{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,1]],"date-time":"2026-04-01T09:26:25Z","timestamp":1775035585246,"version":"3.50.1"},"publisher-location":"New York, NY","reference-count":15,"publisher":"Springer US","isbn-type":[{"value":"9781071636282","type":"print"},{"value":"9781071636299","type":"electronic"}],"license":[{"start":{"date-parts":[[2024,1,1]],"date-time":"2024-01-01T00:00:00Z","timestamp":1704067200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2024,1,1]],"date-time":"2024-01-01T00:00:00Z","timestamp":1704067200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2024]]},"DOI":"10.1007\/978-1-0716-3629-9_10","type":"book-chapter","created":{"date-parts":[[2024,3,21]],"date-time":"2024-03-21T07:01:51Z","timestamp":1711004511000},"page":"185-192","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Preparation of Tau Condensates by Liquid\u2013Liquid Phase Separation to Study Tau Amyloid Aggregation"],"prefix":"10.1007","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-9902-1885","authenticated-orcid":false,"given":"Yanxian","family":"Lin","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2024,3,22]]},"reference":[{"key":"10_CR1","doi-asserted-by":"publisher","first-page":"899","DOI":"10.1038\/nphys3532","volume":"11","author":"CP Brangwynne","year":"2015","unstructured":"Brangwynne CP, Tompa P, Pappu RV (2015) Polymer physics of intracellular phase transitions. Nat Phys 11:899\u2013904. https:\/\/doi.org\/10.1038\/nphys3532","journal-title":"Nat Phys"},{"key":"10_CR2","doi-asserted-by":"publisher","first-page":"39","DOI":"10.1146\/annurev-cellbio-100913-013325","volume":"30","author":"AA Hyman","year":"2014","unstructured":"Hyman AA, Weber CA, J\u00fclicher F (2014) Liquid-liquid phase separation in biology. Annu Rev Cell Dev Biol 30:39\u201358. https:\/\/doi.org\/10.1146\/annurev-cellbio-100913-013325","journal-title":"Annu Rev Cell Dev Biol"},{"key":"10_CR3","doi-asserted-by":"publisher","first-page":"1910","DOI":"10.1016\/j.jmb.2020.03.004","volume":"432","author":"WM Babinchak","year":"2020","unstructured":"Babinchak WM, Surewicz WK (2020) Liquid-liquid phase separation and its mechanistic role in pathological protein aggregation. J Mol Biol 432:1910\u20131925. https:\/\/doi.org\/10.1016\/j.jmb.2020.03.004","journal-title":"J Mol Biol"},{"key":"10_CR4","doi-asserted-by":"publisher","first-page":"38a","DOI":"10.1016\/j.bpj.2015.11.272","volume":"110","author":"S Elbaum-Garfinkle","year":"2016","unstructured":"Elbaum-Garfinkle S, Taylor N, Brangwynne CP (2016) From physiological fluids to pathological gels: disordered proteins at the nexus of liquid phase separation and neurodegenerative disease. Biophys J 110:38a. https:\/\/doi.org\/10.1016\/j.bpj.2015.11.272","journal-title":"Biophys J"},{"key":"10_CR5","doi-asserted-by":"publisher","first-page":"123","DOI":"10.1016\/j.cell.2015.09.015","volume":"163","author":"A Molliex","year":"2015","unstructured":"Molliex A, Temirov J, Lee J, Coughlin M, Kanagaraj AP, Kim HJ, Mittag T, Taylor JP (2015) Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization. Cell 163:123\u2013133. https:\/\/doi.org\/10.1016\/j.cell.2015.09.015","journal-title":"Cell"},{"key":"10_CR6","doi-asserted-by":"publisher","first-page":"3696","DOI":"10.1074\/jbc.RA118.006351","volume":"294","author":"Y Chen","year":"2019","unstructured":"Chen Y, Cohen TJ (2019) Aggregation of the nucleic acid\u2013binding protein TDP-43 occurs via distinct routes that are coordinated with stress granule formation. J Biol Chem 294:3696\u20133706. https:\/\/doi.org\/10.1074\/jbc.RA118.006351","journal-title":"J Biol Chem"},{"key":"10_CR7","doi-asserted-by":"publisher","first-page":"1326","DOI":"10.1002\/pro.4025","volume":"30","author":"A Siegert","year":"2021","unstructured":"Siegert A, Rankovic M, Favretto F, Ukmar-Godec T, Stroh\u00e4ker T, Becker S, Zweckstetter M (2021) Interplay between tau and \u03b1-synuclein liquid\u2013liquid phase separation. Protein Sci 30:1326\u20131336. https:\/\/doi.org\/10.1002\/pro.4025","journal-title":"Protein Sci"},{"key":"10_CR8","doi-asserted-by":"publisher","first-page":"275","DOI":"10.1038\/s41467-017-00480-0","volume":"8","author":"S Ambadipudi","year":"2017","unstructured":"Ambadipudi S, Biernat J, Riedel D, Mandelkow E, Zweckstetter M (2017) Liquid\u2013liquid phase separation of the microtubule-binding repeats of the Alzheimer-related protein tau. Nat Commun 8:275. https:\/\/doi.org\/10.1038\/s41467-017-00480-0","journal-title":"Nat Commun"},{"key":"10_CR9","doi-asserted-by":"publisher","first-page":"e98049","DOI":"10.15252\/embj.201798049","volume":"37","author":"S Wegmann","year":"2018","unstructured":"Wegmann S, Eftekharzadeh B, Tepper K, Zoltowska KM, Bennett RE, Dujardin S, Laskowski PR, MacKenzie D, Kamath T, Commins C, Vanderburg C, Roe AD, Fan Z, Molliex AM, Hernandez-Vega A, Muller D, Hyman AA, Mandelkow E, Taylor JP, Hyman BT (2018) Tau protein liquid\u2013liquid phase separation can initiate tau aggregation. EMBO J 37:e98049. https:\/\/doi.org\/10.15252\/embj.201798049","journal-title":"EMBO J"},{"key":"10_CR10","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pbio.2002183","volume":"15","author":"X Zhang","year":"2017","unstructured":"Zhang X, Lin Y, Eschmann NA, Zhou H, Rauch JN, Hernandez I, Guzman E, Kosik KS, Han S (2017) RNA stores tau reversibly in complex coacervates. PLoS Biol 15:e2002183. https:\/\/doi.org\/10.1371\/journal.pbio.2002183","journal-title":"PLoS Biol"},{"key":"10_CR11","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.42571","volume":"8","author":"Y Lin","year":"2019","unstructured":"Lin Y, McCarty J, Rauch JN, Delaney KT, Kosik KS, Fredrickson GH, Shea J-E, Han S (2019) Narrow equilibrium window for complex coacervation of tau and RNA under cellular conditions. eLife 8:e42571. https:\/\/doi.org\/10.7554\/eLife.42571","journal-title":"eLife"},{"key":"10_CR12","doi-asserted-by":"publisher","first-page":"615","DOI":"10.1021\/acschemneuro.9b00627","volume":"11","author":"Y Lin","year":"2020","unstructured":"Lin Y, Fichou Y, Zeng Z, Hu NY, Han S (2020) Electrostatically driven complex coacervation and amyloid aggregation of tau are independent processes with overlapping conditions. ACS Chem Neurosci 11:615\u2013627. https:\/\/doi.org\/10.1021\/acschemneuro.9b00627","journal-title":"ACS Chem Neurosci"},{"key":"10_CR13","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmb.2020.166731","volume":"433","author":"Y Lin","year":"2021","unstructured":"Lin Y, Fichou Y, Longhini AP, Llanes LC, Yin P, Bazan GC, Kosik KS, Han S (2021) Liquid-liquid phase separation of tau driven by hydrophobic interaction facilitates fibrillization of tau. J Mol Biol 433:166731. https:\/\/doi.org\/10.1016\/j.jmb.2020.166731","journal-title":"J Mol Biol"},{"key":"10_CR14","doi-asserted-by":"publisher","first-page":"11054","DOI":"10.1074\/jbc.AC119.009198","volume":"294","author":"S Boyko","year":"2019","unstructured":"Boyko S, Qi X, Chen T-H, Surewicz K, Surewicz WK (2019) Liquid\u2013liquid phase separation of tau protein: the crucial role of electrostatic interactions. J Biol Chem 294:11054\u201311059. https:\/\/doi.org\/10.1074\/jbc.AC119.009198","journal-title":"J Biol Chem"},{"key":"10_CR15","doi-asserted-by":"publisher","first-page":"238","DOI":"10.1016\/j.brainresbull.2016.08.018","volume":"126","author":"T Arendt","year":"2016","unstructured":"Arendt T, Stieler JT, Holzer M (2016) Tau and tauopathies. Brain Res Bull 126:238\u2013292. https:\/\/doi.org\/10.1016\/j.brainresbull.2016.08.018","journal-title":"Brain Res Bull"}],"container-title":["Methods in Molecular Biology","Tau Protein"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/978-1-0716-3629-9_10","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,3,21]],"date-time":"2024-03-21T07:02:36Z","timestamp":1711004556000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/978-1-0716-3629-9_10"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024]]},"ISBN":["9781071636282","9781071636299"],"references-count":15,"URL":"https:\/\/doi.org\/10.1007\/978-1-0716-3629-9_10","relation":{},"ISSN":["1064-3745","1940-6029"],"issn-type":[{"value":"1064-3745","type":"print"},{"value":"1940-6029","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024]]},"assertion":[{"value":"22 March 2024","order":1,"name":"first_online","label":"First Online","group":{"name":"ChapterHistory","label":"Chapter History"}}]}}