{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T19:23:20Z","timestamp":1791228200239,"version":"4.1.0"},"reference-count":87,"publisher":"Elsevier BV","issue":"17","license":[{"start":{"date-parts":[[2023,9,1]],"date-time":"2023-09-01T00:00:00Z","timestamp":1693526400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2023,9,1]],"date-time":"2023-09-01T00:00:00Z","timestamp":1693526400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2023,6,8]],"date-time":"2023-06-08T00:00:00Z","timestamp":1686182400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100002367","name":"Chinese Academy of Sciences","doi-asserted-by":"publisher","award":["XDB 37040202"],"award-info":[{"award-number":["XDB 37040202"]}],"id":[{"id":"10.13039\/501100002367","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100012166","name":"National Key Research and Development Program of China","doi-asserted-by":"publisher","award":["2019YFA0508403"],"award-info":[{"award-number":["2019YFA0508403"]}],"id":[{"id":"10.13039\/501100012166","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100004337","name":"Roche","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100004337","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["31971128"],"award-info":[{"award-number":["31971128"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Neuron"],"published-print":{"date-parts":[[2023,9]]},"DOI":"10.1016\/j.neuron.2023.05.033","type":"journal-article","created":{"date-parts":[[2023,6,28]],"date-time":"2023-06-28T12:34:25Z","timestamp":1687955665000},"page":"2660-2674.e9","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":36,"title":["Increased G3BP2-Tau interaction in tauopathies is a natural defense against Tau aggregation"],"prefix":"10.1016","volume":"111","author":[{"given":"Congwei","family":"Wang","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marco","family":"Terrigno","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Juan","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tania","family":"Distler","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nikhil J.","family":"Pandya","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Martin","family":"Ebeling","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stefka","family":"Tyanova","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jeroen J.M.","family":"Hoozemans","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anke A.","family":"Dijkstra","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luisa","family":"Fuchs","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shengqi","family":"Xiang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Azad","family":"Bonni","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fiona","family":"Gr\u00fcninger","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9477-7643","authenticated-orcid":false,"given":"Ravi","family":"Jagasia","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.neuron.2023.05.033_bib1","doi-asserted-by":"crossref","first-page":"592","DOI":"10.1038\/s41419-021-03873-8","article-title":"Stress granules, RNA-binding proteins and polyglutamine diseases: too much aggregation?","volume":"12","author":"Marcelo","year":"2021","journal-title":"Cell Death Dis."},{"key":"10.1016\/j.neuron.2023.05.033_bib2","doi-asserted-by":"crossref","first-page":"1455","DOI":"10.1016\/j.celrep.2016.04.045","article-title":"Interaction of tau with the RNA-Binding Protein TIA1 Regulates tau Pathophysiology and Toxicity","volume":"15","author":"Vanderweyde","year":"2016","journal-title":"Cell Rep."},{"key":"10.1016\/j.neuron.2023.05.033_bib3","doi-asserted-by":"crossref","first-page":"89","DOI":"10.3389\/fnmol.2017.00089","article-title":"Dysregulation of RNA binding protein aggregation in neurodegenerative disorders","volume":"10","author":"Maziuk","year":"2017","journal-title":"Front. Mol. Neurosci."},{"key":"10.1016\/j.neuron.2023.05.033_bib4","doi-asserted-by":"crossref","first-page":"35296","DOI":"10.1074\/jbc.M114.562959","article-title":"Aggregation properties of the small nuclear ribonucleoprotein U1-70K in Alzheimer disease","volume":"289","author":"Diner","year":"2014","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.neuron.2023.05.033_bib5","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1016\/j.celrep.2019.08.104","article-title":"Tau-mediated disruption of the spliceosome triggers cryptic RNA splicing and neurodegeneration in Alzheimer's disease","volume":"29","author":"Hsieh","year":"2019","journal-title":"Cell Rep."},{"key":"10.1016\/j.neuron.2023.05.033_bib6","doi-asserted-by":"crossref","first-page":"1675","DOI":"10.1016\/j.neuron.2021.03.026","article-title":"Tau aggregates are RNA-protein assemblies that mislocalize multiple nuclear speckle components","volume":"109","author":"Lester","year":"2021","journal-title":"Neuron"},{"key":"10.1016\/j.neuron.2023.05.033_bib7","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1186\/s40478-018-0574-5","article-title":"RNA binding proteins co-localize with small tau inclusions in tauopathy","volume":"6","author":"Maziuk","year":"2018","journal-title":"Acta Neuropathol. Commun."},{"key":"10.1016\/j.neuron.2023.05.033_bib8","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1038\/s41593-017-0022-z","article-title":"Reducing the RNA binding protein TIA1 protects against tau-mediated neurodegeneration in\u00a0vivo","volume":"21","author":"Apicco","year":"2018","journal-title":"Nat. Neurosci."},{"key":"10.1016\/j.neuron.2023.05.033_bib9","doi-asserted-by":"crossref","first-page":"4305","DOI":"10.1038\/s41467-020-18022-6","article-title":"RNA-binding proteins Musashi and tau soluble aggregates initiate nuclear dysfunction","volume":"11","author":"Montalbano","year":"2020","journal-title":"Nat. Commun."},{"key":"10.1016\/j.neuron.2023.05.033_bib10","doi-asserted-by":"crossref","first-page":"208","DOI":"10.1016\/j.molcel.2015.08.018","article-title":"Formation and maturation of phase-separated liquid droplets by RNA-binding proteins","volume":"60","author":"Lin","year":"2015","journal-title":"Mol. Cell"},{"key":"10.1016\/j.neuron.2023.05.033_bib11","doi-asserted-by":"crossref","DOI":"10.1126\/science.aaf4382","article-title":"Liquid phase condensation in cell physiology and disease","volume":"357","author":"Shin","year":"2017","journal-title":"Science"},{"key":"10.1016\/j.neuron.2023.05.033_bib12","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1007\/978-981-32-9358-8_26","article-title":"The pathophysiology of tau and stress granules in disease","volume":"1184","author":"Cruz","year":"2019","journal-title":"Adv. Exp. Med. Biol."},{"key":"10.1016\/j.neuron.2023.05.033_bib13","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1007\/978-3-030-31434-7_8","article-title":"RNA granules and their role in neurodegenerative diseases","volume":"1203","author":"Sidib\u00e9","year":"2019","journal-title":"Adv. Exp. Med. Biol."},{"key":"10.1016\/j.neuron.2023.05.033_bib14","doi-asserted-by":"crossref","first-page":"649","DOI":"10.1038\/s41583-019-0222-5","article-title":"Stress granules and neurodegeneration","volume":"20","author":"Wolozin","year":"2019","journal-title":"Nat. Rev. Neurosci."},{"key":"10.1016\/j.neuron.2023.05.033_bib15","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1016\/j.tcb.2022.01.011","article-title":"Tau liquid-liquid phase separation in neurodegenerative diseases","volume":"32","author":"Boyko","year":"2022","journal-title":"Trends Cell Biol."},{"key":"10.1016\/j.neuron.2023.05.033_bib16","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1177\/37.2.2492045","article-title":"Distribution of tau proteins in the normal human central and peripheral nervous system","volume":"37","author":"Trojanowski","year":"1989","journal-title":"J.\u00a0Histochem. Cytochem."},{"key":"10.1016\/j.neuron.2023.05.033_bib17","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1016\/j.celrep.2016.02.090","article-title":"mTORC1 inhibition corrects neurodevelopmental and synaptic alterations in a human stem cell model of tuberous sclerosis","volume":"15","author":"Costa","year":"2016","journal-title":"Cell Rep."},{"key":"10.1016\/j.neuron.2023.05.033_bib18","doi-asserted-by":"crossref","first-page":"4869","DOI":"10.1074\/jbc.M305838200","article-title":"CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival","volume":"279","author":"Shimura","year":"2004","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.neuron.2023.05.033_bib19","doi-asserted-by":"crossref","first-page":"1450","DOI":"10.1096\/fj.12-220889","article-title":"Imbalance of Hsp70 family variants fosters tau accumulation","volume":"27","author":"Jinwal","year":"2013","journal-title":"FASEB J."},{"key":"10.1016\/j.neuron.2023.05.033_bib20","doi-asserted-by":"crossref","first-page":"1441","DOI":"10.3390\/biom5031441","article-title":"Comprehensive protein interactome analysis of a key RNA helicase: detection of novel stress granule proteins","volume":"5","author":"Bish","year":"2015","journal-title":"Biomolecules"},{"key":"10.1016\/j.neuron.2023.05.033_bib21","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1016\/S0197-4580(97)00056-0","article-title":"Frequency of stages of Alzheimer-related lesions in different age categories","volume":"18","author":"Braak","year":"1997","journal-title":"Neurobiol. Aging"},{"key":"10.1016\/j.neuron.2023.05.033_bib22","doi-asserted-by":"crossref","first-page":"655","DOI":"10.1016\/j.cell.2020.12.024","article-title":"G3BPs tether the TSC complex to lysosomes and suppress mTORC1 signaling","volume":"184","author":"Prentzell","year":"2021","journal-title":"Cell"},{"key":"10.1016\/j.neuron.2023.05.033_bib84","doi-asserted-by":"crossref","first-page":"360","DOI":"10.1016\/j.bbamcr.2018.09.001","article-title":"Rasputin a decade on and more promiscuous than ever? A review of G3BPs","volume":"1866","author":"Alam","year":"2019","journal-title":"Biochim Biophys Acta Mol Cell Res"},{"key":"10.1016\/j.neuron.2023.05.033_bib85","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1083\/jcb.201408092","article-title":"G3BP1 promotes stress-induced RNA granule interactions to preserve polyadenylated mRNA","volume":"209","author":"Aulas","year":"2015","journal-title":"J Cell Biol"},{"key":"10.1016\/j.neuron.2023.05.033_bib86","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1004242","article-title":"G3BP1, G3BP2 and CAPRIN1 are required for translation of interferon stimulated mRNAs and are targeted by a dengue virus non-coding RNA","volume":"10","author":"Bidet","year":"2014","journal-title":"PLoS Pathog"},{"key":"10.1016\/j.neuron.2023.05.033_bib87","first-page":"2446","article-title":"Wnt3a-stimulated LRP6 phosphorylation is dependent upon arginine methylation of G3BP2","volume":"125","author":"Bikkavilli","year":"2012","journal-title":"J Cell Sci"},{"key":"10.1016\/j.neuron.2023.05.033_bib23","doi-asserted-by":"crossref","first-page":"648","DOI":"10.1126\/science.1262110","article-title":"Human genomics. The Genotype-Tissue Expression (GTEx) pilot analysis: multitissue gene regulation in humans","volume":"348","year":"2015","journal-title":"Science"},{"key":"10.1016\/j.neuron.2023.05.033_bib24","doi-asserted-by":"crossref","first-page":"944","DOI":"10.1111\/jnc.15280","article-title":"The multi-functional RNA-binding protein G3BP1 and its potential implication in neurodegenerative disease","volume":"157","author":"Sidib\u00e9","year":"2021","journal-title":"J.\u00a0Neurochem."},{"key":"10.1016\/j.neuron.2023.05.033_bib25","doi-asserted-by":"crossref","first-page":"16562","DOI":"10.1073\/pnas.1310249110","article-title":"U1 small nuclear ribonucleoprotein complex and RNA splicing alterations in Alzheimer\u2019s disease","volume":"110","author":"Bai","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.neuron.2023.05.033_bib26","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1038\/s41467-017-00922-9","article-title":"LSD1 protects against hippocampal and cortical neurodegeneration","volume":"8","author":"Christopher","year":"2017","journal-title":"Nat. Commun."},{"key":"10.1016\/j.neuron.2023.05.033_bib27","doi-asserted-by":"crossref","DOI":"10.3791\/55835","article-title":"Enrichment of detergent-insoluble protein aggregates from human postmortem brain","author":"Diner","year":"2017","journal-title":"J.\u00a0Vis. Exp."},{"key":"10.1016\/j.neuron.2023.05.033_bib28","doi-asserted-by":"crossref","first-page":"656","DOI":"10.2174\/156720510793611592","article-title":"Tau in Alzheimer disease and related tauopathies","volume":"7","author":"Iqbal","year":"2010","journal-title":"Curr. Alzheimer Res."},{"key":"10.1016\/j.neuron.2023.05.033_bib29","doi-asserted-by":"crossref","first-page":"1858","DOI":"10.1073\/pnas.72.5.1858","article-title":"A protein factor essential for microtubule assembly","volume":"72","author":"Weingarten","year":"1975","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.neuron.2023.05.033_bib30","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1007\/s00401-007-0207-8","article-title":"Disruption of microtubule network by Alzheimer abnormally hyperphosphorylated tau","volume":"113","author":"Li","year":"2007","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.neuron.2023.05.033_bib31","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.neuron.2023.05.033_bib32","doi-asserted-by":"crossref","first-page":"964","DOI":"10.1097\/00005072-199609000-00003","article-title":"Reduction of acetylated alpha-tubulin immunoreactivity in neurofibrillary tangle-bearing neurons in Alzheimer's disease","volume":"55","author":"Hempen","year":"1996","journal-title":"J.\u00a0Neuropathol. Exp. Neurol."},{"key":"10.1016\/j.neuron.2023.05.033_bib33","doi-asserted-by":"crossref","first-page":"13149","DOI":"10.1038\/s41598-020-70174-z","article-title":"Differential protein expression in diverse brain areas of Parkinson\u2019s and Alzheimer\u2019s disease patients","volume":"10","author":"Esteves","year":"2020","journal-title":"Sci. Rep."},{"key":"10.1016\/j.neuron.2023.05.033_bib34","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0161969","article-title":"Self-organizing 3D human neural tissue derived from induced pluripotent stem cells recapitulate Alzheimer\u2019s disease phenotypes","volume":"11","author":"Raja","year":"2016","journal-title":"PLoS One"},{"key":"10.1016\/j.neuron.2023.05.033_bib35","doi-asserted-by":"crossref","first-page":"2363","DOI":"10.1038\/s41380-018-0229-8","article-title":"Modeling amyloid beta and tau pathology in human cerebral organoids","volume":"23","author":"Gonzalez","year":"2018","journal-title":"Mol. Psychiatry"},{"key":"10.1016\/j.neuron.2023.05.033_bib36","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1186\/s40478-018-0557-6","article-title":"Phosphorylation of different tau sites during progression of Alzheimer\u2019s disease","volume":"6","author":"Neddens","year":"2018","journal-title":"Acta Neuropathol. Commun."},{"key":"10.1016\/j.neuron.2023.05.033_bib37","doi-asserted-by":"crossref","DOI":"10.15252\/emmm.202012921","article-title":"Novel tau biomarkers phosphorylated at T181, T217 or T231 rise in the initial stages of the preclinical Alzheimer\u2019s continuum when only subtle changes in Abeta pathology are detected","volume":"12","author":"Su\u00e1rez-Calvet","year":"2020","journal-title":"EMBO Mol. Med."},{"key":"10.1016\/j.neuron.2023.05.033_bib38","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1007\/s004010100423","article-title":"Specific tau phosphorylation sites correlate with severity of neuronal cytopathology in Alzheimer\u2019s disease","volume":"103","author":"Augustinack","year":"2002","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.neuron.2023.05.033_bib39","first-page":"842","article-title":"The prevalence and wide clinical spectrum of the spinocerebellar ataxia type 2 trinucleotide repeat in patients with autosomal dominant cerebellar ataxia","volume":"60","author":"Geschwind","year":"1997","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.neuron.2023.05.033_bib40","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1126\/science.1174447","article-title":"A gene network regulating lysosomal biogenesis and function","volume":"325","author":"Sardiello","year":"2009","journal-title":"Science"},{"key":"10.1016\/j.neuron.2023.05.033_bib41","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.neuroscience.2019.01.010","article-title":"TFEB-mediated enhancement of the autophagy-lysosomal pathway dually modulates the process of amyloid beta-protein generation in neurons","volume":"402","author":"Yamamoto","year":"2019","journal-title":"Neuroscience"},{"key":"10.1016\/j.neuron.2023.05.033_bib42","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1007\/s00401-001-0488-2","article-title":"Cerebellar cortical tau pathology in progressive supranuclear palsy and corticobasal degeneration","volume":"103","author":"Piao","year":"2002","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.neuron.2023.05.033_bib43","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1007\/s00401-019-01970-9","article-title":"Tau drives translational selectivity by interacting with ribosomal proteins","volume":"137","author":"Koren","year":"2019","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.neuron.2023.05.033_bib44","doi-asserted-by":"crossref","first-page":"3000","DOI":"10.1074\/mcp.M115.050724","article-title":"The human tau interactome: binding to the ribonucleoproteome, and impaired binding of the proline-to-leucine mutant at Position 301 (P301L) to chaperones and the proteasome","volume":"14","author":"Gunawardana","year":"2015","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.neuron.2023.05.033_bib45","doi-asserted-by":"crossref","first-page":"1001","DOI":"10.1523\/JNEUROSCI.3029-15.2016","article-title":"Pathological tau promotes neuronal damage by impairing ribosomal function and decreasing protein synthesis","volume":"36","author":"Meier","year":"2016","journal-title":"J.\u00a0Neurosci."},{"key":"10.1016\/j.neuron.2023.05.033_bib46","doi-asserted-by":"crossref","first-page":"5225","DOI":"10.1038\/s41598-020-61777-7","article-title":"Tau protein- induced sequestration of the eukaryotic ribosome: implications in neurodegenerative disease","volume":"10","author":"Banerjee","year":"2020","journal-title":"Sci. Rep."},{"key":"10.1016\/j.neuron.2023.05.033_bib47","doi-asserted-by":"crossref","first-page":"15712","DOI":"10.1073\/pnas.95.26.15712","article-title":"A nucleated assembly mechanism of Alzheimer paired helical filaments","volume":"95","author":"Friedhoff","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.neuron.2023.05.033_bib48","doi-asserted-by":"crossref","first-page":"7025","DOI":"10.1038\/ncomms8025","article-title":"A mechanistic model of tau amyloid aggregation based on direct observation of oligomers","volume":"6","author":"Shammas","year":"2015","journal-title":"Nat. Commun."},{"key":"10.1016\/j.neuron.2023.05.033_bib49","doi-asserted-by":"crossref","first-page":"24978","DOI":"10.1074\/jbc.M501565200","article-title":"Sites of tau important for aggregation populate {beta}-structure and bind to microtubules and polyanions","volume":"280","author":"Mukrasch","year":"2005","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.neuron.2023.05.033_bib50","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1038\/nchem.2889","article-title":"Structure-based inhibitors of tau aggregation","volume":"10","author":"Seidler","year":"2018","journal-title":"Nat. Chem."},{"key":"10.1016\/j.neuron.2023.05.033_bib51","doi-asserted-by":"crossref","first-page":"5129","DOI":"10.1073\/pnas.97.10.5129","article-title":"Assembly of Tau protein into Alzheimer paired helical filaments depends on a local sequence motif ((306)VQIVYK(311)) forming beta structure","volume":"97","author":"von Bergen","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.neuron.2023.05.033_bib52","doi-asserted-by":"crossref","first-page":"48165","DOI":"10.1074\/jbc.M105196200","article-title":"Mutations of Tau protein in frontotemporal dementia promote aggregation of paired helical filaments by enhancing local beta-structure","volume":"276","author":"von Bergen","year":"2001","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.neuron.2023.05.033_bib53","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1016\/j.tig.2011.05.006","article-title":"Biogenesis and function of nuclear bodies","volume":"27","author":"Mao","year":"2011","journal-title":"Trends Genet."},{"key":"10.1016\/j.neuron.2023.05.033_bib54","doi-asserted-by":"crossref","first-page":"803","DOI":"10.1083\/jcb.200512082","article-title":"RNA granules","volume":"172","author":"Anderson","year":"2006","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1016\/j.neuron.2023.05.033_bib55","doi-asserted-by":"crossref","first-page":"101905","DOI":"10.1016\/j.jbc.2022.101905","article-title":"Folding or holding?-Hsp70 and Hsp90 chaperoning of misfolded proteins in neurodegenerative disease","volume":"298","author":"Rutledge","year":"2022","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.neuron.2023.05.033_bib56","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1016\/j.tibs.2021.12.009","article-title":"Chaperoning shape-shifting tau in disease","volume":"47","author":"Ryder","year":"2022","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.neuron.2023.05.033_bib57","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.abc5822","article-title":"Regulation of chaperone function by coupled folding and oligomerization","volume":"6","author":"Mas","year":"2020","journal-title":"Sci. Adv."},{"key":"10.1016\/j.neuron.2023.05.033_bib58","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.35731","article-title":"Oligomerization of a molecular chaperone modulates its activity","volume":"7","author":"Saio","year":"2018","journal-title":"eLife"},{"key":"10.1016\/j.neuron.2023.05.033_bib59","doi-asserted-by":"crossref","first-page":"320","DOI":"10.1074\/mcp.RA118.001044","article-title":"Human stress-inducible Hsp70 has a high propensity to form ATP-dependent antiparallel dimers that are differentially regulated by cochaperone binding","volume":"18","author":"Trcka","year":"2019","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.neuron.2023.05.033_bib60","doi-asserted-by":"crossref","first-page":"81","DOI":"10.3389\/fmolb.2019.00081","article-title":"Oligomerization of Hsp70: current Perspectives on regulation and function","volume":"6","author":"Takakuwa","year":"2019","journal-title":"Front. Mol. Biosci."},{"key":"10.1016\/j.neuron.2023.05.033_bib61","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1016\/j.cell.2020.03.046","article-title":"G3BP1 is a tunable switch that triggers phase separation to assemble stress granules","volume":"181","author":"Yang","year":"2020","journal-title":"Cell"},{"key":"10.1016\/j.neuron.2023.05.033_bib62","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1111\/gtc.12023","article-title":"Both G3BP1 and G3BP2 contribute to stress granule formation","volume":"18","author":"Matsuki","year":"2013","journal-title":"Genes Cells"},{"key":"10.1016\/j.neuron.2023.05.033_bib63","doi-asserted-by":"crossref","first-page":"845","DOI":"10.1083\/jcb.201508028","article-title":"G3BP-Caprin1-USP10 complexes mediate stress granule condensation and associate with 40S subunits","volume":"212","author":"Kedersha","year":"2016","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1016\/j.neuron.2023.05.033_bib64","doi-asserted-by":"crossref","first-page":"712","DOI":"10.1016\/j.cell.2021.12.041","article-title":"Tau interactome maps synaptic and mitochondrial processes associated with neurodegeneration","volume":"185","author":"Tracy","year":"2022","journal-title":"Cell"},{"key":"10.1016\/j.neuron.2023.05.033_bib65","doi-asserted-by":"crossref","first-page":"1946","DOI":"10.1096\/fj.11-199851","article-title":"Identification of oligomers at early stages of tau aggregation in Alzheimer\u2019s disease","volume":"26","author":"Lasagna-Reeves","year":"2012","journal-title":"FASEB J."},{"key":"10.1016\/j.neuron.2023.05.033_bib66","doi-asserted-by":"crossref","first-page":"6","DOI":"10.3390\/biom6010006","article-title":"Tau protein hyperphosphorylation and aggregation in Alzheimer\u2019s disease and other tauopathies, and possible neuroprotective strategies","volume":"6","author":"\u0160imi\u0107","year":"2016","journal-title":"Biomolecules"},{"key":"10.1016\/j.neuron.2023.05.033_bib67","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.neuron.2023.05.033_bib68","doi-asserted-by":"crossref","first-page":"4893","DOI":"10.1007\/s12035-015-9415-8","article-title":"The role of MAPT in neurodegenerative diseases: genetics, mechanisms and therapy","volume":"53","author":"Zhang","year":"2016","journal-title":"Mol. Neurobiol."},{"key":"10.1016\/j.neuron.2023.05.033_bib69","doi-asserted-by":"crossref","first-page":"1341","DOI":"10.1038\/s41591-021-01465-9","article-title":"Tau-targeting antibody therapies: too late, wrong epitope or wrong target?","volume":"27","author":"Jabbari","year":"2021","journal-title":"Nat. Med."},{"key":"10.1016\/j.neuron.2023.05.033_bib70","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1186\/s40478-019-0664-z","article-title":"A walk through tau therapeutic strategies","volume":"7","author":"Jadhav","year":"2019","journal-title":"Acta Neuropathol. Commun."},{"key":"10.1016\/j.neuron.2023.05.033_bib71","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1093\/brain\/awaa373","article-title":"CSF tau microtubule binding region identifies tau tangle and clinical stages of Alzheimer\u2019s disease","volume":"144","author":"Horie","year":"2021","journal-title":"Brain"},{"key":"10.1016\/j.neuron.2023.05.033_bib72","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1186\/s40478-020-0884-2","article-title":"Pre-clinical characterisation of E2814, a high-affinity antibody targeting the microtubule-binding repeat domain of tau for passive immunotherapy in Alzheimer\u2019s disease","volume":"8","author":"Roberts","year":"2020","journal-title":"Acta Neuropathol. Commun."},{"key":"10.1016\/j.neuron.2023.05.033_bib73","doi-asserted-by":"crossref","first-page":"1484","DOI":"10.1016\/j.ymthe.2022.01.009","article-title":"Inhibition of Tau seeding by targeting Tau nucleation core within neurons with a single domain antibody fragment","volume":"30","author":"Danis","year":"2022","journal-title":"Mol. Ther."},{"key":"10.1016\/j.neuron.2023.05.033_bib78","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1002\/(SICI)1097-4547(19970415)48:2<128::AID-JNR5>3.0.CO;2-E","article-title":"Alz-50 and MC-1, a new monoclonal antibody raised to paired helical filaments, recognize conformational epitopes on recombinant tau","volume":"48","author":"Jicha","year":"1997","journal-title":"J.\u00a0Neurosci. Res."},{"key":"10.1016\/j.neuron.2023.05.033_bib77","doi-asserted-by":"crossref","DOI":"10.1093\/nar\/gky1131","article-title":"STRING v11: protein-protein association networks with increased coverage, supporting functional discovery in genome-wide experimental datasets","volume":"47","author":"Szklarczyk","year":"2019","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.neuron.2023.05.033_bib79","doi-asserted-by":"crossref","first-page":"676","DOI":"10.1038\/nmeth.2019","article-title":"Fiji: an open-source platform for biological-image analysis","volume":"9","author":"Schindelin","year":"2012","journal-title":"Nat. Methods"},{"key":"10.1016\/j.neuron.2023.05.033_bib82","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1007\/BF00197809","article-title":"NMRPipe: a multidimensional spectral processing system based on UNIX pipes","volume":"6","author":"Delaglio","year":"1995","journal-title":"J.\u00a0Biomol. NMR"},{"key":"10.1016\/j.neuron.2023.05.033_bib83","doi-asserted-by":"crossref","first-page":"1325","DOI":"10.1093\/bioinformatics\/btu830","article-title":"NMRFAM-SPARKY: enhanced software for biomolecular NMR spectroscopy","volume":"31","author":"Lee","year":"2015","journal-title":"Bioinformatics"},{"key":"10.1016\/j.neuron.2023.05.033_bib74","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1038\/nbt.1529","article-title":"Highly efficient neural conversion of human ES and iPS cells by dual inhibition of SMAD signaling","volume":"27","author":"Chambers","year":"2009","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.neuron.2023.05.033_bib75","doi-asserted-by":"crossref","first-page":"100360","DOI":"10.1016\/j.xcrm.2021.100360","article-title":"Secreted retrovirus-like GAG-domain-containing protein PEG10 is regulated by UBE3A and is involved in Angelman syndrome pathophysiology","volume":"2","author":"Pandya","year":"2021","journal-title":"Cell Rep. Med."},{"key":"10.1016\/j.neuron.2023.05.033_bib76","doi-asserted-by":"crossref","first-page":"9440","DOI":"10.1073\/pnas.1530509100","article-title":"Statistical significance for genomewide studies","volume":"100","author":"Storey","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.neuron.2023.05.033_bib80","doi-asserted-by":"crossref","first-page":"34389","DOI":"10.1074\/jbc.M114.611368","article-title":"Oligomer formation of Tau protein hyperphosphorylated in cells","volume":"289","author":"Tepper","year":"2014","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.neuron.2023.05.033_bib81","doi-asserted-by":"crossref","first-page":"16357","DOI":"10.1073\/pnas.1906839116","article-title":"In\u00a0vitro 0N4R tau fibrils contain a monomorphic beta-sheet core enclosed by dynamically heterogeneous fuzzy coat segments","volume":"116","author":"Dregni","year":"2019","journal-title":"Proc. Natl. Acad. Sci. USA"}],"container-title":["Neuron"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0896627323004348?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0896627323004348?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,12]],"date-time":"2025-10-12T07:45:32Z","timestamp":1760255132000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0896627323004348"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,9]]},"references-count":87,"journal-issue":{"issue":"17","published-print":{"date-parts":[[2023,9]]}},"alternative-id":["S0896627323004348"],"URL":"https:\/\/doi.org\/10.1016\/j.neuron.2023.05.033","relation":{},"ISSN":["0896-6273"],"issn-type":[{"value":"0896-6273","type":"print"}],"subject":[],"published":{"date-parts":[[2023,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Increased G3BP2-Tau interaction in tauopathies is a natural defense against Tau aggregation","name":"articletitle","label":"Article Title"},{"value":"Neuron","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.neuron.2023.05.033","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2023 The Authors. Published by Elsevier Inc.","name":"copyright","label":"Copyright"}]}}