjona, J.4    Ulloa, F.5
  • 94
    • 81055124828 scopus 로고    scopus 로고
    • GSK3beta is involved in the relief of mitochondria pausing in a tau-dependent manner
    • doi: 10.1371/journal.pone.0027686
    • Llorens-Martin, M., Lopez-Domenech, G., Soriano, E., and Avila, J. (2011). GSK3beta is involved in the relief of mitochondria pausing in a tau-dependent manner. PLoS ONE 6:e27686. doi: 10.1371/journal.pone.0027686
    • (2011) PLoS ONE , vol.6
    • Llorens-Martin, M.1    Lopez-Domenech, G.2    Soriano, E.3    Avila, J.4
  • 95
    • 0036830441 scopus 로고    scopus 로고
    • Enhanced glycogen synthase kinase-3beta activity mediates hypoxia-induced apoptosis of vascular smooth muscle cells andis preventedbyglucose transportand metabolism
    • doi: 10.1074/jbc.M206405200
    • Loberg, R. D., Vesely, E., and Brosius, F. C. III. (2002). Enhanced glycogen synthase kinase-3beta activity mediates hypoxia-induced apoptosis of vascular smooth muscle cells andis preventedbyglucose transportand metabolism. J. Biol. Chem. 4 41667-41673. doi: 10.1074/jbc.M206405200
    • (2002) J. Biol. Chem , vol.4 , pp. 41667-41673
    • Loberg, R.D.1    Vesely, E.2    Brosius III, F.C.3
  • 96
    • 0029994754 scopus 로고    scopus 로고
    • Phosphorylation of tau by glycogen synthase kinase-3 beta in intact mammalian cells: The effects on the organization and stability of microtubules
    • doi: 10.1016/0306-4522(96)00126-1
    • Lovestone, S., Hartley, C. L., Pearce, J., andAnderton, B. H. (1996). Phosphorylation of tau by glycogen synthase kinase-3 beta in intact mammalian cells: the effects on the organization and stability of microtubules. Neuroscience 73, 1145-1157. doi: 10.1016/0306-4522(96)00126-1
    • (1996) Neuroscience , vol.73 , pp. 1145-1157
    • Lovestone, S.1    Hartley, C.L.2    Pearce, J.3    Andanderton, B.H.4
  • 97
    • 0035863188 scopus 로고    scopus 로고
    • Decreasednuclear beta-catenin, tau hyperphosphorylation and neurode-generation in GSK-3beta conditional transgenic mice
    • doi: 10.1093/emboj/20.1.27
    • Lucas, J. J., Hernandez, F., Gomez-Ramos, P., Moran, M. A., Hen, R., and Avila, J. (2001). Decreasednuclear beta-catenin, tau hyperphosphorylation and neurode-generation in GSK-3beta conditional transgenic mice. EMBO J. 20, 27-39. doi: 10.1093/emboj/20.1.27
    • (2001) EMBO J , vol.20 , pp. 27-39
    • Lucas, J.J.1    Hernandez, F.2    Gomez-Ramos, P.3    Moran, M.A.4    Hen, R.5    Avila, J.6
  • 98
    • 38049030324 scopus 로고    scopus 로고
    • Earliest stages of tau conformational changes are related to the appearance of a sequence of specific phospho-dependent tau epitopes in Alzheimer's disease
    • Luna-Munoz, J., Chavez-Macias, L., Garcia-Sierra, F., and Mena, R. (2007). Earliest stages of tau conformational changes are related to the appearance of a sequence of specific phospho-dependent tau epitopes in Alzheimer's disease. J. Alzheimers Dis. 12, 365-375.
    • (2007) J. Alzheimers Dis , vol.12 , pp. 365-375
    • Luna-Munoz, J.1    Chavez-Macias, L.2    Garcia-Sierra, F.3    Mena, R.4
  • 99
    • 0035116273 scopus 로고    scopus 로고
    • Mice deficient in BACE1, the Alzheimer's beta-secretase, have normal pheno-type and abolished beta-amyloid generation
    • doi: 10.1038/85059
    • Luo, Y., Bolon, B., Kahn, S., Bennett, B. D., Babu-Khan, S., Denis, P., et al. (2001). Mice deficient in BACE1, the Alzheimer's beta-secretase, have normal pheno-type and abolished beta-amyloid generation. Nat. Neurosci. 4, 231-232. doi: 10.1038/85059
    • (2001) Nat. Neurosci , vol.4 , pp. 231-232
    • Luo, Y.1    Bolon, B.2    Kahn, S.3    Bennett, B.D.4    Babu-Khan, S.5    Denis, P.6
  • 100
    • 0033213634 scopus 로고    scopus 로고
    • Hippocampal LTD expression involves a pool of AMPARs regulated by the NSF-GluR2 interaction
    • doi: 10.1016/S0896-6273(00)80852-1
    • Luthi, A., Chittajallu, R., Duprat, F., Palmer, M. J., Benke, T. A., Kidd, F. L., et al. (1999). Hippocampal LTD expression involves a pool of AMPARs regulated by the NSF-GluR2 interaction. Neuron 24, 389-399. doi: 10.1016/S0896-6273(00)80852-1
    • (1999) Neuron , vol.24 , pp. 389-399
    • Luthi, A.1    Chittajallu, R.2    Duprat, F.3    Palmer, M.J.4    Benke, T.A.5    Kidd, F.L.6
  • 101
    • 84873802341 scopus 로고    scopus 로고
    • Inhi-bition of GSK3beta-mediated BACE1 expression reduces Alzheimer-associated phenotypes
    • doi: 10.1172/JCI64516
    • Ly, P. T., Wu, Y., Zou, H., Wang, R., Zhou, W., Kinoshita, A., et al. (2013). Inhi-bition of GSK3beta-mediated BACE1 expression reduces Alzheimer-associated phenotypes. J. Clin. Invest. 123, 224-235. doi: 10.1172/JCI64516
    • (2013) J. Clin. Invest , vol.123 , pp. 224-235
    • Ly, P.T.1    Wu, Y.2    Zou, H.3    Wang, R.4    Zhou, W.5    Kinoshita, A.6
  • 103
    • 44049089139 scopus 로고    scopus 로고
    • Amyloid-beta binds to the extracellular cysteine-rich domain of Frizzled and inhibits Wnt/beta-catenin signaling
    • doi: 10.1074/jbc.M707108200
    • Magdesian, M. H., Carvalho, M. M., Mendes, F. A., Saraiva, L. M., Juliano, M. A., Juliano, L. J., et al. (2008). Amyloid-beta binds to the extracellular cysteine-rich domain of Frizzled and inhibits Wnt/beta-catenin signaling. J. Biol. Chem. 283, 9359-9368. doi: 10.1074/jbc.M707108200
    • (2008) J. Biol. Chem , vol.283 , pp. 9359-9368
    • Magdesian, M.H.1    Carvalho, M.M.2    Mendes, F.A.3    Saraiva, L.M.4    Juliano, M.A.5    Juliano, L.J.6
  • 104
    • 76949095680 scopus 로고    scopus 로고
    • MicroRNAs contribute to LTP in the hippocampus in vivo (Commentary on Wibrand et al.)
    • doi: 10.1111/j.1460-9568.2010.07140.x
    • Manahan-Vaughan, D. (2010). MicroRNAs contribute to LTP in the hippocampus in vivo (Commentary on Wibrand et al.). Eur. J. Neurosci. 31, 634-635. doi: 10.1111/j.1460-9568.2010.07140.x
    • (2010) Eur. J. Neurosci , vol.31 , pp. 634-635
    • Manahan-Vaughan, D.1
  • 105
    • 23944486750 scopus 로고    scopus 로고
    • Toll-like receptor-mediated cytokine production is differentially regulated by glycogen synthase kinase 3
    • doi: 10.1038/ni1221
    • Martin, M., Rehani, K., Jope, R. S., and Michalek, S. M. (2005). Toll-like receptor-mediated cytokine production is differentially regulated by glycogen synthase kinase 3. Nat. Immunol. 6, 777-784. doi: 10.1038/ni1221
    • (2005) Nat. Immunol , vol.6 , pp. 777-784
    • Martin, M.1    Rehani, K.2    Jope, R.S.3    Michalek, S.M.4
  • 106
    • 0037075791 scopus 로고    scopus 로고
    • First non-ATP competitive glycogen synthase kinase 3 beta (GSK-3beta) inhibitors: Thiadiazolidinones (TDZD) as potential drugs for the treatment of Alzheimer's disease
    • doi: 10.1021/jm011020u
    • Martinez, A., Alonso, M., Castro, A., Perez, C., and Moreno, F. J. (2002). First non-ATP competitive glycogen synthase kinase 3 beta (GSK-3beta) inhibitors: thiadiazolidinones (TDZD) as potential drugs for the treatment of Alzheimer's disease. J. Med. Chem. 45, 1292-1299. doi: 10.1021/jm011020u
    • (2002) J. Med. Chem , vol.45 , pp. 1292-1299
    • Martinez, A.1    Alonso, M.2    Castro, A.3    Perez, C.4    Moreno, F.J.5
  • 107
    • 80052658723 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3 inhibitors in the next horizon forAlzheimer's disease treatment
    • doi: 10.4061/2011/280502
    • Martinez, A., Gil, C., and Perez, D. I. (2011). Glycogen synthase kinase 3 inhibitors in the next horizon forAlzheimer's disease treatment. Int. J. AlzheimersDis. 2011, 280502. doi: 10.4061/2011/280502
    • (2011) Int. J. AlzheimersDis , vol.2011 , pp. 280502
    • Martinez, A.1    Gil, C.2    Perez, D.I.3
  • 108
    • 77958072692 scopus 로고    scopus 로고
    • MAP1B regulates axonal development by modulating Rho-GTPase Rac1 activity
    • doi: 10.1091/mbc.E09-08-0709
    • Montenegro-Venegas, C., Tortosa, E., Rosso, S., Peretti, D., Bollati, F., Bisbal, M., et al. (2010). MAP1B regulates axonal development by modulating Rho-GTPase Rac1 activity. Mol. Biol. Cell 21, 3518-3528. doi: 10.1091/mbc.E09-08-0709
    • (2010) Mol. Biol. Cell , vol.21 , pp. 3518-3528
    • Montenegro-Venegas, C.1    Tortosa, E.2    Rosso, S.3    Peretti, D.4    Bollati, F.5    Bisbal, M.6
  • 109
    • 0030742818 scopus 로고    scopus 로고
    • Cell cycle markers in the hippocampus in Alzheimer's disease
    • doi: 10.1007/s004010050665
    • Nagy, Z., Esiri, M. M., Cato, A. M., and Smith, A. D. (1997a). Cell cycle markers in the hippocampus in Alzheimer's disease. Acta Neuropathol. 94, 6-15. doi: 10.1007/s004010050665
    • (1997) Acta Neuropathol , vol.94 , pp. 6-15
    • Nagy, Z.1    Esiri, M.M.2    Cato, A.M.3    Smith, A.D.4
  • 110
    • 0031043049 scopus 로고    scopus 로고
    • Expression of cell division markers in the hippocampus in Alzheimer's disease and other neurodegenerative conditions
    • doi: 10.1007/s004010050617
    • Nagy, Z., Esiri, M. M., and Smith, A. D. (1997b). Expression of cell division markers in the hippocampus in Alzheimer's disease and other neurodegenerative conditions. Acta Neuropathol. 93, 294-300. doi: 10.1007/s004010050617
    • (1997) Acta Neuropathol , vol.93 , pp. 294-300
    • Nagy, Z.1    Esiri, M.M.2    Smith, A.D.3
  • 111
    • 34147210411 scopus 로고    scopus 로고
    • Lithium and risk for Alzheimer's disease in elderly patients with bipolar disorder
    • doi: 10.1192/bjp.bp.106.029868
    • Nunes, P. V., Forlenza, O. V., and Gattaz, W. F. (2007). Lithium and risk for Alzheimer's disease in elderly patients with bipolar disorder. Br. J. Psychiatry 190, 359-360. doi: 10.1192/bjp.bp.106.029868
    • (2007) Br. J. Psychiatry , vol.190 , pp. 359-360
    • Nunes, P.V.1    Forlenza, O.V.2    Gattaz, W.F.3
  • 112
    • 84055217601 scopus 로고    scopus 로고
    • Exploring the binding sites of glycogen synthase kinase 3. Identification and characterization of allosteric modulation cavities
    • doi: 10.1021/jm200996g
    • Palomo, V., Soteras, I., Perez, D. I., Perez, C., Gil, C., Campillo, N. E., et al. (2011). Exploring the binding sites of glycogen synthase kinase 3. Identification and characterization of allosteric modulation cavities. J. Med. Chem. 54, 8461-8470. doi: 10.1021/jm200996g
    • (2011) J. Med. Chem , vol.54 , pp. 8461-8470
    • Palomo, V.1    Soteras, I.2    Perez, D.I.3    Perez, C.4    Gil, C.5    Campillo, N.E.6
  • 113
    • 0032493729 scopus 로고    scopus 로고
    • Role of glycogen synthase kinase-3 in the phosphatidylinositol 3-kinase/Akti cell survival pathway
    • doi: 10.1074/jbc.273.32.19929
    • Pap, M., and Cooper, G. M. (1998). Role of glycogen synthase kinase-3 in the phosphatidylinositol 3-kinase/Akti cell survival pathway. J. Biol. Chem. 273, 19929-19932. doi: 10.1074/jbc.273.32.19929
    • (1998) J. Biol. Chem , vol.273 , pp. 19929-19932
    • Pap, M.1    Cooper, G.M.2
  • 114
    • 0036136897 scopus 로고    scopus 로고
    • Role oftranslationinitiation factor 2Bincontrol of cell survival bythe phosphatidylinositol 3-kinase/Akt/glycogen synthase kinase 3betasignalingpathway
    • doi: 10.1128/MCB.22.2.578-586.2002
    • Pap, M., and Cooper, G. M. (2002). Role oftranslationinitiation factor 2Bincontrol of cell survival bythe phosphatidylinositol 3-kinase/Akt/glycogen synthase kinase 3betasignalingpathway. Mol. Cell. Biol. 22, 578-586. doi: 10.1128/MCB.22.2.578-586.2002
    • (2002) Mol. Cell. Biol , vol.22 , pp. 578-586
    • Pap, M.1    Cooper, G.M.2
  • 115
    • 33847113902 scopus 로고    scopus 로고
    • LTP inhibits LTD in the hippocampus via regulation of GSK3beta
    • doi: 10.1016/j.neuron.2007.01.029
    • Peineau, S., Taghibiglou, C., Bradley, C., Wong, T. P., Liu, L. Lu, J., et al. (2007). LTP inhibits LTD in the hippocampus via regulation of GSK3beta. Neuron 53, 703-717. doi: 10.1016/j.neuron.2007.01.029
    • (2007) Neuron , vol.53 , pp. 703-717
    • Peineau, S.1    Taghibiglou, C.2    Bradley, C.3    Wong, T.P.4    Liu, L.5    Lu, J.6
  • 116
    • 0038187674 scopus 로고    scopus 로고
    • GSK-3alpha regulates production of Alzheimer's disease amyloid-beta peptides
    • doi: 10.1038/nature01640
    • Phiel, C. J., Wilson, C. A., Lee, V. M., and Klein, P. S. (2003). GSK-3alpha regulates production of Alzheimer's disease amyloid-beta peptides. Nature 423, 435-439. doi: 10.1038/nature01640
    • (2003) Nature , vol.423 , pp. 435-439
    • Phiel, C.J.1    Wilson, C.A.2    Lee, V.M.3    Klein, P.S.4
  • 117
  • 118
    • 33748752882 scopus 로고    scopus 로고
    • The roles of cyclin-dependent kinase 5 and glycogen synthase kinase 3 in tau hyperphosphorylation
    • doi: 10.1074/jbc.M603469200
    • 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. doi: 10.1074/jbc.M603469200
    • (2006) J. Biol. Chem , vol.281 , pp. 25457-25465
    • Plattner, F.1    Angelo, M.2    Giese, K.P.3
  • 119
    • 0038811796 scopus 로고    scopus 로고
    • Insulin mimetic action of synthetic phosphorylated peptide inhibitors of glycogen synthase kinase-3
    • doi: 10.1124/jpet.102.047381
    • Plotkin, B., Kaidanovich, O., Talior, I., and Eldar-Finkelman, H. (2003). Insulin mimetic action of synthetic phosphorylated peptide inhibitors of glycogen synthase kinase-3. J. Pharmacol. Exp. Ther. 305, 974-980. doi: 10.1124/jpet.102.047381
    • (2003) J. Pharmacol. Exp. Ther , vol.305 , pp. 974-980
    • Plotkin, B.1    Kaidanovich, O.2    Talior, I.3    Eldar-Finkelman, H.4
  • 120
    • 0023028305 scopus 로고
    • Cholinergic dysfunction in Alzheimer dis-ease: Cause or effect? Prog
    • doi: 10.1016/S0079-6123(08) 60644-5
    • Plotkin, D. A., and Jarvik, L. F. (1986). Cholinergic dysfunction in Alzheimer dis-ease: cause or effect? Prog. Brain Res. 65, 91-103. doi: 10.1016/S0079-6123(08) 60644-5
    • (1986) Brain Res , vol.65 , pp. 91-103
    • Plotkin, D.A.1    Jarvik, L.F.2
  • 121
    • 67649416075 scopus 로고    scopus 로고
    • Lithium treatment in Alzheimer's disease does not pro-mote cognitive enhancement, but may exert long-term neuroprotective effects
    • doi: 10.1007/s00213-009-1510-y
    • Pomara, N. (2009). Lithium treatment in Alzheimer's disease does not pro-mote cognitive enhancement, but may exert long-term neuroprotective effects. Psychopharmacology(Berl.)205, 169-170. doi: 10.1007/s00213-009-1510-y
    • (2009) Psychopharmacology(Berl.)205 , pp. 169-170
    • Pomara, N.1
  • 122
    • 0027509787 scopus 로고
    • Phosphorylated tau epitope of Alzheimer's disease is coupled to axon development in the avian central nervous system
    • doi: 10.1006/exnr.1993.1044
    • Pope, W., Enam, S. A., Bawa, N., Miller, B. E., Ghanbari, H. A., and Klein, W. L. (1993). Phosphorylated tau epitope of Alzheimer's disease is coupled to axon development in the avian central nervous system. Exp. Neurol. 120, 106-113. doi: 10.1006/exnr.1993.1044
    • (1993) Exp. Neurol , vol.120 , pp. 106-113
    • Pope, W.1    Enam, S.A.2    Bawa, N.3    Miller, B.E.4    Ghanbari, H.A.5    Klein, W.L.6
  • 123
    • 0026485673 scopus 로고
    • Role of the target in synapse elimination: Studies in cerebellum of developing lurcher mutants and adult chimeric mice
    • Rabacchi, S. A., Bailly, Y., Delhaye-Bouchaud, N., Herrup, K., and Mariani, J. (1992). Role of the target in synapse elimination: studies in cerebellum of developing lurcher mutants and adult chimeric mice. J. Neurosci. 12, 4712-4720.
    • (1992) J. Neurosci , vol.12 , pp. 4712-4720
    • Rabacchi, S.A.1    Bailly, Y.2    Delhaye-Bouchaud, N.3    Herrup, K.4    Mariani, J.5
  • 125
    • 39749196738 scopus 로고    scopus 로고
    • Whyis the amyloid betapeptide ofAlzheimer's disease neurotoxic?
    • doi: 10.1039/b718601k
    • Rauk, A. (2008).Whyis the amyloid betapeptide ofAlzheimer's disease neurotoxic? Dalton Trans. 1273-1282. doi: 10.1039/b718601k
    • (2008) Dalton Trans , pp. 1273-1282
    • Rauk, A.1
  • 126
    • 34248181511 scopus 로고    scopus 로고
    • Reducing endogenous tau ameliorates amyloid beta-induced deficits in an Alzheimer's disease mouse model
    • doi: 10.1126/science.1141736
    • Roberson, E. D., Scearce-Levie, K., Palop, J. J., Yan, F., Cheng, I. H., Wu, T., et al. (2007). Reducing endogenous tau ameliorates amyloid beta-induced deficits in an Alzheimer's disease mouse model. Science 316, 750-754. doi: 10.1126/science.1141736
    • (2007) Science , vol.316 , pp. 750-754
    • Roberson, E.D.1    Scearce-Levie, K.2    Palop, J.J.3    Yan, F.4    Cheng, I.H.5    Wu, T.6
  • 127
    • 33846991261 scopus 로고    scopus 로고
    • Tau and tauopathies
    • doi: 10.4103/0028-3886.30420
    • Robert, M., and Mathuranath, P. S. (2007). Tau and tauopathies. Neurol. India 55, 11-16. doi: 10.4103/0028-3886.30420
    • (2007) Neurol. India , vol.55 , pp. 11-16
    • Robert, M.1    Mathuranath, P.S.2
  • 128
    • 35348932113 scopus 로고    scopus 로고
    • Transgenic animal models of neurodegenerative diseases and their application to treatment development. Adv. DrugDeliv
    • doi: 10.1016/j.addr.2007.08.013
    • Rockenstein, E., Crews, L., and Masliah, E. (2007a). Transgenic animal models of neurodegenerative diseases and their application to treatment development. Adv. DrugDeliv. Rev. 59, 1093-1102. doi: 10.1016/j.addr.2007.08.013
    • (2007) Rev , vol.59 , pp. 1093-1102
    • Rockenstein, E.1    Crews, L.2    Masliah, E.3
  • 129
    • 33847214486 scopus 로고    scopus 로고
    • Neuroprotective effects of regulators of the glycogen synthase kinase-3beta signaling pathway in a transgenic model of Alzheimer's disease are associated with reduced amyloid precursor protein phosphorylation
    • doi: 10.1523/JNEUROSCI.4321-06.2007
    • Rockenstein, E., Torrance, M., Adame, A., Mante, M., Bar-On, P., Rose, J. B., et al. (2007b). Neuroprotective effects of regulators of the glycogen synthase kinase-3beta signaling pathway in a transgenic model of Alzheimer's disease are associated with reduced amyloid precursor protein phosphorylation. J. Neurosci. 27, 1981-1991. doi: 10.1523/JNEUROSCI.4321-06.2007
    • (2007) J. Neurosci , vol.27 , pp. 1981-1991
    • Rockenstein, E.1    Torrance, M.2    Adame, A.3    Mante, M.4    Bar-On, P.5    Rose, J.B.6
  • 130
    • 27544442991 scopus 로고    scopus 로고
    • Activation of GSK-3 and phosphorylation of CRMP2 in transgenic mice expressing APP intracellular domain
    • doi: 10.1083/jcb.200505078
    • Ryan, K. A., and Pimplikar, S. W. (2005). Activation of GSK-3 and phosphorylation of CRMP2 in transgenic mice expressing APP intracellular domain. J. Cell Biol. 171, 327-335. doi: 10.1083/jcb.200505078
    • (2005) J. Cell Biol , vol.171 , pp. 327-335
    • Ryan, K.A.1    Pimplikar, S.W.2
  • 131
    • 78951495484 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3beta2 has lower phosphorylation activity to tau than glycogen synthase kinase-3beta1
    • doi: 10.1248/bpb.34.146
    • Saeki, K., Machida, M., Kinoshita, Y., Takasawa, R., and Tanuma, S. (2011). Glycogen synthase kinase-3beta2 has lower phosphorylation activity to tau than glycogen synthase kinase-3beta1. Biol. Pharm. Bull. 34, 146-149. doi: 10.1248/bpb.34.146
    • (2011) Biol. Pharm. Bull , vol.34 , pp. 146-149
    • Saeki, K.1    Machida, M.2    Kinoshita, Y.3    Takasawa, R.4    Tanuma, S.5
  • 132
    • 0028021566 scopus 로고
    • The mechanism by which epi-dermal growth factor inhibits glycogen synthase kinase 3 in A431 cells
    • Saito, Y., Vandenheede, J. R., and Cohen, P. (1994). The mechanism by which epi-dermal growth factor inhibits glycogen synthase kinase 3 in A431 cells. Biochem. J. 303(Pt 1), 27-31.
    • (1994) Biochem. J , vol.303 , Issue.PART 1 , pp. 27-31
    • Saito, Y.1    Vandenheede, J.R.2    Cohen, P.3
  • 133
    • 78650757374 scopus 로고    scopus 로고
    • Cholinergic and neuroprotective drugs for the treatment of Alzheimer and neuronal vascular diseases. II. Synthesis, biologi-cal assessment, and molecular modelling of new tacrine analogues from highly substituted 2-aminopyridine-3-carbonitriles
    • doi: 10.1016/j.bmc.2010.11.040
    • Samadi, A., Valderas, C., de los Rios, C., Bastida, A., Chioua, M., Gonzalez-Lafuente, L., et al. (2011). Cholinergic and neuroprotective drugs for the treatment of Alzheimer and neuronal vascular diseases. II. Synthesis, biologi-cal assessment, and molecular modelling of new tacrine analogues from highly substituted 2-aminopyridine-3-carbonitriles. Bioorg. Med. Chem. 19, 122-133. doi: 10.1016/j.bmc.2010.11.040
    • (2011) Bioorg. Med. Chem , vol.19 , pp. 122-133
    • Samadi, A.1    Valderas, C.2    de los Rios, C.3    Bastida, A.4    Chioua, M.5    Gonzalez-Lafuente, L.6
  • 134
    • 0033625696 scopus 로고    scopus 로고
    • GSK3beta-mediated phosphorylation of the microtubule-associated protein 2C (MAP2C) prevents microtubule bundling
    • doi: 10.1078/S0171-9335(04)70028-X
    • Sanchez, C., Perez, M., and Avila, J. (2000). GSK3beta-mediated phosphorylation of the microtubule-associated protein 2C (MAP2C) prevents microtubule bundling. Eur. J. Cell Biol. 79, 252-260. doi: 10.1078/S0171-9335(04)70028-X
    • (2000) Eur. J. Cell Biol , vol.79 , pp. 252-260
    • Sanchez, C.1    Perez, M.2    Avila, J.3
  • 135
    • 22344438508 scopus 로고    scopus 로고
    • Tau suppression in a neurodegenerative mouse model improves memory function
    • doi: 10.1126/science.1113694
    • Santacruz, K., Lewis, J., Spires, T., Paulson, J., Kotilinek, L., Ingelsson, M., et al. Tau suppression in a neurodegenerative mouse model improves memory function. Science 309, 476-481. doi: 10.1126/science.1113694
    • Science , vol.309 , pp. 476-481
    • Santacruz, K.1    Lewis, J.2    Spires, T.3    Paulson, J.4    Kotilinek, L.5    Ingelsson, M.6
  • 136
    • 0032530145 scopus 로고    scopus 로고
    • Phosphorylation of tau at both Thr 231 and Ser 262 is required for maximal inhibition of its binding to microtubules
    • doi: 10.1006/abbi.1998.0813
    • Sengupta, A., Kabat, J., Novak, M., Wu, Q., Grundke-Iqbal, I., and Iqbal, K. (1998). Phosphorylation of tau at both Thr 231 and Ser 262 is required for maximal inhibition of its binding to microtubules. Arch. Biochem. Biophys. 357, 299-309. doi: 10.1006/abbi.1998.0813
    • (1998) Arch. Biochem. Biophys , vol.357 , pp. 299-309
    • Sengupta, A.1    Kabat, J.2    Novak, M.3    Wu, Q.4    Grundke-Iqbal, I.5    Iqbal, K.6
  • 137
    • 33750072653 scopus 로고    scopus 로고
    • Regu-lation of phosphorylation of tau by cyclin-dependent kinase 5 and glyco-gen synthase kinase-3 at substrate level
    • doi: 10.1016/j.febslet.2006.09.060
    • Sengupta, A., Novak, M., Grundke-Iqbal, I., and Iqbal, K. (2006). Regu-lation of phosphorylation of tau by cyclin-dependent kinase 5 and glyco-gen synthase kinase-3 at substrate level. FEBS Lett. 580, 5925-5933. doi: 10.1016/j.febslet.2006.09.060
    • (2006) FEBS Lett , vol.580 , pp. 5925-5933
    • Sengupta, A.1    Novak, M.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 138
    • 68149150844 scopus 로고    scopus 로고
    • A novel GSK-3beta inhibitor reduces Alzheimer's pathol-ogy and rescues neuronal loss in vivo
    • doi: 10.1016/j.nbd.2009.05.025
    • Sereno, L., Coma, M., Rodriguez, M., Sanchez-Ferrer, P., Sanchez, M. B., Gich, L., et al. (2009). A novel GSK-3beta inhibitor reduces Alzheimer's pathol-ogy and rescues neuronal loss in vivo. Neurobiol. Dis. 35, 359-367. doi: 10.1016/j.nbd.2009.05.025
    • (2009) Neurobiol. Dis , vol.35 , pp. 359-367
    • Sereno, L.1    Coma, M.2    Rodriguez, M.3    Sanchez-Ferrer, P.4    Sanchez, M.B.5    Gich, L.6
  • 139
    • 43449128899 scopus 로고    scopus 로고
    • Biochemistry of tau in Alzheimer's disease and related neurological disorders. Expert
    • doi: 10.1586/14789450.5.2.207
    • Sergeant, N., Bretteville, A., Hamdane, M., Caillet-Boudin, M. L., Grognet, P., Bombois, S., et al. (2008). Biochemistry of tau in Alzheimer's disease and related neurological disorders. Expert Rev. Proteomics 5, 207-224. doi: 10.1586/14789450.5.2.207
    • (2008) Rev. Proteomics , vol.5 , pp. 207-224
    • Sergeant, N.1    Bretteville, A.2    Hamdane, M.3    Caillet-Boudin, M.L.4    Grognet, P.5    Bombois, S.6
  • 140
    • 79551510136 scopus 로고    scopus 로고
    • Tau protein is required for amyloid {beta}-induced impair-ment of hippocampal long-term potentiation
    • doi: 10.1523/JNEUROSCI.2610-10.2011
    • Shipton, O. A., Leitz, J. R., Dworzak, J., Acton, C. E., Tunbridge, E. M., Denk, F., et al. (2011). Tau protein is required for amyloid {beta}-induced impair-ment of hippocampal long-term potentiation. J. Neurosci. 31, 1688-1692. doi: 10.1523/JNEUROSCI.2610-10.2011
    • (2011) J. Neurosci , vol.31 , pp. 1688-1692
    • Shipton, O.A.1    Leitz, J.R.2    Dworzak, J.3    Acton, C.E.4    Tunbridge, E.M.5    Denk, F.6
  • 141
    • 79960622123 scopus 로고    scopus 로고
    • GSK3beta overexpression induces neuronal death and a depletion of the neurogenic niches in the dentate gyrus
    • Sirerol-Piquer, M., Gomez-Ramos, P., Hernandez, F., Perez, M., Moran, M. A., Fuster-Matanzo, A., et al. (2011). GSK3beta overexpression induces neuronal death and a depletion of the neurogenic niches in the dentate gyrus. Hippocampus 21, 910-922.
    • (2011) Hippocampus , vol.21 , pp. 910-922
    • Sirerol-Piquer, M.1    Gomez-Ramos, P.2    Hernandez, F.3    Perez, M.4    Moran, M.A.5    Fuster-Matanzo, A.6
  • 142
    • 77958597709 scopus 로고    scopus 로고
    • Evidence that glycogen synthase kinase-3 isoforms have distinct substrate preference in the brain
    • doi: 10.1111/j.1471-4159.2010.06988.x
    • Soutar, M. P., Kim, W. Y., Williamson, R., Peggie, M., Hastie, C. J., McLauch-lan, H., et al. (2010). Evidence that glycogen synthase kinase-3 isoforms have distinct substrate preference in the brain. J. Neurochem. 115, 974-983. doi: 10.1111/j.1471-4159.2010.06988.x
    • (2010) J. Neurochem , vol.115 , pp. 974-983
    • Soutar, M.P.1    Kim, W.Y.2    Williamson, R.3    Peggie, M.4    Hastie, C.J.5    McLauch-Lan, H.6
  • 143
    • 0037056024 scopus 로고    scopus 로고
    • Neonatal neuronal overexpression of glycogen synthase kinase-C. beta reduces brain size in transgenic mice
    • doi: 10.1016/S0306-4522(02)00236-1
    • Spittaels, K., Van den Haute, C., Van Dorpe, J., Terwel, D., Vandezande, K., Lasrado, R., et al. (2002). Neonatal neuronal overexpression of glycogen synthase kinase-C. beta reduces brain size in transgenic mice. Neuroscience 113, 797-808. doi: 10.1016/S0306-4522(02)00236-1
    • (2002) Neuroscience , vol.113 , pp. 797-808
    • Spittaels, K.1    Van den Haute, C.2    van Dorpe, J.3    Terwel, D.4    Vandezande, K.5    Lasrado, R.6
  • 144
    • 84872337044 scopus 로고    scopus 로고
    • Neuroinflam-matory phenotype in early Alzheimer's disease
    • doi: 10.1016/j.neurobiolaging.2012.09.012
    • Sudduth, T. L., Schmitt, F. A., Nelson, P. T., and Wilcock, D. M. (2013). Neuroinflam-matory phenotype in early Alzheimer's disease. Neurobiol. Aging 34, 1051-1059. doi: 10.1016/j.neurobiolaging.2012.09.012
    • (2013) Neurobiol. Aging , vol.34 , pp. 1051-1059
    • Sudduth, T.L.1    Schmitt, F.A.2    Nelson, P.T.3    Wilcock, D.M.4
  • 145
    • 84863057878 scopus 로고    scopus 로고
    • Lithium treatment of APPSwDI/NOS2-/-mice leads to reduced hyperphosphorylated tau, increased amyloid deposition and altered inflammatory phenotype
    • doi: 10.1371/journal.pone. 0031993
    • Sudduth, T. L., Wilson, J. G., Everhart, A., Colton, C. A., and Wilcock, D. M. (2012). Lithium treatment of APPSwDI/NOS2-/-mice leads to reduced hyperphosphorylated tau, increased amyloid deposition and altered inflammatory phenotype. PLoS ONE 7:e31993. doi: 10.1371/journal.pone. 0031993
    • (2012) PLoS ONE , vol.7
    • Sudduth, T.L.1    Wilson, J.G.2    Everhart, A.3    Colton, C.A.4    Wilcock, D.M.5
  • 146
    • 0037023679 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3beta is complexed with tau protein in brain microtubules
    • doi: 10.1074/jbc. M107182200
    • Sun, W., Qureshi, H. Y., Cafferty, P. W., Sobue, K., Agarwal-Mawal, A., et al. (2002). Glycogen synthase kinase-3beta is complexed with tau protein in brain microtubules. J. Biol. Chem. 277, 11933-11940. doi: 10.1074/jbc. M107182200
    • (2002) J. Biol. Chem , vol.277 , pp. 11933-11940
    • Sun, W.1    Qureshi, H.Y.2    Cafferty, P.W.3    Sobue, K.4    Agarwal-Mawal, A.5
  • 147
    • 0028177965 scopus 로고
    • The alpha-isoform of glycogen syn-thase kinase-3 from rabbit skelet al muscle is inactivated by p70 S6 kinase or MAP kinase-activated protein kinase-1 in vitro
    • doi: 10.1016/0014-5793(94)80112-6
    • Sutherland, C., and Cohen, P. (1994). The alpha-isoform of glycogen syn-thase kinase-3 from rabbit skelet al muscle is inactivated by p70 S6 kinase or MAP kinase-activated protein kinase-1 in vitro. FEBS Lett. 338, 37-42. doi: 10.1016/0014-5793(94)80112-6
    • (1994) FEBS Lett , vol.338 , pp. 37-42
    • Sutherland, C.1    Cohen, P.2
  • 148
    • 0027515127 scopus 로고
    • Inactivation of glycogen synthase kinase-3 beta by phosphorylation: New kinase connections in insulin and growth-factor signalling
    • Sutherland, C., Leighton, I. A., and Cohen, P. (1993). Inactivation of glycogen synthase kinase-3 beta by phosphorylation: new kinase connections in insulin and growth-factor signalling. Biochem. J. 296(Pt 1), 15-19.
    • (1993) Biochem. J , vol.296 , Issue.PART 1 , pp. 15-19
    • Sutherland, C.1    Leighton, I.A.2    Cohen, P.3
  • 149
    • 0030044463 scopus 로고    scopus 로고
    • Exposure of rat hippocampal neurons to amyloid beta peptide (25-35) induces the inactivation of phosphatidyl inositol-3 kinase and the activation of tau protein kinase I/glycogen syn-thase kinase-3 beta
    • doi: 10.1016/0304-3940(95) 12257-5
    • Takashima, A., Noguchi, K., Michel, G., Mercken, M., Hoshi, M., Ishiguro, K., et al. (1996a). Exposure of rat hippocampal neurons to amyloid beta peptide (25-35) induces the inactivation of phosphatidyl inositol-3 kinase and the activation of tau protein kinase I/glycogen syn-thase kinase-3 beta. Neurosci. Lett. 203, 33-36. doi: 10.1016/0304-3940(95) 12257-5
    • (1996) Neurosci. Lett , vol.203 , pp. 33-36
    • Takashima, A.1    Noguchi, K.2    Michel, G.3    Mercken, M.4    Hoshi, M.5    Ishiguro, K.6
  • 150
    • 0030583605 scopus 로고    scopus 로고
    • Localization of Alzheimer-associated presenilin 1 in transfected COS-7 cells
    • doi: 10.1006/bbrc.1996.1523
    • Takashima, A., Sato, M., Mercken, M., Tanaka, S., Kondo, S., Honda, T., et al. (1996b). Localization of Alzheimer-associated presenilin 1 in transfected COS-7 cells. Biochem. Biophys. Res. Commun. 227, 423-426. doi: 10.1006/bbrc.1996.1523
    • (1996) Biochem. Biophys. Res. Commun , vol.227 , pp. 423-426
    • Takashima, A.1    Sato, M.2    Mercken, M.3    Tanaka, S.4    Kondo, S.5    Honda, T.6
  • 151
    • 40449098952 scopus 로고    scopus 로고
    • Amyloid activates GSK-3beta to aggravate neuronal tauopa-thy in bigenic mice
    • doi: 10.2353/ajpath.2008. 070904
    • Terwel, D., Muyllaert, D., Dewachter, I., Borghgraef, P., Croes, S., Devijver, H., et al. (2008). Amyloid activates GSK-3beta to aggravate neuronal tauopa-thy in bigenic mice. Am. J. Pathol. 172, 786-798. doi: 10.2353/ajpath.2008. 070904
    • (2008) Am. J. Pathol , vol.172 , pp. 786-798
    • Terwel, D.1    Muyllaert, D.2    Dewachter, I.3    Borghgraef, P.4    Croes, S.5    Devijver, H.6
  • 152
    • 48649088987 scopus 로고    scopus 로고
    • Inhibition of glyco-gen synthase kinase 3 beta attenuates neurocognitive dysfunction resulting from cranial irradiation
    • doi: 10.1158/0008-5472.CAN-07-6327
    • Thotala, D. K., Hallahan, D. E., and Yazlovitskaya, E. M. (2008). Inhibition of glyco-gen synthase kinase 3 beta attenuates neurocognitive dysfunction resulting from cranial irradiation. CancerRes. 68, 5859-5868. doi: 10.1158/0008-5472.CAN-07-6327
    • (2008) CancerRes , vol.68 , pp. 5859-5868
    • Thotala, D.K.1    Hallahan, D.E.2    Yazlovitskaya, E.M.3
  • 153
    • 77249109792 scopus 로고    scopus 로고
    • Activation of Wnt signaling by lithium and rosiglitazone reduced spatial memory impairment and neuro degeneration in brains of an APPswe/PSEN1DeltaE9 mouse model of Alzheimer's disease
    • 228. doi: 10.1038/mp.2009.72
    • Toledo, E. M., and Inestrosa, N. C. (2010). Activation of Wnt signaling by lithium and rosiglitazone reduced spatial memory impairment and neuro degeneration in brains of an APPswe/PSEN1DeltaE9 mouse model of Alzheimer's disease. Mol. Psychiatry 15, 272-285, 228. doi: 10.1038/mp.2009.72
    • (2010) Mol. Psychiatry , vol.15 , pp. 272-285
    • Toledo, E.M.1    Inestrosa, N.C.2
  • 154
    • 36348935683 scopus 로고    scopus 로고
    • Soluble Abeta inhibits specific signal transduction cascades common to the insulin receptor pathway
    • doi: 10.1074/jbc.M610390200
    • Townsend, M., Mehta, T., and Selkoe, D. J. (2007). Soluble Abeta inhibits specific signal transduction cascades common to the insulin receptor pathway. J. Biol. Chem. 282, 33305-33312. doi: 10.1074/jbc.M610390200
    • (2007) J. Biol. Chem , vol.282 , pp. 33305-33312
    • Townsend, M.1    Mehta, T.2    Selkoe, D.J.3
  • 155
    • 34447500594 scopus 로고    scopus 로고
    • GSK3beta activity modifies the localization and function of presenilin 1
    • doi: 10.1074/jbc.M610708200
    • Uemura, K., Kuzuya, A., Shimozono, Y., Aoyagi, N., Ando, K., Shimohama, S., et al. (2007). GSK3beta activity modifies the localization and function of presenilin 1. J. Biol. Chem. 282, 15823-15832. doi: 10.1074/jbc.M610708200
    • (2007) J. Biol. Chem , vol.282 , pp. 15823-15832
    • Uemura, K.1    Kuzuya, A.2    Shimozono, Y.3    Aoyagi, N.4    Ando, K.5    Shimohama, S.6
  • 156
    • 0025717403 scopus 로고
    • Entorhi-nal cortex pathology in Alzheimer's disease
    • doi: 10.1002/hipo.450010102
    • Van Hoesen, G. W., Hyman, B. T., and Damasio, A. R. (1991). Entorhi-nal cortex pathology in Alzheimer's disease. Hippocampus 1, 1-8. doi: 10.1002/hipo.450010102
    • (1991) Hippocampus , vol.1 , pp. 1-8
    • van Hoesen, G.W.1    Hyman, B.T.2    Damasio, A.R.3
  • 157
    • 58149122808 scopus 로고    scopus 로고
    • Coexistences of insulin signaling-related proteins and choline acetyltransferase in neurons
    • doi:10.1016/j.brainres.2008.10.046
    • Wang, H., Wang, R., Zhao, Z., Ji, Z., Xu, S., Holscher, C., et al. (2009). Coexistences of insulin signaling-related proteins and choline acetyltransferase in neurons. Brain Res. 1249, 237-243.doi:10.1016/j.brainres.2008.10.046
    • (2009) Brain Res , vol.1249 , pp. 237-243
    • Wang, H.1    Wang, R.2    Zhao, Z.3    Ji, Z.4    Xu, S.5    Holscher, C.6
  • 158
    • 4744345382 scopus 로고    scopus 로고
    • alpha-Amino-3-hydroxy-5-methylisoxazole-4-propionic acid subtype glutamate receptor (AMPAR) endocytosis is essential for N-methyl-D-aspartate-induced neuronal apoptosis
    • doi: 10.1074/jbc. C400199200
    • Wang, Y., Ju, W., Liu, L., Fam, S., D'Souza, S., Taghibiglou, C., et al. (2004). alpha-Amino-3-hydroxy-5-methylisoxazole-4-propionic acid subtype glutamate receptor (AMPAR) endocytosis is essential for N-methyl-D-aspartate-induced neuronal apoptosis. J. Biol. Chem. 279, 41267-41270. doi: 10.1074/jbc. C400199200
    • (2004) J. Biol. Chem , vol.279 , pp. 41267-41270
    • Wang, Y.1    Ju, W.2    Liu, L.3    Fam, S.4    D'Souza, S.5    Taghibiglou, C.6
  • 159
    • 0442274617 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3beta (GSK3beta) binds to and promotes the actions of p53
    • doi: 10.1074/jbc. M305870200
    • Watcharasit, P., Bijur, G. N., Song, L., Zhu, J., Chen, X., and Jope, R. S. (2003). Glycogen synthase kinase-3beta (GSK3beta) binds to and promotes the actions of p53. J. Biol. Chem. 278, 48872-48879. doi: 10.1074/jbc. M305870200
    • (2003) J. Biol. Chem , vol.278 , pp. 48872-48879
    • Watcharasit, P.1    Bijur, G.N.2    Song, L.3    Zhu, J.4    Chen, X.5    Jope, R.S.6
  • 160
    • 77956198669 scopus 로고    scopus 로고
    • Regulation of AMPA receptor trafficking and function by glycogen synthase kinase 3
    • doi: 10.1074/jbc.M110.121376
    • Wei, J., Liu, W., and Yan, Z. (2010). Regulation of AMPA receptor trafficking and function by glycogen synthase kinase 3. J. Biol. Chem. 285, 26369-26376. doi: 10.1074/jbc.M110.121376
    • (2010) J. Biol. Chem , vol.285 , pp. 26369-26376
    • Wei, J.1    Liu, W.2    Yan, Z.3
  • 161
    • 0027430039 scopus 로고
    • Glycogen synthase kinase-3 is rapidly inac-tivated in response to insulin and phosphorylates eukaryotic initiation factor eIF-2B
    • Welsh, G. I., and Proud, C. G. (1993). Glycogen synthase kinase-3 is rapidly inac-tivated in response to insulin and phosphorylates eukaryotic initiation factor eIF-2B. Biochem. J. 294(Pt 3), 625-629.
    • (1993) Biochem. J , vol.294 , Issue.PART 3 , pp. 625-629
    • Welsh, G.I.1    Proud, C.G.2
  • 162
    • 0019410162 scopus 로고
    • Alzheimer disease: Evidence for selective loss of cholinergic neurons in the nucleus basalis
    • doi: 10.1002/ana.410100203
    • Whitehouse, P. J., Price, D. L., Clark, A. W., Coyle, J. T., and DeLong, M. R. (1981). Alzheimer disease: evidence for selective loss of cholinergic neurons in the nucleus basalis. Ann. Neurol. 10, 122-126. doi: 10.1002/ana.410100203
    • (1981) Ann. Neurol , vol.10 , pp. 122-126
    • Whitehouse, P.J.1    Price, D.L.2    Clark, A.W.3    Coyle, J.T.4    Delong, M.R.5
  • 163
    • 77958568364 scopus 로고    scopus 로고
    • Altered synap-tic plasticity in the mossy fibre pathway of transgenic mice expressing mutant amyloid precursor protein
    • doi: 10.1186/1756-6606-3-32
    • Witton, J., Brown, J. T., Jones, M. W., and Randall, A. D. (2010). Altered synap-tic plasticity in the mossy fibre pathway of transgenic mice expressing mutant amyloid precursor protein. Mol. Brain 3, 32. doi: 10.1186/1756-6606-3-32
    • (2010) Mol. Brain , vol.3 , pp. 32
    • Witton, J.1    Brown, J.T.2    Jones, M.W.3    Randall, A.D.4
  • 164
    • 33646001713 scopus 로고    scopus 로고
    • Threonine 41 in beta-catenin serves as a key phospho-rylation relay residue in beta-catenin degradation
    • doi: 10.1021/bi0601149
    • Wu, G., and He, X. (2006). Threonine 41 in beta-catenin serves as a key phospho-rylation relay residue in beta-catenin degradation. Biochemistry 45, 5319-5323. doi: 10.1021/bi0601149
    • (2006) Biochemistry , vol.45 , pp. 5319-5323
    • Wu, G.1    He, X.2
  • 165
    • 0021049766 scopus 로고
    • Catecholamines and cholinergic enzymes in pre-senile and senile Alzheimer-type dementia and Down's syndrome
    • doi: 10.1016/0006-8993(83)91179-4
    • Yates, C. M., Simpson, J., Gordon, A., Maloney, A. F., Allison, Y., Ritchie, I. M., et al. (1983). Catecholamines and cholinergic enzymes in pre-senile and senile Alzheimer-type dementia and Down's syndrome. Brain Res. 280, 119-126. doi: 10.1016/0006-8993(83)91179-4
    • (1983) Brain Res , vol.280 , pp. 119-126
    • Yates, C.M.1    Simpson, J.2    Gordon, A.3    Maloney, A.F.4    Allison, Y.5    Ritchie, I.M.6
  • 166
    • 84655160766 scopus 로고    scopus 로고
    • Proteolytic processing of Alzheimer's beta-amyloid precursor protein
    • doi: 10.1111/j.1471-4159.2011.07519.x
    • Zhang, H., Ma, Q., Zhang, Y. W., and Xu, H. (2012). Proteolytic processing of Alzheimer's beta-amyloid precursor protein. J. Neurochem. 120(Suppl. 1), 9-21. doi: 10.1111/j.1471-4159.2011.07519.x
    • (2012) J. Neurochem , vol.120 , Issue.SUPPL. 1 , pp. 9-21
    • Zhang, H.1    Ma, Q.2    Zhang, Y.W.3    Xu, H.4
  • 167
    • 13344261322 scopus 로고    scopus 로고
    • Hedgehog-regulated Costal2-kinase complexes control phosphorylation and proteolytic processing of Cubitus interruptus
    • doi: 10.1016/j.devcel.2005.01.001
    • Zhang, W., Zhao, Y., Tong, C., Wang, G., Wang, B., Jia, J., et al. (2005). Hedgehog-regulated Costal2-kinase complexes control phosphorylation and proteolytic processing of Cubitus interruptus. Dev. Cell 8, 267-278. doi: 10.1016/j.devcel.2005.01.001
    • (2005) Dev. Cell , vol.8 , pp. 267-278
    • Zhang, W.1    Zhao, Y.2    Tong, C.3    Wang, G.4    Wang, B.5    Jia, J.6
  • 168
    • 30644474606 scopus 로고    scopus 로고
    • Dis-tinct morphological stages of dentate granule neuron maturation in the adult mouse hippocampus
    • doi: 10.1523/JNEUR0SCI.3648-05.2006
    • Zhao, C., Teng, E. M., Summers, R. G., Ming, G. L. Jr., and Gage, F. H. (2006). Dis-tinct morphological stages of dentate granule neuron maturation in the adult mouse hippocampus. J. Neurosci. 26, 3-11. doi: 10.1523/JNEUR0SCI.3648-05.2006
    • (2006) J. Neurosci , vol.26 , pp. 3-11
    • Zhao, C.1    Teng, E.M.2    Summers, R.G.3    Ming Jr., G.L.4    Gage, F.H.5
  • 169
    • 0035176077 scopus 로고    scopus 로고
    • Binding of the adenomatous polyposis coli protein to microtubules increases microtubule stability and is regulated by GSK3 beta phosphorylation
    • doi: 10.1016/S0960-9822(01)00002-1
    • Zumbrunn, J., Kinoshita, K., Hyman, A. A., and Nathke, I. S. (2001). Binding of the adenomatous polyposis coli protein to microtubules increases microtubule stability and is regulated by GSK3 beta phosphorylation. Curr. Biol. 11, 44-49. doi: 10.1016/S0960-9822(01)00002-1
    • (2001) Curr. Biol , vol.11 , pp. 44-49
    • Zumbrunn, J.1    Kinoshita, K.2    Hyman, A.A.3    Nathke, I.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.