{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,18]],"date-time":"2026-09-18T06:19:36Z","timestamp":1789712376153,"version":"4.0.1"},"reference-count":68,"publisher":"Elsevier BV","issue":"7","license":[{"start":{"date-parts":[[2013,7,1]],"date-time":"2013-07-01T00:00:00Z","timestamp":1372636800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2014,4,7]],"date-time":"2014-04-07T00:00:00Z","timestamp":1396828800000},"content-version":"vor","delay-in-days":280,"URL":"https:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100008398","name":"Internationale Stichting Alzheimer Onderzoek","doi-asserted-by":"crossref","id":[{"id":"10.13039\/501100008398","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100003246","name":"Netherlands Organisation for Scientific Research","doi-asserted-by":"crossref","id":[{"id":"10.13039\/501100003246","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Neurobiology of Aging"],"published-print":{"date-parts":[[2013,7]]},"DOI":"10.1016\/j.neurobiolaging.2013.01.008","type":"journal-article","created":{"date-parts":[[2013,2,14]],"date-time":"2013-02-14T20:45:34Z","timestamp":1360874734000},"page":"1759-1771","source":"Crossref","is-referenced-by-count":45,"title":["Unfolded protein response activates glycogen synthase kinase-3 via selective lysosomal degradation"],"prefix":"10.1016","volume":"34","author":[{"given":"Diana A.T.","family":"Nijholt","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anna","family":"N\u00f6lle","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elise S.","family":"van Haastert","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hessel","family":"Edelijn","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ruud F.","family":"Toonen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jeroen J.M.","family":"Hoozemans","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wiep","family":"Scheper","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib1","doi-asserted-by":"crossref","first-page":"6923","DOI":"10.1073\/pnas.121119298","article-title":"Hyperphosphorylation induces self-assembly of tau into tangles of paired helical filaments\/straight filaments","volume":"98","author":"Alonso","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U. S. A"},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib2","doi-asserted-by":"crossref","first-page":"30851","DOI":"10.1074\/jbc.M110.110957","article-title":"Phosphorylation of tau at Thr212, Thr231, and Ser262 combined causes neurodegeneration","volume":"285","author":"Alonso","year":"2010","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib3","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1016\/j.tcb.2012.02.006","article-title":"Bidirectional crosstalk between endoplasmic reticulum stress and mTOR signaling","volume":"22","author":"Appenzeller-Herzog","year":"2012","journal-title":"Trends Cell Biol."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib4","doi-asserted-by":"crossref","first-page":"663","DOI":"10.1038\/nrn2194","article-title":"Tau-mediated neurodegeneration in Alzheimer's disease and related disorders","volume":"8","author":"Ballatore","year":"2007","journal-title":"Nat. Rev. Neurosci."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib5","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1016\/0006-8993(89)91396-6","article-title":"Accumulation of abnormally phosphorylated tau precedes the formation of neurofibrillary tangles in Alzheimer's disease","volume":"477","author":"Bancher","year":"1989","journal-title":"Brain Res."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib6","doi-asserted-by":"crossref","first-page":"1143","DOI":"10.1016\/S0969-2126(01)00679-7","article-title":"The structure of phosphorylated GSK-3beta complexed with a peptide, FRATtide, that inhibits beta-catenin phosphorylation","volume":"9","author":"Bax","year":"2001","journal-title":"Structure"},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib7","doi-asserted-by":"crossref","first-page":"6926","DOI":"10.1523\/JNEUROSCI.0800-08.2008","article-title":"Autophagy induction and autophagosome clearance in neurons: relationship to autophagic pathology in Alzheimer's disease","volume":"28","author":"Boland","year":"2008","journal-title":"J.\u00a0Neurosci."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib8","doi-asserted-by":"crossref","first-page":"7972","DOI":"10.1073\/pnas.85.21.7972","article-title":"Bafilomycins: a class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells","volume":"85","author":"Bowman","year":"1988","journal-title":"Proc. Natl. Acad. Sci. U. S. A"},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib9","doi-asserted-by":"crossref","first-page":"3251","DOI":"10.1097\/00001756-199710200-00013","article-title":"Tau phosphorylation in transgenic mice expressing glycogen synthase kinase-3beta transgenes","volume":"8","author":"Brownlees","year":"1997","journal-title":"Neuroreport"},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib10","doi-asserted-by":"crossref","first-page":"2245","DOI":"10.1089\/ars.2007.1797","article-title":"Abeta 1-42 induces mild endoplasmic reticulum stress in an aggregation state-dependent manner","volume":"9","author":"Chafekar","year":"2007","journal-title":"Antioxid. Redox. Signal"},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib11","doi-asserted-by":"crossref","first-page":"469","DOI":"10.2174\/156720508785908883","article-title":"Increased Abeta1-42 production sensitizes neuroblastoma cells for ER stress toxicity","volume":"5","author":"Chafekar","year":"2008","journal-title":"Curr. Alzheimer Res."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib12","doi-asserted-by":"crossref","first-page":"8745","DOI":"10.1073\/pnas.96.15.8745","article-title":"Lithium activates the serine\/threonine kinase Akt-1 and suppresses glutamate-induced inhibition of Akt-1 activity in neurons","volume":"96","author":"Chalecka-Franaszek","year":"1999","journal-title":"Proc. Natl. Acad. Sci. U. S. A"},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib13","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1074\/jbc.M206236200","article-title":"Glycogen synthase kinase 3beta phosphorylates tau at both primed and unprimed sites. Differential impact on microtubule binding","volume":"278","author":"Cho","year":"2003","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib14","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1007\/s00401-010-0716-8","article-title":"Soluble hyper-phosphorylated tau causes microtubule breakdown and functionally compromises normal tau in\u00a0vivo","volume":"120","author":"Cowan","year":"2010","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib15","doi-asserted-by":"crossref","first-page":"3186","DOI":"10.1096\/fj.08-109181","article-title":"Phosphorylation of tau regulates its axonal transport by controlling its binding to kinesin","volume":"22","author":"Cuchillo-Ibanez","year":"2008","journal-title":"FASEB J."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib16","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1523\/JNEUROSCI.3931-08.2009","article-title":"Matrix-dependent local retention of secretory vesicle cargo in cortical neurons","volume":"29","author":"De Wit","year":"2009","journal-title":"J.\u00a0Neurosci."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib17","doi-asserted-by":"crossref","first-page":"8498","DOI":"10.1073\/pnas.92.18.8498","article-title":"Role of glycogen synthase kinase 3 beta as a negative regulator of dorsoventral axis formation in Xenopus embryos","volume":"92","author":"Dominguez","year":"1995","journal-title":"Proc. Natl. Acad. Sci. U. S. A"},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib18","doi-asserted-by":"crossref","first-page":"3902","DOI":"10.1021\/bi00066a008","article-title":"Inhibitory effect of modified bafilomycins and concanamycins on P- and V-type adenosinetriphosphatases","volume":"32","author":"Drose","year":"1993","journal-title":"Biochemistry"},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib19","doi-asserted-by":"crossref","first-page":"11960","DOI":"10.1073\/pnas.220413597","article-title":"Phosphorylation and inactivation of glycogen synthase kinase 3 by protein kinase A","volume":"97","author":"Fang","year":"2000","journal-title":"Proc. Natl. Acad. Sci. U. S. A"},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib20","doi-asserted-by":"crossref","first-page":"14042","DOI":"10.1016\/S0021-9258(18)47901-X","article-title":"Formation of protein kinase recognition sites by covalent modification of the substrate. Molecular mechanism for the synergistic action of casein kinase II and glycogen synthase kinase 3","volume":"262","author":"Fiol","year":"1987","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib21","doi-asserted-by":"crossref","first-page":"1930","DOI":"10.1007\/s00018-007-7045-7","article-title":"Glycogen synthase kinase 3: a key regulator of cellular fate","volume":"64","author":"Forde","year":"2007","journal-title":"Cell Mol. Life Sci."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib22","doi-asserted-by":"crossref","first-page":"1107","DOI":"10.3233\/JAD-2010-100687","article-title":"LiCl attenuates thapsigargin-induced tau hyperphosphorylation by inhibiting GSK-3beta in\u00a0vivo and in\u00a0vitro","volume":"21","author":"Fu","year":"2010","journal-title":"J.\u00a0Alzheimers. Dis."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib23","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1186\/1750-1326-4-13","article-title":"The role of tau in neurodegeneration","volume":"4","author":"Gendron","year":"2009","journal-title":"Mol. Neurodegen."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib24","doi-asserted-by":"crossref","first-page":"2743","DOI":"10.1038\/sj.emboj.7601725","article-title":"Neuronal apoptosis and reversible motor deficit in dominant-negative GSK-3 conditional transgenic mice","volume":"26","author":"Gomez-Sintes","year":"2007","journal-title":"EMBO J."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib25","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1016\/S0301-0082(01)00011-9","article-title":"The multifaceted roles of glycogen synthase kinase 3beta in cellular signaling","volume":"65","author":"Grimes","year":"2001","journal-title":"Prog. Neurobiol."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib26","doi-asserted-by":"crossref","first-page":"23330","DOI":"10.1074\/jbc.M201364200","article-title":"Expression and characterization of GSK-3 mutants and their effect on beta-catenin phosphorylation in intact cells","volume":"277","author":"Hagen","year":"2002","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib27","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1016\/j.molmed.2009.01.003","article-title":"Tau phosphorylation: the therapeutic challenge for neurodegenerative disease","volume":"15","author":"Hanger","year":"2009","journal-title":"Trends Mol. Med."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib28","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1016\/0304-3940(92)90774-2","article-title":"Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: generation of paired helical filament epitopes and neuronal localisation of the kinase","volume":"147","author":"Hanger","year":"1992","journal-title":"Neurosci. Lett."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib29","doi-asserted-by":"crossref","first-page":"352805","DOI":"10.4061\/2011\/352805","article-title":"Functional implications of glycogen synthase kinase-3-mediated tau phosphorylation","volume":"2011","author":"Hanger","year":"2011","journal-title":"Int. J. Alzheimers Dis."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib30","doi-asserted-by":"crossref","first-page":"485","DOI":"10.1006\/bbrc.2001.4986","article-title":"Glycogen synthase kinase 3beta is tyrosine phosphorylated by PYK2","volume":"284","author":"Hartigan","year":"2001","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib31","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1007\/s10565-006-0054-8","article-title":"The plecomacrolide vacuolar-ATPase inhibitor bafilomycin, alters insulin signaling in MIN6 beta-cells","volume":"22","author":"Hettiarachchi","year":"2006","journal-title":"Cell Biol. Toxicol."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib32","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1038\/ng.859","article-title":"Identification of common variants influencing risk of the tauopathy progressive supranuclear palsy","volume":"43","author":"Hoglinger","year":"2011","journal-title":"Nat. Genet."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib33","doi-asserted-by":"crossref","first-page":"1241","DOI":"10.2353\/ajpath.2009.080814","article-title":"The unfolded protein response is activated in pretangle neurons in Alzheimer's disease hippocampus","volume":"174","author":"Hoozemans","year":"2009","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib34","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1007\/s00401-005-1038-0","article-title":"The unfolded protein response is activated in Alzheimer's disease","volume":"110","author":"Hoozemans","year":"2005","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib35","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1186\/1750-1326-7-48","article-title":"Macroautophagy deficiency mediates age-dependent neurodegeneration through a phospho-tau pathway","volume":"7","author":"Inoue","year":"2012","journal-title":"Mol. Neurodegener."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib36","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1016\/0014-5793(93)81066-9","article-title":"Glycogen synthase kinase 3 beta is identical to tau protein kinase I generating several epitopes of paired helical filaments","volume":"325","author":"Ishiguro","year":"1993","journal-title":"FEBS Lett."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib37","doi-asserted-by":"crossref","first-page":"10897","DOI":"10.1016\/S0021-9258(19)50102-8","article-title":"Tau protein kinase I converts normal tau protein into A68-like component of paired helical filaments","volume":"267","author":"Ishiguro","year":"1992","journal-title":"J\u00a0Biol. Chem."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib38","doi-asserted-by":"crossref","first-page":"445","DOI":"10.4161\/auto.19496","article-title":"Guidelines for the use and interpretation of assays for monitoring autophagy","volume":"8","author":"Klionsky","year":"2012","journal-title":"Autophagy"},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib39","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1034\/j.1399-3011.1999.00083.x","article-title":"Expression analysis of glycogen synthase kinase-3 in human tissues","volume":"54","author":"Lau","year":"1999","journal-title":"J.\u00a0Pept. Res."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib40","doi-asserted-by":"crossref","first-page":"1146","DOI":"10.1016\/j.cell.2010.05.008","article-title":"Lysosomal proteolysis and autophagy require presenilin 1 and are disrupted by Alzheimer-related PS1 mutations","volume":"141","author":"Lee","year":"2010","journal-title":"Cell"},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib41","doi-asserted-by":"crossref","first-page":"7817","DOI":"10.1523\/JNEUROSCI.6412-10.2011","article-title":"Lysosomal proteolysis inhibition selectively disrupts axonal transport of degradative organelles and causes an Alzheimer's-like axonal dystrophy","volume":"31","author":"Lee","year":"2011","journal-title":"J.\u00a0Neurosci."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib42","doi-asserted-by":"crossref","first-page":"705","DOI":"10.3233\/JAD-2010-1276","article-title":"Lithium treatment arrests the development of neurofibrillary tangles in mutant tau transgenic mice with advanced neurofibrillary pathology","volume":"19","author":"Leroy","year":"2010","journal-title":"J.\u00a0Alzheimers Dis."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib43","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1007\/s004010100435","article-title":"The active form of glycogen synthase kinase-3beta is associated with granulovacuolar degeneration in neurons in Alzheimer's disease","volume":"103","author":"Leroy","year":"2002","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib44","doi-asserted-by":"crossref","first-page":"576","DOI":"10.1046\/j.1471-4159.1999.0720576.x","article-title":"Insulin transiently increases tau phosphorylation: involvement of glycogen synthase kinase-3beta and Fyn tyrosine kinase","volume":"72","author":"Lesort","year":"1999","journal-title":"J.\u00a0Neurochem."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib45","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1007\/s00702-005-0303-7","article-title":"Activation of glycogen synthase kinase-3 induces Alzheimer-like tau hyperphosphorylation in rat hippocampus slices in culture","volume":"113","author":"Li","year":"2006","journal-title":"J.\u00a0Neural Transm."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib46","doi-asserted-by":"crossref","first-page":"1145","DOI":"10.1016\/0306-4522(96)00126-1","article-title":"Phosphorylation of tau by glycogen synthase kinase-3 beta in intact mammalian cells: the effects on the organization and stability of microtubules","volume":"73","author":"Lovestone","year":"1996","journal-title":"Neuroscience"},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib47","doi-asserted-by":"crossref","first-page":"1077","DOI":"10.1016\/S0960-9822(00)00246-3","article-title":"Alzheimer's disease-like phosphorylation of the microtubule-associated protein tau by glycogen synthase kinase-3 in transfected mammalian cells","volume":"4","author":"Lovestone","year":"1994","journal-title":"Curr. Biol."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib48","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1093\/emboj\/20.1.27","article-title":"Decreased nuclear beta-catenin, tau hyperphosphorylation and neurodegeneration in GSK-3beta conditional transgenic mice","volume":"20","author":"Lucas","year":"2001","journal-title":"EMBO J."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib49","doi-asserted-by":"crossref","first-page":"479249","DOI":"10.4061\/2011\/479249","article-title":"Deconstructing GSK-3: the fine regulation of its activity","volume":"2011","author":"Medina","year":"2011","journal-title":"Int. J. Alzheimers Dis."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib50","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1002\/dmr.5610050105","article-title":"Mechanism and regulation of protein degradation in liver","volume":"5","author":"Mortimore","year":"1989","journal-title":"Diabetes Metab. Rev."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib51","doi-asserted-by":"crossref","first-page":"1071","DOI":"10.1038\/cdd.2010.176","article-title":"Endoplasmic reticulum stress activates autophagy but not the proteasome in neuronal cells: implications for Alzheimer's disease","volume":"18","author":"Nijholt","year":"2011","journal-title":"Cell Death Differ."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib52","doi-asserted-by":"crossref","first-page":"2459","DOI":"10.2174\/092986711795843236","article-title":"Removing protein aggregates: the role of proteolysis in neurodegeneration","volume":"18","author":"Nijholt","year":"2011","journal-title":"Curr. Med. Chem."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib53","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1002\/path.3969","article-title":"The unfolded protein response is associated with early tau pathology in the hippocampus of tauopathies","volume":"226","author":"Nijholt","year":"2011","journal-title":"J.\u00a0Pathol."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib54","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1093\/jnen\/64.2.113","article-title":"Extensive involvement of autophagy in Alzheimer disease: an immuno-electron microscopy study","volume":"64","author":"Nixon","year":"2005","journal-title":"J.\u00a0Neuropathol. Exp. Neurol."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib55","doi-asserted-by":"crossref","first-page":"6990","DOI":"10.1073\/pnas.0500466102","article-title":"Inhibition of glycogen synthase kinase-3 by lithium correlates with reduced tauopathy and degeneration in\u00a0vivo","volume":"102","author":"Noble","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U. S. A"},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib56","doi-asserted-by":"crossref","first-page":"368","DOI":"10.1016\/j.nbd.2008.05.011","article-title":"Pre-assembled tau filaments phosphorylated by GSK-3b form large tangle-like structures","volume":"31","author":"Rankin","year":"2008","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib57","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1006\/abio.1998.2832","article-title":"An assay for glycogen synthase kinase 3 (GSK-3) for use in crude cell extracts","volume":"264","author":"Ryves","year":"1998","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib58","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/j.mrfmmm.2004.06.056","article-title":"ER stress and the unfolded protein response","volume":"569","author":"Schroder","year":"2005","journal-title":"Mutat. Res."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib59","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1016\/j.nbd.2009.05.025","article-title":"A\u00a0novel GSK-3beta inhibitor reduces Alzheimer's pathology and rescues neuronal loss in\u00a0vivo","volume":"35","author":"Sereno","year":"2009","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib60","doi-asserted-by":"crossref","first-page":"44701","DOI":"10.1074\/jbc.M206047200","article-title":"Central role of glycogen synthase kinase-3beta in endoplasmic reticulum stress-induced caspase-3 activation","volume":"277","author":"Song","year":"2002","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib61","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1002\/1097-4652(2001)9999:9999<00::AID-JCP1050>3.0.CO;2-I","article-title":"Starvation-induced lysosomal degradation of aldolase B requires glutamine 111 in a signal sequence for chaperone-mediated transport","volume":"187","author":"Susan","year":"2001","journal-title":"J.\u00a0Cell Physiol."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib62","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1016\/S0168-0102(98)00061-3","article-title":"Activation of tau protein kinase I\/glycogen synthase kinase-3beta by amyloid beta peptide (25-35) enhances phosphorylation of tau in hippocampal neurons","volume":"31","author":"Takashima","year":"1998","journal-title":"Neurosci. Res."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib63","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1007\/s00109-008-0423-2","article-title":"Lysosomal cysteine peptidase cathepsin L protects against cardiac hypertrophy through blocking AKT\/GSK3beta signaling","volume":"87","author":"Tang","year":"2009","journal-title":"J.\u00a0Mol. Med. (Berl)"},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib64","doi-asserted-by":"crossref","first-page":"348","DOI":"10.1097\/01.jnen.0000218445.30535.6f","article-title":"Endoplasmic reticulum stress features are prominent in Alzheimer disease but not in prion diseases in\u00a0vivo","volume":"65","author":"Unterberger","year":"2006","journal-title":"J.\u00a0Neuropathol. Exp. Neurol."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib65","doi-asserted-by":"crossref","first-page":"1537","DOI":"10.1242\/jcs.109.6.1537","article-title":"Cellular phosphorylation of tau by GSK-3 beta influences tau binding to microtubules and microtubule organisation","volume":"109","author":"Wagner","year":"1996","journal-title":"J.\u00a0Cell Sci."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib66","doi-asserted-by":"crossref","first-page":"2431","DOI":"10.1002\/j.1460-2075.1990.tb07419.x","article-title":"Molecular cloning and expression of glycogen synthase kinase-3\/factor A","volume":"9","author":"Woodgett","year":"1990","journal-title":"EMBO J."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib67","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1016\/S0891-0618(02)00014-5","article-title":"Expression of glycogen synthase kinase-3 isoforms in mouse tissues and their transcription in the brain","volume":"23","author":"Yao","year":"2002","journal-title":"J.\u00a0Chem. Neuroanat."},{"key":"10.1016\/j.neurobiolaging.2013.01.008_bib68","doi-asserted-by":"crossref","first-page":"30299","DOI":"10.1074\/jbc.M607007200","article-title":"Endoplasmic reticulum stress triggers autophagy","volume":"281","author":"Yorimitsu","year":"2006","journal-title":"J.\u00a0Biol. Chem."}],"container-title":["Neurobiology of Aging"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0197458013000262?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0197458013000262?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,4,29]],"date-time":"2025-04-29T17:21:48Z","timestamp":1745947308000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0197458013000262"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2013,7]]},"references-count":68,"journal-issue":{"issue":"7","published-print":{"date-parts":[[2013,7]]}},"alternative-id":["S0197458013000262"],"URL":"https:\/\/doi.org\/10.1016\/j.neurobiolaging.2013.01.008","relation":{},"ISSN":["0197-4580"],"issn-type":[{"value":"0197-4580","type":"print"}],"subject":[],"published":{"date-parts":[[2013,7]]}}}