{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,21]],"date-time":"2026-05-21T07:11:28Z","timestamp":1779347488429,"version":"3.51.4"},"reference-count":63,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,4,16]],"date-time":"2026-04-16T00:00:00Z","timestamp":1776297600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001665","name":"Agence Nationale de la Recherche","doi-asserted-by":"publisher","award":["ANR-20-29CE-0004"],"award-info":[{"award-number":["ANR-20-29CE-0004"]}],"id":[{"id":"10.13039\/501100001665","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biophysical Chemistry"],"published-print":{"date-parts":[[2026,8]]},"DOI":"10.1016\/j.bpc.2026.107626","type":"journal-article","created":{"date-parts":[[2026,4,8]],"date-time":"2026-04-08T23:14:09Z","timestamp":1775690049000},"page":"107626","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"special_numbering":"C","title":["Full-length Tau disrupts fluid zwitterionic supported lipid bilayers"],"prefix":"10.1016","volume":"335","author":[{"given":"Vicky","family":"Ury-Thiery","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Michael","family":"Molinari","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sophie","family":"Lecomte","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"C\u00e9cile","family":"Feuillie","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.bpc.2026.107626_bb0005","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1186\/s12915-021-00972-y","article-title":"Plasma membrane integrity: implications for health and disease","volume":"19","author":"Ammendolia","year":"2021","journal-title":"BMC Biol."},{"key":"10.1016\/j.bpc.2026.107626_bb0010","doi-asserted-by":"crossref","unstructured":"Arendt, T., Stieler, J.T., Holzer, M., 2016. Tau and Tauopathies. Cytoskeletal Proteins in Health and Neurodegenerative Disease. 126, 238\u2013292. doi:https:\/\/doi.org\/10.1016\/j.brainresbull.2016.08.018, Brain Res. Bull.","DOI":"10.1016\/j.brainresbull.2016.08.018"},{"key":"10.1016\/j.bpc.2026.107626_bb0015","doi-asserted-by":"crossref","first-page":"3514","DOI":"10.3390\/ijms14023514","article-title":"Preparation of DOPC and DPPC supported planar lipid bilayers for atomic force microscopy and atomic force spectroscopy","volume":"14","author":"Attwood","year":"2013","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.bpc.2026.107626_bb0020","doi-asserted-by":"crossref","first-page":"4244","DOI":"10.1039\/D1NA00055A","article-title":"Interaction of tau construct k18 with model lipid membranes","volume":"3","author":"Azouz","year":"2021","journal-title":"Nanoscale Adv."},{"key":"10.1016\/j.bpc.2026.107626_bb0025","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":"Berriman","year":"2003","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.bpc.2026.107626_bb0030","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1016\/j.biochi.2012.07.011","article-title":"What does make an amyloid toxic: morphology, structure or interaction with membrane?","volume":"95","author":"Berthelot","year":"2013","journal-title":"Biochimie"},{"key":"10.1016\/j.bpc.2026.107626_bb0035","doi-asserted-by":"crossref","first-page":"1327","DOI":"10.1083\/jcb.131.5.1327","article-title":"Interaction of tau with the neural plasma membrane mediated by tau\u2019s amino-terminal projection domain","volume":"131","author":"Brandt","year":"1995","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.bpc.2026.107626_bb0040","doi-asserted-by":"crossref","first-page":"808","DOI":"10.1021\/bi301070v","article-title":"Amyloid-forming proteins alter the local mechanical properties of lipid membranes","volume":"52","author":"Burke","year":"2013","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpc.2026.107626_bb0045","doi-asserted-by":"crossref","first-page":"2167","DOI":"10.3390\/ijms20092167","article-title":"Membrane lipid composition: effect on membrane and organelle structure, function and compartmentalization and therapeutic avenues","volume":"20","author":"Casares","year":"2019","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.bpc.2026.107626_bb0050","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/j.bbamem.2005.07.008","article-title":"Structure and orientation study of fusion peptide FP23 of gp41 from HIV-1 alone or inserted into various lipid membrane models (mono-, bi- and multibi-layers) by FT-IR spectroscopies and Brewster angle microscopy","volume":"1715","author":"Castano","year":"2005","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bpc.2026.107626_bb0055","doi-asserted-by":"crossref","first-page":"25644","DOI":"10.1074\/jbc.M301663200","article-title":"Anionic micelles and vesicles induce tau fibrillization in vitro *","volume":"278","author":"Chirita","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bpc.2026.107626_bb0060","doi-asserted-by":"crossref","DOI":"10.1038\/s42003-023-04847-6","article-title":"Membrane-induced tau amyloid fibrils","volume":"6","author":"El Mammeri","year":"2023","journal-title":"Commun. Biol."},{"key":"10.1016\/j.bpc.2026.107626_bb0065","doi-asserted-by":"crossref","first-page":"1339","DOI":"10.3389\/fnins.2019.01339","article-title":"Tau-cofactor complexes as building blocks of tau fibrils","volume":"13","author":"Fichou","year":"2019","journal-title":"Front. Neurosci."},{"key":"10.1016\/j.bpc.2026.107626_bb0070","doi-asserted-by":"crossref","first-page":"4573","DOI":"10.1039\/C8CC01355A","article-title":"Heparin-induced tau filaments are structurally heterogeneous and differ from Alzheimers disease filaments","volume":"54","author":"Fichou","year":"2018","journal-title":"Chem. Commun."},{"key":"10.1016\/j.bpc.2026.107626_bb0075","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1038\/nature23002","article-title":"Cryo-EM structures of tau filaments from Alzheimers disease brain","volume":"547","author":"Fitzpatrick","year":"2017","journal-title":"Nature"},{"key":"10.1016\/j.bpc.2026.107626_bb0080","doi-asserted-by":"crossref","first-page":"43223","DOI":"10.1074\/jbc.M112.396176","article-title":"Tau oligomers impair artificial membrane integrity and cellular viability *","volume":"287","author":"Flach","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bpc.2026.107626_bb0085","doi-asserted-by":"crossref","first-page":"12874","DOI":"10.1021\/ja1002185","article-title":"Nanomechanics of lipid bilayers: heads or tails?","volume":"132","author":"Garcia-Manyes","year":"2010","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bpc.2026.107626_bb0090","doi-asserted-by":"crossref","DOI":"10.1515\/BC.2006.157","article-title":"Paired helical filaments contain small amounts of cholesterol, phosphatidylcholine and sphingolipids","volume":"387","author":"Gellermann","year":"2006","journal-title":"Biol. Chem."},{"key":"10.1016\/j.bpc.2026.107626_bb0095","doi-asserted-by":"crossref","first-page":"1441","DOI":"10.1016\/j.bpj.2014.07.046","article-title":"Tau binds to lipid membrane surfaces via short amphipathic helices located in its microtubule-binding repeats","volume":"107","author":"Georgieva","year":"2014","journal-title":"Biophys. J."},{"key":"10.1016\/j.bpc.2026.107626_bb0100","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.bpc.2026.107626_bb0105","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1111\/j.1432-1033.1990.tb19354.x","article-title":"Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection fourier-transform infrared spectroscopy on hydrated films","volume":"193","author":"Goormaghtigh","year":"1990","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.bpc.2026.107626_bb0110","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/S0304-4157(99)00004-0","article-title":"Attenuated total reflection infrared spectroscopy of proteins and lipids in biological membranes","volume":"1422","author":"Goormaghtigh","year":"1999","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bpc.2026.107626_bb0115","doi-asserted-by":"crossref","first-page":"755","DOI":"10.1038\/s41580-018-0060-8","article-title":"A new era for understanding amyloid structures and disease","volume":"19","author":"Iadanza","year":"2018","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.bpc.2026.107626_bb0120","doi-asserted-by":"crossref","first-page":"2271","DOI":"10.1016\/j.bpj.2017.10.017","article-title":"Computational lipidomics of the neuronal plasma membrane","volume":"113","author":"Ing\u00f3lfsson","year":"2017","journal-title":"Biophys. J."},{"key":"10.1016\/j.bpc.2026.107626_bb0125","doi-asserted-by":"crossref","first-page":"14554","DOI":"10.1021\/ja507832e","article-title":"Lipid organization of the plasma membrane","volume":"136","author":"Ing\u00f3lfsson","year":"2014","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bpc.2026.107626_bb0130","doi-asserted-by":"crossref","first-page":"2539","DOI":"10.1021\/bi201857v","article-title":"Interaction of tau protein with model lipid membranes induces tau structural compaction and membrane disruption","volume":"51","author":"Jones","year":"2012","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpc.2026.107626_bb0135","doi-asserted-by":"crossref","first-page":"7501","DOI":"10.1073\/pnas.1504081112","article-title":"Tau stabilizes microtubules by binding at the interface between tubulin heterodimers","volume":"112","author":"Kadavath","year":"2015","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.bpc.2026.107626_bb0140","doi-asserted-by":"crossref","first-page":"344","DOI":"10.1016\/S0014-5793(96)01386-5","article-title":"RNA stimulates aggregation of microtubule-associated protein tau into alzheimer-like paired helical filaments","volume":"399","author":"Kampers","year":"1996","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bpc.2026.107626_bb0145","doi-asserted-by":"crossref","first-page":"2039","DOI":"10.1016\/j.celrep.2018.04.056","article-title":"Unconventional secretion mediates the trans-cellular spreading of tau","volume":"23","author":"Katsinelos","year":"2018","journal-title":"Cell Rep."},{"key":"10.1016\/j.bpc.2026.107626_bb0150","series-title":"Encyclopedia of Biophysics","first-page":"1841","article-title":"Phase transitions and phase behavior of lipids","author":"Koynova","year":"2013"},{"key":"10.1016\/j.bpc.2026.107626_bb0155","doi-asserted-by":"crossref","first-page":"2347","DOI":"10.1016\/j.bbamem.2012.10.018","article-title":"Membrane lipid phase transitions and phase organization studied by Fourier transform infrared spectroscopy","volume":"1828","author":"Lewis","year":"2013","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"10.1016\/j.bpc.2026.107626_bb0160","doi-asserted-by":"crossref","first-page":"3","DOI":"10.3390\/biomimetics6010003","article-title":"Mimicking the mammalian plasma membrane: an overview of lipid membrane models for biophysical studies","volume":"6","author":"Luchini","year":"2020","journal-title":"Biomimetics (Basel)"},{"key":"10.1016\/j.bpc.2026.107626_bb0165","series-title":"Membrane Structural Biology: With Biochemical and Biophysical Foundations","author":"Luckey","year":"2008"},{"key":"10.1016\/j.bpc.2026.107626_bb0170","doi-asserted-by":"crossref","DOI":"10.1002\/pro.4581","article-title":"Partial mimicry of the microtubule binding of tau by its membrane binding","volume":"32","author":"MacAinsh","year":"2023","journal-title":"Protein Sci."},{"key":"10.1016\/j.bpc.2026.107626_bb0175","doi-asserted-by":"crossref","first-page":"15865","DOI":"10.1021\/bi970944+","article-title":"Orientation in lipid bilayers of a synthetic peptide representing the C-terminus of the a1 domain of Shiga toxin. A polarized ATR-FTIR study","volume":"36","author":"Menikh","year":"1997","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpc.2026.107626_bb0180","doi-asserted-by":"crossref","first-page":"2027","DOI":"10.1016\/j.celrep.2018.10.078","article-title":"Secretion of tau via an unconventional non-vesicular mechanism","volume":"25","author":"Merezhko","year":"2018","journal-title":"Cell Rep."},{"key":"10.1016\/j.bpc.2026.107626_bb0185","doi-asserted-by":"crossref","first-page":"1101","DOI":"10.1007\/s11745-004-1336-x","article-title":"What\u2019s so special about cholesterol?","volume":"39","author":"Mouritsen","year":"2004","journal-title":"Lipids"},{"key":"10.1016\/j.bpc.2026.107626_bb0190","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.bpc.2026.107626_bb0195","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":"Nacharaju","year":"1999","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bpc.2026.107626_bb0200","doi-asserted-by":"crossref","first-page":"4849","DOI":"10.1021\/acs.jpcb.2c02836","article-title":"Molecular dynamics simulations of the tau amyloid fibril core dimer at the surface of a lipid bilayer model: I. In Alzheimers disease","volume":"126","author":"Nguyen","year":"2022","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.bpc.2026.107626_bb0205","doi-asserted-by":"crossref","first-page":"3431","DOI":"10.1021\/acs.jpcb.2c01692","article-title":"Molecular dynamics simulations of the tau R3-R4 domain monomer in the bulk solution and at the surface of a lipid bilayer model","volume":"126","author":"Nguyen","year":"2022","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.bpc.2026.107626_bb0210","doi-asserted-by":"crossref","first-page":"431.e27","DOI":"10.1016\/j.neurobiolaging.2011.01.005","article-title":"Dynamic association of tau with neuronal membranes is regulated by phosphorylation","volume":"33","author":"Pooler","year":"2012","journal-title":"Neurobiol. Aging"},{"key":"10.1016\/j.bpc.2026.107626_bb0215","doi-asserted-by":"crossref","first-page":"12851","DOI":"10.1021\/la302620t","article-title":"Influence of cholesterol on the phase transition of lipid bilayers: a temperature-controlled force spectroscopy study","volume":"28","author":"Redondo-Morata","year":"2012","journal-title":"Langmuir"},{"key":"10.1016\/j.bpc.2026.107626_bb0220","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1016\/j.bpj.2016.06.016","article-title":"Effect of statins on the nanomechanical properties of supported lipid bilayers","volume":"111","author":"Redondo-Morata","year":"2016","journal-title":"Biophys. J."},{"key":"10.1016\/j.bpc.2026.107626_bb0225","series-title":"Peptide Self-Assembly, Methods in Molecular Biology","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1007\/978-1-4939-7811-3_3","article-title":"ATR-FTIR analysis of amyloid proteins","author":"Ruysschaert","year":"2018"},{"key":"10.1016\/j.bpc.2026.107626_bb0230","doi-asserted-by":"crossref","first-page":"1245","DOI":"10.1016\/j.bbamem.2006.02.021","article-title":"Peptide\u2013membrane interactions and mechanisms of membrane destruction by amphipathic \u03b1-helical antimicrobial peptides","volume":"1758","author":"Sato","year":"2006","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"10.1016\/j.bpc.2026.107626_bb0235","doi-asserted-by":"crossref","unstructured":"Scheres, S.H., Zhang, W., Falcon, B., Goedert, M., 2020. Cryo-EM structures of tau filaments. Current opinion in structural biology, biophysical and computational methods. Cryo EM 64, 17\u201325. doi:https:\/\/doi.org\/10.1016\/j.sbi.2020.05.011, Curr. Opin. Struct. Biol.","DOI":"10.1016\/j.sbi.2020.05.011"},{"key":"10.1016\/j.bpc.2026.107626_bb0240","doi-asserted-by":"crossref","first-page":"1470","DOI":"10.1038\/s41594-025-01575-9","article-title":"Distinct tau filament folds in human MAPT mutants P301L and P301T","volume":"32","author":"Schweighauser","year":"2025","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.bpc.2026.107626_bb0245","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1006\/abbi.1998.0813","article-title":"Phosphorylation of tau at both thr 231 and ser 262 is required for maximal inhibition of its binding to microtubules","volume":"357","author":"Sengupta","year":"1998","journal-title":"Arch. Biochem. Biophys."},{"issue":"3\u20134","key":"10.1016\/j.bpc.2026.107626_bb0250","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1007\/s12013-017-0792-7","article-title":"2017. High cholesterol\/low cholesterol: effects in biological membranes review","volume":"75","author":"Subczynski","year":"2017","journal-title":"Cell Biochem. Biophys."},{"key":"10.1016\/j.bpc.2026.107626_bb0255","doi-asserted-by":"crossref","first-page":"15738","DOI":"10.1002\/anie.201809636","article-title":"PIP2 phospholipid-induced aggregation of tau filaments probed by tip-enhanced Raman spectroscopy","volume":"57","author":"Talaga","year":"2018","journal-title":"Angew. Chem. Int. Ed."},{"key":"10.1016\/j.bpc.2026.107626_bb0260","doi-asserted-by":"crossref","first-page":"17141","DOI":"10.1039\/D4NR01343C","article-title":"Interaction of full-length tau with negatively charged lipid membranes leads to polymorphic aggregates","volume":"16","author":"Ury-Thiery","year":"2024","journal-title":"Nanoscale"},{"key":"10.1016\/j.bpc.2026.107626_bb0265","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1038\/nrm2330","article-title":"Membrane lipids: where they are and how they behave","volume":"9","author":"van Meer","year":"2008","journal-title":"Nat. Rev. Mol. Cell Biol."},{"issue":"18","key":"10.1016\/j.bpc.2026.107626_bb0270","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2421391122","article-title":"Water-directed pinning is key to tau prion formation","volume":"122","author":"Vigers","year":"2025","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bpc.2026.107626_bb0275","first-page":"2181","article-title":"Free fatty acids stimulate the polymerization of tau and amyloid beta peptides. In vitro evidence for a common effector of pathogenesis in Alzheimers disease","volume":"150","author":"Wilson","year":"1997","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.bpc.2026.107626_bb0280","doi-asserted-by":"crossref","first-page":"1359","DOI":"10.1016\/S0006-3495(01)76109-7","article-title":"Amyloid-\u03b2 peptide assembly: a critical step in fibrillogenesis and membrane disruption","volume":"80","author":"Yip","year":"2001","journal-title":"Biophys. J."},{"key":"10.1016\/j.bpc.2026.107626_bb0285","doi-asserted-by":"crossref","first-page":"1436","DOI":"10.1016\/j.bbamem.2006.03.021","article-title":"Alpha-helical antimicrobial peptides\u2014using a sequence template to guide structure\u2013activity relationship studies","volume":"1758","author":"Zelezetsky","year":"2006","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"10.1016\/j.bpc.2026.107626_bb0290","doi-asserted-by":"crossref","DOI":"10.1016\/j.colsurfb.2020.111353","article-title":"Effect of cholesterol on the fluidity of supported lipid bilayers","volume":"196","author":"Zhang","year":"2020","journal-title":"Colloids Surf. B: Biointerfaces"},{"issue":"9","key":"10.1016\/j.bpc.2026.107626_bb0295","doi-asserted-by":"crossref","DOI":"10.3390\/ijms25094969","article-title":"The enigma of tau protein aggregation: mechanistic insights and future challenges","volume":"25","author":"Zheng","year":"2024","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.bpc.2026.107626_bib296","doi-asserted-by":"crossref","first-page":"3783","DOI":"10.1529\/biophysj.103.036681","article-title":"Investigation of temperature-induced phase transitions in DOPC and DPPC phospholipid bilayers using temperature-controlled scanning force microscopy","volume":"86","author":"Leonenko","year":"2004","journal-title":"Biophys. J."},{"issue":"43","key":"10.1016\/j.bpc.2026.107626_bib297","doi-asserted-by":"crossref","first-page":"20857","DOI":"10.1039\/C9NR06361G","article-title":"Membrane domain modulation of A\u03b2 1\u201342 oligomer interactions with supported lipid bilayers: an atomic force microscopy investigation","volume":"11","author":"Azouz","year":"2019","journal-title":"Nanoscale"},{"key":"10.1016\/j.bpc.2026.107626_bib298","first-page":"86","article-title":"Lipid bilayers: phase behavior and nanomechanics","author":"Redondo-Morata","year":"2020","journal-title":"Memb. Biomechan."},{"issue":"1","key":"10.1016\/j.bpc.2026.107626_bib299","doi-asserted-by":"crossref","first-page":"L01","DOI":"10.1016\/j.bpj.2011.11.4001","article-title":"Direct measurement of the mechanical properties of lipid phases in supported bilayers","volume":"102","author":"Picas","year":"2012","journal-title":"Biophys. J."}],"container-title":["Biophysical Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0301462226000591?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0301462226000591?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,5,21]],"date-time":"2026-05-21T06:46:21Z","timestamp":1779345981000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0301462226000591"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,8]]},"references-count":63,"alternative-id":["S0301462226000591"],"URL":"https:\/\/doi.org\/10.1016\/j.bpc.2026.107626","relation":{},"ISSN":["0301-4622"],"issn-type":[{"value":"0301-4622","type":"print"}],"subject":[],"published":{"date-parts":[[2026,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Full-length Tau disrupts fluid zwitterionic supported lipid bilayers","name":"articletitle","label":"Article Title"},{"value":"Biophysical Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bpc.2026.107626","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 The Authors. Published by Elsevier B.V.","name":"copyright","label":"Copyright"}],"article-number":"107626"}}