{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,29]],"date-time":"2026-10-29T23:24:04Z","timestamp":1793316244390,"version":"4.5.0"},"reference-count":89,"publisher":"Elsevier BV","issue":"7","license":[{"start":{"date-parts":[[2022,7,1]],"date-time":"2022-07-01T00:00:00Z","timestamp":1656633600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2022,7,1]],"date-time":"2022-07-01T00:00:00Z","timestamp":1656633600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2023,6,9]],"date-time":"2023-06-09T00:00:00Z","timestamp":1686268800000},"content-version":"am","delay-in-days":343,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"},{"start":{"date-parts":[[2022,7,1]],"date-time":"2022-07-01T00:00:00Z","timestamp":1656633600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2022,7,1]],"date-time":"2022-07-01T00:00:00Z","timestamp":1656633600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2022,7,1]],"date-time":"2022-07-01T00:00:00Z","timestamp":1656633600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2022,7,1]],"date-time":"2022-07-01T00:00:00Z","timestamp":1656633600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2022,7,1]],"date-time":"2022-07-01T00:00:00Z","timestamp":1656633600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["RF1 AG061797"],"award-info":[{"award-number":["RF1 AG061797"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["bmn.com","cell.com","clinicalkey.com","clinicalkey.com.au","clinicalkey.es","clinicalkey.fr","clinicalkey.jp","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Trends in Cell Biology"],"published-print":{"date-parts":[[2022,7]]},"DOI":"10.1016\/j.tcb.2022.01.011","type":"journal-article","created":{"date-parts":[[2022,2,15]],"date-time":"2022-02-15T17:18:56Z","timestamp":1644945536000},"page":"611-623","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":227,"title":["Tau liquid\u2013liquid phase separation in neurodegenerative diseases"],"prefix":"10.1016","volume":"32","author":[{"given":"Solomiia","family":"Boyko","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7940-6027","authenticated-orcid":false,"given":"Witold K.","family":"Surewicz","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.tcb.2022.01.011_bb0005","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.tcb.2022.01.011_bb0010","doi-asserted-by":"crossref","first-page":"912","DOI":"10.1038\/s41374-019-0197-x","article-title":"MAPT mutations, tauopathy, and mechanisms of neurodegeneration","volume":"99","author":"Strang","year":"2019","journal-title":"Lab. Investig."},{"key":"10.1016\/j.tcb.2022.01.011_bb0015","doi-asserted-by":"crossref","DOI":"10.1101\/cshperspect.a006247","article-title":"Biochemistry and cell biology of tau protein in neurofibrillary degeneration","volume":"2","author":"Mandelkow","year":"2012","journal-title":"Cold Spring Harb. Perspect. Med."},{"key":"10.1016\/j.tcb.2022.01.011_bb0020","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1038\/nrn.2015.1","article-title":"Tau in physiology and pathology","volume":"17","author":"Wang","year":"2016","journal-title":"Nat. Rev. Neurosci."},{"key":"10.1016\/j.tcb.2022.01.011_bb0025","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":"10.1016\/j.tcb.2022.01.011_bb0030","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1146\/annurev-neuro-072116-031153","article-title":"Propagation of tau aggregates and neurodegeneration","volume":"40","author":"Goedert","year":"2017","journal-title":"Annu. Rev. Neurosci."},{"key":"10.1016\/j.tcb.2022.01.011_bb0035","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1038\/nm.3457","article-title":"Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases","volume":"20","author":"Guo","year":"2014","journal-title":"Nat. Med."},{"key":"10.1016\/j.tcb.2022.01.011_bb0040","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":"10.1016\/j.tcb.2022.01.011_bb0045","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1038\/nrm.2017.7","article-title":"Biomolecular condensates: organizers of cellular biochemistry","volume":"18","author":"Banani","year":"2017","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.tcb.2022.01.011_bb0050","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.tcb.2022.01.011_bb0055","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1016\/j.cis.2016.05.012","article-title":"Protein intrinsic disorder-based liquid-liquid phase transitions in biological systems: complex coacervates and membrane-less organelles","volume":"239","author":"Uversky","year":"2017","journal-title":"Adv. Colloid Interf. Sci."},{"key":"10.1016\/j.tcb.2022.01.011_bb0060","doi-asserted-by":"crossref","first-page":"420","DOI":"10.1016\/j.tcb.2018.02.004","article-title":"Protein phase separation: a new phase in cell biology","volume":"28","author":"Boeynaems","year":"2018","journal-title":"Trends Cell Biol."},{"key":"10.1016\/j.tcb.2022.01.011_bb0065","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.tcb.2022.01.011_bb0070","doi-asserted-by":"crossref","first-page":"1066","DOI":"10.1016\/j.cell.2015.07.047","article-title":"A liquid-to-solid phase transition of the ALS protein FUS accelerated by disease mutation","volume":"162","author":"Patel","year":"2015","journal-title":"Cell"},{"key":"10.1016\/j.tcb.2022.01.011_bb0075","doi-asserted-by":"crossref","first-page":"678","DOI":"10.1016\/j.neuron.2015.10.030","article-title":"ALS\/FTD mutation-induced phase transition of FUS liquid droplets and reversible hydrogels into irreversible hydrogels impairs RNP granule function","volume":"88","author":"Murakami","year":"2015","journal-title":"Neuron"},{"key":"10.1016\/j.tcb.2022.01.011_bb0080","doi-asserted-by":"crossref","first-page":"7160","DOI":"10.1074\/jbc.REV118.001188","article-title":"Matter over mind: liquid phase separation and neurodegeneration","volume":"294","author":"Elbaum-Garfinkle","year":"2019","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tcb.2022.01.011_bb0085","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1016\/j.tins.2019.08.005","article-title":"Physiological, pathological, and targetable membraneless organelles in neurons","volume":"42","author":"Ryan","year":"2019","journal-title":"Trends Neurosci."},{"key":"10.1016\/j.tcb.2022.01.011_bb0090","doi-asserted-by":"crossref","first-page":"272","DOI":"10.1038\/s41582-019-0157-5","article-title":"Bridging biophysics and neurology: aberrant phase transitions in neurodegenerative disease","volume":"15","author":"Nedelsky","year":"2019","journal-title":"Nat. Rev. Neurol."},{"key":"10.1016\/j.tcb.2022.01.011_bb0095","doi-asserted-by":"crossref","first-page":"1910","DOI":"10.1016\/j.jmb.2020.03.004","article-title":"Liquid-liquid phase separation and its mechanistic role in pathological protein aggregation","volume":"432","author":"Babinchak","year":"2020","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.tcb.2022.01.011_bb0100","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/j.devcel.2020.09.014","article-title":"Phase separation and neurodegenerative diseases: a disturbance in the force","volume":"55","author":"Zbinden","year":"2020","journal-title":"Dev. Cell"},{"key":"10.1016\/j.tcb.2022.01.011_bb0105","doi-asserted-by":"crossref","first-page":"2304","DOI":"10.1016\/j.celrep.2017.08.042","article-title":"Local nucleation of microtubule bundles through tubulin concentration into a condensed tau phase","volume":"20","author":"Hernandez-Vega","year":"2017","journal-title":"Cell Rep."},{"key":"10.1016\/j.tcb.2022.01.011_bb0110","doi-asserted-by":"crossref","DOI":"10.15252\/embj.201798049","article-title":"Tau protein liquid-liquid phase separation can initiate tau aggregation","volume":"37","author":"Wegmann","year":"2018","journal-title":"EMBO J."},{"key":"10.1016\/j.tcb.2022.01.011_bb0115","doi-asserted-by":"crossref","first-page":"1360","DOI":"10.3390\/ijms19051360","article-title":"Acetylation disfavors tau phase separation","volume":"19","author":"Ferreon","year":"2018","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.tcb.2022.01.011_bb0120","doi-asserted-by":"crossref","first-page":"11054","DOI":"10.1074\/jbc.AC119.009198","article-title":"Liquid-liquid phase separation of tau protein: the crucial role of electrostatic interactions","volume":"294","author":"Boyko","year":"2019","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tcb.2022.01.011_bb0125","doi-asserted-by":"crossref","first-page":"2809","DOI":"10.1038\/s41467-020-16580-3","article-title":"Liquid-liquid phase separation induces pathogenic tau conformations in vitro","volume":"11","author":"Kanaan","year":"2020","journal-title":"Nat. Commun."},{"key":"10.1016\/j.tcb.2022.01.011_bb0130","doi-asserted-by":"crossref","DOI":"10.1016\/j.jmb.2020.166731","article-title":"Liquid-liquid phase separation of tau driven by hydrophobic interaction facilitates fibrillization of tau","volume":"433","author":"Lin","year":"2021","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.tcb.2022.01.011_bb0135","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1038\/s41467-017-00480-0","article-title":"Liquid-liquid phase separation of the microtubule-binding repeats of the Alzheimer-related protein tau","volume":"8","author":"Ambadipudi","year":"2017","journal-title":"Nat. Commun."},{"key":"10.1016\/j.tcb.2022.01.011_bb0140","doi-asserted-by":"crossref","first-page":"3929","DOI":"10.1021\/acs.jpclett.9b01731","article-title":"Liquid-liquid phase separation is driven by large-scale conformational unwinding and fluctuations of intrinsically disordered protein molecules","volume":"10","author":"Majumdar","year":"2019","journal-title":"J. Phys. Chem. Lett."},{"key":"10.1016\/j.tcb.2022.01.011_bb0145","doi-asserted-by":"crossref","first-page":"6503","DOI":"10.1039\/C9SC00531E","article-title":"Residue-specific identification of phase separation hot spots of Alzheimer's-related protein tau","volume":"10","author":"Ambadipudi","year":"2019","journal-title":"Chem. Sci."},{"key":"10.1016\/j.tcb.2022.01.011_bb0150","doi-asserted-by":"crossref","first-page":"2576","DOI":"10.1021\/acs.jpclett.1c00208","article-title":"Liquid-liquid phase separation of tau protein is encoded at the monomeric level","volume":"12","author":"Dong","year":"2021","journal-title":"J. Phys. Chem. Lett."},{"key":"10.1016\/j.tcb.2022.01.011_bb0155","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pbio.2002183","article-title":"RNA stores tau reversibly in complex coacervates","volume":"15","author":"Zhang","year":"2017","journal-title":"PLoS Biol."},{"key":"10.1016\/j.tcb.2022.01.011_bb0160","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.42571","article-title":"Narrow equilibrium window for complex coacervation of tau and RNA under cellular conditions","volume":"8","author":"Lin","year":"2019","journal-title":"eLife"},{"key":"10.1016\/j.tcb.2022.01.011_bb0165","doi-asserted-by":"crossref","first-page":"11354","DOI":"10.1002\/anie.201703191","article-title":"Reentrant phase transition drives dynamic substructure formation in ribonucleoprotein droplets","volume":"56","author":"Banerjee","year":"2017","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"10.1016\/j.tcb.2022.01.011_bb0170","doi-asserted-by":"crossref","first-page":"2470","DOI":"10.1021\/acs.biochem.8b00001","article-title":"Reentrant phase transitions and non-equilibrium dynamics in membraneless organelles","volume":"57","author":"Milin","year":"2018","journal-title":"Biochemistry"},{"key":"10.1016\/j.tcb.2022.01.011_bb0175","doi-asserted-by":"crossref","first-page":"1393","DOI":"10.1002\/pro.4101","article-title":"Liquid-liquid phase separation of tau by self and complex coacervation","volume":"30","author":"Najafi","year":"2021","journal-title":"Protein Sci."},{"key":"10.1016\/j.tcb.2022.01.011_bb0180","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.tcb.2022.01.011_bb0185","doi-asserted-by":"crossref","first-page":"4209","DOI":"10.1016\/j.molcel.2021.07.038","article-title":"Interaction of tau with HNRNPA2B1 and N(6)-methyladenosine RNA mediates the progression of tauopathy","volume":"81","author":"Jiang","year":"2021","journal-title":"Mol. Cell"},{"key":"10.1016\/j.tcb.2022.01.011_bb0190","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1021\/acschemneuro.9b00627","article-title":"Electrostatically driven complex coacervation and amyloid aggregation of tau are independent processes with overlapping conditions","volume":"11","author":"Lin","year":"2020","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.tcb.2022.01.011_bb0195","doi-asserted-by":"crossref","first-page":"31882","DOI":"10.1073\/pnas.2012460117","article-title":"Regulatory mechanisms of tau protein fibrillation under the conditions of liquid-liquid phase separation","volume":"117","author":"Boyko","year":"2020","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.tcb.2022.01.011_bb0200","doi-asserted-by":"crossref","first-page":"550","DOI":"10.1038\/383550a0","article-title":"Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans","volume":"383","author":"Goedert","year":"1996","journal-title":"Nature"},{"key":"10.1016\/j.tcb.2022.01.011_bb0205","doi-asserted-by":"crossref","first-page":"10098","DOI":"10.1038\/s41598-020-67119-x","article-title":"Cellular polyamines condense hyperphosphorylated tau, triggering Alzheimer's disease","volume":"10","author":"Ivanov","year":"2020","journal-title":"Sci. Rep."},{"key":"10.1016\/j.tcb.2022.01.011_bb0210","doi-asserted-by":"crossref","first-page":"5850","DOI":"10.1074\/jbc.AC120.013166","article-title":"Zinc promotes liquid-liquid phase separation of tau protein","volume":"295","author":"Singh","year":"2020","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tcb.2022.01.011_bb0215","doi-asserted-by":"crossref","first-page":"5574","DOI":"10.1038\/s41467-020-19211-z","article-title":"Small molecules as potent biphasic modulators of protein liquid-liquid phase separation","volume":"11","author":"Babinchak","year":"2020","journal-title":"Nat. Commun."},{"key":"10.1016\/j.tcb.2022.01.011_bb0220","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2021.101222","article-title":"Myricetin slows liquid-liquid phase separation of Tau and activates ATG5-dependent autophagy to suppress tau toxicity","volume":"297","author":"Dai","year":"2021","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tcb.2022.01.011_bb0225","doi-asserted-by":"crossref","first-page":"1989","DOI":"10.1021\/acschemneuro.1c00098","article-title":"C1 inhibits liquid-liquid phase separation and oligomerization of tau and protects neuroblastoma cells against toxic tau oligomers","volume":"12","author":"Pradhan","year":"2021","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.tcb.2022.01.011_bb0230","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2014188118","article-title":"TIA1 potentiates tau phase separation and promotes generation of toxic oligomeric tau","volume":"118","author":"Ash","year":"2021","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.tcb.2022.01.011_bb0235","doi-asserted-by":"crossref","first-page":"1326","DOI":"10.1002\/pro.4025","article-title":"Interplay between tau and alpha-synuclein liquid-liquid phase separation","volume":"30","author":"Siegert","year":"2021","journal-title":"Protein Sci."},{"key":"10.1016\/j.tcb.2022.01.011_bb0240","doi-asserted-by":"crossref","first-page":"1350","DOI":"10.1002\/pro.4060","article-title":"Small heat shock protein 22 kDa can modulate the aggregation and liquid-liquid phase separation behavior of tau","volume":"30","author":"Darling","year":"2021","journal-title":"Protein Sci."},{"key":"10.1016\/j.tcb.2022.01.011_bb0245","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1212\/01.wnl.0000223644.08653.b5","article-title":"Elevated cortical zinc in Alzheimer disease","volume":"67","author":"Religa","year":"2006","journal-title":"Neurology"},{"key":"10.1016\/j.tcb.2022.01.011_bb0250","doi-asserted-by":"crossref","first-page":"2506","DOI":"10.3390\/ijms18122506","article-title":"Zinc signal in brain diseases","volume":"18","author":"Portbury","year":"2017","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.tcb.2022.01.011_bb0255","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1016\/j.cell.2018.12.035","article-title":"Considerations and challenges in studying liquid-liquid phase separation and biomolecular condensates","volume":"176","author":"Alberti","year":"2019","journal-title":"Cell"},{"key":"10.1016\/j.tcb.2022.01.011_bb0260","doi-asserted-by":"crossref","first-page":"726","DOI":"10.1002\/anie.202011157","article-title":"Disease-associated tau phosphorylation hinders tubulin assembly within tau condensates","volume":"60","author":"Savastano","year":"2021","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"10.1016\/j.tcb.2022.01.011_bb0265","article-title":"Tau post-translational modifications: dynamic transformers of tau function, degradation, and aggregation","volume":"11","author":"Alquezar","year":"2020","journal-title":"Front. Neurol."},{"key":"10.1016\/j.tcb.2022.01.011_bb0270","doi-asserted-by":"crossref","first-page":"2909","DOI":"10.1038\/s41467-019-10792-y","article-title":"Lysine\/RNA-interactions drive and regulate biomolecular condensation","volume":"10","author":"Ukmar-Godec","year":"2019","journal-title":"Nat. Commun."},{"key":"10.1016\/j.tcb.2022.01.011_bb0275","doi-asserted-by":"crossref","first-page":"452","DOI":"10.1016\/j.tcb.2019.02.007","article-title":"Tau: it's not what you think","volume":"29","author":"Baas","year":"2019","journal-title":"Trends Cell Biol."},{"key":"10.1016\/j.tcb.2022.01.011_bb0280","doi-asserted-by":"crossref","first-page":"1078","DOI":"10.1038\/s41556-019-0375-5","article-title":"Microtubules gate tau condensation to spatially regulate microtubule functions","volume":"21","author":"Tan","year":"2019","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.tcb.2022.01.011_bb0285","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1126\/science.abb8032","article-title":"Beyond aggregation: pathological phase transitions in neurodegenerative disease","volume":"370","author":"Mathieu","year":"2020","journal-title":"Science"},{"key":"10.1016\/j.tcb.2022.01.011_bb0290","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1007\/BF00296367","article-title":"Abnormal tau proteins in progressive supranuclear palsy. Similarities and differences with the neurofibrillary degeneration of the Alzheimer type","volume":"81","author":"Flament","year":"1991","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.tcb.2022.01.011_bb0295","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1097\/00005072-199602000-00004","article-title":"Specific pathological tau protein variants characterize Pick's disease","volume":"55","author":"Delacourte","year":"1996","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"10.1016\/j.tcb.2022.01.011_bb0300","doi-asserted-by":"crossref","first-page":"9728","DOI":"10.3390\/ijms22189728","article-title":"Tau N-terminal inserts regulate tau liquid-liquid phase separation and condensates maturation in a neuronal cell model","volume":"22","author":"Wu","year":"2021","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.tcb.2022.01.011_bb0305","doi-asserted-by":"crossref","DOI":"10.1083\/jcb.202006054","article-title":"The proline-rich domain promotes tau liquid-liquid phase separation in cells","volume":"219","author":"Zhang","year":"2020","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.tcb.2022.01.011_bb0310","doi-asserted-by":"crossref","first-page":"8270","DOI":"10.1523\/JNEUROSCI.1592-12.2012","article-title":"Contrasting pathology of the stress granule proteins TIA-1 and G3BP in tauopathies","volume":"32","author":"Vanderweyde","year":"2012","journal-title":"J. Neurosci."},{"key":"10.1016\/j.tcb.2022.01.011_bb0315","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.tcb.2022.01.011_bb0320","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 vivo","volume":"21","author":"Apicco","year":"2018","journal-title":"Nat. Neurosci."},{"key":"10.1016\/j.tcb.2022.01.011_bb0325","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.tcb.2022.01.011_bb0330","doi-asserted-by":"crossref","first-page":"30498","DOI":"10.1038\/srep30498","article-title":"Internalized tau sensitizes cells to stress by promoting formation and stability of stress granules","volume":"6","author":"Brunello","year":"2016","journal-title":"Sci. Rep."},{"key":"10.1016\/j.tcb.2022.01.011_bb0335","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1186\/s12915-021-01132-y","article-title":"Pathologic tau conformer ensembles induce dynamic, liquid-liquid phase separation events at the nuclear envelope","volume":"19","author":"Kang","year":"2021","journal-title":"BMC Biol."},{"key":"10.1016\/j.tcb.2022.01.011_bb0340","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1038\/s41586-021-03911-7","article-title":"Structure-based classification of tauopathies","volume":"598","author":"Shi","year":"2021","journal-title":"Nature"},{"key":"10.1016\/j.tcb.2022.01.011_bb0345","doi-asserted-by":"crossref","first-page":"1435","DOI":"10.1038\/s41587-019-0341-6","article-title":"Probing and engineering liquid-phase organelles","volume":"37","author":"Bracha","year":"2019","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.tcb.2022.01.011_bb0350","doi-asserted-by":"crossref","first-page":"801","DOI":"10.1083\/jcb.201112098","article-title":"A promiscuous biotin ligase fusion protein identifies proximal and interacting proteins in mammalian cells","volume":"196","author":"Roux","year":"2012","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.tcb.2022.01.011_bb0355","doi-asserted-by":"crossref","first-page":"1467","DOI":"10.1016\/j.cell.2018.10.048","article-title":"Mapping local and global liquid phase behavior in living cells using photo-oligomerizable seeds","volume":"175","author":"Bracha","year":"2018","journal-title":"Cell"},{"key":"10.1016\/j.tcb.2022.01.011_bb0360","doi-asserted-by":"crossref","first-page":"3243","DOI":"10.1002\/1873-3468.13948","article-title":"The promise and the challenges of cryo-electron tomography","volume":"594","author":"Turk","year":"2020","journal-title":"FEBS Lett."},{"key":"10.1016\/j.tcb.2022.01.011_bb0365","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pbio.1000034","article-title":"Structural polymorphism of 441-residue tau at single residue resolution","volume":"7","author":"Mukrasch","year":"2009","journal-title":"PLoS Biol."},{"key":"10.1016\/j.tcb.2022.01.011_bb0370","doi-asserted-by":"crossref","first-page":"11714","DOI":"10.1021\/bi000850r","article-title":"Structure, microtubule interactions, and paired helical filament aggregation by tau mutants of frontotemporal dementias","volume":"39","author":"Barghorn","year":"2000","journal-title":"Biochemistry"},{"key":"10.1016\/j.tcb.2022.01.011_bb0375","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. Biol. Chem."},{"key":"10.1016\/j.tcb.2022.01.011_bb0380","doi-asserted-by":"crossref","first-page":"8597","DOI":"10.1021\/bi3010818","article-title":"FTDP-17 tau mutations induce distinct effects on aggregation and microtubule interactions","volume":"51","author":"Combs","year":"2012","journal-title":"Biochemistry"},{"key":"10.1016\/j.tcb.2022.01.011_bb0385","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":"10.1016\/j.tcb.2022.01.011_bb0390","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1016\/j.conb.2021.03.003","article-title":"A current view on tau protein phosphorylation in Alzheimer's disease","volume":"69","author":"Wegmann","year":"2021","journal-title":"Curr. Opin. Neurobiol."},{"key":"10.1016\/j.tcb.2022.01.011_bb0395","doi-asserted-by":"crossref","first-page":"3704","DOI":"10.1021\/acs.analchem.5b04509","article-title":"FLEXITau: quantifying post-translational modifications of tau protein in vitro and in human disease","volume":"88","author":"Mair","year":"2016","journal-title":"Anal. Chem."},{"key":"10.1016\/j.tcb.2022.01.011_bb0400","doi-asserted-by":"crossref","first-page":"W329","DOI":"10.1093\/nar\/gky384","article-title":"IUPred2A: context-dependent prediction of protein disorder as a function of redox state and protein binding","volume":"46","author":"Meszaros","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.tcb.2022.01.011_bb0405","doi-asserted-by":"crossref","first-page":"7115","DOI":"10.1074\/jbc.TM118.001192","article-title":"The molecular language of membraneless organelles","volume":"294","author":"Gomes","year":"2019","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tcb.2022.01.011_bb0410","doi-asserted-by":"crossref","first-page":"688","DOI":"10.1016\/j.cell.2018.06.006","article-title":"A molecular grammar governing the driving forces for phase separation of prion-like RNA binding proteins","volume":"174","author":"Wang","year":"2018","journal-title":"Cell"},{"key":"10.1016\/j.tcb.2022.01.011_bb0415","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/j.cell.2015.09.015","article-title":"Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization","volume":"163","author":"Molliex","year":"2015","journal-title":"Cell"},{"key":"10.1016\/j.tcb.2022.01.011_bb0420","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.06807","article-title":"Promiscuous interactions and protein disaggregases determine the material state of stress-inducible RNP granules","volume":"4","author":"Kroschwald","year":"2015","journal-title":"eLife"},{"key":"10.1016\/j.tcb.2022.01.011_bb0425","doi-asserted-by":"crossref","first-page":"829","DOI":"10.1016\/j.cell.2015.10.040","article-title":"The LC domain of hnRNPA2 adopts similar conformations in hydrogel polymers, liquid-like droplets, and nuclei","volume":"163","author":"Xiang","year":"2015","journal-title":"Cell"},{"key":"10.1016\/j.tcb.2022.01.011_bb0430","doi-asserted-by":"crossref","first-page":"753","DOI":"10.1016\/j.cell.2012.04.017","article-title":"Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels","volume":"149","author":"Kato","year":"2012","journal-title":"Cell"},{"key":"10.1016\/j.tcb.2022.01.011_bb0435","doi-asserted-by":"crossref","DOI":"10.1101\/cshperspect.a023598","article-title":"Cross-beta polymerization of low complexity sequence domains","volume":"9","author":"Kato","year":"2017","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"10.1016\/j.tcb.2022.01.011_bb0440","doi-asserted-by":"crossref","first-page":"875","DOI":"10.1083\/jcb.201308087","article-title":"Phase transitions and size scaling of membrane-less organelles","volume":"203","author":"Brangwynne","year":"2013","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.tcb.2022.01.011_bb0445","doi-asserted-by":"crossref","first-page":"1317","DOI":"10.1126\/science.aaw4951","article-title":"Protein condensates as aging Maxwell fluids","volume":"370","author":"Jawerth","year":"2020","journal-title":"Science"}],"container-title":["Trends in Cell Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0962892422000265?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0962892422000265?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,18]],"date-time":"2025-10-18T12:57:56Z","timestamp":1760792276000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0962892422000265"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,7]]},"references-count":89,"journal-issue":{"issue":"7","published-print":{"date-parts":[[2022,7]]}},"alternative-id":["S0962892422000265"],"URL":"https:\/\/doi.org\/10.1016\/j.tcb.2022.01.011","relation":{},"ISSN":["0962-8924"],"issn-type":[{"value":"0962-8924","type":"print"}],"subject":[],"published":{"date-parts":[[2022,7]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Tau liquid\u2013liquid phase separation in neurodegenerative diseases","name":"articletitle","label":"Article Title"},{"value":"Trends in Cell Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.tcb.2022.01.011","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2022 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}