{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,22]],"date-time":"2026-09-22T06:46:26Z","timestamp":1790059586214,"version":"4.0.1"},"reference-count":140,"publisher":"SAGE Publications","issue":"2","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["JAD"],"published-print":{"date-parts":[[2019,5,21]]},"DOI":"10.3233\/jad-180917","type":"journal-article","created":{"date-parts":[[2019,4,16]],"date-time":"2019-04-16T17:17:17Z","timestamp":1555435037000},"page":"339-353","source":"Crossref","is-referenced-by-count":13,"title":["Tau Protein and Zebrafish Models for Tau-Induced Neurodegeneration"],"prefix":"10.1177","volume":"69","author":[{"given":"Yuanting","family":"Ding","sequence":"first","affiliation":[{"name":"Department of Clinical Laboratory, The First Affliated Hospital of Guizhou University of Traditional Chinese Medicine, Guiyang, Guizhou, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lijuan","family":"Lei","sequence":"additional","affiliation":[{"name":"Department of Clinical Laboratory, The First Affliated Hospital of Guizhou University of Traditional Chinese Medicine, Guiyang, Guizhou, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chencen","family":"Lai","sequence":"additional","affiliation":[{"name":"Clinical Research Center, The First Affiliated Hospital of Guizhou University of Traditional Chinese Medicine, Guiyang, Guizhou, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhi","family":"Tang","sequence":"additional","affiliation":[{"name":"Clinical Research Center, The First Affiliated Hospital of Guizhou University of Traditional Chinese Medicine, Guiyang, Guizhou, China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"179","reference":[{"key":"10.3233\/JAD-180917_ref1","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1038\/nrneurol.2015.225","article-title":"Tau and neurodegenerative disease: The story so far","volume":"12","author":"Iqbal","year":"2016","journal-title":"Nat Rev Neurol"},{"key":"10.3233\/JAD-180917_ref2","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1007\/s00415-017-8644-3","article-title":"Corticobasal degeneration: Key emerging issues","volume":"265","author":"Ali","year":"2018","journal-title":"J Neurol"},{"key":"10.3233\/JAD-180917_ref3","doi-asserted-by":"crossref","first-page":"374","DOI":"10.1002\/1531-8249(200003)47:3<374::AID-ANA15>3.0.CO;2-8","article-title":"Corticobasal degeneration shares a common genetic background with progressive supranuclear palsy","volume":"47","author":"Di","year":"2000","journal-title":"Ann Neurol"},{"key":"10.3233\/JAD-180917_ref4","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1006\/nbdi.2002.0551","article-title":"Niemann-Pick disease type C yields possible clue for why cerebellar neurons do not form neurofibrillary tangles","volume":"11","author":"Bu","year":"2002","journal-title":"Neurobiol Dis"},{"key":"10.3233\/JAD-180917_ref5","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1111\/j.1582-4934.2008.00225.x","article-title":"Alzheimer neurofibrillary degeneration: Significance, etiopathogenesis, therapeutics and prevention","volume":"12","author":"Iqbal","year":"2008","journal-title":"J Cell Mol Med"},{"key":"10.3233\/JAD-180917_ref6","doi-asserted-by":"crossref","first-page":"962","DOI":"10.1042\/BST0380962","article-title":"Alzheimer\u2019s disease neurofibrillary degeneration: Pivotal and multifactorial","volume":"38","author":"Iqbal","year":"2010","journal-title":"Biochem Soc Trans"},{"key":"10.3233\/JAD-180917_ref7","doi-asserted-by":"crossref","first-page":"20","DOI":"10.2174\/157488911794079091","article-title":"Recent developments in tau-based therapeutics for neurodegenerative diseases","volume":"6","author":"Medina","year":"2011","journal-title":"Recent Pat CNS Drug Discov"},{"key":"10.3233\/JAD-180917_ref8","doi-asserted-by":"crossref","first-page":"863","DOI":"10.1038\/nrd.2017.155","article-title":"Tau-based therapies in neurodegeneration: Opportunities and challenges","volume":"16","author":"Li","year":"2017","journal-title":"Nat Rev Drug Discov"},{"key":"10.3233\/JAD-180917_ref9","doi-asserted-by":"crossref","first-page":"E1160","DOI":"10.3390\/ijms19041160","article-title":"An overview on the clinical development of tau-based therapeutics","volume":"19","author":"Medina","year":"2018","journal-title":"Int J Mol Sci"},{"key":"10.3233\/JAD-180917_ref10","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1007\/s00401-017-1707-9","article-title":"Roles of tau protein in health and disease","volume":"133","author":"Guo","year":"2017","journal-title":"Acta Neuropathol"},{"key":"10.3233\/JAD-180917_ref11","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1016\/j.bbadis.2004.08.010","article-title":"Tau gene alternative splicing: Expression patterns, regulation and modulation of function in normal brain and neurodegenerative diseases","volume":"1739","author":"Andreadis","year":"2005","journal-title":"Biochim Biophys Acta"},{"key":"10.3233\/JAD-180917_ref12","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1152\/physrev.00024.2003","article-title":"Role of tau protein in both physiological and pathological conditions","volume":"84","author":"Avila","year":"2004","journal-title":"Physiol Rev"},{"key":"10.3233\/JAD-180917_ref13","doi-asserted-by":"crossref","first-page":"1449","DOI":"10.1083\/jcb.107.4.1449","article-title":"Tau proteins: The molecular structure and mode of binding on microtubules","volume":"107","author":"Hirokawa","year":"1988","journal-title":"J Cell Biol"},{"key":"10.3233\/JAD-180917_ref14","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1016\/j.bbadis.2004.08.009","article-title":"Regulation of tau isoform expression and dementia","volume":"1739","author":"D\u2019Souza","year":"2005","journal-title":"Biochim Biophys Acta"},{"key":"10.3233\/JAD-180917_ref15","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/j.neulet.2006.06.036","article-title":"Immunohistochemical investigation of neurofibrillary tangles and their tau isoforms in brains of limbic neurofibrillary tangle dementia","volume":"405","author":"Iseki","year":"2006","journal-title":"Neurosci Lett"},{"key":"10.3233\/JAD-180917_ref16","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"},{"key":"10.3233\/JAD-180917_ref17","doi-asserted-by":"crossref","first-page":"458","DOI":"10.1016\/j.neuint.2010.12.023","article-title":"Post-translational modifications of tau protein: Imlications for Alzheimer\u2019s disease","volume":"58","author":"Martin","year":"2011","journal-title":"Neurochem Int"},{"key":"10.3233\/JAD-180917_ref18","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"},{"key":"10.3233\/JAD-180917_ref19","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 U S A"},{"key":"10.3233\/JAD-180917_ref20","doi-asserted-by":"crossref","first-page":"965","DOI":"10.1007\/s10571-017-0574-1","article-title":"Tau proteins and tauopathies in Alzheimer\u2019s disease","volume":"38","author":"Chong","year":"2018","journal-title":"Cell Mol Neurobiol"},{"key":"10.3233\/JAD-180917_ref21","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1186\/1750-1326-4-13","article-title":"The role of tau in neurodegeneration","volume":"4","author":"Gendron","year":"2009","journal-title":"Mol Neurodegener"},{"key":"10.3233\/JAD-180917_ref22","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1042\/bse0560111","article-title":"The physiology and pathology of microtubule-associated protein tau","volume":"56","author":"Wang","year":"2014","journal-title":"Essays Biochem"},{"key":"10.3233\/JAD-180917_ref23","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1016\/j.pneurobio.2008.03.002","article-title":"Microtubule-associated protein tau in development, degeneration and protection of neurons","volume":"85","author":"Wang","year":"2008","journal-title":"Prog Neurobiol"},{"key":"10.3233\/JAD-180917_ref24","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1042\/bj2690061","article-title":"The tubulin-binding sequence of brain microtubule-associated proteins, tau and MAP-2, is also involved in actin binding","volume":"269","author":"Correas","year":"1990","journal-title":"Biochem J"},{"key":"10.3233\/JAD-180917_ref25","doi-asserted-by":"crossref","first-page":"9143","DOI":"10.1016\/S0021-9258(18)34254-6","article-title":"The interaction of actin filaments with microtubules and microtubule-associated proteins","volume":"257","author":"Griffith","year":"1982","journal-title":"J Biol Chem"},{"key":"10.3233\/JAD-180917_ref26","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1016\/0300-9084(84)90007-5","article-title":"Interaction between microtubule-associated protein tau and spectrin","volume":"66","author":"Carlier","year":"1984","journal-title":"Biochimie"},{"key":"10.3233\/JAD-180917_ref27","doi-asserted-by":"crossref","first-page":"25481","DOI":"10.1074\/jbc.274.36.25481","article-title":"alpha-synuclein binds to Tau and stimulates the protein kinase A-catalyzed tau phosphorylation of serine residues 262 and 356","volume":"274","author":"Jensen","year":"1999","journal-title":"J Biol Chem"},{"key":"10.3233\/JAD-180917_ref28","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1006\/exnr.1997.6739","article-title":"Immunoreactivity of presenilin-1 and tau in Alzheimer\u2019s disease brain","volume":"149","author":"Hendriks","year":"1998","journal-title":"Exp Neurol"},{"key":"10.3233\/JAD-180917_ref29","doi-asserted-by":"crossref","first-page":"21901","DOI":"10.1074\/jbc.273.34.21901","article-title":"Protein phosphatase 1 is targeted to microtubules by the microtubule-associated protein Tau","volume":"273","author":"Liao","year":"1998","journal-title":"J Biol Chem"},{"key":"10.3233\/JAD-180917_ref30","doi-asserted-by":"crossref","first-page":"25490","DOI":"10.1074\/jbc.274.36.25490","article-title":"Molecular interactions among protein phosphatase 2A, tau, and microtubules. Implications for the regulation of tau phosphorylation and the development of tauopathies","volume":"274","author":"Sontag","year":"1999","journal-title":"J Biol Chem"},{"key":"10.3233\/JAD-180917_ref31","doi-asserted-by":"crossref","first-page":"16673","DOI":"10.1074\/jbc.M000784200","article-title":"Interaction of neuronal Cdc2-like protein kinase with microtubule-associated protein tau","volume":"275","author":"Sobue","year":"2000","journal-title":"J Biol Chem"},{"key":"10.3233\/JAD-180917_ref32","doi-asserted-by":"crossref","first-page":"1010","DOI":"10.1097\/00005072-199909000-00011","article-title":"Distribution of active glycogen synthase kinase 3beta (GSK-3beta) in brains staged for Alzheimer disease neurofibrillary changes","volume":"58","author":"Pei","year":"1999","journal-title":"J Neuropathol Exp Neurol"},{"key":"10.3233\/JAD-180917_ref33","doi-asserted-by":"crossref","first-page":"18342","DOI":"10.1074\/jbc.271.31.18342","article-title":"Activation of phospholipase C-gamma by the concerted action of tau proteins and arachidonic acid","volume":"271","author":"Hwang","year":"1996","journal-title":"J Biol Chem"},{"key":"10.3233\/JAD-180917_ref34","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1097\/00001756-199801050-00014","article-title":"Tau complexes with phospholipase C-gamma in situ","volume":"9","author":"Jenkins","year":"1998","journal-title":"Neuroreport"},{"key":"10.3233\/JAD-180917_ref35","doi-asserted-by":"crossref","first-page":"698","DOI":"10.1523\/JNEUROSCI.22-03-00698.2002","article-title":"Process outgrowth of oligodendrocytes is promoted by interaction of fyn kinase with the cytoskeletal protein tau","volume":"22","author":"Klein","year":"2002","journal-title":"J Neurosci"},{"issue":"Pt 21","key":"10.3233\/JAD-180917_ref36","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"},{"key":"10.3233\/JAD-180917_ref37","doi-asserted-by":"crossref","first-page":"332","DOI":"10.1006\/excr.1995.1323","article-title":"Localization andphosphorylation state of nuclear tau","volume":"220","author":"Greenwood","year":"1995","journal-title":"Exp Cell Res"},{"key":"10.3233\/JAD-180917_ref38","doi-asserted-by":"crossref","first-page":"1327","DOI":"10.1083\/jcb.131.5.1327","article-title":"Interaction of tau with the neural plasma membrane mediated by tau\u2019s amino-terminal projection domain","volume":"131","author":"Brandt","year":"1995","journal-title":"J Cell Biol"},{"key":"10.3233\/JAD-180917_ref39","doi-asserted-by":"crossref","first-page":"431 e427","DOI":"10.1016\/j.neurobiolaging.2011.01.005","article-title":"Dynamic association of tau with neuronal membranes is regulated by phosphorylation","volume":"33","author":"Pooler","year":"2012","journal-title":"Neurobiol Aging"},{"key":"10.3233\/JAD-180917_ref40","doi-asserted-by":"crossref","first-page":"83","DOI":"10.3389\/fneur.2013.00083","article-title":"The importance of tau phosphorylation for neurodegenerative diseases","volume":"4","author":"Noble","year":"2013","journal-title":"Front Neurol"},{"key":"10.3233\/JAD-180917_ref41","doi-asserted-by":"crossref","first-page":"49","DOI":"10.3389\/fnins.2010.00049","article-title":"Intracellular and extracellular tau","volume":"4","author":"Avila","year":"2010","journal-title":"Front Neurosci"},{"key":"10.3233\/JAD-180917_ref42","doi-asserted-by":"crossref","first-page":"582","DOI":"10.1046\/j.1471-4159.2003.01879.x","article-title":"Hyperphosphorylation and aggregation of tau in mice expressing normal human tau isoforms","volume":"86","author":"Andorfer","year":"2003","journal-title":"J Neurochem"},{"key":"10.3233\/JAD-180917_ref43","doi-asserted-by":"crossref","first-page":"960","DOI":"10.1097\/NEN.0b013e318232a379","article-title":"Stages of the pathologic process in Alzheimer disease: Age categories from 1 to 100 years","volume":"70","author":"Braak","year":"2011","journal-title":"J Neuropathol Exp Neurol"},{"key":"10.3233\/JAD-180917_ref44","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1016\/S0962-8924(98)01368-3","article-title":"Tau in Alzheimer\u2019s disease","volume":"8","author":"Mandelkow","year":"1998","journal-title":"Trends Cell Biol"},{"key":"10.3233\/JAD-180917_ref45","doi-asserted-by":"crossref","first-page":"871","DOI":"10.1038\/nm0896-871","article-title":"Glycosylation of microtubule-associated protein tau: An abnormal posttranslational modification in Alzheimer\u2019s disease","volume":"2","author":"Wang","year":"1996","journal-title":"Nat Med"},{"key":"10.3233\/JAD-180917_ref46","doi-asserted-by":"crossref","first-page":"708","DOI":"10.2174\/156720510793611556","article-title":"Tau truncation is a productive posttranslational modification of neurofibrillary degeneration in Alzheimer\u2019s disease","volume":"7","author":"Kovacech","year":"2010","journal-title":"Curr Alzheimer Res"},{"key":"10.3233\/JAD-180917_ref47","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"},{"key":"10.3233\/JAD-180917_ref48","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"},{"key":"10.3233\/JAD-180917_ref49","doi-asserted-by":"crossref","first-page":"1641","DOI":"10.1126\/science.3029875","article-title":"Ubiquitin is a component of paired helical filaments in Alzheimer\u2019s disease","volume":"235","author":"Mori","year":"1987","journal-title":"Science"},{"key":"10.3233\/JAD-180917_ref50","doi-asserted-by":"crossref","first-page":"23645","DOI":"10.1074\/jbc.M703269200","article-title":"Novel phosphorylation sites in tau from Alzheimer brain support a role for casein kinase 1 in disease pathogenesis","volume":"282","author":"Hanger","year":"2007","journal-title":"J Biol Chem"},{"key":"10.3233\/JAD-180917_ref51","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"},{"key":"10.3233\/JAD-180917_ref52","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1042\/bj2750099","article-title":"Tau in Alzheimer\u2019s disease and Down\u2019s syndrome is insoluble and abnormally phosphorylated","volume":"275 (Pt 1)","author":"Hanger","year":"1991","journal-title":"Biochem J"},{"key":"10.3233\/JAD-180917_ref53","doi-asserted-by":"crossref","first-page":"15418","DOI":"10.1074\/jbc.M112.448183","article-title":"Prostate-derived sterile 20-like kinases (PSKs\/TAOKs) phosphorylate tau protein and are activated in tangle-bearing neurons in Alzheimer disease","volume":"288","author":"Tavares","year":"2013","journal-title":"J Biol Chem"},{"key":"10.3233\/JAD-180917_ref54","doi-asserted-by":"crossref","first-page":"5721","DOI":"10.1242\/jcs.01558","article-title":"Tau phosphorylation in neuronal cell function and dysfunction","volume":"117","author":"Johnson","year":"2004","journal-title":"J Cell Sci"},{"issue":"Suppl 1","key":"10.3233\/JAD-180917_ref55","first-page":"S123","article-title":"Abnormal hyperphosphorylation of tau: Sites, regulation, and molecular mechanism of neurofibrillary degeneration","volume":"33","author":"Wang","year":"2013","journal-title":"J Alzheimers Dis"},{"key":"10.3233\/JAD-180917_ref56","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1016\/j.bbamcr.2013.03.019","article-title":"Substrate recognition in selective autophagy and the ubiquitin-proteasome system","volume":"1843","author":"Schreiber","year":"2014","journal-title":"Biochim Biophys Acta"},{"key":"10.3233\/JAD-180917_ref57","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":"10.3233\/JAD-180917_ref58","doi-asserted-by":"crossref","first-page":"E645","DOI":"10.3390\/ijms19030645","article-title":"Tau spreading mechanisms; implications for dysfunctional tauopathies","volume":"19","author":"Fuster-Matanzo","year":"2018","journal-title":"Int J Mol Sci"},{"key":"10.3233\/JAD-180917_ref59","doi-asserted-by":"crossref","first-page":"a024372","DOI":"10.1101\/cshperspect.a024372","article-title":"The prion-like behavior of assembled tau in transgenic mice","volume":"7","author":"Clavaguera","year":"2017","journal-title":"Cold Spring Harb Perspect Med"},{"key":"10.3233\/JAD-180917_ref60","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1007\/s00401-014-1254-6","article-title":"A novel in vivo model of tau propagation with rapid and progressive neurofibrillary tangle pathology: The pattern of spread is determined by connectivity, not proximity","volume":"127","author":"Ahmed","year":"2014","journal-title":"Acta Neuropathol"},{"key":"10.3233\/JAD-180917_ref61","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1016\/j.neuropharm.2013.08.037","article-title":"Intercellular transfer of tau aggregates and spreading of tau pathology: Implications for therapeutic strategies","volume":"76 Pt A","author":"Clavaguera","year":"2014","journal-title":"Neuropharmacology"},{"key":"10.3233\/JAD-180917_ref62","doi-asserted-by":"crossref","first-page":"9535","DOI":"10.1073\/pnas.1301175110","article-title":"Brain homogenates from human tauopathies induce tau inclusions in mouse brain","volume":"110","author":"Clavaguera","year":"2013","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.3233\/JAD-180917_ref63","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1051\/medsci\/2010262121","article-title":"[Induction and spreading of tau pathology in a mouse model of Alzheimer\u2019s disease]","volume":"26","author":"Clavaguera","year":"2010","journal-title":"Med Sci (Paris)"},{"key":"10.3233\/JAD-180917_ref64","doi-asserted-by":"crossref","first-page":"2012","DOI":"10.2353\/ajpath.2007.070403","article-title":"Induction of tau pathology by intracerebral infusion of amyloid-beta -containing brain extract and by amyloid-beta deposition in APP x Tau transgenic mice","volume":"171","author":"Bolmont","year":"2007","journal-title":"Am J Pathol"},{"key":"10.3233\/JAD-180917_ref65","doi-asserted-by":"crossref","first-page":"42751","DOI":"10.1074\/jbc.M112.380642","article-title":"Extracellular Tau levels are influenced by variability in Tau that is associated with tauopathies","volume":"287","author":"Karch","year":"2012","journal-title":"J Biol Chem"},{"key":"10.3233\/JAD-180917_ref66","doi-asserted-by":"crossref","first-page":"700","DOI":"10.1038\/srep00700","article-title":"Alzheimer brain-derived tau oligomers propagate pathology from endogenous tau","volume":"2","author":"Lasagna-Reeves","year":"2012","journal-title":"Sci Rep"},{"key":"10.3233\/JAD-180917_ref67","doi-asserted-by":"crossref","first-page":"647","DOI":"10.3233\/JAD-2010-1273","article-title":"Interneuronal transfer of human tau between Lamprey central neurons in situ","volume":"19","author":"Kim","year":"2010","journal-title":"J Alzheimers Dis"},{"key":"10.3233\/JAD-180917_ref68","first-page":"172837","article-title":"Accumulation of vesicle-associated human tau in distal dendrites drives degeneration and tau secretion in an in situ cellular tauopathy model","volume":"2012","author":"Lee","year":"2012","journal-title":"Int J Alzheimers Dis"},{"key":"10.3233\/JAD-180917_ref69","doi-asserted-by":"crossref","first-page":"13110","DOI":"10.1523\/JNEUROSCI.2569-11.2011","article-title":"In vivo microdialysis reveals age-dependent decrease of brain interstitial fluid tau levels in P301S human tau transgenic mice","volume":"31","author":"Yamada","year":"2011","journal-title":"J Neurosci"},{"key":"10.3233\/JAD-180917_ref70","doi-asserted-by":"crossref","first-page":"909","DOI":"10.1038\/ncb1901","article-title":"Transmission and spreading of tauopathy in transgenic mouse brain","volume":"11","author":"Clavaguera","year":"2009","journal-title":"Nat Cell Biol"},{"key":"10.3233\/JAD-180917_ref71","doi-asserted-by":"crossref","first-page":"1066","DOI":"10.1016\/j.jalz.2016.01.014","article-title":"Hyperphosphorylation determines both the spread and the morphology of tau pathology","volume":"12","author":"Hu","year":"2016","journal-title":"Alzheimers Dement"},{"key":"10.3233\/JAD-180917_ref72","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1097\/00005072-199701000-00007","article-title":"Distribution, levels, and activity of glycogen synthase kinase-3 in the Alzheimer disease brain","volume":"56","author":"Pei","year":"1997","journal-title":"J Neuropathol Exp Neurol"},{"key":"10.3233\/JAD-180917_ref73","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1016\/0014-5793(93)80849-P","article-title":"Abnormal Alzheimer-like phosphorylation of tau-protein by cyclin-dependent kinases cdk2 and cdk5","volume":"336","author":"Baumann","year":"1993","journal-title":"FEBS Lett"},{"key":"10.3233\/JAD-180917_ref74","doi-asserted-by":"crossref","first-page":"1190","DOI":"10.1093\/jnen\/60.12.1190","article-title":"Activation of the JNK\/p38 pathway occurs in diseases characterized by tau protein pathology and is related to tau phosphorylation but not to apoptosis","volume":"60","author":"Atzori","year":"2001","journal-title":"J Neuropathol Exp Neurol"},{"key":"10.3233\/JAD-180917_ref75","doi-asserted-by":"crossref","first-page":"1397","DOI":"10.1007\/s007020100016","article-title":"Phosphorylated mitogen-activated protein kinase (MAPK\/ERK-P), protein kinase of 38 kDa (p38-P), stress-activated protein kinase (SAPK\/JNK-P), and calcium\/calmodulin-dependent kinase II (CaM kinase II) are differentially expressed in tau deposits in neurons and glial cells in tauopathies","volume":"108","author":"Ferrer","year":"2001","journal-title":"J Neural Transm"},{"key":"10.3233\/JAD-180917_ref76","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/S0169-328X(02)00488-6","article-title":"Up-regulation of mitogen-activated protein kinases ERK1\/2 and MEK1\/2 is associated with the progression of neurofibrillary degeneration in Alzheimer\u2019s disease","volume":"109","author":"Pei","year":"2002","journal-title":"Brain Res Mol Brain Res"},{"key":"10.3233\/JAD-180917_ref77","doi-asserted-by":"crossref","first-page":"1434","DOI":"10.1038\/ng.2007.43","article-title":"Mutations in TTBK2, encoding a kinase implicated in tau phosphorylation, segregate with spinocerebellar ataxia type 11","volume":"39","author":"Houlden","year":"2007","journal-title":"Nat Genet"},{"key":"10.3233\/JAD-180917_ref78","doi-asserted-by":"crossref","first-page":"332","DOI":"10.1016\/j.tibs.2009.03.008","article-title":"The tau of MARK: A polarized view of the cytoskeleton","volume":"34","author":"Matenia","year":"2009","journal-title":"Trends Biochem Sci"},{"issue":"Pt 2","key":"10.3233\/JAD-180917_ref79","doi-asserted-by":"crossref","first-page":"655","DOI":"10.1042\/bj3160655","article-title":"Tau protein is phosphorylated by cyclic AMP-dependent protein kinase and calcium\/calmodulin-dependent protein kinase II within its microtubule-binding domains at Ser-262 and Ser-356","volume":"316","author":"Litersky","year":"1996","journal-title":"Biochem J"},{"key":"10.3233\/JAD-180917_ref80","doi-asserted-by":"crossref","first-page":"929","DOI":"10.3233\/JAD-2009-1113","article-title":"Interactions between glycogen synthase kinase 3beta, protein kinase B, and protein phosphatase 2A in tau phosphorylation in mouse N2a neuroblastoma cells","volume":"17","author":"Zhou","year":"2009","journal-title":"J Alzheimers Dis"},{"key":"10.3233\/JAD-180917_ref81","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/j.tips.2006.12.002","article-title":"PKC signaling deficits: A mechanistic hypothesis for the origins of Alzheimer\u2019s disease","volume":"28","author":"Alkon","year":"2007","journal-title":"Trends Pharmacol Sci"},{"key":"10.3233\/JAD-180917_ref82","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1210\/mend.14.1.0414","article-title":"Regulatory cascades involving calmodulin-dependent protein kinases","volume":"14","author":"Means","year":"2000","journal-title":"Mol Endocrinol"},{"key":"10.3233\/JAD-180917_ref83","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"},{"key":"10.3233\/JAD-180917_ref84","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":"10.3233\/JAD-180917_ref85","doi-asserted-by":"crossref","first-page":"732","DOI":"10.1046\/j.1471-4159.1995.65020732.x","article-title":"Phosphatase activity toward abnormally phosphorylated tau: Decrease in Alzheimer disease brain","volume":"65","author":"Gong","year":"1995","journal-title":"J Neurochem"},{"key":"10.3233\/JAD-180917_ref86","doi-asserted-by":"crossref","first-page":"188","DOI":"10.1016\/j.neurobiolaging.2014.07.035","article-title":"Cross talk between PI3K-AKT-GSK-3beta and PP2A pathways determines tau hyperphosphorylation","volume":"36","author":"Wang","year":"2015","journal-title":"Neurobiol Aging"},{"key":"10.3233\/JAD-180917_ref87","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/j.arr.2012.06.008","article-title":"Tau protein phosphatases in Alzheimer\u2019s disease: The leading role of PP2A","volume":"12","author":"Martin","year":"2013","journal-title":"Ageing Res Rev"},{"key":"10.3233\/JAD-180917_ref88","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"},{"key":"10.3233\/JAD-180917_ref89","doi-asserted-by":"crossref","first-page":"8229","DOI":"10.1073\/pnas.96.14.8229","article-title":"Structure of tau exon 10 splicing regulatory element RNA and destabilization by mutations of frontotemporal dementia and parkinsonism linked to chromosome 17","volume":"96","author":"Varani","year":"1999","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.3233\/JAD-180917_ref90","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1016\/S0014-5793(99)00210-0","article-title":"Polymerization of tau peptides into fibrillar structures. The effect of FTDP-17 mutations","volume":"446","author":"Arrasate","year":"1999","journal-title":"FEBS Lett"},{"key":"10.3233\/JAD-180917_ref91","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":"10.3233\/JAD-180917_ref92","doi-asserted-by":"crossref","first-page":"681","DOI":"10.1111\/j.1750-3639.1999.tb00550.x","article-title":"Comparative biochemistry of tau in progressive supranuclear palsy, corticobasal degeneration, FTDP-17 and Pick\u2019s disease","volume":"9","author":"Buee","year":"1999","journal-title":"Brain Pathol"},{"key":"10.3233\/JAD-180917_ref93","doi-asserted-by":"crossref","first-page":"1304","DOI":"10.1002\/j.1460-2075.1995.tb07116.x","article-title":"Somatodendritic localization and hyperphosphorylation of tau protein in transgenic mice expressing the longest human brain tau isoform","volume":"14","author":"Gotz","year":"1995","journal-title":"EMBO J"},{"key":"10.3233\/JAD-180917_ref94","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1016\/S0002-9440(10)65272-8","article-title":"Transgenic expression of the shortest human tau affects its compartmentalization and its phosphorylation as in the pretangle stage of Alzheimer\u2019s disease","volume":"154","author":"Brion","year":"1999","journal-title":"Am J Pathol"},{"key":"10.3233\/JAD-180917_ref95","doi-asserted-by":"crossref","first-page":"751","DOI":"10.1016\/S0896-6273(00)81127-7","article-title":"Age-dependent emergence and progression of a tauopathy in transgenic mice overexpressing the shortest human tau isoform","volume":"24","author":"Ishihara","year":"1999","journal-title":"Neuron"},{"key":"10.3233\/JAD-180917_ref96","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1007\/s004010051148","article-title":"Axonopathy and amyotrophy in mice transgenic for human four-repeat tau protein","volume":"99","author":"Probst","year":"2000","journal-title":"Acta Neuropathol"},{"key":"10.3233\/JAD-180917_ref97","doi-asserted-by":"crossref","first-page":"126","DOI":"10.1111\/j.1749-6632.2000.tb06914.x","article-title":"In vivo analysis of wild-type and FTDP-17 tau transgenic mice","volume":"920","author":"Gotz","year":"2000","journal-title":"Ann N Y Acad Sci"},{"key":"10.3233\/JAD-180917_ref98","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1111\/nan.12200","article-title":"Invited review: Animal models of tauopathies and their implications for research\/translation into the clinic","volume":"41","author":"Dujardin","year":"2015","journal-title":"Neuropathol Appl Neurobiol"},{"key":"10.3233\/JAD-180917_ref99","doi-asserted-by":"crossref","first-page":"266","DOI":"10.1016\/S0165-0173(01)00055-8","article-title":"Tau and transgenic animal models","volume":"35","author":"Gotz","year":"2001","journal-title":"Brain Res Brain Res Rev"},{"key":"10.3233\/JAD-180917_ref100","doi-asserted-by":"crossref","first-page":"9340","DOI":"10.1523\/JNEUROSCI.22-21-09340.2002","article-title":"Abundant tau filaments and nonapoptotic neurodegeneration in transgenic mice expressing human P301S tau protein","volume":"22","author":"Allen","year":"2002","journal-title":"J Neurosci"},{"key":"10.3233\/JAD-180917_ref101","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1038\/78078","article-title":"Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein","volume":"25","author":"Lewis","year":"2000","journal-title":"Nat Genet"},{"key":"10.3233\/JAD-180917_ref102","doi-asserted-by":"crossref","first-page":"702","DOI":"10.1006\/mcne.2001.1051","article-title":"FTDP-17 mutations in tau transgenic mice provoke lysosomal abnormalities and Tau filaments in forebrain","volume":"18","author":"Lim","year":"2001","journal-title":"Mol Cell Neurosci"},{"key":"10.3233\/JAD-180917_ref103","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":"10.3233\/JAD-180917_ref104","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1074\/jbc.M006531200","article-title":"Tau filament formation in transgenic mice expressing P301L tau","volume":"276","author":"Gotz","year":"2001","journal-title":"J Biol Chem"},{"key":"10.3233\/JAD-180917_ref105","doi-asserted-by":"crossref","first-page":"1036","DOI":"10.1006\/nbdi.2001.0439","article-title":"Formation of filamentous tau aggregations in transgenic mice expressing V337M human tau","volume":"8","author":"Tanemura","year":"2001","journal-title":"Neurobiol Dis"},{"key":"10.3233\/JAD-180917_ref106","doi-asserted-by":"crossref","first-page":"13896","DOI":"10.1073\/pnas.202205599","article-title":"Tau filament formation and associative memory deficit in aged mice expressing mutant (R406W) human tau","volume":"99","author":"Tatebayashi","year":"2002","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.3233\/JAD-180917_ref107","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1016\/j.bbadis.2010.09.011","article-title":"Zebrafish models for the functional genomics of neurogenetic disorders","volume":"1812","author":"Kabashi","year":"2011","journal-title":"Biochim Biophys Acta"},{"key":"10.3233\/JAD-180917_ref108","doi-asserted-by":"crossref","first-page":"189","DOI":"10.3389\/fgene.2014.00189","article-title":"Using the zebrafish model for Alzheimer\u2019s disease research","volume":"5","author":"Newman","year":"2014","journal-title":"Front Genet"},{"key":"10.3233\/JAD-180917_ref109","doi-asserted-by":"crossref","first-page":"346","DOI":"10.1016\/j.bbadis.2010.09.012","article-title":"Zebrafish as a tool in Alzheimer\u2019s disease research","volume":"1812","author":"Newman","year":"2011","journal-title":"Biochim Biophys Acta"},{"key":"10.3233\/JAD-180917_ref110","doi-asserted-by":"crossref","first-page":"264","DOI":"10.1016\/j.tins.2014.02.011","article-title":"Zebrafish models for translational neuroscience research: From tank to bedside","volume":"37","author":"Stewart","year":"2014","journal-title":"Trends Neurosci"},{"key":"10.3233\/JAD-180917_ref111","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1002\/aja.1002030302","article-title":"Stages of embryonic development of the zebrafish","volume":"203","author":"Kimmel","year":"1995","journal-title":"Dev Dyn"},{"key":"10.3233\/JAD-180917_ref112","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1007\/BF00195012","article-title":"The zebrafish brain: A neuroanatomical comparison with the goldfish","volume":"194","author":"Rupp","year":"1996","journal-title":"Anat Embryol (Berl)"},{"key":"10.3233\/JAD-180917_ref113","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1016\/j.brainres.2004.02.073","article-title":"The adult central nervous cholinergic system of a neurogenetic model animal, the zebrafish Danio rerio","volume":"1011","author":"Mueller","year":"2004","journal-title":"Brain Res"},{"key":"10.3233\/JAD-180917_ref114","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1016\/S0165-3806(02)00583-7","article-title":"Anatomy of neurogenesis in the early zebrafish brain","volume":"140","author":"Mueller","year":"2003","journal-title":"Brain Res Dev Brain Res"},{"key":"10.3233\/JAD-180917_ref115","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1016\/S0165-3806(02)00354-1","article-title":"Development of the catecholaminergic system in the early zebrafish brain: An immunohistochemical study","volume":"137","author":"Rink","year":"2002","journal-title":"Brain Res Dev Brain Res"},{"key":"10.3233\/JAD-180917_ref116","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/j.tips.2013.12.002","article-title":"Zebrafish as an emerging model for studying complex brain disorders","volume":"35","author":"Kalueff","year":"2014","journal-title":"Trends Pharmacol Sci"},{"key":"10.3233\/JAD-180917_ref117","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1089\/zeb.2006.3.235","article-title":"Modulatory neurotransmitter systems and behavior: Towards zebrafish models of neurodegenerative diseases","volume":"3","author":"Panula","year":"2006","journal-title":"Zebrafish"},{"key":"10.3233\/JAD-180917_ref118","doi-asserted-by":"crossref","first-page":"916","DOI":"10.1016\/j.cell.2008.04.037","article-title":"Live imaging of neuronal degradation by microglia reveals a role for v0-ATPase a1 in phagosomal fusion in vivo","volume":"133","author":"Peri","year":"2008","journal-title":"Cell"},{"key":"10.3233\/JAD-180917_ref119","doi-asserted-by":"crossref","first-page":"406","DOI":"10.1002\/glia.1126","article-title":"Three-dimensional distribution of astrocytes in zebrafish spinal cord","volume":"36","author":"Kawai","year":"2001","journal-title":"Glia"},{"key":"10.3233\/JAD-180917_ref120","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1002\/jnr.20516","article-title":"Oligodendrocyte development and myelination in GFP-transgenic zebrafish","volume":"81","author":"Yoshida","year":"2005","journal-title":"J Neurosci Res"},{"key":"10.3233\/JAD-180917_ref121","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1007\/s11064-006-9136-5","article-title":"Myelin structure and composition in zebrafish","volume":"32","author":"Avila","year":"2007","journal-title":"Neurochem Res"},{"key":"10.3233\/JAD-180917_ref122","doi-asserted-by":"crossref","first-page":"619","DOI":"10.1016\/j.brainresbull.2007.10.043","article-title":"Functional and developmental analysis of the blood-brain barrier in zebrafish","volume":"75","author":"Jeong","year":"2008","journal-title":"Brain Res Bull"},{"key":"10.3233\/JAD-180917_ref123","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1002\/dneu.20918","article-title":"Adult neurogenesis and brain regeneration in zebrafish","volume":"72","author":"Kizil","year":"2012","journal-title":"Dev Neurobiol"},{"key":"10.3233\/JAD-180917_ref124","doi-asserted-by":"crossref","first-page":"5815439","DOI":"10.1155\/2016\/5815439","article-title":"Regeneration of zebrafish CNS: Adult neurogenesis","volume":"2016","author":"Ghosh","year":"2016","journal-title":"Neural Plast"},{"key":"10.3233\/JAD-180917_ref125","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1016\/j.ydbio.2006.03.040","article-title":"Neural stem cells and neurogenesis in the adult zebrafish brain: Origin, proliferation dynamics, migration and cell fate.","volume":"295","author":"Grandel","year":"2006","journal-title":"Dev Biol"},{"key":"10.3233\/JAD-180917_ref126","doi-asserted-by":"crossref","first-page":"692","DOI":"10.1096\/fasebj.8.10.8050667","article-title":"Early neurogenesis in the zebrafish embryo","volume":"8","author":"Strahle","year":"1994","journal-title":"FASEB J"},{"key":"10.3233\/JAD-180917_ref127","doi-asserted-by":"crossref","first-page":"192","DOI":"10.1002\/biot.201200129","article-title":"Microfluidic tools for developmental studies of small model organisms\u2013nematodes, fruit flies, and zebrafish","volume":"8","author":"Hwang","year":"2013","journal-title":"Biotechnol J"},{"key":"10.3233\/JAD-180917_ref128","doi-asserted-by":"crossref","first-page":"11403","DOI":"10.1073\/pnas.97.21.11403","article-title":"Identification of a functional transposase of the Tol2 element, an Ac-like element from the Japanese medaka fish, and its transposition in the zebrafish germ lineage","volume":"97","author":"Kawakami","year":"2000","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.3233\/JAD-180917_ref129","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1089\/zeb.2008.0530","article-title":"Gal4\/UAS transgenic tools and their application to zebrafish","volume":"5","author":"Halpern","year":"2008","journal-title":"Zebrafish"},{"key":"10.3233\/JAD-180917_ref130","doi-asserted-by":"crossref","first-page":"e4640","DOI":"10.1371\/journal.pone.0004640","article-title":"Temporally-controlled site-specific recombination in zebrafish","volume":"4","author":"Hans","year":"2009","journal-title":"PLoS One"},{"key":"10.3233\/JAD-180917_ref131","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1038\/nbt.2501","article-title":"Efficient genome editing in zebrafish using a CRISPR-Cas system","volume":"31","author":"Hwang","year":"2013","journal-title":"Nat Biotechnol"},{"key":"10.3233\/JAD-180917_ref132","doi-asserted-by":"crossref","first-page":"305","DOI":"10.3233\/JAD-2009-1145","article-title":"Complex splicing and neural expression of duplicated tau genes in zebrafish embryos","volume":"18","author":"Chen","year":"2009","journal-title":"J Alzheimers Dis"},{"key":"10.3233\/JAD-180917_ref133","doi-asserted-by":"crossref","first-page":"734","DOI":"10.1002\/jnr.10451","article-title":"Transgenic zebrafish model of neurodegeneration","volume":"70","author":"Tomasiewicz","year":"2002","journal-title":"J Neurosci Res"},{"key":"10.3233\/JAD-180917_ref134","doi-asserted-by":"crossref","first-page":"6501","DOI":"10.1093\/nar\/gkm608","article-title":"Generation of a transgenic zebrafish model of Tauopathy using a novel promoter element derived from the zebrafish eno2 gene","volume":"35","author":"Bai","year":"2007","journal-title":"Nucleic Acids Res"},{"key":"10.3233\/JAD-180917_ref135","doi-asserted-by":"crossref","first-page":"1382","DOI":"10.1172\/JCI37537","article-title":"A zebrafish model of tauopathy allows in vivo imaging of neuronal cell death and drug evaluation","volume":"119","author":"Paquet","year":"2009","journal-title":"J Clin Invest"},{"key":"10.3233\/JAD-180917_ref136","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1186\/s12929-016-0237-4","article-title":"Multiple signaling factors and drugs alleviate neuronal death induced by expression of human and zebrafish tau proteins in vivo","volume":"23","author":"Wu","year":"2016","journal-title":"J Biomed Sci"},{"key":"10.3233\/JAD-180917_ref137","doi-asserted-by":"crossref","first-page":"1128","DOI":"10.1093\/brain\/awx005","article-title":"A152T tau allele causes neurodegeneration that can be ameliorated in a zebrafish model by autophagy induction","volume":"140","author":"Lopez","year":"2017","journal-title":"Brain"},{"key":"10.3233\/JAD-180917_ref138","doi-asserted-by":"crossref","first-page":"12959","DOI":"10.1038\/s41598-017-13311-5","article-title":"Human TAU(P301L) overexpression results in TAU hyperphosphorylation without neurofibrillary tangles in adult zebrafish brain","volume":"7","author":"Cosacak","year":"2017","journal-title":"Sci Rep"},{"key":"10.3233\/JAD-180917_ref139","doi-asserted-by":"crossref","first-page":"450","DOI":"10.1016\/j.ydbio.2006.06.010","article-title":"A developmental transition in growth control during zebrafish caudal fin development","volume":"296","author":"Goldsmith","year":"2006","journal-title":"Dev Biol"},{"key":"10.3233\/JAD-180917_ref140","doi-asserted-by":"crossref","first-page":"935","DOI":"10.1016\/S0531-5565(03)00159-1","article-title":"Growth versus lifespan: Perspectives from evolutionary ecology","volume":"38","author":"Metcalfe","year":"2003","journal-title":"Exp Gerontol"}],"container-title":["Journal of Alzheimer's Disease"],"original-title":[],"link":[{"URL":"https:\/\/content.iospress.com\/download?id=10.3233\/JAD-180917","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,4,28]],"date-time":"2026-04-28T10:09:35Z","timestamp":1777370975000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.sagepub.com\/doi\/full\/10.3233\/JAD-180917"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,5,21]]},"references-count":140,"journal-issue":{"issue":"2"},"URL":"https:\/\/doi.org\/10.3233\/jad-180917","relation":{},"ISSN":["1387-2877","1875-8908"],"issn-type":[{"value":"1387-2877","type":"print"},{"value":"1875-8908","type":"electronic"}],"subject":[],"published":{"date-parts":[[2019,5,21]]}}}