{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T23:01:55Z","timestamp":1791241315331,"version":"4.1.0"},"reference-count":176,"publisher":"Elsevier BV","issue":"8","license":[{"start":{"date-parts":[[2022,8,1]],"date-time":"2022-08-01T00:00:00Z","timestamp":1659312000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2022,8,1]],"date-time":"2022-08-01T00:00:00Z","timestamp":1659312000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2022,6,4]],"date-time":"2022-06-04T00:00:00Z","timestamp":1654300800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2022,8]]},"DOI":"10.1016\/j.jbc.2022.102108","type":"journal-article","created":{"date-parts":[[2022,6,7]],"date-time":"2022-06-07T20:43:24Z","timestamp":1654634604000},"page":"102108","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":50,"title":["The association of lipids with amyloid fibrils"],"prefix":"10.1016","volume":"298","author":[{"given":"John M.","family":"Sanderson","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jbc.2022.102108_bib1","doi-asserted-by":"crossref","first-page":"1295","DOI":"10.1515\/BC.1999.165","article-title":"Prion rods contain an inert polysaccharide scaffold","volume":"380","author":"Appel","year":"1999","journal-title":"Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102108_bib2","doi-asserted-by":"crossref","DOI":"10.1016\/j.nbd.2021.105417","article-title":"Lewy body-associated proteins: victims, instigators, or innocent bystanders? The case of AIMP2 and alpha-synuclein","volume":"156","author":"Lashuel","year":"2021","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.jbc.2022.102108_bib3","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1177\/095952876705000105","article-title":"On the nature of the waxy, lardaceous, or amyloid deposit","volume":"50","author":"Dickinson","year":"1867","journal-title":"Med. Chir. Trans."},{"key":"10.1016\/j.jbc.2022.102108_bib4","doi-asserted-by":"crossref","first-page":"1663","DOI":"10.1016\/j.bbamem.2018.04.004","article-title":"Interactions between amyloid \u03b2 peptide and lipid membranes","volume":"1860","author":"Niu","year":"2018","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2022.102108_bib5","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1046\/j.1365-2141.2001.02999.x","article-title":"Amyloidosis: a convoluted story","volume":"114","author":"Kyle","year":"2001","journal-title":"Br. J. Haematol."},{"key":"10.1016\/j.jbc.2022.102108_bib6","first-page":"869","article-title":"The lipid content of amyloid fibrils purified by a variety of methods","volume":"50","author":"Kim","year":"1967","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.jbc.2022.102108_bib7","first-page":"1","article-title":"The chemical and immunochemical identity of amyloid","volume":"74","author":"Rimon","year":"1976","journal-title":"Curr. Top. Microbiol. Immunol."},{"key":"10.1016\/j.jbc.2022.102108_bib8","doi-asserted-by":"crossref","DOI":"10.1016\/j.chemphyslip.2020.105010","article-title":"The human islet amyloid polypeptide in protein misfolding disorders: mechanisms of aggregation and interaction with biomembranes","volume":"234","author":"Saghir","year":"2021","journal-title":"Chem. Phys. Lipids"},{"key":"10.1016\/j.jbc.2022.102108_bib9","doi-asserted-by":"crossref","first-page":"E27","DOI":"10.3390\/cells8010027","article-title":"The role of lipids in Parkinson\u2019s disease","volume":"8","author":"Xicoy","year":"2019","journal-title":"Cells"},{"key":"10.1016\/j.jbc.2022.102108_bib10","doi-asserted-by":"crossref","first-page":"2545","DOI":"10.1021\/acs.chemrev.0c01122","article-title":"Amyloid oligomers: a joint experimental\/computational perspective on Alzheimer\u2019s disease, Parkinson\u2019s disease, type II diabetes, and amyotrophic lateral sclerosis","volume":"121","author":"Nguyen","year":"2021","journal-title":"Chem. Rev."},{"key":"10.1016\/j.jbc.2022.102108_bib11","doi-asserted-by":"crossref","first-page":"1520","DOI":"10.1016\/j.bpj.2009.12.4304","article-title":"Phospholipid composition of membranes directs prions down alternative aggregation pathways","volume":"98","author":"Robinson","year":"2010","journal-title":"Biophys. J."},{"key":"10.1016\/j.jbc.2022.102108_bib12","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1038\/nchembio.1750","article-title":"Lipid vesicles trigger \u03b1-synuclein aggregation by stimulating primary nucleation","volume":"11","author":"Galvagnion","year":"2015","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.jbc.2022.102108_bib13","doi-asserted-by":"crossref","first-page":"13324","DOI":"10.1038\/s41598-020-70208-6","article-title":"Lipid membrane templated misfolding and self-assembly of intrinsically disordered tau protein","volume":"10","author":"Majewski","year":"2020","journal-title":"Sci. Rep."},{"key":"10.1016\/j.jbc.2022.102108_bib14","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1007\/978-3-319-17344-3_6","article-title":"Interactions of lipid membranes with fibrillar protein aggregates","volume":"855","author":"Gorbenko","year":"2015","journal-title":"Adv. Exp. Med. Biol."},{"key":"10.1016\/j.jbc.2022.102108_bib15","doi-asserted-by":"crossref","first-page":"7226","DOI":"10.1523\/JNEUROSCI.21-18-07226.2001","article-title":"A\u00a0novel action of Alzheimer\u2019s amyloid \u03b2-protein (A\u03b2): oligomeric A\u03b2 promotes lipid release","volume":"21","author":"Michikawa","year":"2001","journal-title":"J.\u00a0Neurosci."},{"key":"10.1016\/j.jbc.2022.102108_bib16","doi-asserted-by":"crossref","first-page":"8285","DOI":"10.1021\/acs.chemrev.1c00196","article-title":"Amyloid-type protein aggregation and prion-like properties of amyloids","volume":"121","author":"Willbold","year":"2021","journal-title":"Chem. Rev."},{"key":"10.1016\/j.jbc.2022.102108_bib17","doi-asserted-by":"crossref","first-page":"a023572","DOI":"10.1101\/cshperspect.a023572","article-title":"The three-dimensional structures of amyloids","volume":"9","author":"Riek","year":"2017","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"10.1016\/j.jbc.2022.102108_bib18","doi-asserted-by":"crossref","first-page":"1965","DOI":"10.1021\/acschemneuro.0c00166","article-title":"Comparison of synthetic neuronal model membrane mimics in amyloid aggregation at atomic resolution","volume":"11","author":"Bera","year":"2020","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.jbc.2022.102108_bib19","doi-asserted-by":"crossref","first-page":"1567","DOI":"10.1002\/pro.3674","article-title":"\u03b2-Amyloid aggregation and heterogeneous nucleation","volume":"28","author":"Srivastava","year":"2019","journal-title":"Protein Sci."},{"key":"10.1016\/j.jbc.2022.102108_bib20","doi-asserted-by":"crossref","first-page":"E1195","DOI":"10.3390\/molecules25051195","article-title":"Structure and aggregation mechanisms in amyloids","volume":"25","author":"Almeida","year":"2020","journal-title":"Molecules"},{"key":"10.1016\/j.jbc.2022.102108_bib21","doi-asserted-by":"crossref","first-page":"3946","DOI":"10.1039\/C8CS00034D","article-title":"Effects of in\u00a0vivo conditions on amyloid aggregation","volume":"48","author":"Owen","year":"2019","journal-title":"Chem. Soc. Rev."},{"key":"10.1016\/j.jbc.2022.102108_bib22","doi-asserted-by":"crossref","first-page":"E144","DOI":"10.3390\/life10080144","article-title":"Amyloidogenic intrinsically disordered proteins: new insights into their self-assembly and their interaction with membranes","volume":"10","author":"Scollo","year":"2020","journal-title":"Life"},{"key":"10.1016\/j.jbc.2022.102108_bib23","doi-asserted-by":"crossref","first-page":"5473","DOI":"10.1039\/C9CS00199A","article-title":"Half a century of amyloids: past, present and future","volume":"49","author":"Ke","year":"2020","journal-title":"Chem. Soc. Rev."},{"key":"10.1016\/j.jbc.2022.102108_bib24","doi-asserted-by":"crossref","first-page":"13447","DOI":"10.1021\/bi0611107","article-title":"Characteristics of fibers formed by cytochrome c and induced by anionic phospholipids","volume":"45","author":"Alakoskela","year":"2006","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2022.102108_bib25","doi-asserted-by":"crossref","first-page":"4726","DOI":"10.1529\/biophysj.108.134379","article-title":"Pinched multilamellar structure of aggregates of lysozyme and phosphatidylserine-containing membranes revealed by FRET","volume":"95","author":"Coutinho","year":"2008","journal-title":"Biophys. J."},{"key":"10.1016\/j.jbc.2022.102108_bib26","doi-asserted-by":"crossref","first-page":"E881","DOI":"10.3390\/biom10060881","article-title":"Fibrillization of 40-residue \u03b2-amyloid peptides in membrane-like environments leads to different fibril structures and reduced molecular polymorphisms","volume":"10","author":"Cheng","year":"2020","journal-title":"Biomolecules"},{"key":"10.1016\/j.jbc.2022.102108_bib27","doi-asserted-by":"crossref","first-page":"1652","DOI":"10.1016\/j.bbamem.2018.03.004","article-title":"Cause and consequence of A\u03b2 \u2013 lipid interactions in Alzheimer disease pathogenesis","volume":"1860","author":"Rangachari","year":"2018","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2022.102108_bib28","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1146\/annurev.biophys.050708.133622","article-title":"The interplay of catalysis and toxicity by amyloid intermediates on lipid bilayers: insights from type II diabetes","volume":"38","author":"Hebda","year":"2009","journal-title":"Annu. Rev. Biophys."},{"key":"10.1016\/j.jbc.2022.102108_bib29","doi-asserted-by":"crossref","first-page":"1863","DOI":"10.1016\/j.bbamem.2018.04.011","article-title":"Membranes as modulators of amyloid protein misfolding and target of toxicity","volume":"1860","author":"Rawat","year":"2018","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2022.102108_bib30","doi-asserted-by":"crossref","first-page":"1897","DOI":"10.1016\/j.bbamem.2015.01.018","article-title":"Interactions between misfolded protein oligomers and membranes: a central topic in neurodegenerative diseases","volume":"1848","author":"Andreasen","year":"2015","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2022.102108_bib31","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1007\/s12013-008-9033-4","article-title":"Disordered proteins: biological membranes as two-dimensional aggregation matrices","volume":"52","author":"Bystr\u00f6m","year":"2008","journal-title":"Cell Biochem. Biophys."},{"key":"10.1016\/j.jbc.2022.102108_bib32","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1111\/jnc.15025","article-title":"The lipid component of Alzheimer\u2019s disease research: an editorial highlight for \u201cBrain region-specific amyloid plaque-associated myelin lipid loss, APOE deposition and disruption of the myelin sheath in familial Alzheimer\u2019s disease mice\u201d on page 84","volume":"154","author":"Munter","year":"2020","journal-title":"J.\u00a0Neurochem."},{"key":"10.1016\/j.jbc.2022.102108_bib33","doi-asserted-by":"crossref","first-page":"2285","DOI":"10.1021\/acs.biochem.1c00308","article-title":"Site-specific alkylation of the islet amyloid polypeptide accelerates self-assembly and potentiates perturbation of lipid membranes","volume":"60","author":"Babych","year":"2021","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2022.102108_bib34","doi-asserted-by":"crossref","first-page":"5862","DOI":"10.1074\/jbc.M608126200","article-title":"Effect of 4-hydroxy-2-nonenal modification on alpha-synuclein aggregation","volume":"282","author":"Qin","year":"2007","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102108_bib35","doi-asserted-by":"crossref","DOI":"10.1002\/bies.201900147","article-title":"Far from inert: membrane lipids possess intrinsic reactivity that has consequences for cell biology","volume":"42","author":"Sanderson","year":"2020","journal-title":"BioEssays"},{"key":"10.1016\/j.jbc.2022.102108_bib36","doi-asserted-by":"crossref","first-page":"19284","DOI":"10.1523\/JNEUROSCI.2542-13.2013","article-title":"Membrane-anchored A\u03b2 accelerates amyloid formation and exacerbates amyloid-associated toxicity in mice","volume":"33","author":"Nagarathinam","year":"2013","journal-title":"J.\u00a0Neurosci."},{"key":"10.1016\/j.jbc.2022.102108_bib37","doi-asserted-by":"crossref","first-page":"673","DOI":"10.1038\/s41557-018-0031-x","article-title":"Cholesterol catalyses A\u03b242 aggregation through a heterogeneous nucleation pathway in the presence of lipid membranes","volume":"10","author":"Habchi","year":"2018","journal-title":"Nat. Chem."},{"key":"10.1016\/j.jbc.2022.102108_bib38","doi-asserted-by":"crossref","first-page":"6236","DOI":"10.1039\/C9SC06501F","article-title":"Identification of on- and off-pathway oligomers in amyloid fibril formation","volume":"11","author":"Dear","year":"2020","journal-title":"Chem. Sci."},{"key":"10.1016\/j.jbc.2022.102108_bib39","doi-asserted-by":"crossref","first-page":"S567","DOI":"10.3233\/JAD-179941","article-title":"The amyloid-\u03b2 oligomer hypothesis: beginning of the third decade","volume":"64","author":"Cline","year":"2018","journal-title":"J.\u00a0Alzheimer\u2019s Dis."},{"key":"10.1016\/j.jbc.2022.102108_bib40","doi-asserted-by":"crossref","first-page":"491","DOI":"10.2337\/diabetes.48.3.491","article-title":"The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles","volume":"48","author":"Janson","year":"1999","journal-title":"Diabetes"},{"key":"10.1016\/j.jbc.2022.102108_bib41","doi-asserted-by":"crossref","first-page":"6033","DOI":"10.1073\/pnas.0708354105","article-title":"Membrane damage by human islet amyloid polypeptide through fibril growth at the membrane","volume":"105","author":"Engel","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2022.102108_bib42","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1210\/er.2007-0037","article-title":"Islet amyloid in type 2 diabetes, and the toxic oligomer hypothesis","volume":"29","author":"Haataja","year":"2008","journal-title":"Endocr. Rev."},{"key":"10.1016\/j.jbc.2022.102108_bib43","doi-asserted-by":"crossref","first-page":"3614","DOI":"10.1111\/j.1742-4658.2006.05367.x","article-title":"The aggregation potential of human amylin determines its cytotoxicity towards islet beta-cells","volume":"273","author":"Konarkowska","year":"2006","journal-title":"FEBS J."},{"key":"10.1016\/j.jbc.2022.102108_bib44","doi-asserted-by":"crossref","first-page":"71","DOI":"10.3390\/biom7040071","article-title":"Why are functional amyloids non-toxic in humans","volume":"7","author":"Jackson","year":"2017","journal-title":"Biomolecules"},{"key":"10.1016\/j.jbc.2022.102108_bib45","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1016\/j.jmb.2007.11.077","article-title":"Islet amyloid polypeptide forms rigid lipid-protein amyloid fibrils on supported phospholipid bilayers","volume":"376","author":"Domanov","year":"2008","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.jbc.2022.102108_bib46","doi-asserted-by":"crossref","first-page":"10302","DOI":"10.1021\/bi049002c","article-title":"formation of amyloid fibers triggered by phosphatidylserine-containing membranes","volume":"43","author":"Zhao","year":"2004","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2022.102108_bib47","doi-asserted-by":"crossref","first-page":"1547","DOI":"10.1002\/cphc.202100124","article-title":"The role of amyloid \u03b2-Biomembrane interactions in the pathogenesis of Alzheimer\u2019s disease: insights from liposomes as membrane models","volume":"22","author":"Andrade","year":"2021","journal-title":"ChemPhysChem"},{"key":"10.1016\/j.jbc.2022.102108_bib48","doi-asserted-by":"crossref","first-page":"105062","DOI":"10.1016\/j.chemphyslip.2021.105062","article-title":"Exploring interactions between lipids and amyloid-forming proteins: a review on applying fluorescence and NMR techniques","volume":"236","author":"Chang","year":"2021","journal-title":"Chem. Phys. Lipids"},{"key":"10.1016\/j.jbc.2022.102108_bib49","doi-asserted-by":"crossref","first-page":"9188","DOI":"10.1039\/B925228B","article-title":"Formation of lipid\/peptide tubules by IAPP and temporin B on supported lipid membranes","volume":"11","author":"Kinnunen","year":"2015","journal-title":"Soft Matter"},{"key":"10.1016\/j.jbc.2022.102108_bib50","doi-asserted-by":"crossref","first-page":"9108","DOI":"10.1021\/bi050497v","article-title":"Oxidation of low-density lipoproteins induces amyloid-like structures that are recognized by macrophages","volume":"44","author":"Stewart","year":"2005","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2022.102108_bib51","doi-asserted-by":"crossref","first-page":"743","DOI":"10.1515\/revneuro-2020-0013","article-title":"The role of exosome lipids in central nervous system diseases","volume":"31","author":"Wang","year":"2020","journal-title":"Rev. Neurosci."},{"key":"10.1016\/j.jbc.2022.102108_bib52","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1016\/j.jprot.2017.10.003","article-title":"Comprehensive proteomic profiles of mouse AApoAII amyloid fibrils provide insights into the involvement of lipoproteins in the pathology of amyloidosis","volume":"172","author":"Miyahara","year":"2018","journal-title":"J.\u00a0Proteomics"},{"key":"10.1016\/j.jbc.2022.102108_bib53","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1186\/s40478-020-01091-5","article-title":"Label-free vibrational imaging of different A\u03b2 plaque types in Alzheimer\u2019s disease reveals sequential events in plaque development","volume":"8","author":"R\u00f6hr","year":"2020","journal-title":"Acta Neuropathol. Commun."},{"key":"10.1016\/j.jbc.2022.102108_bib54","doi-asserted-by":"crossref","DOI":"10.1038\/srep13489","article-title":"Plaque-associated lipids in Alzheimer\u2019s diseased brain tissue visualized by nonlinear microscopy","volume":"5","author":"Kiskis","year":"2015","journal-title":"Sci. Rep."},{"key":"10.1016\/j.jbc.2022.102108_bib55","doi-asserted-by":"crossref","first-page":"723","DOI":"10.1093\/jnen\/59.8.723","article-title":"Amyloid beta protein (Abeta) starts to deposit as plasma membrane-bound form in diffuse plaques of brains from hereditary cerebral hemorrhage with amyloidosis-Dutch type, Alzheimer disease and nondemented aged subjects","volume":"59","author":"Yamaguchi","year":"2000","journal-title":"J.\u00a0Neuropathol. Exp. Neurol."},{"key":"10.1016\/j.jbc.2022.102108_bib56","doi-asserted-by":"crossref","first-page":"9742","DOI":"10.1038\/s41598-020-66129-z","article-title":"Three-dimensional real time imaging of amyloid \u03b2 aggregation on living cells","volume":"10","author":"Kuragano","year":"2020","journal-title":"Sci. Rep."},{"key":"10.1016\/j.jbc.2022.102108_bib57","doi-asserted-by":"crossref","first-page":"1062","DOI":"10.1038\/nm1095-1062","article-title":"GM1 ganglioside-bound amyloid beta-protein (A beta): a possible form of preamyloid in Alzheimer\u2019s disease","volume":"1","author":"Yanagisawa","year":"1995","journal-title":"Nat. Med."},{"key":"10.1016\/j.jbc.2022.102108_bib58","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1111\/jnc.15216","article-title":"Spatially resolved mass spectrometry analysis of amyloid plaque-associated lipids","volume":"159","author":"Blank","year":"2020","journal-title":"J.\u00a0Neurochem."},{"key":"10.1016\/j.jbc.2022.102108_bib59","doi-asserted-by":"crossref","first-page":"4107","DOI":"10.1021\/acs.biochem.7b00262","article-title":"A\u00a0multimodal spectroscopic imaging method to characterize the metal and macromolecular content of proteinaceous aggregates (\u201dAmyloid plaques\u201d)","volume":"56","author":"Summers","year":"2017","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2022.102108_bib60","doi-asserted-by":"crossref","first-page":"3991","DOI":"10.1039\/c3an00295k","article-title":"Synchrotron FTIR reveals lipid around and within amyloid plaques in transgenic mice and Alzheimer\u2019s disease brain","volume":"138","author":"Liao","year":"2013","journal-title":"Analyst"},{"key":"10.1016\/j.jbc.2022.102108_bib61","doi-asserted-by":"crossref","first-page":"629","DOI":"10.1021\/acschemneuro.6b00362","article-title":"Iron, Copper, and Zinc concentration in A\u03b2 plaques in the APP\/PS1 mouse model of Alzheimer\u2019s disease correlates with metal levels in the surrounding neuropil","volume":"8","author":"James","year":"2017","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.jbc.2022.102108_bib62","doi-asserted-by":"crossref","first-page":"729","DOI":"10.1006\/jmbi.1997.1348","article-title":"Common core structure of amyloid fibrils by synchrotron X-ray diffraction","volume":"273","author":"Sunde","year":"1997","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.jbc.2022.102108_bib63","doi-asserted-by":"crossref","first-page":"173","DOI":"10.3109\/13506129509036922","article-title":"Structural studies on FAP fibrils: removal of contaminants is essential for the interpretation of X-ray data","volume":"2","author":"Damas","year":"1995","journal-title":"Amyloid: J. Protein Folding Disorders"},{"key":"10.1016\/j.jbc.2022.102108_bib64","doi-asserted-by":"crossref","first-page":"5371","DOI":"10.1039\/c2ob07113d","article-title":"The innate reactivity of a membrane associated peptide towards lipids: acyl transfer to melittin without enzyme catalysis","volume":"10","author":"Dods","year":"2012","journal-title":"Org. Biomol. Chem."},{"key":"10.1016\/j.jbc.2022.102108_bib65","doi-asserted-by":"crossref","first-page":"4379","DOI":"10.1016\/j.jmb.2013.07.013","article-title":"Acyl transfer from membrane lipids to peptides is a generic process","volume":"425","author":"Dods","year":"2013","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.jbc.2022.102108_bib66","doi-asserted-by":"crossref","first-page":"6297","DOI":"10.1073\/pnas.0407035102","article-title":"Raft lipids as common components of human extracellular amyloid fibrils","volume":"102","author":"Gellermann","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2022.102108_bib67","doi-asserted-by":"crossref","first-page":"1267","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.jbc.2022.102108_bib68","doi-asserted-by":"crossref","first-page":"11172","DOI":"10.1073\/pnas.0603838103","article-title":"Alzheimer\u2019s disease beta-amyloid peptides are released in association with exosomes","volume":"103","author":"Rajendran","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2022.102108_bib69","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1038\/s41586-020-2043-0","article-title":"Novel tau filament fold in corticobasal degeneration","volume":"580","author":"Zhang","year":"2020","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2022.102108_bib70","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1038\/nature23002","article-title":"Cryo-EM structures of tau filaments from Alzheimer\u2019s disease","volume":"547","author":"Fitzpatrick","year":"2017","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2022.102108_bib71","doi-asserted-by":"crossref","first-page":"7566","DOI":"10.1074\/jbc.AC118.007195","article-title":"Amyloid-\u03b2 oligomers have a profound detergent-like effect on lipid membrane bilayers, imaged by atomic force and electron microscopy","volume":"294","author":"Bode","year":"2019","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102108_bib72","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1016\/j.ab.2015.04.014","article-title":"Uptake of raft components into amyloid \u03b2-peptide aggregates and membrane damage","volume":"481","author":"Sasahara","year":"2015","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.jbc.2022.102108_bib73","doi-asserted-by":"crossref","first-page":"266","DOI":"10.1016\/j.bbamem.2014.04.011","article-title":"Fibrillation of \u03b2 amyloid peptides in the presence of phospholipid bilayers and the consequent membrane disruption","volume":"1848","author":"Qiang","year":"2015","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2022.102108_bib74","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1002\/9780470034590.emrstm1410","article-title":"Solid-state NMR studies of the membrane disruption induced by the \u03b2 amyloid peptides: perspective and difficulties","volume":"4","author":"Qiang","year":"2015","journal-title":"eMagRes"},{"key":"10.1016\/j.jbc.2022.102108_bib75","doi-asserted-by":"crossref","first-page":"759","DOI":"10.1016\/j.jmb.2005.11.091","article-title":"Amyloid-beta peptide disruption of lipid membranes and the effect of metal ions","volume":"356","author":"Lau","year":"2006","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.jbc.2022.102108_bib76","doi-asserted-by":"crossref","first-page":"eaaz8598","DOI":"10.1126\/sciadv.aaz8598","article-title":"Lysis of membrane lipids promoted by small organic molecules: reactivity depends on structure but not lipophilicity","volume":"6","author":"Britt","year":"2020","journal-title":"Sci. Adv."},{"key":"10.1016\/j.jbc.2022.102108_bib77","doi-asserted-by":"crossref","first-page":"1059","DOI":"10.1016\/j.bpj.2012.01.039","article-title":"How type II diabetes-related islet amyloid polypeptide damages lipid bilayers","volume":"102","author":"Lee","year":"2012","journal-title":"Biophys. J."},{"key":"10.1016\/j.jbc.2022.102108_bib78","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/j.febslet.2004.09.075","article-title":"Islet amyloid polypeptide-induced membrane leakage involves uptake of lipids by forming amyloid fibers","volume":"577","author":"Sparr","year":"2004","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jbc.2022.102108_bib79","doi-asserted-by":"crossref","first-page":"2026","DOI":"10.1016\/j.bbamem.2007.07.001","article-title":"Membrane fragmentation by an amyloidogenic fragment of human Islet Amyloid Polypeptide detected by solid-state NMR spectroscopy of membrane nanotubes","volume":"1768","author":"Brender","year":"2007","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2022.102108_bib80","doi-asserted-by":"crossref","first-page":"9155","DOI":"10.1039\/c3cc44880k","article-title":"Membrane destabilization by monomeric hIAPP observed by imaging fluorescence correlation spectroscopy","volume":"49","author":"Bag","year":"2013","journal-title":"Chem. Commun."},{"key":"10.1016\/j.jbc.2022.102108_bib81","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/j.bpj.2012.11.3811","article-title":"Cations as switches of amyloid-mediated membrane disruption mechanisms: calcium and IAPP","volume":"104","author":"Sciacca","year":"2013","journal-title":"Biophys. J."},{"key":"10.1016\/j.jbc.2022.102108_bib82","doi-asserted-by":"crossref","first-page":"4131","DOI":"10.1002\/smll.201500562","article-title":"Nanoscale heterogeneity of the molecular structure of individual hIAPP amyloid fibrils revealed with tip-enhanced Raman spectroscopy","volume":"11","author":"vandenAkker","year":"2015","journal-title":"Small"},{"key":"10.1016\/j.jbc.2022.102108_bib83","doi-asserted-by":"crossref","first-page":"1439","DOI":"10.1016\/j.febslet.2009.03.059","article-title":"Fluorescence microscopy studies on islet amyloid polypeptide fibrillation at heterogeneous and cellular membrane interfaces and its inhibition by resveratrol","volume":"583","author":"Radovan","year":"2009","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jbc.2022.102108_bib84","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1001\/archneur.1969.00480180071006","article-title":"Sphingomyelin in Lewy inclusion bodies in Parkinson\u2019s disease","volume":"21","author":"den Jager","year":"1969","journal-title":"Arch. Neurol."},{"key":"10.1016\/j.jbc.2022.102108_bib85","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1006\/exnr.2000.7527","article-title":"In situ and in\u00a0vitro study of colocalization and segregation of \u03b1-synuclein, Ubiquitin, and lipids in Lewy bodies","volume":"166","author":"Gai","year":"2000","journal-title":"Exp. Neurol."},{"key":"10.1016\/j.jbc.2022.102108_bib86","doi-asserted-by":"crossref","first-page":"1099","DOI":"10.1038\/s41593-019-0423-2","article-title":"Lewy pathology in Parkinson\u2019s disease consists of crowded organelles and lipid membranes","volume":"22","author":"Shahmoradian","year":"2019","journal-title":"Nat. Neurosci."},{"key":"10.1016\/j.jbc.2022.102108_bib87","doi-asserted-by":"crossref","first-page":"4971","DOI":"10.1073\/pnas.1913904117","article-title":"The process of Lewy body formation, rather than simply \u03b1-synuclein fibrillization, is one of the major drivers of neurodegeneration","volume":"117","author":"Mahul-Mellier","year":"2020","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2022.102108_bib88","doi-asserted-by":"crossref","first-page":"2110","DOI":"10.1038\/s41467-021-22108-0","article-title":"In situ architecture of neuronal \u03b1-Synuclein inclusions","volume":"12","author":"Trinkaus","year":"2021","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2022.102108_bib89","doi-asserted-by":"crossref","DOI":"10.1016\/j.nbd.2020.104876","article-title":"Do Lewy bodies contain alpha-synuclein fibrils? And does it matter? A brief history and critical analysis of recent reports","volume":"141","author":"Lashuel","year":"2020","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.jbc.2022.102108_bib90","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1074\/jbc.M107045200","article-title":"Membrane-bound alpha-synuclein has a high aggregation propensity and the ability to seed the aggregation of the cytosolic form","volume":"277","author":"Lee","year":"2002","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102108_bib91","doi-asserted-by":"crossref","first-page":"359","DOI":"10.3233\/JPD-2011-11067","article-title":"Membrane interaction of \u03b1-synuclein in different aggregation states","volume":"1","author":"Grey","year":"2011","journal-title":"J.\u00a0Parkinson\u2019s Dis."},{"key":"10.1016\/j.jbc.2022.102108_bib92","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0077235","article-title":"Membrane lipid co-aggregation with \u03b1-synuclein fibrils","volume":"8","author":"Hellstrand","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.jbc.2022.102108_bib93","doi-asserted-by":"crossref","first-page":"1620","DOI":"10.1002\/cphc.201700050","article-title":"Direct visualization of model membrane remodeling by \u03b1-synuclein fibrillization","volume":"18","author":"Chaudhary","year":"2017","journal-title":"ChemPhysChem"},{"key":"10.1016\/j.jbc.2022.102108_bib94","doi-asserted-by":"crossref","first-page":"4457","DOI":"10.1016\/j.febslet.2014.10.016","article-title":"Membrane interactions and fibrillization of \u03b1-synuclein play an essential role in membrane disruption","volume":"588","author":"Chaudhary","year":"2014","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jbc.2022.102108_bib95","doi-asserted-by":"crossref","first-page":"19366","DOI":"10.1021\/ja2029848","article-title":"Mechanism of membrane interaction and disruption by \u03b1-synuclein","volume":"133","author":"Reynolds","year":"2011","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.jbc.2022.102108_bib96","doi-asserted-by":"crossref","first-page":"7872","DOI":"10.1021\/acs.jpclett.9b03005","article-title":"Lipid dynamics and phase transition within \u03b1-synuclein amyloid fibrils","volume":"10","author":"Galvagnion","year":"2019","journal-title":"J.\u00a0Phys. Chem. Lett."},{"key":"10.1016\/j.jbc.2022.102108_bib97","doi-asserted-by":"crossref","first-page":"9741","DOI":"10.1073\/pnas.0702662104","article-title":"Formation of native prions from minimal components in\u00a0vitro","volume":"104","author":"Deleault","year":"2007","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2022.102108_bib98","doi-asserted-by":"crossref","first-page":"655","DOI":"10.1515\/bchm.1998.379.6.655","article-title":"Prion rods contain small amounts of two host sphingolipids as revealed by thin-layer chromatography and mass spectrometry","volume":"379","author":"Klein","year":"1998","journal-title":"Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102108_bib99","doi-asserted-by":"crossref","first-page":"8460","DOI":"10.1074\/jbc.RA119.012348","article-title":"Native nanodiscs formed by styrene maleic acid copolymer derivatives help recover infectious prion multimers bound to brain-derived lipids","volume":"295","author":"Esmaili","year":"2020","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102108_bib100","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1016\/j.chemphyslip.2006.02.022","article-title":"The role of rafts in the fibrillization and aggregation of prions","volume":"141","author":"Pinheiro","year":"2006","journal-title":"Chem. Phys. Lipids"},{"key":"10.1016\/j.jbc.2022.102108_bib101","doi-asserted-by":"crossref","first-page":"2422","DOI":"10.1016\/j.bbamem.2015.07.014","article-title":"Membrane-mediated amyloid formation of PrP 106-126: a kinetic study","volume":"1848","author":"Sun","year":"2015","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2022.102108_bib102","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1016\/j.bbrc.2013.07.104","article-title":"Shadoo binds lipid membranes and undergoes aggregation and fibrillization","volume":"438","author":"Li","year":"2013","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.jbc.2022.102108_bib103","doi-asserted-by":"crossref","DOI":"10.1038\/srep29096","article-title":"In situ characterization of protein aggregates in human tissues affected by light chain amyloidosis: A FTIR microspectroscopy study","volume":"6","author":"Ami","year":"2016","journal-title":"Sci. Rep."},{"key":"10.1016\/j.jbc.2022.102108_bib104","doi-asserted-by":"crossref","first-page":"696","DOI":"10.1111\/j.1471-4159.2010.07000.x","article-title":"FRET studies of lipid-protein aggregates related to amyloid-like fibers","volume":"116","author":"Coutinho","year":"2011","journal-title":"J.\u00a0Neurochem."},{"key":"10.1016\/j.jbc.2022.102108_bib105","doi-asserted-by":"crossref","first-page":"840","DOI":"10.1039\/C3SM52586D","article-title":"Electrostatically driven lipid-lysozyme mixed fibers display a multilamellar structure without amyloid features","volume":"10","author":"Melo","year":"2014","journal-title":"Soft Matter"},{"key":"10.1016\/j.jbc.2022.102108_bib106","doi-asserted-by":"crossref","first-page":"2906","DOI":"10.1021\/jp310396v","article-title":"Fluorescence detection of lipid-induced oligomeric intermediates involved in lysozyme \u201camyloid-like\u201d fiber formation driven by anionic membranes","volume":"117","author":"Melo","year":"2013","journal-title":"J.\u00a0Phys. Chem. B"},{"key":"10.1016\/j.jbc.2022.102108_bib107","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1007\/s00249-006-0105-3","article-title":"The bovine seminal plasma protein PDC-109 extracts phosphorylcholine-containing lipids from the outer membrane leaflet","volume":"36","author":"Tannert","year":"2007","journal-title":"Eur. Biophys. J."},{"key":"10.1016\/j.jbc.2022.102108_bib108","doi-asserted-by":"crossref","first-page":"924","DOI":"10.1016\/j.bpj.2020.07.029","article-title":"Rapid formation of peptide\/lipid coaggregates by the amyloidogenic seminal peptide PAP248-286","volume":"119","author":"Vane","year":"2020","journal-title":"Biophys. J."},{"key":"10.1016\/j.jbc.2022.102108_bib109","doi-asserted-by":"crossref","first-page":"1199","DOI":"10.1007\/s10895-008-0378-2","article-title":"Thioflavin T displays enhanced fluorescence selectively inside anionic micelles and mammalian cells","volume":"18","author":"Kumar","year":"2008","journal-title":"J.\u00a0Fluoresc."},{"key":"10.1016\/j.jbc.2022.102108_bib110","doi-asserted-by":"crossref","first-page":"9579","DOI":"10.1021\/bi201192r","article-title":"NBD-labeled phospholipid accelerates apolipoprotein C-II amyloid fibril formation but is not incorporated into mature fibrils","volume":"50","author":"Ryan","year":"2011","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2022.102108_bib111","doi-asserted-by":"crossref","first-page":"7443","DOI":"10.1073\/pnas.0812033106","article-title":"Seeded growth of beta-amyloid fibrils from Alzheimer\u2019s brain-derived fibrils produces a distinct fibril structure","volume":"106","author":"Paravastu","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2022.102108_bib112","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1038\/nature20814","article-title":"Structural variation in amyloid-\u03b2 fibrils from Alzheimer\u2019s disease clinical subtypes","volume":"541","author":"Qiang","year":"2017","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2022.102108_bib113","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1038\/s41589-020-00708-z","article-title":"Hierarchical chemical determination of amyloid polymorphs in neurodegenerative disease","volume":"17","author":"Li","year":"2021","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.jbc.2022.102108_bib114","doi-asserted-by":"crossref","DOI":"10.1016\/j.neuint.2021.105208","article-title":"Aggregation and structure of amyloid \u03b2-protein","volume":"151","author":"Ono","year":"2021","journal-title":"Neurochem. Int."},{"key":"10.1016\/j.jbc.2022.102108_bib115","doi-asserted-by":"crossref","first-page":"464","DOI":"10.1038\/s41586-020-2317-6","article-title":"Structures of \u03b1-synuclein filaments from multiple system atrophy","volume":"585","author":"Schweighauser","year":"2020","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2022.102108_bib116","doi-asserted-by":"crossref","first-page":"1419","DOI":"10.3390\/biom11101419","article-title":"Structural and functional insights into \u03b1-synuclein fibril polymorphism","volume":"11","author":"Mehra","year":"2021","journal-title":"Biomolecules"},{"key":"10.1016\/j.jbc.2022.102108_bib117","doi-asserted-by":"crossref","first-page":"724","DOI":"10.1038\/s41594-021-00646-x","article-title":"Cryo-EM structures of hIAPP fibrils seeded by patient-extracted fibrils reveal new polymorphs and conserved fibril cores","volume":"28","author":"Cao","year":"2021","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.jbc.2022.102108_bib118","doi-asserted-by":"crossref","first-page":"4822","DOI":"10.1002\/anie.201511524","article-title":"Polymorphism of amyloid fibrils in\u00a0vivo","volume":"55","author":"Annamalai","year":"2016","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"10.1016\/j.jbc.2022.102108_bib119","doi-asserted-by":"crossref","first-page":"5604","DOI":"10.1073\/pnas.1523496113","article-title":"Electron tomography reveals the fibril structure and lipid interactions in amyloid deposits","volume":"113","author":"Kollmer","year":"2016","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2022.102108_bib120","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1016\/j.sbi.2019.05.003","article-title":"Cryo-EM of amyloid fibrils and cellular aggregates","volume":"58","author":"Fitzpatrick","year":"2019","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.jbc.2022.102108_bib121","doi-asserted-by":"crossref","DOI":"10.1016\/j.jsb.2021.107792","article-title":"The role of the half-turn in determining structures of Alzheimer\u2019s A\u03b2 wild-type and mutants","volume":"213","author":"Hayward","year":"2021","journal-title":"J.\u00a0Struct. Biol."},{"key":"10.1016\/j.jbc.2022.102108_bib122","doi-asserted-by":"crossref","DOI":"10.3389\/fnagi.2021.782617","article-title":"Recent high-resolution structures of amyloids involved in neurodegenerative diseases","volume":"13","author":"Diaz-Espinoza","year":"2021","journal-title":"Front. Aging Neurosci."},{"key":"10.1016\/j.jbc.2022.102108_bib123","doi-asserted-by":"crossref","first-page":"360","DOI":"10.1038\/s41422-020-0299-4","article-title":"Cryo-EM structure of full-length \u03b1-synuclein amyloid fibril with Parkinson\u2019s disease familial A53T mutation","volume":"30","author":"Sun","year":"2020","journal-title":"Cell. Res."},{"key":"10.1016\/j.jbc.2022.102108_bib124","doi-asserted-by":"crossref","DOI":"10.3389\/fmolb.2020.582033","article-title":"Asparagine and glutamine side-chains and ladders in HET-s(218-289) amyloid fibrils studied by fast magic-angle spinning NMR","volume":"7","author":"Wiegand","year":"2020","journal-title":"Front. Mol. Biosci."},{"key":"10.1016\/j.jbc.2022.102108_bib125","doi-asserted-by":"crossref","first-page":"7425","DOI":"10.1039\/C4SM00907J","article-title":"Molecular understanding of a potential functional link between antimicrobial and amyloid peptides","volume":"10","author":"Zhang","year":"2014","journal-title":"Soft Matter"},{"key":"10.1016\/j.jbc.2022.102108_bib126","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1038\/s41594-017-0018-0","article-title":"Sub-\u00e5ngstr\u00f6m cryo-EM structure of a prion protofibril reveals a polar clasp","volume":"25","author":"Gallagher-Jones","year":"2018","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.jbc.2022.102108_bib127","doi-asserted-by":"crossref","first-page":"773","DOI":"10.1038\/nature03680","article-title":"Structure of the cross-beta spine of amyloid-like fibrils","volume":"435","author":"Nelson","year":"2005","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2022.102108_bib128","doi-asserted-by":"crossref","first-page":"999","DOI":"10.1002\/2211-5463.13110","article-title":"Seeded assembly in\u00a0vitro does not replicate the structures of \u03b1-synuclein filaments from multiple system atrophy","volume":"11","author":"L\u00f6vestam","year":"2021","journal-title":"FEBS Open Bio"},{"key":"10.1016\/j.jbc.2022.102108_bib129","doi-asserted-by":"crossref","first-page":"E4976","DOI":"10.1073\/pnas.1600749113","article-title":"Atomic-resolution structure of a disease-relevant A\u03b2(1-42) amyloid fibril","volume":"113","author":"W\u00e4lti","year":"2016","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2022.102108_bib130","doi-asserted-by":"crossref","first-page":"25272","DOI":"10.1073\/pnas.2002956117","article-title":"The role of fibril structure and surface hydrophobicity in secondary nucleation of amyloid fibrils","volume":"117","author":"Thacker","year":"2020","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2022.102108_bib131","doi-asserted-by":"crossref","first-page":"1923","DOI":"10.1016\/j.bbamem.2006.12.014","article-title":"Kinetics of amyloid formation and membrane interaction with amyloidogenic proteins","volume":"1768","author":"Murphy","year":"2007","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2022.102108_bib132","doi-asserted-by":"crossref","first-page":"8329","DOI":"10.1021\/acs.jpclett.0c01967","article-title":"Time-dependent lipid dynamics, organization and peptide-lipid interaction in phospholipid bilayers with incorporated \u03b2-amyloid oligomers","volume":"11","author":"Qiang","year":"2020","journal-title":"J.\u00a0Phys. Chem. Lett."},{"key":"10.1016\/j.jbc.2022.102108_bib133","doi-asserted-by":"crossref","first-page":"12233","DOI":"10.1074\/jbc.M116.720656","article-title":"Distinct membrane disruption pathways are induced by 40-residue \u03b2-amyloid peptides","volume":"291","author":"Delgado","year":"2016","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102108_bib134","doi-asserted-by":"crossref","first-page":"7503","DOI":"10.1021\/bi501003n","article-title":"Structural evolution and membrane interaction of the 40-residue \u03b2 amyloid peptides: differences in the initial proximity between peptides and the membrane bilayer studied by solid-state nuclear magnetic resonance spectroscopy","volume":"53","author":"Qiang","year":"2014","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2022.102108_bib135","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":"Paravastu","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2022.102108_bib136","doi-asserted-by":"crossref","first-page":"20555","DOI":"10.1073\/pnas.0910978107","article-title":"Inconvenient facts about pathological amyloid fibrils","volume":"106","author":"Caspar","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2022.102108_bib137","doi-asserted-by":"crossref","first-page":"1257","DOI":"10.1016\/j.cell.2013.08.035","article-title":"Molecular structure of \u03b2-amyloid fibrils in Alzheimer\u2019s disease brain tissue","volume":"154","author":"Lu","year":"2013","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2022.102108_bib138","doi-asserted-by":"crossref","DOI":"10.1083\/jcb.202001161","article-title":"Cryo-EM reconstruction of a VPS13 fragment reveals a long groove to channel lipids between membranes","volume":"219","author":"Li","year":"2020","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1016\/j.jbc.2022.102108_bib139","doi-asserted-by":"crossref","first-page":"3625","DOI":"10.1083\/jcb.201807019","article-title":"VPS13A and VPS13C are lipid transport proteins differentially localized at ER contact sites","volume":"217","author":"Kumar","year":"2018","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1016\/j.jbc.2022.102108_bib140","doi-asserted-by":"crossref","first-page":"2905","DOI":"10.3390\/ijms22062905","article-title":"The Vps13 family of lipid transporters and its role at membrane contact sites","volume":"22","author":"Dziurdzik","year":"2021","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.jbc.2022.102108_bib141","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1038\/s41594-019-0203-4","article-title":"Atg2 mediates direct lipid transfer between membranes for autophagosome formation","volume":"26","author":"Osawa","year":"2019","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.jbc.2022.102108_bib142","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1126\/science.aao2825","article-title":"Fibril structure of amyloid-\u03b2(1-42) by cryo-electron microscopy","volume":"358","author":"Gremer","year":"2017","journal-title":"Science"},{"key":"10.1016\/j.jbc.2022.102108_bib143","doi-asserted-by":"crossref","first-page":"4453","DOI":"10.1021\/acs.jpclett.1c00524","article-title":"Promoted aggregation of A\u03b2 on lipid bilayers in an open flowing system","volume":"12","author":"Iida","year":"2021","journal-title":"J.\u00a0Phys. Chem. Lett."},{"key":"10.1016\/j.jbc.2022.102108_bib144","doi-asserted-by":"crossref","first-page":"2473","DOI":"10.1016\/j.polymer.2013.02.029","article-title":"Amyloids: from molecular structure to mechanical properties","volume":"54","author":"Schleeger","year":"2013","journal-title":"Polymer"},{"key":"10.1016\/j.jbc.2022.102108_bib145","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1038\/nnano.2011.102","article-title":"Nanomechanics of functional and pathological amyloid materials","volume":"6","author":"Knowles","year":"2011","journal-title":"Nat. Nanotechnol."},{"key":"10.1016\/j.jbc.2022.102108_bib146","doi-asserted-by":"crossref","first-page":"1205","DOI":"10.1038\/aps.2017.28","article-title":"Amyloid beta: structure, biology and structure-based therapeutic development","volume":"38","author":"Chen","year":"2017","journal-title":"Acta Pharmacol. Sin."},{"key":"10.1016\/j.jbc.2022.102108_bib147","doi-asserted-by":"crossref","DOI":"10.1016\/j.chemphyslip.2021.105072","article-title":"The interplay between lipid and A\u03b2 amyloid homeostasis in Alzheimer\u2019s disease: risk factors and therapeutic opportunities","volume":"236","author":"Garc\u00eda-Vi\u00f1uales","year":"2021","journal-title":"Chem. Phys. Lipids"},{"key":"10.1016\/j.jbc.2022.102108_bib148","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1146\/annurev-pathol-031920-092547","article-title":"The membrane interactions of synuclein: physiology and pathology","volume":"16","author":"Runwal","year":"2021","journal-title":"Annu. Rev. Pathol."},{"key":"10.1016\/j.jbc.2022.102108_bib149","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1016\/j.neuint.2017.12.014","article-title":"Pathological role of lipid interaction with \u03b1-synuclein in Parkinson\u2019s disease","volume":"119","author":"Suzuki","year":"2018","journal-title":"Neurochem. Int."},{"key":"10.1016\/j.jbc.2022.102108_bib150","doi-asserted-by":"crossref","first-page":"175","DOI":"10.3389\/fncel.2019.00175","article-title":"Lipids at the crossroad of \u03b1-synuclein function and dysfunction: biological and pathological implications","volume":"13","author":"Alza","year":"2019","journal-title":"Front. Cell. Neurosci."},{"key":"10.1016\/j.jbc.2022.102108_bib151","doi-asserted-by":"crossref","first-page":"584536","DOI":"10.3389\/fnsyn.2020.584536","article-title":"From synaptic protein to prion: the long and controversial journey of \u03b1-synuclein","volume":"12","author":"Heras-Garvin","year":"2020","journal-title":"Front. Synaptic Neurosci."},{"key":"10.1016\/j.jbc.2022.102108_bib152","doi-asserted-by":"crossref","first-page":"1128","DOI":"10.1046\/j.1471-4159.2003.01612.x","article-title":"Lipid interaction of alpha-synuclein during the metal-catalyzed oxidation in the presence of Cu2+ and H2O2","volume":"84","author":"Lee","year":"2003","journal-title":"J.\u00a0Neurochem."},{"key":"10.1016\/j.jbc.2022.102108_bib153","doi-asserted-by":"crossref","first-page":"34393","DOI":"10.1074\/jbc.M004851200","article-title":"Interaction of human alpha-Synuclein and Parkinson\u2019s disease variants with phospholipids. Structural analysis using site-directed mutagenesis","volume":"275","author":"Perrin","year":"2000","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102108_bib154","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0082732","article-title":"\u03b1-Synuclein oligomers induced by docosahexaenoic acid affect membrane integrity","volume":"8","author":"Fecchio","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.jbc.2022.102108_bib155","doi-asserted-by":"crossref","DOI":"10.3389\/fnins.2020.578993","article-title":"Interaction of alpha-synuclein with lipids: mitochondrial cardiolipin as a critical player in the pathogenesis of Parkinson\u2019s disease","volume":"14","author":"Gilmozzi","year":"2020","journal-title":"Front. Neurosci."},{"key":"10.1016\/j.jbc.2022.102108_bib156","doi-asserted-by":"crossref","first-page":"5052","DOI":"10.1021\/acs.biochem.9b00925","article-title":"Distinct \u03b1-synuclein:lipid Co-structure complexes affect amyloid nucleation through fibril mimetic behavior","volume":"58","author":"Cholak","year":"2019","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2022.102108_bib157","doi-asserted-by":"crossref","DOI":"10.3389\/fneur.2021.661117","article-title":"Modulation of the interactions between \u03b1-synuclein and lipid membranes by post-translational modifications","volume":"12","author":"Bell","year":"2021","journal-title":"Front. Neurol."},{"key":"10.1016\/j.jbc.2022.102108_bib158","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1007\/s00401-021-02266-7","article-title":"Lipids, lysosomes and mitochondria: insights into Lewy body formation from rare monogenic disorders","volume":"141","author":"Erskine","year":"2021","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.jbc.2022.102108_bib159","doi-asserted-by":"crossref","first-page":"1845","DOI":"10.1021\/acs.chemrev.0c00981","article-title":"Proteostasis of islet amyloid polypeptide: a molecular perspective of risk factors and protective strategies for type II diabetes","volume":"121","author":"Milardi","year":"2021","journal-title":"Chem. Rev."},{"key":"10.1016\/j.jbc.2022.102108_bib160","doi-asserted-by":"crossref","first-page":"9662","DOI":"10.1073\/pnas.86.24.9662","article-title":"Molecular and functional characterization of amylin, a peptide associated with type 2 diabetes mellitus","volume":"86","author":"Roberts","year":"1989","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2022.102108_bib161","doi-asserted-by":"crossref","first-page":"2002","DOI":"10.1016\/j.bbamem.2007.01.022","article-title":"Membrane interaction of islet amyloid polypeptide","volume":"1768","author":"Jayasinghe","year":"2007","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2022.102108_bib162","doi-asserted-by":"crossref","first-page":"17205","DOI":"10.1074\/jbc.M801383200","article-title":"Structure of alpha-helical membrane-bound human islet amyloid polypeptide and its implications for membrane-mediated misfolding","volume":"283","author":"Apostolidou","year":"2008","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102108_bib163","doi-asserted-by":"crossref","first-page":"1175","DOI":"10.1016\/j.jmb.2004.06.086","article-title":"Phospholipid catalysis of diabetic amyloid assembly","volume":"341","author":"Knight","year":"2004","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.jbc.2022.102108_bib164","doi-asserted-by":"crossref","first-page":"1051","DOI":"10.1083\/jcb.200108057","article-title":"Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress","volume":"156","author":"Stamer","year":"2002","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1016\/j.jbc.2022.102108_bib165","doi-asserted-by":"crossref","first-page":"223","DOI":"10.4161\/pri.19912","article-title":"Is tau ready for admission to the prion club","volume":"6","author":"Hall","year":"2012","journal-title":"Prion"},{"key":"10.1016\/j.jbc.2022.102108_bib166","doi-asserted-by":"crossref","first-page":"2302","DOI":"10.1016\/j.bbamem.2012.03.019","article-title":"Binding of the three-repeat domain of tau to phospholipid membranes induces an aggregated-like state of the protein","volume":"1818","author":"K\u00fcnze","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2022.102108_bib167","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1016\/0092-8674(87)90150-4","article-title":"Scrapie prion protein contains a phosphatidylinositol glycolipid","volume":"51","author":"Stahl","year":"1987","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2022.102108_bib168","doi-asserted-by":"crossref","DOI":"10.1016\/j.chemphyslip.2021.105063","article-title":"Multisite interactions of prions with membranes and native nanodiscs","volume":"236","author":"Overduin","year":"2021","journal-title":"Chem. Phys. Lipids"},{"key":"10.1016\/j.jbc.2022.102108_bib169","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1515\/BC.2007.010","article-title":"Interaction of the cellular prion protein with raft-like lipid membranes","volume":"388","author":"Elfrink","year":"2007","journal-title":"Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102108_bib170","doi-asserted-by":"crossref","first-page":"485","DOI":"10.1093\/abbs\/gmt038","article-title":"Role of lipid in forming an infectious prion","volume":"45","author":"Wang","year":"2013","journal-title":"Acta Biochim. Biophys. Sin (Shanghai)"},{"key":"10.1016\/j.jbc.2022.102108_bib171","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1083\/jcb.201308028","article-title":"Live imaging of prions reveals nascent PrPSc in cell-surface, raft-associated amyloid strings and webs","volume":"204","author":"Rouvinski","year":"2014","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1016\/j.jbc.2022.102108_bib172","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1111\/j.1365-2990.1997.tb01191.x","article-title":"In\u00a0vivo toxicity of prion protein in murine scrapie: ultrastructural and immunogold studies","volume":"23","author":"Jeffrey","year":"1997","journal-title":"Neuropathol. Appl. Neurobiol."},{"key":"10.1016\/j.jbc.2022.102108_bib173","doi-asserted-by":"crossref","first-page":"2857","DOI":"10.1021\/bi048510j","article-title":"Binding of endostatin to phosphatidylserine-containing membranes and formation of amyloid-like fibers","volume":"44","author":"Zhao","year":"2005","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2022.102108_bib174","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1038\/s41586-021-03911-7","article-title":"Structure-based classification of tauopathies","volume":"598","author":"Shi","year":"2021","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2022.102108_bib175","doi-asserted-by":"crossref","first-page":"4760","DOI":"10.1038\/s41467-019-12683-8","article-title":"Cryo-EM structure and polymorphism of A\u03b2 amyloid fibrils purified from Alzheimer\u2019s brain tissue","volume":"10","author":"Kollmer","year":"2019","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2022.102108_bib176","doi-asserted-by":"crossref","first-page":"5008","DOI":"10.1038\/s41467-019-13038-z","article-title":"Cryo-EM structure of a transthyretin-derived amyloid fibril from a patient with hereditary ATTR amyloidosis","volume":"10","author":"Schmidt","year":"2019","journal-title":"Nat. Commun."}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S002192582200549X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S002192582200549X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,19]],"date-time":"2025-09-19T00:17:57Z","timestamp":1758241077000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S002192582200549X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,8]]},"references-count":176,"journal-issue":{"issue":"8","published-print":{"date-parts":[[2022,8]]}},"alternative-id":["S002192582200549X"],"URL":"https:\/\/doi.org\/10.1016\/j.jbc.2022.102108","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2022,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"The association of lipids with amyloid fibrils","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jbc.2022.102108","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2022 The Author. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}],"article-number":"102108"}}