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

References

• Alzheimer A. [On certain peculiar diseases of old age]. Arch. Psychiatr. Nervenkr. Z. Gesamte Neurol. Psychiatr.4, 356–386 (1911).
   Google Scholar
• Whitehouse PJ, Price DL, Struble RG, Clark AW, Coyle JT, Delon MR. Alzheimer’s disease and senile dementia: loss of neurons in the basal forebrain. Science215(4537), 1237–1239 (1982).
   PubMed Web of Science ®Google Scholar
• Masters CL, Multhaup G, Simms G, Pottgiesser J, Martins RN, Beyreuther K. Neuronal origin of a cerebral amyloid: neurofibrillary 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).
   PubMed Web of Science ®Google Scholar
• Glenner GG, Wong CW. Alzheimer’s disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem. Biophys. Res. Commun.120(3), 885–890 (1984).
   PubMed Web of Science ®Google Scholar
• Price DL, Sisodia SS. Mutant genes in familial Alzheimer’s disease and transgenic models. Annu. Rev. Neurosci.21, 479–505 (1998).
   PubMed Web of Science ®Google Scholar
• Grundke-Iqbal I, Iqbal K, Tung YC, Quinlan M, Wisniewski HM, Binder LI. Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology. Proc. Natl Acad. Sci. USA83(13), 4913–4917 (1986).
   PubMed Web of Science ®Google Scholar
• 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).
   PubMed Web of Science ®Google Scholar
• Hanger DP, Anderton BH, Noble W. Tau phosphorylation: the therapeutic challenge for neurodegenerative disease. Trends Mol. Med.15(3), 112–119 (2009).
   PubMed Web of Science ®Google Scholar
• Nishiura C, Takeuchi K, Minoura K et al. Importance of Tyr310 residue in the third repeat of microtubule binding domain for filament formation of tau protein. J. Biochem.147(3), 405–414 (2009).
   PubMedGoogle Scholar
• Hardy J, Selkoe DJ. The amyloid hypothesis of Alzheimer’s disease: progress and problems on the road to therapeutics. Science297(5580), 353–356 (2002).
   PubMed Web of Science ®Google Scholar
• Murayama O, Tomita T, Nihonmatsu N et al. Enhancement of amyloid β 42 secretion by 28 different presenilin 1 mutations of familial Alzheimer’s disease. Neurosci. Lett.265(1), 61–63 (1999).
   PubMed Web of Science ®Google Scholar
• Dermaut B, Kumar-Singh S, Engelborghs S et al. A novel presenilin 1 mutation associated with Pick’s disease but not β-amyloid plaques. Ann. Neurol.55(5), 617–626 (2004).
   PubMed Web of Science ®Google Scholar
• Santacruz K, Lewis J, Spires T et al. Tau suppression in a neurodegenerative mouse model improves memory function. Science309(5733), 476–481 (2005).
   PubMed Web of Science ®Google Scholar
• Avila J. Tau phosphorylation and aggregation in Alzheimer’s disease pathology. FEBS Lett.580(12), 2922–2927 (2006).
   PubMed Web of Science ®Google Scholar
• 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).
   PubMed Web of Science ®Google Scholar
• 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).
   PubMed Web of Science ®Google Scholar
• Embi N, Rylatt DB, Cohen P. Glycogen synthase kinase-3 from rabbit skeletal muscle. Separation from cyclic-AMP-dependent protein kinase and phosphorylase kinase. Eur. J. Biochem.107(2), 519–527 (1980).
   PubMedGoogle Scholar
• Woodgett JR. Molecular cloning and expression of glycogen synthase kinase-3/factor A. EMBO J.9(8), 2431–2438 (1990).
   PubMed Web of Science ®Google Scholar
• Hansen L, Arden KC, Rasmussen SB et al. Chromosomal mapping and mutational analysis of the coding region of the glycogen synthase kinase-3α and β isoforms in patients with NIDDM. Diabetologia40(8), 940–946 (1997).
   PubMed Web of Science ®Google Scholar
• Shaw PC, Davies AF, Lau KF et al. Isolation and chromosomal mapping of human glycogen synthase kinase-3α and -3β encoding genes. Genome41(5), 720–727 (1998).
   PubMed Web of Science ®Google Scholar
• Mukai F, Ishiguro K, Sano Y, Fujita SC. Alternative splicing isoform of tau protein kinase I/glycogen synthase kinase 3β. J. Neurochem.81(5), 1073–1083 (2002).
   PubMed Web of Science ®Google Scholar
• Jope RS, Johnson GV. The glamour and gloom of glycogen synthase kinase-3. Trends Biochem. Sci.29(2), 95–102 (2004).
   PubMed Web of Science ®Google Scholar
• Cross DA, Alessi DR, Cohen P, Andjelkovich M, Hemmings BA. Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature378(6559), 785–789 (1995).
   PubMed Web of Science ®Google Scholar
• Nakashima H, Ishihara T, Suguimoto P et al. Chronic lithium treatment decreases tau lesions by promoting ubiquitination in a mouse model of tauopathies. Acta Neuropathol.110(6), 547–556 (2005).
   PubMed Web of Science ®Google Scholar
• Thornton TM, Pedraza-Alva G, Deng B et al. Phosphorylation by p38 MAPK as an alternative pathway for GSK3β inactivation. Science320(5876), 667–670 (2008).
   PubMed Web of Science ®Google Scholar
• Lochhead PA, Kinstrie R, Sibbet G, Rawjee T, Morrice N, Cleghon V. A chaperone-dependent GSK3β transitional intermediate mediates activation-loop autophosphorylation. Mol. Cell24(4), 627–633 (2006).
   PubMed Web of Science ®Google Scholar
• Simon D, Benitez MJ, Gimenez-Cassina A et al. Pharmacological inhibition of GSK-3 is not strictly correlated with a decrease in tyrosine phosphorylation of residues 216/279. J. Neurosci. Res.86(3), 668–674 (2008).
   PubMedGoogle Scholar
• 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).
   PubMed Web of Science ®Google Scholar
• Castano Z, Gordon-Weeks PR, Kypta RM. The neuron-specific 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).
   PubMedGoogle Scholar
• Wu D, Pan W. GSK3, a multifaceted kinase in Wnt signaling. Trends Biochem. Sci.35(3), 161–168 (2010).
   PubMed Web of Science ®Google Scholar
• Grimes CA, Jope RS. The multifaceted roles of glycogen synthase kinase 3β in cellular signaling. Prog. Neurobiol.65(4), 391–426 (2001).
   PubMed Web of Science ®Google Scholar
• Uemura K, Kuzuya A, Shimozono Y et al. GSK3β activity modifies the localization and function of presenilin 1. J. Biol. Chem.282(21), 15823–15832 (2007).
   PubMed Web of Science ®Google Scholar
• 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).
   PubMed Web of Science ®Google Scholar
• Zhang Z, Hartmann H, Do VM et al. Destabilization of β-catenin by mutations in presenilin-1 potentiates neuronal apoptosis. Nature395(6703), 698–702 (1998).
   PubMed Web of Science ®Google Scholar
• 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).
   PubMed Web of Science ®Google Scholar
• 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).
   PubMed Web of Science ®Google Scholar
• 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).
   PubMed Web of Science ®Google Scholar
• 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).
   PubMed Web of Science ®Google Scholar
• Farias GG, Godoy JA, Hernandez F, Avila J, Fisher A, Inestrosa NC. M1 muscarinic receptor activation protects neurons from β-amyloid toxicity. A role for Wnt signaling pathway. Neurobiol. Dis.17(2), 337–348 (2004).
   PubMed Web of Science ®Google Scholar
• 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).
   PubMed Web of Science ®Google Scholar
• Meshorer E, Soreq H. Pre-mRNA splicing modulations in senescence. Aging Cell1(1), 10–16 (2002).
   PubMedGoogle Scholar
• ter Haar E, Coll JT, Austen DA, Hsiao HM, Swenson L, Jain J. Structure of GSK3β reveals a primed phosphorylation mechanism. Nat. Struct. Biol.8(7), 593–596 (2001).
   PubMedGoogle Scholar
• Dajani R, Fraser E, Roe SM et al. Crystal structure of glycogen synthase kinase 3β: structural basis for phosphate-primed substrate specificity and autoinhibition. Cell105(6), 721–732 (2001).
   PubMed Web of Science ®Google Scholar
• Alonso Adel C, Li B, Grundke-Iqbal I, Iqbal K. Polymerization of hyperphosphorylated tau into filaments eliminates its inhibitory activity. Proc. Natl Acad. Sci. USA103(23), 8864–8869 (2006).
   PubMed Web of Science ®Google Scholar
• Noble W, Olm V, Takata K et al. Cdk5 is a key factor in tau aggregation and tangle formation in vivo. Neuron38(4), 555–565 (2003).
   PubMed Web of Science ®Google Scholar
• Sengupta A, Wu Q, Grundke-Iqbal I, Iqbal K, Singh TJ. Potentiation of GSK-3-catalyzed Alzheimer-like phosphorylation of human tau by cdk5. Mol. Cell. Biochem.167(1–2), 99–105 (1997).
   PubMed Web of Science ®Google Scholar
• 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. Cell116(5), 671–682 (2004).
   PubMed Web of Science ®Google Scholar
• Amit S, Hatzubai A, Birman Y et al. Axin-mediated CKI phosphorylation of β-catenin at Ser 45, a molecular switch for the Wnt pathway. Genes Dev16(9), 1066–1076 (2002).
   PubMed Web of Science ®Google Scholar
• Liu SJ, Zhang AH, Li HL et al. 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(6), 1333–1344 (2003).
   PubMed Web of Science ®Google Scholar
• 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).
   PubMed Web of Science ®Google Scholar
• 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).
   PubMed Web of Science ®Google Scholar
• Eom TY, Jope RS. Blocked inhibitory serine-phosphorylation of glycogen synthase kinase-3α/β impairs in vivo neural precursor cell proliferation. Biol. Psychiatry66(5), 494–502 (2009).
   PubMed Web of Science ®Google Scholar
• 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).
   PubMedGoogle Scholar
• 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).
   Google Scholar
• Gomez de Barreda E, Pérez M, Gómez-Ramos P et al. Tau-knock-out mice mice show reduced GSK3 induced hippocampal degeneration and learning deficits. Neurobiol. Dis.37(3), 622–629 (2010).
   PubMedGoogle Scholar
• Takashima A, Noguchi K, Sato K, Hoshino T, Imahori K. Tau protein kinase I is essential for amyloid β-protein-induced neurotoxicity. Proc. Natl Acad. Sci. USA90(16), 7789–7793 (1993).
   PubMed Web of Science ®Google Scholar
• Phiel CJ, Wilson CA, Lee VM, Klein PS. GSK-3α regulates production of Alzheimer’s disease amyloid-β peptides. Nature423(6938), 435–439 (2003).
   PubMed Web of Science ®Google Scholar
• 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).
   PubMed Web of Science ®Google Scholar
• Noble W, Planel E, Zehr C et al. Inhibition of glycogen synthase kinase-3 by lithium correlates with reduced tauopathy and degeneration in vivo. Proc. Natl Acad. Sci. USA102(19), 6990–6995 (2005).
   PubMed Web of Science ®Google Scholar
• 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 filaments. Neurosci. Lett.148(1–2), 202–206 (1992).
   PubMed Web of Science ®Google Scholar
• 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 filaments. FEBS Lett.325(3), 167–172 (1993).
   PubMed Web of Science ®Google Scholar
• 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. Aging24(8), 1087–1094 (2003).
   PubMedGoogle Scholar
• Kimura T, Ono T, Takamatsu J et al. Sequential changes of tau-site-specific phosphorylation during development of paired helical filaments. Dementia7(4), 177–181 (1996).
   PubMedGoogle Scholar
• 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).
   PubMed Web of Science ®Google Scholar
• Pei JJ, Braak E, Braak H et al. Distribution of active glycogen synthase kinase 3β (GSK-3β) in brains staged for Alzheimer disease neurofibrillary changes. J. Neuropathol. Exp. Neurol.58(9), 1010–1019 (1999).
   PubMed Web of Science ®Google Scholar
• Pei JJ, Tanaka T, Tung YC, Braak E, Iqbal K, Grundke-Iqbal I. Distribution, levels, and activity of glycogen synthase kinase-3 in the Alzheimer disease brain. J. Neuropathol. Exp. Neurol.56(1), 70–78 (1997).
   PubMed Web of Science ®Google Scholar
• Yamaguchi H, Ishiguro K, Uchida T, Takashima A, Lemere CA, Imahori K. 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. Acta Neuropathol. (Berl.)92(3), 232–241 (1996).
   PubMed Web of Science ®Google Scholar
• Schaffer BA, Bertram L, Miller BL et al. Association of GSK3β with Alzheimer disease and frontotemporal dementia. Arch. Neurol.65(10), 1368–1374 (2008).
   PubMedGoogle Scholar
• 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).
   PubMedGoogle Scholar
• Mao Y, Ge X, Frank CL et al. Disrupted in schizophrenia 1 regulates neuronal progenitor proliferation via modulation of GSK3β/β-catenin signaling. Cell136(6), 1017–1031 (2009).
   PubMed Web of Science ®Google Scholar
• Jackson GR, Wiedau-Pazos M, Sang TK et al. Human wild-type tau interacts with wingless pathway components and produces neurofibrillary pathology in Drosophila. Neuron34(4), 509–519 (2002).
   PubMed Web of Science ®Google Scholar
• Brownlees J, Irving NG, Brion JP et al. Tau phosphorylation in transgenic mice expressing glycogen synthase kinase-3β transgenes. Neuroreport8(15), 3251–3255 (1997).
   PubMed Web of Science ®Google Scholar
• Spittaels K, Van den Haute C, Van Dorpe J et al. Neonatal neuronal overexpression of glycogen synthase kinase-3 β reduces brain size in transgenic mice. Neuroscience113(4), 797–808 (2002).
   PubMed Web of Science ®Google Scholar
• Li B, Ryder J, Su Y et al. Overexpression of GSK3βS9A 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).
   PubMed Web of Science ®Google Scholar
• 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).
   PubMed Web of Science ®Google Scholar
• Hernandez F, Borrell J, Guaza C, Avila J, Lucas JJ. Spatial learning deficit in transgenic mice that conditionally over-express GSK-3β in the brain but do not form tau filaments. J. Neurochem.83(6), 1529–1533 (2002).
   PubMed Web of Science ®Google Scholar
• 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).
   PubMed Web of Science ®Google Scholar
• 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 neurofibrillary tangle formation, but pre-formed neurofibrillary tangles do not revert. J. Neurochem.99(6), 1445–1455 (2006).
   PubMed Web of Science ®Google Scholar
• 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. Aging27(9), 1258–1268 (2006).
   PubMed Web of Science ®Google Scholar
• Hoeflich KP, Luo J, Rubie EA, Tsao MS, Jin O, Woodgett JR. Requirement for glycogen synthase kinase-3β in cell survival and NF-κB activation. Nature406(6791), 86–90 (2000).
   PubMed Web of Science ®Google Scholar
• Gomez-Sintes R, Hernandez F, Bortolozzi A et al. Neuronal apoptosis and reversible motor deficit in dominant-negative GSK-3 conditional transgenic mice. EMBO J.26(11), 2743–2754 (2007).
   PubMed Web of Science ®Google Scholar
• Meares GP, Jope RS. Resolution of the nuclear localization mechanism of glycogen synthase kinase-3, functional effects in apoptosis. J. Biol. Chem.282(23), 16989–17001 (2007).
   PubMed Web of Science ®Google Scholar
• Dominguez I, Itoh K, Sokol SY. Role of glycogen synthase kinase 3β as a negative regulator of dorsoventral axis formation in Xenopus embryos. Proc. Natl Acad. Sci. USA92(18), 8498–8502 (1995).
   PubMed Web of Science ®Google Scholar
• Zhang YW, Liu S, Zhang X et al. A Functional mouse retroposed gene Rps23r1 reduces Alzheimer’s β-amyloid levels and tau phosphorylation. Neuron64(3), 328–340 (2009).
   PubMedGoogle Scholar
• Klein PS, Melton DA. A molecular mechanism for the effect of lithium on development. Proc. Natl Acad. Sci. USA93(16), 8455–8459 (1996).
   PubMed Web of Science ®Google Scholar
• Ryves WJ, Dajani R, Pearl L, Harwood AJ. 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).
   PubMed Web of Science ®Google Scholar
• Caccamo A, Oddo S, Tran LX, LaFerla FM. Lithium reduces tau phosphorylation but not Aβ or working memory deficits in a transgenic model with both plaques and tangles. Am. J. Pathol.170(5), 1669–1675 (2007).
   PubMed Web of Science ®Google Scholar
• Hampel H, Ewers M, Burger K et al. Lithium trial in Alzheimer’s disease: a randomized, single-blind, placebo-controlled, multicenter 10-week study. J. Clin. Psychiatry70(6), 922–931 (2009).
   PubMed Web of Science ®Google Scholar
• Bhat R, Xue Y, Berg S et al. Structural insights and biological effects of glycogen synthase kinase 3-specific inhibitor AR-A014418. J. Biol. Chem.278(46), 45937–45945 (2003).
   PubMed Web of Science ®Google Scholar
• Leclerc S, Garnier M, Hoessel R et al. Indirubins inhibit glycogen synthase kinase-3 β 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(1), 251–260 (2001).
   PubMed Web of Science ®Google Scholar
• 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).
   PubMed Web of Science ®Google Scholar
• Martinez A, Alonso M, Castro A, Perez C, Moreno FJ. First non-ATP competitive glycogen synthase kinase 3 β (GSK-3β) inhibitors: thiadiazolidinones (TDZD) as potential drugs for the treatment of Alzheimer’s disease. J. Med. Chem.45(6), 1292–1299 (2002).
   PubMed Web of Science ®Google Scholar
• 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).
   PubMed Web of Science ®Google Scholar
• Rao KV, Donia MS, Peng J et al. Manzamine B, E and ircinal A related alkaloids from an Indonesian Acanthostrongylophora sponge and their activity against infectious, tropical parasitic, and Alzheimer’s diseases. J. Nat. Prod.69(7), 1034–1040 (2006).
   PubMed Web of Science ®Google Scholar
• Mazanetz MP, Fischer PM. Untangling tau hyperphosphorylation in drug design for neurodegenerative diseases. Nat. Rev. Drug Discov.6(6), 464–479 (2007).
   PubMed Web of Science ®Google Scholar
• Medina M, Castro A. Glycogen synthase kinase-3 (GSK-3) inhibitors reach the clinic. Curr. Opin. Drug Discov. Devel.11(4), 533–543 (2008).
   PubMedGoogle Scholar
• 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).
   PubMedGoogle Scholar
• Kimura T, Yamashita S, Nakao S et al. GSK-3β is required for memory reconsolidation in adult brain. PLoS One3(10), e3540 (2008).
   PubMed Web of Science ®Google Scholar
• Hooper C, Markevich V, Plattner F et al. Glycogen synthase kinase-3 inhibition is integral to long-term potentiation. Eur. J. Neurosci.25(1), 81–86 (2007).
   PubMed Web of Science ®Google Scholar
• Peineau S, Taghibiglou C, Bradley C et al. LTP inhibits LTD in the hippocampus via regulation of GSK3β. Neuron53(5), 703–717 (2007).
   PubMed Web of Science ®Google Scholar
• Son H, Yu IT, Hwang SJ et al. Lithium enhances long-term potentiation independently of hippocampal neurogenesis in the rat dentate gyrus. J. Neurochem.85(4), 872–881 (2003).
   PubMed Web of Science ®Google Scholar
• Lau KF, Miller CC, Anderton BH, Shaw PC. Molecular cloning and characterization of the human glycogen synthase kinase-3β promoter. Genomics60(2), 121–128 (1999).
   PubMed Web of Science ®Google Scholar
• Russ C, Lovestone S, Powell JF. Identification of sequence variants and analysis of the role of the glycogen synthase kinase 3β gene and promoter in late onset Alzheimer’s disease. Mol. Psychiatry6(3), 320–324 (2001).
   PubMed Web of Science ®Google Scholar