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Volumn 4, Issue , 2011, Pages

Modulation of GSK-3 as a therapeutic strategy on tau pathologies

Author keywords

Alzheimer; GSK 3; Kinases modulation; Tau pathologies

Indexed keywords

AZD 1080; GLYCOGEN SYNTHASE KINASE 3; GLYCOGEN SYNTHASE KINASE 3 INHIBITOR; LITHIUM; MULTIPROTEIN COMPLEX; TIDEGLUSIB; UNCLASSIFIED DRUG; VALPROIC ACID;

EID: 84856619287     PISSN: 16625099     EISSN: None     Source Type: Journal    
DOI: 10.3389/fnmol.2011.00024     Document Type: Review
Times cited : (106)

References (141)
  • 1
    • 0030978351 scopus 로고    scopus 로고
    • Beta-catenin is a target for the ubiquitin-proteasome pathway
    • Aberle, H., Bauer, A., Stappert, J., Kispert, A., and Kemler, R. (1997). beta-catenin is a target for the ubiquitin-proteasome pathway. EMBOJ. 16,3797-3804.
    • (1997) EMBOJ , vol.16 , pp. 3797-3804
    • Aberle, H.1    Bauer, A.2    Stappert, J.3    Kispert, A.4    Kemler, R.5
  • 2
    • 0030590875 scopus 로고    scopus 로고
    • Molecular basis for the substrate specificity of protein kinase B; comparison with MAPKAP kinase-1 and p70 S6 kinase
    • Alessi, D. R., Caudwell, F. B., And-jelkovic, M., Hemmings, B. A., and Cohen, P. (1996). Molecular basis for the substrate specificity of protein kinase B; comparison with MAPKAP kinase-1 and p70 S6 kinase. FEBS Lett. 399, 333-338.
    • (1996) FEBS Lett , vol.399 , pp. 333-338
    • Alessi, D.R.1    Caudwell, F.B.2    -Jelkovic, M.3    Hemmings, B.A.4    Cohen, P.5
  • 3
    • 33745024475 scopus 로고    scopus 로고
    • Polymerization of hyperphosphorylated tau into filaments eliminates its inhibitory activity
    • Alonso Adel, C., Li, B., Grundke-Iqbal, I., and Iqbal, K. (2006). Polymerization of hyperphosphorylated tau into filaments eliminates its inhibitory activity. Proc. Natl. Acad. Sci. U.S.A. 103, 8864-8869.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 8864-8869
    • Alonso Adel, C.1    Li, B.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 5
    • 0036571011 scopus 로고    scopus 로고
    • Axin-mediated CKI phosphorylation of beta-catenin at Ser 45: A molecular switch for the Wnt pathway
    • Amit, S., Hatzubai, A., Birman, Y., Andersen, J. S., Ben-Shushan, E., Mann, M., Ben-Neriah, Y., and Alka-lay, I. (2002). Axin-mediated CKI phosphorylation of beta-catenin at Ser 45: a molecular switch for the Wnt pathway. Genes Dev. 16, 1066-1076.
    • (2002) Genes Dev , vol.16 , pp. 1066-1076
    • Amit, S.1    Hatzubai, A.2    Birman, Y.3    Ersen, J.S.4    Ben-Shushan, E.5    Mann, M.6    Ben-Neriah, Y.7    Alka-Lay, I.8
  • 6
    • 1642289188 scopus 로고    scopus 로고
    • Role of tau protein inboth physiological andpatho-logical conditions.
    • Avila, J., Lucas, J. J., Perez, M., and Hernandez, F. (2004). Role of tau protein inboth physiological andpatho-logical conditions. Physiol. Rev. 84, 361-384.
    • (2004) Physiol. Rev , vol.84 , pp. 361-384
    • Avila, J.1    Lucas, J.J.2    Perez, M.3    Hernandez, F.4
  • 8
    • 34548036227 scopus 로고    scopus 로고
    • Tau-mediated neurodegeneration in Alzheimer’s disease and related disorders.
    • Ballatore, C., Lee, V. M., and Tro-Janowski, J. Q. (2007).Tau-mediated neurodegeneration in Alzheimer’s disease and related disorders. Nat. Rev. Neurosci. 8, 663-672.
    • (2007) Nat. Rev. Neurosci , vol.8 , pp. 663-672
    • Ballatore, C.1    Lee, V.M.2    Tro-Janowski, J.Q.3
  • 10
    • 0034718421 scopus 로고    scopus 로고
    • Regulation and localization of tyrosine216 phosphorylation of glycogen synthase kinase-3beta in cellular and animal models of neuronal degeneration
    • Bhat, R. V., Shanley, J., Correll, M. P., Fieles, W. E., Keith, R. A., Scott, C. W., and Lee, C. M. (2000). Regulation and localization of tyrosine216 phosphorylation of glycogen synthase kinase-3beta in cellular and animal models of neuronal degeneration. Proc. Natl. Acad. Sci. U.S.A. 97, 11074-11079.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 11074-11079
    • Bhat, R.V.1    Shanley, J.2    Correll, M.P.3    Fieles, W.E.4    Keith, R.A.5    Scott, C.W.6    Lee, C.M.7
  • 11
    • 0442290275 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 beta is highly activated in nuclei and mitochondria
    • Bijur, G. N., and Jope, R. S. (2003). Glycogen synthase kinase-3 beta is highly activated in nuclei and mitochondria. Neuroreport 14, 2415-2419.
    • (2003) Neuroreport , vol.14 , pp. 2415-2419
    • Bijur, G.N.1    Jope, R.S.2
  • 12
    • 0033850407 scopus 로고    scopus 로고
    • Tau protein isoforms, phosphorylation and role in neurodegenerative disorders. Brain Res. Brain Res
    • Buee, L., Bussiere, T., Buee-Scherrer, V., Delacourte, A., and Hof, P. R. (2000). Tau protein isoforms, phosphorylation and role in neurodegenerative disorders. Brain Res. Brain Res. Rev. 33, 95-130.
    • (2000) Rev , vol.33 , pp. 95-130
    • Buee, L.1    Bussiere, T.2    Buee-Scherrer, V.3    Delacourte, A.4    Hof, P.R.5
  • 13
    • 34250818767 scopus 로고    scopus 로고
    • Lithium reduces tau phosphorylation but not A beta or working memory deficits in a transgenic model with both plaques and tangles
    • 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 transgenic model with both plaques and tangles. Am. J. Pathol. 170, 1669-1675.
    • (2007) Am. J. Pathol , vol.170 , pp. 1669-1675
    • Caccamo, A.1    Oddo, S.2    Tran, L.X.3    Laferla, F.M.4
  • 14
    • 1642375658 scopus 로고    scopus 로고
    • Estradiol inhibits GSK3 and regulates interaction of estrogen receptors, GSK3, and beta-catenin in the hippocampus.
    • Cardona-Gomez, P., Perez, M., Avila, J., Garcia-Segura, L. M., and Wan-dosell, F. (2004). Estradiol inhibits GSK3 and regulates interaction of estrogen receptors, GSK3, and beta-catenin in the hippocampus. Mol. Cell. Neurosci. 25, 363-373.
    • (2004) Mol. Cell. Neurosci , vol.25 , pp. 363-373
    • Cardona-Gomez, P.1    Perez, M.2    Avila, J.3    Garcia-Segura, L.M.4    Wan-Dosell, F.5
  • 15
    • 77749243065 scopus 로고    scopus 로고
    • The neuron-specific isoform of GSK-3b2 is required for axon growth
    • Castano, Z., Gordon-Weeks, P., and Kypta, R. (2010). The neuron-specific isoform of GSK-3b2 is required for axon growth. J. Neu-rochem. 113, 117-130.
    • (2010) J. Neu-Rochem , vol.113 , pp. 117-130
    • Castano, Z.1    Gordon-Weeks, P.2    Kypta, R.3
  • 18
    • 0033611663 scopus 로고    scopus 로고
    • The Croonian Lecture 1998. Identification ofaprotein kinase cascade of major importance in insulin signal transduction
    • Cohen, P. (1999). The Croonian Lecture 1998. Identification ofaprotein kinase cascade of major importance in insulin signal transduction. Philos. Trans. R. Soc. Lond. B Biol. Sci. 354, 485-495.
    • (1999) Philos. Trans. R. Soc. Lond. B Biol. Sci , vol.354 , pp. 485-495
    • Cohen, P.1
  • 20
    • 1642494586 scopus 로고    scopus 로고
    • Further evidence that the tyrosine phosphorylation of glycogen synthase kinase-3 (GSK3) in mammalian cells is an autophosphorylation event
    • Cole, A., Frame, S., and Cohen, P. (2004). Further evidence that the tyrosine phosphorylation of glycogen synthase kinase-3 (GSK3) in mammalian cells is an autophosphorylation event. Biochem. J. 377, 249-255.
    • (2004) Biochem. J , vol.377 , pp. 249-255
    • Cole, A.1    Frame, S.2    Cohen, P.3
  • 21
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediated byprotein kinase B
    • Cross, D. A., Alessi, D. R., Cohen, P., Andjelkovich, M., and Hemmings, B. A. (1995). Inhibition of glycogen synthase kinase-3 by insulin mediated byprotein kinase B. Nature 378, 785-789.
    • (1995) Nature , vol.378 , pp. 785-789
    • Cross, D.A.1    Alessi, D.R.2    Cohen, P.3    Jelkovich, M.4    Hemmings, B.A.5
  • 22
    • 0035875098 scopus 로고    scopus 로고
    • Crystal structure of glycogen synthase kinase 3 beta: Structural basis for phosphate-primed substrate specificity and autoinhibition
    • Dajani, R., Fraser, E., Roe, S. M., Young, N., Good, V., Dale, T. C., and Pearl, L. H. (2001). Crystal structure of glycogen synthase kinase 3 beta: structural basis for phosphate-primed substrate specificity and autoinhibition. Cell 105, 721-732.
    • (2001) Cell , vol.105 , pp. 721-732
    • Dajani, R.1    Fraser, E.2    Roe, S.M.3    Young, N.4    Good, V.5    Dale, T.C.6    Pearl, L.H.7
  • 23
    • 31844447759 scopus 로고    scopus 로고
    • In vivo regulation of GSK3 phosphorylation by cholinergic and NMDA receptors.
    • De Sarno, P., Bijur, G. N., Zmijew-ska, A. A., Li, X., and Jope, R. S. (2006). In vivo regulation of GSK3 phosphorylation by cholinergic and NMDA receptors. Neurobiol. Aging 27,413-422.
    • (2006) Neurobiol. Aging , vol.27 , pp. 413-422
    • De Sarno, P.1    Bijur, G.N.2    Zmijew-Ska, A.A.3    Li, X.4    Jope, R.S.5
  • 26
    • 78951488216 scopus 로고    scopus 로고
    • The purinergic receptor P2 x 7 triggers alpha-secretase-dependent processing of the amyloid precursor protein
    • Delarasse, C., Auger, R., Gonnord, P., Fontaine, B., and Kanellopoulos, J. M. (2010). The purinergic receptor P2 x 7 triggers alpha-secretase-dependent processing of the amyloid precursor protein. J. Biol. Chem. 286, 2596-2606.
    • (2010) J. Biol. Chem , vol.286 , pp. 2596-2606
    • Delarasse, C.1    Auger, R.2    Gonnord, P.3    Fontaine, B.4    Kanellopoulos, J.M.5
  • 27
    • 0032530482 scopus 로고    scopus 로고
    • Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase
    • Delcommenne, M., Tan, C., Gray, V., Rue, L., Woodgett, J., and Ded-har, S. (1998). Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase. Proc. Natl. Acad. Sci. U.S.A. 95, 11211-11216.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 11211-11216
    • Delcommenne, M.1    Tan, C.2    Gray, V.3    Rue, L.4    Woodgett, J.5    Ded-Har, S.6
  • 30
    • 0037092042 scopus 로고    scopus 로고
    • An inactive pool of GSK-3 at the leading edge of growth cones is implicated in Semaphorin 3A signaling
    • Eickholt, B. J., Walsh, F. S., and Doherty, P. (2002). An inactive pool of GSK-3 at the leading edge of growth cones is implicated in Semaphorin 3A signaling. J. Cell Biol. 157, 211-217.
    • (2002) J. Cell Biol , vol.157 , pp. 211-217
    • Eickholt, B.J.1    Walsh, F.S.2    Doherty, P.3
  • 32
    • 33845530335 scopus 로고    scopus 로고
    • Chronic lithium administration to FTDP-17 tau and GSK-3beta overexpressing mice prevents tau hyperphosphorylation and neurofibrillary tangle formation, but pre-formed neurofibrillarytangles do not revert
    • Engel, T., Goni-Oliver, P., Lucas, J. J., Avila, J., and Hernandez, F. (2006a). Chronic lithium administration to FTDP-17 tau and GSK-3beta overexpressing mice prevents tau hyperphosphorylation and neurofibrillary tangle formation, but pre-formed neurofibrillarytangles do not revert. J. Neurochem. 99, 1445-1455.
    • (2006) J. Neurochem , vol.99 , pp. 1445-1455
    • Engel, T.1    Goni-Oliver, P.2    Lucas, J.J.3    Avila, J.4    Hernandez, F.5
  • 33
    • 33646922314 scopus 로고    scopus 로고
    • Full reversal of Alzheimer’s disease-like phenotype in a mouse model with conditional overexpression of glycogen synthase kinase-3
    • Engel, T., Hernandez, F., Avila, J., and Lucas, J. J. (2006b). Full reversal of Alzheimer’s disease-like phenotype in a mouse model with conditional overexpression of glycogen synthase kinase-3. J. Neurosci. 26, 5083-5090.
    • (2006) J. Neurosci , vol.26 , pp. 5083-5090
    • Engel, T.1    Hernandez, F.2    Avila, J.3    Lucas, J.J.4
  • 34
    • 12944250922 scopus 로고    scopus 로고
    • Phosphorylation and inactivation of glycogen synthase kinase 3 by protein kinaseA
    • Fang, X., Yu, S. X., Lu, Y., Bast, R. C. Jr., Woodgett, J. R., and Mills, G. B. (2000). Phosphorylation and inactivation of glycogen synthase kinase 3 by protein kinaseA. Proc. Natl. Acad. Sci. U.S.A. 97, 11960-11965.
    • (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, J.R.5    Mills, G.B.6
  • 35
    • 0037013313 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 beta mutagenesis identifies a common binding domain for GBP and Axin
    • Ferkey, D. M., and Kimelman, D. (2002). Glycogen synthase kinase-3 beta mutagenesis identifies a common binding domain for GBP and Axin. J. Biol. Chem. 277, 16147-16152.
    • (2002) J. Biol. Chem , vol.277 , pp. 16147-16152
    • Ferkey, D.M.1    Kimelman, D.2
  • 36
    • 79955546563 scopus 로고    scopus 로고
    • Disease-modifying properties of long-term lithium treatment for amnesic milsd cognitive impair-ment:Randomised controlled trial
    • Forleza, O., Diniz, B., Radanovic, M., Santos, F., Talib, L., and Gattaz, W. (2011). Disease-modifying properties of long-term lithium treatment for amnesic milsd cognitive impair-ment:randomised controlled trial. Br. J. Psychol. 198,351-356.
    • (2011) Br. J. Psychol , vol.198 , pp. 351-356
    • Forleza, O.1    Diniz, B.2    Radanovic, M.3    Santos, F.4    Talib, L.5    Gattaz, W.6
  • 37
    • 0035477020 scopus 로고    scopus 로고
    • GSK3 takes centre stage more than 20 years after its discovery
    • Frame, S., and Cohen, P. (2001). GSK3 takes centre stage more than 20 years after its discovery. Biochem. J. 359, 1-16.
    • (2001) Biochem. J , vol.359 , pp. 1-16
    • Frame, S.1    Cohen, P.2
  • 38
    • 0034969088 scopus 로고    scopus 로고
    • Acommon phosphate binding site explains the unique substrate specificity of GSK3 and its inactivation by phosphorylation.
    • Frame, S., Cohen, P., and Biondi, R. M. (2001).Acommon phosphate binding site explains the unique substrate specificity of GSK3 and its inactivation by phosphorylation. Mol. Cell 7, 1321-1327.
    • (2001) Mol. Cell , vol.7 , pp. 1321-1327
    • Frame, S.1    Cohen, P.2    Biondi, R.M.3
  • 40
    • 34547699174 scopus 로고    scopus 로고
    • Pose prediction accuracy in docking studies and enrichment of actives in the active site of GSK-3beta
    • Gadakar, P., Phukan, S., Dattatreya, P., and Balaji, V. (2007). Pose prediction accuracy in docking studies and enrichment of actives in the active site of GSK-3beta. J. Chem. Inf. Model. 47, 446-459.
    • (2007) J. Chem. Inf. Model , vol.47 , pp. 446-459
    • Gadakar, P.1    Phukan, S.2    Dattatreya, P.3    Balaji, V.4
  • 41
    • 34047093866 scopus 로고    scopus 로고
    • GSK3 alpha and GSK3 beta are necessary for axon formation
    • Garrido, J. J., Simon, D., Varea, O., and Wandosell, F. (2007). GSK3 alpha and GSK3 beta are necessary for axon formation. FEBS Lett. 581, 1579-1586.
    • (2007) FEBS Lett , vol.581 , pp. 1579-1586
    • Garrido, J.J.1    Simon, D.2    Varea, O.3    Wandosell, F.4
  • 42
    • 0027214404 scopus 로고
    • Phos-phoprotein phosphatase activities in Alzheimer disease brain
    • Gong, C. X., Singh, T. J., Grundke-Iqbal, I., and Iqbal, K. (1993). Phos-phoprotein phosphatase activities in Alzheimer disease brain. J. Neu-rochem. 61, 921-927.
    • (1993) J. Neu-Rochem , vol.61 , pp. 921-927
    • Gong, C.X.1    Singh, T.J.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 43
    • 34547929974 scopus 로고    scopus 로고
    • N-terminal cleavage of GSK-3 by calpain: A new form of GSK-3 regulation
    • Goni-Oliver, P., Lucas, J. J., Avila, J., and Hernandez, F. (2007). N-terminal cleavage of GSK-3 by calpain: a new form of GSK-3 regulation. J. Biol. Chem. 282,22406-22413.
    • (2007) J. Biol. Chem , vol.282 , pp. 22406-22413
    • Goni-Oliver, P.1    Lucas, J.J.2    Avila, J.3    Hernandez, F.4
  • 46
    • 0036788036 scopus 로고    scopus 로고
    • The Wnt signaling pathway in bipolar disorder
    • Gould, T. D., and Manji, H. K. (2002). The Wnt signaling pathway in bipolar disorder. Neuroscientist 8, 497-511.
    • (2002) Neuroscientist , vol.8 , pp. 497-511
    • Gould, T.D.1    Manji, H.K.2
  • 47
    • 0034859101 scopus 로고    scopus 로고
    • The multifaceted roles of glycogen synthase kinase 3beta in cellular signaling. Prog
    • Grimes, C. A., and Jope, R. S. (2001). The multifaceted roles of glycogen synthase kinase 3beta in cellular signaling. Prog. Neurobiol. 65, 391-426.
    • (2001) Neurobiol , vol.65 , pp. 391-426
    • Grimes, C.A.1    Jope, R.S.2
  • 49
    • 0026487365 scopus 로고
    • Glycogen synthase kinase-3 induces Alzheimer’s disease-like phosphorylation of tau: Generation of paired helical filament epitopes and neuronal localisation of the kinase.
    • Hanger, D. P., Hughes, K., Woodgett, J. R., Brion, J. P., and Anderton, B. H. (1992). Glycogen synthase kinase-3 induces Alzheimer’s disease-like phosphorylation of tau: generation of paired helical filament epitopes and neuronal localisation of the kinase. Neurosci. Lett. 147, 58-62.
    • (1992) Neurosci.Lett , vol.147 , pp. 58-62
    • Hanger, D.P.1    Hughes, K.2    Woodgett, J.R.3    Brion, J.P.4    Anderton, B.H.5
  • 50
    • 0029992869 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3 alpha and 3 beta do not colocalize with neurofibrillary tangles.
    • Harr, S. D., Hollister, R. D., and Hyman, B. T. (1996). Glycogen synthase kinase 3 alpha and 3 beta do not colocalize with neurofibrillary tangles. Neurobiol. Aging 17, 343-348.
    • (1996) Neurobiol. Aging , vol.17 , pp. 343-348
    • Harr, S.D.1    Hollister, R.D.2    Hyman, B.T.3
  • 51
    • 0032492954 scopus 로고    scopus 로고
    • Downregulation of beta-catenin by human Axin and its association with the APC tumor suppressor, beta-catenin and GSK3 beta
    • Hart, M. J., de los Santos, R., Albert, I. N., Rubinfeld, B., and Polakis, P. (1998). Downregulation of beta-catenin by human Axin and its association with the APC tumor suppressor, beta-catenin and GSK3 beta. Curr. Biol. 8, 573-581.
    • (1998) Curr. Biol , vol.8 , pp. 573-581
    • Hart, M.J.1    De Los Santos, R.2    Albert, I.N.3    Rubinfeld, B.4    Polakis, P.5
  • 52
    • 0034804850 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3beta is tyrosine phosphorylated by PYK2.
    • Hartigan, J. A., Xiong, W. C., and Johnson, G. V. (2001). Glycogen synthase kinase 3beta is tyrosine phosphorylated by PYK2. Biochem. Biophys. Res. Commun. 284, 485-489.
    • (2001) Biochem. Biophys. Res. Commun , vol.284 , pp. 485-489
    • Hartigan, J.A.1    Xiong, W.C.2    Johnson, G.V.3
  • 53
    • 0035967897 scopus 로고    scopus 로고
    • Regulation of GSK-3: A cellular multiprocessor
    • Harwood, A. J. (2001). Regulation of GSK-3: a cellular multiprocessor. Cell 105,821-824.
    • (2001) Cell , vol.105 , pp. 821-824
    • Harwood, A.J.1
  • 54
    • 0020379073 scopus 로고
    • Successful treatment of dementia with lithium
    • Havens, W. W. II, and Cole. J. (1982). Successful treatment of dementia with lithium. J. Clin. Psychopharma-col. 2, 71-72.
    • (1982) J. Clin. Psychopharma-Col , vol.2 , pp. 71-72
    • Havens, W.W.1
  • 55
    • 49149116213 scopus 로고    scopus 로고
    • Tau aggregates and tau pathology
    • Hernandez, F., and Avila, J. (2008). Tau aggregates and tau pathology. J. Alzheimers Dis. 14, 449-452.
    • (2008) J. Alzheimers Dis , vol.14 , pp. 449-452
    • Hernandez, F.1    Avila, J.2
  • 59
    • 0027255817 scopus 로고
    • Glycogen synthase kinase 3 beta is identical to tau protein kinase I generating several epitopes of paired helical filaments
    • Ishiguro, K., Shiratsuchi, A., Sato, S., Omori, A., Arioka, M., Kobayashi, S., Uchida, T., and Imahori, K. (1993). Glycogen synthase kinase 3 beta is identical to tau protein kinase I generating several epitopes of paired helical filaments. FEBS Lett. 325, 167-172.
    • (1993) FEBS Lett , vol.325 , pp. 167-172
    • Ishiguro, K.1    Shiratsuchi, A.2    Sato, S.3    Omori, A.4    Arioka, M.5    Kobayashi, S.6    Uchida, T.7    Imahori, K.8
  • 60
    • 0029590306 scopus 로고
    • Specific modulation of ectodermal cell fates in Xenopus embryos by glycogen synthase kinase
    • Itoh, K., Tang, T. L., Neel, B. G., and Sokol, S. Y. (1995). Specific modulation of ectodermal cell fates in Xenopus embryos by glycogen synthase kinase. Development 121, 3979-3988.
    • (1995) Development , vol.121 , pp. 3979-3988
    • Itoh, K.1    Tang, T.L.2    Neel, B.G.3    Sokol, S.Y.4
  • 61
    • 29244456731 scopus 로고    scopus 로고
    • Long-term treatment with novel glycogen synthase kinase-3 inhibitor improves glucose homeostasis in ob/ob mice: Molecular characterization in liver and muscle
    • Kaidanovich-Beilin, O., and Eldar-Finkelman, H. (2006). Long-term treatment with novel glycogen synthase kinase-3 inhibitor improves glucose homeostasis in ob/ob mice: molecular characterization in liver and muscle. J. Pharmacol. Exp. Ther. 316, 17-24.
    • (2006) J. Pharmacol. Exp. Ther , vol.316 , pp. 17-24
    • Kaidanovich-Beilin, O.1    Eldar-Finkelman, H.2
  • 62
    • 68949160008 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3beta is activated by matrix metalloproteinase-2 mediated proteolysis in cardiomyoblasts.
    • Kandasamy, A. D., and Schulz, R. (2009). Glycogen synthase kinase-3beta is activated by matrix metalloproteinase-2 mediated proteolysis in cardiomyoblasts. Cardiovasc. Res. 83, 698-706.
    • (2009) Cardiovasc. Res , vol.83 , pp. 698-706
    • Kandasamy, A.D.1    Schulz, R.2
  • 63
    • 0036775935 scopus 로고    scopus 로고
    • Receptor-dependent and tyrosine phosphatase-mediated inhibition of GSK3 regulates cell fate choice.
    • Kim, L., Harwood, A., and Kimmel, A. R. (2002). Receptor-dependent and tyrosine phosphatase-mediated inhibition of GSK3 regulates cell fate choice. Dev. Cell 3, 523-532.
    • (2002) Dev.Cell , vol.3 , pp. 523-532
    • Kim, L.1    Harwood, A.2    Kimmel, A.R.3
  • 64
    • 0032734021 scopus 로고    scopus 로고
    • The novel tyrosine kinase ZAK1 activates GSK3 to direct cell fate specification
    • Kim, L., Liu, J., and Kimmel, A. R. (1999). The novel tyrosine kinase ZAK1 activates GSK3 to direct cell fate specification. Cell 99, 399-408.
    • (1999) Cell , vol.99 , pp. 399-408
    • Kim, L.1    Liu, J.2    Kimmel, A.R.3
  • 65
    • 0029776032 scopus 로고    scopus 로고
    • A molecular mechanism for the effect of lithium on development
    • 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.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 8455-8459
    • Klein, P.S.1    Melton, D.A.2
  • 66
    • 0032955426 scopus 로고    scopus 로고
    • Insulin transiently increases tau phosphorylation: Involvement of glycogen synthase kinase-3beta and Fyn tyrosine kinase
    • Lesort, M., Jope, R. S., and Johnson, G. V. (1999). Insulin transiently increases tau phosphorylation: involvement of glycogen synthase kinase-3beta and Fyn tyrosine kinase. J. Neurochem. 72, 576-584.
    • (1999) J. Neurochem , vol.72 , pp. 576-584
    • Lesort, M.1    Jope, R.S.2    Johnson, G.V.3
  • 67
    • 34248570473 scopus 로고    scopus 로고
    • 5-HT4 receptor and Alzheimer’s disease: The amyloid connection. Exp
    • Lezoualc’h, F. (2007). 5-HT4 receptor and Alzheimer’s disease: the amyloid connection. Exp. Neurol. 205, 325-329.
    • (2007) Neurol , vol.205 , pp. 325-329
    • Lezoualc’H, F.1
  • 68
    • 0033517102 scopus 로고    scopus 로고
    • Axin and Frat1 interact with dvl and GSK, bridging Dvl to GSK in Wnt-mediated regulation of LEF-1
    • Li, L., Yuan, H., Weaver, C. D., Mao, J., Farr, G. H. III, Sussman, D. J., Jonkers, J., Kimelman, D., and Wu, D. (1999). Axin and Frat1 interact with dvl and GSK, bridging Dvl to GSK in Wnt-mediated regulation of LEF-1. EMBO J. 18, 4233-4240.
    • (1999) EMBO J , vol.18 , pp. 4233-4240
    • Li, L.1    Yuan, H.2    Weaver, C.D.3    Mao, J.4    Farr, G.H.5    Sussman, D.J.6    Jonkers, J.7    Kimelman, D.8    Wu, D.9
  • 69
    • 0036103182 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3beta, mood stabilizers, and neuroprotection
    • Li, X., Bijur, G. N., and Jope, R. S. (2002). Glycogen synthase kinase-3beta, mood stabilizers, and neuroprotection. Bipolar Disord. 4, 137-144.
    • (2002) Bipolar Disord , vol.4 , pp. 137-144
    • Li, X.1    Bijur, G.N.2    Jope, R.S.3
  • 70
    • 28844449366 scopus 로고    scopus 로고
    • The inhibition of glycogen synthase kinase 3beta by a metabotropic glutamate receptor 5 mediated pathway confers neuroprotection to Abeta peptides
    • Liu, F., Gong, X., Zhang, G., Marquis, K., Reinhart, P., and Andree, T. H. (2005). The inhibition of glycogen synthase kinase 3beta by a metabotropic glutamate receptor 5 mediated pathway confers neuroprotection to Abeta peptides. J. Neurochem. 95, 1363-1372.
    • (2005) J. Neurochem , vol.95 , pp. 1363-1372
    • Liu, F.1    Gong, X.2    Zhang, G.3    Marquis, K.4    Reinhart, P.5    Andree, T.H.6
  • 71
    • 0346434153 scopus 로고    scopus 로고
    • Overactivation of glycogen synthase kinase-3 by inhibition of phosphoinositol-3 kinase and protein kinase C leads to hyperphosphorylation of tau and impairment of spatial memory
    • Liu, S. J., Zhang, A. H., Li, H. L., Wang, Q., Deng, H. M., Netzer, W. J., Xu, H., andWang, J. Z. (2003). Overactivation of glycogen synthase kinase-3 by inhibition of phosphoinositol-3 kinase and protein kinase C leads to hyperphosphorylation of tau and impairment of spatial memory. J. Neurochem. 87, 1333-1344.
    • (2003) J. Neurochem , vol.87 , pp. 1333-1344
    • Liu, S.J.1    Zhang, A.H.2    Li, H.L.3    Wang, Q.4    Deng, H.M.5    Netzer, W.J.6    Xu, H.7    Wang, J.Z.8
  • 73
    • 0031469645 scopus 로고    scopus 로고
    • WNT-7a induces axonal remodeling and increases synapsin I levels in cerebellar neurons.
    • Lucas, F. R., and Salinas, P. C. (1997). WNT-7a induces axonal remodeling and increases synapsin I levels in cerebellar neurons. Dev. Biol. 192, 31-44.
    • (1997) Dev. Biol , vol.192 , pp. 31-44
    • Lucas, F.R.1    Salinas, P.C.2
  • 74
    • 0035863188 scopus 로고    scopus 로고
    • Decreased nuclear beta-catenin, tau hyperphosphorylation and neurodegeneration in GSK-3beta conditional transgenic mice
    • Lucas, J. J., Hernandez, F., Gomez-Ramos, P., Moran, M. A., Hen, R., and Avila, J. (2001a). Decreased nuclear beta-catenin, tau hyperphosphorylation and neurodegeneration in GSK-3beta conditional transgenic mice. EMBO J. 20, 27-39.
    • (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
  • 75
    • 0035863188 scopus 로고    scopus 로고
    • Decreased nuclear beta-catenin, tau hyperphosphorylation and neurodegeneration in GSK-3beta conditional transgenic mice
    • Lucas, J. J., Hernandez, F., Gomez-Ramos, P., Moran, M. A., Hen, R., and Avila, J. (2001b). Decreased nuclear beta-catenin, tau hyperphosphorylation and neurodegeneration in GSK-3beta conditional transgenic mice. EMBO J. 20, 27-39.
    • (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
  • 79
    • 0037005956 scopus 로고    scopus 로고
    • P24, a glycogen synthase kinase 3 (GSK 3) inhibitor. Biochim. Biophys
    • Martin, C. P., Vazquez, J., Avila, J., and Moreno, F. J. (2002). P24, a glycogen synthase kinase 3 (GSK 3) inhibitor. Biochim. Biophys. Acta 1586, 113-122.
    • (2002) Acta , vol.1586 , pp. 113-122
    • Martin, C.P.1    Vazquez, J.2    Avila, J.3    Moreno, F.J.4
  • 80
    • 79956298780 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 regulates endoplasmic reticulum (ER) stress-induced CHOP expression in neuronal cells. Exp
    • Meares, G. P., Mines, M. A., Beurel, E., Eom, T. Y., Song, L., Zmijew-ska, A. A., and Jope, R. S. (2011). Glycogen synthase kinase-3 regulates endoplasmic reticulum (ER) stress-induced CHOP expression in neuronal cells. Exp. Cell Res. 317, 1621-1628.
    • (2011) Cell Res , vol.317 , pp. 1621-1628
    • Meares, G.P.1    Mines, M.A.2    Beurel, E.3    Eom, T.Y.4    Song, L.5    Zmijew-Ska, A.A.6    Jope, R.S.7
  • 81
    • 77957954068 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 (GSK-3) inhibitors for the treatment of Alzheimer’s disease
    • Medina, M., and Avila, J. (2010). Glycogen synthase kinase-3 (GSK-3) inhibitors for the treatment of Alzheimer’s disease. Curr. Pharm. Des. 16, 2790-2798.
    • (2010) Curr. Pharm. Des , vol.16 , pp. 2790-2798
    • Medina, M.1    Avila, J.2
  • 82
    • 46749128127 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 (GSK-3) inhibitors reach the clinic
    • Medina, M., and Castro, A. (2008). Glycogen synthase kinase-3 (GSK-3) inhibitors reach the clinic. Curr. Opin. Drug Discov. Dev. 11, 533-543.
    • (2008) Curr. Opin. Drug Discov. Dev , vol.11 , pp. 533-543
    • Medina, M.1    Castro, A.2
  • 83
    • 79959222357 scopus 로고    scopus 로고
    • Deconstructing GSK-3: The fine regulation of its activity
    • Medina, M., and Wandosell, F. (2011). Deconstructing GSK-3: the fine regulation of its activity. Int. J. Alzheimers Dis. 2011, 479249.
    • (2011) Int. J. Alzheimers Dis , vol.2011
    • Medina, M.1    Wandosell, F.2
  • 84
    • 17844399257 scopus 로고    scopus 로고
    • Interdependence of oestrogen and insulinlike growth factor-I in the brain: Potential for analysing neuroprotec-tive mechanisms
    • Mendez, P., Azcoitia, I., and Garcia-Segura, L. M. (2005). Interdependence of oestrogen and insulinlike growth factor-I in the brain: potential for analysing neuroprotec-tive mechanisms. J. Endocrinol. 185, 11-17.
    • (2005) J. Endocrinol , vol.185 , pp. 11-17
    • Mendez, P.1    Azcoitia, I.2    Garcia-Segura, L.M.3
  • 85
    • 4344584730 scopus 로고    scopus 로고
    • WNT and beta-catenin signalling: Diseases and therapies. Nat
    • Moon, R. T., Kohn, A. D., De Ferrari, G. V., and Kaykas, A. (2004). WNT and beta-catenin signalling: diseases and therapies. Nat. Rev. Genet. 5, 691-701.
    • (2004) Rev. Genet , vol.5 , pp. 691-701
    • Moon, R.T.1    Kohn, A.D.2    De Ferrari, G.V.3    Kaykas, A.4
  • 86
    • 0035983533 scopus 로고    scopus 로고
    • Alternative splicing isoform of tau protein kinase I/glycogen synthase kinase 3beta
    • Mukai, F., Ishiguro, K., Sano, Y., and Fujita, S. C. (2002). Alternative splicing isoform of tau protein kinase I/glycogen synthase kinase 3beta. J. Neurochem. 81, 1073-1083.
    • (2002) J. Neurochem , vol.81 , pp. 1073-1083
    • Mukai, F.1    Ishiguro, K.2    Sano, Y.3    Fujita, S.C.4
  • 87
    • 0031567583 scopus 로고    scopus 로고
    • Lithium inhibits Alzheimer’s disease-like tau protein phosphorylation in neurons
    • Munoz-Montano, J. R., Moreno, F. J., Avila, J., and Diaz-Nido, J. (1997). Lithium inhibits Alzheimer’s disease-like tau protein phosphorylation in neurons. FEBS Lett. 411, 183-188.
    • (1997) FEBS Lett , vol.411 , pp. 183-188
    • Munoz-Montano, J.R.1    Moreno, F.J.2    Avila, J.3    Diaz-Nido, J.4
  • 89
    • 1542358895 scopus 로고    scopus 로고
    • PAR-1 kinase plays an initiator role in a temporally ordered phosphorylation process that confers tau toxicity in Drosophila
    • Nishimura, I., Yang, Y., and Lu, B. (2004). PAR-1 kinase plays an initiator role in a temporally ordered phosphorylation process that confers tau toxicity in Drosophila. Cell 116, 671-682.
    • (2004) Cell , vol.116 , pp. 671-682
    • Nishimura, I.1    Yang, Y.2    Lu, B.3
  • 92
    • 0032493729 scopus 로고    scopus 로고
    • Role of glycogen synthase kinase-3 in the phosphatidylinositol 3- Kinase/Akt cell survival pathway
    • Pap, M., and Cooper, G. M. (1998). Role of glycogen synthase kinase-3 in the phosphatidylinositol 3- Kinase/Akt cell survival pathway. J. Biol. Chem. 273, 19929-19932.
    • (1998) J. Biol. Chem , vol.273 , pp. 19929-19932
    • Pap, M.1    Cooper, G.M.2
  • 93
    • 34548232341 scopus 로고    scopus 로고
    • Structure-based approaches in the design of GSK-3 selective inhibitors
    • Patel, D. S., Dessalew, N., Iqbal, P., and Bharatam, P. V. (2007). Structure-based approaches in the design of GSK-3 selective inhibitors. Curr. Protein Pept. Sci. 8, 352-364.
    • (2007) Curr. Protein Pept. Sci , vol.8 , pp. 352-364
    • Patel, D.S.1    Dessalew, N.2    Iqbal, P.3    Bharatam, P.V.4
  • 94
    • 40449100017 scopus 로고    scopus 로고
    • Dopamine receptor activation is required for corticostriatal spike-timing-dependent plasticity
    • Pawlak, V., and Kerr, J. N. (2008). Dopamine receptor activation is required for corticostriatal spike-timing-dependent plasticity. J. Neu-rosci. 28, 2435-2446.
    • (2008) J. Neu-Rosci , vol.28 , pp. 2435-2446
    • Pawlak, V.1    Kerr, J.N.2
  • 95
    • 0030635495 scopus 로고    scopus 로고
    • Distribution, levels, and activity of glycogen synthase kinase-3 in the Alzheimer disease brain
    • Pei, J. J., Tanaka, T., Tung, Y. C., Braak, E., Iqbal, K., and Grundke-Iqbal, I. (1997). Distribution, levels, and activity of glycogen synthase kinase-3 in the Alzheimer disease brain. J. Neuropathol. Exp. Neurol. 56, 70-78.
    • (1997) J. Neuropathol. Exp. Neurol , vol.56 , pp. 70-78
    • Pei, J.J.1    Tanaka, T.2    Tung, Y.C.3    Braak, E.4    Iqbal, K.5    Grundke-Iqbal, I.6
  • 97
    • 0242720372 scopus 로고    scopus 로고
    • Chronic lithium treatment decreases mutant tau protein aggregation in a transgenic mouse model
    • Perez, M., Hernandez, F., Lim, F., Diaz-Nido, J., and Avila, J. (2003a). Chronic lithium treatment decreases mutant tau protein aggregation in a transgenic mouse model. J. Alzheimers Dis. 5, 301-308.
    • (2003) J. Alzheimers Dis , vol.5 , pp. 301-308
    • Perez, M.1    Hernandez, F.2    Lim, F.3    Diaz-Nido, J.4    Avila, J.5
  • 98
    • 0038292054 scopus 로고    scopus 로고
    • Prion peptide induces neuronal cell death through a pathway involving glycogen synthase kinase 3
    • Perez, M., Rojo, A. I., Wandosell, F., Diaz-Nido, J., and Avila, J. (2003b). Prion peptide induces neuronal cell death through a pathway involving glycogen synthase kinase 3. Biochem. J. 372, 129-136.
    • (2003) Biochem. J , vol.372 , pp. 129-136
    • Perez, M.1    Rojo, A.I.2    Wandosell, F.3    Diaz-Nido, J.4    Avila, J.5
  • 99
    • 0038187674 scopus 로고    scopus 로고
    • GSK-3alpharegu-lates production of Alzheimer’s disease amyloid-beta peptides
    • Phiel, C. J., Wilson, C. A., Lee, V. M., and Klein, P. S. (2003). GSK-3alpharegu-lates production of Alzheimer’s disease amyloid-beta peptides. Nature 423, 435-439.
    • (2003) Nature , vol.423 , pp. 435-439
    • Phiel, C.J.1    Wilson, C.A.2    Lee, V.M.3    Klein, P.S.4
  • 101
    • 0038811796 scopus 로고    scopus 로고
    • Insulin mimetic action of synthetic phosphorylated peptide inhibitors of glycogen synthase kinase-3
    • 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.
    • (2003) J. Pharmacol. Exp. Ther , vol.305 , pp. 974-980
    • Plotkin, B.1    Kaidanovich, O.2    Talior, I.3    Eldar-Finkelman, H.4
  • 102
    • 17644410079 scopus 로고    scopus 로고
    • Phosphothreonine-212 of Alzheimer abnormally hyper-phosphorylated tau is a preferred substrate of protein phosphatase-1. Neurochem
    • Rahman, A., Grundke-Iqbal, I., and Iqbal, K. (2005). Phosphothreonine-212 of Alzheimer abnormally hyper-phosphorylated tau is a preferred substrate of protein phosphatase-1. Neurochem. Res. 30, 277-287.
    • (2005) Res , vol.30 , pp. 277-287
    • Rahman, A.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 103
    • 0017861963 scopus 로고
    • The binding of lithium and of anionic metabolites to phospho-glucomutase.
    • Ray, W. J. Jr., Szymanki, E. S., and Ng, L. (1978). The binding of lithium and of anionic metabolites to phospho-glucomutase. Biochim. Biophys. Acta 522, 434-442.
    • (1978) Biochim. Biophys. Acta , vol.522 , pp. 434-442
    • Ray, W.J.1    Szymanki, E.S.2    Ng, L.3
  • 104
    • 16644381829 scopus 로고    scopus 로고
    • Wnt signaling through Dishevelled, Rac and JNK regulates dendritic development. Nat
    • Rosso, S. B., Sussman, D., Wynshaw-Boris, A., and Salinas, P. C. (2005). Wnt signaling through Dishevelled, Rac and JNK regulates dendritic development. Nat. Neurosci. 8, 34-42.
    • (2005) Neurosci , vol.8 , pp. 34-42
    • Rosso, S.B.1    Sussman, D.2    Wynshaw-Boris, A.3    Salinas, P.C.4
  • 105
    • 34548012115 scopus 로고    scopus 로고
    • GSK-3 is a viable potential target for therapeutic intervention in bipolar disorder.
    • Rowe, M. K., Wiest, C., and Chuang, D. M. (2007). GSK-3 is a viable potential target for therapeutic intervention in bipolar disorder. Neurosci. Biobehav. Rev. 31, 920-931.
    • (2007) Neurosci. Biobehav. Rev , vol.31 , pp. 920-931
    • Rowe, M.K.1    Wiest, C.2    Chuang, D.M.3
  • 106
    • 0027418602 scopus 로고
    • Drosophila shaggy kinase and rat glycogen synthase kinase-3 have conserved activities and act downstream of Notch
    • Ruel, L., Bourouis, M., Heitzler, P., Pan-tesco, V., and Simpson, P. (1993). Drosophila shaggy kinase and rat glycogen synthase kinase-3 have conserved activities and act downstream of Notch. Nature 362, 557-560.
    • (1993) Nature , vol.362 , pp. 557-560
    • Ruel, L.1    Bourouis, M.2    Heitzler, P.3    Pan-Tesco, V.4    Simpson, P.5
  • 107
    • 0019025978 scopus 로고
    • Glycogen synthase from rabbit skeletal muscle. Amino acid sequence at the sites phosphorylated by glycogen synthase kinase-3, and extension of the N-terminal sequence containing the site phosphorylated by phosphory-lase kinase
    • Rylatt, D. B., Aitken, A., Bilham, T., Condon, G. D., Embi, N., and Cohen, P. (1980). Glycogen synthase from rabbit skeletal muscle. Amino acid sequence at the sites phosphorylated by glycogen synthase kinase-3, and extension of the N-terminal sequence containing the site phosphorylated by phosphory-lase kinase. Eur. J. Biochem. 107, 529-537.
    • (1980) Eur. J. Biochem , vol.107 , pp. 529-537
    • Rylatt, D.B.1    Aitken, A.2    Bilham, T.3    Condon, G.D.4    Embi, N.5    Cohen, P.6
  • 109
    • 0037162094 scopus 로고    scopus 로고
    • Regulation of neuronal cytoskeleton by lysophospha-tidic acid: Role of GSK-3. Biochim. Biophys
    • Sayas, C. L., Avila, J., and Wan-dosell, F. (2002). Regulation of neuronal cytoskeleton by lysophospha-tidic acid: role of GSK-3. Biochim. Biophys. Acta 1582,144-153.
    • (2002) Acta , vol.1582 , pp. 144-153
    • Sayas, C.L.1    Avila, J.2    Wan-Dosell, F.3
  • 110
    • 0033601337 scopus 로고    scopus 로고
    • The neurite retraction induced by lysophosphatidic acid increases Alzheimer’s disease-like Tau phosphorylation
    • Sayas, C. L., Moreno-Flores, M. T., Avila, J., and Wandosell, F. (1999). The neurite retraction induced by lysophosphatidic acid increases Alzheimer’s disease-like Tau phosphorylation. J. Biol. Chem. 274, 37046-37052.
    • (1999) J. Biol. Chem , vol.274 , pp. 37046-37052
    • Sayas, C.L.1    Moreno-Flores, M.T.2    Avila, J.3    Wandosell, F.4
  • 111
    • 0037413694 scopus 로고    scopus 로고
    • Gene structure and alternative splicing of glycogen synthase kinase 3 beta (GSK-3beta) in neural and non-neural tissues
    • Schaffer, B., Wiedau-Pazos, M., and Geschwind, D. H. (2003). Gene structure and alternative splicing of glycogen synthase kinase 3 beta (GSK-3beta) in neural and non-neural tissues. Gene 302, 73-81.
    • (2003) Gene , vol.302 , pp. 73-81
    • Schaffer, B.1    Wiedau-Pazos, M.2    Geschwind, D.H.3
  • 112
    • 0031052339 scopus 로고    scopus 로고
    • Potentiation of GSK-3-catalyzed Alzheimer-like phosphorylation of human tau by cdk5. Mol. Cell
    • Sengupta, A., Wu, Q., Grundke-Iqbal, I., Iqbal, K., and Singh, T. J. (1997). Potentiation of GSK-3-catalyzed Alzheimer-like phosphorylation of human tau by cdk5. Mol. Cell. Biochem. 167, 99-105.
    • (1997) Biochem , vol.167 , pp. 99-105
    • Sengupta, A.1    Wu, Q.2    Grundke-Iqbal, I.3    Iqbal, K.4    Singh, T.J.5
  • 113
    • 0035037851 scopus 로고    scopus 로고
    • The mechanism of lithium action: State of the art, ten years later. Prog. Neuropsy-chopharmacol. Biol
    • Shaldubina, A., Agam, G., and Bel-maker, R. H. (2001). The mechanism of lithium action: state of the art, ten years later. Prog. Neuropsy-chopharmacol. Biol. Psychiatry 25, 855-866.
    • (2001) Psychiatry , vol.25 , pp. 855-866
    • Shaldubina, A.1    Agam, G.2    Bel-Maker, R.H.3
  • 114
    • 9244249219 scopus 로고    scopus 로고
    • APC and GSK-3beta are involved in mPar3 targeting to the nascent axon and establishment of neuronal polarity
    • Shi, S. H., Cheng, T., Jan, L. Y., and Jan, Y. N. (2004). APC and GSK-3beta are involved in mPar3 targeting to the nascent axon and establishment of neuronal polarity. Curr. Biol. 14, 2025-2032.
    • (2004) Curr. Biol , vol.14 , pp. 2025-2032
    • Shi, S.H.1    Cheng, T.2    Jan, L.Y.3    Jan, Y.N.4
  • 115
    • 38849099839 scopus 로고    scopus 로고
    • Pharmacological inhibition of GSK-3 is not strictly correlated with a decrease in tyrosine phosphorylation of residues 216/279
    • Simon, D., Benitez, M. J., Gimenez-Cassina, A., Garrido, J. J., Bhat, R. V., Diaz-Nido, J., and Wandosell, F. (2008). Pharmacological inhibition of GSK-3 is not strictly correlated with a decrease in tyrosine phosphorylation of residues 216/279. J. Neurosci. Res. 86, 668-674.
    • (2008) J. Neurosci. Res , vol.86 , pp. 668-674
    • Simon, D.1    Benitez, M.J.2    Gimenez-Cassina, A.3    Garrido, J.J.4    Bhat, R.V.5    Diaz-Nido, J.6    Wandosell, F.7
  • 116
    • 79551679637 scopus 로고    scopus 로고
    • Overcoming cell death and tau phosphorylation mediated by PI3K-inhibition: A cell assay to measure neuroprotection. CNSNeurol. Disord
    • Simon, D., Medina, M., Avila, J., and Wandosell, F. (2011). Overcoming cell death and tau phosphorylation mediated by PI3K-inhibition: a cell assay to measure neuroprotection. CNSNeurol. Disord. DrugTargets 10, 208-214.
    • (2011) Drugtargets , vol.10 , pp. 208-214
    • Simon, D.1    Medina, M.2    Avila, J.3    Wandosell, F.4
  • 117
    • 79955385225 scopus 로고    scopus 로고
    • The role of GSK3 in presynap-tic function
    • Smillie, K. J., and Cousin, M. A. (2011). The role of GSK3 in presynap-tic function. Int. J. Alzheimers Dis. 263-673.
    • (2011) Int. J. Alzheimers Dis , pp. 263-673
    • Smillie, K.J.1    Cousin, M.A.2
  • 119
    • 0027960448 scopus 로고
    • Mitogen inactivation of glycogen synthase kinase-3 beta in intact cells via serine 9 phosphorylation
    • Stambolic, V., and Woodgett, J. R. (1994). Mitogen inactivation of glycogen synthase kinase-3 beta in intact cells via serine 9 phosphorylation. Biochem. J. 303(Pt 3), 701-704.
    • (1994) Biochem. J , vol.303 , pp. 701-704
    • Stambolic, V.1    Woodgett, J.R.2
  • 120
    • 12844282895 scopus 로고    scopus 로고
    • FRAT-2 preferentially increases glycogen synthase kinase 3 beta-mediated phosphorylation of primed sites, which results in enhanced tau phosphorylation
    • Stoothoff, W. H., Cho, J. H., McDonald, R. P., and Johnson, G. V. (2005). FRAT-2 preferentially increases glycogen synthase kinase 3 beta-mediated phosphorylation of primed sites, which results in enhanced tau phosphorylation. J. Biol. Chem. 280, 270-276.
    • (2005) J. Biol. Chem , vol.280 , pp. 270-276
    • Stoothoff, W.H.1    Cho, J.H.2    McDonald, R.P.3    Johnson, G.V.4
  • 121
    • 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, 15-19.
    • (1993) Biochem. J , vol.296 , pp. 15-19
    • Sutherland, C.1    Leighton, I.A.2    Cohen, P.3
  • 122
    • 2942589223 scopus 로고    scopus 로고
    • Increased MAP kinase activity in Alzheimer’s and Down syndrome but not in schizophrenia human brain
    • Swatton, J. E., Sellers, L. A., Faull, R. L., Holland, A., Iritani, S., and Bahn, S. (2004). Increased MAP kinase activity in Alzheimer’s and Down syndrome but not in schizophrenia human brain. Eur. J. Neurosci. 19, 2711-2719.
    • (2004) Eur. J. Neurosci , vol.19 , pp. 2711-2719
    • Swatton, J.E.1    Sellers, L.A.2    Faull, R.L.3    Holland, A.4    Iritani, S.5    Bahn, S.6
  • 123
    • 0028357787 scopus 로고
    • Localization and developmental changes of tau protein kinase I/glycogen synthase kinase-3 beta in rat brain
    • Takahashi, M., Tomizawa, K., Kato, R., Sato, K., Uchida, T., Fujita, S. C., and Imahori, K. (1994). Localization and developmental changes of tau protein kinase I/glycogen synthase kinase-3 beta in rat brain. J. Neurochem. 63, 245-255.
    • (1994) J. Neurochem , vol.63 , pp. 245-255
    • Takahashi, M.1    Tomizawa, K.2    Kato, R.3    Sato, K.4    Uchida, T.5    Fujita, S.C.6    Imahori, K.7
  • 124
    • 0031695652 scopus 로고    scopus 로고
    • Activation of tau protein kinase I/glycogen synthase kinase-3beta by amyloid beta peptide (25-35) enhances phosphorylation of tau in hippocampal neurons.
    • Takashima, A., Honda, T., Yasutake, K., Michel, G., Murayama, O., Murayama, M., Ishiguro, K., and Yamaguchi, H. (1998). Activation of tau protein kinase I/glycogen synthase kinase-3beta by amyloid beta peptide (25-35) enhances phosphorylation of tau in hippocampal neurons. Neurosci. Res. 31, 317-323.
    • (1998) Neurosci. Res , vol.31 , pp. 317-323
    • Takashima, A.1    Honda, T.2    Yasutake, K.3    Michel, G.4    Murayama, O.5    Murayama, M.6    Ishiguro, K.7    Yamaguchi, H.8
  • 127
    • 33745229378 scopus 로고    scopus 로고
    • Lithium and dementia: A preliminary study. Prog. Neuropsychopharmacol.
    • Terao, T., Nakano, H., Inoue, Y., Okamoto, T., Nakamura, J., and Iwata, N. (2006). Lithium and dementia: a preliminary study. Prog. Neuropsychopharmacol. Biol. Psychiatry 30, 1125-1128.
    • (2006) Biol. Psychiatry , vol.30 , pp. 1125-1128
    • Terao, T.1    Nakano, H.2    Inoue, Y.3    Okamoto, T.4    Nakamura, J.5    Iwata, N.6
  • 129
    • 0030049359 scopus 로고    scopus 로고
    • Lysophos-phatidic acid-induced neurite retraction in PC12 cells: Neurite-protective effects of cyclic AMP signaling
    • Tigyi, G., Fischer, D. J., Sebok, A., Marshall, F., Dyer, D. L., and Miledi, R. (1996). Lysophos-phatidic acid-induced neurite retraction in PC12 cells: neurite-protective effects of cyclic AMP signaling. J. Neurochem. 66, 549-558.
    • (1996) J. Neurochem , vol.66 , pp. 549-558
    • Tigyi, G.1    Fischer, D.J.2    Sebok, A.3    Marshall, F.4    Dyer, D.L.5    Miledi, R.6
  • 130
    • 27744491956 scopus 로고    scopus 로고
    • Pathological tau: A loss of normal function or a gain in toxicity? Nat
    • Trojanowski, J. Q., and Lee, V.M. (2005). Pathological tau: a loss of normal function or a gain in toxicity? Nat. Neurosci. 8, 1136-1137.
    • (2005) Neurosci , vol.8 , pp. 1136-1137
    • Trojanowski, J.Q.1    Lee, V.M.2
  • 131
    • 33745853091 scopus 로고    scopus 로고
    • Presenilin-1 is an unprimed glycogen synthase kinase-3beta substrate
    • Twomey, C., and McCarthy, J. V. (2006). Presenilin-1 is an unprimed glycogen synthase kinase-3beta substrate. FEBSLett. 580,4015-4020.
    • (2006) Febslett , vol.580 , pp. 4015-4020
    • Twomey, C.1    McCarthy, J.V.2
  • 133
    • 0028176021 scopus 로고
    • Glycogen synthase kinase-3 beta is a dual specificity kinase differentially regulated by tyrosine and serine/threonine phosphorylation
    • Wang, Q. M., Fiol, C. J., DePaoli-Roach, A. A., and Roach, P. J. (1994). Glycogen synthase kinase-3 beta is a dual specificity kinase differentially regulated by tyrosine and serine/threonine phosphorylation. J. Biol. Chem. 269, 14566-14574.
    • (1994) J. Biol. Chem , vol.269 , pp. 14566-14574
    • Wang, Q.M.1    Fiol, C.J.2    Depaoli-Roach, A.A.3    Roach, P.J.4
  • 136
    • 0025286104 scopus 로고
    • Molecular cloning and expression of glycogen synthase kinase-3/factorA
    • Woodgett, J. R. (1990). Molecular cloning and expression of glycogen synthase kinase-3/factorA. EMBO J. 9, 2431-2438.
    • (1990) EMBO J , vol.9 , pp. 2431-2438
    • Woodgett, J.R.1
  • 137
    • 74849138924 scopus 로고    scopus 로고
    • Regulation of protein stability by GSK3 mediated phosphorylation
    • Xu, C., Kim, N. G., and Gumbiner, B. M. (2009). Regulation of protein stability by GSK3 mediated phosphorylation. Cell Cycle 8, 4032-4039.
    • (2009) Cell Cycle , vol.8 , pp. 4032-4039
    • Xu, C.1    Kim, N.G.2    Gumbiner, B.M.3
  • 138
    • 0029036695 scopus 로고
    • Definition of a metal-dependent/Li(+)-inhibited phosphomonoesterase protein family based upon a conserved three-dimensional core structure
    • York, J. D., Ponder, J. W., and Majerus, P. W. (1995). Definition of a metal-dependent/Li(+)-inhibited phosphomonoesterase protein family based upon a conserved three-dimensional core structure. Proc. Natl. Acad. Sci. U.S.A. 92, 5149-5153.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 5149-5153
    • York, J.D.1    Ponder, J.W.2    Majerus, P.W.3
  • 139
    • 0032511194 scopus 로고    scopus 로고
    • GBP, an inhibitor of GSK-3, is implicated in Xenopus development and oncogenesis
    • Yost, C., Farr, G. H. III, Pierce, S. B., Fer-key, D. M., Chen, M. M., and Kimel-Man, D. (1998). GBP, an inhibitor of GSK-3, is implicated in Xenopus development and oncogenesis. Cell 93, 1031-1041.
    • (1998) Cell , vol.93 , pp. 1031-1041
    • Yost, C.1    Farr, G.2    Pierce, S.B.3    Fer-Key, D.M.4    Chen, M.M.5    Kimel-Man, D.6
  • 140
    • 61349097283 scopus 로고    scopus 로고
    • Developmental regulation of tau phosphorylation, tau kinases, and tau phosphatases
    • Yu, Y., Run, X., Liang, Z., Li, Y., Liu, F., Liu, Y., Iqbal, K., Grundke-Iqbal, I., and Gong, C. X. (2009). Developmental regulation of tau phosphorylation, tau kinases, and tau phosphatases. J. Neurochem. 108, 1480-1494.
    • (2009) J. Neurochem , vol.108 , pp. 1480-1494
    • Yu, Y.1    Run, X.2    Liang, Z.3    Li, Y.4    Liu, F.5    Liu, Y.6    Iqbal, K.7    Grundke-Iqbal, I.8    Gong, C.X.9
  • 141
    • 2942735115 scopus 로고    scopus 로고
    • NGF-induced axon growth is mediated by localized inactivation of GSK-3beta and functions of the microtubule plus end binding protein APC
    • Zhou, F. Q., Zhou, J., Dedhar, S., Wu, Y. H., and Snider, W. D. (2004). NGF-induced axon growth is mediated by localized inactivation of GSK-3beta and functions of the microtubule plus end binding protein APC. Neuron 42, 897-912.
    • (2004) Neuron , vol.42 , pp. 897-912
    • Zhou, F.Q.1    Zhou, J.2    Dedhar, S.3    Wu, Y.H.4    Snider, W.D.5


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