메뉴 건너뛰기




Volumn 10, Issue 5, 2010, Pages 703-710

Role of glycogen synthase kinase-3 in Alzheimer's disease pathogenesis and glycogen synthase kinase-3 inhibitors

Author keywords

Alzheimer's disease; Amyloid peptide; GSK 3; Lithium; Tau

Indexed keywords

AMYLOID BETA PROTEIN; AR A 014418; GLYCOGEN SYNTHASE KINASE 3; GLYCOGEN SYNTHASE KINASE 3 INHIBITOR; INDIRUBIN; LITHIUM; MALEIMIDE DERIVATIVE; NP 12; TAU PROTEIN; THIADIAZOLIDINONE DERIVATIVE; THIAZOLE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 77951875902     PISSN: 14737175     EISSN: 17448360     Source Type: Journal    
DOI: 10.1586/ern.10.40     Document Type: Review
Times cited : (115)

References (103)
  • 1
    • 33646906138 scopus 로고
    • On certain peculiar diseases of old age
    • • First step in the study of the disease
    • Alzheimer A. [On certain peculiar diseases of old age]. Arch. Psychiatr. Nervenkr. Z. Gesamte Neurol. Psychiatr. 4, 356-386 (1911). • First step in the study of the disease.
    • (1911) Arch. Psychiatr. Nervenkr. Z. Gesamte Neurol. Psychiatr , vol.4 , pp. 356-386
    • Alzheimer, A.1
  • 2
    • 0020072221 scopus 로고
    • Alzheimer's disease and senile dementia: Loss of neurons in the basal forebrain
    • Whitehouse PJ, Price DL, Struble RG, Clark AW, Coyle JT, Delon MM. Alzheimer's disease and senile dementia: loss of neurons in the basal forebrain. Science 215 (4537), 1237-1239 (1982). •• Key paper describing the main composition of senile plaques. (Pubitemid 12106486)
    • (1982) Science , vol.215 , Issue.4537 , pp. 1237-1239
    • Whitehouse, P.J.1    Price, D.L.2    Struble, R.G.3
  • 3
    • 0022156464 scopus 로고
    • Neuronal origin of a cerebral amyloid: Neurofbrillary tangles of alzheimer's disease contain the same protein as the amyloid of plaque cores and blood vessels
    • •• Key paper describing the main composition of senile plaques
    • Masters CL, Multhaup G, Simms G, Pottgiesser J, Martins RN, Beyreuther K. Neuronal origin of a cerebral amyloid: neurofbrillary tangles of Alzheimer's disease contain the same protein as the amyloid of plaque cores and blood vessels. EMBO J. 4 (11), 2757-2763 (1985). •• Key paper describing the main composition of senile plaques.
    • (1985) EMBO J. , vol.4 , Issue.11 , pp. 2757-2763
    • Masters, C.L.1    Multhaup, G.2    Simms, G.3    Pottgiesser, J.4    Martins, R.N.5    Beyreuther, K.6
  • 4
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner GG, Wong CC. Alzheimer's disease: initial report of the purifcation and characterization of a novel cerebrovascular amyloid protein. Biochem. Biophys. Res. Commun. 120 (3), 885-890 (1984). (Pubitemid 14104991)
    • (1984) Biochemical and Biophysical Research Communications , vol.120 , Issue.3 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 5
    • 0031921466 scopus 로고    scopus 로고
    • Mutant genes in familial Alzheimer's disease and transgenic models
    • DOI 10.1146/annurev.neuro.21.1.479
    • Price DL, Sisodia SS. Mutant genes in familial Alzheimer's disease and transgenic models. Annu. Rev. Neurosci. 21, 479-505 (1998). (Pubitemid 28150671)
    • (1998) Annual Review of Neuroscience , vol.21 , pp. 479-505
    • Price, D.L.1    Sisodia, S.S.2
  • 6
    • 0022744803 scopus 로고
    • Abnormal phosphorylation of the microtubule-associated protein τ (tau) in Alzheimer cytoskeletal pathology
    • Grundke-Iqbal I, Iqbal K, Tung YC, Quinlan M, Wisniewski HM, Binder LL. Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskelet al. pathology. Proc. Natl Acad. Sci. USA 83 (13), 4913-4917 (1986). •• Key paper describing phosphorylated tau in Alzheimer's disease (AD). (Pubitemid 16075509)
    • (1986) Proceedings of the National Academy of Sciences of the United States of America , vol.83 , Issue.13 , pp. 44913-4917
    • Grundke-Iqbal, I.1    Iqbal, K.2    Tung, Y.-C.3
  • 7
    • 0028899714 scopus 로고
    • Proline-directed and non-proline-directed phosphorylation of phf-tau
    • Morishima-Kawashima M, Hasegawa M, Takio K et al. Proline-directed and non-proline-directed phosphorylation of PHF-tau. J. Biol. Chem. 270 (2), 823-829 (1995).
    • (1995) J. Biol. Chem. , vol.270 , Issue.2 , pp. 823-829
    • Morishima-Kawashima, M.1    Hasegawa, M.2    Takio, K.3
  • 8
    • 61849088424 scopus 로고    scopus 로고
    • Tau phosphorylation: The therapeutic challenge for neurodegenerative disease
    • Hanger DP, Anderton BH, Noble W. Tau phosphorylation: the therapeutic challenge for neurodegenerative disease. Trends Mol. Med. 15 (3), 112-119 (2009).
    • (2009) Trends Mol. Med. , vol.15 , Issue.3 , pp. 112-119
    • Hanger, D.P.1    Anderton, B.H.2    Noble, W.3
  • 9
    • 77249165544 scopus 로고    scopus 로고
    • Importance of tyr310 residue in the third repeat of microtubule binding domain for flament formation of tau protein
    • Nishiura C, Takeuchi K, Minoura K et al. Importance of Tyr310 residue in the third repeat of microtubule binding domain for flament formation of tau protein. J. Biochem. 147 (3), 405-414 (2009).
    • (2009) J. Biochem. , vol.147 , Issue.3 , pp. 405-414
    • Nishiura, C.1    Takeuchi, K.2    Minoura, K.3
  • 10
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • DOI 10.1126/science.1072994
    • Hardy J, Selkoe DD. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297 (5580), 353-356 (2002). • Main hypothesis for the origin of AD. (Pubitemid 34790756)
    • (2002) Science , vol.297 , Issue.5580 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 11
    • 0033537921 scopus 로고    scopus 로고
    • Enhancement of amyloid β 42 secretion by 28 different presenilin 1 mutations of familial Alzheimer's disease
    • DOI 10.1016/S0304-3940(99)00187-1, PII S0304394099001871
    • Murayama O, Tomita T, Nihonmatsu N et al. Enhancement of amyloid b 42 secretion by 28 different presenilin 1 mutations of familial Alzheimer's disease. Neurosci. Lett. 265 (1), 61-63 (1999). (Pubitemid 29210198)
    • (1999) Neuroscience Letters , vol.265 , Issue.1 , pp. 61-63
    • Murayama, O.1    Tomita, T.2    Nihonmatsu, N.3    Murayama, M.4    Sun, X.5    Honda, T.6    Iwatsubo, T.7    Takashima, A.8
  • 14
    • 33745140951 scopus 로고    scopus 로고
    • Tau phosphorylation and aggregation in Alzheimer's disease pathology
    • DOI 10.1016/j.febslet.2006.02.067, PII S0014579306002705
    • Avila, J. Tau phosphorylation and aggregation in Alzheimer's disease pathology. FEBS Lett. 580 (12), 2922-2927 (2006). (Pubitemid 44250900)
    • (2006) FEBS Letters , vol.580 , Issue.12 , pp. 2922-2927
    • Avila, J.1
  • 15
    • 33747862732 scopus 로고    scopus 로고
    • Extracellular tau is toxic to neuronal cells
    • DOI 10.1016/j.febslet.2006.07.078, PII S001457930600946X
    • Gomez-Ramos A, Diaz-Hernandez M, Cuadros R, Hernandez F, Avila J. Extracellular tau is toxic to neuronal cells. FEBS Lett. 580 (20), 4842-4850 (2006). (Pubitemid 44286844)
    • (2006) FEBS Letters , vol.580 , Issue.20 , pp. 4842-4850
    • Gomez-Ramos, A.1    Diaz-Hernandez, M.2    Cuadros, R.3    Hernandez, F.4    Avila, J.5
  • 16
    • 67650077008 scopus 로고    scopus 로고
    • Transmission and spreading of tauopathy in transgenic mouse brain
    • Clavaguera F, Bolmont T, Crowther RA et al. Transmission and spreading of tauopathy in transgenic mouse brain. Nat. Cell Biol. 11 (7), 909-913 (2009).
    • (2009) Nat. Cell. Biol. , vol.11 , Issue.7 , pp. 909-913
    • Clavaguera, F.1    Bolmont, T.2    Crowther, R.A.3
  • 17
    • 0019026208 scopus 로고
    • Glycogen synthase kinase-3 from rabbit skelet al. Muscle. Separation from cyclic-AMP-dependent protein kinase and phosphorylase kinase
    • Embi N, Rylatt DB, Cohen P. Glycogen synthase kinase-3 from rabbit skelet al. muscle. Separation from cyclic-AMP-dependent protein kinase and phosphorylase kinase. Eur. J. Biochem. 107 (2), 519-527 (1980).
    • (1980) Eur. J. Biochem. , vol.107 , Issue.2 , pp. 519-527
    • Embi, N.1    Rylatt, D.B.2    Cohen, P.3
  • 18
    • 0025286104 scopus 로고
    • Molecular cloning and expression of glycogen synthase kinase-3/Factor A
    • Woodgett JJ. Molecular cloning and expression of glycogen synthase kinase-3/factor A. EMBO J. 9 (8), 2431-2438 (1990). •• Key paper on the molecular features of glycogen synthase kinase (GSK)-3. (Pubitemid 20218338)
    • (1990) EMBO Journal , vol.9 , Issue.8 , pp. 2431-2438
    • Woodgett, J.R.1
  • 20
    • 0032193702 scopus 로고    scopus 로고
    • Isolation and chromosomal mapping of human glycogen synthase kinase-3α And-3β Encoding genes
    • Shaw PC, Davies AF, Lau KF et al. Isolation and chromosomal mapping of human glycogen synthase kinase-3α and-3β encoding genes. Genome 41 (5) , 720-727 (1998).
    • (1998) Genome , vol.41 , Issue.5 , pp. 720-727
    • Shaw, P.C.1    Davies, A.F.2    Lau, K.F.3
  • 21
    • 0035983533 scopus 로고    scopus 로고
    • Aternative splicing isoform of tau protein kinase I/glycogen synthase kinase 3β
    • DOI 10.1046/j.1471-4159.2002.00918.x
    • Mukai F, Ishiguro K, Sano Y, Fujita SS. Alternative splicing isoform of tau protein kinase I/glycogen synthase kinase 3β. J. Neurochem. 81 (5), 1073-1083 (2002). (Pubitemid 34809290)
    • (2002) Journal of Neurochemistry , vol.81 , Issue.5 , pp. 1073-1083
    • Mukai, F.1    Ishiguro, K.2    Sano, Y.3    Fujita, S.C.4
  • 22
    • 0442276554 scopus 로고    scopus 로고
    • The glamour and gloom of glycogen synthase kinase-3
    • • Excellent review on GSK-3
    • Jope RS, Johnson GG. The glamour and gloom of glycogen synthase kinase-3. Trends Biochem. Sci. 29 (2), 95-102 (2004). • Excellent review on GSK-3.
    • (2004) Trends Biochem. Sci. , vol.29 , Issue.2 , pp. 95-102
    • Jope, R.S.1    Johnson, G.G.2
  • 23
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
    • DOI 10.1038/378785a0
    • Cross DA, Alessi DR, Cohen P, Andjelkovich M, Hemmings BB. Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature 378 (6559), 785-789 (1995). (Pubitemid 26004411)
    • (1995) Nature , vol.378 , Issue.6559 , pp. 785-789
    • Cross, D.A.E.1    Alessi, D.R.2    Cohen, P.3    Andjelkovich, M.4    Hemmings, B.A.5
  • 26
    • 34247865533 scopus 로고    scopus 로고
    • A chaperone-dependent GSK3β transitional intermediate mediates activation-loop autophosphorylation
    • DOI 10.1016/j.molcel.2006.10.009
    • Lochhead PA, Kinstrie R, Sibbet G, Rawjee T, Morrice N, Cleghon V. A chaperone-dependent GSK3β transitional intermediate mediates activation-loop autophosphorylation. Mol. Cell 24 (4), 627-633 (2006). (Pubitemid 350284229)
    • (2006) Molecular Cell , vol.24 , Issue.4 , pp. 627-633
    • Lochhead, P.A.1    Kinstrie, R.2    Sibbet, G.3    Rawjee, T.4    Morrice, N.5    Cleghone, V.6
  • 28
    • 0030978351 scopus 로고    scopus 로고
    • β-Catenin is a target for the ubiquitin-proteasome pathway
    • Aberle H, Bauer A, Stappert J, Kispert A, Kemler R. β-catenin is a target for the ubiquitin-proteasome pathway. EMBO J. 16 (13), 3797-3804 (1997).
    • (1997) EMBO J. , vol.16 , Issue.13 , pp. 3797-3804
    • Aberle, H.1    Bauer, A.2    Stappert, J.3    Kispert, A.4    Kemler, R.5
  • 29
    • 77749243065 scopus 로고    scopus 로고
    • The neuron-specifc isoform of glycogen synthase kinase-3β Is required for axon growth
    • DOI: 10.1111/j. 1471-4159.2010.06581.x, (Epub ahead of print)
    • Castano Z, Gordon-Weeks PR, Kypta RR. The neuron-specifc isoform of glycogen synthase kinase-3β is required for axon growth. J. Neurochem. DOI: 10.1111/j. 1471-4159.2010.06581.x (2010) (Epub ahead of print).
    • (2010) J. Neurochem.
    • Castano, Z.1    Gordon-Weeks, P.R.2    Kypta, R.R.3
  • 30
    • 77649129121 scopus 로고    scopus 로고
    • Gsk3, a multifaceted kinase in wnt signaling
    • Wu D, Pan W GSK3, a multifaceted kinase in Wnt signaling. Trends Biochem. Sci. 35 (3), 161-168 (2010).
    • (2010) Trends Biochem. Sci. , vol.35 , Issue.3 , pp. 161-168
    • Wu, D.1    Pan, W.2
  • 31
    • 0034859101 scopus 로고    scopus 로고
    • The multifaceted roles of glycogen synthase kinase 3b in cellular signaling
    • • Good review on GSK-3
    • Grimes CA, Jope RR. The multifaceted roles of glycogen synthase kinase 3b in cellular signaling. Prog. Neurobiol. 65 (4), 391-426 (2001). • Good review on GSK-3.
    • (2001) Prog. Neurobiol. , vol.65 , Issue.4 , pp. 391-426
    • Grimes, C.A.1    Jope, R.R.2
  • 33
    • 0031695652 scopus 로고    scopus 로고
    • Activation of tau protein kinase I/glycogen synthase kinase-3β by amyloid β peptide (25-35) enhances phosphorylation of tau in hippocampal neurons
    • DOI 10.1016/S0168-0102(98)00061-3, PII S0168010298000613
    • Takashima A, Honda T, Yasutake K et al. Activation of tau protein kinase I/glycogen synthase kinase-3β: By amyloid β peptide (25-35) enhances phosphorylation of tau in hippocampal neurons. Neurosci. Res. 31 (4), 317-323 (1998). (Pubitemid 28446014)
    • (1998) Neuroscience Research , vol.31 , Issue.4 , 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
  • 35
    • 3343005434 scopus 로고    scopus 로고
    • PS1 activates PI3K thus inhibiting GSK-3 activity and tau overphosphorylation: Effects of FAD mutations
    • DOI 10.1038/sj.emboj.7600251
    • Baki L, Shioi J, Wen P et al. PS1 activates PI3K thus inhibiting GSK-3 activity and tau overphosphorylation: effects of FAD mutations. EMBO J. 23 (13), 2586-2596 (2004). (Pubitemid 38988230)
    • (2004) EMBO Journal , vol.23 , Issue.13 , pp. 2586-2596
    • Baki, L.1    Shioi, J.2    Wen, P.3    Shao, Z.4    Schwarzman, A.5    Gama-Sosa, M.6    Neve, R.7    Robakis, N.K.8
  • 36
    • 0031567583 scopus 로고    scopus 로고
    • Lithium inhibits Alzheimer's disease-like tau protein phosphorylation in neurons
    • DOI 10.1016/S0014-5793(97)00688-1, PII S0014579397006881
    • Munoz-Montano JR, Moreno FJ, Avila J, Diaz-Nido J. Lithium inhibits Alzheimer's disease-like tau protein phosphorylation in neurons. FEBS Lett. 411 (2-3), 183-188 (1997). •• One of the first papers showing the effect of lithium on AD. (Pubitemid 27301451)
    • (1997) FEBS Letters , vol.411 , Issue.2-3 , pp. 183-188
    • Munoz-Montano, J.R.1    Moreno, F.J.2    Avila, J.3    Diaz-Nido, J.4
  • 37
    • 0344517353 scopus 로고    scopus 로고
    • Lithium protects cultured neurons against β-amyloid-induced neurodegeneration
    • DOI 10.1016/S0014-5793(99)00685-7, PII S0014579399006857
    • Alvarez G, Munoz-Montano JR, Satrustegui J, Avila J, Bogonez E, Diaz-Nido J. Lithium protects cultured neurons against β-amyloid-induced neurodegeneration. FEBS Lett. 453 (3), 260-264 (1999). (Pubitemid 29326659)
    • (1999) FEBS Letters , vol.453 , Issue.3 , pp. 260-264
    • Alvarez, G.1    Munoz-Montano, J.R.2    Satrustegui, J.3    Avila, J.4    Bogonez, E.5    Diaz-Nido, J.6
  • 38
    • 33746456956 scopus 로고    scopus 로고
    • Effects of endogenous β-amyloid overproduction on tau phosphorylation in cell culture
    • Wang ZF, Li HL, Li XC et al. Effects of endogenous β-amyloid overproduction on tau phosphorylation in cell culture. J. Neurochem. 98 (4), 1167-1175 (2006).
    • (2006) J. Neurochem. , vol.98 , Issue.4 , pp. 1167-1175
    • Wang, Z.F.1    Li, H.L.2    Li, X.C.3
  • 39
    • 5144234244 scopus 로고    scopus 로고
    • M1 muscarinic receptor activation protects neurons from β-amyloid toxicity. A role for Wnt signaling pathway
    • DOI 10.1016/j.nbd.2004.07.016, PII S0969996104001536
    • Farias GG, Godoy JA, Hernandez F, Avila J, Fisher A, Inestrosa NN. M1 muscarinic receptor activation protects neurons from β-amyloid toxicity. A role for Wnt signaling pathway. Neurobiol. Dis. 17 (2), 337-348 (2004). (Pubitemid 39345789)
    • (2004) Neurobiology of Disease , vol.17 , Issue.2 , pp. 337-348
    • Farias, G.G.1    Godoy, J.A.2    Hernandez, F.3    Avila, J.4    Fisher, A.5    Inestrosa, N.C.6
  • 40
    • 1642289188 scopus 로고    scopus 로고
    • Role of tau protein in both physiological and pathological conditions
    • DOI 10.1152/physrev.00024.2003
    • Avila J, Lucas JJ, Perez M, Hernandez F. Role of tau protein in both physiological and pathological conditions. Physiol. Rev. 84 (2), 361-384 (2004). (Pubitemid 38365487)
    • (2004) Physiological Reviews , vol.84 , Issue.2 , pp. 361-384
    • Avila, J.1    Lucas, J.J.2    Perez, M.3    Hernandez, F.4
  • 41
    • 0037718047 scopus 로고    scopus 로고
    • Pre-mrna splicing modulations in senescence
    • Meshorer E, Soreq H. Pre-mRNA splicing modulations in senescence. Aging Cell 1 (1), 10-16 (2002).
    • (2002) Aging Cell. , vol.1 , Issue.1 , pp. 10-16
    • Meshorer, E.1    Soreq, H.2
  • 43
    • 0035875098 scopus 로고    scopus 로고
    • Crystal structure of glycogen synthase kinase 3β: Structural basis for phosphate-primed substrate specificity and autoinhibition
    • DOI 10.1016/S0092-8674(01)00374-9
    • Dajani R, Fraser E, Roe SM et al. Crystal structure of glycogen synthase kinase 3β: structural basis for phosphate-primed substrate specifcity and autoinhibition. Cell 105 (6), 721-732 (2001). (Pubitemid 32635102)
    • (2001) Cell , vol.105 , Issue.6 , pp. 721-732
    • Dajani, R.1    Fraser, E.2    Roe S.Mark3    Young, N.4    Good, V.5    Dale, T.C.6    Pearl, L.H.7
  • 46
    • 0031052339 scopus 로고    scopus 로고
    • Potentiation of GSK-3-catalyzed Alzheimer-like phosphorylation of human tau by cdk5
    • DOI 10.1023/A:1006883924775
    • Sengupta A, Wu Q, Grundke-Iqbal I, Iqbal K, Singh TT. Potentiation of GSK-3-catalyzed Alzheimer-like phosphorylation of human tau by cdk5. Mol. Cell. Biochem. 167 (1-2), 99-105 (1997). (Pubitemid 27081337)
    • (1997) Molecular and Cellular Biochemistry , vol.167 , Issue.1-2 , pp. 99-105
    • Sengupta, A.1    Wu, Q.2    Grundke-Iqbal, I.3    Iqbal, K.4    Singh, T.J.5
  • 47
    • 1542358895 scopus 로고    scopus 로고
    • PAR-1 kinase plays an initiator role in a temporally ordered phosphorylation process that confers tau toxicity in Drosophila
    • DOI 10.1016/S0092-8674(04)00170-9, PII S0092867404001709
    • Nishimura I, Yang Y, Lu B. PAR-1 kinase plays an initiator role in a temporally ordered phosphorylation process that confers tau toxicity in Drosophila. Cell 116 (5), 671-682 (2004). (Pubitemid 38326726)
    • (2004) Cell , vol.116 , Issue.5 , pp. 671-682
    • Nishimura, I.1    Yang, Y.2    Lu, B.3
  • 49
    • 0346434153 scopus 로고    scopus 로고
    • Over activation 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 SJ, Zhang AH, Li HL et al. Over activation 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 (6), 1333-1344 (2003).
    • (2003) J. Neurochem. , vol.87 , Issue.6 , pp. 1333-1344
    • Liu, S.J.1    Zhang, A.H.2    Li, H.L.3
  • 50
    • 34547929974 scopus 로고    scopus 로고
    • N-terminal cleavage of GSK-3 by calpain: A new form of GSK-3 regulation
    • DOI 10.1074/jbc.M702793200
    • Goni-Oliver P, Lucas JJ, Avila J, Hernandez F. N-terminal cleavage of GSK-3 by calpain: a new form of GSK-3 regulation. J. Biol. Chem. 282 (31), 22406-22413 (2007). • Calpain removes the N-terminal end regulatory domain, activating GSK-3. (Pubitemid 47267365)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.31 , pp. 22406-22413
    • Goni-Oliver, P.1    Lucas, J.J.2    Avila, J.3    Hernandez, F.4
  • 51
    • 80051806451 scopus 로고    scopus 로고
    • Gsk-3 is a master regulator of neural progenitor homeostasis
    • Kim WY, Wang X, Wu Y et al. GSK-3 is a master regulator of neural progenitor homeostasis. Nat. Neurosci. 12 (11), 1390-1397 (2009).
    • (2009) Nat. Neurosci. , vol.12 , Issue.11 , pp. 1390-1397
    • Kim, W.Y.1    Wang, X.2    Wu, Y.3
  • 52
    • 68049121855 scopus 로고    scopus 로고
    • Blocked inhibitory serine-phosphorylation of glycogen synthase kinase-3α/β Impairs in vivo neural precursor cell proliferation
    • Eom TY, Jope RR. Blocked inhibitory serine-phosphorylation of glycogen synthase kinase-3α/β impairs in vivo neural precursor cell proliferation. Biol Psychiatry 66 (5), 494-502 (2009).
    • (2009) Biol. Psychiatry , vol.66 , Issue.5 , pp. 494-502
    • Eom, T.Y.1    Jope, R.R.2
  • 53
    • 70249097351 scopus 로고    scopus 로고
    • Function of tau protein in adult newborn neurons
    • • First indication of a novel role of tau protein in neuron migration
    • Fuster-Matanzo A, de Barreda EG, Dawson HN, Vitek MP, Avila J, Hernandez F. Function of tau protein in adult newborn neurons. FEBS Lett. 583 (18), 3063-3068 (2009). • First indication of a novel role of tau protein in neuron migration.
    • (2009) FEBS Lett , vol.583 , Issue.18 , pp. 3063-3068
    • Fuster-Matanzo, A.1    De Barreda, E.G.2    Dawson, H.N.3    Vitek, M.P.4    Avila, J.5    Hernandez, F.6
  • 54
    • 77951812710 scopus 로고    scopus 로고
    • Essential role of tau phosphorylation in adult hippocampal neurogenesis
    • DOI: 10.1002/hipo.20712, (Epub ahead of print)
    • Hong XP, Peng CX, Wei W et al. Essential role of tau phosphorylation in adult hippocampal neurogenesis. Hippocampus DOI: 10.1002/hipo.20712 (2009) (Epub ahead of print).
    • (2009) Hippocampus
    • Hong, X.P.1    Peng, C.X.2    Wei, W.3
  • 55
    • 75949107662 scopus 로고    scopus 로고
    • Tau-knock-out mice mice show reduced gsk3 induced hippocampal degeneration and learning defcits
    • • Demonstrates a toxic role for phosphorylated tau
    • Gomez de Barreda E, Pérez M, Gómez-Ramos P et al. Tau-knock-out mice mice show reduced GSK3 induced hippocampal degeneration and learning defcits. Neurobiol. Dis. 37 (3), 622-629 (2010). • Demonstrates a toxic role for phosphorylated tau.
    • (2010) Neurobiol. Dis. , vol.37 , Issue.3 , pp. 622-629
    • De Barreda, G.E.1    Pérez, M.2    Gómez-Ramos, P.3
  • 57
    • 0038187674 scopus 로고    scopus 로고
    • GSK-3α regulates production of Alzheimer's disease amyloid-β peptides
    • DOI 10.1038/nature01640
    • Phiel CJ, Wilson CA, Lee VM, Klein PP. GSK-3α regulates production of Alzheimer's disease amyloid-βpeptides. Nature 423 (6938), 435-439 (2003). (Pubitemid 36626994)
    • (2003) Nature , vol.423 , Issue.6938 , pp. 435-439
    • Phiel, C.J.1    Wilson, C.A.2    Lee, V.M.-Y.3    Klein, P.S.4
  • 58
    • 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, Avila J. Chronic lithium treatment decreases mutant tau protein aggregation in a transgenic mouse model. J. Alzheimers Dis. 5 (4), 301-308 (2003). •• First paper showing the effect of lithium on tau aggregation in an AD mouse model. (Pubitemid 37411777)
    • (2003) Journal of Alzheimer's Disease , vol.5 , Issue.4 , pp. 301-308
    • Perez, M.1    Hernandez, F.2    Lim, F.3    Diaz-Nido, J.4    Avila, J.5
  • 60
    • 0026619472 scopus 로고
    • Phosphorylation sites on tau by tau protein kinase I, a bovine derived kinase generating an epitope of paired helical filaments
    • DOI 10.1016/0304-3940(92)90839-Y
    • Ishiguro K, Omori A, Takamatsu M et al. Phosphorylation sites on tau by tau protein kinase I, a bovine derived kinase generating an epitope of paired helical flaments. Neurosci. Lett. 148 (1-2), 202-206 (1992). (Pubitemid 23007739)
    • (1992) Neuroscience Letters , vol.148 , Issue.1-2 , pp. 202-206
    • Ishiguro, K.1    Omori, A.2    Takamatsu, M.3    Sato, K.4    Arioka, M.5    Uchida, T.6    Imahori, K.7
  • 61
    • 0027255817 scopus 로고
    • Glycogen synthase kinase 3β is identical to tau protein kinase I generating several epitopes of paired helical filaments
    • DOI 10.1016/0014-5793(93)81066-9
    • Ishiguro K, Shiratsuchi A, Sato S et al. Glycogen synthase kinase 3β is identical to tau protein kinase I generating several epitopes of paired helical flaments. FEBS Lett. 325 (3), 167-172 (1993). • Key paper describing GSK-3 as one of the main tau kinases. (Pubitemid 23186470)
    • (1993) FEBS Letters , vol.325 , Issue.3 , 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
  • 62
    • 0345276564 scopus 로고    scopus 로고
    • GSK-3 dependent phosphoepitopes recognized by PHF-1 and AT-8 antibodies are present in different tau isoforms
    • DOI 10.1016/j.neurobiolaging.2003.04.002
    • Hernandez F, Lucas JJ, Cuadros R, Avila J. GSK-3 dependent phosphoepitopes recognized by PHF-1 and AT-8 antibodies are present in different tau isoforms. Neurobiol. Aging 24 (8), 1087-1094 (2003). (Pubitemid 37487886)
    • (2003) Neurobiology of Aging , vol.24 , Issue.8 , pp. 1087-1094
    • Hernandez, F.1    Lucas, J.J.2    Cuadros, R.3    Avila, J.4
  • 64
    • 0036942843 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 is associated with neuronal and glial hyperphosphorylated tau deposits in Alzheimer's diasese, Pick's disease, progressive supranuclear palsy and corticobasal degeneration
    • Ferrer I, Barrachina M, Puig B. Glycogen synthase kinase-3 is associated with neuronal and glial hyperphosphorylated tau deposits in Alzheimer's disease, Pick's disease, progressive supranuclear palsy and corticobasal degeneration. Acta Neuropathol (Berl.) 104 (6), 583-591 (2002). (Pubitemid 36075423)
    • (2002) Acta Neuropathologica , vol.104 , Issue.6 , pp. 583-591
    • Ferrer, I.1    Barrachina, M.2    Puig, B.3
  • 67
    • 0029737421 scopus 로고    scopus 로고
    • Preferential labeling of Alzheimer neurofibrillary tangles with antisera for tau protein kinase (TPK) I/glycogen synthase kinase-3β and cyclin-dependent kinase 5, a component of TPK II
    • DOI 10.1007/s004010050513
    • Yamaguchi H, Ishiguro K, Uchida T, Takashima A, Lemere CA, Imahori K Preferential labeling of Alzheimer neurofbrillary tangles with antisera for tau protein kinase (TPK) I/glycogen synthase kinase-3β and cyclin-dependent kinase 5, a component of TPK II. Acta Neuropathol (Berl.) 92 (3), 232-241 (1996). (Pubitemid 26278953)
    • (1996) Acta Neuropathologica , vol.92 , Issue.3 , pp. 232-241
    • Yamaguchi, H.1    Ishiguro, K.2    Uchida, T.3    Takashima, A.4    Lemere, C.A.5    Imahori, K.6
  • 68
    • 54049111843 scopus 로고    scopus 로고
    • Association of gsk3b with alzheimer disease and frontotemporal dementia
    • Schaffer BA, Bertram L, Miller BL et al. Association of GSK3B with Alzheimer disease and frontotemporal dementia. Arch. Neurol. 65 (10), 1368-1374 (2008).
    • (2008) Arch. Neurol. , vol.65 , Issue.10 , pp. 1368-1374
    • Schaffer, B.A.1    Bertram, L.2    Miller, B.L.3
  • 69
    • 70350459011 scopus 로고    scopus 로고
    • Understanding the role of disc1 in psychiatric disease and during normal development
    • Brandon NJ, Millar JK, Korth C, Sive H, Singh KK, Sawa A. Understanding the role of DISC1 in psychiatric disease and during normal development. J. Neurosci. 29 (41), 12768-12775 (2009).
    • (2009) J. Neurosci. , vol.29 , Issue.41 , pp. 12768-12775
    • Brandon, N.J.1    Millar, J.K.2    Korth, C.3    Sive, H.4    Singh, K.K.5    Sawa, A.6
  • 70
    • 62149083806 scopus 로고    scopus 로고
    • Disrupted in schizophrenia 1 regulates neuronal progenitor proliferation via modulation of gsk3β/β-catenin signaling
    • • Demonstrated a new way to regulate GSK-3 activity
    • Mao Y, Ge X, Frank CL et al. Disrupted in schizophrenia 1 regulates neuronal progenitor proliferation via modulation of GSK3β/β-catenin signaling. Cell 136 (6), 1017-1031 (2009). • Demonstrated a new way to regulate GSK-3 activity.
    • (2009) Cell. , vol.136 , Issue.6 , pp. 1017-1031
    • Mao, Y.1    Ge, X.2    Frank, C.L.3
  • 71
    • 0037118247 scopus 로고    scopus 로고
    • Human wild-type tau interacts with wingless pathway components and produces neurofibrillary pathology in Drosophila
    • DOI 10.1016/S0896-6273(02)00706-7
    • Jackson GR, Wiedau-Pazos M, Sang TK et al. Human wild-type tau interacts with wingless pathway components and produces neurofbrillary pathology in Drosophila. Neuron 34 (4), 509-519 (2002). (Pubitemid 34628749)
    • (2002) Neuron , vol.34 , Issue.4 , pp. 509-519
    • Jackson, G.R.1    Wiedau-Pazos, M.2    Sang, T.-K.3    Wagle, N.4    Brown, C.A.5    Massachi, S.6    Geschwind, D.H.7
  • 74
    • 4444281337 scopus 로고    scopus 로고
    • S9A resulted in tau hyperphosphorylation and morphology reminiscent of pretangle-like neurons in the brain of PDGSK3β transgenic mice
    • DOI 10.1023/B:TRAG.0000040039.44899.6f
    • Li B, Ryder J, Su Y et al. Over expression of GSK3bS9A resulted in tau hyperphosphorylation and morphology reminiscent of pretangle-like neurons in the brain of PDGSK3β transgenic mice. Transgenic Res. 13 (4), 385-396 (2004). (Pubitemid 39182836)
    • (2004) Transgenic Research , vol.13 , Issue.4 , pp. 385-396
    • Li, B.1    Ryder, J.2    Su, Y.3    Moore Jr., S.A.4    Liu, F.5    Solenberg, P.6    Brune, K.7    Fox, N.8    Ni, B.9    Liu, R.10    Zhou, Y.11
  • 75
    • 0035863188 scopus 로고    scopus 로고
    • Decreased nuclear β-catenin, tau hyperphosphorylation and neurodegeneration in GSK-3β conditional transgenic mice
    • DOI 10.1093/emboj/20.1.27
    • Lucas JJ, Hernandez F, Gomez-Ramos P, Moran MA, Hen R, Avila J. Decreased nuclear β-catenin, tau hyperphosphorylation and neurodegeneration in GSK-3β conditional transgenic mice. EMBO J. 20 (1-2), 27-39 (2001). • Animal model to study the role of GSK-3β in different brain areas. (Pubitemid 32099099)
    • (2001) EMBO Journal , vol.20 , Issue.1-2 , pp. 27-39
    • Lucas, J.J.1    Hernandez, F.2    Gomez-Ramos, P.3    Moran, M.A.4    Hen, R.5    Avila, J.6
  • 76
    • 1642363745 scopus 로고    scopus 로고
    • Spatial learning deficit in transgenic mice that conditionally over-express GSK-3β 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, Lucas JJ. Spatial learning defcit in transgenic mice that conditionally over-express GSK-3β in the brain but do not form tau flaments. J. Neurochem. 83 (6), 1529-1533 (2002). (Pubitemid 35477491)
    • (2002) Journal of Neurochemistry , vol.83 , Issue.6 , pp. 1529-1533
    • Hernandez, F.1    Borrell, J.2    Guaza, C.3    Avila, J.4    Lucas, J.J.5
  • 77
    • 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
    • DOI 10.1523/JNEUROSCI.0604-06.2006
    • Engel T, Hernandez F, Avila J, Lucas JJ. Full reversal of Alzheimer's disease-like phenotype in a mouse model with conditional overexpression of glycogen synthase kinase-3. J. Neurosci. 26 (19), 5083-5090 (2006). (Pubitemid 44315289)
    • (2006) Journal of Neuroscience , vol.26 , Issue.19 , pp. 5083-5090
    • Engel, T.1    Hernandez, F.2    Avila, J.3    Lucas, J.J.4
  • 78
    • 33845530335 scopus 로고    scopus 로고
    • Chronic lithium administration to FTDP-17 tau and GSK-3β overexpressing mice prevents tau hyperphosphorylation and neurofibrillary tangle formation, but pre-formed neurofibrillary tangles do not revert
    • DOI 10.1111/j.1471-4159.2006.04139.x
    • Engel T, Goni-Oliver P, Lucas JJ, Avila J, Hernandez F. Chronic lithium administration to FTDP-17 tau and GSK-3β overexpressing mice prevents tau hyperphosphorylation and neurofbrillary tangle formation, but pre-formed neurofbrillary tangles do not revert. J. Neurochem. 99 (6), 1445-1455 (2006). (Pubitemid 44924224)
    • (2006) Journal of Neurochemistry , vol.99 , Issue.6 , pp. 1445-1455
    • Engel, T.1    Goni-Oliver, P.2    Lucas, J.J.3    Avila, J.4    Hernandez, F.5
  • 79
    • 33746210131 scopus 로고    scopus 로고
    • Cooexpression of FTDP-17 tau and GSK-3β in transgenic mice induce tau polymerization and neurodegeneration
    • DOI 10.1016/j.neurobiolaging.2005.06.010, PII S0197458005001855
    • Engel T, Lucas JJ, Gomez-Ramos P, Moran MA, Avila J, Hernandez F. Cooexpression of FTDP-17 tau and GSK-3β in transgenic mice induce tau polymerization and neurodegeneration. Neurobiol. Aging 27 (9), 1258-1268 (2006). (Pubitemid 44088576)
    • (2006) Neurobiology of Aging , vol.27 , Issue.9 , pp. 1258-1268
    • Engel, T.1    Lucas, J.J.2    Gomez-Ramos, P.3    Moran, M.A.4    Avila, J.5    Hernandez, F.6
  • 80
    • 0034612636 scopus 로고    scopus 로고
    • Requirement for glycogen synthase kinase-3β in cell survival and NF-κB activation
    • DOI 10.1038/35017574
    • Hoefich KP, Luo J, Rubie EA, Tsao MS, Jin O, Woodgett JJ. Requirement for glycogen synthase kinase-3β in cell survival and NF-κB activation. Nature 406 (6791), 86-90 (2000). (Pubitemid 30460216)
    • (2000) Nature , vol.406 , Issue.6791 , pp. 86-90
    • Hoeflich, K.P.1    Luo, J.2    Rubie, E.A.3    Tsao, M.-S.4    Jin, O.5    Woodgett, J.R.6
  • 81
    • 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, PII 7601725
    • Gomez-Sintes R, Hernandez F, Bortolozzi A et al. Neuronal apoptosis and reversible motor defcit in dominantnegative GSK-3 conditional transgenic mice. EMBO J. 26 (11), 2743-2754 (2007). • Mice overexpressing a dominant-negative GSK-3β form show us that extensive GSK-3 inhibition can induce apoptosis. (Pubitemid 46884288)
    • (2007) EMBO Journal , vol.26 , Issue.11 , pp. 2743-2754
    • Gomez-Sintes, R.1    Hernandez, F.2    Bortolozzi, A.3    Artigas, F.4    Avila, J.5    Zaratin, P.6    Gotteland, J.P.7    Lucas, J.J.8
  • 82
    • 34447119530 scopus 로고    scopus 로고
    • Resolution of the nuclear localization mechanism of glycogen synthase kinase-3, functional effects in apoptosis
    • Meares GP, Jope RR. Resolution of the nuclear localization mechanism of glycogen synthase kinase-3, functional effects in apoptosis. J. Biol. Chem. 282 (23), 16989-17001 (2007).
    • (2007) J. Biol. Chem. , vol.282 , Issue.23 , pp. 16989-17001
    • Meares, G.P.1    Jope, R.R.2
  • 83
    • 0029152786 scopus 로고
    • Role of glycogen synthase kinase 3β As a negative regulator of dorsoventral axis formation in xenopus embryos
    • USA
    • Dominguez I, Itoh K, Sokol SS. Role of glycogen synthase kinase 3β as a negative regulator of dorsoventral axis formation in Xenopus embryos. Proc. Natl Acad. Sci. USA 92 (18), 8498-8502 (1995).
    • (1995) Proc. Natl. Acad. Sci. , vol.92 , Issue.18 , pp. 8498-8502
    • Dominguez, I.1    Itoh, K.2    Sokol, S.S.3
  • 84
    • 70350747578 scopus 로고    scopus 로고
    • A functional mouse retroposed gene rps23r1 reduces alzheimer's β-amyloid levels and tau phosphorylation
    • Zhang YW, Liu S, Zhang X et al. A Functional mouse retroposed gene Rps23r1 reduces Alzheimer's β-amyloid levels and tau phosphorylation. Neuron 64 (3), 328-340 (2009).
    • (2009) Neuron , vol.64 , Issue.3 , pp. 328-340
    • Zhang, Y.W.1    Liu, S.2    Zhang, X.3
  • 85
    • 0029776032 scopus 로고    scopus 로고
    • A molecular mechanism for the effect of lithium on development
    • USA
    • Klein PS, Melton DD. A molecular mechanism for the effect of lithium on development. Proc. Natl Acad. Sci. USA 93 (16), 8455-8459 (1996).
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , Issue.16 , pp. 8455-8459
    • Klein, P.S.1    Melton, D.D.2
  • 86
    • 0036295233 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 inhibition by lithium and beryllium suggests the presence of two magnesium binding sites
    • DOI 10.1006/bbrc.2001.6305
    • Ryves WJ, Dajani R, Pearl L, Harwood AA. Glycogen synthase kinase-3 inhibition by lithium and beryllium suggests the presence of two magnesium binding sites. Biochem. Biophys. Res. Commun. 290 (3), 967-972 (2002). (Pubitemid 34687456)
    • (2002) Biochemical and Biophysical Research Communications , vol.290 , Issue.3 , pp. 967-972
    • Ryves W.Jonathan1    Dajani, R.2    Pearl, L.3    Harwood, A.J.4
  • 87
    • 34250818767 scopus 로고    scopus 로고
    • Lithium reduces tau phosphorylation but not Aβ or working memory deficits in a transgenic model with both plaques and tangles
    • DOI 10.2353/ajpath.2007.061178
    • Caccamo A, Oddo S, Tran LX, LaFerla FF. Lithium reduces tau phosphorylation but not Aβ or working memory defcits in a transgenic model with both plaques and tangles. Am. J. Pathol. 170 (5), 1669-1675 (2007). (Pubitemid 47339311)
    • (2007) American Journal of Pathology , vol.170 , Issue.5 , pp. 1669-1675
    • Caccamo, A.1    Oddo, S.2    Tran, L.X.3    LaFerla, F.M.4
  • 88
    • 67649206084 scopus 로고    scopus 로고
    • Lithium trial in alzheimer's disease: A randomized, single-blind, placebocontrolled, multicenter 10-week study
    • Hampel H, Ewers M, Burger K et al. Lithium trial in Alzheimer's disease: a randomized, single-blind, placebocontrolled, multicenter 10-week study. J. Clin. Psychiatry 70 (6), 922-931 (2009).
    • (2009) J. Clin. Psychiatry , vol.70 , Issue.6 , pp. 922-931
    • Hampel, H.1    Ewers, M.2    Burger, K.3
  • 91
    • 0033776383 scopus 로고    scopus 로고
    • Selective small molecule inhibitors of glycogen synthase kinase-3 modulate glycogen metabolism and gene transcription
    • Coghlan MP, Culbert AA, Cross DA et al. Selective small molecule inhibitors of glycogen synthase kinase-3 modulate glycogen metabolism and gene transcription. Chem. Biol. 7 (10), 793-803 (2000).
    • (2000) Chem. Biol. , vol.7 , Issue.10 , pp. 793-803
    • Coghlan, M.P.1    Culbert, A.A.2    Cross, D.A.3
  • 92
    • 0037075791 scopus 로고    scopus 로고
    • First non-ATP competitive glycogen synthase kinase 3 β (GSK-3β) 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, Moreno FF. First non-ATP competitive glycogen synthase kinase 3β (GSK-3β:) inhibitors: thiadiazolidinones (TDZD) as potential drugs for the treatment of Alzheimer's disease. J. Med. Chem. 45 (6), 1292-1299 (2002). (Pubitemid 34263565)
    • (2002) Journal of Medicinal Chemistry , vol.45 , Issue.6 , pp. 1292-1299
    • Martinez, A.1    Alonso, M.2    Castro, A.3    Perez, C.4    Moreno, F.J.5
  • 93
    • 68149150844 scopus 로고    scopus 로고
    • A novel gsk-3β Inhibitor reduces alzheimer's pathology and rescues neuronal loss in vivo
    • Sereno L, Coma M, Rodriguez M et al. A novel GSK-3β inhibitor reduces Alzheimer's pathology and rescues neuronal loss in vivo. Neurobiol. Dis. 35 (3), 359-367 (2009).
    • (2009) Neurobiol. Dis. , vol.35 , Issue.3 , pp. 359-367
    • Sereno, L.1    Coma, M.2    Rodriguez, M.3
  • 95
    • 34447503455 scopus 로고    scopus 로고
    • Untangling tau hyperphosphorylation in drug design for neurodegenerative diseases
    • Mazanetz MP, Fischer PP. Untangling tau hyperphosphorylation in drug design for neurodegenerative diseases. Nat. Rev. Drug Discov. 6 (6), 464-479 (2007).
    • (2007) Nat. Rev. Drug Discov , vol.6 , Issue.6 , pp. 464-479
    • Mazanetz, M.P.1    Fischer, P.P.2
  • 96
  • 97
    • 70349974745 scopus 로고    scopus 로고
    • Characterization and development of novel small-molecules inhibiting gsk3 and activating wnt signaling
    • Zhong H, Zou H, Semenov MV et al. Characterization and development of novel small-molecules inhibiting GSK3 and activating Wnt signaling. Mol. Biosyst. 5 (11), 1356-1360 (2009).
    • (2009) Mol. Biosyst , vol.5 , Issue.11 , pp. 1356-1360
    • Zhong, H.1    Zou, H.2    Semenov, M.V.3
  • 98
    • 56149105343 scopus 로고    scopus 로고
    • Gsk-3β Is required for memory reconsolidation in adult brain
    • Kimura T, Yamashita S, Nakao S et al. GSK-3β is required for memory reconsolidation in adult brain. PLoS One 3 (10), e3540 (2008).
    • (2008) PLoS One , vol.3 , Issue.10
    • Kimura, T.1    Yamashita, S.2    Nakao, S.3
  • 102
    • 0033198715 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the human glycogen synthase kinase-3β promoter
    • DOI 10.1006/geno.1999.5875
    • Lau KF, Miller CC, Anderton BH, Shaw PP. Molecular cloning and characterization of the human glycogen synthase kinase-3β promoter. Genomics 60 (2), 121-128 (1999). (Pubitemid 29463670)
    • (1999) Genomics , vol.60 , Issue.2 , pp. 121-128
    • Lau, K.-F.1    Miller, C.C.J.2    Anderton, B.H.3    Shaw, P.-C.4
  • 103
    • 0035062230 scopus 로고    scopus 로고
    • Identification of sequence variants and analysis of the role of the glycogen synthase kinase 3 β gene and promoter in late onset Alzheimer's disease
    • DOI 10.1038/sj.mp.4000852
    • Russ C, Lovestone S, Powell JJ. Identifcation of sequence variants and analysis of the role of the glycogen synthase kinase 3β gene and promoter in late onset Alzheimer's disease. Mol. Psychiatry 6 (3), 320-324 (2001). (Pubitemid 32275679)
    • (2001) Molecular Psychiatry , vol.6 , Issue.3 , pp. 320-324
    • Russ, C.1    Lovestone, S.2    Powell, J.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.