{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,15]],"date-time":"2026-10-15T13:06:28Z","timestamp":1792069588736,"version":"4.4.0"},"reference-count":57,"publisher":"American Chemical Society (ACS)","issue":"1","license":[{"start":{"date-parts":[[2015,12,3]],"date-time":"2015-12-03T00:00:00Z","timestamp":1449100800000},"content-version":"vor","delay-in-days":365,"URL":"https:\/\/pubs.acs.org\/page\/policy\/authorchoice_termsofuse.html"}],"funder":[{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R01GM107487"],"award-info":[{"award-number":["R01GM107487"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R15GM097723"],"award-info":[{"award-number":["R15GM097723"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2015,1,12]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Self-assembly of proteins into amyloid fibrils plays a key role in a multitude of human disorders that range from Alzheimer\u2019s disease to type II diabetes. Compact oligomeric species, observed early during amyloid formation, are reported as the molecular entities responsible for the toxic effects of amyloid self-assembly. However, the relation between early-stage oligomeric aggregates and late-stage rigid fibrils, which are the hallmark structure of amyloid plaques, has remained unclear. We show that these different structures occupy well-defined regions in a peculiar phase diagram. Lysozyme amyloid oligomers and their curvilinear fibrils only form after they cross a salt and protein concentration-dependent threshold. We also determine a boundary for the onset of amyloid oligomer precipitation. The oligomeric aggregates are structurally distinct from rigid fibrils and are metastable against nucleation and growth of rigid fibrils. These experimentally determined boundaries match well with colloidal model predictions that account for salt-modulated charge repulsion. The model also incorporates the metastable and kinetic character of oligomer phases. Similarities and differences of amyloid oligomer assembly to metastable liquid\u2013liquid phase separation of proteins and to surfactant aggregation are discussed.<\/jats:p>","DOI":"10.1021\/bm501521r","type":"journal-article","created":{"date-parts":[[2014,12,3]],"date-time":"2014-12-03T14:25:11Z","timestamp":1417616711000},"page":"326-335","source":"Crossref","is-referenced-by-count":88,"title":["Stable, Metastable, and Kinetically Trapped Amyloid\nAggregate Phases"],"prefix":"10.1021","volume":"16","author":[{"given":"Tatiana","family":"Miti","sequence":"first","affiliation":[{"name":"University of South Florida , , , ,","place":["Tampa, Florida, United States, 33620"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mentor","family":"Mulaj","sequence":"additional","affiliation":[{"name":"University of South Florida , , , ,","place":["Tampa, Florida, United States, 33620"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jeremy D.","family":"Schmit","sequence":"additional","affiliation":[{"name":"Kansas State University , , , ,","place":["Manhattan, Kansas, United States, 66506"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Martin","family":"Muschol","sequence":"additional","affiliation":[{"name":"University of South Florida , , , ,","place":["Tampa, Florida, United States, 33620"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2014,12,3]]},"reference":[{"key":"2026090117353444200_cit1","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/S0959-440X(96)80089-3","article-title":"Alternative\nConformations of Amyloidogenic Proteins Govern Their Behavior","volume":"6","author":"Kelly","year":"1996","journal-title":"Curr. Opin. Struct. Biol."},{"key":"2026090117353444200_cit2","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1146\/annurev.biochem.75.101304.123901","article-title":"Protein Misfolding, Functional Amyloid, and Human Disease","volume":"75","author":"Chiti","year":"2006","journal-title":"Annu. Rev. Biochem."},{"key":"2026090117353444200_cit3","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1016\/S0968-0004(99)01445-0","article-title":"Protein\nMisfolding, Evolution, and Disease","volume":"24","author":"Dobson","year":"1999","journal-title":"Trends Biochem.\nSci."},{"key":"2026090117353444200_cit4","doi-asserted-by":"crossref","first-page":"1720","DOI":"10.1016\/j.bpj.2011.08.024","article-title":"Chain Collapse of an Amyloidogenic\nIntrinsically Disordered Protein","volume":"101","author":"Jain","year":"2011","journal-title":"Biophys. J."},{"key":"2026090117353444200_cit5","doi-asserted-by":"crossref","first-page":"7174","DOI":"10.1021\/la025531a","article-title":"Novel Amyloid\nFibrillar Networks Derived from a Globular Protein: \u03b2-Lactoglobulin","volume":"18","author":"Gosal","year":"2002","journal-title":"Langmuir"},{"key":"2026090117353444200_cit6","doi-asserted-by":"crossref","first-page":"1128","DOI":"10.1016\/j.bbapap.2007.06.008","article-title":"Aggregation\nand Fibrillation of Bovine Serum Albumin","volume":"1774","author":"Holm","year":"2007","journal-title":"Biochim.\nBiophys. Acta, Proteins Proteomics"},{"key":"2026090117353444200_cit7","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1039\/B403014A","article-title":"Aggregation Across the Length-Scales\nin \u03b2-Lactoglobulin","volume":"128","author":"Bromley","year":"2005","journal-title":"Faraday Discuss."},{"key":"2026090117353444200_cit8","doi-asserted-by":"crossref","first-page":"16052","DOI":"10.1073\/pnas.252340199","article-title":"De Novo Designed Peptide-Based\nAmyloid Fibrils","volume":"99","author":"Lopez de la Paz","year":"2002","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026090117353444200_cit9","doi-asserted-by":"crossref","first-page":"5262","DOI":"10.1021\/ja9937831","article-title":"Protofilaments,\nFilaments, Ribbons, and Fibrils from Peptidomimetic Self-Assembly:\nImplications for Amyloid Fibril Formation and Materials Science","volume":"122","author":"Lashuel","year":"2000","journal-title":"J. Am. Chem. Soc."},{"key":"2026090117353444200_cit10","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1073\/pnas.0406847102","article-title":"Molecular Basis for Amyloid Fibril Formation and Stability","volume":"102","author":"Makin","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026090117353444200_cit11","doi-asserted-by":"crossref","first-page":"5682","DOI":"10.1093\/emboj\/cdf573","article-title":"The Behavior of Polyamino Acids Reveals an Inverse\nSide Chain Effect in Amyloid Structure Formation","volume":"21","author":"Fa\u0308ndrich","year":"2002","journal-title":"EMBO J."},{"key":"2026090117353444200_cit12","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1146\/annurev.biochem.66.1.385","article-title":"Models\nof Amyloid Seeding in Alzheimer\u2019s Disease\nand Scrapie: Mechanistic Truths and Physiological Consequences of\nthe Time-Dependent Solubility of Amyloid Proteins","volume":"66","author":"Harper","year":"1997","journal-title":"Annu. Rev. Biochem."},{"key":"2026090117353444200_cit13","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1016\/j.jmb.2012.02.031","article-title":"From Macroscopic\nMeasurements to Microscopic Mechanisms of Protein Aggregation","volume":"421","author":"Cohen","year":"2012","journal-title":"J. Mol. Biol."},{"key":"2026090117353444200_cit14","doi-asserted-by":"crossref","first-page":"36046","DOI":"10.1074\/jbc.M201750200","article-title":"Oligomeric and Fibrillar Species\nof Amyloid-\u03b2 Peptides Differentially Affect Neuronal Viability","volume":"277","author":"Dahlgren","year":"2002","journal-title":"J. Biol. Chem."},{"key":"2026090117353444200_cit15","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1038\/416535a","article-title":"Naturally Secreted\nOligomers of Amyloid-\u03b2 Protein Potently Inhibit Hippocampal\nLong-Term Potentiation in Vivo","volume":"416","author":"Walsh","year":"2002","journal-title":"Nature"},{"key":"2026090117353444200_cit16","doi-asserted-by":"crossref","first-page":"673","DOI":"10.1021\/cb900112v","article-title":"Novel Pentameric Thiophene Derivatives\nfor in Vitro and in Vivo Optical Imaging of a Plethora of Protein\nAggregates in Cerebral Amyloidoses","volume":"4","author":"\u00c5slund","year":"2009","journal-title":"ACS Chem.\nBiol."},{"key":"2026090117353444200_cit17","doi-asserted-by":"crossref","first-page":"121901\/1","DOI":"10.1063\/1.4811343","article-title":"Structural Fingerprints\nand their Evolution during\nOligomeric versus Oligomer-Free Amyloid Fibril Growth","volume":"139","author":"Foley","year":"2013","journal-title":"J. Chem. Phys."},{"key":"2026090117353444200_cit18","doi-asserted-by":"crossref","first-page":"850","DOI":"10.1016\/j.jmb.2005.06.040","article-title":"Competing Pathways Determine Fibril Morphology in the\nSelf-Assembly of \u03b22-Microglobulin into Amyloid","volume":"351","author":"Gosal","year":"2005","journal-title":"J. Mol. Biol."},{"key":"2026090117353444200_cit19","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1016\/S0166-2236(00)01749-5","article-title":"Targeting Small A\u03b2 Oligomers:\nThe Solution to an Alzheimer\u2019s Disease Conundrum?","volume":"24","author":"Klein","year":"2001","journal-title":"Trends Neurosci."},{"key":"2026090117353444200_cit20","doi-asserted-by":"crossref","first-page":"11612","DOI":"10.1074\/jbc.M210207200","article-title":"In Vitro\nCharacterization of Conditions for Amyloid-\u03b2 Peptide Oligomerization\nand Fibrillogenesis","volume":"278","author":"Stine","year":"2003","journal-title":"J. Biol. Chem."},{"key":"2026090117353444200_cit21","doi-asserted-by":"crossref","first-page":"2940","DOI":"10.1111\/j.1742-4658.2010.07721.x","article-title":"Mysterious\nOligomerization of the Amyloidogenic Proteins","volume":"277","author":"Uversky","year":"2010","journal-title":"FEBS J."},{"key":"2026090117353444200_cit22","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1042\/BJ20090379","article-title":"Antiparallel \u03b2-Sheet: A Signature\nStructure of the Oligomeric Amyloid \u03b2-Peptide","volume":"421","author":"Cerf","year":"2009","journal-title":"Biochem. J."},{"key":"2026090117353444200_cit23","doi-asserted-by":"crossref","first-page":"4003","DOI":"10.1021\/jp4003559","article-title":"Parallel \u03b2-Sheet\nFibril and Antiparallel \u03b2-Sheet Oligomer: New Insights into\nAmyloid Formation of Hen Egg White Lysozyme under Heat and Acidic\nCondition from FTIR Spectroscopy","volume":"117","author":"Zou","year":"2013","journal-title":"J. Phys. Chem.\nB"},{"key":"2026090117353444200_cit24","doi-asserted-by":"crossref","first-page":"7717","DOI":"10.1073\/pnas.1203193109","article-title":"Toxic Fibrillar Oligomers of Amyloid-\u03b2\nHave Cross-\u03b2 Structure","volume":"109","author":"Stroud","year":"2012","journal-title":"Proc. Natl. Acad.\nSci. U.S.A."},{"key":"2026090117353444200_cit25","doi-asserted-by":"crossref","first-page":"1228","DOI":"10.1126\/science.1213151","article-title":"Atomic View\nof a Toxic Amyloid Small Oligomer","volume":"335","author":"Laganowsky","year":"2012","journal-title":"Science"},{"key":"2026090117353444200_cit26","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1016\/j.abb.2007.05.015","article-title":"Folding versus Aggregation:\nPolypeptide Conformations\non Competing Pathways","volume":"469","author":"Jahn","year":"2008","journal-title":"Arch. Biochem. Biophys."},{"key":"2026090117353444200_cit27","doi-asserted-by":"crossref","first-page":"3480","DOI":"10.1016\/S0006-3495(03)70068-X","article-title":"Micelle Formation by\na Fragment of Human Islet Amyloid Polypeptide","volume":"84","author":"Rhoades","year":"2003","journal-title":"Biophys. J."},{"key":"2026090117353444200_cit28","doi-asserted-by":"crossref","first-page":"e18171.1","DOI":"10.1371\/journal.pone.0018171","article-title":"Spatial Extent of Charge\nRepulsion Regulates Assembly Pathways for Lysozyme Amyloid Fibrils","volume":"6","author":"Hill","year":"2011","journal-title":"PLoS One"},{"key":"2026090117353444200_cit29","doi-asserted-by":"crossref","first-page":"14446","DOI":"10.1073\/pnas.1208228109","article-title":"Distinguishing Crystal-Like\nAmyloid Fibrils and Glass-Like Amorphous Aggregates from Their Kinetics\nof Formation","volume":"109","author":"Yoshimura","year":"2012","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026090117353444200_cit30","doi-asserted-by":"crossref","first-page":"2477","DOI":"10.1021\/bm800502j","article-title":"Structure\nof Heat-Induced \u03b2-Lactoglobulin Aggregates and Their Complexes\nwith Sodium-Dodecyl Sulfate","volume":"9","author":"Jung","year":"2008","journal-title":"Biomacromolecules"},{"key":"2026090117353444200_cit31","doi-asserted-by":"crossref","first-page":"3241","DOI":"10.1021\/bm301005w","article-title":"Gelation, Phase Behavior,\nand Dynamics of \u03b2-Lactoglobulin Amyloid Fibrils at Varying Concentrations\nand Ionic Strengths","volume":"13","author":"Bolisetty","year":"2012","journal-title":"Biomacromolecules"},{"key":"2026090117353444200_cit32","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1016\/j.sbi.2007.01.007","article-title":"Polymorphism in the\nIntermediates and Products of Amyloid\nAssembly","volume":"17","author":"Kodali","year":"2007","journal-title":"Curr. Opin. Struct. Biol."},{"key":"2026090117353444200_cit33","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1006\/jmbi.2000.3862","article-title":"Formation\nand Seeding of Amyloid Fibrils from Wild-Type Hen Lysozyme and a Peptide\nFragment from the \u03b2-Domain","volume":"300","author":"Krebs","year":"2000","journal-title":"J. Mol. Biol."},{"key":"2026090117353444200_cit34","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1529\/biophysj.104.048819","article-title":"Thermally Induced Fibrillar\nAggregation of Hen Egg\nWhite Lysozyme","volume":"88","author":"Arnaudov","year":"2005","journal-title":"Biophys. J."},{"key":"2026090117353444200_cit35","doi-asserted-by":"crossref","first-page":"3781","DOI":"10.1016\/j.bpj.2009.01.044","article-title":"Amyloid Protofibrils\nof Lysozyme Nucleate and Grow via Oligomer Fusion","volume":"96","author":"Hill","year":"2009","journal-title":"Biophys. J."},{"key":"2026090117353444200_cit36","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1016\/j.bpc.2007.06.002","article-title":"Submicron Lysozyme Clusters Distort\nKinetics of Crystal Nucleation in Supersaturated Lysozyme Solutions","volume":"129","author":"Parmar","year":"2007","journal-title":"Biophys. Chem."},{"key":"2026090117353444200_cit37","doi-asserted-by":"crossref","first-page":"4020","DOI":"10.1021\/jp9107188","article-title":"The Stabilities of Protein Crystals","volume":"114","author":"Schmit","year":"2010","journal-title":"J. Phys. Chem. B"},{"key":"2026090117353444200_cit38","doi-asserted-by":"crossref","first-page":"1368","DOI":"10.1021\/jp983852i","article-title":"Lysozyme Net Charge and Ion Binding in Concentrated\nAqueous Electrolyte Solutions","volume":"103","author":"Kuehner","year":"1999","journal-title":"J. Phys. Chem.\nB"},{"key":"2026090117353444200_cit39","doi-asserted-by":"crossref","first-page":"085103\/1","DOI":"10.1063\/1.3626803","article-title":"Electrostatics and Aggregation: How\nCharge Can Turn a Crystal into a Gel","volume":"135","author":"Schmit","year":"2011","journal-title":"J. Chem.\nPhys."},{"key":"2026090117353444200_cit40","doi-asserted-by":"crossref","first-page":"1","DOI":"10.6028\/jres.056.001","article-title":"Dielectric\nConstant of Water from 0\u2013100 \u00b0C","volume":"56","author":"Malmberg","year":"1956","journal-title":"J. Res. Natl. Bur. Stand."},{"key":"2026090117353444200_cit41","doi-asserted-by":"crossref","first-page":"302","DOI":"10.1038\/jid.1967.140","article-title":"Serum and Urinary Lysozyme in Patients with Mastocytosis\n(Urticaria Pigmentosa), Systemic Scleroderma, and Psoriasis1","volume":"49","author":"Sasaki","year":"1967","journal-title":"J. Invest. Dermatol."},{"key":"2026090117353444200_cit42","doi-asserted-by":"crossref","first-page":"921","DOI":"10.1084\/jem.124.5.921","article-title":"Serum and Urinary Lysozyme (Muramidase) in Monocytic\nand Monomyelocytic Leukemia","volume":"124","author":"Osserman","year":"1966","journal-title":"J. Exp. Med."},{"key":"2026090117353444200_cit43","doi-asserted-by":"crossref","first-page":"1153","DOI":"10.1016\/j.jmb.2004.05.056","article-title":"A Highly Amyloidogenic\nRegion of Hen Lysozyme","volume":"340","author":"Frare","year":"2004","journal-title":"J. Mol. Biol."},{"key":"2026090117353444200_cit44","doi-asserted-by":"crossref","first-page":"2525","DOI":"10.1110\/ps.28101","article-title":"Characterization\nof the Structure and Dynamics of Amyloidogenic Variants of Human Lysozyme\nby NMR Spectroscopy","volume":"10","author":"Chamberlain","year":"2001","journal-title":"Protein Sci."},{"key":"2026090117353444200_cit45","doi-asserted-by":"crossref","first-page":"2066","DOI":"10.1007\/s00018-007-7110-2","article-title":"On the Structural\nDefinition of Amyloid Fibrils and Other Polypeptide Aggregates","volume":"64","author":"Fa\u0308ndrich","year":"2007","journal-title":"Cell. Mol. Life Sci."},{"key":"2026090117353444200_cit46","doi-asserted-by":"crossref","first-page":"3314","DOI":"10.1110\/ps.041024904","article-title":"FTIR Reveals\nStructural Differences between Native \u03b2-Sheet Proteins and Amyloid\nFibrils","volume":"13","author":"Zandomeneghi","year":"2004","journal-title":"Protein Sci."},{"key":"2026090117353444200_cit47","doi-asserted-by":"crossref","first-page":"360","DOI":"10.1038\/339360a0","article-title":"Universality in Colloid Aggregation","volume":"339","author":"Lin","year":"1989","journal-title":"Nature"},{"key":"2026090117353444200_cit48","doi-asserted-by":"crossref","first-page":"8947","DOI":"10.1021\/ja502529m","article-title":"Amyloid Oligomers and Protofibrils,\nbut Not Filaments, Self-Replicate from Native Lysozyme","volume":"136","author":"Mulaj","year":"2014","journal-title":"J. Am. Chem. Soc."},{"key":"2026090117353444200_cit49","doi-asserted-by":"crossref","first-page":"10202","DOI":"10.1021\/ja403001q","article-title":"Crystal Structure of a Human Prion\nProtein Fragment Reveals a Motif for Oligomer Formation","volume":"135","author":"Apostol","year":"2013","journal-title":"J. Am. Chem. Soc."},{"key":"2026090117353444200_cit50","doi-asserted-by":"crossref","first-page":"031902","DOI":"10.1103\/PhysRevE.80.031902","article-title":"Isotropic\u2013Nematic\nPhase Transition in Amyloid Fibrilization","volume":"80","author":"Lee","year":"2009","journal-title":"Phys.\nRev. E"},{"key":"2026090117353444200_cit51","doi-asserted-by":"crossref","first-page":"450","DOI":"10.1016\/j.bpj.2010.11.041","article-title":"Why Do Amyloid Molecules Assemble\ninto Oligomers and Fibrils","volume":"100","author":"Schmit","year":"2011","journal-title":"Biophys. J."},{"key":"2026090117353444200_cit52","doi-asserted-by":"crossref","first-page":"1953","DOI":"10.1063\/1.474547","article-title":"Liquid\u2013Liquid\nPhase Separation in Supersaturated\nLysozyme Solutions and Associated Precipitate Formation\/Crystallization","volume":"107","author":"Muschol","year":"1997","journal-title":"J. Chem. Phys."},{"key":"2026090117353444200_cit53","doi-asserted-by":"crossref","first-page":"4093","DOI":"10.1063\/1.467526","article-title":"Determination of Phase-Diagrams for the Hard-Core Attractive\nYukawa System","volume":"101","author":"Hagen","year":"1994","journal-title":"J. Chem. Phys."},{"key":"2026090117353444200_cit54","doi-asserted-by":"crossref","first-page":"1214","DOI":"10.1073\/pnas.89.4.1214","article-title":"Solid\u2013Liquid\nPhase Boundaries\nof Lens Protein Solutions","volume":"89","author":"Berland","year":"1992","journal-title":"Proc. Natl. Acad.\nSci. U.S.A."},{"key":"2026090117353444200_cit55","doi-asserted-by":"crossref","first-page":"723","DOI":"10.1016\/j.jmb.2012.06.022","article-title":"Two-Step Nucleation of Amyloid Fibrils:\nOmnipresent or Not?","volume":"422","author":"Auer","year":"2012","journal-title":"J. Mol. Biol."},{"key":"2026090117353444200_cit56","doi-asserted-by":"crossref","first-page":"460","DOI":"10.1126\/science.1082193","article-title":"On the Origins of\nMorphological Complexity in Block\nCopolymer Surfactants","volume":"300","author":"Jain","year":"2003","journal-title":"Science"},{"key":"2026090117353444200_cit57","doi-asserted-by":"crossref","first-page":"7214","DOI":"10.1021\/ja312469n","article-title":"Direct Observation\nof the Formation\nof Surfactant Micelles under Nonisothermal Conditions by Synchrotron\nSAXS","volume":"135","author":"Jensen","year":"2013","journal-title":"J. Am. Chem. Soc."}],"container-title":["Biomacromolecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/bm501521r","content-type":"application\/pdf","content-version":"vor","intended-application":"unspecified"},{"URL":"https:\/\/pubs.acs.org\/bomaf6\/article-pdf\/16\/1\/326\/7897651\/bm501521r.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pubs.acs.org\/bomaf6\/article-pdf\/16\/1\/326\/7897651\/bm501521r.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T21:35:45Z","timestamp":1788298545000},"score":1,"resource":{"primary":{"URL":"https:\/\/pubs.acs.org\/bomaf6\/article\/16\/1\/326\/774778\/Stable-Metastable-and-Kinetically-Trapped-Amyloid"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,12,3]]},"references-count":57,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2014,12,3]]},"published-print":{"date-parts":[[2015,1,12]]}},"URL":"https:\/\/doi.org\/10.1021\/bm501521r","relation":{},"ISSN":["1525-7797","1526-4602"],"issn-type":[{"value":"1525-7797","type":"print"},{"value":"1526-4602","type":"electronic"}],"subject":[],"published":{"date-parts":[[2014,12,3]]}}}