{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T01:33:12Z","timestamp":1790472792036,"version":"4.1.0"},"publisher-location":"Singapore","reference-count":107,"publisher":"Springer Singapore","isbn-type":[{"value":"9789813293571","type":"print"},{"value":"9789813293588","type":"electronic"}],"license":[{"start":{"date-parts":[[2019,1,1]],"date-time":"2019-01-01T00:00:00Z","timestamp":1546300800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2019]]},"DOI":"10.1007\/978-981-32-9358-8_25","type":"book-chapter","created":{"date-parts":[[2020,2,24]],"date-time":"2020-02-24T17:08:40Z","timestamp":1582564120000},"page":"341-357","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":28,"title":["Liquid-Liquid Phase Separation of Tau Protein in Neurobiology and Pathology"],"prefix":"10.1007","author":[{"given":"Susanne","family":"Wegmann","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2020,2,25]]},"reference":[{"issue":"2","key":"25_CR1","doi-asserted-by":"publisher","first-page":"399","DOI":"10.1371\/journal.pbio.1000034","volume":"7","author":"MD Mukrasch","year":"2009","unstructured":"Mukrasch MD, Bibow S, Korukottu J, Jeganathan S, Biernat J, Griesinger C, et al. Structural polymorphism of 441-residue Tau at single residue resolution. PLoS Biol. 2009;7(2):399\u2013414.","journal-title":"PLoS Biol"},{"issue":"46","key":"25_CR2","doi-asserted-by":"publisher","first-page":"32066","DOI":"10.1074\/jbc.M805300200","volume":"283","author":"S Jeganathan","year":"2008","unstructured":"Jeganathan S, Hascher A, Chinnathambi S, Biernat J, Mandelkow EM, Mandelkow E. Proline-directed pseudo-phosphorylation at AT8 and PHF1 epitopes induces a compaction of the paperclip folding of tau and generates a pathological (MC-1) conformation. J Biol Chem. 2008;283(46):32066\u201376.","journal-title":"J Biol Chem"},{"issue":"23","key":"25_CR3","doi-asserted-by":"publisher","first-page":"4191","DOI":"10.2174\/1381612811319230005","volume":"19","author":"VN Uversky","year":"2013","unstructured":"Uversky VN. Intrinsic disorder-based protein interactions and their modulators. Curr Pharm Des. 2013;19(23):4191\u2013213.","journal-title":"Curr Pharm Des"},{"issue":"32","key":"25_CR4","doi-asserted-by":"publisher","first-page":"9511","DOI":"10.1021\/bi00198a017","volume":"33","author":"N Gustke","year":"1994","unstructured":"Gustke N, Trinczek B, Biernat J, Mandelkow EM, Mandelkow E. Domains of tau protein and interactions with microtubules. Biochemistry. 1994;33(32):9511\u201322.","journal-title":"Biochemistry"},{"issue":"22","key":"25_CR5","doi-asserted-by":"publisher","first-page":"3541","DOI":"10.1091\/mbc.e14-06-1099","volume":"25","author":"D Janning","year":"2014","unstructured":"Janning D, Igaev M, Sundermann F, Bruhmann J, Beutel O, Heinisch JJ, et al. Single-molecule tracking of tau reveals fast kiss-and-hop interaction with microtubules in living neurons. Mol Biol Cell. 2014;25(22):3541\u201351.","journal-title":"Mol Biol Cell"},{"issue":"24","key":"25_CR6","doi-asserted-by":"publisher","first-page":"7501","DOI":"10.1073\/pnas.1504081112","volume":"112","author":"H Kadavath","year":"2015","unstructured":"Kadavath H, Hofele RV, Biernat J, Kumar S, Tepper K, Urlaub H, et al. Tau stabilizes microtubules by binding at the interface between tubulin heterodimers. Proc Natl Acad Sci. 2015;112(24):7501\u20136.","journal-title":"Proc Natl Acad Sci"},{"key":"25_CR7","doi-asserted-by":"publisher","first-page":"9964","DOI":"10.1038\/srep09964","volume":"5","author":"A Elie","year":"2015","unstructured":"Elie A, Prezel E, Gu\u00e9rin C, Denarier E, Ramirez-Rios S, Serre L, et al. Tau co-organizes dynamic microtubule and actin networks. Sci Rep. 2015;5:9964.","journal-title":"Sci Rep"},{"issue":"1","key":"25_CR8","doi-asserted-by":"publisher","first-page":"1981","DOI":"10.1038\/s41467-017-02230-8","volume":"8","author":"Y Cabrales Fontela","year":"2017","unstructured":"Cabrales Fontela Y, Kadavath H, Biernat J, Riedel D, Mandelkow E, Zweckstetter M. Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau. Nat Commun. 2017;8(1):1981.","journal-title":"Nat Commun"},{"issue":"11","key":"25_CR9","doi-asserted-by":"publisher","first-page":"2722","DOI":"10.1016\/j.bpj.2010.03.013","volume":"98","author":"S Elbaum-Garfinkle","year":"2010","unstructured":"Elbaum-Garfinkle S, Ramlall T, Rhoades E. The role of the lipid bilayer in tau aggregation. Biophys J. 2010;98(11):2722\u201330.","journal-title":"Biophys J"},{"issue":"5","key":"25_CR10","doi-asserted-by":"publisher","first-page":"3271","DOI":"10.1021\/acs.nanolett.8b01085","volume":"18","author":"SA Mari","year":"2018","unstructured":"Mari SA, Wegmann S, Tepper K, Hyman BT, Mandelkow EM, Mandelkow E, et al. Reversible cation-selective attachment and self-assembly of human tau on supported brain lipid membranes. Nano Lett. 2018;18(5):3271\u201381.","journal-title":"Nano Lett"},{"issue":"5","key":"25_CR11","doi-asserted-by":"publisher","first-page":"1327","DOI":"10.1083\/jcb.131.5.1327","volume":"131","author":"R Brandt","year":"1995","unstructured":"Brandt R, L\u00e9ger J, Lee G. Interaction of tau with the neural plasma membrane mediated by tau\u2019s amino-terminal projection domain. J Cell Biol. 1995;131(5):1327\u201340.","journal-title":"J Cell Biol"},{"issue":"16","key":"25_CR12","doi-asserted-by":"publisher","first-page":"2927","DOI":"10.1111\/j.1742-4658.2011.08218.x","volume":"278","author":"A Usardi","year":"2011","unstructured":"Usardi A, Pooler AM, Seereeram A, Reynolds CH, Derkinderen P, Anderton B, et al. Tyrosine phosphorylation of tau regulates its interactions with Fyn SH2 domains, but not SH3 domains, altering the cellular localization of tau. FEBS J. 2011;278(16):2927\u201337.","journal-title":"FEBS J"},{"issue":"26","key":"25_CR13","doi-asserted-by":"publisher","first-page":"18177","DOI":"10.1074\/jbc.M709715200","volume":"283","author":"CH Reynolds","year":"2008","unstructured":"Reynolds CH, Garwood CJ, Wray S, Price C, Kellie S, Perera T, et al. Phosphorylation regulates tau interactions with Src homology 3 domains of phosphatidylinositol 3-kinase, phospholipase C\u03b31, Grb2, and Src family kinases. J Biol Chem. 2008;283(26):18177\u201386.","journal-title":"J Biol Chem"},{"issue":"5","key":"25_CR14","doi-asserted-by":"publisher","first-page":"925","DOI":"10.1016\/j.neuron.2018.07.039","volume":"99","author":"B Eftekharzadeh","year":"2018","unstructured":"Eftekharzadeh B, Daigle JG, Kapinos LE, Dujardin S, Coyne A, Miller SJ, et al. Tau protein disrupts nucleocytoplasmic transport in Alzheimer\u2019s disease. Neuron. 2018;99(5):925\u2013940.e7.","journal-title":"Neuron"},{"issue":"4","key":"25_CR15","doi-asserted-by":"publisher","first-page":"389","DOI":"10.1007\/s00401-010-0658-1","volume":"119","author":"GG Kovacs","year":"2010","unstructured":"Kovacs GG, Botond G, Budka H. Protein coding of neurodegenerative dementias: the neuropathological basis of biomarker diagnostics. Acta Neuropathol. 2010;119(4):389\u2013408.","journal-title":"Acta Neuropathol"},{"issue":"Pt 1","key":"25_CR16","doi-asserted-by":"publisher","first-page":"43","DOI":"10.1093\/brain\/aws307","volume":"136","author":"AC McKee","year":"2013","unstructured":"McKee AC, Stein TD, Nowinski CJ, Stern RA, Daneshvar DH, Alvarez VE, et al. The spectrum of disease in chronic traumatic encephalopathy. Brain. 2013;136(Pt 1):43\u201364.","journal-title":"Brain"},{"key":"25_CR17","volume-title":"Prions and diseases","author":"GG Kovacs","year":"2012","unstructured":"Kovacs GG, Budka H. The spectrum of tau pathology in human prion disease. In: Zou WQ, Gambetti P, editors. Prions and diseases. 1st ed. New York: Springer; 2012.","edition":"1"},{"key":"25_CR18","doi-asserted-by":"publisher","first-page":"101","DOI":"10.1007\/978-1-4939-2978-8_7","volume":"1345","author":"CJ Huseby","year":"2015","unstructured":"Huseby CJ, Kuret J. Analyzing Tau aggregation with electron microscopy. Methods Mol Biol. 2015;1345:101\u201312.","journal-title":"Methods Mol Biol"},{"issue":"35","key":"25_CR19","doi-asserted-by":"publisher","first-page":"27302","DOI":"10.1074\/jbc.M110.145318","volume":"285","author":"S Wegmann","year":"2010","unstructured":"Wegmann S, Yu JJ, Chinnathambi S, Mandelkow EM, Mandelkow E, Muller DJ. Human tau isoforms assemble into ribbon-like fibrils that display polymorphic structure and stability. J Biol Chem. 2010;285(35):27302\u201313.","journal-title":"J Biol Chem"},{"issue":"7662","key":"25_CR20","doi-asserted-by":"publisher","first-page":"185","DOI":"10.1038\/nature23002","volume":"547","author":"AWP Fitzpatrick","year":"2017","unstructured":"Fitzpatrick AWP, Falcon B, He S, Murzin AG, Murshudov G, Garringer HJ, et al. Cryo-EM structures of tau filaments from Alzheimer\u2019s disease. Nature. 2017;547(7662):185\u201390.","journal-title":"Nature"},{"issue":"5","key":"25_CR21","doi-asserted-by":"publisher","first-page":"699","DOI":"10.1007\/s00401-018-1914-z","volume":"136","author":"B Falcon","year":"2018","unstructured":"Falcon B, Zhang W, Schweighauser M, Murzin AG, Vidal R, Garringer HJ, et al. Tau filaments from multiple cases of sporadic and inherited Alzheimer\u2019s disease adopt a common fold. Acta Neuropathol. 2018;136(5):699\u2013708.","journal-title":"Acta Neuropathol"},{"issue":"5","key":"25_CR22","doi-asserted-by":"publisher","first-page":"1946","DOI":"10.1096\/fj.11-199851","volume":"26","author":"CA Lasagna-Reeves","year":"2012","unstructured":"Lasagna-Reeves CA, Castillo-Carranza DL, Sengupta U, Sarmiento J, Troncoso J, Jackson GR, et al. Identification of oligomers at early stages of tau aggregation in Alzheimer\u2019s disease. FASEB J. 2012;26(5):1946\u201359.","journal-title":"FASEB J"},{"issue":"4","key":"25_CR23","doi-asserted-by":"publisher","first-page":"667","DOI":"10.1042\/BST20120134","volume":"40","author":"SM Ward","year":"2012","unstructured":"Ward SM, Himmelstein DS, Lancia JK, Binder LI. Tau oligomers and tau toxicity in neurodegenerative disease. Biochem Soc Trans. 2012;40(4):667\u201371.","journal-title":"Biochem Soc Trans"},{"issue":"11","key":"25_CR24","doi-asserted-by":"publisher","first-page":"1270","DOI":"10.1016\/j.jalz.2017.04.002","volume":"13","author":"S Kaniyappan","year":"2017","unstructured":"Kaniyappan S, Chandupatla RR, Mandelkow EM, Mandelkow E. Extracellular low-n oligomers of tau cause selective synaptotoxicity without affecting cell viability. Alzheimers Dement. 2017;13(11):1270\u201391.","journal-title":"Alzheimers Dement"},{"key":"25_CR25","doi-asserted-by":"publisher","first-page":"39","DOI":"10.1186\/1750-1326-6-39","volume":"6","author":"CA Lasagna-Reeves","year":"2011","unstructured":"Lasagna-Reeves CA, Castillo-Carranza DL, Sengupta U, Clos AL, Jackson GR, Kayed R. Tau oligomers impair memory and induce synaptic and mitochondrial dysfunction in wild-type mice. Mol Neurodegener. 2011;6:39.","journal-title":"Mol Neurodegener"},{"issue":"49","key":"25_CR26","doi-asserted-by":"publisher","first-page":"34389","DOI":"10.1074\/jbc.M114.611368","volume":"289","author":"K Tepper","year":"2014","unstructured":"Tepper K, Biernat J, Kumar S, Wegmann S, Timm T, H\u00fcbschmann S, et al. Oligomer formation of tau protein hyperphosphorylated in cells. J Biol Chem. 2014;289(49):34389\u2013407.","journal-title":"J Biol Chem"},{"issue":"7","key":"25_CR27","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, et al. RNA stores tau reversibly in complex coacervates. PLoS Biol. 2017;15(7):e2002183.","journal-title":"PLoS Biol"},{"issue":"1","key":"25_CR28","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. Liquid-liquid phase separation of the microtubule-binding repeats of the Alzheimer-related protein Tau. Nat Commun. 2017;8(1):275.","journal-title":"Nat Commun"},{"issue":"10","key":"25_CR29","doi-asserted-by":"publisher","first-page":"2304","DOI":"10.1016\/j.celrep.2017.08.042","volume":"20","author":"A Hern\u00e1ndez-Vega","year":"2017","unstructured":"Hern\u00e1ndez-Vega A, Braun M, Scharrel L, Jahnel M, Wegmann S, Hyman BT, et al. Local nucleation of microtubule bundles through tubulin concentration into a condensed tau phase. Cell Rep. 2017;20(10):2304\u201312.","journal-title":"Cell Rep"},{"issue":"7","key":"25_CR30","doi-asserted-by":"publisher","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, et al. Tau protein liquid\u2013liquid phase separation can initiate tau aggregation. EMBO J. 2018;37(7):pii: e98049.","journal-title":"EMBO J"},{"key":"25_CR31","unstructured":"Brangwynne CP, Eckmann CR, Courson DS, Rybarska A, Hoege C, Gharakhani J, et al. Germline P granules are liquid droplets that localize by controlled dissolution\/condensation. 2009;Science (80-), 324(5935):1729\u201332. Available from: \nhttp:\/\/www.sciencemag.org\/cgi\/doi\/10.1126\/science.1172046"},{"issue":"5","key":"25_CR32","doi-asserted-by":"publisher","first-page":"936","DOI":"10.1016\/j.molcel.2015.01.013","volume":"57","author":"TJ Nott","year":"2015","unstructured":"Nott TJ, Petsalaki E, Farber P, Jervis D, Fussner E, Plochowietz A, et al. Phase transition of a disordered nuage protein generates environmentally responsive membraneless organelles. Mol Cell. 2015;57(5):936\u201347.","journal-title":"Mol Cell"},{"issue":"1","key":"25_CR33","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. Liquid-liquid phase separation in biology. Annu Rev Cell Dev Biol. 2014;30(1):39\u201358. Available from: \nhttp:\/\/www.annualreviews.org\/doi\/abs\/10.1146\/annurev-cellbio-100913-013325","journal-title":"Annu Rev Cell Dev Biol"},{"issue":"9","key":"25_CR34","doi-asserted-by":"publisher","first-page":"668","DOI":"10.1016\/j.tcb.2016.05.004","volume":"26","author":"DSW Protter","year":"2016","unstructured":"Protter DSW, Parker R. Principles and properties of stress granules. Trends Cell Biol. 2016;26(9):668\u201379.","journal-title":"Trends Cell Biol"},{"key":"25_CR35","doi-asserted-by":"publisher","first-page":"pii:e18413","DOI":"10.7554\/eLife.18413","volume":"5","author":"JR Wheeler","year":"2016","unstructured":"Wheeler JR, Matheny T, Jain S, Abrisch R, Parker R. Distinct stages in stress granule assembly and disassembly. Elife. 2016;5:pii:e18413.","journal-title":"Elife"},{"issue":"5","key":"25_CR36","doi-asserted-by":"publisher","first-page":"1066","DOI":"10.1016\/j.cell.2015.07.047","volume":"162","author":"A Patel","year":"2015","unstructured":"Patel A, Lee HO, Jawerth L, Maharana S, Jahnel M, Hein MY, et al. A liquid-to-solid phase transition of the ALS protein FUS accelerated by disease mutation. Cell. 2015;162(5):1066\u201377.","journal-title":"Cell"},{"issue":"3","key":"25_CR37","doi-asserted-by":"publisher","first-page":"706\u2013719.e13","DOI":"10.1016\/j.cell.2018.03.004","volume":"173","author":"M Hofweber","year":"2018","unstructured":"Hofweber M, Hutten S, Bourgeois B, Spreitzer E, Niedner-Boblenz A, Schifferer M, et al. Phase separation of FUS is suppressed by its nuclear import receptor and arginine methylation. Cell. 2018;173(3):706\u2013719.e13.","journal-title":"Cell"},{"issue":"1","key":"25_CR38","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, et al. Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization. Cell. 2015;163(1):123\u201333.","journal-title":"Cell"},{"issue":"9","key":"25_CR39","doi-asserted-by":"publisher","first-page":"1537","DOI":"10.1016\/j.str.2016.07.007","volume":"24","author":"AE Conicella","year":"2016","unstructured":"Conicella AE, Zerze GH, Mittal J, Fawzi NL. ALS mutations disrupt phase separation mediated by \u03b1-helical structure in the TDP-43 low-complexity C-terminal domain. Structure. 2016;24(9):1537\u201349.","journal-title":"Structure"},{"issue":"3","key":"25_CR40","doi-asserted-by":"publisher","first-page":"774-788.e17","DOI":"10.1016\/j.cell.2016.10.002","volume":"167","author":"Kyung-Ha Lee","year":"2016","unstructured":"Lee KH, Zhang P, Kim HJ, Mitrea DM, Sarkar M, Freibaum BD, et al. C9orf72 dipeptide repeats impair the assembly, dynamics, and function of membrane-less organelles. Cell. 2016;167(3):774\u2013788.e17. Available from: \nhttp:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0092867416313836","journal-title":"Cell"},{"issue":"6","key":"25_CR41","doi-asserted-by":"publisher","first-page":"1044","DOI":"10.1016\/j.molcel.2017.02.013","volume":"65","author":"S Boeynaems","year":"2017","unstructured":"Boeynaems S, Bogaert E, Kovacs D, Konijnenberg A, Timmerman E, Volkov A, et al. Phase separation of C9orf72 dipeptide repeats perturbs stress granule dynamics. Mol Cell. 2017;65(6):1044\u20131055.e5.","journal-title":"Mol Cell"},{"issue":"5","key":"25_CR42","doi-asserted-by":"publisher","first-page":"1163","DOI":"10.1016\/j.cell.2016.07.008","volume":"166","author":"M Zeng","year":"2016","unstructured":"Zeng M, Shang Y, Araki Y, Guo T, Huganir RL, Zhang M. Phase transition in postsynaptic densities underlies formation of synaptic complexes and synaptic plasticity. Cell. 2016;166(5):1163\u20131175.e12.","journal-title":"Cell"},{"issue":"6402","key":"25_CR43","doi-asserted-by":"publisher","first-page":"604","DOI":"10.1126\/science.aat5671","volume":"361","author":"D Milovanovic","year":"2018","unstructured":"Milovanovic D, Wu Y, Bian X, De Camilli P. A liquid phase of synapsin and lipid vesicles. Science (80-). 2018;361(6402):604\u20137.","journal-title":"Science (80-)"},{"issue":"1","key":"25_CR44","doi-asserted-by":"publisher","first-page":"19","DOI":"10.1016\/j.molcel.2018.08.027","volume":"72","author":"JJ Bouchard","year":"2018","unstructured":"Bouchard JJ, Otero JH, Scott DC, Szulc E, Martin EW, Sabri N, et al. Cancer mutations of the tumor suppressor SPOP disrupt the formation of active, phase-separated compartments. Mol Cell. 2018;72(1):19\u201336.e8.","journal-title":"Mol Cell"},{"issue":"38","key":"25_CR45","doi-asserted-by":"publisher","first-page":"E5237","DOI":"10.1073\/pnas.1509317112","volume":"112","author":"Joel Berry","year":"2015","unstructured":"Berry J, Weber SC, Vaidya N, Haataja M, Brangwynne CP. RNA transcription modulates phase transition-driven nuclear body assembly. Proc Natl Acad Sci U S A. 2015;112(38):E5237\u201345. Available from: \nhttp:\/\/www.pnas.org\/content\/112\/38\/E5237.full","journal-title":"Proceedings of the National Academy of Sciences"},{"issue":"4","key":"25_CR46","doi-asserted-by":"publisher","first-page":"529","DOI":"10.1083\/jcb.201504117","volume":"210","author":"S Hennig","year":"2015","unstructured":"Hennig S, Kong G, Mannen T, Sadowska A, Kobelke S, Blythe A, et al. Prion-like domains in RNA binding proteins are essential for building subnuclear paraspeckles. J Cell Biol. 2015;210(4):529\u201339.","journal-title":"J Cell Biol"},{"issue":"7662","key":"25_CR47","doi-asserted-by":"publisher","first-page":"236","DOI":"10.1038\/nature22822","volume":"547","author":"AG Larson","year":"2017","unstructured":"Larson AG, Elnatan D, Keenen MM, Trnka MJ, Johnston JB, Burlingame AL, et al. Liquid droplet formation by HP1\u03b1 suggests a role for phase separation in heterochromatin. Nature. 2017;547(7662):236\u201340.","journal-title":"Nature"},{"issue":"1","key":"25_CR48","doi-asserted-by":"publisher","first-page":"108","DOI":"10.1016\/j.cell.2015.08.010","volume":"163","author":"H Jiang","year":"2015","unstructured":"Jiang H, Wang S, Huang Y, He X, Cui H, Zhu X, et al. Phase transition of spindle-associated protein regulate spindle apparatus assembly. Cell. 2015;163(1):108\u201322.","journal-title":"Cell"},{"issue":"11","key":"25_CR49","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. Polymer physics of intracellular phase transitions. Nat Phys. 2015;11(11):899\u2013904.","journal-title":"Nat Phys"},{"issue":"3","key":"25_CR50","doi-asserted-by":"publisher","first-page":"688","DOI":"10.1016\/j.cell.2018.06.006","volume":"174","author":"J Wang","year":"2018","unstructured":"Wang J, Choi JM, Holehouse AS, Lee HO, Zhang X, Jahnel M, et al. A molecular grammar governing the driving forces for phase separation of prion-like RNA binding proteins. Cell. 2018;174(3):688\u2013699.e16.","journal-title":"Cell"},{"issue":"4","key":"25_CR51","doi-asserted-by":"publisher","first-page":"678","DOI":"10.1016\/j.neuron.2015.10.030","volume":"88","author":"T Murakami","year":"2015","unstructured":"Murakami T, Qamar S, Lin JQ, Schierle GSK, Rees E, Miyashita A, et al. ALS\/FTD mutation-induced phase transition of fus liquid droplets and reversible hydrogels into irreversible hydrogels impairs RNP granule function. Neuron. 2015;88(4):678\u201390.","journal-title":"Neuron"},{"issue":"20","key":"25_CR52","doi-asserted-by":"publisher","first-page":"2951","DOI":"10.15252\/embj.201696394","volume":"36","author":"Zachary Monahan","year":"2017","unstructured":"Monahan Z, Ryan VH, Janke AM, Burke KA, Rhoads SN, Zerze GH, et al. Phosphorylation of the FUS low-complexity domain disrupts phase separation, aggregation, and toxicity. EMBO J. 2017;36(20):2951\u201367. Available from: \nhttp:\/\/emboj.embopress.org\/lookup\/doi\/10.15252\/embj.201696394","journal-title":"The EMBO Journal"},{"issue":"Pt 9","key":"25_CR53","doi-asserted-by":"publisher","first-page":"2079","DOI":"10.1242\/jcs.jcs124404","volume":"126","author":"YL Chew","year":"2013","unstructured":"Chew YL, Fan X, Gotz J, Nicholas HR. PTL-1 regulates neuronal integrity and lifespan in C. elegans. J Cell Sci. 2013;126(Pt 9):2079\u201391.","journal-title":"J Cell Sci"},{"issue":"2","key":"25_CR54","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0191526","volume":"13","author":"G Farah","year":"2018","unstructured":"Farah G, Siwek D, Cummings P. Tau accumulations in the brains of woodpeckers. PLoS One. 2018;13(2):e0191526.","journal-title":"PLoS One"},{"issue":"4","key":"25_CR55","doi-asserted-by":"publisher","first-page":"519","DOI":"10.1016\/0896-6273(89)90210-9","volume":"3","author":"M Goedert","year":"1989","unstructured":"Goedert M, Spillantini MG, Jakes R, Rutherford D, Crowther RA. Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer\u2019s disease. Neuron. 1989;3(4):519\u201326.","journal-title":"Neuron"},{"issue":"2","key":"25_CR56","doi-asserted-by":"publisher","first-page":"121","DOI":"10.1016\/S0165-3806(03)00056-7","volume":"142","author":"H Takuma","year":"2003","unstructured":"Takuma H, Arawaka S, Mori H. Isoforms changes of tau protein during development in various species. Dev Brain Res. 2003;142(2):121\u20137.","journal-title":"Dev Brain Res"},{"issue":"4","key":"25_CR57","doi-asserted-by":"publisher","first-page":"1389","DOI":"10.1016\/0896-6273(89)90077-9","volume":"2","author":"KS Kosik","year":"1989","unstructured":"Kosik KS, Orecchio LD, Bakalis S, Neve RL. Developmentally regulated expression of specific tau sequences. Neuron. 1989;2(4):1389\u201397.","journal-title":"Neuron"},{"issue":"7","key":"25_CR58","doi-asserted-by":"publisher","first-page":"1922.e7","DOI":"10.1016\/j.neurobiolaging.2013.01.017","volume":"34","author":"E Majounie","year":"2013","unstructured":"Majounie E, Cross W, Newsway V, Dillman A, Vandrovcova J, Morris CM, et al. Tau expression varies in different brain regions and disease state. Neurobiol Aging. 2013;34(7):1922.e7\u20131922.e12.","journal-title":"Neurobiol Aging"},{"issue":"40","key":"25_CR59","doi-asserted-by":"publisher","first-page":"10526","DOI":"10.1021\/bi800783d","volume":"47","author":"S Jeganathan","year":"2008","unstructured":"Jeganathan S, Von Bergen M, Mandelkow EM, Mandelkow E. The natively unfolded character of Tau and its aggregation to Alzheimer-like paired helical filaments. Biochemistry. 2008;47(40):10526\u201339.","journal-title":"Biochemistry"},{"issue":"10","key":"25_CR60","doi-asserted-by":"publisher","first-page":"5129","DOI":"10.1073\/pnas.97.10.5129","volume":"97","author":"M Bergen von","year":"2000","unstructured":"von Bergen M, Friedhoff P, Biernat J, Heberle J, Mandelkow EM, Mandelkow E. Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif ((306)VQIVYK(311)) forming beta structure. Proc Natl Acad Sci U S A. 2000;97(10):5129\u201334.","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"2\u20133","key":"25_CR61","doi-asserted-by":"publisher","first-page":"158","DOI":"10.1016\/j.bbadis.2004.09.010","volume":"1739","author":"M Bergen Von","year":"2005","unstructured":"Von Bergen M, Barghorn S, Biernat J, Mandelkow EM, Mandelkow E. Tau aggregation is driven by a transition from random coil to beta sheet structure. Biochim Biophys Acta. 2005;1739(2\u20133):158\u201366.","journal-title":"Biochim Biophys Acta"},{"key":"25_CR62","doi-asserted-by":"crossref","unstructured":"Wegmann S, Medalsy ID, Mandelkow E, M\u00fcller DJ. The fuzzy coat of pathological human Tau fibrils is a two-layered polyelectrolyte brush. Proc Natl Acad Sci U S A. 2013;110(4):E313\u201321. Available from: \nhttp:\/\/www.pubmedcentral.nih.gov\/articlerender.fcgi?artid=3557036&tool=pmcentrez&rendertype=abstract","DOI":"10.1073\/pnas.1212100110"},{"issue":"17","key":"25_CR63","doi-asserted-by":"publisher","first-page":"2478","DOI":"10.1021\/acs.biochem.8b00008","volume":"57","author":"EW Martin","year":"2018","unstructured":"Martin EW, Mittag T. Relationship of sequence and phase separation in protein low-complexity regions. Biochemistry. 2018;57(17):2478\u201387.","journal-title":"Biochemistry"},{"issue":"4","key":"25_CR64","doi-asserted-by":"publisher","first-page":"753","DOI":"10.1016\/j.cell.2012.04.017","volume":"149","author":"M Kato","year":"2012","unstructured":"Kato M, Han TW, Xie S, Shi K, Du X, Wu LC, et al. Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels. Cell. 2012;149(4):753\u201367.","journal-title":"Cell"},{"issue":"5","key":"25_CR65","doi-asserted-by":"publisher","first-page":"1799","DOI":"10.1083\/jcb.101.5.1799","volume":"101","author":"DG Drubin","year":"1985","unstructured":"Drubin DG, Feinstein SC, Shooter EM, Kirschner MW. Nerve growth factor-induced neurite outgrowth in PC12 cells involves the coordinate induction of microtubule assembly and assembly-promoting factors. J Cell Biol. 1985;101(5):1799\u2013807.","journal-title":"J Cell Biol"},{"issue":"39","key":"25_CR66","doi-asserted-by":"publisher","first-page":"30335","DOI":"10.1074\/jbc.M002590200","volume":"275","author":"M Ackmann","year":"2000","unstructured":"Ackmann M, Wiech H, Mandelkow E. Nonsaturable binding indicates clustering of Tau on the microtubule surface in a paired helical filament-like conformation. J Biol Chem. 2000;275(39):30335\u201343.","journal-title":"J Biol Chem"},{"issue":"7","key":"25_CR67","doi-asserted-by":"publisher","first-page":"332","DOI":"10.1016\/j.tibs.2009.03.008","volume":"34","author":"D Matenia","year":"2009","unstructured":"Matenia D, Mandelkow EM. The tau of MARK: a polarized view of the cytoskeleton. Trends Biochem Sci. 2009;34(7):332\u201342.","journal-title":"Trends Biochem Sci"},{"issue":"50","key":"25_CR68","doi-asserted-by":"publisher","first-page":"9068","DOI":"10.1021\/bi401266n","volume":"52","author":"M Schwalbe","year":"2013","unstructured":"Schwalbe M, Biernat J, Bibow S, Ozenne V, Jensen MR, Kadavath H, et al. Phosphorylation of human tau protein by microtubule affinity-regulating kinase 2. Biochemistry. 2013;52(50):9068\u201379.","journal-title":"Biochemistry"},{"issue":"1","key":"25_CR69","doi-asserted-by":"publisher","first-page":"21","DOI":"10.4161\/pri.1.1.4055","volume":"1","author":"G Lippens","year":"2007","unstructured":"Lippens G, Sillen A, Landrieu I, Amniai L, Sibille N, Barbier P, et al. Tau aggregation in Alzheimer\u2019s disease: what role for phosphorylation? Prion. 2007;1(1):21\u20135.","journal-title":"Prion"},{"issue":"1","key":"25_CR70","doi-asserted-by":"publisher","first-page":"30","DOI":"10.1186\/s40478-017-0435-7","volume":"5","author":"R Rubenstein","year":"2017","unstructured":"Rubenstein R, Chang B, Grinkina N, Drummond E, Davies P, Ruditzky M, et al. Tau phosphorylation induced by severe closed head traumatic brain injury is linked to the cellular prion protein. Acta Neuropathol Commun. 2017;5(1):30.","journal-title":"Acta Neuropathol Commun"},{"issue":"26","key":"25_CR71","doi-asserted-by":"publisher","first-page":"E3755","DOI":"10.1073\/pnas.1600953113","volume":"113","author":"Sofia Lopes","year":"2016","unstructured":"Lopes S, Vaz-Silva J, Pinto V, Dalla C, Kokras N, Bedenk B, et al. Tau protein is essential for stress-induced brain pathology. Proc Natl Acad Sci. 2016;113(26):E3755\u201363. Available from: \nhttp:\/\/www.pnas.org\/lookup\/doi\/10.1073\/pnas.1600953113","journal-title":"Proceedings of the National Academy of Sciences"},{"key":"25_CR72","doi-asserted-by":"publisher","first-page":"41","DOI":"10.1186\/1742-2094-6-41","volume":"6","author":"A Salminen","year":"2009","unstructured":"Salminen A, Kauppinen A, Suuronen T, Kaarniranta K, Ojala J. ER stress in Alzheimer\u2019s disease: a novel neuronal trigger for inflammation and Alzheimer\u2019s pathology. J Neuroinflammation. 2009;6:41.","journal-title":"J Neuroinflammation"},{"issue":"4","key":"25_CR73","doi-asserted-by":"publisher","first-page":"879","DOI":"10.1016\/0896-6273(95)90232-5","volume":"14","author":"J Busciglio","year":"1995","unstructured":"Busciglio J, Lorenzo A, Yeh J, Yankner BA. \u03b2-Amyloid fibrils induce tau phosphorylation and loss of microtubule binding. Neuron. 1995;14(4):879\u201388.","journal-title":"Neuron"},{"issue":"18","key":"25_CR74","doi-asserted-by":"publisher","first-page":"6972","DOI":"10.1523\/JNEUROSCI.23-18-06972.2003","volume":"23","author":"T Arendt","year":"2003","unstructured":"Arendt T, Stieler J, Strijkstra AM, Hut RA, R\u00fcdiger J, Van der Zee EA, et al. Reversible paired helical filament-like phosphorylation of tau is an adaptive process associated with neuronal plasticity in hibernating animals. J Neurosci. 2003;23(18):6972\u201381.","journal-title":"J Neurosci"},{"issue":"10","key":"25_CR75","doi-asserted-by":"publisher","first-page":"2574","DOI":"10.1021\/bi061318s","volume":"46","author":"D Fischer","year":"2007","unstructured":"Fischer D, Mukrasch MD, Von Bergen M, Klos-Witkowska A, Biemat J, Griesinger C, et al. Structural and microtubule binding properties of tau mutants of frontotemporal dementias. Biochemistry. 2007;46(10):2574\u201382.","journal-title":"Biochemistry"},{"issue":"51","key":"25_CR76","doi-asserted-by":"publisher","first-page":"48165","DOI":"10.1074\/jbc.M105196200","volume":"276","author":"M Bergen Von","year":"2001","unstructured":"Von Bergen M, Barghorn S, Li L, Marx A, Biernat J, Mandelkow EM, et al. Mutations of tau protein in frontotemporal dementia promote aggregation of paired helical filaments by enhancing local beta-structure. J Biol Chem. 2001;276(51):48165\u201374.","journal-title":"J Biol Chem"},{"issue":"15","key":"25_CR77","doi-asserted-by":"publisher","first-page":"3500","DOI":"10.1093\/hmg\/dds161","volume":"21","author":"G Coppola","year":"2012","unstructured":"Coppola G, Chinnathambi S, Lee JJY, Dombroski BA, Baker MC, Soto-ortolaza AI, et al. Evidence for a role of the rare p.A152T variant in mapt in increasing the risk for FTD-spectrum and Alzheimer\u2019s diseases. Hum Mol Genet. 2012;21(15):3500\u201312.","journal-title":"Hum Mol Genet"},{"key":"25_CR78","doi-asserted-by":"crossref","unstructured":"Pir GJ, Choudhary B, Mandelkow E, Mandelkow E-M. Tau mutant A152T, a risk factor for FTD\/PSP, induces neuronal dysfunction and reduced lifespan independently of aggregation in a C. elegans Tauopathy model. Mol Neurodegener. 2016;11:33. Available from: \nhttp:\/\/www.ncbi.nlm.nih.gov\/pubmed\/27118310%5Cn\n\n. \nhttp:\/\/www.pubmedcentral.nih.gov\/articlerender.fcgi?artid=PMC4847334","DOI":"10.1186\/s13024-016-0096-1"},{"issue":"4","key":"25_CR79","doi-asserted-by":"publisher","first-page":"530","DOI":"10.15252\/embr.201541438","volume":"17","author":"S Maeda","year":"2016","unstructured":"Maeda S, Djukic B, Taneja P, Yu G, Lo I, Davis A, et al. Expression of A152T human tau causes age-dependent neuronal dysfunction and loss in transgenic mice. EMBO Rep. 2016;17(4):530\u201351.","journal-title":"EMBO Rep"},{"issue":"4","key":"25_CR80","doi-asserted-by":"publisher","first-page":"552","DOI":"10.15252\/embr.201541439","volume":"17","author":"JM Decker","year":"2016","unstructured":"Decker JM, Kr\u00fcger L, Sydow A, Dennissen FJ, Siskova Z, Mandelkow E, et al. The Tau\/A152T mutation, a risk factor for frontotemporal-spectrum disorders, leads to NR2B receptor-mediated excitotoxicity. EMBO Rep. 2016;17(4):552\u201369.","journal-title":"EMBO Rep"},{"issue":"7","key":"25_CR81","doi-asserted-by":"publisher","first-page":"1455","DOI":"10.1016\/j.celrep.2016.04.045","volume":"15","author":"T Vanderweyde","year":"2016","unstructured":"Vanderweyde T, Apicco DJ, Youmans-Kidder K, Ash PEA, Cook C, Lummertz da Rocha E, et al. Interaction of tau with the RNA-binding protein TIA1 regulates tau pathophysiology and toxicity. Cell Rep. 2016;15(7):1455\u201366.","journal-title":"Cell Rep"},{"issue":"1","key":"25_CR82","doi-asserted-by":"publisher","first-page":"72","DOI":"10.1038\/s41593-017-0022-z","volume":"21","author":"DJ Apicco","year":"2018","unstructured":"Apicco DJ, Ash PEA, Maziuk B, Leblang C, Medalla M, Al Abdullatif A, et al. Reducing the RNA binding protein TIA1 protects against tau-mediated neurodegeneration in vivo. Nat Neurosci. 2018;21(1):72\u201380.","journal-title":"Nat Neurosci"},{"issue":"3","key":"25_CR83","doi-asserted-by":"publisher","first-page":"271","DOI":"10.1016\/0197-4580(95)00021-6","volume":"16","author":"H Braak","year":"1995","unstructured":"Braak H, Braak E. Staging of Alzheimer\u2019s disease-related neurofibrillary changes. Neurobiol Aging. 1995;16(3):271\u20138.","journal-title":"Neurobiol Aging"},{"issue":"1","key":"25_CR84","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1007\/s00401-011-0910-3","volume":"123","author":"TJ Montine","year":"2012","unstructured":"Montine TJ, Phelps CH, Beach TG, Bigio EH, Cairns NJ, Dickson DW, et al. National institute on aging-Alzheimer\u2019s association guidelines for the neuropathologic assessment of Alzheimer\u2019s disease: a practical approach. Acta Neuropathol. 2012;123(1):1\u201311.","journal-title":"Acta Neuropathol"},{"issue":"5","key":"25_CR85","doi-asserted-by":"publisher","first-page":"49","DOI":"10.1186\/alzrt214","volume":"5","author":"AM Pooler","year":"2013","unstructured":"Pooler AM, Polydoro M, Wegmann S, Nicholls SB, Spires-Jones TL, Hyman BT. Propagation of tau pathology in Alzheimer\u2019s disease: identification of novel therapeutic targets. Alzheimers Res Ther. 2013;5(5):49. Available from: \nhttp:\/\/alzres.com\/content\/5\/5\/49","journal-title":"Alzheimers Res Ther"},{"issue":"3","key":"25_CR86","doi-asserted-by":"publisher","first-page":"368","DOI":"10.1111\/jnc.12991","volume":"133","author":"S Sokolow","year":"2015","unstructured":"Sokolow S, Henkins KM, Bilousova T, Gonzalez B, Vinters HV, Miller CA, et al. Pre-synaptic C-terminal truncated tau is released from cortical synapses in Alzheimer\u2019s disease. J Neurochem. 2015;133(3):368\u201379.","journal-title":"J Neurochem"},{"issue":"1","key":"25_CR87","doi-asserted-by":"publisher","first-page":"5","DOI":"10.1186\/s13024-016-0143-y","volume":"12","author":"Y Wang","year":"2017","unstructured":"Wang Y, Balaji V, Kaniyappan S, Kr\u00fcger L, Irsen S, Tepper K, et al. The release and trans-synaptic transmission of Tau via exosomes. Mol Neurodegener. 2017;12(1):5.","journal-title":"Mol Neurodegener"},{"issue":"6","key":"25_CR88","doi-asserted-by":"publisher","first-page":"3842","DOI":"10.1074\/jbc.M111.277061","volume":"287","author":"S Saman","year":"2012","unstructured":"Saman S, Kim WH, Raya M, Visnick Y, Miro S, Saman S, et al. Exosome-associated tau is secreted in tauopathy models and is selectively phosphorylated in cerebrospinal fluid in early Alzheimer disease. J Biol Chem. 2012;287(6):3842\u20139.","journal-title":"J Biol Chem"},{"issue":"6","key":"25_CR89","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0100760","volume":"9","author":"S Dujardin","year":"2014","unstructured":"Dujardin S, B\u00e9gard S, Caillierez R, Lachaud C, Delattre L, Carrier S, et al. Ectosomes: a new mechanism for non-exosomal secretion of Tau protein. PLoS One. 2014;9(6):e100760.","journal-title":"PLoS One"},{"issue":"7","key":"25_CR90","doi-asserted-by":"publisher","first-page":"2039","DOI":"10.1016\/j.celrep.2018.04.056","volume":"23","author":"T Katsinelos","year":"2018","unstructured":"Katsinelos T, Zeitler M, Dimou E, Karakatsani A, M\u00fcller HM, Nachman E, et al. Unconventional secretion mediates the trans-cellular spreading of tau. Cell Rep. 2018;23(7):2039\u201355.","journal-title":"Cell Rep"},{"key":"25_CR91","doi-asserted-by":"crossref","unstructured":"Pooler AM, Polydoro M, Maury EA, Nicholls SB, Reddy SM, Wegmann S, et al. Amyloid accelerates tau propagation and toxicity in a model of early Alzheimer\u2019s disease. Acta Neuropathol Commun. 2015;3:14. Available from: \nhttp:\/\/www.pubmedcentral.nih.gov\/articlerender.fcgi?artid=4371800&tool=pmcentrez&rendertype=abstract","DOI":"10.1186\/s40478-015-0199-x"},{"issue":"8","key":"25_CR92","doi-asserted-by":"publisher","first-page":"1085","DOI":"10.1038\/nn.4328","volume":"19","author":"JW Wu","year":"2016","unstructured":"Wu JW, Hussaini SA, Bastille IM, Rodriguez GA, Mrejeru A, Rilett K, et al. Neuronal activity enhances tau propagation and tau pathology in vivo. Nat Neurosci. 2016;19(8):1085\u201392.","journal-title":"Nat Neurosci"},{"key":"25_CR93","doi-asserted-by":"crossref","unstructured":"Dujardin S, Lecolle K, Caillierez R, Begard S, Zommer N, Lachaud C, et al. Neuron-to-neuron wild-type Tau protein transfer through a trans-synaptic mechanism: relevance to sporadic tauopathies. Acta Neuropathol Commun. 2014;2:14. Available from: \nhttp:\/\/www.ncbi.nlm.nih.gov\/pubmed\/24479894","DOI":"10.1186\/2051-5960-2-14"},{"issue":"4","key":"25_CR94","doi-asserted-by":"publisher","first-page":"685","DOI":"10.1016\/j.neuron.2011.11.033","volume":"73","author":"A Calignon De","year":"2012","unstructured":"De Calignon A, Polydoro M, Su\u00e1rez-Calvet M, William C, Adamowicz DH, Kopeikina KJ, et al. Propagation of tau pathology in a model of early Alzheimer\u2019s disease. Neuron. 2012;73(4):685\u201397.","journal-title":"Neuron"},{"issue":"2","key":"25_CR95","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0031302","volume":"7","author":"L Liu","year":"2012","unstructured":"Liu L, Drouet V, Wu JW, Witter MP, Small SA, Clelland C, et al. Trans-synaptic spread of tau pathology in vivo. PLoS One. 2012;7(2):e31302.","journal-title":"PLoS One"},{"issue":"24","key":"25_CR96","doi-asserted-by":"publisher","first-page":"3028","DOI":"10.15252\/embj.201592748","volume":"34","author":"Susanne Wegmann","year":"2015","unstructured":"Wegmann S, Maury EA, Kirk MJ, Saqran L, Roe A, DeVos SL, et al. Removing endogenous tau does not prevent tau propagation yet reduces its neurotoxicity. EMBO J. 2015;34(24):1\u201314. Available from: \nhttp:\/\/www.ncbi.nlm.nih.gov\/pubmed\/26538322","journal-title":"The EMBO Journal"},{"issue":"23","key":"25_CR97","doi-asserted-by":"publisher","first-page":"19440","DOI":"10.1074\/jbc.M112.346072","volume":"287","author":"N Kfoury","year":"2012","unstructured":"Kfoury N, Holmes BB, Jiang H, Holtzman DM, Diamond MI. Trans-cellular propagation of Tau aggregation by fibrillar species. J Biol Chem. 2012;287(23):19440\u201351.","journal-title":"J Biol Chem"},{"key":"25_CR98","doi-asserted-by":"publisher","first-page":"8490","DOI":"10.1038\/ncomms9490","volume":"6","author":"S Takeda","year":"2015","unstructured":"Takeda S, Wegmann S, Cho H, DeVos SL, Commins C, Roe AD, et al. Neuronal uptake and propagation of a rare phosphorylated high-molecular-weight tau derived from Alzheimer\u2019s disease brain. Nat Commun. 2015;6:8490. Available from: \nhttp:\/\/www.pubmedcentral.nih.gov\/articlerender.fcgi?artid=4608380&tool=pmcentrez&rendertype=abstract","journal-title":"Nat Commun"},{"issue":"3","key":"25_CR99","doi-asserted-by":"publisher","first-page":"1856","DOI":"10.1074\/jbc.M112.394528","volume":"288","author":"JW Wu","year":"2013","unstructured":"Wu JW, Herman M, Liu L, Simoes S, Acker CM, Figueroa H, et al. Small misfolded tau species are internalized via bulk endocytosis and anterogradely and retrogradely transported in neurons. J Biol Chem. 2013;288(3):1856\u201370.","journal-title":"J Biol Chem"},{"issue":"13","key":"25_CR100","doi-asserted-by":"publisher","first-page":"3612","DOI":"10.1016\/j.celrep.2018.03.021","volume":"22","author":"LD Evans","year":"2018","unstructured":"Evans LD, Wassmer T, Fraser G, Smith J, Perkinton M, Billinton A, et al. Extracellular monomeric and aggregated tau efficiently enter human neurons through overlapping but distinct pathways. Cell Rep. 2018;22(13):3612\u201324.","journal-title":"Cell Rep"},{"issue":"33","key":"25_CR101","doi-asserted-by":"publisher","first-page":"E3138","DOI":"10.1073\/pnas.1301440110","volume":"110","author":"BB Holmes","year":"2013","unstructured":"Holmes BB, DeVos SL, Kfoury N, Li M, Jacks R, Yanamandra K, et al. Heparan sulfate proteoglycans mediate internalization and propagation of specific proteopathic seeds. Proc Natl Acad Sci. 2013;110(33):E3138\u201347.","journal-title":"Proc Natl Acad Sci"},{"key":"25_CR102","doi-asserted-by":"crossref","unstructured":"Weingarten MD, Lockwood AH, Hwo SY, Kirschner MW. A protein factor essential for microtubule assembly. Proc Natl Acad Sci U S A. 1975;72(5):1858\u201362. Available from: \nhttp:\/\/www.pubmedcentral.nih.gov\/articlerender.fcgi?artid=432646&tool=pmcentrez&rendertype=abstract","DOI":"10.1073\/pnas.72.5.1858"},{"issue":"6","key":"25_CR103","doi-asserted-by":"publisher","first-page":"2720","DOI":"10.1091\/mbc.e04-01-0062","volume":"15","author":"JM Bunker","year":"2004","unstructured":"Bunker JM, Wilson L, Jordan MA, Feinstein SC. Modulation of microtubule dynamics by tau in living cells: implications for development and neurodegeneration. Mol Biol Cell. 2004;15(6):2720\u20138.","journal-title":"Mol Biol Cell"},{"issue":"5866","key":"25_CR104","doi-asserted-by":"publisher","first-page":"1086","DOI":"10.1126\/science.1152993","volume":"319","author":"R Dixit","year":"2008","unstructured":"Dixit R, Ross JL, Goldman YE, Holzbaur ELF. Differential regulation of dynein and kinesin motor proteins by tau. Science (80-). 2008;319(5866):1086\u20139.","journal-title":"Science (80-)"},{"issue":"8","key":"25_CR105","doi-asserted-by":"publisher","first-page":"5535","DOI":"10.1074\/jbc.275.8.5535","volume":"275","author":"CX Gong","year":"2000","unstructured":"Gong CX, Lidsky T, Wegiel J, Zuck L, Grundke-Iqbal I, Iqbal K. Phosphorylation of microtubule-associated protein tau is regulated by protein phosphatase 2A in mammalian brain. Implications for neurofibrillary degeneration in Alzheimer\u2019s disease. J Biol Chem. 2000;275(8):5535\u201344.","journal-title":"J Biol Chem"},{"key":"25_CR106","doi-asserted-by":"publisher","unstructured":"Tan R, Lam AJ, Tan T, Han J, Nowakowski DW, Vershinin M, et al. Microtubules gate tau condensation to spatially regulate microtubule functions. bioRxiv. 2018; \nhttps:\/\/doi.org\/10.1101\/423376\n\n.","DOI":"10.1101\/423376"},{"issue":"41","key":"25_CR107","doi-asserted-by":"publisher","first-page":"11597","DOI":"10.1073\/pnas.1603119113","volume":"113","author":"FJA Dennissen","year":"2016","unstructured":"Dennissen FJA, Anglada-Huguet M, Sydow A, Mandelkow E, Mandelkow E-M. Adenosine A1 receptor antagonist rolofylline alleviates axonopathy caused by human Tau \u0394K280. Proc Natl Acad Sci. 2016;113(41):11597\u2013602.","journal-title":"Proc Natl Acad Sci"}],"container-title":["Advances in Experimental Medicine and Biology","Tau Biology"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/978-981-32-9358-8_25","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2020,2,24]],"date-time":"2020-02-24T17:18:26Z","timestamp":1582564706000},"score":1,"resource":{"primary":{"URL":"http:\/\/link.springer.com\/10.1007\/978-981-32-9358-8_25"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019]]},"ISBN":["9789813293571","9789813293588"],"references-count":107,"URL":"https:\/\/doi.org\/10.1007\/978-981-32-9358-8_25","relation":{},"ISSN":["0065-2598","2214-8019"],"issn-type":[{"value":"0065-2598","type":"print"},{"value":"2214-8019","type":"electronic"}],"subject":[],"published":{"date-parts":[[2019]]},"assertion":[{"value":"25 February 2020","order":1,"name":"first_online","label":"First Online","group":{"name":"ChapterHistory","label":"Chapter History"}}]}}