{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T18:05:51Z","timestamp":1791223551719,"version":"4.1.0"},"reference-count":153,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2019,3,1]],"date-time":"2019-03-01T00:00:00Z","timestamp":1551398400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2019,3,1]],"date-time":"2019-03-01T00:00:00Z","timestamp":1551398400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2020,1,23]],"date-time":"2020-01-23T00:00:00Z","timestamp":1579737600000},"content-version":"am","delay-in-days":328,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["RO1NS094516"],"award-info":[{"award-number":["RO1NS094516"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["RO1EY025622"],"award-info":[{"award-number":["RO1EY025622"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"name":"University of Pittsburgh and Copeland Foundation to N.S"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Mechanisms of Ageing and Development"],"published-print":{"date-parts":[[2019,3]]},"DOI":"10.1016\/j.mad.2019.01.007","type":"journal-article","created":{"date-parts":[[2019,1,19]],"date-time":"2019-01-19T12:08:14Z","timestamp":1547899694000},"page":"72-79","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":126,"special_numbering":"C","title":["Tauopathy: A common mechanism for neurodegeneration and brain aging"],"prefix":"10.1016","volume":"178","author":[{"given":"Pampa","family":"Saha","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nilkantha","family":"Sen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"3","key":"10.1016\/j.mad.2019.01.007_bib0005","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1038\/nrn1868","article-title":"Expanding insights of mitochondrial dysfunction in Parkinson\u2019s disease","volume":"7","author":"Abou-Sleiman","year":"2006","journal-title":"Nat. Rev. Neurosci."},{"issue":"12","key":"10.1016\/j.mad.2019.01.007_bib0010","doi-asserted-by":"crossref","first-page":"5562","DOI":"10.1073\/pnas.91.12.5562","article-title":"Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease","volume":"91","author":"Alonso","year":"1994","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"7","key":"10.1016\/j.mad.2019.01.007_bib0015","doi-asserted-by":"crossref","first-page":"783","DOI":"10.1038\/nm0796-783","article-title":"Alzheimer\u2019s disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules","volume":"2","author":"Alonso","year":"1996","journal-title":"Nat. Med."},{"issue":"1","key":"10.1016\/j.mad.2019.01.007_bib0020","doi-asserted-by":"crossref","first-page":"298","DOI":"10.1073\/pnas.94.1.298","article-title":"Abnormal phosphorylation of tau and the mechanism of Alzheimer neurofibrillary degeneration: sequestration of microtubule-associated proteins 1 and 2 and the disassembly of microtubules by the abnormal tau","volume":"94","author":"Alonso","year":"1997","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"41","key":"10.1016\/j.mad.2019.01.007_bib0025","doi-asserted-by":"crossref","first-page":"37967","DOI":"10.1074\/jbc.M105365200","article-title":"Interaction of tau isoforms with Alzheimer\u2019s disease abnormally hyperphosphorylated tau and in vitro phosphorylation into the disease-like protein","volume":"276","author":"Alonso","year":"2001","journal-title":"J. Biol. Chem."},{"issue":"2","key":"10.1016\/j.mad.2019.01.007_bib0030","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1111\/j.1471-4159.1993.tb03173.x","article-title":"Tau protein kinase II is involved in the regulation of the normal phosphorylation state of tau protein","volume":"60","author":"Arioka","year":"1993","journal-title":"J. Neurochem."},{"issue":"46","key":"10.1016\/j.mad.2019.01.007_bib0035","doi-asserted-by":"crossref","first-page":"28741","DOI":"10.1074\/jbc.271.46.28741","article-title":"The microtubule-associated protein tau is extensively modified with O-linked N-acetylglucosamine","volume":"271","author":"Arnold","year":"1996","journal-title":"J. Biol. Chem."},{"issue":"3 Pt 1","key":"10.1016\/j.mad.2019.01.007_bib0040","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1212\/WNL.42.3.631","article-title":"Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer\u2019s disease","volume":"42","author":"Arriagada","year":"1992","journal-title":"Neurology"},{"issue":"9","key":"10.1016\/j.mad.2019.01.007_bib0045","doi-asserted-by":"crossref","first-page":"663","DOI":"10.1038\/nrn2194","article-title":"Tau-mediated neurodegeneration in Alzheimer\u2019s disease and related disorders","volume":"8","author":"Ballatore","year":"2007","journal-title":"Nat. Rev. Neurosci."},{"issue":"6","key":"10.1016\/j.mad.2019.01.007_bib0050","doi-asserted-by":"crossref","first-page":"565","DOI":"10.1007\/BF00296494","article-title":"Neurofibrillary tangle predominant form of senile dementia of Alzheimer type: a rare subtype in very old subjects","volume":"88","author":"Bancher","year":"1994","journal-title":"Acta Neuropathol."},{"issue":"12","key":"10.1016\/j.mad.2019.01.007_bib0055","doi-asserted-by":"crossref","first-page":"5876","DOI":"10.1016\/S0021-9258(18)60647-7","article-title":"Interactions between the microtubule-associated tau proteins and S100b regulate tau phosphorylation by the Ca2+\/calmodulin-dependent protein kinase II","volume":"263","author":"Baudier","year":"1988","journal-title":"J. Biol. Chem."},{"issue":"4","key":"10.1016\/j.mad.2019.01.007_bib0060","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1177\/0891988710383571","article-title":"Genetics of Alzheimer disease","volume":"23","author":"Bekris","year":"2010","journal-title":"J. Geriatr. Psychiatry Neurol."},{"issue":"1","key":"10.1016\/j.mad.2019.01.007_bib0065","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1016\/S0014-5793(00)02203-1","article-title":"Role of protein phosphatase-2A and -1 in the regulation of GSK-3, cdk5 and cdc2 and the phosphorylation of tau in rat forebrain","volume":"485","author":"Bennecib","year":"2000","journal-title":"FEBS Lett."},{"issue":"1","key":"10.1016\/j.mad.2019.01.007_bib0070","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1001\/archneur.1995.00540250089017","article-title":"Neocortical neurofibrillary tangles correlate with dementia severity in Alzheimer\u2019s disease","volume":"52","author":"Bierer","year":"1995","journal-title":"Arch. Neurol."},{"issue":"7288","key":"10.1016\/j.mad.2019.01.007_bib0075","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1038\/nature08983","article-title":"Neural mechanisms of ageing and cognitive decline","volume":"464","author":"Bishop","year":"2010","journal-title":"Nature"},{"issue":"5","key":"10.1016\/j.mad.2019.01.007_bib0080","doi-asserted-by":"crossref","first-page":"437","DOI":"10.2174\/156720506779025242","article-title":"Pathways by which Abeta facilitates tau pathology","volume":"3","author":"Blurton-Jones","year":"2006","journal-title":"Curr. Alzheimer Res."},{"issue":"3","key":"10.1016\/j.mad.2019.01.007_bib0085","doi-asserted-by":"crossref","first-page":"e1759","DOI":"10.1371\/journal.pone.0001759","article-title":"SirT1 regulates energy metabolism and response to caloric restriction in mice","volume":"3","author":"Boily","year":"2008","journal-title":"PLoS One"},{"issue":"17","key":"10.1016\/j.mad.2019.01.007_bib0090","doi-asserted-by":"crossref","first-page":"17187","DOI":"10.1074\/jbc.M501250200","article-title":"Mechanism of human SIRT1 activation by resveratrol","volume":"280","author":"Borra","year":"2005","journal-title":"J. Biol. Chem."},{"issue":"2","key":"10.1016\/j.mad.2019.01.007_bib0095","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1016\/0304-3940(93)90305-5","article-title":"Neurofibrillary tangle densities in the hippocampal formation in a non-demented population define subgroups of patients with differential early pathologic changes","volume":"153","author":"Bouras","year":"1993","journal-title":"Neurosci. Lett."},{"issue":"6","key":"10.1016\/j.mad.2019.01.007_bib0100","doi-asserted-by":"crossref","first-page":"1089","DOI":"10.1016\/0896-6273(93)90057-X","article-title":"Abnormal tau phosphorylation at Ser396 in Alzheimer\u2019s disease recapitulates development and contributes to reduced microtubule binding","volume":"10","author":"Bramblett","year":"1993","journal-title":"Neuron"},{"issue":"1","key":"10.1016\/j.mad.2019.01.007_bib0105","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1016\/S0165-0173(00)00019-9","article-title":"Tau protein isoforms, phosphorylation and role in neurodegenerative disorders","volume":"33","author":"Buee","year":"2000","journal-title":"Brain Res. Brain Res. Rev."},{"issue":"4","key":"10.1016\/j.mad.2019.01.007_bib0110","doi-asserted-by":"crossref","first-page":"879","DOI":"10.1016\/0896-6273(95)90232-5","article-title":"Beta-amyloid fibrils induce tau phosphorylation and loss of microtubule binding","volume":"14","author":"Busciglio","year":"1995","journal-title":"Neuron"},{"issue":"1-2","key":"10.1016\/j.mad.2019.01.007_bib0115","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1016\/S0006-8993(02)02244-8","article-title":"Expression and activity of antioxidants in the brain in progressive supranuclear palsy","volume":"930","author":"Cantuti-Castelvetri","year":"2002","journal-title":"Brain Res."},{"issue":"1-2","key":"10.1016\/j.mad.2019.01.007_bib0120","doi-asserted-by":"crossref","first-page":"268","DOI":"10.1016\/0006-8993(95)00535-X","article-title":"Evidence for oxidative stress in Pick disease and corticobasal degeneration","volume":"696","author":"Castellani","year":"1995","journal-title":"Brain Res."},{"issue":"12","key":"10.1016\/j.mad.2019.01.007_bib0125","doi-asserted-by":"crossref","first-page":"4857","DOI":"10.1523\/JNEUROSCI.4989-14.2015","article-title":"Tau immunotherapy modulates both pathological tau and upstream amyloid pathology in an Alzheimer\u2019s disease mouse model","volume":"35","author":"Castillo-Carranza","year":"2015","journal-title":"J. Neurosci."},{"issue":"48","key":"10.1016\/j.mad.2019.01.007_bib0130","doi-asserted-by":"crossref","first-page":"17345","DOI":"10.1523\/JNEUROSCI.0172-12.2012","article-title":"Soluble abeta promotes wild-type tau pathology in vivo","volume":"32","author":"Chabrier","year":"2012","journal-title":"J. Neurosci."},{"key":"10.1016\/j.mad.2019.01.007_bib0135","doi-asserted-by":"crossref","first-page":"122","DOI":"10.3389\/fneur.2013.00122","article-title":"Tau clearance mechanisms and their possible role in the pathogenesis of Alzheimer disease","volume":"4","author":"Chesser","year":"2013","journal-title":"Front. Neurol."},{"key":"10.1016\/j.mad.2019.01.007_bib0140","doi-asserted-by":"crossref","first-page":"e444","DOI":"10.1038\/cddis.2012.184","article-title":"Chemotherapeutic induction of mitochondrial oxidative stress activates GSK-3alpha\/beta and Bax, leading to permeability transition pore opening and tumor cell death","volume":"3","author":"Chiara","year":"2012","journal-title":"Cell Death Dis."},{"key":"10.1016\/j.mad.2019.01.007_bib0145","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1038\/ncomms1255","article-title":"The acetylation of tau inhibits its function and promotes pathological tau aggregation","volume":"2","author":"Cohen","year":"2011","journal-title":"Nat. Commun."},{"issue":"6","key":"10.1016\/j.mad.2019.01.007_bib0150","doi-asserted-by":"crossref","first-page":"756","DOI":"10.1038\/nsmb.2555","article-title":"The microtubule-associated tau protein has intrinsic acetyltransferase activity","volume":"20","author":"Cohen","year":"2013","journal-title":"Nat. Struct. Mol. Biol."},{"issue":"3","key":"10.1016\/j.mad.2019.01.007_bib0155","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1186\/alzrt259","article-title":"Acetylation: a new key to unlock tau\u2019s role in neurodegeneration","volume":"6","author":"Cook","year":"2014","journal-title":"Alzheimers Res. Ther."},{"issue":"6","key":"10.1016\/j.mad.2019.01.007_bib0160","doi-asserted-by":"crossref","first-page":"755","DOI":"10.1007\/s00401-014-1349-0","article-title":"Primary age-related tauopathy (PART): a common pathology associated with human aging","volume":"128","author":"Crary","year":"2014","journal-title":"Acta Neuropathol."},{"issue":"16","key":"10.1016\/j.mad.2019.01.007_bib0165","doi-asserted-by":"crossref","first-page":"10825","DOI":"10.1074\/jbc.M512786200","article-title":"Alzheimer disease-specific conformation of hyperphosphorylated paired helical filament-Tau is polyubiquitinated through Lys-48, Lys-11, and Lys-6 ubiquitin conjugation","volume":"281","author":"Cripps","year":"2006","journal-title":"J. Biol. Chem."},{"issue":"11","key":"10.1016\/j.mad.2019.01.007_bib0170","doi-asserted-by":"crossref","first-page":"1954","DOI":"10.1016\/j.bbamcr.2011.03.001","article-title":"Regulation of FoxO transcription factors by acetylation and protein-protein interactions","volume":"1813","author":"Daitoku","year":"2011","journal-title":"Biochim. Biophys. Acta"},{"issue":"9","key":"10.1016\/j.mad.2019.01.007_bib0175","doi-asserted-by":"crossref","first-page":"664","DOI":"10.1038\/nchembio.194","article-title":"Redox-sensitive cysteines bridge p300\/CBP-mediated acetylation and FoxO4 activity","volume":"5","author":"Dansen","year":"2009","journal-title":"Nat. Chem. Biol."},{"issue":"2","key":"10.1016\/j.mad.2019.01.007_bib0180","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1097\/00005072-199602000-00004","article-title":"Specific pathological Tau protein variants characterize Pick\u2019s disease","volume":"55","author":"Delacourte","year":"1996","journal-title":"J. Neuropathol. Exp. Neurol."},{"issue":"1","key":"10.1016\/j.mad.2019.01.007_bib0185","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1172\/JCI28769","article-title":"Oxidative stress mediates tau-induced neurodegeneration in Drosophila","volume":"117","author":"Dias-Santagata","year":"2007","journal-title":"J. Clin. Invest."},{"issue":"3","key":"10.1016\/j.mad.2019.01.007_bib0190","doi-asserted-by":"crossref","first-page":"648","DOI":"10.1172\/JCI29715","article-title":"The high-affinity HSP90-CHIP complex recognizes and selectively degrades phosphorylated tau client proteins","volume":"117","author":"Dickey","year":"2007","journal-title":"J. Clin. Invest."},{"issue":"15","key":"10.1016\/j.mad.2019.01.007_bib0195","doi-asserted-by":"crossref","first-page":"9919","DOI":"10.1074\/jbc.M510127200","article-title":"Small ubiquitin-like modifier (SUMO) modification of natively unfolded proteins tau and alpha-synuclein","volume":"281","author":"Dorval","year":"2006","journal-title":"J. Biol. Chem."},{"issue":"2","key":"10.1016\/j.mad.2019.01.007_bib0200","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1016\/S0092-8674(00)80208-1","article-title":"MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption","volume":"89","author":"Drewes","year":"1997","journal-title":"Cell"},{"issue":"6","key":"10.1016\/j.mad.2019.01.007_bib0205","doi-asserted-by":"crossref","first-page":"847","DOI":"10.1016\/j.neurobiolaging.2008.06.009","article-title":"Long-term proteasome dysfunction in the mouse brain by expression of aberrant ubiquitin","volume":"30","author":"Fischer","year":"2009","journal-title":"Neurobiol. Aging"},{"issue":"6","key":"10.1016\/j.mad.2019.01.007_bib0210","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1007\/BF00296367","article-title":"Abnormal Tau proteins in progressive supranuclear palsy. Similarities and differences with the neurofibrillary degeneration of the Alzheimer type","volume":"81","author":"Flament","year":"1991","journal-title":"Acta Neuropathol."},{"issue":"6","key":"10.1016\/j.mad.2019.01.007_bib0215","doi-asserted-by":"crossref","first-page":"706","DOI":"10.1002\/ana.410410606","article-title":"Frontotemporal dementia and parkinsonism linked to chromosome 17: a consensus conference. Conference Participants","volume":"41","author":"Foster","year":"1997","journal-title":"Ann. Neurol."},{"issue":"17","key":"10.1016\/j.mad.2019.01.007_bib0220","doi-asserted-by":"crossref","first-page":"10032","DOI":"10.1073\/pnas.1630428100","article-title":"Caspase cleavage of tau: linking amyloid and neurofibrillary tangles in Alzheimer\u2019s disease","volume":"100","author":"Gamblin","year":"2003","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"8","key":"10.1016\/j.mad.2019.01.007_bib0225","doi-asserted-by":"crossref","first-page":"408","DOI":"10.1016\/j.tcb.2004.07.006","article-title":"The interaction between FOXO and SIRT1: tipping the balance towards survival","volume":"14","author":"Giannakou","year":"2004","journal-title":"Trends Cell Biol."},{"issue":"5800","key":"10.1016\/j.mad.2019.01.007_bib0230","doi-asserted-by":"crossref","first-page":"777","DOI":"10.1126\/science.1132814","article-title":"A century of Alzheimer\u2019s disease","volume":"314","author":"Goedert","year":"2006","journal-title":"Science"},{"issue":"1","key":"10.1016\/j.mad.2019.01.007_bib0235","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1016\/0896-6273(92)90117-V","article-title":"Tau proteins of Alzheimer paired helical filaments: abnormal phosphorylation of all six brain isoforms","volume":"8","author":"Goedert","year":"1992","journal-title":"Neuron"},{"issue":"8","key":"10.1016\/j.mad.2019.01.007_bib0240","doi-asserted-by":"crossref","first-page":"5535","DOI":"10.1074\/jbc.275.8.5535","article-title":"Phosphorylation of microtubule-associated protein tau is regulated by protein phosphatase 2A in mammalian brain. Implications for neurofibrillary degeneration in Alzheimer\u2019s disease","volume":"275","author":"Gong","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mad.2019.01.007_bib0245","doi-asserted-by":"crossref","first-page":"22685","DOI":"10.1038\/srep22685","article-title":"Acetylation mimic of lysine 280 exacerbates human Tau neurotoxicity in vivo","volume":"6","author":"Gorsky","year":"2016","journal-title":"Sci. Rep."},{"issue":"1","key":"10.1016\/j.mad.2019.01.007_bib0250","doi-asserted-by":"crossref","first-page":"9984","DOI":"10.1038\/s41598-017-10225-0","article-title":"Pseudo-acetylation of multiple sites on human Tau proteins alters Tau phosphorylation and microtubule binding, and ameliorates amyloid beta toxicity","volume":"7","author":"Gorsky","year":"2017","journal-title":"Sci. Rep."},{"issue":"5534","key":"10.1016\/j.mad.2019.01.007_bib0255","doi-asserted-by":"crossref","first-page":"1491","DOI":"10.1126\/science.1062097","article-title":"Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Abeta 42 fibrils","volume":"293","author":"Gotz","year":"2001","journal-title":"Science"},{"key":"10.1016\/j.mad.2019.01.007_bib0260","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1146\/annurev-med-042915-103753","article-title":"Update on Alzheimer\u2019s disease therapy and prevention strategies","volume":"68","author":"Graham","year":"2017","journal-title":"Annu. Rev. Med."},{"issue":"45","key":"10.1016\/j.mad.2019.01.007_bib0265","doi-asserted-by":"crossref","first-page":"11500","DOI":"10.1523\/JNEUROSCI.3203-08.2008","article-title":"Nicotinamide restores cognition in Alzheimer\u2019s disease transgenic mice via a mechanism involving sirtuin inhibition and selective reduction of Thr231-phosphotau","volume":"28","author":"Green","year":"2008","journal-title":"J. Neurosci."},{"issue":"2-3","key":"10.1016\/j.mad.2019.01.007_bib0270","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1007\/s12035-010-8113-9","article-title":"Redox reactions induced by nitrosative stress mediate protein misfolding and mitochondrial dysfunction in neurodegenerative diseases","volume":"41","author":"Gu","year":"2010","journal-title":"Mol. Neurobiol."},{"issue":"8","key":"10.1016\/j.mad.2019.01.007_bib0275","doi-asserted-by":"crossref","first-page":"1104","DOI":"10.1038\/aps.2016.128","article-title":"LX2343 alleviates cognitive impairments in AD model rats by inhibiting oxidative stress-induced neuronal apoptosis and tauopathy","volume":"38","author":"Guo","year":"2017","journal-title":"Acta Pharmacol. Sin."},{"issue":"6","key":"10.1016\/j.mad.2019.01.007_bib0280","doi-asserted-by":"crossref","first-page":"2465","DOI":"10.1046\/j.1471-4159.1998.71062465.x","article-title":"New phosphorylation sites identified in hyperphosphorylated tau (paired helical filament-tau) from Alzheimer\u2019s disease brain using nanoelectrospray mass spectrometry","volume":"71","author":"Hanger","year":"1998","journal-title":"J. Neurochem."},{"issue":"7253","key":"10.1016\/j.mad.2019.01.007_bib0285","doi-asserted-by":"crossref","first-page":"392","DOI":"10.1038\/nature08221","article-title":"Rapamycin fed late in life extends lifespan in genetically heterogeneous mice","volume":"460","author":"Harrison","year":"2009","journal-title":"Nature"},{"issue":"24","key":"10.1016\/j.mad.2019.01.007_bib0290","doi-asserted-by":"crossref","first-page":"17047","DOI":"10.1016\/S0021-9258(18)41890-X","article-title":"Protein sequence and mass spectrometric analyses of tau in the Alzheimer\u2019s disease brain","volume":"267","author":"Hasegawa","year":"1992","journal-title":"J. Biol. Chem."},{"issue":"3","key":"10.1016\/j.mad.2019.01.007_bib0295","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1016\/S0014-5793(98)01217-4","article-title":"Tau proteins with FTDP-17 mutations have a reduced ability to promote microtubule assembly","volume":"437","author":"Hasegawa","year":"1998","journal-title":"FEBS Lett."},{"issue":"2","key":"10.1016\/j.mad.2019.01.007_bib0300","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1016\/j.neuron.2016.04.008","article-title":"Bad Ac-etylated Tau","volume":"90","author":"Hettinger","year":"2016","journal-title":"Neuron"},{"issue":"5395","key":"10.1016\/j.mad.2019.01.007_bib0305","doi-asserted-by":"crossref","first-page":"1914","DOI":"10.1126\/science.282.5395.1914","article-title":"Mutation-specific functional impairments in distinct tau isoforms of hereditary FTDP-17","volume":"282","author":"Hong","year":"1998","journal-title":"Science"},{"issue":"3","key":"10.1016\/j.mad.2019.01.007_bib0310","doi-asserted-by":"crossref","first-page":"1021","DOI":"10.1016\/S0002-9440(10)63462-1","article-title":"Nitration of tau protein is linked to neurodegeneration in tauopathies","volume":"163","author":"Horiguchi","year":"2003","journal-title":"Am. J. Pathol."},{"issue":"1","key":"10.1016\/j.mad.2019.01.007_bib0315","doi-asserted-by":"crossref","first-page":"265","DOI":"10.3233\/JAD-170490","article-title":"Cognitive Decline in Preclinical Alzheimer\u2019s Disease: Amyloid-Beta versus Tauopathy","volume":"61","author":"Huber","year":"2018","journal-title":"J. Alzheimers Dis."},{"issue":"6686","key":"10.1016\/j.mad.2019.01.007_bib0320","doi-asserted-by":"crossref","first-page":"702","DOI":"10.1038\/31508","article-title":"Association of missense and 5\u2019-splice-site mutations in tau with the inherited dementia FTDP-17","volume":"393","author":"Hutton","year":"1998","journal-title":"Nature"},{"issue":"7632","key":"10.1016\/j.mad.2019.01.007_bib0325","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1038\/nature20587","article-title":"Gamma frequency entrainment attenuates amyloid load and modifies microglia","volume":"540","author":"Iaccarino","year":"2016","journal-title":"Nature"},{"issue":"5","key":"10.1016\/j.mad.2019.01.007_bib0330","first-page":"455","article-title":"[A case of atypical senile dementia of Alzheimer type]","volume":"45","author":"Ikeda","year":"1993","journal-title":"No To Shinkei"},{"issue":"1","key":"10.1016\/j.mad.2019.01.007_bib0335","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1016\/0014-5793(94)00650-4","article-title":"Alzheimer paired helical filaments. Restoration of the biological activity by dephosphorylation","volume":"349","author":"Iqbal","year":"1994","journal-title":"FEBS Lett."},{"issue":"Pt 3","key":"10.1016\/j.mad.2019.01.007_bib0340","doi-asserted-by":"crossref","first-page":"807","DOI":"10.1093\/brain\/aws013","article-title":"Acetylated tau, a novel pathological signature in Alzheimer\u2019s disease and other tauopathies","volume":"135","author":"Irwin","year":"2012","journal-title":"Brain"},{"issue":"2","key":"10.1016\/j.mad.2019.01.007_bib0345","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1159\/000117216","article-title":"Dementia characterized by abundant neurofibrillary tangles and scarce senile plaques: a quantitative pathological study","volume":"36","author":"Itoh","year":"1996","journal-title":"Eur. Neurol."},{"issue":"3","key":"10.1016\/j.mad.2019.01.007_bib0350","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1016\/j.cell.2010.06.036","article-title":"Dendritic function of tau mediates amyloid-beta toxicity in Alzheimer\u2019s disease mouse models","volume":"142","author":"Ittner","year":"2010","journal-title":"Cell"},{"issue":"1","key":"10.1016\/j.mad.2019.01.007_bib0355","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1515\/tnsci-2015-0023","article-title":"Tau-mediated synaptic damage in Alzheimer\u2019s disease","volume":"6","author":"Jadhav","year":"2015","journal-title":"Transl. Neurosci."},{"issue":"1","key":"10.1016\/j.mad.2019.01.007_bib0360","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1007\/s10549-012-2069-6","article-title":"Auto-acetylation stabilizes p300 in cardiac myocytes during acute oxidative stress, promoting STAT3 accumulation and cell survival","volume":"135","author":"Jain","year":"2012","journal-title":"Breast Cancer Res. Treat."},{"issue":"2","key":"10.1016\/j.mad.2019.01.007_bib0365","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1007\/s00401-006-0156-7","article-title":"Neurofibrillary tangle-predominant dementia: comparison with classical Alzheimer disease","volume":"113","author":"Jellinger","year":"2007","journal-title":"Acta Neuropathol."},{"issue":"44","key":"10.1016\/j.mad.2019.01.007_bib0370","doi-asserted-by":"crossref","first-page":"9626","DOI":"10.1021\/acs.jafc.7b03252","article-title":"Resveratrol Ameliorates Tau Hyperphosphorylation at Ser396 Site and Oxidative Damage in Rat Hippocampal Slices Exposed to Vanadate: Implication of ERK1\/2 and GSK-3beta Signaling Cascades","volume":"65","author":"Jhang","year":"2017","journal-title":"J. Agric. Food Chem."},{"issue":"8","key":"10.1016\/j.mad.2019.01.007_bib0375","doi-asserted-by":"crossref","first-page":"1290","DOI":"10.1016\/j.biocel.2012.05.001","article-title":"Human fetal tau protein isoform: possibilities for Alzheimer\u2019s disease treatment","volume":"44","author":"Jovanov-Milosevic","year":"2012","journal-title":"Int. J. Biochem. Cell Biol."},{"issue":"18","key":"10.1016\/j.mad.2019.01.007_bib0380","doi-asserted-by":"crossref","first-page":"3020","DOI":"10.1021\/bi500006v","article-title":"Nuclear magnetic resonance analysis of the acetylation pattern of the neuronal Tau protein","volume":"53","author":"Kamah","year":"2014","journal-title":"Biochemistry"},{"issue":"32","key":"10.1016\/j.mad.2019.01.007_bib0385","doi-asserted-by":"crossref","first-page":"24374","DOI":"10.1016\/S0021-9258(20)80536-5","article-title":"Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease","volume":"268","author":"Kopke","year":"1993","journal-title":"J. Biol. Chem."},{"issue":"2-3","key":"10.1016\/j.mad.2019.01.007_bib0390","doi-asserted-by":"crossref","first-page":"298","DOI":"10.1016\/j.bbadis.2004.10.011","article-title":"Phosphorylated tau and the neurodegenerative foldopathies","volume":"1739","author":"Kosik","year":"2005","journal-title":"Biochim. Biophys. Acta"},{"issue":"6","key":"10.1016\/j.mad.2019.01.007_bib0395","first-page":"1496","article-title":"Ultrastructure and biochemical composition of paired helical filaments in corticobasal degeneration","volume":"145","author":"Ksiezak-Reding","year":"1994","journal-title":"Am. J. Pathol."},{"issue":"2","key":"10.1016\/j.mad.2019.01.007_bib0400","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1016\/0014-5793(92)81278-T","article-title":"Implication of brain cdc2 and MAP2 kinases in the phosphorylation of tau protein in Alzheimer\u2019s disease","volume":"308","author":"Ledesma","year":"1992","journal-title":"FEBS Lett."},{"issue":"34","key":"10.1016\/j.mad.2019.01.007_bib0405","doi-asserted-by":"crossref","first-page":"21614","DOI":"10.1016\/S0021-9258(17)31849-5","article-title":"Analysis of microtubule-associated protein tau glycation in paired helical filaments","volume":"269","author":"Ledesma","year":"1994","journal-title":"J. Biol. Chem."},{"issue":"4","key":"10.1016\/j.mad.2019.01.007_bib0410","doi-asserted-by":"crossref","first-page":"1658","DOI":"10.1046\/j.1471-4159.1995.65041658.x","article-title":"Tau protein from Alzheimer\u2019s disease patients is glycated at its tubulin-binding domain","volume":"65","author":"Ledesma","year":"1995","journal-title":"J. Neurochem."},{"issue":"4994","key":"10.1016\/j.mad.2019.01.007_bib0415","doi-asserted-by":"crossref","first-page":"675","DOI":"10.1126\/science.1899488","article-title":"A68: a major subunit of paired helical filaments and derivatized forms of normal Tau","volume":"251","author":"Lee","year":"1991","journal-title":"Science"},{"issue":"Pt 21","key":"10.1016\/j.mad.2019.01.007_bib0420","doi-asserted-by":"crossref","first-page":"3167","DOI":"10.1242\/jcs.111.21.3167","article-title":"Tau interacts with src-family non-receptor tyrosine kinases","volume":"111","author":"Lee","year":"1998","journal-title":"J. Cell. Sci."},{"issue":"9","key":"10.1016\/j.mad.2019.01.007_bib0425","doi-asserted-by":"crossref","first-page":"2304","DOI":"10.1523\/JNEUROSCI.4162-03.2004","article-title":"Phosphorylation of tau by fyn: implications for Alzheimer\u2019s disease","volume":"24","author":"Lee","year":"2004","journal-title":"J. Neurosci."},{"issue":"5534","key":"10.1016\/j.mad.2019.01.007_bib0430","doi-asserted-by":"crossref","first-page":"1487","DOI":"10.1126\/science.1058189","article-title":"Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP","volume":"293","author":"Lewis","year":"2001","journal-title":"Science"},{"key":"10.1016\/j.mad.2019.01.007_bib0435","doi-asserted-by":"crossref","first-page":"12082","DOI":"10.1038\/ncomms12082","article-title":"The neuritic plaque facilitates pathological conversion of tau in an Alzheimer\u2019s disease mouse model","volume":"7","author":"Li","year":"2016","journal-title":"Nat. Commun."},{"issue":"8","key":"10.1016\/j.mad.2019.01.007_bib0440","doi-asserted-by":"crossref","first-page":"1942","DOI":"10.1111\/j.1460-9568.2005.04391.x","article-title":"Contributions of protein phosphatases PP1, PP2A, PP2B and PP5 to the regulation of tau phosphorylation","volume":"22","author":"Liu","year":"2005","journal-title":"Eur. J. Neurosci."},{"issue":"9","key":"10.1016\/j.mad.2019.01.007_bib0445","doi-asserted-by":"crossref","first-page":"3224","DOI":"10.1096\/fj.07-104539","article-title":"Overexpression of Dyrk1A contributes to neurofibrillary degeneration in Down syndrome","volume":"22","author":"Liu","year":"2008","journal-title":"FASEB J."},{"issue":"6","key":"10.1016\/j.mad.2019.01.007_bib0450","doi-asserted-by":"crossref","first-page":"659","DOI":"10.3233\/JAD-2004-6610","article-title":"Induction of hyperphosphorylated tau in primary rat cortical neuron cultures mediated by oxidative stress and glycogen synthase kinase-3","volume":"6","author":"Lovell","year":"2004","journal-title":"J. Alzheimers Dis."},{"issue":"28","key":"10.1016\/j.mad.2019.01.007_bib0455","doi-asserted-by":"crossref","first-page":"9078","DOI":"10.1523\/JNEUROSCI.1071-09.2009","article-title":"Beta-amyloid oligomers induce phosphorylation of tau and inactivation of insulin receptor substrate via c-Jun N-terminal kinase signaling: suppression by omega-3 fatty acids and curcumin","volume":"29","author":"Ma","year":"2009","journal-title":"J. Neurosci."},{"key":"10.1016\/j.mad.2019.01.007_bib0460","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1146\/annurev.biochem.77.061206.171059","article-title":"Aging and survival: the genetics of life span extension by dietary restriction","volume":"77","author":"Mair","year":"2008","journal-title":"Annu. Rev. Biochem."},{"issue":"12","key":"10.1016\/j.mad.2019.01.007_bib0465","doi-asserted-by":"crossref","first-page":"1122","DOI":"10.1097\/NEN.0b013e31818e06f3","article-title":"Type-dependent oxidative damage in frontotemporal lobar degeneration: cortical astrocytes are targets of oxidative damage","volume":"67","author":"Martinez","year":"2008","journal-title":"J. Neuropathol. Exp. Neurol."},{"issue":"7000","key":"10.1016\/j.mad.2019.01.007_bib0470","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1038\/nature02621","article-title":"Pathways towards and away from Alzheimer\u2019s disease","volume":"430","author":"Mattson","year":"2004","journal-title":"Nature"},{"issue":"6","key":"10.1016\/j.mad.2019.01.007_bib0475","doi-asserted-by":"crossref","first-page":"953","DOI":"10.1016\/j.neuron.2010.08.044","article-title":"Acetylation of tau inhibits its degradation and contributes to tauopathy","volume":"67","author":"Min","year":"2010","journal-title":"Neuron"},{"issue":"10","key":"10.1016\/j.mad.2019.01.007_bib0480","doi-asserted-by":"crossref","first-page":"1154","DOI":"10.1038\/nm.3951","article-title":"Critical role of acetylation in tau-mediated neurodegeneration and cognitive deficits","volume":"21","author":"Min","year":"2015","journal-title":"Nat. Med."},{"issue":"8","key":"10.1016\/j.mad.2019.01.007_bib0485","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1097\/01.jnen.0000173890.79058.1d","article-title":"Visualization of newly deposited tau in neurofibrillary tangles and neuropil threads","volume":"64","author":"Miyasaka","year":"2005","journal-title":"J. Neuropathol. Exp. Neurol."},{"issue":"11","key":"10.1016\/j.mad.2019.01.007_bib0490","doi-asserted-by":"crossref","DOI":"10.4172\/2155-9880.1000216","article-title":"The Sirtuin System: The Holy Grail of Resveratrol?","volume":"3","author":"Mohar","year":"2012","journal-title":"J. Clin. Exp. Cardiolog."},{"issue":"2","key":"10.1016\/j.mad.2019.01.007_bib0495","doi-asserted-by":"crossref","first-page":"823","DOI":"10.1074\/jbc.270.2.823","article-title":"Proline-directed and non-proline-directed phosphorylation of PHF-tau","volume":"270","author":"Morishima-Kawashima","year":"1995","journal-title":"J. Biol. Chem."},{"issue":"8","key":"10.1016\/j.mad.2019.01.007_bib0500","doi-asserted-by":"crossref","first-page":"1183","DOI":"10.1038\/nn.4067","article-title":"Tau post-translational modifications in wild-type and human amyloid precursor protein transgenic mice","volume":"18","author":"Morris","year":"2015","journal-title":"Nat. Neurosci."},{"issue":"7","key":"10.1016\/j.mad.2019.01.007_bib0505","doi-asserted-by":"crossref","DOI":"10.1101\/cshperspect.a006338","article-title":"Neurotoxicity of amyloid beta-protein: synaptic and network dysfunction","volume":"2","author":"Mucke","year":"2012","journal-title":"Cold Spring Harb. Perspect. Med."},{"issue":"5","key":"10.1016\/j.mad.2019.01.007_bib0510","doi-asserted-by":"crossref","first-page":"1131","DOI":"10.1086\/301594","article-title":"Familial multiple-system tauopathy with presenile dementia is localized to chromosome 17","volume":"61","author":"Murrell","year":"1997","journal-title":"Am. J. Hum. Genet."},{"issue":"4","key":"10.1016\/j.mad.2019.01.007_bib0515","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1007\/s10495-008-0301-y","article-title":"Cell death: protein misfolding and neurodegenerative diseases","volume":"14","author":"Nakamura","year":"2009","journal-title":"Apoptosis"},{"issue":"3","key":"10.1016\/j.mad.2019.01.007_bib0520","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1089\/ars.2012.4703","article-title":"Emerging role of protein-protein transnitrosylation in cell signaling pathways","volume":"18","author":"Nakamura","year":"2013","journal-title":"Antioxid. Redox Signal."},{"issue":"7400","key":"10.1016\/j.mad.2019.01.007_bib0525","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1038\/nature11060","article-title":"Prion-like behaviour and tau-dependent cytotoxicity of pyroglutamylated amyloid-beta","volume":"485","author":"Nussbaum","year":"2012","journal-title":"Nature"},{"issue":"4","key":"10.1016\/j.mad.2019.01.007_bib0530","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1016\/j.biopsych.2017.06.004","article-title":"Targeting fyn kinase in Alzheimer\u2019s disease","volume":"83","author":"Nygaard","year":"2018","journal-title":"Biol. Psychiatry"},{"issue":"1","key":"10.1016\/j.mad.2019.01.007_bib0535","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1186\/alzrt238","article-title":"Fyn kinase inhibition as a novel therapy for Alzheimer\u2019s disease","volume":"6","author":"Nygaard","year":"2014","journal-title":"Alzheimers Res. Ther."},{"issue":"3","key":"10.1016\/j.mad.2019.01.007_bib0540","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1016\/j.neuron.2004.07.003","article-title":"Abeta immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome","volume":"43","author":"Oddo","year":"2004","journal-title":"Neuron"},{"issue":"5","key":"10.1016\/j.mad.2019.01.007_bib0545","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1093\/jnen\/59.5.393","article-title":"Lipoperoxidation is selectively involved in progressive supranuclear palsy","volume":"59","author":"Odetti","year":"2000","journal-title":"J. Neuropathol. Exp. Neurol."},{"issue":"3","key":"10.1016\/j.mad.2019.01.007_bib0550","doi-asserted-by":"crossref","first-page":"288","DOI":"10.1016\/j.neulet.2005.05.003","article-title":"Palmitic and stearic fatty acids induce Alzheimer-like hyperphosphorylation of tau in primary rat cortical neurons","volume":"384","author":"Patil","year":"2005","journal-title":"Neurosci. Lett."},{"issue":"3","key":"10.1016\/j.mad.2019.01.007_bib0555","doi-asserted-by":"crossref","first-page":"270","DOI":"10.1016\/S0014-5793(00)02323-1","article-title":"Phosphorylated, but not native, tau protein assembles following reaction with the lipid peroxidation product, 4-hydroxy-2-nonenal","volume":"486","author":"Perez","year":"2000","journal-title":"FEBS Lett."},{"issue":"7","key":"10.1016\/j.mad.2019.01.007_bib0560","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1093\/hmg\/ddh083","article-title":"CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation","volume":"13","author":"Petrucelli","year":"2004","journal-title":"Hum. Mol. Genet."},{"issue":"8517","key":"10.1016\/j.mad.2019.01.007_bib0565","doi-asserted-by":"crossref","first-page":"1211","DOI":"10.1016\/S0140-6736(86)92212-9","article-title":"Filamentous aggregates in Pick\u2019s disease, progressive supranuclear palsy, and Alzheimer\u2019s disease share antigenic determinants with microtubule-associated protein, tau","volume":"2","author":"Pollock","year":"1986","journal-title":"Lancet"},{"issue":"6","key":"10.1016\/j.mad.2019.01.007_bib0570","doi-asserted-by":"crossref","first-page":"815","DOI":"10.1002\/ana.410430617","article-title":"Tau is a candidate gene for chromosome 17 frontotemporal dementia","volume":"43","author":"Poorkaj","year":"1998","journal-title":"Ann. Neurol."},{"issue":"3","key":"10.1016\/j.mad.2019.01.007_bib0575","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1042\/BJ20060463","article-title":"Phosphorylation inhibits turnover of the tau protein by the proteasome: influence of RCAN1 and oxidative stress","volume":"400","author":"Poppek","year":"2006","journal-title":"Biochem. J."},{"issue":"2","key":"10.1016\/j.mad.2019.01.007_bib0580","doi-asserted-by":"crossref","first-page":"111","DOI":"10.31887\/DCNS.2009.11.2\/cqiu","article-title":"Epidemiology of Alzheimer\u2019s disease: occurrence, determinants, and strategies toward intervention","volume":"11","author":"Qiu","year":"2009","journal-title":"Dialogues Clin. Neurosci."},{"issue":"9","key":"10.1016\/j.mad.2019.01.007_bib0585","doi-asserted-by":"crossref","first-page":"6364","DOI":"10.1073\/pnas.092136199","article-title":"Tau is essential to beta -amyloid-induced neurotoxicity","volume":"99","author":"Rapoport","year":"2002","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"6","key":"10.1016\/j.mad.2019.01.007_bib0590","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1038\/ng1362","article-title":"Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease","volume":"36","author":"Ravikumar","year":"2004","journal-title":"Nat. Genet."},{"issue":"13","key":"10.1016\/j.mad.2019.01.007_bib0595","doi-asserted-by":"crossref","first-page":"4314","DOI":"10.1021\/bi052142h","article-title":"Peroxynitrite-mediated tau modifications stabilize preformed filaments and destabilize microtubules through distinct mechanisms","volume":"45","author":"Reynolds","year":"2006","journal-title":"Biochemistry"},{"issue":"5825","key":"10.1016\/j.mad.2019.01.007_bib0600","doi-asserted-by":"crossref","first-page":"750","DOI":"10.1126\/science.1141736","article-title":"Reducing endogenous tau ameliorates amyloid beta-induced deficits in an Alzheimer\u2019s disease mouse model","volume":"316","author":"Roberson","year":"2007","journal-title":"Science"},{"issue":"2","key":"10.1016\/j.mad.2019.01.007_bib0605","doi-asserted-by":"crossref","first-page":"700","DOI":"10.1523\/JNEUROSCI.4152-10.2011","article-title":"Amyloid-beta\/Fyn-induced synaptic, network, and cognitive impairments depend on tau levels in multiple mouse models of Alzheimer\u2019s disease","volume":"31","author":"Roberson","year":"2011","journal-title":"J. Neurosci."},{"issue":"45","key":"10.1016\/j.mad.2019.01.007_bib0610","doi-asserted-by":"crossref","first-page":"15998","DOI":"10.1073\/pnas.0404184101","article-title":"Sir2 mediates longevity in the fly through a pathway related to calorie restriction","volume":"101","author":"Rogina","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"2","key":"10.1016\/j.mad.2019.01.007_bib0615","doi-asserted-by":"crossref","first-page":"3834","DOI":"10.3390\/ijms14023834","article-title":"Crosstalk between oxidative stress and SIRT1: impact on the aging process","volume":"14","author":"Salminen","year":"2013","journal-title":"Int. J. Mol. Sci."},{"issue":"10-11","key":"10.1016\/j.mad.2019.01.007_bib0620","first-page":"1357","article-title":"Mitochondrial signaling, TOR, and life span","volume":"387","author":"Schieke","year":"2006","journal-title":"Biol. Chem."},{"issue":"11","key":"10.1016\/j.mad.2019.01.007_bib0625","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1016\/j.tins.2010.07.004","article-title":"Protein modifications involved in neurotransmitter and gasotransmitter signaling","volume":"33","author":"Sen","year":"2010","journal-title":"Trends Neurosci."},{"issue":"522","key":"10.1016\/j.mad.2019.01.007_bib0630","doi-asserted-by":"crossref","DOI":"10.1126\/scisignal.aao6765","article-title":"Nitrosylation of GAPDH augments pathological tau acetylation upon exposure to amyloid-beta","volume":"11","author":"Sen","year":"2018","journal-title":"Sci. Signal."},{"issue":"2-3","key":"10.1016\/j.mad.2019.01.007_bib0635","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/j.bbadis.2004.06.020","article-title":"Tau protein as a differential biomarker of tauopathies","volume":"1739","author":"Sergeant","year":"2005","journal-title":"Biochim. Biophys. Acta"},{"issue":"5","key":"10.1016\/j.mad.2019.01.007_bib0640","doi-asserted-by":"crossref","first-page":"1688","DOI":"10.1523\/JNEUROSCI.2610-10.2011","article-title":"Tau protein is required for amyloid {beta}-induced impairment of hippocampal long-term potentiation","volume":"31","author":"Shipton","year":"2011","journal-title":"J. Neurosci."},{"issue":"5","key":"10.1016\/j.mad.2019.01.007_bib0645","doi-asserted-by":"crossref","first-page":"276","DOI":"10.1016\/S1474-4422(02)00130-8","article-title":"Pathological tau proteins in argyrophilic grain disease","volume":"1","author":"Simic","year":"2002","journal-title":"Lancet Neurol."},{"issue":"1","key":"10.1016\/j.mad.2019.01.007_bib0650","doi-asserted-by":"crossref","first-page":"6","DOI":"10.3390\/biom6010006","article-title":"Tau Protein Hyperphosphorylation and Aggregation in Alzheimer\u2019s Disease and Other Tauopathies, and Possible Neuroprotective Strategies","volume":"6","author":"Simic","year":"2016","journal-title":"Biomolecules"},{"issue":"1","key":"10.1016\/j.mad.2019.01.007_bib0655","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1006\/abbi.1996.0140","article-title":"Differential phosphorylation of human tau isoforms containing three repeats by several protein kinases","volume":"328","author":"Singh","year":"1996","journal-title":"Arch. Biochem. Biophys."},{"issue":"2","key":"10.1016\/j.mad.2019.01.007_bib0660","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1007\/BF00226782","article-title":"Non-proline-dependent protein kinases phosphorylate several sites found in tau from Alzheimer disease brain","volume":"154","author":"Singh","year":"1996","journal-title":"Mol. Cell. Biochem."},{"issue":"3","key":"10.1016\/j.mad.2019.01.007_bib0665","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1016\/S0014-5793(98)01185-5","article-title":"Ser-262 in human recombinant tau protein is a markedly more favorable site for phosphorylation by CaMKII than PKA or PhK","volume":"436","author":"Sironi","year":"1998","journal-title":"FEBS Lett."},{"issue":"6","key":"10.1016\/j.mad.2019.01.007_bib0670","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1016\/S1474-4422(13)70090-5","article-title":"Tau pathology and neurodegeneration","volume":"12","author":"Spillantini","year":"2013","journal-title":"Lancet Neurol."},{"issue":"13","key":"10.1016\/j.mad.2019.01.007_bib0675","doi-asserted-by":"crossref","first-page":"7737","DOI":"10.1073\/pnas.95.13.7737","article-title":"Mutation in the tau gene in familial multiple system tauopathy with presenile dementia","volume":"95","author":"Spillantini","year":"1998","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"3","key":"10.1016\/j.mad.2019.01.007_bib0680","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1016\/j.tins.2008.11.007","article-title":"Tau pathophysiology in neurodegeneration: a tangled issue","volume":"32","author":"Spires-Jones","year":"2009","journal-title":"Trends Neurosci."},{"issue":"6","key":"10.1016\/j.mad.2019.01.007_bib0685","doi-asserted-by":"crossref","first-page":"1051","DOI":"10.1083\/jcb.200108057","article-title":"Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress","volume":"156","author":"Stamer","year":"2002","journal-title":"J. Cell Biol."},{"issue":"2-3","key":"10.1016\/j.mad.2019.01.007_bib0690","doi-asserted-by":"crossref","first-page":"280","DOI":"10.1016\/j.bbadis.2004.06.017","article-title":"Tau phosphorylation: physiological and pathological consequences","volume":"1739","author":"Stoothoff","year":"2005","journal-title":"Biochim. Biophys. Acta"},{"issue":"3","key":"10.1016\/j.mad.2019.01.007_bib0695","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1016\/j.neulet.2009.11.010","article-title":"Chronic oxidative stress causes increased tau phosphorylation in M17 neuroblastoma cells","volume":"468","author":"Su","year":"2010","journal-title":"Neurosci. Lett."},{"issue":"10","key":"10.1016\/j.mad.2019.01.007_bib0700","doi-asserted-by":"crossref","first-page":"2658","DOI":"10.1128\/MCB.01639-08","article-title":"Acetylation of Nrf2 by p300\/CBP augments promoter-specific DNA binding of Nrf2 during the antioxidant response","volume":"29","author":"Sun","year":"2009","journal-title":"Mol. Cell. Biol."},{"issue":"42","key":"10.1016\/j.mad.2019.01.007_bib0705","doi-asserted-by":"crossref","first-page":"35222","DOI":"10.1074\/jbc.M112.348300","article-title":"Hyperphosphorylation of Tau induced by naturally secreted amyloid-beta at nanomolar concentrations is modulated by insulin-dependent Akt-GSK3beta signaling pathway","volume":"287","author":"Tokutake","year":"2012","journal-title":"J. Biol. Chem."},{"issue":"2","key":"10.1016\/j.mad.2019.01.007_bib0710","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1016\/j.neuron.2016.03.005","article-title":"Acetylated Tau Obstructs KIBRA-Mediated Signaling in Synaptic Plasticity and Promotes Tauopathy-Related Memory Loss","volume":"90","author":"Tracy","year":"2016","journal-title":"Neuron"},{"key":"10.1016\/j.mad.2019.01.007_bib0715","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1146\/annurev-pathol-020712-163927","article-title":"Emerging concepts in Alzheimer\u2019s disease","volume":"10","author":"Vinters","year":"2015","journal-title":"Annu. Rev. Pathol."},{"issue":"6001","key":"10.1016\/j.mad.2019.01.007_bib0720","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1126\/science.1194653","article-title":"Tau reduction prevents Abeta-induced defects in axonal transport","volume":"330","author":"Vossel","year":"2010","journal-title":"Science"},{"issue":"2","key":"10.1016\/j.mad.2019.01.007_bib0725","doi-asserted-by":"crossref","first-page":"200","DOI":"10.1016\/0169-328X(95)00316-K","article-title":"Restoration of biological activity of Alzheimer abnormally phosphorylated tau by dephosphorylation with protein phosphatase-2A, -2B and -1","volume":"38","author":"Wang","year":"1996","journal-title":"Brain Res. Mol. Brain Res."},{"issue":"1","key":"10.1016\/j.mad.2019.01.007_bib0730","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1111\/j.1460-9568.2006.05226.x","article-title":"Kinases and phosphatases and tau sites involved in Alzheimer neurofibrillary degeneration","volume":"25","author":"Wang","year":"2007","journal-title":"Eur. J. Neurosci."},{"issue":"4","key":"10.1016\/j.mad.2019.01.007_bib0735","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1007\/s00401-018-1891-2","article-title":"Physiological clearance of tau in the periphery and its therapeutic potential for tauopathies","volume":"136","author":"Wang","year":"2018","journal-title":"Acta Neuropathol."},{"issue":"6","key":"10.1016\/j.mad.2019.01.007_bib0740","first-page":"1159","article-title":"Localization of disinhibition-dementia-parkinsonism-amyotrophy complex to 17q21-22","volume":"55","author":"Wilhelmsen","year":"1994","journal-title":"Am. J. Hum. Genet."},{"issue":"4","key":"10.1016\/j.mad.2019.01.007_bib0745","doi-asserted-by":"crossref","first-page":"612","DOI":"10.1111\/j.1750-3639.2008.00197.x","article-title":"Transglutaminases and transglutaminase-catalyzed cross-links colocalize with the pathological lesions in Alzheimer\u2019s disease brain","volume":"19","author":"Wilhelmus","year":"2009","journal-title":"Brain Pathol."},{"issue":"Pt 3","key":"10.1016\/j.mad.2019.01.007_bib0750","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1042\/bj3550609","article-title":"The kinase DYRK phosphorylates protein-synthesis initiation factor eIF2Bepsilon at Ser539 and the microtubule-associated protein tau at Thr212: potential role for DYRK as a glycogen synthase kinase 3-priming kinase","volume":"355","author":"Woods","year":"2001","journal-title":"Biochem. J."},{"issue":"3","key":"10.1016\/j.mad.2019.01.007_bib0755","doi-asserted-by":"crossref","first-page":"733","DOI":"10.1007\/s12640-018-9895-1","article-title":"Clearance of Amyloid Beta and Tau in Alzheimer\u2019s Disease: from Mechanisms to Therapy","volume":"34","author":"Xin","year":"2018","journal-title":"Neurotox. Res."},{"issue":"16","key":"10.1016\/j.mad.2019.01.007_bib0760","doi-asserted-by":"crossref","first-page":"7787","DOI":"10.1073\/pnas.91.16.7787","article-title":"Glycated tau protein in Alzheimer disease: a mechanism for induction of oxidant stress","volume":"91","author":"Yan","year":"1994","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"3","key":"10.1016\/j.mad.2019.01.007_bib0765","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1159\/000362239","article-title":"Hypoxia-induced tau phosphorylation and memory deficit in rats","volume":"14","author":"Zhang","year":"2014","journal-title":"Neurodegener. Dis."}],"container-title":["Mechanisms of Ageing and Development"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0047637418302422?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0047637418302422?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,23]],"date-time":"2025-09-23T17:39:55Z","timestamp":1758649195000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0047637418302422"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,3]]},"references-count":153,"alternative-id":["S0047637418302422"],"URL":"https:\/\/doi.org\/10.1016\/j.mad.2019.01.007","relation":{},"ISSN":["0047-6374"],"issn-type":[{"value":"0047-6374","type":"print"}],"subject":[],"published":{"date-parts":[[2019,3]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Tauopathy: A common mechanism for neurodegeneration and brain aging","name":"articletitle","label":"Article Title"},{"value":"Mechanisms of Ageing and Development","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.mad.2019.01.007","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2019 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}]}}