{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T19:37:08Z","timestamp":1791920228433,"version":"4.3.4"},"reference-count":79,"publisher":"Public Library of Science (PLoS)","issue":"8","license":[{"start":{"date-parts":[[2013,8,12]],"date-time":"2013-08-12T00:00:00Z","timestamp":1376265600000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["www.plosone.org"],"crossmark-restriction":false},"short-container-title":["PLoS ONE"],"DOI":"10.1371\/journal.pone.0073303","type":"journal-article","created":{"date-parts":[[2013,8,12]],"date-time":"2013-08-12T21:15:11Z","timestamp":1376342111000},"page":"e73303","update-policy":"https:\/\/doi.org\/10.1371\/journal.pone.corrections_policy","source":"Crossref","is-referenced-by-count":49,"title":["Interactions between A\u03b2 and Mutated Tau Lead to Polymorphism and Induce Aggregation of A\u03b2-Mutated Tau Oligomeric Complexes"],"prefix":"10.1371","volume":"8","author":[{"given":"Yoav","family":"Raz","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yifat","family":"Miller","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2013,8,12]]},"reference":[{"key":"ref1","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1146\/annurev.pharmtox.43.100901.140248","article-title":"Alzheimer&apos;s disease: molecular understanding predicts amyloid-based therapeutics","volume":"43","author":"DJ Selkoe","year":"2003","journal-title":"Annu Rev Pharmacol Toxicol"},{"key":"ref2","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1016\/S0962-8924(98)01368-3","article-title":"Tau in Alzheimer&apos;s disease","volume":"8","author":"EM Mandelkow","year":"1998","journal-title":"Trends Cell Biol"},{"key":"ref3","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":"S Barghorn","year":"2000","journal-title":"Biochemistry"},{"key":"ref4","doi-asserted-by":"crossref","first-page":"10278","DOI":"10.1073\/pnas.0401911101","article-title":"Template-assisted filament growth by parallel stacking of tau","volume":"101","author":"M Margittai","year":"2004","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref5","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":"MD Mukrasch","year":"2005","journal-title":"J Biol Chem"},{"key":"ref6","doi-asserted-by":"crossref","first-page":"12230","DOI":"10.1074\/jbc.M607159200","article-title":"The &quot;jaws&quot; of the tau-microtubule interaction","volume":"282","author":"MD Mukrasch","year":"2007","journal-title":"J Biol Chem"},{"key":"ref7","doi-asserted-by":"crossref","first-page":"1026","DOI":"10.1021\/bi048953n","article-title":"Residual structure in the repeat domain of tau: echoes of microtubule binding and paired helical filament formation","volume":"44","author":"D Eliezer","year":"2005","journal-title":"Biochemistry"},{"key":"ref8","doi-asserted-by":"crossref","first-page":"141","DOI":"10.3233\/JAD-2009-1130","article-title":"Tau aggregation followed by atomic force microscopy and surface plasmon resonance, and single molecule tau-tau interaction probed by atomic force spectroscopy","volume":"18","author":"A Barrantes","year":"2009","journal-title":"J Alzheimers Dis"},{"key":"ref9","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1371\/journal.pbio.1000034","article-title":"Structural Polymorphism of 441-Residue Tau at Single Residue Resolution","volume":"7","author":"MD Mukrasch","year":"2009","journal-title":"PLOS Biol"},{"key":"ref10","doi-asserted-by":"crossref","first-page":"1694","DOI":"10.1021\/bi0357006","article-title":"Tau paired helical filaments from Alzheimer&apos;s disease brain and assembled in vitro are based on beta-structure in the core domain","volume":"43","author":"S Barghorn","year":"2004","journal-title":"Biochemistry"},{"key":"ref11","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1038\/nature05695","article-title":"Atomic structures of amyloid cross-beta spines reveal varied steric zippers","volume":"447","author":"MR Sawaya","year":"2007","journal-title":"Nature"},{"key":"ref12","doi-asserted-by":"crossref","first-page":"14950","DOI":"10.1074\/jbc.M112.340794","article-title":"Cross-seeding and Conformational Selection between Three- and Four-repeat Human Tau Proteins","volume":"287","author":"X Yu","year":"2012","journal-title":"J Biol Chem"},{"key":"ref13","doi-asserted-by":"crossref","first-page":"9034","DOI":"10.1073\/pnas.1530287100","article-title":"Tau filaments from human brain and from in vitro assembly of recombinant protein show cross-\u03b2 structure","volume":"100","author":"J Berriman","year":"2003","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref14","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":"M von Bergen","year":"2001","journal-title":"J Biol Chem"},{"key":"ref15","doi-asserted-by":"crossref","first-page":"5129","DOI":"10.1073\/pnas.97.10.5129","article-title":"Assembly of \u03c4 protein into Alzheimer paired helical filaments depends on a local sequence motif (306VQIVYK311) forming \u03b2 structure","volume":"97","author":"M von Bergen","year":"2000","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref16","doi-asserted-by":"crossref","first-page":"26868","DOI":"10.1074\/jbc.M402379200","article-title":"The formation of straight and twisted filaments from short tau peptides","volume":"279","author":"WJ Goux","year":"2004","journal-title":"J Biol Chem"},{"key":"ref17","doi-asserted-by":"crossref","first-page":"10271","DOI":"10.1021\/ja303498q","article-title":"Conformational Basis for Asymmetric Seeding Barrier in Filaments of Three- and Four-Repeat Tau","volume":"134","author":"A Siddiqua","year":"2012","journal-title":"J Am Chem Soc"},{"key":"ref18","doi-asserted-by":"crossref","first-page":"1953","DOI":"10.1073\/pnas.0509386103","article-title":"Abeta and tau form soluble complexes that may promote self aggregation of both into the insoluble forms observed in Alzheimer&apos;s disease","volume":"103","author":"JP Guo","year":"2006","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref19","doi-asserted-by":"crossref","first-page":"20057","DOI":"10.1073\/pnas.0905529106","article-title":"Amyloid-beta and tau synergistically impair the oxidative phosphorylation system in triple transgenic Alzheimer&apos;s disease mice","volume":"106","author":"V Rhein","year":"2009","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref20","doi-asserted-by":"crossref","first-page":"23802","DOI":"10.1074\/jbc.M500356200","article-title":"Proteomic and Functional Analyses Reveal a Mitochondrial Dysfunction in P301L Tau Transgenic Mice","volume":"280","author":"DC David","year":"2005","journal-title":"J Biol Chem"},{"key":"ref21","doi-asserted-by":"crossref","first-page":"668","DOI":"10.1016\/j.exger.2006.03.012","article-title":"Mitochondrial dysfunction in sporadic and genetic Alzheimer&apos;s disease","volume":"41","author":"S Hauptmann","year":"2006","journal-title":"Exp Gerontol"},{"key":"ref22","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1159\/000113689","article-title":"Soluble beta-amyloid leads to mitochondrial defects in amyloid precursor protein and tau transgenic mice","volume":"5","author":"A Eckert","year":"2008","journal-title":"Neurodegener Dis"},{"key":"ref23","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1159\/000283475","article-title":"Dissecting toxicity of tau and beta-amyloid","volume":"7","author":"J G\u00f6tz","year":"2010","journal-title":"Neurodegener Dis"},{"key":"ref24","doi-asserted-by":"crossref","first-page":"5172","DOI":"10.1021\/bi200400u","article-title":"Synergistic interactions between repeats in tau protein and Abeta amyloids may be responsible for accelerated aggregation via polymorphic states","volume":"50","author":"Y Miller","year":"2011","journal-title":"Biochemistry"},{"key":"ref25","doi-asserted-by":"crossref","first-page":"702","DOI":"10.1038\/31508","article-title":"Association of missense and 5[prime]-splice-site mutations in tau with the inherited dementia FTDP-17","volume":"393","author":"M Hutton","year":"1998","journal-title":"Nature"},{"key":"ref26","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1016\/S0014-5793(98)01217-4","article-title":"Tau proteins with FTDP-17 mutations have a reduced ability to promote microtubule assembly","volume":"437","author":"M Hasegawa","year":"1998","journal-title":"FEBS Lett"},{"key":"ref27","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1097\/nen.0b013e31802c39a4","article-title":"The [DELTA]K280 Mutation in MAP tau Favors Exon 10 Skipping In Vivo","volume":"66","author":"JC van Swieten","year":"2007","journal-title":"J Neuropathol Exp Neurol"},{"key":"ref28","doi-asserted-by":"crossref","first-page":"27302","DOI":"10.1074\/jbc.M110.145318","article-title":"Human Tau Isoforms Assemble into Ribbon-like Fibrils That Display Polymorphic Structure and Stability","volume":"285","author":"S Wegmann","year":"2010","journal-title":"J Biol Chem"},{"key":"ref29","doi-asserted-by":"crossref","first-page":"2574","DOI":"10.1021\/bi061318s","article-title":"Structural and microtubule binding properties of tau mutants of frontotemporal dementias","volume":"46","author":"D Fischer","year":"2007","journal-title":"Biochemistry"},{"key":"ref30","doi-asserted-by":"crossref","first-page":"414","DOI":"10.1086\/302256","article-title":"High prevalence of mutations in the microtubule-associated protein tau in a population study of frontotemporal dementia in the Netherlands","volume":"64","author":"P Rizzu","year":"1999","journal-title":"Am J Hum Genet"},{"key":"ref31","doi-asserted-by":"crossref","first-page":"1359","DOI":"10.1016\/S0002-9440(10)65721-5","article-title":"Tau pathology in two Dutch families with mutations in the microtubule-binding region of tau","volume":"153","author":"MG Spillantini","year":"1998","journal-title":"Am J Pathol"},{"key":"ref32","doi-asserted-by":"crossref","first-page":"4093","DOI":"10.1091\/mbc.11.12.4093","article-title":"Distinct FTDP-17 missense mutations in tau produce tau aggregates and other pathological phenotypes in transfected CHO cells","volume":"11","author":"V Vogelsberg-Ragaglia","year":"2000","journal-title":"Mol Biol Cell"},{"key":"ref33","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1006\/jcph.1999.6201","article-title":"NAMD2 : Greater Scalability for Parallel Molecular Dynamics","volume":"151","author":"L Kal\u00e9","year":"1999","journal-title":"J Comput Phys"},{"key":"ref34","doi-asserted-by":"crossref","first-page":"3586","DOI":"10.1021\/jp973084f","article-title":"All - Atom Empirical Potential for Molecular Modeling and Dynamics Studies of Proteins &lt; sup &gt; \u2020 &lt; \/ sup &gt;","volume":"102","author":"AD MacKerell","year":"1998","journal-title":"J Phys Chem B"},{"key":"ref35","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1002\/jcc.540040211","article-title":"<named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"gene\" xlink:type=\"simple\">CHARMM<\/named-content>: A program for macromolecular energy, minimization, and dynamics calculations","volume":"4","author":"BR Brooks","year":"1983","journal-title":"J Comput Chem"},{"key":"ref36","doi-asserted-by":"crossref","first-page":"8910","DOI":"10.1063\/1.481505","article-title":"A five-site model for liquid water and the reproduction of the density anomaly by rigid, nonpolarizable potential functions","volume":"112","author":"MW Mahoney","year":"2000","journal-title":"J Chem Phys"},{"key":"ref37","doi-asserted-by":"crossref","first-page":"926","DOI":"10.1063\/1.445869","article-title":"Comparison of simple potential functions for simulating liquid water","volume":"79","author":"WL Jorgensen","year":"1983","journal-title":"J Chem Phys"},{"key":"ref38","doi-asserted-by":"crossref","first-page":"2558","DOI":"10.1016\/S0006-3495(95)80126-8","article-title":"Constant pressure and temperature molecular dynamics simulation of a fully hydrated liquid crystal phase dipalmitoylphosphatidylcholine bilayer","volume":"69","author":"K Tu","year":"1995","journal-title":"Biophys J"},{"key":"ref39","doi-asserted-by":"crossref","first-page":"4613","DOI":"10.1063\/1.470648","article-title":"Constant pressure molecular dynamics simulation: The Langevin piston method","volume":"103","author":"SE Feller","year":"1995","journal-title":"J Chem Phys"},{"key":"ref40","doi-asserted-by":"crossref","first-page":"8577","DOI":"10.1063\/1.470117","article-title":"A smooth particle mesh Ewald method","volume":"103","author":"U Essmann","year":"1995","journal-title":"J Chem Phys"},{"key":"ref41","doi-asserted-by":"crossref","first-page":"10089","DOI":"10.1063\/1.464397","article-title":"Particle mesh Ewald: An N [center-dot] log(N) method for Ewald sums in large systems","volume":"98","author":"T Darden","year":"1993","journal-title":"J Chem Phys"},{"key":"ref42","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1016\/0021-9991(77)90098-5","article-title":"Numerical integration of the cartesian equations of motion of a system with constraints : molecular dynamics of n - alkanes","volume":"23","author":"J-P Ryckaert","year":"1977","journal-title":"J Comput Phys"},{"key":"ref43","doi-asserted-by":"crossref","first-page":"17342","DOI":"10.1073\/pnas.0506723102","article-title":"3D structure of Alzheimer\u2019s amyloid-beta(1-42) fibrils","volume":"102","author":"T L\u00fchrs","year":"2005","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref44","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/S0301-4622(99)00016-2","article-title":"Quantifying the kinetic parameters of prion replication","volume":"77","author":"J Masel","year":"1999","journal-title":"Biophys Chem"},{"key":"ref45","doi-asserted-by":"crossref","first-page":"2335","DOI":"10.1110\/ps.4270102","article-title":"Molecular dynamics simulations of alanine rich beta-sheet oligomers: Insight into amyloid formation","volume":"11","author":"B Ma","year":"2002","journal-title":"Protein Sci"},{"key":"ref46","doi-asserted-by":"crossref","first-page":"1168","DOI":"10.1016\/j.bpj.2009.05.042","article-title":"Polymorphism of Alzheimer\u2019s Abeta17-42 (p3) oligomers: the importance of the turn location and its conformation","volume":"97","author":"Y Miller","year":"2009","journal-title":"Biophys J"},{"key":"ref47","doi-asserted-by":"crossref","first-page":"24414","DOI":"10.1074\/jbc.M602363200","article-title":"Distinct early folding and aggregation properties of Alzheimer amyloid-beta peptides Abeta40 and Abeta42: stable trimer or tetramer formation by Abeta42","volume":"281","author":"YR Chen","year":"2006","journal-title":"J Biol Chem"},{"key":"ref48","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1073\/pnas.0809057106","article-title":"Increasing Cu bioavailability inhibits A\u03b2 oligomers and tau phosphorylation","volume":"106","author":"PJ Crouch","year":"2009","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref49","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1113\/jphysiol.2005.103754","article-title":"Effects of secreted oligomers of amyloid beta-protein on hippocampal synaptic plasticity: a potent role for trimers","volume":"572","author":"M Townsend","year":"2006","journal-title":"J Physiol"},{"key":"ref50","doi-asserted-by":"crossref","first-page":"e41479","DOI":"10.1371\/journal.pone.0041479","article-title":"Structure and Dynamics of Amyloid-\u03b2 Segmental Polymorphisms","volume":"7","author":"WM Berhanu","year":"2012","journal-title":"PLOS ONE"},{"key":"ref51","doi-asserted-by":"crossref","first-page":"3046","DOI":"10.1529\/biophysj.107.110700","article-title":"Modeling the Alzheimer Abeta17-42 fibril architecture: tight intermolecular sheet-sheet association and intramolecular hydrated cavities","volume":"93","author":"J Zheng","year":"2007","journal-title":"Biophys J"},{"key":"ref52","doi-asserted-by":"crossref","first-page":"e1000693","DOI":"10.1371\/journal.pcbi.1000693","article-title":"Molecular Structures of Quiescently Grown and Brain-Derived Polymorphic Fibrils of the Alzheimer Amyloid A\u03b2 &lt; sub &gt; 9-40&lt;\/sub &gt; Peptide: A Comparison to Agitated Fibrils","volume":"6","author":"C Wu","year":"2010","journal-title":"PLOS Comput Biol"},{"key":"ref53","doi-asserted-by":"crossref","first-page":"16742","DOI":"10.1073\/pnas.262663499","article-title":"A structural model for Alzheimer\u2019s beta -amyloid fibrils based on experimental constraints from solid state NMR","volume":"99","author":"AT Petkova","year":"2002","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref54","doi-asserted-by":"crossref","first-page":"1467","DOI":"10.1110\/ps.036509.108","article-title":"Atomic structure of the cross-\u03b2 spine of islet amyloid polypeptide (amylin)","volume":"17","author":"JJW Wiltzius","year":"2008","journal-title":"Protein Sci"},{"key":"ref55","doi-asserted-by":"crossref","first-page":"2497","DOI":"10.1021\/bi7019194","article-title":"\u03b22-Microglobulin Amyloid Fragment Organization and Morphology and Its Comparison to A\u03b2 Suggests That Amyloid Aggregation Pathways Are Sequence Specific\u2020","volume":"47","author":"J Zheng","year":"2008","journal-title":"Biochemistry"},{"key":"ref56","doi-asserted-by":"crossref","first-page":"19754","DOI":"10.1073\/pnas.0609638103","article-title":"Amyloid of the prion domain of Sup35p has an in - register parallel beta - sheet structure","volume":"103","author":"F Shewmaker","year":"2006","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref57","doi-asserted-by":"crossref","first-page":"3622","DOI":"10.1039\/c000755m","article-title":"Structural diversity of dimers of the Alzheimer amyloid-[small beta](25-35) peptide and polymorphism of the resulting fibrils","volume":"12","author":"G Wei","year":"2010","journal-title":"Phys Chem Chem Phys"},{"key":"ref58","doi-asserted-by":"crossref","first-page":"18349","DOI":"10.1073\/pnas.0806270105","article-title":"Molecular structural basis for polymorphism in Alzheimer\u2019s beta-amyloid fibrils","volume":"105","author":"AK Paravastu","year":"2008","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref59","doi-asserted-by":"crossref","first-page":"5267","DOI":"10.1039\/c1sm05162h","article-title":"Polymorphism of amyloid [small beta] peptide in different environments: implications for membrane insertion and pore formation","volume":"7","author":"FT Arce","year":"2011","journal-title":"Soft Matter"},{"key":"ref60","doi-asserted-by":"crossref","first-page":"4820","DOI":"10.1021\/cr900377t","article-title":"Polymorphism in Alzheimer A\u03b2 Amyloid Organization Reflects Conformational Selection in a Rugged Energy Landscape","volume":"110","author":"Y Miller","year":"2010","journal-title":"Chem Rev"},{"key":"ref61","doi-asserted-by":"crossref","first-page":"18349","DOI":"10.1073\/pnas.0806270105","article-title":"Molecular structural basis for polymorphism in Alzheimer\u2019s \u03b2-amyloid fibrils","volume":"105","author":"AK Paravastu","year":"2008","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref62","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1083\/jcb.200605187","article-title":"Tau-dependent microtubule disassembly initiated by prefibrillar beta-amyloid","volume":"175","author":"ME King","year":"2006","journal-title":"J Cell Biol"},{"key":"ref63","doi-asserted-by":"crossref","first-page":"1487","DOI":"10.1126\/science.1058189","article-title":"Enhanced Neurofibrillary Degeneration in Transgenic Mice Expressing Mutant Tau and APP","volume":"293","author":"J Lewis","year":"2001","journal-title":"Science"},{"key":"ref64","doi-asserted-by":"crossref","first-page":"1491","DOI":"10.1126\/science.1062097","article-title":"Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Abeta 42 fibrils","volume":"293","author":"J G\u00f6tz","year":"2001","journal-title":"Science"},{"key":"ref65","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1016\/S0896-6273(03)00434-3","article-title":"Triple-Transgenic Model of Alzheimer&apos;s Disease with Plaques and Tangles: Intracellular A\u03b2 and Synaptic Dysfunction","volume":"39","author":"S Oddo","year":"2003","journal-title":"Neuron"},{"key":"ref66","doi-asserted-by":"crossref","first-page":"437","DOI":"10.2174\/156720506779025242","article-title":"Pathways by Which A\u03b2 Facilitates Tau Pathology","volume":"3","author":"M Blurton-Jones","year":"2006","journal-title":"Curr Alzheimer Res"},{"key":"ref67","doi-asserted-by":"crossref","first-page":"993","DOI":"10.1042\/BST0380993","article-title":"Pathways linking Abeta and tau pathologies","volume":"38","author":"FM LaFerla","year":"2010","journal-title":"Biochem Soc Trans"},{"key":"ref68","doi-asserted-by":"crossref","first-page":"17345","DOI":"10.1523\/JNEUROSCI.0172-12.2012","article-title":"Soluble abeta promotes wild-type tau pathology in vivo","volume":"32","author":"MA Chabrier","year":"2012","journal-title":"J Neurosci"},{"key":"ref69","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1016\/j.bbadis.2004.09.010","article-title":"Tau aggregation is driven by a transition from random coil to beta sheet structure","volume":"1739","author":"M von Bergen","year":"2005","journal-title":"Biochim Biophys Acta Mol Basis Dis"},{"key":"ref70","doi-asserted-by":"crossref","first-page":"306","DOI":"10.1016\/S0014-5793(99)00508-6","article-title":"Effects of frontotemporal dementia FTDP -17 mutations on heparin - induced assembly of tau filaments","volume":"450","author":"M Goedert","year":"1999","journal-title":"FEBS Lett"},{"key":"ref71","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1016\/S0014-5793(99)00210-0","article-title":"Polymerization of tau peptides into fibrillar structures. The effect of FTDP-17 mutations","volume":"446","author":"M Arrasate","year":"1999","journal-title":"FEBS Lett"},{"key":"ref72","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1016\/S0014-5793(99)00294-X","article-title":"Accelerated filament formation from tau protein with specific FTDP -17 missense mutations","volume":"447","author":"P Nacharaju","year":"1999","journal-title":"FEBS Lett"},{"key":"ref73","doi-asserted-by":"crossref","first-page":"6136","DOI":"10.1021\/bi000201f","article-title":"In vitro polymerization of tau protein monitored by laser light scattering: method and application to the study of FTDP-17 mutants","volume":"39","author":"TC Gamblin","year":"2000","journal-title":"Biochemistry"},{"key":"ref74","doi-asserted-by":"crossref","first-page":"1914","DOI":"10.1126\/science.282.5395.1914","article-title":"Mutation-Specific Functional Impairments in Distinct Tau Isoforms of Hereditary FTDP-17","volume":"282","author":"M Hong","year":"1998","journal-title":"Science"},{"key":"ref75","doi-asserted-by":"crossref","first-page":"5598","DOI":"10.1073\/pnas.96.10.5598","article-title":"Missense and silent tau gene mutations cause frontotemporal dementia with parkinsonism-chromosome 17 type, by affecting multiple alternative RNA splicing regulatory elements","volume":"96","author":"I D\u2019Souza","year":"1999","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref76","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1016\/S0006-8993(99)02124-1","article-title":"Missense tau mutations identified in FTDP-17 have a small effect on tau\u2013microtubule interactions","volume":"853","author":"M DeTure","year":"2000","journal-title":"Brain Res"},{"key":"ref77","doi-asserted-by":"crossref","first-page":"10039","DOI":"10.1021\/bi1016233","article-title":"Preparation and Characterization of Neurotoxic Tau Oligomers","volume":"49","author":"CA Lasagna-Reeves","year":"2010","journal-title":"Biochemistry"},{"key":"ref78","doi-asserted-by":"crossref","first-page":"1348","DOI":"10.1002\/jcc.10272","article-title":"New analytic approximation to the standard molecular volume definition and its application to generalized Born calculations","volume":"24","author":"MS Lee","year":"2003","journal-title":"J Comput Chem"},{"key":"ref79","doi-asserted-by":"crossref","first-page":"10606","DOI":"10.1063\/1.1480013","article-title":"Novel generalized Born methods","volume":"116","author":"MS Lee","year":"2002","journal-title":"J Chem Phys"}],"container-title":["PLoS ONE"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.pone.0073303","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2019,7,20]],"date-time":"2019-07-20T21:32:19Z","timestamp":1563658339000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pone.0073303"}},"subtitle":[],"editor":[{"given":"Pratul\u00a0K.","family":"Agarwal","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2013,8,12]]},"references-count":79,"journal-issue":{"issue":"8","published-online":{"date-parts":[[2013,8,12]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pone.0073303","relation":{},"ISSN":["1932-6203"],"issn-type":[{"value":"1932-6203","type":"electronic"}],"subject":[],"published":{"date-parts":[[2013,8,12]]}}}