CoChat
Sign Up
Cited by 451Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroscience and Neuropharmacology Research

GSK-3β, a pivotal kinase in Alzheimer disease

Open access
Llorens-Marítin, María, Jurado, Jerónimo, Hernández, Félix, Ávila, Jesús·2014·Frontiers in Molecular Neuroscience
DOI 10.3389/fnmol.2014.00046PMC PMC4033045
Open this paper in CoChat — free accountOpen PDF

Abstract

Alzheimer disease (AD) is the most common form of age-related dementia. The etiology of AD is considered to be multifactorial as only a negligible percentage of cases have a familial or genetic origin. Glycogen synthase kinase-3 (GSK-3) is regarded as a critical molecular link between the two histopathological hallmarks of the disease, namely senile plaques and neurofibrillary tangles. In this review, we summarize current data regarding the involvement of this kinase in several aspects of AD development and progression, as well as key observations highlighting GSK-3 as one of the most relevant targets for AD treatment.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.3389/fnmol.2014.00046

Cites

6 of 6 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • Inhibition of the tau kinases CDK5 or GSK-3β reduces Aβ-induced neuronal cell death and malfunction.

    “and inhibition of the tau kinases CDK5 or GSK-3β reduces Aβ-induced neuronal cell death and malfunction (Llorens-Marítin et al., 2014) suggesting that abnormal tau mediates some of the effects of Aβ.”

    From Wild-Type, but Not Mutant N296H, Human Tau Restores Aβ-Mediated Inhibition of LTP in Tau−/− mice (2017) · cites this paper as Llorens-Marítin et al., 2014

    In “GSK-3β as a Molecular Link Between Aβ and Tau” (page unavailable), the review says GSK-3β inhibition decreases Aβ-induced neurotoxicity in cultured neurons. Its “Synaptic Effects” section also says GSK-3β inhibitors protect synapses from Aβ. The cited passages discuss CDK-5 as a tau kinase but do not establish that inhibiting CDK5 reduces Aβ-induced neuronal death or malfunction. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Cites

Flagged first, then by citations

Research works printed but not linked: 163

  1. Alvarez A. R. Godoy J. A. Mullendorff K. Olivares G. H. Bronfman M. Inestrosa N. C. (2004). Wnt-3a overcomes beta-amyloid toxicity in rat hippocampal neurons. Exp. Cell Res. 297 186– 196 10.1016/j.yexcr.2004.02.028 15194435 · DOI
  2. Alzheimer’s Association. (2012). 2012 Alzheimer’s disease facts and figures. Alzheimers Dement. 8 131– 168 10.1016/j.jalz.2012.02.001 22404854 · DOI
  3. Arendt T. (2003). Synaptic plasticity and cell cycle activation in neurons are alternative effector pathways: the ‘Dr. Jekyll and Mr. Hyde concept’ of Alzheimer’s disease or the yin and yang of neuroplasticity. Prog. Neurobiol. 71 83– 248 10.1016/j.pneurobio.2003.09.007 14687983 · DOI
  4. Arendt T. (2009). Synaptic degeneration in Alzheimer’s disease. Acta Neuropathol. 118 167– 179 10.1007/s00401-009-0536-x 19390859 · DOI · Paper page
  5. Arendt T. Rodel L. Gartner U. Holzer M. (1996). Expression of the cyclin-dependent kinase inhibitor p16 in Alzheimer’s disease. Neuroreport 7 3047– 3049 10.1097/00001756-199611250-00050 9116237 · DOI · Paper page
  6. Augustinack J. C. Schneider A. Mandelkow E. M. Hyman B. T. (2002). Specific tau phosphorylation sites correlate with severity of neuronal cytopathology in Alzheimer’s disease. Acta Neuropathol. 103 26– 35 10.1007/s004010100423 11837744 · DOI · Paper page
  7. Avrahami L. Farfara D. Shaham-Kol M. Vassar R. Frenkel D. Eldar-Finkelman H. (2013). Inhibition of glycogen synthase kinase-3 ameliorates beta-amyloid pathology and restores lysosomal acidification and mammalian target of rapamycin activity in the Alzheimer disease mouse model: in vivo and in vitro studies. J. Biol. Chem. 288 1295– 1306 10.1074/jbc.M112.409250 23155049 PMC3543013 · DOI
  8. Bartzokis G. Cummings J. L. Sultzer D. Henderson V. W. Nuechterlein K. H. Mintz J. (2003). White matter structural integrity in healthy aging adults and patients with Alzheimer disease: a magnetic resonance imaging study. Arch. Neurol. 60 393– 398 10.1001/archneur.60.3.393 12633151 · DOI
  9. Bastrikova N. Gardner G. A. Reece J. M. Jeromin A. Dudek S. M. (2008). Synapse elimination accompanies functional plasticity in hippocampal neurons. Proc. Natl. Acad. Sci. U.S.A. 105 3123– 3127 10.1073/pnas.0800027105 18287055 PMC2268595 · DOI
  10. Beurel E. Jope R. S. (2006). The paradoxical pro- and anti-apoptotic actions of GSK3 in the intrinsic and extrinsic apoptosis signaling pathways. Prog. Neurobiol. 79 173– 189 10.1016/j.pneurobio.2006.07.006 16935409 PMC1618798 · DOI
  11. Bhat R. Xue Y. Berg S. Hellberg S. Ormo M. Nilsson Y. (2003). Structural insights and biological effects of glycogen synthase kinase 3-specific inhibitor AR-A014418. J. Biol. Chem. 278 45937– 45945 10.1074/jbc.M306268200 12928438 · DOI
  12. Bhatt D. H. Zhang S. Gan W. B. (2009). Dendritic spine dynamics. Annu. Rev. Physiol. 71 261– 282 10.1146/annurev.physiol.010908.163140 19575680 · DOI · Paper page
  13. Bijur G. N. De Sarno P. Jope R. S. (2000). Glycogen synthase kinase-3beta facilitates staurosporine- and heat shock-induced apoptosis. Protection by lithium. J. Biol. Chem. 275 7583– 7590 10.1074/jbc.275.11.7583 10713065 · DOI
  14. Billingsley M. L. Kincaid R. L. (1997). Regulated phosphorylation and dephosphorylation of tau protein: effects on microtubule interaction, intracellular trafficking and neurodegeneration. Biochem. J. 323(Pt 3) 577– 591 9169588 PMC1218358
  15. Bischofberger J. (2007). Young and excitable: new neurons in memory networks. Nat. Neurosci. 10 273– 275 10.1038/nn0307-273 17318218 · DOI
  16. Blennow K. de Leon M. J. Zetterberg H. (2006). Alzheimer’s disease. Lancet 368 387– 403 10.1016/S0140-6736(06)69113-7 16876668 · DOI · Paper page
  17. Bradley C. A. Peineau S. Taghibiglou C. Nicolas C. S. Whitcomb D. J. Bortolotto Z. A. (2012). A pivotal role of GSK-3 in synaptic plasticity. Front. Mol. Neurosci. 5: 13 10.3389/fnmol.2012.00013 PMC3279748 22363262 · DOI
  18. Bretteville A. Planel E. (2008). Tau aggregates: toxic, inert, or protective species? J. Alzheimers Dis. 14 431– 436 18688094
  19. Buxbaum J. D. Thinakaran G. Koliatsos V. O’Callahan J. Slunt H. H. Price D. L. (1998). Alzheimer amyloid protein precursor in the rat hippocampus: transport and processing through the perforant path. J. Neurosci. 18 9629– 9637 9822724 PMC6793291
  20. Caccamo A. Oddo S. Tran L. X. 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 10.2353/ajpath.2007.061178 17456772 PMC1854961 · DOI
  21. Cai H. Wang Y. McCarthy D. Wen H. Borchelt D. R. Price D. L. (2001). BACE1 is the major beta-secretase for generation of Abeta peptides by neurons. Nat. Neurosci. 4 233– 234 10.1038/85064 11224536 · DOI
  22. Cai Z. Zhao Y. Zhao B. (2012). Roles of glycogen synthase kinase 3 in Alzheimer’s disease. Curr. Alzheimer Res. 9 864– 879 10.2174/156720512802455386 22272620 · DOI
  23. Coghlan M. P. Culbert A. A. Cross D. A. Corcoran S. L. Yates J. W. Pearce N. J. (2000). Selective small molecule inhibitors of glycogen synthase kinase-3 modulate glycogen metabolism and gene transcription. Chem. Biol. 7 793– 803 10.1016/S1074-5521(00)00025-9 11033082 · DOI
  24. Cross D. A. Alessi D. R. Cohen P. Andjelkovich M. Hemmings B. A. (1995). Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature 378 785– 789 10.1038/378785a0 8524413 · DOI · Paper page
  25. Christian S. L. Sims P. V. Gold M. R. (2002). The B cell antigen receptor regulates the transcriptional activator beta-catenin via protein kinase C-mediated inhibition of glycogen synthase kinase-3. J. Immunol. 169 758– 769 10.4049/jimmunol.169.2.758 12097378 · DOI
  26. Chun J. Kwon T. Lee E. J. Kim C. H. Han Y. S. Hong S. K. (2004). 14-3-3 Protein mediates phosphorylation of microtubule-associated protein tau by serum- and glucocorticoid-induced protein kinase 1. Mol. Cells 18 360– 368 15650334
  27. Cullen W. K. Suh Y. H. Anwyl R. Rowan M. J. (1997). Block of LTP in rat hippocampus in vivo by beta-amyloid precursor protein fragments. Neuroreport 8 3213– 3217 10.1097/00001756-199710200-00006 9351645 · DOI
  28. De Ferrari G. V. Chacon M. A. Barria M. I. Garrido J. L. Godoy J. A. Olivares G. (2003). Activation of Wnt signaling rescues neurodegeneration and behavioral impairments induced by beta-amyloid fibrils. Mol. Psychiatry 8 195– 208 10.1038/sj.mp.4001208 12610652 · DOI
  29. del Ser T. Steinwachs K. C. Gertz H. J. Andres M. V. Gomez-Carrillo B. Medina M. (2013). Treatment of Alzheimer’s disease with the GSK-3 inhibitor tideglusib: a pilot study. J. Alzheimers Dis. 33 205– 215 10.3233/JAD-2012-120805 22936007 · DOI · Paper page
  30. Deng Y. Xiong Z. Chen P. Wei J. Chen S. S. Yan Z. (2014). beta-amyloid impairs the regulation of N-methyl-D-aspartate receptors by glycogen synthase kinase 3. Neurobiol. Aging 35 449– 459 10.1016/j.neurobiolaging.2013.08.031 24094580 PMC7034321 · DOI
  31. Dewachter I. Ris L. Jaworski T. Seymour C. M. Kremer A. Borghgraef P. (2009). GSK3beta, a centre-staged kinase in neuropsychiatric disorders, modulates long term memory by inhibitory phosphorylation at serine-9. Neurobiol. Dis. 35 193– 200 10.1016/j.nbd.2009.04.003 19379814 · DOI
  32. Dickson D. W. Ksiezak-Reding H. Liu W. K. Davies P. Crowe A. Yen S. H. (1992). Immunocytochemistry of neurofibrillary tangles with antibodies to subregions of tau protein: identification of hidden and cleaved tau epitopes and a new phosphorylation site. Acta Neuropathol. 84 596– 605 10.1007/BF00227736 1281953 · DOI
  33. Ding Y. Qiao A. Fan G. H. (2010). Indirubin-3′-monoxime rescues spatial memory deficits and attenuates beta-amyloid-associated neuropathology in a mouse model of Alzheimer’s disease. Neurobiol. Dis. 39 156– 168 10.1016/j.nbd.2010.03.022 20381617 · DOI
  34. Doble B. W. Woodgett J. R. (2007). Role of glycogen synthase kinase-3 in cell fate and epithelial–mesenchymal transitions. Cells Tissues Organs 185 73– 84 10.1159/000101306 17587811 · DOI
  35. Du J. Wei Y. Liu L. Wang Y. Khairova R. Blumenthal R. (2010). A kinesin signaling complex mediates the ability of GSK-3beta to affect mood-associated behaviors. Proc. Natl. Acad. Sci. U.S.A. 107 11573– 11578 10.1073/pnas.0913138107 20534517 PMC2895136 · DOI
  36. Egashira Y. Tanaka T. Soni P. Sakuragi S. Tominaga-Yoshino K. Ogura A. (2010). Involvement of the p75(NTR) signaling pathway in persistent synaptic suppression coupled with synapse elimination following repeated long-term depression induction. J. Neurosci. Res. 88 3433– 3446 10.1002/jnr.22505 20890994 · DOI
  37. Embi N. Rylatt D. B. Cohen P. (1980). Glycogen synthase kinase-3 from rabbit skeletal muscle. Separation from cyclic-AMP-dependent protein kinase and phosphorylase kinase. Eur. J. Biochem. 107 519– 527 10.1111/j.1432-1033.1980.tb06059.x 6249596 · DOI
  38. Engel T. Hernandez F. Avila J. Lucas J. J. (2006). 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 10.1523/JNEUROSCI.0604-06.2006 16687499 PMC6674262 · DOI
  39. Fang X. Yu S. X. Lu Y. Bast R. C. Woodgett J. R. Jr. Mills G. B. (2000). Phosphorylation and inactivation of glycogen synthase kinase 3 by protein kinase A. Proc. Natl. Acad. Sci. U.S.A. 97 11960– 11965 10.1073/pnas.220413597 11035810 PMC17277 · DOI
  40. Ferrari A. Hoerndli F. Baechi T. Nitsch R. M. Gotz J. (2003). beta-Amyloid induces paired helical filament-like tau filaments in tissue culture. J. Biol. Chem. 278 40162– 40168 10.1074/jbc.M308243200 12893817 · DOI
  41. Fiorentini A. Rosi M. C. Grossi C. Luccarini I. Casamenti F. (2010). Lithium improves hippocampal neurogenesis, neuropathology and cognitive functions in APP mutant mice. PLoS ONE 5: e14382 10.1371/journal.pone.0014382 PMC3004858 21187954 · DOI
  42. Forde J. E. Dale T. C. (2007). Glycogen synthase kinase 3: a key regulator of cellular fate. Cell. Mol. Life Sci. 64 1930– 1944 10.1007/s00018-007-7045-7 17530463 PMC11136264 · DOI
  43. Forlenza O. V. de Paula V. J. Machado-Vieira R. Diniz B. S. Gattaz W. F. (2012). Does lithium prevent Alzheimer’s disease? Drugs Aging 29 335– 342 10.2165/11599180-000000000-00000 22500970 · DOI
  44. Forlenza O. V. Diniz B. S. Radanovic M. Santos F. S. Talib L. L. Gattaz W. F. (2011). Disease-modifying properties of long-term lithium treatment for amnestic mild cognitive impairment: randomised controlled trial. Br. J. Psychiatry 198 351– 356 10.1192/bjp.bp.110.080044 21525519 · DOI
  45. Fukumoto S. Hsieh C. M. Maemura K. Layne M. D. Yet S. F. Lee K. H. (2001). Akt participation in the Wnt signaling pathway through Dishevelled. J. Biol. Chem. 276 17479– 17483 10.1074/jbc.C000880200 11278246 · DOI
  46. Fuster-Matanzo A. Llorens-Martin M. de Barreda E. G. Avila J. Hernandez F. (2011). Different susceptibility to neurodegeneration of dorsal and ventral hippocampal dentate gyrus: a study with transgenic mice overexpressing GSK3beta. PLoS ONE 6: e27262 10.1371/journal.pone.0027262 PMC3207840 22073301 · DOI
  47. Fuster-Matanzo A. Llorens-Martin M. Jurado-Arjona J. Avila J. Hernandez F. (2012). Tau protein and adult hippocampal neurogenesis. Front. Neurosci. 6: 104 10.3389/fnins.2012.00104 PMC3391648 22787440 · DOI
  48. Fuster-Matanzo A. Llorens-Martin M. Sirerol-Piquer M. S. Garcia-Verdugo J. M. Avila J. Hernandez F. (2013). Dual effects of increased glycogen synthase kinase-3beta activity on adult neurogenesis. Hum. Mol. Genet. 22 1300– 1315 10.1093/hmg/dds533 23257288 · DOI
  49. Ghosal K. Vogt D. L. Liang M. Shen Y. Lamb B. T. Pimplikar S. W. (2009). Alzheimer’s disease-like pathological features in transgenic mice expressing the APP intracellular domain. Proc. Natl. Acad. Sci. U.S.A. 106 18367– 18372 10.1073/pnas.0907652106 19837693 PMC2762847 · DOI · Paper page
  50. Godemann R. Biernat J. Mandelkow E. Mandelkow E. M. (1999). Phosphorylation of tau protein by recombinant GSK-3beta: pronounced phosphorylation at select Ser/Thr-Pro motifs but no phosphorylation at Ser262 in the repeat domain. FEBS Lett. 454 157– 164 10.1016/S0014-5793(99)00741-3 10413115 · DOI
  51. Gomez de Barreda E. Perez M. Gomez Ramos P. de Cristobal J. Martin-Maestro P. Moran A. (2010). Tau-knockout mice show reduced GSK3-induced hippocampal degeneration and learning deficits. Neurobiol. Dis. 37 622– 629 10.1016/j.nbd.2009.11.017 20004245 · DOI
  52. Gomez-Sintes R. Hernandez F. Bortolozzi A. Artigas F. Avila J. J. Zaratin P. (2007). Neuronal apoptosis and reversible motor deficit in dominant-negative GSK-3 conditional transgenic mice. EMBO J. 26 2743– 2754 10.1038/sj.emboj.7601725 17510631 PMC1888681 · DOI
  53. Gomez-Sintes R. Hernandez F. Lucas J. J. Avila J. (2011). GSK-3 mouse models to study neuronal apoptosis and neurodegeneration. Front. Mol. Neurosci. 4: 45 10.3389/fnmol.2011.00045 PMC3217194 22110426 · DOI
  54. Goni-Oliver P. Avila J. Hernandez F. (2009). Calpain-mediated truncation of GSK-3 in post-mortem brain samples. J. Neurosci. Res. 87 1156– 1161 10.1002/jnr.21932 19006085 · DOI
  55. Goni-Oliver P. Lucas J. J. Avila J. Hernandez F. (2007). N-terminal cleavage of GSK-3 by calpain: a new form of GSK-3 regulation. J. Biol. Chem. 282 22406– 22413 10.1074/jbc.M702793200 17569662 · DOI
  56. Gotz J. Probst A. Spillantini M. G. Schafer T. Jakes R. Burki K. (1995). Somatodendritic localization and hyperphosphorylation of tau protein in transgenic mice expressing the longest human brain tau isoform. EMBO J. 14 1304– 1313 7729409 PMC398215
  57. Hanger D. P. Byers H. L. Wray S. Leung K. Y. Saxton M. J. Seereeram A. (2007). Novel phosphorylation sites in tau from Alzheimer brain support a role for casein kinase 1 in disease pathogenesis. J. Biol. Chem. 282 23645– 23654 10.1074/jbc.M703269200 17562708 · DOI · Paper page
  58. Hashiguchi M. Hashiguchi T. (2013). Kinase-kinase interaction and modulation of tau phosphorylation. Int. Rev. Cell Mol. Biol. 300 121– 160 10.1016/B978-0-12-405210-9.00004-7 23273861 · DOI
  59. Hebert L. E. Beckett L. A. Scherr P. A. Evans D. A. (2001). Annual incidence of Alzheimer disease in the United States projected to the years 2000 through 2050. Alzheimer Dis. Assoc. Disord. 15 169– 173 10.1097/00002093-200110000-00002 11723367 · DOI · Paper page
  60. Hernandez F. Borrell J. Guaza C. Avila J. Lucas J. J. (2002). Spatial learning deficit in transgenic mice that conditionally over-express GSK-3beta in the brain but do not form tau filaments. J. Neurochem. 83 1529– 1533 10.1046/j.1471-4159.2002.01269.x 12472906 · DOI · Paper page
  61. Holsinger R. M. McLean C. A. Beyreuther K. Masters C. L. Evin G. (2002). Increased expression of the amyloid precursor beta-secretase in Alzheimer’s disease. Ann. Neurol. 51 783– 786 10.1002/ana.10208 12112088 · DOI · Paper page
  62. Hooper C. Markevich V. Plattner F. Killick R. Schofield E. Engel T. (2007). Glycogen synthase kinase-3 inhibition is integral to long-term potentiation. Eur. J. Neurosci. 25 81– 86 10.1111/j.1460-9568.2006.05245.x 17241269 · DOI
  63. Hoshi M. Takashima A. Noguchi K. Murayama M. Sato M. Kondo S. (1996). Regulation of mitochondrial pyruvate dehydrogenase activity by tau protein kinase I/glycogen synthase kinase 3beta in brain. Proc. Natl. Acad. Sci. U.S.A. 93 2719– 2723 10.1073/pnas.93.7.2719 8610107 PMC39697 · DOI
  64. Hurtado D. E. Molina-Porcel L. Carroll J. C. Macdonald C. Aboagye A. K. Trojanowski J. Q. (2012). Selectively silencing GSK-3 isoforms reduces plaques and tangles in mouse models of Alzheimer’s disease. J. Neurosci. 32 7392– 7402 10.1523/JNEUROSCI.0889-12.2012 22623685 PMC3368584 · DOI · Paper page
  65. Illenberger S. Zheng-Fischhofer Q. Preuss U. Stamer K. Baumann K. Trinczek B. (1998). The endogenous and cell cycle-dependent phosphorylation of tau protein in living cells: implications for Alzheimer’s disease. Mol. Biol. Cell 9 1495– 1512 10.1091/mbc.9.6.1495 9614189 PMC25374 · DOI
  66. Isaac J. T. Nicoll R. A. Malenka R. C. (1995). Evidence for silent synapses: implications for the expression of LTP. Neuron 15 427– 434 10.1016/0896-6273(95)90046-2 7646894 · DOI · Paper page
  67. Jimenez-Mateos E. M. Gonzalez-Billault C. Dawson H. N. Vitek M. P. Avila J. (2006). Role of MAP1B in axonal retrograde transport of mitochondria. Biochem. J. 397 53– 59 10.1042/BJ20060205 16536727 PMC1479764 · DOI · Paper page
  68. Johnson-Farley N. N. Travkina T. Cowen D. S. (2006). Cumulative activation of Akt and consequent inhibition of glycogen synthase kinase-3 by brain-derived neurotrophic factor and insulin-like growth factor-1 in cultured hippocampal neurons. J. Pharmacol. Exp. Ther. 316 1062– 1069 10.1124/jpet.105.094433 16284277 · DOI · Paper page
  69. Jope R. S. (2003). Lithium and GSK-3: one inhibitor, two inhibitory actions, multiple outcomes. Trends Pharmacol. Sci. 24 441– 443 10.1016/S0165-6147(03)00206-2 12967765 · DOI
  70. Jope R. S. (2011). Glycogen synthase kinase-3 in the etiology and treatment of mood disorders. Front. Mol. Neurosci. 4: 16 10.3389/fnmol.2011.00016 PMC3152743 21886606 · DOI
  71. Jope R. S. Yuskaitis C. J. Beurel E. (2007). Glycogen synthase kinase-3 (GSK3): inflammation, diseases, and therapeutics. Neurochem. Res. 32 577– 595 10.1007/s11064-006-9128-5 16944320 PMC1970866 · DOI · Paper page
  72. Kaidanovich-Beilin O. Milman A. Weizman A. Pick C. G. Eldar-Finkelman H. (2004). Rapid antidepressive-like activity of specific glycogen synthase kinase-3 inhibitor and its effect on beta-catenin in mouse hippocampus. Biol. Psychiatry 55 781– 784 10.1016/j.biopsych.2004.01.008 15050857 · DOI
  73. Kannan N. Neuwald A. F. (2004). Evolutionary constraints associated with functional specificity of the CMGC protein kinases MAPK, CDK, GSK, SRPK, DYRK, and CK2alpha. Protein Sci. 13 2059– 2077 10.1110/ps.04637904 15273306 PMC2279817 · DOI
  74. Kempermann G. Kuhn H. G. Gage F. H. (1998). Experience-induced neurogenesis in the senescent dentate gyrus. J. Neurosci. 18 3206– 3212 9547229 PMC6792643
  75. Kessing L. V. Forman J. L. Andersen P. K. (2010). Does lithium protect against dementia? Bipolar Disord. 12 87– 94 10.1111/j.1399-5618.2009.00788.x 20148870 · DOI
  76. Kimura T. Yamashita S. Nakao S. Park J. M. Murayama M. Mizoroki T. (2008). GSK-3beta is required for memory reconsolidation in adult brain. PLoS ONE 3: e3540 10.1371/journal.pone.0003540 PMC2568810 18958152 · DOI
  77. King M. K. Pardo M. Cheng Y. Downey K. Jope R. S. Beurel E. (2014). Glycogen synthase kinase-3 inhibitors: rescuers of cognitive impairments. Pharmacol. Ther. 141 1– 12 10.1016/j.pharmthera.2013.07.010 23916593 PMC3867580 · DOI
  78. Klein P. S. Melton D. A. (1996). A molecular mechanism for the effect of lithium on development. Proc. Natl. Acad. Sci. U.S.A. 93 8455– 8459 10.1073/pnas.93.16.8455 8710892 PMC38692 · DOI
  79. Knoth R. Singec I. Ditter M. Pantazis G. Capetian P. Meyer R. P. (2010). Murine features of neurogenesis in the human hippocampus across the lifespan from 0 to 100 years. PLoS ONE 5: e8809 10.1371/journal.pone.0008809 PMC2813284 20126454 · DOI · Paper page
  80. Koh S. H. Noh M. Y. Kim S. H. (2008). Amyloid-beta-induced neurotoxicity is reduced by inhibition of glycogen synthase kinase-3. Brain Res. 1188 254– 262 10.1016/j.brainres.2007.10.064 18031715 · DOI
  81. Koike H. Tomioka S. Sorimachi H. Saido T. C. Maruyama K. Okuyama A. (1999). Membrane-anchored metalloprotease MDC9 has an alpha-secretase activity responsible for processing the amyloid precursor protein. Biochem. J. 343(Pt 2) 371– 375 10.1042/0264-6021:3430371 10510302 PMC1220563 · DOI
  82. Kokubo H. Kayed R. Glabe C. G. Yamaguchi H. (2005). Soluble Abeta oligomers ultrastructurally localize to cell processes and might be related to synaptic dysfunction in Alzheimer’s disease brain. Brain Res. 1031 222– 228 10.1016/j.brainres.2004.10.041 15649447 · DOI
  83. Leclerc S. Garnier M. Hoessel R. Marko D. Bibb J. A. Snyder G. L. (2001). Indirubins inhibit glycogen synthase kinase-3 beta and CDK5/p25, two protein kinases involved in abnormal tau phosphorylation in Alzheimer’s disease. A property common to most cyclin-dependent kinase inhibitors? J. Biol. Chem. 276 251– 260 10.1074/jbc.M002466200 11013232 · DOI
  84. Leost M. Schultz C. Link A. Wu Y. Z. Biernat J. Mandelkow E. M. (2000). Paullones are potent inhibitors of glycogen synthase kinase-3beta and cyclin-dependent kinase 5/p25. Eur. J. Biochem. 267 5983– 5994 10.1046/j.1432-1327.2000.01673.x 10998059 · DOI
  85. Leroy K. Yilmaz Z. Brion J. P. (2007). Increased level of active GSK-3beta in Alzheimer’s disease and accumulation in argyrophilic grains and in neurones at different stages of neurofibrillary degeneration. Neuropathol. Appl. Neurobiol. 33 43– 55 10.1111/j.1365-2990.2006.00795.x 17239007 · DOI · Paper page
  86. Leyhe T. Eschweiler G. W. Stransky E. Gasser T. Annas P. Basun H. (2009). Increase of BDNF serum concentration in lithium treated patients with early Alzheimer’s disease. J. Alzheimers Dis. 16 649– 656 10.3233/JAD-2009-1004 19276559 · DOI
  87. Li T. Hawkes C. Qureshi H. Y. Kar S. Paudel H. K. (2006). Cyclin-dependent protein kinase 5 primes microtubule-associated protein tau site-specifically for glycogen synthase kinase 3beta. Biochemistry 45 3134– 3145 10.1021/bi051635j 16519508 · DOI
  88. Liao D. Hessler N. A. Malinow R. (1995). Activation of postsynaptically silent synapses during pairing-induced LTP in CA1 region of hippocampal slice. Nature 375 400– 404 10.1038/375400a0 7760933 · DOI · Paper page
  89. Liu X. S. Xue Q. S. Zeng Q. W. Li Q. Liu J. Feng X. M. (2010). Sevoflurane impairs memory consolidation in rats, possibly through inhibiting phosphorylation of glycogen synthase kinase-3beta in the hippocampus. Neurobiol. Learn. Mem. 94 461– 467 10.1016/j.nlm.2010.08.011 20807582 · DOI
  90. Llorens-Martin M. Fuster-Matanzo A. Teixeira C. M. Jurado-Arjona J. Ulloa F. (2013). GSK-3beta overexpression causes reversible alterations on postsynaptic densities and dendritic morphology of hippocampal granule neurons in vivo. Mol. Psychiatry 18 451– 460 10.1038/mp.2013.4 23399915 · DOI
  91. Llorens-Martin M. Lopez-Domenech G. Soriano E. Avila J. (2011). GSK3beta is involved in the relief of mitochondria pausing in a tau-dependent manner. PLoS ONE 6: e27686 10.1371/journal.pone.0027686 PMC3215736 22110721 · DOI
  92. Loberg R. D. Vesely E Brosius F. C. III. (2002). Enhanced glycogen synthase kinase-3beta activity mediates hypoxia-induced apoptosis of vascular smooth muscle cells and is prevented by glucose transport and metabolism. J. Biol. Chem. 277 41667– 41673 10.1074/jbc.M206405200 12200436 · DOI
  93. Lovestone S. Hartley C. L. Pearce J. Anderton B. H. (1996). Phosphorylation of tau by glycogen synthase kinase-3 beta in intact mammalian cells: the effects on the organization and stability of microtubules. Neuroscience 73 1145– 1157 10.1016/0306-4522(96)00126-1 8809831 · DOI · Paper page
  94. Lucas J. J. Hernandez F. Gomez-Ramos P. Moran M. A. Hen R. Avila J. (2001). Decreased nuclear beta-catenin, tau hyperphosphorylation and neurodegeneration in GSK-3beta conditional transgenic mice. EMBO J. 20 27– 39 10.1093/emboj/20.1.27 11226152 PMC140191 · DOI
  95. Luna-Munoz J. Chavez-Macias L. Garcia-Sierra F. Mena R. (2007). Earliest stages of tau conformational changes are related to the appearance of a sequence of specific phospho-dependent tau epitopes in Alzheimer’s disease. J. Alzheimers Dis. 12 365– 375 18198423
  96. Luo Y. Bolon B. Kahn S. Bennett B. D. Babu-Khan S. Denis P. (2001). Mice deficient in BACE1, the Alzheimer’s beta-secretase, have normal phenotype and abolished beta-amyloid generation. Nat. Neurosci. 4 231– 232 10.1038/85059 11224535 · DOI · Paper page
  97. Luthi A. Chittajallu R. Duprat F. Palmer M. J. Benke T. A. Kidd F. L. (1999). Hippocampal LTD expression involves a pool of AMPARs regulated by the NSF–GluR2 interaction. Neuron 24 389– 399 10.1016/S0896-6273(00)80852-1 10571232 · DOI
  98. Macdonald A. Briggs K. Poppe M. Higgins A. Velayudhan L. Lovestone S. (2008). A feasibility and tolerability study of lithium in Alzheimer’s disease. Int. J. Geriatr. Psychiatry 23 704– 711 10.1002/gps.1964 18181229 · DOI
  99. Magdesian M. H. Carvalho M. M. Mendes F. A. Saraiva L. M. Juliano M. A. Juliano L. J. (2008). Amyloid-beta binds to the extracellular cysteine-rich domain of Frizzled and inhibits Wnt/beta-catenin signaling. J. Biol. Chem. 283 9359– 9368 10.1074/jbc.M707108200 18234671 PMC2431018 · DOI
  100. Manahan-Vaughan D. (2010). MicroRNAs contribute to LTP in the hippocampus in vivo (Commentary on Wibrand et al.). Eur. J. Neurosci. 31 634– 635 10.1111/j.1460-9568.2010.07140.x 20384809 · DOI
  101. Martin M. Rehani K. Jope R. S. Michalek S. M. (2005). Toll-like receptor-mediated cytokine production is differentially regulated by glycogen synthase kinase 3. Nat. Immunol. 6 777– 784 10.1038/ni1221 16007092 PMC1933525 · DOI
  102. Martinez A. Alonso M. Castro A. Perez C. Moreno F. J. (2002). First non-ATP competitive glycogen synthase kinase 3 beta (GSK-3beta) inhibitors: thiadiazolidinones (TDZD) as potential drugs for the treatment of Alzheimer’s disease. J. Med. Chem. 45 1292– 1299 10.1021/jm011020u 11881998 · DOI
  103. Martinez A. Gil C. Perez D. I. (2011). Glycogen synthase kinase 3 inhibitors in the next horizon for Alzheimer’s disease treatment. Int. J. Alzheimers Dis. 2011 280502 10.4061/2011/280502 PMC3132520 21760986 · DOI
  104. Montenegro-Venegas C. Tortosa E. Rosso S. Peretti D. Bollati F. Bisbal M. (2010). MAP1B regulates axonal development by modulating Rho-GTPase Rac1 activity. Mol. Biol. Cell 21 3518– 3528 10.1091/mbc.E09-08-0709 20719958 PMC2954117 · DOI
  105. Nagy Z. Esiri M. M. Cato A. M. Smith A. D. (1997a). Cell cycle markers in the hippocampus in Alzheimer’s disease. Acta Neuropathol. 94 6– 15 10.1007/s004010050665 9224524 · DOI
  106. Nagy Z. Esiri M. M. Smith A. D. (1997b). Expression of cell division markers in the hippocampus in Alzheimer’s disease and other neurodegenerative conditions. Acta Neuropathol. 93 294– 300 10.1007/s004010050617 9083562 · DOI
  107. Nunes P. V. Forlenza O. V. Gattaz W. F. (2007). Lithium and risk for Alzheimer’s disease in elderly patients with bipolar disorder. Br. J. Psychiatry 190 359– 360 10.1192/bjp.bp.106.029868 17401045 · DOI
  108. Palomo V. Soteras I. Perez D. I. Perez C. Gil C. Campillo N. E. (2011). Exploring the binding sites of glycogen synthase kinase 3. Identification and characterization of allosteric modulation cavities. J. Med. Chem. 54 8461– 8470 10.1021/jm200996g 22050263 · DOI
  109. Pap M. Cooper G. M. (1998). Role of glycogen synthase kinase-3 in the phosphatidylinositol 3-kinase/Akti cell survival pathway. J. Biol. Chem. 273 19929– 19932 10.1074/jbc.273.32.19929 9685326 · DOI
  110. Pap M. Cooper G. M. (2002). Role of translation initiation factor 2B in control of cell survival by the phosphatidylinositol 3-kinase/Akt/glycogen synthase kinase 3beta signaling pathway. Mol. Cell. Biol. 22 578– 586 10.1128/MCB.22.2.578-586.2002 11756553 PMC139729 · DOI
  111. Peineau S. Taghibiglou C. Bradley C. Wong T. P. Liu L. Lu J. (2007). LTP inhibits LTD in the hippocampus via regulation of GSK3beta. Neuron 53 703– 717 10.1016/j.neuron.2007.01.029 17329210 · DOI
  112. Phiel C. J. Wilson C. A. Lee V. M. Klein P. S. (2003). GSK-3alpha regulates production of Alzheimer’s disease amyloid-beta peptides. Nature 423 435– 439 10.1038/nature01640 12761548 · DOI
  113. Pigino G. G. Morfini Pelsman A. Mattson M. P. Brady S. T. Busciglio J. (2003). Alzheimer’s presenilin 1 mutations impair kinesin-based axonal transport. J. Neurosci. 23 4499– 4508 12805290 PMC6740780
  114. Plattner F. Angelo M. Giese K. P. (2006). The roles of cyclin-dependent kinase 5 and glycogen synthase kinase 3 in tau hyperphosphorylation. J. Biol. Chem. 281 25457– 25465 10.1074/jbc.M603469200 16803897 · DOI · Paper page
  115. Plotkin B. Kaidanovich O. Talior I. Eldar-Finkelman H. (2003). Insulin mimetic action of synthetic phosphorylated peptide inhibitors of glycogen synthase kinase-3. J. Pharmacol. Exp. Ther. 305 974– 980 10.1124/jpet.102.047381 12626660 · DOI
  116. Plotkin D. A. Jarvik L. F. (1986). Cholinergic dysfunction in Alzheimer disease: cause or effect? Prog. Brain Res. 65 91– 103 10.1016/S0079-6123(08)60644-5 2878469 · DOI
  117. Pomara N. (2009). Lithium treatment in Alzheimer’s disease does not promote cognitive enhancement, but may exert long-term neuroprotective effects. Psychopharmacology (Berl.) 205 169– 170 10.1007/s00213-009-1510-y 19300981 · DOI
  118. Pope W. Enam S. A. Bawa N. Miller B. E. Ghanbari H. A. Klein W. L. (1993). Phosphorylated tau epitope of Alzheimer’s disease is coupled to axon development in the avian central nervous system. Exp. Neurol. 120 106– 113 10.1006/exnr.1993.1044 7682967 · DOI
  119. Rabacchi S. A. Bailly Y. Delhaye-Bouchaud N. Herrup K. Mariani J. (1992). Role of the target in synapse elimination: studies in cerebellum of developing lurcher mutants and adult chimeric mice. J. Neurosci. 12 4712– 4720 1464763 PMC6575771
  120. Rapoport M. Dawson H. N. Binder L. I. Vitek M. P. Ferreira A. (2002). Tau is essential to beta -amyloid-induced neurotoxicity. Proc. Natl. Acad. Sci. U.S.A. 99 6364– 6369 10.1073/pnas.092136199 11959919 PMC122954 · DOI · Paper page
  121. Rauk A. (2008). Why is the amyloid beta peptide of Alzheimer’s disease neurotoxic? Dalton Trans. 1273– 1282 10.1039/b718601k 18305836 · DOI · Paper page
  122. Roberson E. D. Scearce-Levie K. Palop J. J. Yan F. Cheng I. H. Wu T. (2007). Reducing endogenous tau ameliorates amyloid beta-induced deficits in an Alzheimer’s disease mouse model. Science 316 750– 754 10.1126/science.1141736 17478722 · DOI · Paper page
  123. Robert M. Mathuranath P. S. (2007). Tau and tauopathies. Neurol. India 55 11– 16 10.4103/0028-3886.30420 17272893 · DOI
  124. Rockenstein E. Crews L. Masliah E. (2007a). Transgenic animal models of neurodegenerative diseases and their application to treatment development. Adv. Drug Deliv. Rev. 59 1093– 1102 10.1016/j.addr.2007.08.013 17869376 · DOI
  125. Rockenstein E. Torrance M. Adame A. Mante M. Bar-On P. Rose J. B. (2007b). Neuroprotective effects of regulators of the glycogen synthase kinase-3beta signaling pathway in a transgenic model of Alzheimer’s disease are associated with reduced amyloid precursor protein phosphorylation. J. Neurosci. 27 1981– 1991 10.1523/JNEUROSCI.4321-06.2007 17314294 PMC6673566 · DOI
  126. Ryan K. A. Pimplikar S. W. (2005). Activation of GSK-3 and phosphorylation of CRMP2 in transgenic mice expressing APP intracellular domain. J. Cell Biol. 171 327– 335 10.1083/jcb.200505078 16230462 PMC2171208 · DOI
  127. Saeki K. Machida M. Kinoshita Y. Takasawa R. Tanuma S. (2011). Glycogen synthase kinase-3beta2 has lower phosphorylation activity to tau than glycogen synthase kinase-3beta1. Biol. Pharm. Bull. 34 146– 149 10.1248/bpb.34.146 21212533 · DOI
  128. Saito Y. Vandenheede J. R. Cohen P. (1994). The mechanism by which epidermal growth factor inhibits glycogen synthase kinase 3 in A431 cells. Biochem. J. 303(Pt 1) 27– 31 7945252 PMC1137551
  129. Samadi A. Valderas C. de los Rios C. Bastida A. Chioua M. Gonzalez-Lafuente L. (2011). Cholinergic and neuroprotective drugs for the treatment of Alzheimer and neuronal vascular diseases. II. Synthesis, biological assessment, and molecular modelling of new tacrine analogues from highly substituted 2-aminopyridine-3-carbonitriles. Bioorg. Med. Chem. 19 122– 133 10.1016/j.bmc.2010.11.040 21163662 · DOI
  130. Sanchez C. Perez M. Avila J. (2000). GSK3beta-mediated phosphorylation of the microtubule-associated protein 2C (MAP2C) prevents microtubule bundling. Eur. J. Cell Biol. 79 252– 260 10.1078/S0171-9335(04)70028-X 10826493 · DOI
  131. Santacruz K. Lewis J. Spires T. Paulson J. Kotilinek L. Ingelsson M. (2005). Tau suppression in a neurodegenerative mouse model improves memory function. Science 309 476– 481 10.1126/science.1113694 16020737 PMC1574647 · DOI · Paper page
  132. Sengupta A. Kabat J. Novak M. Wu Q. Grundke-Iqbal I. Iqbal K. (1998). Phosphorylation of tau at both Thr 231 and Ser 262 is required for maximal inhibition of its binding to microtubules. Arch. Biochem. Biophys. 357 299– 309 10.1006/abbi.1998.0813 9735171 · DOI · Paper page
  133. Sengupta A. Novak M. Grundke-Iqbal I. Iqbal K. (2006). Regulation of phosphorylation of tau by cyclin-dependent kinase 5 and glycogen synthase kinase-3 at substrate level. FEBS Lett. 580 5925– 5933 10.1016/j.febslet.2006.09.060 17045592 PMC1679721 · DOI
  134. Sereno L. Coma M. Rodriguez M. Sanchez-Ferrer P. Sanchez M. B. Gich I. (2009). A novel GSK-3beta inhibitor reduces Alzheimer’s pathology and rescues neuronal loss in vivo. Neurobiol. Dis. 35 359– 367 10.1016/j.nbd.2009.05.025 19523516 · DOI · Paper page
  135. Sergeant N. Bretteville A. Hamdane M. Caillet-Boudin M. L. Grognet P. Bombois S. (2008). Biochemistry of tau in Alzheimer’s disease and related neurological disorders. Expert Rev. Proteomics 5 207– 224 10.1586/14789450.5.2.207 18466052 · DOI · Paper page
  136. Shipton O. A. Leitz J. R. Dworzak J. Acton C. E. Tunbridge E. M. Denk F. (2011). Tau protein is required for amyloid {beta}-induced impairment of hippocampal long-term potentiation. J. Neurosci. 31 1688– 1692 10.1523/JNEUROSCI.2610-10.2011 21289177 PMC3836238 · DOI · Paper page
  137. Sirerol-Piquer M. Gomez-Ramos P. Hernandez F. Perez M. Moran M. A. Fuster-Matanzo A. (2011). GSK3beta overexpression induces neuronal death and a depletion of the neurogenic niches in the dentate gyrus. Hippocampus 21 910– 922 20575007
  138. Soutar M. P. Kim W. Y. Williamson R. Peggie M. Hastie C. J. McLauchlan H. (2010). Evidence that glycogen synthase kinase-3 isoforms have distinct substrate preference in the brain. J. Neurochem. 115 974– 983 10.1111/j.1471-4159.2010.06988.x 20831597 · DOI
  139. Spittaels K. Van den Haute C. Van Dorpe J. Terwel D. Vandezande K. Lasrado R. (2002). Neonatal neuronal overexpression of glycogen synthase kinase-3 beta reduces brain size in transgenic mice. Neuroscience 113 797– 808 10.1016/S0306-4522(02)00236-1 12182887 · DOI
  140. Sudduth T. L. Schmitt F. A. Nelson P. T. Wilcock D. M. (2013). Neuroinflammatory phenotype in early Alzheimer’s disease. Neurobiol. Aging 34 1051– 1059 10.1016/j.neurobiolaging.2012.09.012 23062700 PMC3579221 · DOI
  141. Sudduth T. L. Wilson J. G. Everhart A. Colton C. A. Wilcock D. M. (2012). Lithium treatment of APPSwDI/NOS2-/- mice leads to reduced hyperphosphorylated tau, increased amyloid deposition and altered inflammatory phenotype. PLoS ONE 7: e31993 10.1371/journal.pone.0031993 PMC3276493 22347510 · DOI
  142. Sun W. Qureshi H. Y. Cafferty P. W. Sobue K. Agarwal-Mawal A. (2002). Glycogen synthase kinase-3beta is complexed with tau protein in brain microtubules. J. Biol. Chem. 277 11933– 11940 10.1074/jbc.M107182200 11812770 · DOI
  143. Sutherland C. Cohen P. (1994). The alpha-isoform of glycogen synthase kinase-3 from rabbit skeletal muscle is inactivated by p70 S6 kinase or MAP kinase-activated protein kinase-1 in vitro. FEBS Lett. 338 37– 42 10.1016/0014-5793(94)80112-6 8307153 · DOI
  144. Sutherland C. Leighton I. A. Cohen P. (1993). Inactivation of glycogen synthase kinase-3 beta by phosphorylation: new kinase connections in insulin and growth-factor signalling. Biochem. J. 296(Pt 1) 15– 19 8250835 PMC1137648
  145. Takashima A. Sato M. Mercken M. Tanaka S. Kondo S. Honda T. (1996b). Localization of Alzheimer-associated presenilin 1 in transfected COS-7 cells. Biochem. Biophys. Res. Commun. 227 423– 426 10.1006/bbrc.1996.1523 8878531 · DOI
  146. Terwel D. Muyllaert D. Dewachter I. Borghgraef P. Croes S. Devijver H. (2008). Amyloid activates GSK-3beta to aggravate neuronal tauopathy in bigenic mice. Am. J. Pathol. 172 786– 798 10.2353/ajpath.2008.070904 18258852 PMC2258274 · DOI · Paper page
  147. Thotala D. K. Hallahan D. E. Yazlovitskaya E. M. (2008). Inhibition of glycogen synthase kinase 3 beta attenuates neurocognitive dysfunction resulting from cranial irradiation. Cancer Res. 68 5859– 5868 10.1158/0008-5472.CAN-07-6327 18632640 · DOI
  148. Toledo E. M. Inestrosa N. C. (2010). Activation of Wnt signaling by lithium and rosiglitazone reduced spatial memory impairment and neurodegeneration in brains of an APPswe/PSEN1DeltaE9 mouse model of Alzheimer’s disease. Mol. Psychiatry 15 272– 285 228 10.1038/mp.2009.72 19621015 · DOI
  149. Uemura K. Kuzuya A. Shimozono Y. Aoyagi N. Ando K. Shimohama S. (2007). GSK3beta activity modifies the localization and function of presenilin 1. J. Biol. Chem. 282 15823– 15832 10.1074/jbc.M610708200 17389597 · DOI
  150. Van Hoesen G. W. Hyman B. T. Damasio A. R. (1991). Entorhinal cortex pathology in Alzheimer’s disease. Hippocampus 1 1– 8 10.1002/hipo.450010102 1669339 · DOI · Paper page
  151. Wang H. Wang R. Zhao Z. Ji Z. Xu S. Holscher C. (2009). Coexistences of insulin signaling-related proteins and choline acetyltransferase in neurons. Brain Res. 1249 237– 243 10.1016/j.brainres.2008.10.046 19013138 · DOI
  152. Wang Y. Ju W. Liu L. Fam S. D’Souza S. Taghibiglou C. (2004). alpha-Amino-3-hydroxy-5-methylisoxazole-4-propionic acid subtype glutamate receptor (AMPAR) endocytosis is essential for N-methyl-D-aspartate-induced neuronal apoptosis. J. Biol. Chem. 279 41267– 41270 10.1074/jbc.C400199200 15319422 · DOI
  153. Watcharasit P. Bijur G. N. Song L. Zhu J. Chen X. Jope R. S. (2003). Glycogen synthase kinase-3beta (GSK3beta) binds to and promotes the actions of p53. J. Biol. Chem. 278 48872– 48879 10.1074/jbc.M305870200 14523002 PMC1361697 · DOI
  154. Wei J. Liu W. Yan Z. (2010). Regulation of AMPA receptor trafficking and function by glycogen synthase kinase 3. J. Biol. Chem. 285 26369– 26376 10.1074/jbc.M110.121376 20584904 PMC2924064 · DOI
  155. Welsh G. I. Proud C. G. (1993). Glycogen synthase kinase-3 is rapidly inactivated in response to insulin and phosphorylates eukaryotic initiation factor eIF-2B. Biochem. J. 294(Pt 3) 625– 629 8397507 PMC1134506
  156. Whitehouse P. J. Price D. L. Clark A. W. Coyle J. T. DeLong M. R. (1981). Alzheimer disease: evidence for selective loss of cholinergic neurons in the nucleus basalis. Ann. Neurol. 10 122– 126 10.1002/ana.410100203 7283399 · DOI · Paper page
  157. Witton J. Brown J. T. Jones M. W. Randall A. D. (2010). Altered synaptic plasticity in the mossy fibre pathway of transgenic mice expressing mutant amyloid precursor protein. Mol. Brain 3 32 10.1186/1756-6606-3-32 PMC2988062 21040543 · DOI
  158. Wu G. He X. (2006). Threonine 41 in beta-catenin serves as a key phosphorylation relay residue in beta-catenin degradation. Biochemistry 45 5319– 5323 10.1021/bi0601149 16618120 · DOI
  159. Yates C. M. Simpson J. Gordon A. Maloney A. F. Allison Y. Ritchie I. M. (1983). Catecholamines and cholinergic enzymes in pre-senile and senile Alzheimer-type dementia and Down’s syndrome. Brain Res. 280 119– 126 10.1016/0006-8993(83)91179-4 6228286 · DOI
  160. Zhang H. Ma Q. Zhang Y. W. Xu H. (2012). Proteolytic processing of Alzheimer’s beta-amyloid precursor protein. J. Neurochem. 120(Suppl.1) 9– 21 10.1111/j.1471-4159.2011.07519.x 22122372 PMC3254787 · DOI
  161. Zhang W. Zhao Y. Tong C. Wang G. Wang B. Jia J. (2005). Hedgehog-regulated Costal2-kinase complexes control phosphorylation and proteolytic processing of Cubitus interruptus. Dev. Cell 8 267– 278 10.1016/j.devcel.2005.01.001 15691767 · DOI
  162. Zhao C. Teng E. M. Summers R. G. Ming G. L. Jr. Gage F. H. (2006). Distinct morphological stages of dentate granule neuron maturation in the adult mouse hippocampus. J. Neurosci. 26 3– 11 10.1523/JNEUROSCI.3648-05.2006 16399667 PMC6674324 · DOI · Paper page
  163. Zumbrunn J. Kinoshita K. Hyman A. A. Nathke I. S. (2001). Binding of the adenomatous polyposis coli protein to microtubules increases microtubule stability and is regulated by GSK3 beta phosphorylation. Curr. Biol. 11 44– 49 10.1016/S0960-9822(01)00002-1 11166179 · DOI

Cited by

Sorted by citations

Authors
Llorens-Marítin, M., Jurado, J., Hernández, F., & Ávila, J.
Affiliations
Consejo Superior de Investigaciones Científicas (ES)
Venue
Frontiers in Molecular Neuroscience
Publisher
Frontiers Media SA
Published
2014-05-21
Volume
7
Pages
46-46
ISSN
1662-5099 (ISSN-L)
DOI
10.3389/fnmol.2014.00046
PMC
PMC4033045
OpenAlex
W2144091853
Cited by
451
References
6
Citations by year
2026: 18 · 2025: 30 · 2024: 28 · 2023: 41 · 2022: 30 · 2021: 56 · 2020: 77 · 2019: 44 · 2018: 33 · 2017: 34 · 2016: 27 · 2015: 25 · 2014: 8
FWCI
3.64
Type
journal article
Language
en
Open access
Licence
cc-by
Locations
  • Frontiers in Molecular Neuroscience (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DIGITAL.CSIC (Spanish National Research Council (CSIC)) (submittedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Topics
  • Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
  • Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
Keywords
Alzheimer's disease, glycogen synthase kinase-3β, glycogen synthase kinase-3, amyloid plaques, neurofibrillary tangles, disease progression, age-related dementia

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review