{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,7]],"date-time":"2026-05-07T00:39:35Z","timestamp":1778114375155,"version":"3.51.4"},"reference-count":124,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2022,2,1]],"date-time":"2022-02-01T00:00:00Z","timestamp":1643673600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2022,2,1]],"date-time":"2022-02-01T00:00:00Z","timestamp":1643673600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2022,2,1]],"date-time":"2022-02-01T00:00:00Z","timestamp":1643673600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2022,2,1]],"date-time":"2022-02-01T00:00:00Z","timestamp":1643673600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2022,2,1]],"date-time":"2022-02-01T00:00:00Z","timestamp":1643673600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2022,2,1]],"date-time":"2022-02-01T00:00:00Z","timestamp":1643673600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2022,2,1]],"date-time":"2022-02-01T00:00:00Z","timestamp":1643673600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biophysical Chemistry"],"published-print":{"date-parts":[[2022,2]]},"DOI":"10.1016\/j.bpc.2021.106711","type":"journal-article","created":{"date-parts":[[2021,10,30]],"date-time":"2021-10-30T19:25:51Z","timestamp":1635621951000},"page":"106711","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":46,"special_numbering":"C","title":["Transient disorder along pathways to amyloid"],"prefix":"10.1016","volume":"281","author":[{"given":"Gareth J.","family":"Morgan","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.bpc.2021.106711_bb0005","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.bpc.2021.106711_bb0010","doi-asserted-by":"crossref","first-page":"4857","DOI":"10.1016\/j.cell.2021.08.013","article-title":"The expanding amyloid family: structure, stability, function, and pathogenesis","volume":"184","author":"Sawaya","year":"2021","journal-title":"Cell"},{"key":"10.1016\/j.bpc.2021.106711_bb0015","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1080\/13506129.2020.1835263","article-title":"Amyloid nomenclature 2020: update and recommendations by the International Society of Amyloidosis (ISA) nomenclature committee","volume":"27","author":"Benson","year":"2020","journal-title":"Amyloid."},{"key":"10.1016\/j.bpc.2021.106711_bb0020","doi-asserted-by":"crossref","DOI":"10.3390\/microorganisms8121951","article-title":"Functional amyloids are the rule rather than the exception in cellular biology","volume":"8","author":"Balistreri","year":"2020","journal-title":"Microorganisms"},{"key":"10.1016\/j.bpc.2021.106711_bb0025","doi-asserted-by":"crossref","first-page":"5682","DOI":"10.1093\/emboj\/cdf573","article-title":"The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation","volume":"21","author":"F\u00e4ndrich","year":"2002","journal-title":"EMBO J."},{"key":"10.1016\/j.bpc.2021.106711_bb0030","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1146\/annurev-biochem-061516-045115","article-title":"Protein misfolding, amyloid formation, and human disease: a summary of progress over the last decade","volume":"86","author":"Chiti","year":"2017","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.bpc.2021.106711_bb0035","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1016\/j.jmb.2011.12.060","article-title":"The transthyretin amyloidoses: from delineating the molecular mechanism of aggregation linked to pathology to a regulatory-agency-approved drug","volume":"421","author":"Johnson","year":"2012","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bpc.2021.106711_bb0040","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1038\/s41572-018-0034-3","article-title":"Systemic immunoglobulin light chain amyloidosis","volume":"4","author":"Merlini","year":"2018","journal-title":"Nat. Rev. Dis. Primers"},{"key":"10.1016\/j.bpc.2021.106711_bb0045","doi-asserted-by":"crossref","first-page":"550","DOI":"10.1016\/j.tibs.2020.12.005","article-title":"FUS and TDP-43 phases in health and disease","volume":"46","author":"Portz","year":"2021","journal-title":"Trends Biochem. Sci."},{"issue":"21","key":"10.1016\/j.bpc.2021.106711_bb0050","doi-asserted-by":"crossref","first-page":"4540","DOI":"10.1016\/j.molcel.2021.08.011","article-title":"High-resolution structure and strain comparison of infectious mammalian prions","volume":"81","author":"Kraus","year":"2021","journal-title":"Mol. Cell"},{"key":"10.1016\/j.bpc.2021.106711_bb0055","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."},{"key":"10.1016\/j.bpc.2021.106711_bb0060","doi-asserted-by":"crossref","first-page":"8770","DOI":"10.1073\/pnas.1705091114","article-title":"Atomic structure of a toxic, oligomeric segment of SOD1 linked to amyotrophic lateral sclerosis (ALS)","volume":"114","author":"Sangwan","year":"2017","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bpc.2021.106711_bb0065","doi-asserted-by":"crossref","DOI":"10.1038\/s41580-018-0060-8","article-title":"A new era for understanding amyloid structures and disease","author":"Iadanza","year":"2018","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.bpc.2021.106711_bb0070","doi-asserted-by":"crossref","DOI":"10.1146\/annurev-biochem-061516-045104","article-title":"Structural studies of amyloid proteins at the molecular level","author":"Eisenberg","year":"2017","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.bpc.2021.106711_bb0075","doi-asserted-by":"crossref","first-page":"262","DOI":"10.1126\/science.1105850","article-title":"Self-propagating, molecular-level polymorphism in Alzheimer\u2019s beta-amyloid fibrils","volume":"307","author":"Petkova","year":"2005","journal-title":"Science."},{"key":"10.1016\/j.bpc.2021.106711_bb0080","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.bpc.2021.106711_bb0085","doi-asserted-by":"crossref","first-page":"1104","DOI":"10.1038\/s41467-019-09033-z","article-title":"Cryo-EM fibril structures from systemic AA amyloidosis reveal the species complementarity of pathological amyloids","volume":"10","author":"Liberta","year":"2019","journal-title":"Nat. Commun."},{"key":"10.1016\/j.bpc.2021.106711_bb0090","doi-asserted-by":"crossref","first-page":"875","DOI":"10.1038\/s41467-021-21126-2","article-title":"Cryo-EM reveals structural breaks in a patient-derived amyloid fibril from systemic AL amyloidosis","volume":"12","author":"Radamaker","year":"2021","journal-title":"Nat. Commun."},{"key":"10.1016\/j.bpc.2021.106711_bb0095","doi-asserted-by":"crossref","first-page":"1103","DOI":"10.1038\/s41467-019-09032-0","article-title":"Cryo-EM structure of a light chain-derived amyloid fibril from a patient with systemic AL amyloidosis","volume":"10","author":"Radamaker","year":"2019","journal-title":"Nat. Commun."},{"key":"10.1016\/j.bpc.2021.106711_bb0100","doi-asserted-by":"crossref","first-page":"1269","DOI":"10.1038\/s41467-019-09133-w","article-title":"Cryo-EM structure of cardiac amyloid fibrils from an immunoglobulin light chain AL amyloidosis patient","volume":"10","author":"Swuec","year":"2019","journal-title":"Nat. Commun."},{"key":"10.1016\/j.bpc.2021.106711_bb0105","doi-asserted-by":"crossref","first-page":"4517","DOI":"10.1038\/s41467-018-06761-6","article-title":"The structure of a \u03b22-microglobulin fibril suggests a molecular basis for its amyloid polymorphism","volume":"9","author":"Iadanza","year":"2018","journal-title":"Nat. Commun."},{"key":"10.1016\/j.bpc.2021.106711_bb0110","doi-asserted-by":"crossref","DOI":"10.1038\/s41594-020-0441-5","article-title":"Cryo-EM structure of an amyloid fibril formed by full-length human prion protein","author":"Wang","year":"2020","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.bpc.2021.106711_bb0115","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1016\/S0065-3233(06)73008-X","article-title":"Structural models of amyloid-like fibrils","volume":"73","author":"Nelson","year":"2006","journal-title":"Adv. Protein Chem."},{"key":"10.1016\/j.bpc.2021.106711_bb0120","doi-asserted-by":"crossref","first-page":"8654","DOI":"10.1021\/bi00151a036","article-title":"Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro","volume":"31","author":"Colon","year":"1992","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpc.2021.106711_bb0125","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1111\/j.1432-1033.1974.tb03707.x","article-title":"Renaturation of Escherichia coli tryptophanase after exposure to 8 M urea. Evidence for the existence of nucleation centers","volume":"47","author":"London","year":"1974","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.bpc.2021.106711_bb0130","doi-asserted-by":"crossref","first-page":"1829","DOI":"10.1002\/pro.2790","article-title":"Mutations can cause light chains to be too stable or too unstable to form amyloid fibrils","volume":"24","author":"Marin-Argany","year":"2015","journal-title":"Protein Sci."},{"key":"10.1016\/j.bpc.2021.106711_bb0135","doi-asserted-by":"crossref","first-page":"R9","DOI":"10.1016\/S1359-0278(98)00002-9","article-title":"Protein aggregation: folding aggregates, inclusion bodies and amyloid","volume":"3","author":"Fink","year":"1998","journal-title":"Fold. Des."},{"key":"10.1016\/j.bpc.2021.106711_bb0140","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1016\/0167-7799(94)90082-5","article-title":"Mutations and off-pathway aggregation of proteins","volume":"12","author":"Wetzel","year":"1994","journal-title":"Trends Biotechnol."},{"key":"10.1016\/j.bpc.2021.106711_bb0145","doi-asserted-by":"crossref","first-page":"10697","DOI":"10.1021\/bi00034a001","article-title":"A molecular model for self-assembly of amyloid fibrils: immunoglobulin light chains","volume":"34","author":"Stevens","year":"1995","journal-title":"Biochemistry."},{"key":"10.1016\/j.bpc.2021.106711_bb0150","doi-asserted-by":"crossref","first-page":"16672","DOI":"10.1073\/pnas.0505905102","article-title":"The amyloid stretch hypothesis: recruiting proteins toward the dark side","volume":"102","author":"Esteras-Chopo","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bpc.2021.106711_bb0155","doi-asserted-by":"crossref","first-page":"4074","DOI":"10.1073\/pnas.0511295103","article-title":"The 3D profile method for identifying fibril-forming segments of proteins","volume":"103","author":"Thompson","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bpc.2021.106711_bb0160","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/j.cell.2005.01.018","article-title":"The biological and chemical basis for tissue-selective amyloid disease","volume":"121","author":"Sekijima","year":"2005","journal-title":"Cell"},{"key":"10.1016\/j.bpc.2021.106711_bb0165","doi-asserted-by":"crossref","first-page":"5446","DOI":"10.1073\/pnas.91.12.5446","article-title":"A role for destabilizing amino acid replacements in light-chain amyloidosis","volume":"91","author":"Hurle","year":"1994","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bpc.2021.106711_bb0170","first-page":"101","article-title":"Intralysosomal formation of amyloid fibrils","volume":"81","author":"Shirahama","year":"1975","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.bpc.2021.106711_bb0175","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1080\/13506120601116575","article-title":"Cellular events associated with the initial phase of AA amyloidogenesis: insights from a human monocyte model","volume":"14","author":"Magy","year":"2007","journal-title":"Amyloid."},{"key":"10.1016\/j.bpc.2021.106711_bb0180","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1146\/annurev.biophys.37.092707.153558","article-title":"The protein folding problem","volume":"37","author":"Dill","year":"2008","journal-title":"Annu. Rev. Biophys."},{"key":"10.1016\/j.bpc.2021.106711_bb0185","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1038\/s41580-019-0183-6","article-title":"The molecular principles governing the activity and functional diversity of AAA+ proteins","volume":"21","author":"Puchades","year":"2020","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.bpc.2021.106711_bb0190","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.48907","article-title":"Two new polymorphic structures of human full-length alpha-synuclein fibrils solved by cryo-electron microscopy","volume":"8","author":"Guerrero-Ferreira","year":"2019","journal-title":"Elife"},{"key":"10.1016\/j.bpc.2021.106711_bb0195","doi-asserted-by":"crossref","DOI":"10.1038\/s41586-021-03911-7","article-title":"Structure-based classification of tauopathies","author":"Shi","year":"2021","journal-title":"Nature"},{"key":"10.1016\/j.bpc.2021.106711_bb0200","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41467-021-21129-z","article-title":"AA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrils","volume":"12","author":"Bansal","year":"2021","journal-title":"Nat. Commun."},{"key":"10.1016\/j.bpc.2021.106711_bb0205","first-page":"505","article-title":"The AL amyloid fibril: looking for a link between fibril formation and structure","volume":"2","author":"Haupt","year":"2021","journal-title":"Hematology."},{"key":"10.1016\/j.bpc.2021.106711_bb0210","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pbio.0060195","article-title":"Bacterial inclusion bodies contain amyloid-like structure","volume":"6","author":"Wang","year":"2008","journal-title":"PLoS Biol."},{"key":"10.1016\/j.bpc.2021.106711_bb0215","doi-asserted-by":"crossref","first-page":"796","DOI":"10.1002\/jps.23839","article-title":"Structural characterization of IgG1 mAb aggregates and particles generated under various stress conditions","volume":"103","author":"Telikepalli","year":"2014","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.bpc.2021.106711_bb0220","doi-asserted-by":"crossref","first-page":"698","DOI":"10.1126\/science.aan6398","article-title":"Atomic structures of low-complexity protein segments reveal kinked \u03b2 sheets that assemble networks","volume":"359","author":"Hughes","year":"2018","journal-title":"Science"},{"key":"10.1016\/j.bpc.2021.106711_bb0225","doi-asserted-by":"crossref","first-page":"101194","DOI":"10.1016\/j.jbc.2021.101194","article-title":"Prevalence and species distribution of the low-complexity, amyloid-like, reversible, kinked segment structural motif in amyloid-like fibrils","volume":"297","author":"Hughes","year":"2021","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bpc.2021.106711_bb0230","doi-asserted-by":"crossref","first-page":"1338","DOI":"10.1038\/s41467-017-01424-4","article-title":"Competition between crystal and fibril formation in molecular mutations of amyloidogenic peptides","volume":"8","author":"Reynolds","year":"2017","journal-title":"Nat. Commun."},{"key":"10.1016\/j.bpc.2021.106711_bb0235","doi-asserted-by":"crossref","first-page":"554","DOI":"10.1038\/nature03986","article-title":"Molecular recycling within amyloid fibrils","volume":"436","author":"Carulla","year":"2005","journal-title":"Nature"},{"key":"10.1016\/j.bpc.2021.106711_bb0240","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1016\/j.jmb.2007.10.033","article-title":"Exclusion of the native alpha-helix from the amyloid fibrils of a mixed alpha\/beta protein","volume":"375","author":"Morgan","year":"2008","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bpc.2021.106711_bb0245","article-title":"Heparin-induced tau filaments are polymorphic and differ from those in Alzheimer\u2019s and Pick\u2019s diseases","volume":"8","author":"Zhang","year":"2019","journal-title":"Elife"},{"key":"10.1016\/j.bpc.2021.106711_bb0250","doi-asserted-by":"crossref","first-page":"7133","DOI":"10.1021\/bi00483a001","article-title":"Dominant forces in protein folding","volume":"29","author":"Dill","year":"1990","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpc.2021.106711_bb0255","doi-asserted-by":"crossref","first-page":"684","DOI":"10.1038\/nsmb.1610","article-title":"Localized thermodynamic coupling between hydrogen bonding and microenvironment polarity substantially stabilizes proteins","volume":"16","author":"Gao","year":"2009","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.bpc.2021.106711_bb0260","doi-asserted-by":"crossref","DOI":"10.1021\/acs.biochem.7b00942","article-title":"Biological roles of protein kinetic stability","author":"Colon","year":"2017","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpc.2021.106711_bb0265","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.bpc.2010.02.004","article-title":"Protein kinetic stability","volume":"148","author":"Sanchez-Ruiz","year":"2010","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.bpc.2021.106711_bb0270","doi-asserted-by":"crossref","first-page":"569","DOI":"10.1016\/j.molcel.2009.04.028","article-title":"An unfolded CH1 domain controls the assembly and secretion of IgG antibodies","volume":"34","author":"Feige","year":"2009","journal-title":"Mol. Cell"},{"key":"10.1016\/j.bpc.2021.106711_bb0275","doi-asserted-by":"crossref","first-page":"524","DOI":"10.1016\/j.sbi.2009.07.002","article-title":"Folding of glycoproteins: toward understanding the biophysics of the glycosylation code","volume":"19","author":"Shental-Bechor","year":"2009","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.bpc.2021.106711_bb0280","doi-asserted-by":"crossref","first-page":"3131","DOI":"10.1073\/pnas.0810318105","article-title":"The core trisaccharide of an N-linked glycoprotein intrinsically accelerates folding and enhances stability","volume":"106","author":"Hanson","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bpc.2021.106711_bb0285","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1126\/science.1198461","article-title":"Protein native-state stabilization by placing aromatic side chains in N-glycosylated reverse turns","volume":"331","author":"Culyba","year":"2011","journal-title":"Science"},{"key":"10.1016\/j.bpc.2021.106711_bb0290","doi-asserted-by":"crossref","first-page":"14259","DOI":"10.1021\/bi7013773","article-title":"Heterogeneity in primary structure, post-translational modifications, and germline gene usage of nine full-length amyloidogenic kappa1 immunoglobulin light chains","volume":"46","author":"Connors","year":"2007","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpc.2021.106711_bb0295","doi-asserted-by":"crossref","first-page":"200","DOI":"10.3109\/13506120009146835","article-title":"Four structural risk factors identify most fibril-forming kappa light chains","volume":"7","author":"Stevens","year":"2000","journal-title":"Amyloid"},{"key":"10.1016\/j.bpc.2021.106711_bb0300","doi-asserted-by":"crossref","first-page":"E368","DOI":"10.1002\/ajh.25244","article-title":"MASS-FIX may allow identification of patients at risk for light chain amyloidosis before the onset of symptoms","volume":"93","author":"Kourelis","year":"2018","journal-title":"Am. J. Hematol."},{"key":"10.1016\/j.bpc.2021.106711_bb0305","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1038\/s41408-021-00444-0","article-title":"MASS-FIX for the detection of monoclonal proteins and light chain N-glycosylation in routine clinical practice: a cross-sectional study of 6315 patients","volume":"11","author":"Mellors","year":"2021","journal-title":"Blood Cancer J."},{"key":"10.1016\/j.bpc.2021.106711_bb0310","doi-asserted-by":"crossref","first-page":"1901","DOI":"10.1073\/pnas.1711720115","article-title":"Adaptive antibody diversification through N-linked glycosylation of the immunoglobulin variable region","volume":"115","author":"van de Bovenkamp","year":"2018","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bpc.2021.106711_bb0315","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1016\/j.ijms.2016.11.006","article-title":"Oxidative post-translational modifications of an amyloidogenic immunoglobulin light chain protein","volume":"416","author":"Lu","year":"2017","journal-title":"Int. J. Mass Spectrom."},{"key":"10.1016\/j.bpc.2021.106711_bb0320","article-title":"Protease-sensitive regions in amyloid light chains: what a common pattern of fragmentation across organs suggests about aggregation","author":"Mazzini","year":"2021","journal-title":"FEBS J."},{"key":"10.1016\/j.bpc.2021.106711_bb0325","doi-asserted-by":"crossref","first-page":"1467","DOI":"10.1016\/j.jmb.2004.08.085","article-title":"Probing the high energy states in proteins by proteolysis","volume":"343","author":"Park","year":"2004","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bpc.2021.106711_bb0330","doi-asserted-by":"crossref","first-page":"4953","DOI":"10.1021\/bi00693a026","article-title":"Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues","volume":"14","author":"Brandts","year":"1975","journal-title":"Biochemistry."},{"key":"10.1016\/j.bpc.2021.106711_bb0335","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1038\/nsmb1058","article-title":"Amyloid formation under physiological conditions proceeds via a native-like folding intermediate","volume":"13","author":"Jahn","year":"2006","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.bpc.2021.106711_bb0340","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1038\/nsmb1068","article-title":"A native to amyloidogenic transition regulated by a backbone trigger","volume":"13","author":"Eakin","year":"2006","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.bpc.2021.106711_bb0345","doi-asserted-by":"crossref","first-page":"719","DOI":"10.1016\/j.jmb.2010.04.032","article-title":"Dissecting the alternatively folded state of the antibody fab fragment","volume":"399","author":"Feige","year":"2010","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bpc.2021.106711_bb0350","doi-asserted-by":"crossref","first-page":"6597","DOI":"10.1021\/acs.biochem.7b00579","article-title":"Incomplete refolding of antibody light chains to non-native, protease-sensitive conformations leads to aggregation: a mechanism of amyloidogenesis in patients?","volume":"56","author":"Morgan","year":"2017","journal-title":"Biochemistry."},{"key":"10.1016\/j.bpc.2021.106711_bb0355","doi-asserted-by":"crossref","first-page":"1287","DOI":"10.1016\/0006-291X(70)90227-5","article-title":"An amyloid protein: the amino-terminal variable fragment of an immunoglobulin light chain","volume":"41","author":"Glenner","year":"1970","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bpc.2021.106711_bb0360","doi-asserted-by":"crossref","first-page":"126","DOI":"10.1126\/science.1439760","article-title":"Production of the Alzheimer amyloid beta protein by normal proteolytic processing","volume":"258","author":"Shoji","year":"1992","journal-title":"Science"},{"key":"10.1016\/j.bpc.2021.106711_bb0365","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1146\/annurev-pathol-020712-163913","article-title":"AA amyloidosis: pathogenesis and targeted therapy","volume":"10","author":"Westermark","year":"2015","journal-title":"Annu. Rev. Pathol."},{"key":"10.1016\/j.bpc.2021.106711_bb0370","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1007\/s11883-020-00888-y","article-title":"Structural basis for vital function and malfunction of serum amyloid a: an acute-phase protein that wears hydrophobicity on its sleeve","volume":"22","author":"Gursky","year":"2020","journal-title":"Curr. Atheroscler. Rep."},{"key":"10.1016\/j.bpc.2021.106711_bb0375","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1002\/path.1759","article-title":"Amyloid deposits in transthyretin-derived amyloidosis: cleaved transthyretin is associated with distinct amyloid morphology","volume":"206","author":"Bergstr\u00f6m","year":"2005","journal-title":"J. Pathol."},{"key":"10.1016\/j.bpc.2021.106711_bb0380","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.1802977115","article-title":"Unusual duplication mutation in a surface loop of human transthyretin leads to an aggressive drug-resistant amyloid disease","author":"Klimtchuk","year":"2018","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bpc.2021.106711_bb0385","doi-asserted-by":"crossref","first-page":"1539","DOI":"10.1073\/pnas.1317488111","article-title":"Proteolytic cleavage of Ser52Pro variant transthyretin triggers its amyloid fibrillogenesis","volume":"111","author":"Mangione","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bpc.2021.106711_bb0390","doi-asserted-by":"crossref","first-page":"2319","DOI":"10.1021\/acs.biochem.0c00079","article-title":"Disruption of the CD loop by enzymatic cleavage promotes the formation of toxic transthyretin oligomers through a common transthyretin misfolding pathway","volume":"59","author":"Dasari","year":"2020","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpc.2021.106711_bb0395","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1002\/prot.21919","article-title":"Unfolding and aggregation of transthyretin by the truncation of 50 N-terminal amino acids","volume":"72","author":"Mizuguchi","year":"2008","journal-title":"Proteins."},{"key":"10.1016\/j.bpc.2021.106711_bb0400","doi-asserted-by":"crossref","first-page":"4280","DOI":"10.1016\/j.jmb.2016.08.021","article-title":"The kinetic stability of a full-length antibody light chain dimer determines whether endoproteolysis can release amyloidogenic variable domains","volume":"428","author":"Morgan","year":"2016","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bpc.2021.106711_bb0405","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1016\/S0889-8588(18)30347-2","article-title":"Mechanisms of disease: monoclonal immunoglobulin deposition. Amyloidosis, light chain deposition disease, and light and heavy chain deposition disease","volume":"6","author":"Buxbaum","year":"1992","journal-title":"Hematol. Oncol. Clin. North Am."},{"key":"10.1016\/j.bpc.2021.106711_bb0410","doi-asserted-by":"crossref","DOI":"10.1074\/jbc.RA120.013461","article-title":"Mass spectrometry characterization of light chain fragmentation sites in cardiac AL amyloidosis:insights into the timing of proteolysis","author":"Lavatelli","year":"2020","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bpc.2021.106711_bb0415","doi-asserted-by":"crossref","first-page":"256","DOI":"10.1016\/S0076-6879(99)09019-9","article-title":"Analysis of protein aggregation kinetics","volume":"309","author":"Ferrone","year":"1999","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.bpc.2021.106711_bb0420","doi-asserted-by":"crossref","first-page":"122","DOI":"10.1529\/biophysj.105.073767","article-title":"The kinetics of nucleated polymerizations at high concentrations: amyloid fibril formation near and above the \u201csupercritical concentration\u201d","volume":"91","author":"Powers","year":"2006","journal-title":"Biophys. J."},{"key":"10.1016\/j.bpc.2021.106711_bb0425","doi-asserted-by":"crossref","first-page":"1533","DOI":"10.1126\/science.1178250","article-title":"An analytical solution to the kinetics of breakable filament assembly","volume":"326","author":"Knowles","year":"2009","journal-title":"Science"},{"key":"10.1016\/j.bpc.2021.106711_bb0430","doi-asserted-by":"crossref","first-page":"12709","DOI":"10.1021\/bi050927h","article-title":"Thermodynamics of A\u03b2(1\u221240) amyloid fibril elongation","volume":"44","author":"O\u2019Nuallain","year":"2005","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpc.2021.106711_bb0435","doi-asserted-by":"crossref","first-page":"8926","DOI":"10.1073\/pnas.0711664105","article-title":"Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly","volume":"105","author":"Xue","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bpc.2021.106711_bb0440","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1038\/nprot.2016.010","article-title":"Molecular mechanisms of protein aggregation from global fitting of kinetic models","volume":"11","author":"Meisl","year":"2016","journal-title":"Nat. Protoc."},{"key":"10.1016\/j.bpc.2021.106711_bb0445","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/j.sbi.2015.11.009","article-title":"Revisiting supersaturation as a factor determining amyloid fibrillation","volume":"36","author":"So","year":"2016","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.bpc.2021.106711_bb0450","doi-asserted-by":"crossref","first-page":"1015","DOI":"10.1073\/pnas.1910444117","article-title":"Proteome-wide observation of the phenomenon of life on the edge of solubility","volume":"117","author":"Vecchi","year":"2020","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bpc.2021.106711_bb0455","doi-asserted-by":"crossref","first-page":"6979","DOI":"10.1073\/pnas.092205999","article-title":"Transmissibility of systemic amyloidosis by a prion-like mechanism","volume":"99","author":"Lundmark","year":"2002","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bpc.2021.106711_bb0460","doi-asserted-by":"crossref","first-page":"6098","DOI":"10.1073\/pnas.0501814102","article-title":"Protein fibrils in nature can enhance amyloid protein A amyloidosis in mice: cross-seeding as a disease mechanism","volume":"102","author":"Lundmark","year":"2005","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.bpc.2021.106711_bb0465","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.53111","article-title":"A gut bacterial amyloid promotes \u03b1-synuclein aggregation and motor impairment in mice","volume":"9","author":"Sampson","year":"2020","journal-title":"Elife"},{"key":"10.1016\/j.bpc.2021.106711_bb0470","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41598-021-00588-w","article-title":"AA amyloid in human food chain is a possible biohazard","volume":"11","author":"Rising","year":"2021","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bpc.2021.106711_bb0475","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1111\/j.1600-6143.2006.01585.x","article-title":"Progressive wild-type transthyretin deposition after liver transplantation preferentially occurs onto myocardium in FAP patients","volume":"7","author":"Yazaki","year":"2007","journal-title":"Am. J. Transplant."},{"key":"10.1016\/j.bpc.2021.106711_bb0480","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.1805131115","article-title":"Amyloid seeding of transthyretin by ex vivo cardiac fibrils and its inhibition","author":"Saelices","year":"2018","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bpc.2021.106711_bb0485","doi-asserted-by":"crossref","first-page":"2967","DOI":"10.1021\/acs.biochem.6b00090","article-title":"Recruitment of light chains by homologous and heterologous fibrils shows distinctive kinetic and conformational specificity","volume":"55","author":"Blancas-Mej\u00eda","year":"2016","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpc.2021.106711_bb0490","doi-asserted-by":"crossref","first-page":"3571","DOI":"10.3390\/molecules26123571","article-title":"Barriers to small molecule drug discovery for systemic amyloidosis","volume":"26","author":"Morgan","year":"2021","journal-title":"Molecules"},{"key":"10.1016\/j.bpc.2021.106711_bb0495","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1212\/WNL.0b013e3182661eb1","article-title":"Tafamidis for transthyretin familial amyloid polyneuropathy: a randomized, controlled trial","volume":"79","author":"Coelho","year":"2012","journal-title":"Neurology"},{"key":"10.1016\/j.bpc.2021.106711_bb0500","doi-asserted-by":"crossref","first-page":"1007","DOI":"10.1056\/NEJMoa1805689","article-title":"ATTR-ACT study investigators, tafamidis treatment for patients with transthyretin amyloid cardiomyopathy","volume":"379","author":"Maurer","year":"2018","journal-title":"N. Engl. J. Med."},{"key":"10.1016\/j.bpc.2021.106711_bb0505","doi-asserted-by":"crossref","first-page":"2658","DOI":"10.1001\/jama.2013.283815","article-title":"Repurposing diflunisal for familial amyloid polyneuropathy: a randomized clinical trial","volume":"310","author":"Berk","year":"2013","journal-title":"JAMA"},{"key":"10.1016\/j.bpc.2021.106711_bb0510","doi-asserted-by":"crossref","first-page":"9992","DOI":"10.1073\/pnas.1300761110","article-title":"AG10 inhibits amyloidogenesis and cellular toxicity of the familial amyloid cardiomyopathy-associated V122I transthyretin","volume":"110","author":"Penchala","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bpc.2021.106711_bb0515","first-page":"645","article-title":"Light chain stabilization: a therapeutic approach to ameliorate AL amyloidosis","volume":"2","author":"Morgan","year":"2021","journal-title":"Hematology"},{"key":"10.1016\/j.bpc.2021.106711_bb0520","doi-asserted-by":"crossref","first-page":"8360","DOI":"10.1073\/pnas.1817567116","article-title":"Stabilization of amyloidogenic immunoglobulin light chains by small molecules","volume":"116","author":"Morgan","year":"2019","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bpc.2021.106711_bb0525","doi-asserted-by":"crossref","first-page":"13357","DOI":"10.1073\/pnas.0603772103","article-title":"Inhibition of protein aggregation in vitro and in vivo by a natural osmoprotectant","volume":"103","author":"Ignatova","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bpc.2021.106711_bb0530","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.bpc.2006.12.007","article-title":"Suppression of protein interactions by arginine: a proposed mechanism of the arginine effects","volume":"127","author":"Arakawa","year":"2007","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.bpc.2021.106711_bb0535","doi-asserted-by":"crossref","first-page":"49636","DOI":"10.1074\/jbc.M307996200","article-title":"Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104","volume":"278","author":"Kryndushkin","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bpc.2021.106711_bb0540","doi-asserted-by":"crossref","first-page":"e87133","DOI":"10.1371\/journal.pone.0087133","article-title":"Targeting the intrinsically disordered structural ensemble of \u03b1-synuclein by small molecules as a potential therapeutic strategy for Parkinson\u2019s disease","volume":"9","author":"T\u00f3th","year":"2014","journal-title":"PLoS One"},{"key":"10.1016\/j.bpc.2021.106711_bb0545","doi-asserted-by":"crossref","DOI":"10.1021\/acs.molpharmaceut.9b01080","article-title":"A small molecule inhibitor prevents insulin fibrillogenesis and preserves activity","author":"Das","year":"2020","journal-title":"Mol. Pharm."},{"key":"10.1016\/j.bpc.2021.106711_bb0550","doi-asserted-by":"crossref","first-page":"2349","DOI":"10.1056\/NEJMoa065644","article-title":"Eprodisate for the treatment of renal disease in AA amyloidosis","volume":"356","author":"Dember","year":"2007","journal-title":"N. Engl. J. Med."},{"key":"10.1016\/j.bpc.2021.106711_bb0555","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1038\/nature10154","article-title":"Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation","volume":"475","author":"Sievers","year":"2011","journal-title":"Nature"},{"key":"10.1016\/j.bpc.2021.106711_bb0560","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1006\/jmbi.1999.3110","article-title":"Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm","volume":"293","author":"Wright","year":"1999","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bpc.2021.106711_bb0565","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1016\/S1093-3263(00)00138-8","article-title":"Intrinsically disordered protein","volume":"19","author":"Dunker","year":"2001","journal-title":"J. Mol. Graph. Model."},{"key":"10.1016\/j.bpc.2021.106711_bb0570","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1002\/1097-0134(20001115)41:3<415::AID-PROT130>3.0.CO;2-7","article-title":"Why are \u201cnatively unfolded\u201d proteins unstructured under physiologic conditions?","volume":"41","author":"Uversky","year":"2000","journal-title":"Proteins"},{"key":"10.1016\/j.bpc.2021.106711_bb0575","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1007\/s10858-019-00280-2","article-title":"Perspective: the essential role of NMR in the discovery and characterization of intrinsically disordered proteins","volume":"73","author":"Dyson","year":"2019","journal-title":"J. Biomol. NMR"},{"key":"10.1016\/j.bpc.2021.106711_bb0580","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1146\/annurev-biophys-062920-063704","article-title":"Recent developments in the field of intrinsically disordered proteins: intrinsic disorder-based emergence in cellular biology in light of the physiological and pathological liquid-liquid phase transitions","volume":"50","author":"Uversky","year":"2021","journal-title":"Annu. Rev. Biophys."},{"key":"10.1016\/j.bpc.2021.106711_bb0585","doi-asserted-by":"crossref","first-page":"4661","DOI":"10.1039\/C6CS00542J","article-title":"Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology","volume":"46","author":"Wei","year":"2017","journal-title":"Chem. Soc. Rev."},{"key":"10.1016\/j.bpc.2021.106711_bb0590","doi-asserted-by":"crossref","first-page":"12301","DOI":"10.1073\/pnas.1818206116","article-title":"Unfolded states under folding conditions accommodate sequence-specific conformational preferences with random coil-like dimensions","volume":"116","author":"Peran","year":"2019","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bpc.2021.106711_bb0595","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1016\/j.molcel.2011.05.013","article-title":"Opposing effects of glutamine and asparagine govern prion formation by intrinsically disordered proteins","volume":"43","author":"Halfmann","year":"2011","journal-title":"Mol. Cell"},{"key":"10.1016\/j.bpc.2021.106711_bb0600","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1016\/j.sbi.2021.03.015","article-title":"NMR illuminates intrinsic disorder","volume":"70","author":"Dyson","year":"2021","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.bpc.2021.106711_bb0605","doi-asserted-by":"crossref","DOI":"10.1038\/nature25762","article-title":"Extreme disorder in an ultrahigh-affinity protein complex","author":"Borgia","year":"2018","journal-title":"Nature"},{"key":"10.1016\/j.bpc.2021.106711_bb0610","doi-asserted-by":"crossref","first-page":"871","DOI":"10.1126\/science.abj8754","article-title":"Accurate prediction of protein structures and interactions using a three-track neural network","volume":"373","author":"Baek","year":"2021","journal-title":"Science"},{"key":"10.1016\/j.bpc.2021.106711_bb0615","doi-asserted-by":"crossref","DOI":"10.1038\/s41586-021-03819-2","article-title":"Highly accurate protein structure prediction with AlphaFold","author":"Jumper","year":"2021","journal-title":"Nature"},{"key":"10.1016\/j.bpc.2021.106711_bb0620","article-title":"AlphaFold and the amyloid world","volume":"167059","author":"Pinheiro","year":"2021","journal-title":"J. Mol. Biol."}],"container-title":["Biophysical Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0301462221001940?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0301462221001940?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,4]],"date-time":"2025-10-04T07:57:13Z","timestamp":1759564633000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0301462221001940"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,2]]},"references-count":124,"alternative-id":["S0301462221001940"],"URL":"https:\/\/doi.org\/10.1016\/j.bpc.2021.106711","relation":{},"ISSN":["0301-4622"],"issn-type":[{"value":"0301-4622","type":"print"}],"subject":[],"published":{"date-parts":[[2022,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Transient disorder along pathways to amyloid","name":"articletitle","label":"Article Title"},{"value":"Biophysical Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bpc.2021.106711","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2021 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"106711"}}