{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T06:43:46Z","timestamp":1791269026485,"version":"4.1.0"},"reference-count":163,"publisher":"Elsevier BV","issue":"8","license":[{"start":{"date-parts":[[2012,11,1]],"date-time":"2012-11-01T00:00:00Z","timestamp":1351728000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2012,11,1]],"date-time":"2012-11-01T00:00:00Z","timestamp":1351728000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"content-domain":{"domain":["clinicalkey.com","clinicalkey.com.au","clinicalkey.es","clinicalkey.fr","clinicalkey.jp","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Archives of Medical Research"],"published-print":{"date-parts":[[2012,11]]},"DOI":"10.1016\/j.arcmed.2012.10.012","type":"journal-article","created":{"date-parts":[[2012,11,7]],"date-time":"2012-11-07T04:22:57Z","timestamp":1352262177000},"page":"645-654","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":58,"title":["Role of Tau Protein in Neuronal Damage in Alzheimer's Disease and Down Syndrome"],"prefix":"10.1016","volume":"43","author":[{"given":"Ana M.","family":"C\u00e1rdenas","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alvaro O.","family":"Ardiles","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Natalia","family":"Barraza","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ximena","family":"Ba\u00e9z-Matus","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pablo","family":"Caviedes","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.arcmed.2012.10.012_bib1","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1016\/0896-6273(89)90210-9","article-title":"Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer\u2019s disease","volume":"3","author":"Goedert","year":"1989","journal-title":"Neuron"},{"key":"10.1016\/j.arcmed.2012.10.012_bib2","doi-asserted-by":"crossref","first-page":"2300","DOI":"10.1046\/j.1471-4159.1994.63062300.x","article-title":"Diversity of high-molecular-weight tau proteins in different regions of the nervous system","volume":"63","author":"Mavilia","year":"1994","journal-title":"J Neurochem"},{"key":"10.1016\/j.arcmed.2012.10.012_bib3","doi-asserted-by":"crossref","first-page":"1389","DOI":"10.1016\/0896-6273(89)90077-9","article-title":"Developmentally regulated expression of specific tau sequences","volume":"2","author":"Kosik","year":"1989","journal-title":"Neuron"},{"key":"10.1016\/j.arcmed.2012.10.012_bib4","doi-asserted-by":"crossref","first-page":"4225","DOI":"10.1002\/j.1460-2075.1990.tb07870.x","article-title":"Expression of separate isoforms of human tau protein: correlation with the tau pattern in brain and effects on tubulin polymerization","volume":"9","author":"Goedert","year":"1990","journal-title":"EMBO J"},{"key":"10.1016\/j.arcmed.2012.10.012_bib5","doi-asserted-by":"crossref","first-page":"9548","DOI":"10.1073\/pnas.1633508100","article-title":"Differential regulation of microtubule dynamics by three- and four-repeat tau: implications for the onset of neurodegenerative disease","volume":"100","author":"Panda","year":"2003","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.arcmed.2012.10.012_bib6","doi-asserted-by":"crossref","first-page":"769","DOI":"10.1083\/jcb.124.5.769","article-title":"Identification of a novel microtubule binding and assembly domain in the developmentally regulated inter-repeat region of tau","volume":"124","author":"Goode","year":"1994","journal-title":"J Cell Biol"},{"key":"10.1016\/j.arcmed.2012.10.012_bib7","doi-asserted-by":"crossref","first-page":"1615","DOI":"10.1016\/0896-6273(89)90050-0","article-title":"The microtubule binding domain of tau protein","volume":"2","author":"Lee","year":"1989","journal-title":"Neuron"},{"key":"10.1016\/j.arcmed.2012.10.012_bib8","doi-asserted-by":"crossref","first-page":"28660","DOI":"10.1074\/jbc.M802645200","article-title":"Increased dosage of Dyrk1A alters alternative splicing factor (ASF)-regulated alternative splicing of tau in Down syndrome","volume":"283","author":"Shi","year":"2008","journal-title":"J Biol Chem"},{"key":"10.1016\/j.arcmed.2012.10.012_bib9","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1016\/S1471-4914(02)02440-1","article-title":"Tau gene mutations: dissecting the pathogenesis of FTDP-17","volume":"8","author":"Ingram","year":"2002","journal-title":"Trends Mol Med"},{"key":"10.1016\/j.arcmed.2012.10.012_bib10","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1097\/nen.0b013e31802c39a4","article-title":"The DeltaK280 mutation in MAP tau favors exon 10 skipping in\u00a0vivo","volume":"66","author":"van Swieten","year":"2007","journal-title":"J Neuropathol Exp Neurol"},{"key":"10.1016\/j.arcmed.2012.10.012_bib11","doi-asserted-by":"crossref","first-page":"2645","DOI":"10.1093\/brain\/awh591","article-title":"Hereditary Pick\u2019s disease with the G272V tau mutation shows predominant three-repeat tau pathology","volume":"128","author":"Bronner","year":"2005","journal-title":"Brain"},{"key":"10.1016\/j.arcmed.2012.10.012_bib12","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1002\/1531-8249(199909)46:3<325::AID-ANA8>3.0.CO;2-V","article-title":"Overexpression of four-repeat tau mRNA isoforms in progressive supranuclear palsy but not in Alzheimer\u2019s disease","volume":"46","author":"Chambers","year":"1999","journal-title":"Ann Neurol"},{"key":"10.1016\/j.arcmed.2012.10.012_bib13","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1007\/s00401-007-0280-z","article-title":"Increase in the relative expression of tau with four microtubule binding repeat regions in frontotemporal lobar degeneration and progressive supranuclear palsy brains","volume":"114","author":"Ingelsson","year":"2007","journal-title":"Acta Neuropathol"},{"key":"10.1016\/j.arcmed.2012.10.012_bib14","doi-asserted-by":"crossref","first-page":"4016","DOI":"10.1093\/hmg\/ddr330","article-title":"MicroRNA-132 loss is associated with tau exon 10 inclusion in progressive supranuclear palsy","volume":"20","author":"Smith","year":"2011","journal-title":"Hum Mol Genet"},{"key":"10.1016\/j.arcmed.2012.10.012_bib15","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1007\/s004010000283","article-title":"Distinct isoforms of tau aggregated in neurons and glial cells in brains of patients with Pick\u2019s disease, corticobasal degeneration and progressive supranuclear palsy","volume":"101","author":"Arai","year":"2001","journal-title":"Acta Neuropathol"},{"key":"10.1016\/j.arcmed.2012.10.012_bib16","doi-asserted-by":"crossref","first-page":"5301","DOI":"10.1016\/S0021-9258(17)42989-9","article-title":"Phosphorylation affects the ability of tau protein to promote microtubule assembly","volume":"259","author":"Lindwall","year":"1984","journal-title":"J Biol Chem"},{"key":"10.1016\/j.arcmed.2012.10.012_bib17","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/0896-6273(93)90279-Z","article-title":"Phosphorylation of Ser262 strongly reduces binding of tau to microtubules: distinction between PHF-like immunoreactivity and microtubule binding","volume":"11","author":"Biernat","year":"1993","journal-title":"Neuron"},{"key":"10.1016\/j.arcmed.2012.10.012_bib18","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"},{"key":"10.1016\/j.arcmed.2012.10.012_bib19","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 Cell Sci"},{"key":"10.1016\/j.arcmed.2012.10.012_bib20","doi-asserted-by":"crossref","first-page":"3549","DOI":"10.1021\/bi981874p","article-title":"Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments","volume":"38","author":"Schneider","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/j.arcmed.2012.10.012_bib21","doi-asserted-by":"crossref","first-page":"10506","DOI":"10.1074\/jbc.M211964200","article-title":"Tau phosphorylation by cyclin-dependent kinase 5\/p39 during brain development reduces its affinity for microtubules","volume":"278","author":"Takahashi","year":"2003","journal-title":"J Biol Chem"},{"key":"10.1016\/j.arcmed.2012.10.012_bib22","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.arcmed.2012.10.012_bib23","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1016\/j.bbadis.2004.09.002","article-title":"Tau and src family tyrosine kinases","volume":"1739","author":"Lee","year":"2005","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/j.arcmed.2012.10.012_bib24","doi-asserted-by":"crossref","first-page":"1587","DOI":"10.1046\/j.1471-4159.2000.0741587.x","article-title":"Phosphorylation sites on tau identified by nanoelectrospray mass spectrometry: differences in\u00a0vitro between the mitogen-activated protein kinases ERK2, c-Jun N-terminal kinase and P38, and glycogen synthase kinase-3beta","volume":"74","author":"Reynolds","year":"2000","journal-title":"J Neurochem"},{"key":"10.1016\/j.arcmed.2012.10.012_bib25","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"},{"key":"10.1016\/j.arcmed.2012.10.012_bib26","doi-asserted-by":"crossref","first-page":"577","DOI":"10.1042\/bj3230577","article-title":"Regulated phosphorylation and dephosphorylation of tau protein: effects on microtubule interaction, intracellular trafficking and neurodegeneration","volume":"323","author":"Billingsley","year":"1997","journal-title":"Biochem J"},{"key":"10.1016\/j.arcmed.2012.10.012_bib27","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 USA"},{"key":"10.1016\/j.arcmed.2012.10.012_bib28","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"},{"key":"10.1016\/j.arcmed.2012.10.012_bib29","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 USA"},{"key":"10.1016\/j.arcmed.2012.10.012_bib30","doi-asserted-by":"crossref","first-page":"5083","DOI":"10.1523\/JNEUROSCI.0604-06.2006","article-title":"Full reversal of Alzheimer\u2019s disease-like phenotype in a mouse model with conditional overexpression of glycogen synthase kinase-3","volume":"26","author":"Engel","year":"2006","journal-title":"J Neurosci"},{"key":"10.1016\/j.arcmed.2012.10.012_bib31","doi-asserted-by":"crossref","first-page":"25457","DOI":"10.1074\/jbc.M603469200","article-title":"The roles of cyclin-dependent kinase 5 and glycogen synthase kinase 3 in tau hyperphosphorylation","volume":"281","author":"Plattner","year":"2006","journal-title":"J Biol Chem"},{"key":"10.1016\/j.arcmed.2012.10.012_bib32","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1186\/1750-1326-2-12","article-title":"Tau phosphorylation by GSK-3beta promotes tangle-like filament morphology","volume":"2","author":"Rankin","year":"2007","journal-title":"Mol Neurodegener"},{"key":"10.1016\/j.arcmed.2012.10.012_bib33","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1016\/S0006-8993(98)00296-0","article-title":"Accumulation of cyclin-dependent kinase 5 (cdk5) in neurons with early stages of Alzheimer\u2019s disease neurofibrillary degeneration","volume":"797","author":"Pei","year":"1998","journal-title":"Brain Res"},{"key":"10.1016\/j.arcmed.2012.10.012_bib34","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1016\/S0896-6273(03)00627-5","article-title":"Aberrant Cdk5 activation by p25 triggers pathological events leading to neurodegeneration and neurofibrillary tangles","volume":"40","author":"Cruz","year":"2003","journal-title":"Neuron"},{"key":"10.1016\/j.arcmed.2012.10.012_bib35","doi-asserted-by":"crossref","first-page":"3134","DOI":"10.1021\/bi051635j","article-title":"Cyclin-dependent protein kinase 5 primes microtubule-associated protein tau site-specifically for glycogen synthase kinase 3beta","volume":"45","author":"Li","year":"2006","journal-title":"Biochemistry"},{"key":"10.1016\/j.arcmed.2012.10.012_bib36","doi-asserted-by":"crossref","first-page":"355","DOI":"10.3233\/JAD-2011-102016","article-title":"Potentiation of tau aggregation by cdk5 and GSK3\u03b2","volume":"26","author":"Lee","year":"2011","journal-title":"J Alzheimers Dis"},{"key":"10.1016\/j.arcmed.2012.10.012_bib37","doi-asserted-by":"crossref","first-page":"6584","DOI":"10.1523\/JNEUROSCI.1487-05.2005","article-title":"Tyrosine 394 is phosphorylated in Alzheimer's paired helical filament tau and in fetal tau with c-Abl as the candidate tyrosine kinase","volume":"25","author":"Derkinderen","year":"2005","journal-title":"J Neurosci"},{"key":"10.1016\/j.arcmed.2012.10.012_bib38","doi-asserted-by":"crossref","first-page":"460","DOI":"10.1111\/j.1471-4159.2011.07331.x","article-title":"AMP-activated protein kinase. A potential player in Alzheimer's disease","volume":"118","author":"Salminen","year":"2011","journal-title":"J Neurochem"},{"key":"10.1016\/j.arcmed.2012.10.012_bib39","doi-asserted-by":"crossref","first-page":"721","DOI":"10.3233\/JAD-2010-1271","article-title":"Tau phosphorylated at tyrosine 394 is found in Alzheimer\u2019s disease tangles and can be a product of the Abl-related kinase","volume":"19","author":"Tremblay","year":"2010","journal-title":"Arg. J Alzheimers Dis"},{"key":"10.1016\/j.arcmed.2012.10.012_bib40","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1096\/fj.10-167361","article-title":"Novel synthetic small-molecule activators of AMPK as enhancers of autophagy and amyloid-beta peptide degradation","volume":"25","author":"Vingtdeux","year":"2011","journal-title":"FASEB J"},{"key":"10.1016\/j.arcmed.2012.10.012_bib41","doi-asserted-by":"crossref","first-page":"392","DOI":"10.1016\/j.nbd.2005.03.020","article-title":"Constitutive Dyrk1A is abnormally expressed in Alzheimer disease, Down syndrome, Pick disease, and related transgenic models","volume":"20","author":"Ferrer","year":"2005","journal-title":"Neurobiol Dis"},{"key":"10.1016\/j.arcmed.2012.10.012_bib42","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"},{"key":"10.1016\/j.arcmed.2012.10.012_bib43","doi-asserted-by":"crossref","first-page":"34850","DOI":"10.1074\/jbc.M707358200","article-title":"DYRK1A-mediated hyperphosphorylation of Tau. A functional link between Down syndrome and Alzheimer disease","volume":"282","author":"Ryoo","year":"2007","journal-title":"J Biol Chem"},{"key":"10.1016\/j.arcmed.2012.10.012_bib44","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1007\/s00401-008-0419-6","article-title":"The role of overexpressed DYRK1A protein in the early onset of neurofibrillary degeneration in Down syndrome","volume":"116","author":"Wegiel","year":"2008","journal-title":"Acta Neuropathol"},{"key":"10.1016\/j.arcmed.2012.10.012_bib45","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1097\/NEN.0b013e318202bfa1","article-title":"Link between DYRK1A overexpression and several-fold enhancement of neurofibrillary degeneration with 3-repeat tau protein in Down syndrome","volume":"70","author":"Wegiel","year":"2011","journal-title":"J Neuropathol Exp Neurol"},{"key":"10.1016\/j.arcmed.2012.10.012_bib46","first-page":"439","article-title":"Biochemical characterization of an immune serum which specifically marks neurons in neurofibrillary degeneration in Alzheimer\u2019s disease","volume":"303","author":"Delacourte","year":"1986","journal-title":"CR Acad Sci III"},{"key":"10.1016\/j.arcmed.2012.10.012_bib47","doi-asserted-by":"crossref","first-page":"4913","DOI":"10.1073\/pnas.83.13.4913","article-title":"Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology","volume":"83","author":"Grundke-Iqbal","year":"1986","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.arcmed.2012.10.012_bib48","doi-asserted-by":"crossref","first-page":"4044","DOI":"10.1073\/pnas.83.11.4044","article-title":"Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease","volume":"83","author":"Kosik","year":"1986","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.arcmed.2012.10.012_bib49","doi-asserted-by":"crossref","first-page":"1541","DOI":"10.1093\/oxfordjournals.jbchem.a135625","article-title":"One of the antigenic determinants of paired helical filaments is related to tau protein","volume":"99","author":"Nukina","year":"1986","journal-title":"J Biochem"},{"key":"10.1016\/j.arcmed.2012.10.012_bib50","doi-asserted-by":"crossref","first-page":"4040","DOI":"10.1073\/pnas.83.11.4040","article-title":"Neurofibrillary tangles of Alzheimer disease share antigenic determinants with the axonal microtubule-associated protein tau (tau)","volume":"83","author":"Wood","year":"1986","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.arcmed.2012.10.012_bib51","doi-asserted-by":"crossref","first-page":"1807","DOI":"10.1093\/oxfordjournals.jbchem.a135662","article-title":"Phosphorylated tau protein is integrated into paired helical filaments in Alzheimer\u2019s disease","volume":"99","author":"Ihara","year":"1986","journal-title":"J Biochem"},{"key":"10.1016\/j.arcmed.2012.10.012_bib52","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1016\/S0140-6736(86)92134-3","article-title":"Defective brain microtubule assembly in Alzheimer\u2019s disease","volume":"2","author":"Iqbal","year":"1986","journal-title":"Lancet"},{"key":"10.1016\/j.arcmed.2012.10.012_bib53","doi-asserted-by":"crossref","first-page":"514","DOI":"10.1002\/ana.410220411","article-title":"Tau antisera recognize neurofibrillary tangles in a range of neurodegenerative disorders","volume":"22","author":"Joachim","year":"1987","journal-title":"Ann Neurol"},{"key":"10.1016\/j.arcmed.2012.10.012_bib54","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1002\/ana.410250207","article-title":"Immunocytochemical characterization of neurofibrillary tangles in amyotrophic lateral sclerosis and parkinsonism-dementia of Guam","volume":"25","author":"Shankar","year":"1989","journal-title":"Ann Neurol"},{"key":"10.1016\/j.arcmed.2012.10.012_bib55","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1093\/brain\/118.1.119","article-title":"Neurofibrillary tangles in Niemann-Pick disease type C","volume":"118","author":"Love","year":"1995","journal-title":"Brain"},{"key":"10.1016\/j.arcmed.2012.10.012_bib56","doi-asserted-by":"crossref","first-page":"460","DOI":"10.1001\/archneur.65.4.460","article-title":"Refining frontotemporal dementia with parkinsonism linked to chromosome 17: introducing FTDP-17 (MAPT) and FTDP-17 (PGRN)","volume":"65","author":"Boeve","year":"2008","journal-title":"Arch Neurol"},{"key":"10.1016\/j.arcmed.2012.10.012_bib57","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1016\/j.bbadis.2004.08.007","article-title":"Mutations causing neurodegenerative tauopathies","volume":"1739","author":"Goedert","year":"2005","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/j.arcmed.2012.10.012_bib58","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"},{"key":"10.1016\/j.arcmed.2012.10.012_bib59","doi-asserted-by":"crossref","first-page":"2583","DOI":"10.1046\/j.1471-4159.2000.0742583.x","article-title":"The FTDP-17-linked mutation R406W abolishes the interaction of phosphorylated tau with microtubules","volume":"4","author":"P\u00e9rez","year":"2000","journal-title":"J Neurochem"},{"key":"10.1016\/j.arcmed.2012.10.012_bib60","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"},{"key":"10.1016\/j.arcmed.2012.10.012_bib61","doi-asserted-by":"crossref","first-page":"11856","DOI":"10.1074\/jbc.M509420200","article-title":"FTDP-17 mutations compromise the ability of tau to regulate microtubule dynamics in cells","volume":"281","author":"Bunker","year":"2006","journal-title":"J Biol Chem"},{"key":"10.1016\/j.arcmed.2012.10.012_bib62","doi-asserted-by":"crossref","first-page":"36406","DOI":"10.1074\/jbc.M803519200","article-title":"FTDP-17 mutations in Tau alter the regulation of microtubule dynamics: an alternative core model for normal and pathological Tau action","volume":"283","author":"LeBoeuf","year":"2008","journal-title":"J Biol Chem"},{"key":"10.1016\/j.arcmed.2012.10.012_bib63","doi-asserted-by":"crossref","first-page":"13422","DOI":"10.1074\/jbc.M901095200","article-title":"Familial FTDP-17 missense mutations inhibit microtubule assembly-promoting activity of tau by increasing phosphorylation at Ser202 in\u00a0vitro","volume":"284","author":"Han","year":"2009","journal-title":"J Biol Chem"},{"key":"10.1016\/j.arcmed.2012.10.012_bib64","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1006\/jsbi.2000.4270","article-title":"Abnormal tau-containing filaments in neurodegenerative diseases","volume":"130","author":"Crowther","year":"2000","journal-title":"J Struct Biol"},{"key":"10.1016\/j.arcmed.2012.10.012_bib65","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1016\/S0002-9440(10)63812-6","article-title":"Filamentous tau in oligodendrocytes and astrocytes of transgenic mice expressing the human tau isoform with the P301L mutation","volume":"162","author":"Lin","year":"2003","journal-title":"Am J Pathol"},{"key":"10.1016\/j.arcmed.2012.10.012_bib66","doi-asserted-by":"crossref","first-page":"5704","DOI":"10.1016\/j.febslet.2005.09.047","article-title":"Transgenic mice expressing mutant (N279K) human tau show mutation dependent cognitive deficits without neurofibrillary tangle formation","volume":"579","author":"Taniguchi","year":"2005","journal-title":"FEBS Lett"},{"key":"10.1016\/j.arcmed.2012.10.012_bib67","doi-asserted-by":"crossref","first-page":"9155","DOI":"10.1523\/JNEUROSCI.5492-06.2007","article-title":"The tau N279K exon 10 splicing mutation recapitulates frontotemporal dementia and parkinsonism linked to chromosome 17 tauopathy in a mouse model","volume":"27","author":"Dawson","year":"2007","journal-title":"J Neurosci"},{"key":"10.1016\/j.arcmed.2012.10.012_bib68","doi-asserted-by":"crossref","first-page":"741","DOI":"10.1152\/physrev.2001.81.2.741","article-title":"Alzheimer\u2019s disease: genes, proteins, and therapy","volume":"81","author":"Selkoe","year":"2001","journal-title":"Physiol Rev"},{"key":"10.1016\/j.arcmed.2012.10.012_bib69","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"},{"key":"10.1016\/j.arcmed.2012.10.012_bib70","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1016\/0306-4522(94)90546-0","article-title":"Abnormally phosphorylated tau protein in Alzheimer\u2019s disease: heterogeneity of individual regional distribution and relationship to clinical severity","volume":"63","author":"Holzer","year":"1994","journal-title":"Neuroscience"},{"key":"10.1016\/j.arcmed.2012.10.012_bib71","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1016\/0197-4580(95)00013-5","article-title":"Correlations of synaptic and pathological markers with cognition of the elderly","volume":"16","author":"Dickson","year":"1995","journal-title":"Neurobiol Aging"},{"key":"10.1016\/j.arcmed.2012.10.012_bib72","doi-asserted-by":"crossref","first-page":"1063","DOI":"10.1016\/j.neurobiolaging.2003.08.012","article-title":"Amyloid deposition precedes tangle formation in a triple transgenic model of Alzheimer\u2019s disease","volume":"24","author":"Oddo","year":"2003","journal-title":"Neurobiol Aging"},{"key":"10.1016\/j.arcmed.2012.10.012_bib73","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1126\/science.1566067","article-title":"Alzheimer\u2019s disease: the amyloid cascade hypothesis","volume":"256","author":"Hardy","year":"1992","journal-title":"Science"},{"key":"10.1016\/j.arcmed.2012.10.012_bib74","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1126\/science.1072994","article-title":"The amyloid hypothesis of Alzheimer\u2019s disease: progress and problems on the road to therapeutics","volume":"297","author":"Hardy","year":"2002","journal-title":"Science"},{"key":"10.1016\/j.arcmed.2012.10.012_bib75","doi-asserted-by":"crossref","first-page":"546","DOI":"10.1016\/S0021-9258(18)48529-8","article-title":"Assembly and aggregation properties of synthetic Alzheimer\u2019s A4\/beta amyloid peptide analogs","volume":"267","author":"Burdick","year":"1992","journal-title":"J Biol Chem"},{"key":"10.1016\/j.arcmed.2012.10.012_bib76","doi-asserted-by":"crossref","first-page":"4693","DOI":"10.1021\/bi00069a001","article-title":"The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer\u2019s disease","volume":"32","author":"Jarrett","year":"1993","journal-title":"Biochemistry"},{"key":"10.1016\/j.arcmed.2012.10.012_bib77","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1073\/pnas.222681699","article-title":"Amyloid beta-protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways","volume":"100","author":"Bitan","year":"2003","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.arcmed.2012.10.012_bib78","doi-asserted-by":"crossref","first-page":"5161","DOI":"10.1073\/pnas.0600948103","article-title":"Early-onset behavioral and synaptic deficits in a mouse model of Alzheimer\u2019s disease","volume":"103","author":"Jacobsen","year":"2006","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.arcmed.2012.10.012_bib79","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1038\/nature04533","article-title":"A specific amyloid-beta protein assembly in the brain impairs memory","volume":"440","author":"Lesne","year":"2006","journal-title":"Nature"},{"key":"10.1016\/j.arcmed.2012.10.012_bib80","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1016\/j.bbr.2008.02.016","article-title":"Soluble oligomers of the amyloid beta-protein impair synaptic plasticity and behavior","volume":"192","author":"Selkoe","year":"2008","journal-title":"Behav Brain Res"},{"key":"10.1016\/j.arcmed.2012.10.012_bib81","doi-asserted-by":"crossref","first-page":"837","DOI":"10.1038\/nm1782","article-title":"Amyloid-beta protein dimers isolated directly from Alzheimer\u2019s brains impair synaptic plasticity and memory","volume":"14","author":"Shankar","year":"2008","journal-title":"Nat Med"},{"key":"10.1016\/j.arcmed.2012.10.012_bib82","doi-asserted-by":"crossref","first-page":"13835","DOI":"10.1073\/pnas.1201209109","article-title":"Postsynaptic dysfunction is associated with spatial and object recognition memory loss in a natural model of Alzheimer\u2019s disease","volume":"109","author":"Ardiles","year":"2012","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.arcmed.2012.10.012_bib83","doi-asserted-by":"crossref","first-page":"1128","DOI":"10.1038\/nature07761","article-title":"Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers","volume":"457","author":"Lauren","year":"2009","journal-title":"Nature"},{"key":"10.1016\/j.arcmed.2012.10.012_bib84","doi-asserted-by":"crossref","first-page":"7619","DOI":"10.1074\/jbc.M109.057182","article-title":"Inhibition of calcineurin-mediated endocytosis and alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors prevents amyloid beta oligomer-induced synaptic disruption","volume":"285","author":"Zhao","year":"2010","journal-title":"J Biol Chem"},{"key":"10.1016\/j.arcmed.2012.10.012_bib85","doi-asserted-by":"crossref","first-page":"796","DOI":"10.1523\/JNEUROSCI.3501-06.2007","article-title":"Abeta oligomer-induced aberrations in synapse composition, shape, and density provide a molecular basis for loss of connectivity in Alzheimer\u2019s disease","volume":"27","author":"Lacor","year":"2007","journal-title":"J\u00a0Neurosci"},{"key":"10.1016\/j.arcmed.2012.10.012_bib86","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1016\/j.neuron.2010.04.029","article-title":"Deleterious effects of amyloid beta oligomers acting as an extracellular scaffold for mGluR5","volume":"66","author":"Renner","year":"2010","journal-title":"Neuron"},{"key":"10.1016\/j.arcmed.2012.10.012_bib87","doi-asserted-by":"crossref","first-page":"a006338","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"},{"key":"10.1016\/j.arcmed.2012.10.012_bib88","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.arcmed.2012.10.012_bib89","doi-asserted-by":"crossref","first-page":"814","DOI":"10.1016\/j.nbd.2005.05.027","article-title":"Accelerated amyloid deposition, neurofibrillary degeneration and neuronal loss in double mutant APP\/tau transgenic mice","volume":"20","author":"Ribe","year":"2005","journal-title":"Neurobiol Dis"},{"key":"10.1016\/j.arcmed.2012.10.012_bib90","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1006\/exnr.2001.7630","article-title":"PP2A mRNA expression is quantitatively decreased in Alzheimer\u2019s disease hippocampus","volume":"168","author":"Vogelsberg-Ragaglia","year":"2001","journal-title":"Exp Neurol"},{"key":"10.1016\/j.arcmed.2012.10.012_bib91","doi-asserted-by":"crossref","first-page":"417","DOI":"10.3233\/JAD-2002-4508","article-title":"AbetaPP induces cdk5-dependent tau hyperphosphorylation in transgenic mice Tg2576","volume":"4","author":"Otth","year":"2002","journal-title":"J Alzheimers Dis"},{"key":"10.1016\/j.arcmed.2012.10.012_bib92","doi-asserted-by":"crossref","first-page":"6370","DOI":"10.1073\/pnas.1237107100","article-title":"Spherical aggregates of beta-amyloid (amylospheroid) show high neurotoxicity and activate tau protein kinase I\/glycogen synthase kinase-3beta","volume":"100","author":"Hoshi","year":"2003","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.arcmed.2012.10.012_bib93","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1016\/S0306-4522(02)00404-9","article-title":"Amyloid beta peptide induces tau phosphorylation and loss of cholinergic neurons in rat primary septal cultures","volume":"115","author":"Zheng","year":"2002","journal-title":"Neuroscience"},{"key":"10.1016\/j.arcmed.2012.10.012_bib94","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.arcmed.2012.10.012_bib95","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.arcmed.2012.10.012_bib96","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"},{"key":"10.1016\/j.arcmed.2012.10.012_bib97","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1016\/S0014-5793(02)02376-1","article-title":"Direct interaction of soluble human recombinant tau protein with Abeta 1-42 results in tau aggregation and hyperphosphorylation by tau protein kinase II","volume":"514","author":"Rank","year":"2002","journal-title":"FEBS Lett"},{"key":"10.1016\/j.arcmed.2012.10.012_bib98","doi-asserted-by":"crossref","first-page":"39413","DOI":"10.1074\/jbc.M608485200","article-title":"Reduction of soluble Abeta and tau, but not soluble Abeta alone, ameliorates cognitive decline in transgenic mice with plaques and tangles","volume":"281","author":"Oddo","year":"2006","journal-title":"J Biol Chem"},{"key":"10.1016\/j.arcmed.2012.10.012_bib99","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"},{"key":"10.1016\/j.arcmed.2012.10.012_bib100","doi-asserted-by":"crossref","first-page":"773","DOI":"10.1098\/rstb.2002.1264","article-title":"Elements of a neurobiological theory of the hippocampus: the role of activity-dependent synaptic plasticity in memory","volume":"358","author":"Morris","year":"2003","journal-title":"Philos Trans R Soc Lond B Biol Sci"},{"key":"10.1016\/j.arcmed.2012.10.012_bib101","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"},{"key":"10.1016\/j.arcmed.2012.10.012_bib102","doi-asserted-by":"crossref","first-page":"10741","DOI":"10.1523\/JNEUROSCI.1065-09.2009","article-title":"Age-dependent impairment of cognitive and synaptic function in the htau mouse model of tau pathology","volume":"29","author":"Polydoro","year":"2009","journal-title":"J Neurosci"},{"key":"10.1016\/j.arcmed.2012.10.012_bib103","doi-asserted-by":"crossref","first-page":"210","DOI":"10.1002\/cm.970080303","article-title":"Phosphorylation determines two distinct species of Tau in the central nervous system","volume":"8","author":"Papasozomenos","year":"1987","journal-title":"Cell Motil Cytoskeleton"},{"key":"10.1016\/j.arcmed.2012.10.012_bib104","doi-asserted-by":"crossref","first-page":"1067","DOI":"10.1016\/j.neuron.2010.11.030","article-title":"Tau mislocalization to dendritic spines mediates synaptic dysfunction independently of neurodegeneration","volume":"68","author":"Hoover","year":"2010","journal-title":"Neuron"},{"key":"10.1016\/j.arcmed.2012.10.012_bib105","doi-asserted-by":"crossref","first-page":"1079","DOI":"10.1016\/j.neurobiolaging.2003.04.007","article-title":"Clogging of axons by tau, inhibition of axonal traffic and starvation of synapses","volume":"24","author":"Mandelkow","year":"2003","journal-title":"Neurobiol Aging"},{"key":"10.1016\/j.arcmed.2012.10.012_bib106","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"},{"key":"10.1016\/j.arcmed.2012.10.012_bib107","doi-asserted-by":"crossref","first-page":"e15477","DOI":"10.1371\/journal.pone.0015477","article-title":"Multiple events lead to dendritic spine loss in triple transgenic Alzheimer\u2019s disease mice","volume":"5","author":"Bittner","year":"2010","journal-title":"PLoS ONE"},{"key":"10.1016\/j.arcmed.2012.10.012_bib108","doi-asserted-by":"crossref","first-page":"11938","DOI":"10.1523\/JNEUROSCI.2357-10.2010","article-title":"Abeta oligomers cause localized Ca2+ elevation, missorting of endogenous Tau into dendrites, Tau phosphorylation, and destruction of microtubules and spines","volume":"30","author":"Zempel","year":"2010","journal-title":"J Neurosci"},{"key":"10.1016\/j.arcmed.2012.10.012_bib109","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1146\/annurev.neuro.31.061307.090711","article-title":"Role of axonal transport in neurodegenerative diseases","volume":"31","author":"De Vos","year":"2008","journal-title":"Annu Rev Neurosci"},{"key":"10.1016\/j.arcmed.2012.10.012_bib110","doi-asserted-by":"crossref","first-page":"5907","DOI":"10.1073\/pnas.0901229106","article-title":"Disruption of fast axonal transport is a pathogenic mechanism for intraneuronal amyloid beta","volume":"106","author":"Pigino","year":"2009","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.arcmed.2012.10.012_bib111","doi-asserted-by":"crossref","first-page":"20523","DOI":"10.1073\/pnas.1006869107","article-title":"Deficits in axonal transport precede ALS symptoms in\u00a0vivo","volume":"107","author":"Bilsland","year":"2010","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.arcmed.2012.10.012_bib112","doi-asserted-by":"crossref","first-page":"835","DOI":"10.1152\/physrev.1995.75.4.835","article-title":"Role of microtubule-associated proteins in the control of microtubule assembly","volume":"75","author":"Maccioni","year":"1995","journal-title":"Physiol Rev"},{"key":"10.1016\/j.arcmed.2012.10.012_bib113","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"},{"key":"10.1016\/j.arcmed.2012.10.012_bib114","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 USA"},{"key":"10.1016\/j.arcmed.2012.10.012_bib115","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1083\/jcb.200605187","article-title":"Tau-dependent microtubule disassembly initiated by prefibrillar beta-amyloid","volume":"175","author":"King","year":"2006","journal-title":"J Cell Biol"},{"key":"10.1016\/j.arcmed.2012.10.012_bib116","doi-asserted-by":"crossref","first-page":"9166","DOI":"10.1523\/JNEUROSCI.1074-10.2010","article-title":"Amyloid-beta peptide oligomers disrupt axonal transport through an NMDA receptor-dependent mechanism that is mediated by glycogen synthase kinase 3beta in primary cultured hippocampal neurons","volume":"30","author":"Decker","year":"2010","journal-title":"J Neurosci"},{"key":"10.1016\/j.arcmed.2012.10.012_bib117","doi-asserted-by":"crossref","first-page":"376","DOI":"10.1523\/JNEUROSCI.12-02-00376.1992","article-title":"Beta-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity","volume":"12","author":"Mattson","year":"1992","journal-title":"J Neurosci"},{"key":"10.1016\/j.arcmed.2012.10.012_bib118","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 USA"},{"key":"10.1016\/j.arcmed.2012.10.012_bib119","doi-asserted-by":"crossref","first-page":"14439","DOI":"10.1523\/JNEUROSCI.3590-09.2009","article-title":"Divergent pathways mediate spine alterations and cell death induced by amyloid-beta, wild-type tau, and R406W tau","volume":"29","author":"Tackenberg","year":"2009","journal-title":"J Neurosci"},{"key":"10.1016\/j.arcmed.2012.10.012_bib120","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"},{"key":"10.1016\/j.arcmed.2012.10.012_bib121","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"},{"key":"10.1016\/j.arcmed.2012.10.012_bib122","doi-asserted-by":"crossref","first-page":"698","DOI":"10.1038\/nrd3505","article-title":"The amyloid cascade hypothesis for Alzheimer\u2019s disease: an appraisal for the development of therapeutics","volume":"10","author":"Karran","year":"2011","journal-title":"Nat Rev Drug Discov"},{"key":"10.1016\/j.arcmed.2012.10.012_bib123","doi-asserted-by":"crossref","first-page":"1117","DOI":"10.1007\/BF01941286","article-title":"Developmental genetics","volume":"42","author":"Epstein","year":"1986","journal-title":"Experientia"},{"key":"10.1016\/j.arcmed.2012.10.012_bib124","first-page":"191","article-title":"Abnormalities in the interferon response and immune systems in Down syndrome: studies in human trisomy 21 and mouse trisomy 16","volume":"246","author":"Epstein","year":"1987","journal-title":"Prog Clin Biol Res"},{"key":"10.1016\/j.arcmed.2012.10.012_bib125","doi-asserted-by":"crossref","first-page":"412536","DOI":"10.1155\/2012\/412536","article-title":"Aging and Down Syndrome","volume":"2012","author":"Head","year":"2012","journal-title":"Curr Gerontol Geriatr Res"},{"key":"10.1016\/j.arcmed.2012.10.012_bib126","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1017\/S1355617700001016","article-title":"The neuropsychology of mental retardation","volume":"2","author":"Pulsifer","year":"1996","journal-title":"J Int Neuropsychol Soc"},{"key":"10.1016\/j.arcmed.2012.10.012_bib127","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1038\/35012518","article-title":"Chromosome 21 mapping and sequencing consortium. The DNA sequence of human chromosome 21","volume":"405","author":"Hattori","year":"2000","journal-title":"Nature"},{"key":"10.1016\/j.arcmed.2012.10.012_bib128","doi-asserted-by":"crossref","first-page":"803","DOI":"10.1016\/0361-9230(86)90076-6","article-title":"Genetic basis for a mouse model of Down syndrome","volume":"16","author":"Reeves","year":"1986","journal-title":"Brain Res Bull"},{"key":"10.1016\/j.arcmed.2012.10.012_bib129","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1016\/0006-8993(89)90678-1","article-title":"Neurophysiological abnormalities in cultured dorsal root ganglion neurons from the trisomy-16 mouse fetus, a model for Down syndrome","volume":"485","author":"Ault","year":"1989","journal-title":"Brain Res"},{"key":"10.1016\/j.arcmed.2012.10.012_bib130","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1007\/978-3-7091-6721-2_12","article-title":"The MNB\/DYRK1A protein kinase: genetic and biochemical properties","volume":"67","author":"Galceran","year":"2003","journal-title":"J Neural Transm Suppl"},{"key":"10.1016\/j.arcmed.2012.10.012_bib131","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"},{"key":"10.1016\/j.arcmed.2012.10.012_bib132","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1093\/hmg\/ddl437","article-title":"The DYRK1A gene, encoded in chromosome 21 Down syndrome critical region, bridges between beta-amyloid production and tau phosphorylation in Alzheimer disease","volume":"16","author":"Kimura","year":"2007","journal-title":"Hum Mol Genet"},{"key":"10.1016\/j.arcmed.2012.10.012_bib133","doi-asserted-by":"crossref","first-page":"6161","DOI":"10.1093\/nar\/gkr195","article-title":"Regulation of the alternative splicing of tau exon 10 by SC35 and Dyrk1A","volume":"39","author":"Qian","year":"2011","journal-title":"Nucleic Acids Res"},{"key":"10.1016\/j.arcmed.2012.10.012_bib134","doi-asserted-by":"crossref","first-page":"30497","DOI":"10.1074\/jbc.M112.355412","article-title":"Dual-specificity-tyrosine-phosphorylated and regulated kinase 1A (Dyrk1A) modulates serine-arginine rich protein 55 (SRp55)-promoted tau exon 10 inclusion","volume":"287","author":"Yin","year":"2012","journal-title":"J Biol Chem"},{"key":"10.1016\/j.arcmed.2012.10.012_bib135","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1006\/abbi.1995.1225","article-title":"Transient adaptation of oxidative stress in mammalian cells","volume":"318","author":"Wiese","year":"1995","journal-title":"Arch Biochem Biophys"},{"key":"10.1016\/j.arcmed.2012.10.012_bib136","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1006\/abbi.1997.0109","article-title":"Hamster adapt78 mRNA is a Down syndrome critical region homologue that is inducible by oxidative stress","volume":"342","author":"Crawford","year":"1997","journal-title":"Arch Biochem Biophys"},{"key":"10.1016\/j.arcmed.2012.10.012_bib137","doi-asserted-by":"crossref","first-page":"1935","DOI":"10.1093\/hmg\/4.10.1935","article-title":"A new human gene from the Down syndrome critical region encodes a proline-rich protein highly expressed in fetal brain and heart","volume":"4","author":"Fuentes","year":"1995","journal-title":"Hum Mol Genet"},{"key":"10.1016\/j.arcmed.2012.10.012_bib138","doi-asserted-by":"crossref","first-page":"1681","DOI":"10.1093\/hmg\/9.11.1681","article-title":"DSCR1, overexpressed in Down syndrome, is an inhibitor of calcineurin-mediated signaling pathways","volume":"9","author":"Fuentes","year":"2000","journal-title":"Hum Mol Genet"},{"key":"10.1016\/j.arcmed.2012.10.012_bib139","doi-asserted-by":"crossref","first-page":"38787","DOI":"10.1074\/jbc.M102829200","article-title":"Chronic overexpression of the calcineurin inhibitory gene DSCR1 (Adapt78) is associated with Alzheimer\u2019s disease","volume":"276","author":"Ermak","year":"2001","journal-title":"J Biol Chem"},{"key":"10.1016\/j.arcmed.2012.10.012_bib140","doi-asserted-by":"crossref","first-page":"63","DOI":"10.3233\/JAD-2005-8108","article-title":"Expression of calcipressin1, an inhibitor of the phosphatase calcineurin, is altered with aging and Alzheimer\u2019s disease","volume":"8","author":"Cook","year":"2005","journal-title":"J Alzheimers Dis"},{"key":"10.1016\/j.arcmed.2012.10.012_bib141","doi-asserted-by":"crossref","first-page":"1715","DOI":"10.1111\/j.1742-4658.2007.05717.x","article-title":"RCAN1-1L is overexpressed in\u00a0neurons of Alzheimer\u2019s disease patients","volume":"274","author":"Harris","year":"2007","journal-title":"FEBS J"},{"key":"10.1016\/j.arcmed.2012.10.012_bib142","doi-asserted-by":"crossref","first-page":"924","DOI":"10.1097\/00005072-199608000-00008","article-title":"Reduction of calcineurin enzymatic activity in Alzheimer\u2019s disease: correlation with neuropathologic changes","volume":"55","author":"Ladner","year":"1996","journal-title":"J Neuropathol Exp Neurol"},{"key":"10.1016\/j.arcmed.2012.10.012_bib143","doi-asserted-by":"crossref","first-page":"1668","DOI":"10.1046\/j.1471-4159.1997.68041668.x","article-title":"Cytoskeletal changes in the brains of mice lacking calcineurin A alpha","volume":"68","author":"Kayyali","year":"1997","journal-title":"J Neurochem"},{"key":"10.1016\/j.arcmed.2012.10.012_bib144","doi-asserted-by":"crossref","first-page":"2100","DOI":"10.1111\/j.1742-4658.2006.05217.x","article-title":"RCAN1 (DSCR1 or Adapt78) stimulates expression of GSK-3beta","volume":"273","author":"Ermak","year":"2006","journal-title":"FEBS J"},{"key":"10.1016\/j.arcmed.2012.10.012_bib145","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 Cell Sci"},{"key":"10.1016\/j.arcmed.2012.10.012_bib146","doi-asserted-by":"crossref","first-page":"619","DOI":"10.1002\/j.1460-2075.1992.tb05094.x","article-title":"Dysregulation of gene expression in mouse trisomy 16, an animal model of Down syndrome","volume":"11","author":"Holtzman","year":"1992","journal-title":"EMBO J"},{"key":"10.1016\/j.arcmed.2012.10.012_bib147","doi-asserted-by":"crossref","first-page":"6788","DOI":"10.1523\/JNEUROSCI.23-17-06788.2003","article-title":"App gene dosage modulates endosomal abnormalities of Alzheimer\u2019s disease in a segmental trisomy 16 mouse model of Down syndrome","volume":"23","author":"Cataldo","year":"2003","journal-title":"J Neurosci"},{"key":"10.1016\/j.arcmed.2012.10.012_bib148","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1007\/s12035-010-8109-5","article-title":"Convergence of amyloid-beta and tau pathologies on mitochondria in\u00a0vivo","volume":"41","author":"Eckert","year":"2010","journal-title":"Mol Neurobiol"},{"key":"10.1016\/j.arcmed.2012.10.012_bib149","doi-asserted-by":"crossref","first-page":"92","DOI":"10.2174\/156720508783954721","article-title":"Processing of amyloid precursor protein and amyloid peptide neurotoxicity","volume":"5","author":"Nathalie","year":"2008","journal-title":"Curr Alzheimer Res"},{"key":"10.1016\/j.arcmed.2012.10.012_bib150","article-title":"Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy","author":"Selenica","year":"2012","journal-title":"Neurodegener Dis"},{"key":"10.1016\/j.arcmed.2012.10.012_bib151","doi-asserted-by":"crossref","first-page":"1333","DOI":"10.1111\/j.1471-4159.2007.05075.x","article-title":"Dual-specificity tyrosine(Y)-phosphorylation regulated kinase 1A-mediated phosphorylation of amyloid precursor protein: evidence for a functional link between Down syndrome and Alzheimer\u2019s disease","volume":"104","author":"Ryoo","year":"2008","journal-title":"J Neurochem"},{"key":"10.1016\/j.arcmed.2012.10.012_bib152","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1083\/jcb.200301115","article-title":"APP processing is regulated by cytoplasmic phosphorylation","volume":"163","author":"Lee","year":"2003","journal-title":"J Cell Biol"},{"key":"10.1016\/j.arcmed.2012.10.012_bib153","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1186\/1750-1326-6-80","article-title":"Mitosis-specific phosphorylation of amyloid precursor protein at threonine 668 leads to its altered processing and association with centrosomes","volume":"6","author":"Judge","year":"2011","journal-title":"Mol Neurodegener"},{"key":"10.1016\/j.arcmed.2012.10.012_bib154","doi-asserted-by":"crossref","first-page":"701","DOI":"10.3233\/JAD-2011-110890","article-title":"Amyloid-\u03b2 toxicity and tau hyperphosphorylation are linked via RCAN1 in Alzheimer\u2019s disease","volume":"27","author":"Lloret","year":"2011","journal-title":"J\u00a0Alzheimers Dis"},{"key":"10.1016\/j.arcmed.2012.10.012_bib155","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1097\/00001756-199902050-00028","article-title":"Calcium signals in cell lines derived from the cerebral cortex of normal and trisomy 16 mice","volume":"10","author":"C\u00e1rdenas","year":"1999","journal-title":"Neuroreport"},{"key":"10.1016\/j.arcmed.2012.10.012_bib156","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1016\/j.jphysparis.2005.12.013","article-title":"Neuronal dysfunction in Down syndrome: contribution of neuronal models in cell culture","volume":"99","author":"Saud","year":"2006","journal-title":"J\u00a0Physiol Paris"},{"key":"10.1016\/j.arcmed.2012.10.012_bib157","doi-asserted-by":"crossref","first-page":"1303","DOI":"10.1002\/jnr.21035","article-title":"Knockdown of amyloid precursor protein normalizes cholinergic function in a cell line derived from the cerebral cortex of a trisomy 16 mouse: an animal model of down syndrome","volume":"84","author":"Opazo","year":"2006","journal-title":"J Neurosci Res"},{"key":"10.1016\/j.arcmed.2012.10.012_bib158","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1016\/j.expneurol.2007.09.024","article-title":"Effect of the knockdown of amyloid precursor protein on intracellular calcium increases in a neuronal cell line derived from the cerebral cortex of a trisomy 16 mouse","volume":"209","author":"Rojas","year":"2008","journal-title":"Exp Neurol"},{"key":"10.1016\/j.arcmed.2012.10.012_bib159","first-page":"152.14","article-title":"RCAN1 overexpression results in enhanced voltage-gated calcium currents via impairment of inactivation in a neuronal cell line derived from cerebral cortex of Ts16 mice, an animal model of Down Syndrome","author":"Acu\u00f1a","year":"2011","journal-title":"Soc Neurosci Abstr"},{"key":"10.1016\/j.arcmed.2012.10.012_bib160","first-page":"152.15","article-title":"Knockdown of Rcan1 and Dyrk1A ameliorate the cholinergic dysfunction in cell lines derived from the cerebral cortex of a Ts16 mouse, a model of Down syndrome: possible role of VaChT and CHT1 proteins as targets","author":"Noriega","year":"2011","journal-title":"Soc Neurosci Abstr"},{"key":"10.1016\/j.arcmed.2012.10.012_bib161","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1007\/BF03262201","article-title":"The impact of cerebrospinal fluid biomarkers on the diagnosis of Alzheimer\u2019s disease","volume":"16","author":"Engelborghs","year":"2012","journal-title":"Mol Diagn Ther"},{"key":"10.1016\/j.arcmed.2012.10.012_bib162","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/j.jalz.2011.07.004","article-title":"Standardization of preanalytical aspects of cerebrospinal fluid biomarker testing for Alzheimer\u2019s disease diagnosis: a consensus paper from the Alzheimer\u2019s Biomarkers Standardization Initiative","volume":"8","author":"Vanderstichele","year":"2012","journal-title":"Alzheimers Dement"},{"key":"10.1016\/j.arcmed.2012.10.012_bib163","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1016\/j.bmcl.2011.11.043","article-title":"Discovery of potent small molecule inhibitors of DYRK1A by structure-based virtual screening and bioassay","volume":"22","author":"Wang","year":"2012","journal-title":"Bioorg Med Chem Lett"}],"container-title":["Archives of Medical Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0188440912002949?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0188440912002949?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,30]],"date-time":"2025-09-30T19:41:59Z","timestamp":1759261319000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0188440912002949"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2012,11]]},"references-count":163,"journal-issue":{"issue":"8","published-print":{"date-parts":[[2012,11]]}},"alternative-id":["S0188440912002949"],"URL":"https:\/\/doi.org\/10.1016\/j.arcmed.2012.10.012","relation":{},"ISSN":["0188-4409"],"issn-type":[{"value":"0188-4409","type":"print"}],"subject":[],"published":{"date-parts":[[2012,11]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Role of Tau Protein in Neuronal Damage in Alzheimer's Disease and Down Syndrome","name":"articletitle","label":"Article Title"},{"value":"Archives of Medical Research","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.arcmed.2012.10.012","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2012 IMSS. Published by Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}