{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,19]],"date-time":"2026-08-19T17:59:45Z","timestamp":1787162385992,"version":"build-2736575974"},"reference-count":181,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2025,6,1]],"date-time":"2025-06-01T00:00:00Z","timestamp":1748736000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,6,1]],"date-time":"2025-06-01T00:00:00Z","timestamp":1748736000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,2,24]],"date-time":"2025-02-24T00:00:00Z","timestamp":1740355200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100009708","name":"Novo Nordisk Foundation","doi-asserted-by":"publisher","award":["NNF22OC0072891"],"award-info":[{"award-number":["NNF22OC0072891"]}],"id":[{"id":"10.13039\/501100009708","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000925","name":"National Health and Medical Research Council","doi-asserted-by":"publisher","award":["APP2009991"],"award-info":[{"award-number":["APP2009991"]}],"id":[{"id":"10.13039\/501100000925","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002855","name":"Ministry of Science and Technology of the People's Republic of China","doi-asserted-by":"publisher","award":["G2023033003L"],"award-info":[{"award-number":["G2023033003L"]}],"id":[{"id":"10.13039\/501100002855","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100008394","name":"Independent Research Fund Denmark","doi-asserted-by":"publisher","award":["8021-00208B"],"award-info":[{"award-number":["8021-00208B"]}],"id":[{"id":"10.13039\/100008394","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003554","name":"Lundbeck Foundation","doi-asserted-by":"publisher","award":["R276-2018-671"],"award-info":[{"award-number":["R276-2018-671"]}],"id":[{"id":"10.13039\/501100003554","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["32460228"],"award-info":[{"award-number":["32460228"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002808","name":"Carlsberg Foundation","doi-asserted-by":"publisher","award":["CF19-0337"],"award-info":[{"award-number":["CF19-0337"]}],"id":[{"id":"10.13039\/501100002808","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002808","name":"Carlsberg Foundation","doi-asserted-by":"publisher","award":["CF20-0610"],"award-info":[{"award-number":["CF20-0610"]}],"id":[{"id":"10.13039\/501100002808","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004607","name":"Guangxi Natural Science Foundation","doi-asserted-by":"publisher","award":["2023GXNSFAA026030"],"award-info":[{"award-number":["2023GXNSFAA026030"]}],"id":[{"id":"10.13039\/501100004607","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Molecular Aspects of Medicine"],"published-print":{"date-parts":[[2025,6]]},"DOI":"10.1016\/j.mam.2025.101351","type":"journal-article","created":{"date-parts":[[2025,3,1]],"date-time":"2025-03-01T17:50:47Z","timestamp":1740851447000},"page":"101351","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":17,"special_numbering":"C","title":["Interactions between pathological and functional amyloid: A match made in Heaven or Hell?"],"prefix":"10.1016","volume":"103","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-2918-8989","authenticated-orcid":false,"given":"Daniel E.","family":"Otzen","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Samuel","family":"Pe\u00f1a-D\u00edaz","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jeremias","family":"Widmann","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anders Ogechi Hostrup","family":"Daugberg","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhefei","family":"Zhang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yanting","family":"Jiang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chandrika","family":"Mittal","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Morten K.D.","family":"Dueholm","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nikolaos","family":"Louros","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Huabing","family":"Wang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ibrahim","family":"Javed","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.mam.2025.101351_bib1","doi-asserted-by":"crossref","first-page":"1561","DOI":"10.1038\/s43587-023-00519-6","article-title":"Senolytic therapy alleviates physiological human brain aging and COVID-19 neuropathology","volume":"3","author":"Aguado","year":"2023","journal-title":"Nature Aging"},{"key":"10.1016\/j.mam.2025.101351_bib2","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1016\/j.ijbiomac.2009.12.017","article-title":"DnaK\/DnaJ\/GrpE of Hsp70 system have differing effects on \u03b1-synuclein fibrillation involved in Parkinson's disease","volume":"46","author":"Ahmad","year":"2010","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.mam.2025.101351_bib3","article-title":"Alzheimer's progenitor Amyloid-\u03b2 targets and dissolves microbial amyloids and impairs biofilm function","volume":"10","author":"Ali","year":"2023","journal-title":"Adv. Sci."},{"key":"10.1016\/j.mam.2025.101351_bib4","doi-asserted-by":"crossref","DOI":"10.3389\/fnagi.2023.1240945","article-title":"Brain-inhabiting bacteria and neurodegenerative diseases: the \u201cbrain microbiome\u201d theory","volume":"15","author":"Arabi","year":"2023","journal-title":"Front. Aging Neurosci."},{"key":"10.1016\/j.mam.2025.101351_bib5","doi-asserted-by":"crossref","first-page":"14160","DOI":"10.1021\/ja2017703","article-title":"Metastability of native proteins and the phenomenon of amyloid formation","volume":"133","author":"Baldwin","year":"2011","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.mam.2025.101351_bib6","doi-asserted-by":"crossref","first-page":"S313","DOI":"10.3233\/JPD-191702","article-title":"Gastrointestinal immunity and alpha-synuclein","volume":"9","author":"Barbut","year":"2019","journal-title":"J. Parkinsons Dis."},{"key":"10.1016\/j.mam.2025.101351_bib7","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.bpc.2015.07.002","article-title":"Aggregate structure, morphology and the effect of aggregation mechanisms on viscosity at elevated protein concentrations","volume":"207","author":"Barnett","year":"2015","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.mam.2025.101351_bib8","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.mam.2025.101351_bib9","doi-asserted-by":"crossref","DOI":"10.1080\/19490976.2023.2221813","article-title":"Systemic exposure to bacterial amyloid curli alters the gut mucosal immune response and the microbiome, exacerbating Salmonella-induced arthritis","volume":"15","author":"Bessho","year":"2023","journal-title":"Gut Microbes"},{"key":"10.1016\/j.mam.2025.101351_bib10","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-020-66602-9","article-title":"Amylin and beta amyloid proteins interact to form amorphous heterocomplexes with enhanced toxicity in neuronal cells","volume":"10","author":"Bharadwaj","year":"2020","journal-title":"Sci. Rep."},{"key":"10.1016\/j.mam.2025.101351_bib11","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-020-66602-9","article-title":"Amylin and beta amyloid proteins interact to form amorphous heterocomplexes with enhanced toxicity in neuronal cells","volume":"10","author":"Bharadwaj","year":"2020","journal-title":"Sci. Rep."},{"key":"10.1016\/j.mam.2025.101351_bib12","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2022.102088","article-title":"Mechanistic insights into accelerated \u03b1-synuclein aggregation mediated by human microbiome-associated functional amyloids","volume":"298","author":"Bhoite","year":"2022","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mam.2025.101351_bib13","doi-asserted-by":"crossref","first-page":"3751","DOI":"10.1016\/j.jmb.2018.06.043","article-title":"Protein engineering reveals mechanisms of functional amyloid formation in Pseudomonas aeruginosa biofilms","volume":"430","author":"Bleem","year":"2018","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.mam.2025.101351_bib14","doi-asserted-by":"crossref","first-page":"474","DOI":"10.1016\/j.nbd.2012.07.018","article-title":"Expression pattern and localization of alpha-synuclein in the human enteric nervous system","volume":"48","author":"B\u00f6ttner","year":"2012","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.mam.2025.101351_bib15","doi-asserted-by":"crossref","first-page":"S281","DOI":"10.3233\/JPD-191721","article-title":"Brain-first versus gut-first Parkinson's disease: a hypothesis","volume":"9","author":"Borghammer","year":"2019","journal-title":"J. Parkinsons Dis."},{"key":"10.1016\/j.mam.2025.101351_bib16","doi-asserted-by":"crossref","DOI":"10.1016\/j.nbd.2021.105557","article-title":"Neuropathological evidence of body-first vs. brain-first Lewy body disease","volume":"161","author":"Borghammer","year":"2021","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.mam.2025.101351_bib17","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1016\/S0197-4580(02)00065-9","article-title":"Staging of brain pathology related to sporadic Parkinson's diseases","volume":"24","author":"Braak","year":"2003","journal-title":"Neurobiol. Aging"},{"key":"10.1016\/j.mam.2025.101351_bib18","doi-asserted-by":"crossref","DOI":"10.1128\/mbio.00419-24","article-title":"Structural insight into Escherichia coli CsgA amyloid fibril assembly","volume":"15","author":"Bu","year":"2024","journal-title":"mBio"},{"key":"10.1016\/j.mam.2025.101351_bib19","doi-asserted-by":"crossref","first-page":"334","DOI":"10.1016\/j.cis.2019.05.002","article-title":"Food protein amyloid fibrils: origin, structure, formation, characterization, applications and health implications","volume":"269","author":"Cao","year":"2019","journal-title":"Adv. Colloid Interface Sci."},{"key":"10.1016\/j.mam.2025.101351_bib20","doi-asserted-by":"crossref","first-page":"851","DOI":"10.1126\/science.1067484","article-title":"Role of Eschericia coli curli operons in directing amyloid fiber formation","volume":"295","author":"Chapman","year":"2002","journal-title":"Science"},{"key":"10.1016\/j.mam.2025.101351_bib21","doi-asserted-by":"crossref","first-page":"11119","DOI":"10.1073\/pnas.0901422106","article-title":"Ultrasonication-dependent production and breakdown lead to minimum-sized amyloid fibrils","volume":"106","author":"Chatani","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.mam.2025.101351_bib22","article-title":"Exposure to the functional bacterial amyloid protein curli enhances alpha-synuclein aggregation in aged fischer 344 rats and Caenorhabditis elegans","volume":"6","author":"Chen","year":"2016","journal-title":"Sci. Rep."},{"key":"10.1016\/j.mam.2025.101351_bib23","doi-asserted-by":"crossref","first-page":"1911","DOI":"10.1002\/mds.28553","article-title":"Increased accumulation of alpha-synuclein in inflamed appendices of Parkinson's disease patients","volume":"36","author":"Chen","year":"2021","journal-title":"Mov. Disord."},{"key":"10.1016\/j.mam.2025.101351_bib24","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.mam.2025.101351_bib25","article-title":"A semi high-throughput method for real-time monitoring of curli producing Salmonella biofilms on air-solid interfaces","volume":"3","author":"Choong","year":"2021","journal-title":"Biofilms"},{"key":"10.1016\/j.mam.2025.101351_bib26","doi-asserted-by":"crossref","first-page":"4029","DOI":"10.1021\/acsomega.8b03590","article-title":"Reducing the amyloidogenicity of functional amyloid protein FapC increases its ability to inhibit \u03b1-synuclein fibrillation","volume":"4","author":"Christensen","year":"2019","journal-title":"ACS Omega"},{"key":"10.1016\/j.mam.2025.101351_bib27","doi-asserted-by":"crossref","first-page":"13031","DOI":"10.1074\/jbc.RA120.013396","article-title":"Quantitating denaturation by formic acid: imperfect repeats are essential to the stability of the functional amyloid protein FapC","volume":"295","author":"Christensen","year":"2020","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mam.2025.101351_bib28","doi-asserted-by":"crossref","first-page":"1854","DOI":"10.1002\/pro.4137","article-title":"Identification of amyloidogenic proteins in the microbiomes of a rat Parkinson's disease model and wild-type rats","volume":"30","author":"Christensen","year":"2021","journal-title":"Protein Sci."},{"key":"10.1016\/j.mam.2025.101351_bib29","doi-asserted-by":"crossref","first-page":"781","DOI":"10.1016\/j.celrep.2013.09.043","article-title":"Widespread aggregation and neurodegenerative diseases are associated with supersaturated proteins","volume":"5","author":"Ciryam","year":"2013","journal-title":"Cell Rep."},{"key":"10.1016\/j.mam.2025.101351_bib30","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1038\/nsmb.2971","article-title":"A molecular chaperone breaks the catalytic cycle that generates toxic Abeta oligomers","volume":"22","author":"Cohen","year":"2015","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.mam.2025.101351_bib31","doi-asserted-by":"crossref","first-page":"16938","DOI":"10.1073\/pnas.1112600108","article-title":"Molecular basis for amyloid-\u03b2 polymorphism","volume":"108","author":"Colletier","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.mam.2025.101351_bib32","doi-asserted-by":"crossref","first-page":"4773","DOI":"10.1128\/jb.173.15.4773-4781.1991","article-title":"Purification and characterization of thin, aggregative fimbriae from Salmonella enteritidis","volume":"173","author":"Collinson","year":"1991","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.mam.2025.101351_bib33","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1186\/1471-2105-8-65","article-title":"AGGRESCAN: a server for the prediction and evaluation of \"hot spots\" of aggregation in polypeptides","volume":"8","author":"Conchillo-Sol\u00e9","year":"2007","journal-title":"BMC Bioinf."},{"key":"10.1016\/j.mam.2025.101351_bib34","series-title":"The Physical and Chemical Basis of Molecular Biology","author":"Creighton","year":"2010"},{"key":"10.1016\/j.mam.2025.101351_bib35","doi-asserted-by":"crossref","first-page":"1013","DOI":"10.1007\/s12192-010-0212-z","article-title":"\u03b1B-Crystallin inhibits the cell toxicity associated with amyloid fibril formation by \u03ba-casein and the amyloid-\u03b2 peptide","volume":"15","author":"Dehle","year":"2010","journal-title":"Cell Stress Chaperones"},{"key":"10.1016\/j.mam.2025.101351_bib36","doi-asserted-by":"crossref","first-page":"884","DOI":"10.1038\/nature02261","article-title":"Protein folding and misfolding","volume":"426","author":"Dobson","year":"2003","journal-title":"Nature"},{"key":"10.1016\/j.mam.2025.101351_bib37","doi-asserted-by":"crossref","first-page":"933","DOI":"10.1007\/s00401-017-1691-0","article-title":"Proteomic differences in amyloid plaques in rapidly progressive and sporadic Alzheimer's disease","volume":"133","author":"Drummond","year":"2017","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.mam.2025.101351_bib38","doi-asserted-by":"crossref","first-page":"2803","DOI":"10.1093\/brain\/awaa223","article-title":"Phosphorylated tau interactome in the human Alzheimer's disease brain","volume":"143","author":"Drummond","year":"2020","journal-title":"Brain"},{"key":"10.1016\/j.mam.2025.101351_bib39","doi-asserted-by":"crossref","first-page":"1009","DOI":"10.1111\/j.1365-2958.2010.07269.x","article-title":"Functional amyloid in Pseudomonas","volume":"77","author":"Dueholm","year":"2010","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.mam.2025.101351_bib40","doi-asserted-by":"crossref","first-page":"8281","DOI":"10.1021\/bi200967c","article-title":"Fibrillation of the Major Curli Subunit CsgA under changing conditions implies robust design of aggregation","volume":"50","author":"Dueholm","year":"2011","journal-title":"Biochemistry"},{"key":"10.1016\/j.mam.2025.101351_bib41","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0051274","article-title":"Curli functional amyloid systems are phylogenetically widespread and display large diversity in operon and protein structure","volume":"7","author":"Dueholm","year":"2012","journal-title":"PLoS One"},{"key":"10.1016\/j.mam.2025.101351_bib42","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0076630","article-title":"Evolutionary insight into the functional amyloids of the Pseudomonads","volume":"8","author":"Dueholm","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.mam.2025.101351_bib43","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1002\/mbo3.81","article-title":"Expression of Fap amyloids in Pseudomonas aeruginosa, P. fluorescens, and P. putida results in aggregation and increased biofilm formation","volume":"2","author":"Dueholm","year":"2013","journal-title":"Microbiology Open"},{"key":"10.1016\/j.mam.2025.101351_bib44","doi-asserted-by":"crossref","DOI":"10.3389\/fnagi.2020.00265","article-title":"Mechanisms of pathogenic tau and A\u03b2 protein spreading in Alzheimer's disease","volume":"12","author":"d\u2018Errico","year":"2020","journal-title":"Front. Aging Neurosci."},{"key":"10.1016\/j.mam.2025.101351_bib45","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1146\/annurev-biochem-061516-045104","article-title":"Structural studies of amyloid proteins at the molecular level","volume":"86","author":"Eisenberg","year":"2017","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.mam.2025.101351_bib46","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1016\/j.molcel.2014.12.025","article-title":"The bacterial curli system possesses a potent and selective inhibitor of amyloid formation","volume":"57","author":"Evans","year":"2015","journal-title":"Mol. Cell"},{"key":"10.1016\/j.mam.2025.101351_bib47","doi-asserted-by":"crossref","first-page":"4150","DOI":"10.1038\/s41467-024-48309-x","article-title":"Gut microbiota produces biofilm-associated amyloids with potential for neurodegeneration","volume":"15","author":"Fern\u00e1ndez-Calvet","year":"2024","journal-title":"Nat. Commun."},{"key":"10.1016\/j.mam.2025.101351_bib48","series-title":"Structure and Mechanism in Protein Science. A Guide to Enzyme Catalysis and Protein Folding","author":"Fersht","year":"1999"},{"key":"10.1016\/j.mam.2025.101351_bib49","doi-asserted-by":"crossref","first-page":"5460","DOI":"10.1021\/acsnano.4c13916","article-title":"Amyloid targeting-gold nanoparticles-assisted X-ray therapy rescues islet \u03b2-cells from amyloid fibrils and restores insulin homeostasis","volume":"19","author":"Forgham","year":"2025","journal-title":"ACS Nano"},{"key":"10.1016\/j.mam.2025.101351_bib50","doi-asserted-by":"crossref","DOI":"10.3390\/ijms222312983","article-title":"Truncation-driven lateral association of \u03b1-synuclein hinders amyloid clearance by the hsp70-based disaggregase","volume":"22","author":"Franco","year":"2021","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.mam.2025.101351_bib51","doi-asserted-by":"crossref","first-page":"569","DOI":"10.1007\/s00428-016-1916-y","article-title":"Amyloid in biopsies of the gastrointestinal tract-a retrospective observational study on 542 patients","volume":"468","author":"Freudenthaler","year":"2016","journal-title":"Virchows Arch."},{"key":"10.1016\/j.mam.2025.101351_bib52","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/j.sbi.2019.09.001","article-title":"Amyloid structures: much more than just a cross-\u03b2 fold","volume":"60","author":"Gallardo","year":"2020","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.mam.2025.101351_bib53","doi-asserted-by":"crossref","first-page":"967","DOI":"10.1021\/acschemneuro.7b00396","article-title":"Islet amyloid Polypeptide promotes amyloid-beta aggregation by binding-induced helix-unfolding of the amyloidogenic core","volume":"9","author":"Ge","year":"2018","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.mam.2025.101351_bib54","series-title":"Bionanoimaging: : Insights into Protein Misfolding and Aggregation","author":"Ghodke","year":"2013"},{"key":"10.1016\/j.mam.2025.101351_bib55","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-024-54212-2","article-title":"The inhibitory action of the chaperone BRICHOS against the \u03b1-Synuclein secondary nucleation pathway","volume":"15","author":"Ghosh","year":"2024","journal-title":"Nat. Commun."},{"key":"10.1016\/j.mam.2025.101351_bib56","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1034\/j.1399-3038.2001.012002083.x","article-title":"Hypoallergenicity of an extensively hydrolyzed whey formula","volume":"12","author":"Giampietro","year":"2001","journal-title":"Pediatr. Allergy Immunol."},{"key":"10.1016\/j.mam.2025.101351_bib57","series-title":"Amyloid Fibrils and Prefibrillar Aggregates","first-page":"295","author":"Giehm","year":"2012"},{"key":"10.1016\/j.mam.2025.101351_bib58","doi-asserted-by":"crossref","DOI":"10.3389\/fmolb.2022.926959","article-title":"Structure and conservation of amyloid spines from the Candida albicans Als5 adhesin","volume":"9","author":"Golan","year":"2022","journal-title":"Front. Mol. Biosci."},{"key":"10.1016\/j.mam.2025.101351_bib59","doi-asserted-by":"crossref","first-page":"3487","DOI":"10.1073\/pnas.0915166107","article-title":"Identifying the amylome, proteins capable of forming amyloid-like fibrils","volume":"107","author":"Goldschmidt","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.mam.2025.101351_bib60","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1038\/s41594-018-0045-5","article-title":"Atomic-level evidence for packing and positional amyloid polymorphism by segment from TDP-43 RRM2","volume":"25","author":"Guenther","year":"2018","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.mam.2025.101351_bib61","article-title":"Integrated microbiome and host transcriptome profiles link Parkinson's disease to Blautia genus: evidence from feces, blood, and brain","volume":"13","author":"Guo","year":"2022","journal-title":"Front. Microbiol."},{"key":"10.1016\/j.mam.2025.101351_bib62","doi-asserted-by":"crossref","first-page":"12494","DOI":"10.1073\/pnas.0703310104","article-title":"The curli nucleator protein, CsgB, contains an amyloidogenic domain that directs CsgA polymerization","volume":"104","author":"Hammer","year":"2007","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.mam.2025.101351_bib63","doi-asserted-by":"crossref","first-page":"376","DOI":"10.1016\/j.jmb.2012.05.043","article-title":"The C-terminal repeating units of CsgB direct bacterial functional amyloid nucleation","volume":"422","author":"Hammer","year":"2012","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.mam.2025.101351_bib64","doi-asserted-by":"crossref","DOI":"10.7717\/peerj.5","article-title":"Bacterial curli protein promotes the conversion of PAP248-286 into the amyloid SEVI: cross-seeding of dissimilar amyloid sequences","volume":"1","author":"Hartman","year":"2013","journal-title":"PeerJ"},{"key":"10.1016\/j.mam.2025.101351_bib65","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.jconrel.2021.06.005","article-title":"Root cause determination of intraperitoneal catheter obstructions: insulin amyloid aggregates vs foreign body reaction","volume":"336","author":"He","year":"2021","journal-title":"J. Contr. Release"},{"key":"10.1016\/j.mam.2025.101351_bib66","doi-asserted-by":"crossref","first-page":"1094","DOI":"10.1016\/j.jmb.2006.02.039","article-title":"Standard conformations of \u03b2-arches in \u03b2-solenoid proteins","volume":"358","author":"Hennetin","year":"2006","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.mam.2025.101351_bib67","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1021\/pr500938x","article-title":"Major proteomic changes associated with amyloid-induced biofilm formation in Pseudomonas aeruginosa PAO1","volume":"14","author":"Herbst","year":"2015","journal-title":"J. Proteome Res."},{"key":"10.1016\/j.mam.2025.101351_bib68","doi-asserted-by":"crossref","first-page":"634","DOI":"10.1038\/s41589-024-01580-x","article-title":"Discovery of potent inhibitors of \u03b1-synuclein aggregation using structure-based iterative learning","volume":"20","author":"Horne","year":"2024","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.mam.2025.101351_bib69","doi-asserted-by":"crossref","first-page":"12473","DOI":"10.1073\/pnas.1610371113","article-title":"Cross-talk between amyloidogenic proteins in type-2 diabetes and Parkinson's disease","volume":"113","author":"Horvath","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.mam.2025.101351_bib70","doi-asserted-by":"crossref","first-page":"172","DOI":"10.1186\/s12974-018-1210-9","article-title":"Co-aggregation of pro-inflammatory S100A9 with \u03b1-synuclein in Parkinson's disease: ex vivo and in vitro studies","volume":"15","author":"Horvath","year":"2018","journal-title":"J. Neuroinflammation"},{"key":"10.1016\/j.mam.2025.101351_bib71","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pbio.3002650","article-title":"Amyloid accelerator polyphosphate fits as the mystery density in \u03b1-synuclein fibrils","volume":"22","author":"Huettemann","year":"2024","journal-title":"PLoS Biol."},{"key":"10.1016\/j.mam.2025.101351_bib72","doi-asserted-by":"crossref","first-page":"698","DOI":"10.1126\/science.aan6398","article-title":"Atomic structures of low-complexity protein segments reveal kinked beta sheets that assemble networks","volume":"359","author":"Hughes","year":"2018","journal-title":"Science"},{"key":"10.1016\/j.mam.2025.101351_bib73","doi-asserted-by":"crossref","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.mam.2025.101351_bib74","doi-asserted-by":"crossref","DOI":"10.1093\/braincomms\/fcaa007","article-title":"Neuroanatomical spread of amyloid \u03b2 and tau in Alzheimer's disease: implications for primary prevention","volume":"2","author":"Insel","year":"2020","journal-title":"Brain Communications"},{"key":"10.1016\/j.mam.2025.101351_bib75","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1007\/s00018-023-04819-3","article-title":"Intestinal infection triggers mitochondria-mediated alpha-synuclein pathology: relevance to Parkinson's disease","volume":"80","author":"J","year":"2023","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.mam.2025.101351_bib76","doi-asserted-by":"crossref","first-page":"1098","DOI":"10.1053\/j.gastro.2024.04.032","article-title":"Gastrointestinal biofilms: endoscopic detection, disease relevance, and therapeutic strategies","volume":"167","author":"Jandl","year":"2024","journal-title":"Gastroenterology"},{"key":"10.1016\/j.mam.2025.101351_bib77","doi-asserted-by":"crossref","first-page":"4316","DOI":"10.1021\/acs.biomac.7b01359","article-title":"Cofibrillization of pathogenic and functional amyloid proteins with gold nanoparticles against amyloidogenesis","volume":"18","author":"Javed","year":"2017","journal-title":"Biomacromolecules"},{"key":"10.1016\/j.mam.2025.101351_bib78","doi-asserted-by":"crossref","first-page":"5797","DOI":"10.1021\/acs.nanolett.8b02446","article-title":"In vivo mitigation of amyloidogenesis through functional\u2013pathogenic double-protein coronae","volume":"18","author":"Javed","year":"2018","journal-title":"Nano Lett."},{"key":"10.1016\/j.mam.2025.101351_bib79","article-title":"Accelerated amyloid beta pathogenesis by bacterial amyloid FapC","volume":"7","author":"Javed","year":"2020","journal-title":"Adv. Sci."},{"key":"10.1016\/j.mam.2025.101351_bib80","article-title":"Accelerated amyloid beta pathogenesis by bacterial amyloid FapC","volume":"7","author":"Javed","year":"2020","journal-title":"Adv. Sci."},{"key":"10.1016\/j.mam.2025.101351_bib81","doi-asserted-by":"crossref","DOI":"10.1002\/adma.202205072","article-title":"Functional coating from amyloid superwetting films","volume":"34","author":"Jin","year":"2022","journal-title":"Adv. Mater."},{"key":"10.1016\/j.mam.2025.101351_bib82","doi-asserted-by":"crossref","DOI":"10.1080\/19490976.2023.2167172","article-title":"Gut-derived \u03b2-amyloid: likely a centerpiece of the gut\u2013brain axis contributing to Alzheimer's pathogenesis","volume":"15","author":"Jin","year":"2023","journal-title":"Gut Microbes"},{"key":"10.1016\/j.mam.2025.101351_bib83","doi-asserted-by":"crossref","first-page":"437","DOI":"10.3233\/JAD-2008-13408","article-title":"Alzheimer's disease and peripheral infections: the possible contribution from periodontal infections, model and hypothesis","volume":"13","author":"Kamer","year":"2008","journal-title":"J Alzheimers Dis"},{"key":"10.1016\/j.mam.2025.101351_bib84","doi-asserted-by":"crossref","first-page":"6492","DOI":"10.1039\/C7CS00372B","article-title":"Implications of peptide assemblies in amyloid diseases","volume":"46","author":"Ke","year":"2017","journal-title":"Chem. Soc. Rev."},{"key":"10.1016\/j.mam.2025.101351_bib85","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.mam.2025.101351_bib86","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-020-68887-2","article-title":"The hot sites of \u03b1-synuclein in amyloid fibril formation","volume":"10","author":"Khammari","year":"2020","journal-title":"Sci. Rep."},{"key":"10.1016\/j.mam.2025.101351_bib87","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1016\/j.neuron.2019.05.035","article-title":"Transneuronal propagation of pathologic \u03b1-synuclein from the gut to the brain models Parkinson's disease","volume":"103","author":"Kim","year":"2019","journal-title":"Neuron"},{"key":"10.1016\/j.mam.2025.101351_bib88","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1016\/j.neuron.2019.05.035","article-title":"Transneuronal Propagation of pathologic \u03b1-Synuclein from the Gut to the brain models Parkinson's disease","volume":"103","author":"Kim","year":"2019","journal-title":"Neuron"},{"key":"10.1016\/j.mam.2025.101351_bib89","doi-asserted-by":"crossref","DOI":"10.15252\/embj.2021108591","article-title":"Heterotypic Amyloid beta interactions facilitate amyloid assembly and modify amyloid structure","volume":"41","author":"Konstantoulea","year":"2022","journal-title":"EMBO J."},{"key":"10.1016\/j.mam.2025.101351_bib90","doi-asserted-by":"crossref","first-page":"2025","DOI":"10.1111\/febs.15719","article-title":"Heterotypic interactions in amyloid function and disease","volume":"289","author":"Konstantoulea","year":"2022","journal-title":"FEBS J."},{"key":"10.1016\/j.mam.2025.101351_bib91","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.jmii.2022.10.003","article-title":"Long COVID: an inevitable sequela of SARS-CoV-2 infection","volume":"56","author":"Lai","year":"2023","journal-title":"J. Microbiol. Immunol. Infect."},{"key":"10.1016\/j.mam.2025.101351_bib92","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pbio.1001080","article-title":"Towards a pharmacophore for amyloid","volume":"9","author":"Landau","year":"2011","journal-title":"PLoS Biol."},{"key":"10.1016\/j.mam.2025.101351_bib93","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1016\/j.foodchem.2015.07.044","article-title":"Evaluation of protease resistance and toxicity of amyloid-like food fibrils from whey, soy, kidney bean, and egg white","volume":"192","author":"Lass\u00e9","year":"2016","journal-title":"Food Chem."},{"key":"10.1016\/j.mam.2025.101351_bib94","doi-asserted-by":"crossref","first-page":"2833","DOI":"10.1038\/s41467-023-38495-5","article-title":"The in-tissue molecular architecture of \u03b2-amyloid pathology in the mammalian brain","volume":"14","author":"Leistner","year":"2023","journal-title":"Nat. Commun."},{"key":"10.1016\/j.mam.2025.101351_bib95","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1038\/s41467-024-44814-1","article-title":"Endothelial leakiness elicited by amyloid protein aggregation","volume":"15","author":"Li","year":"2024","journal-title":"Nat. Commun."},{"key":"10.1016\/j.mam.2025.101351_bib96","doi-asserted-by":"crossref","DOI":"10.1177\/26331055211018709","article-title":"Is there a brain microbiome?","volume":"16","author":"Link","year":"2021","journal-title":"Neurosci Insights"},{"key":"10.1016\/j.mam.2025.101351_bib97","doi-asserted-by":"crossref","DOI":"10.1038\/s41594-020-0505-6","article-title":"Kinetic fingerprints differentiate the mechanisms of action of anti-A\u03b2 antibodies","volume":"27","author":"Linse","year":"2020","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.mam.2025.101351_bib98","doi-asserted-by":"crossref","first-page":"176","DOI":"10.1016\/j.sbi.2021.11.007","article-title":"Heterotypic amyloid interactions: clues to polymorphic bias and selective cellular vulnerability?","volume":"72","author":"Louros","year":"2022","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.mam.2025.101351_bib99","doi-asserted-by":"crossref","first-page":"176","DOI":"10.1016\/j.sbi.2021.11.007","article-title":"Heterotypic amyloid interactions: clues to polymorphic bias and selective cellular vulnerability?","volume":"72","author":"Louros","year":"2022","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.mam.2025.101351_bib100","doi-asserted-by":"crossref","first-page":"2636","DOI":"10.1093\/bioinformatics\/btac126","article-title":"StAmP-DB: a platform for structures of polymorphic amyloid fibril cores","volume":"38","author":"Louros","year":"2022","journal-title":"Bioinformatics"},{"key":"10.1016\/j.mam.2025.101351_bib101","doi-asserted-by":"crossref","first-page":"1351","DOI":"10.1038\/s41467-022-28955-9","article-title":"Mapping the sequence specificity of heterotypic amyloid interactions enables the identification of aggregation modifiers","volume":"13","author":"Louros","year":"2022","journal-title":"Nat. Commun."},{"key":"10.1016\/j.mam.2025.101351_bib102","doi-asserted-by":"crossref","first-page":"1351","DOI":"10.1038\/s41467-022-28955-9","article-title":"Mapping the sequence specificity of heterotypic amyloid interactions enables the identification of aggregation modifiers","volume":"13","author":"Louros","year":"2022","journal-title":"Nat. Commun."},{"key":"10.1016\/j.mam.2025.101351_bib103","doi-asserted-by":"crossref","first-page":"912","DOI":"10.1038\/s41580-023-00647-2","article-title":"Mechanisms and pathology of protein misfolding and aggregation","volume":"24","author":"Louros","year":"2023","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.mam.2025.101351_bib104","doi-asserted-by":"crossref","first-page":"697","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. USA"},{"key":"10.1016\/j.mam.2025.101351_bib105","doi-asserted-by":"crossref","first-page":"883","DOI":"10.1007\/s12640-019-00014-0","article-title":"Abundance of synaptic vesicle-related proteins in alpha-synuclein-containing protein inclusions suggests a targeted formation mechanism","volume":"35","author":"McCormack","year":"2019","journal-title":"Neurotox. Res."},{"key":"10.1016\/j.mam.2025.101351_bib106","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.mam.2025.101351_bib107","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.abn6831","article-title":"Uncovering the universality of self-replication in protein aggregation and its link to disease","volume":"8","author":"Meisl","year":"2022","journal-title":"Sci. Adv."},{"key":"10.1016\/j.mam.2025.101351_bib108","doi-asserted-by":"crossref","first-page":"437","DOI":"10.3233\/JAD-2008-13408","article-title":"Alzheimer's disease and peripheral infections: the possible contribution from periodontal infections, model and hypothesis","volume":"13","author":"Miklossy","year":"2008","journal-title":"J. Alzheim. Dis."},{"key":"10.1016\/j.mam.2025.101351_bib109","doi-asserted-by":"crossref","first-page":"1823","DOI":"10.1021\/acsomega.0c03670","article-title":"Heating wheat gluten promotes the formation of amyloid-like fibrils","volume":"6","author":"Monge-Morera","year":"2021","journal-title":"ACS Omega"},{"key":"10.1016\/j.mam.2025.101351_bib110","doi-asserted-by":"crossref","first-page":"1221","DOI":"10.2174\/092986707780597989","article-title":"A false paradise - mixed blessings in the protein universe: the amyloid as a new challenge in drug development","volume":"14","author":"Morozova-Roche","year":"2007","journal-title":"Curr. Med. Chem."},{"key":"10.1016\/j.mam.2025.101351_bib111","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1016\/j.xphs.2015.11.002","article-title":"Immunogenicity of therapeutic protein aggregates","volume":"105","author":"Moussa","year":"2016","journal-title":"J. Pharmaceut. Sci."},{"key":"10.1016\/j.mam.2025.101351_bib112","doi-asserted-by":"crossref","first-page":"536","DOI":"10.1039\/D1SC05790A","article-title":"Chaperones mainly suppress primary nucleation during formation of functional amyloid required for bacterial biofilm formation","volume":"13","author":"Nagaraj","year":"2022","journal-title":"Chem. Sci."},{"key":"10.1016\/j.mam.2025.101351_bib113","doi-asserted-by":"crossref","first-page":"601","DOI":"10.1016\/j.jmb.2012.01.050","article-title":"Multiple roles of heparin in the aggregation of p25\u03b1","volume":"421","author":"Nielsen","year":"2012","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.mam.2025.101351_bib114","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1080\/13506129.2016.1179183","article-title":"Insulin amyloid at injection sites of patients with diabetes","volume":"23","author":"Nilsson","year":"2016","journal-title":"Amyloid"},{"key":"10.1016\/j.mam.2025.101351_bib115","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1007\/s11892-014-0487-z","article-title":"Diabetes mellitus and Dementia","volume":"14","author":"Ninomiya","year":"2014","journal-title":"Curr. Diabetes Rep."},{"key":"10.1016\/j.mam.2025.101351_bib116","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1038\/s42003-020-01641-6","article-title":"Breakdown of supersaturation barrier links protein folding to amyloid formation","volume":"4","author":"Noji","year":"2021","journal-title":"Commun. Biol."},{"key":"10.1016\/j.mam.2025.101351_bib117","doi-asserted-by":"crossref","first-page":"30773","DOI":"10.1016\/S0021-9258(18)47347-4","article-title":"The Alzheimer A beta peptide develops protease resistance in association with its polymerization into fibrils","volume":"269","author":"Nordstedt","year":"1994","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mam.2025.101351_bib118","doi-asserted-by":"crossref","first-page":"8945","DOI":"10.1021\/jacs.2c03925","article-title":"Amyloidogenesis of SARS-CoV-2 spike protein","volume":"144","author":"Nystr\u00f6m","year":"2022","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.mam.2025.101351_bib119","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1186\/s40780-019-0151-5","article-title":"Investigation of factors that cause insulin precipitation and\/or amyloid formation in insulin formulations","volume":"5","author":"Ohno","year":"2019","journal-title":"Journal of Pharmaceutical Health Care and Sciences"},{"key":"10.1016\/j.mam.2025.101351_bib120","doi-asserted-by":"crossref","DOI":"10.2337\/dc13-1651","article-title":"Localized amyloidosis at the site of repeated insulin injection in a patient with type 2 diabetes","volume":"36","author":"Okamura","year":"2013","journal-title":"Diabetes Care"},{"key":"10.1016\/j.mam.2025.101351_bib121","doi-asserted-by":"crossref","first-page":"883","DOI":"10.1111\/j.1471-4159.2012.07847.x","article-title":"Cross-seeding effects of amyloid \u03b2-protein and \u03b1-synuclein","volume":"122","author":"Ono","year":"2012","journal-title":"J. Neurochem."},{"key":"10.1016\/j.mam.2025.101351_bib122","doi-asserted-by":"crossref","first-page":"834","DOI":"10.1016\/j.ajpath.2014.11.016","article-title":"In vivo seeding and cross-seeding of localized amyloidosis: a molecular link between type 2 diabetes and alzheimer disease","volume":"185","author":"Oskarsson","year":"2015","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.mam.2025.101351_bib123","doi-asserted-by":"crossref","first-page":"1207","DOI":"10.1016\/j.str.2011.08.005","article-title":"Assembling good amyloid: some structures at last","volume":"19","author":"Otzen","year":"2011","journal-title":"Structure"},{"key":"10.1016\/j.mam.2025.101351_bib124","doi-asserted-by":"crossref","DOI":"10.1101\/cshperspect.a033860","article-title":"Functional amyloids","volume":"11","author":"Otzen","year":"2019","journal-title":"Cold Spring Harbor Perspect. Biol."},{"key":"10.1016\/j.mam.2025.101351_bib125","doi-asserted-by":"crossref","first-page":"1872","DOI":"10.1002\/art.41400","article-title":"Persistent bacteriuria and antibodies recognizing curli\/eDNA complexes from Escherichia coli are linked to flares in systemic lupus erythematosus","volume":"72","author":"Pachucki","year":"2020","journal-title":"Arthritis Rheumatol."},{"key":"10.1016\/j.mam.2025.101351_bib126","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1016\/j.jmb.2005.09.100","article-title":"The changing face of glucagon fibrillation: structural polymorphism and conformational imprinting","volume":"355","author":"Pedersen","year":"2006","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.mam.2025.101351_bib127","doi-asserted-by":"crossref","first-page":"4181","DOI":"10.1529\/biophysj.105.070912","article-title":"Sulfates dramatically stabilize a salt dependent type of glucagon fibrils","volume":"90","author":"Pedersen","year":"2006","journal-title":"Biophys. J."},{"key":"10.1016\/j.mam.2025.101351_bib128","doi-asserted-by":"crossref","first-page":"4591","DOI":"10.1111\/j.1742-4658.2010.07888.x","article-title":"Amyloid structure - one but not the same: the many levels of fibrillar polymorphism","volume":"277","author":"Pedersen","year":"2010","journal-title":"FEBS J."},{"key":"10.1016\/j.mam.2025.101351_bib129","article-title":"Functional amyloids: the biomaterials of tomorrow?","author":"Pe\u00f1a-D\u00edaz","year":"2024","journal-title":"Advanced Materials n\/a"},{"key":"10.1016\/j.mam.2025.101351_bib130","doi-asserted-by":"crossref","DOI":"10.3390\/biomedicines10123226","article-title":"Transthyretin cardiac amyloidosis: a cardio-orthopedic disease","volume":"10","author":"Perfetto","year":"2022","journal-title":"Biomedicines"},{"key":"10.1016\/j.mam.2025.101351_bib131","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1007978","article-title":"Structural insights into curli CsgA cross-\u03b2 fibril architecture inspire repurposing of anti-amyloid compounds as anti-biofilm agents","volume":"15","author":"Perov","year":"2019","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.mam.2025.101351_bib132","doi-asserted-by":"crossref","first-page":"5104","DOI":"10.1039\/D2CC00695B","article-title":"Amyloid fibril-UiO-66-NH2 aerogels for environmental remediation","volume":"58","author":"Peydayesh","year":"2022","journal-title":"Chem. Commun."},{"key":"10.1016\/j.mam.2025.101351_bib133","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/j.pbiomolbio.2022.09.001","article-title":"Insulin fibrillation: strategies for inhibition","volume":"175","author":"Qafary","year":"2022","journal-title":"Prog. Biophys. Mol. Biol."},{"key":"10.1016\/j.mam.2025.101351_bib134","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1016\/j.sbi.2021.01.006","article-title":"Functional and pathological amyloid structures in the eyes of 2020 cryo-EM","volume":"68","author":"Ragonis-Bachar","year":"2021","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.mam.2025.101351_bib135","doi-asserted-by":"crossref","first-page":"633","DOI":"10.1002\/pro.3566","article-title":"Imperfect repeats in the functional amyloid protein FapC reduce the tendency to secondary nucleation and fragmentation during fibrillation","volume":"28","author":"Rasmussen","year":"2019","journal-title":"Prot. Sci."},{"key":"10.1016\/j.mam.2025.101351_bib136","doi-asserted-by":"crossref","DOI":"10.1016\/j.jmb.2022.167878","article-title":"FapA is an intrinsically disordered chaperone for Pseudomonas functional amyloid FapC","volume":"435","author":"Rasmussen","year":"2023","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.mam.2025.101351_bib137","doi-asserted-by":"crossref","first-page":"99","DOI":"10.3109\/1547691X.2013.821564","article-title":"Immunogenicity of therapeutic proteins: influence of aggregation","volume":"11","author":"Ratanji","year":"2014","journal-title":"J. Immunot."},{"key":"10.1016\/j.mam.2025.101351_bib138","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1016\/j.sbi.2007.01.004","article-title":"The molecular architecture of protein-protein binding sites","volume":"17","author":"Reichmann","year":"2007","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.mam.2025.101351_bib139","doi-asserted-by":"crossref","first-page":"113","DOI":"10.2147\/JIR.S196552","article-title":"Colonic inflammation affects myenteric alpha-synuclein in nonhuman primates","volume":"12","author":"Resnikoff","year":"2019","journal-title":"J. Inflamm. Res."},{"key":"10.1016\/j.mam.2025.101351_bib140","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.53111","article-title":"A gut bacterial amyloid promotes a-synuclein aggregation and motor impairment in mice","volume":"9","author":"Sampson","year":"2020","journal-title":"Elife"},{"key":"10.1016\/j.mam.2025.101351_bib141","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.53111","article-title":"A gut bacterial amyloid promotes alpha-synuclein aggregation and motor impairment in mice","volume":"9","author":"Sampson","year":"2020","journal-title":"Elife"},{"key":"10.1016\/j.mam.2025.101351_bib142","doi-asserted-by":"crossref","first-page":"12702","DOI":"10.1021\/jacs.4c02262","article-title":"A targetable N-terminal motif orchestrates \u03b1-synuclein oligomer-to-fibril conversion","volume":"146","author":"Santos","year":"2024","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.mam.2025.101351_bib143","doi-asserted-by":"crossref","first-page":"608","DOI":"10.1038\/s41579-022-00767-0","article-title":"The biofilm life cycle: expanding the conceptual model of biofilm formation","volume":"20","author":"Sauer","year":"2022","journal-title":"Nat. Rev. Microbiol."},{"key":"10.1016\/j.mam.2025.101351_bib144","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1038\/nature05695","article-title":"Atomic structures of amyloid cross-\u03b2 spines reveal varied steric zippers","volume":"447","author":"Sawaya","year":"2007","journal-title":"Nature"},{"key":"10.1016\/j.mam.2025.101351_bib145","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.mam.2025.101351_bib146","doi-asserted-by":"crossref","first-page":"W382","DOI":"10.1093\/nar\/gki387","article-title":"The FoldX web server: an online force field","volume":"33","author":"Schymkowitz","year":"2005","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.mam.2025.101351_bib147","doi-asserted-by":"crossref","first-page":"1178","DOI":"10.1038\/s41594-020-00515-z","article-title":"The three-dimensional structure of human \u03b2-endorphin amyloid fibrils","volume":"27","author":"Seuring","year":"2020","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.mam.2025.101351_bib148","doi-asserted-by":"crossref","first-page":"10477","DOI":"10.2147\/CMAR.S208818","article-title":"CDH1 (E-Cadherin) mutation and gastric cancer: genetics, molecular mechanisms and guidelines for management","volume":"11","author":"Shenoy","year":"2019","journal-title":"Cancer Manag. Res."},{"key":"10.1016\/j.mam.2025.101351_bib149","article-title":"Young rat microbiota extracts strongly inhibit fibrillation of \u03b1-synuclein and protect neuroblastoma cells and zebrafish against \u03b1-synuclein toxicity","author":"Shiraz","year":"2024","journal-title":"Mol. Cells"},{"key":"10.1016\/j.mam.2025.101351_bib150","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1038\/msb.2011.75","article-title":"Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega","volume":"7","author":"Sievers","year":"2011","journal-title":"Mol. Syst. Biol."},{"key":"10.1016\/j.mam.2025.101351_bib151","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1186\/s13024-023-00628-1","article-title":"Overexpression of human \u03b1-synuclein leads to dysregulated microbiome\/metabolites with ageing in a rat model of Parkinson disease","volume":"18","author":"Singh","year":"2023","journal-title":"Mol. Neurodegener."},{"key":"10.1016\/j.mam.2025.101351_bib152","doi-asserted-by":"crossref","first-page":"2822","DOI":"10.1038\/s41467-023-38204-2","article-title":"Structural analysis and architectural principles of the bacterial amyloid curli","volume":"14","author":"Sleutel","year":"2023","journal-title":"Nat. Commun."},{"key":"10.1016\/j.mam.2025.101351_bib153","doi-asserted-by":"crossref","first-page":"270","DOI":"10.1080\/19490976.2018.1546522","article-title":"Hydrogen cross-feeders of the human gastrointestinal tract","volume":"10","author":"Smith","year":"2019","journal-title":"Gut Microbes"},{"key":"10.1016\/j.mam.2025.101351_bib154","doi-asserted-by":"crossref","first-page":"4080","DOI":"10.3390\/molecules27134080","article-title":"Functional bacterial amyloids: understanding fibrillation, regulating biofilm fibril formation and organizing surface assemblies","volume":"27","author":"S\u00f8nderby","year":"2022","journal-title":"Molecules"},{"key":"10.1016\/j.mam.2025.101351_bib155","doi-asserted-by":"crossref","DOI":"10.1016\/j.jmb.2023.168039","article-title":"Sequence-targeted peptides divert functional bacterial amyloid towards destabilized aggregates and reduce biofilm formation","volume":"435","author":"S\u00f8nderby","year":"2023","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.mam.2025.101351_bib156","doi-asserted-by":"crossref","first-page":"10998","DOI":"10.1073\/pnas.0700848104","article-title":"Amyloidogenic potential of foie gras","volume":"104","author":"Solomon","year":"2007","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.mam.2025.101351_bib157","doi-asserted-by":"crossref","DOI":"10.1016\/j.jmb.2023.168039","article-title":"Sequence-targeted peptides divert functional bacterial amyloid towards destabilized aggregates and reduce biofilm formation","volume":"435","author":"S\u00f8nderby","year":"2023","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.mam.2025.101351_bib158","doi-asserted-by":"crossref","first-page":"1116","DOI":"10.1016\/j.jmb.2018.03.001","article-title":"Corneal dystrophy mutations drive pathogenesis by targeting TGFBIp stability and solubility in a latent amyloid-forming domain","volume":"430","author":"Stenvang","year":"2018","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.mam.2025.101351_bib159","doi-asserted-by":"crossref","first-page":"4209","DOI":"10.1113\/JP279919","article-title":"Intra-gastrointestinal amyloid-\u03b21\u201342 oligomers perturb enteric function and induce Alzheimer's disease pathology","volume":"598","author":"Sun","year":"2020","journal-title":"J. Physiol."},{"key":"10.1016\/j.mam.2025.101351_bib160","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1005711","article-title":"Staphylococcal bap proteins build amyloid scaffold biofilm matrices in response to environmental signals","volume":"12","author":"Taglialegna","year":"2016","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.mam.2025.101351_bib161","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1038\/s41522-020-0125-2","article-title":"The biofilm-associated surface protein Esp of Enterococcus faecalis forms amyloid-like fibers","volume":"6","author":"Taglialegna","year":"2020","journal-title":"npj Biofilms and Microbiomes"},{"key":"10.1016\/j.mam.2025.101351_bib162","doi-asserted-by":"crossref","first-page":"12XX","DOI":"10.1016\/j.str.2011.05.015","article-title":"Atomic resolution insights into curli fibre biogenesis","volume":"19","author":"Taylor","year":"2011","journal-title":"Structure"},{"key":"10.1016\/j.mam.2025.101351_bib163","doi-asserted-by":"crossref","DOI":"10.1016\/j.brainres.2024.149202","article-title":"Proteostasis disruption and senescence in Alzheimer's disease pathways to neurodegeneration","volume":"1845","author":"Thapa","year":"2024","journal-title":"Brain Res."},{"key":"10.1016\/j.mam.2025.101351_bib164","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1021\/ja5093634","article-title":"Structure of a functional amyloid protein subunit computed using sequence variation","volume":"137","author":"Tian","year":"2015","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.mam.2025.101351_bib165","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.mam.2025.101351_bib166","doi-asserted-by":"crossref","first-page":"1495","DOI":"10.1111\/j.1462-5822.2010.01485.x","article-title":"Toll-like receptors 1 and 2 cooperatively mediate immune responses to curli, a common amyloid from enterobacterial biofilms","volume":"12","author":"Tukel","year":"2010","journal-title":"Cell. Microbiol."},{"key":"10.1016\/j.mam.2025.101351_bib167","doi-asserted-by":"crossref","DOI":"10.3389\/fnins.2020.611285","article-title":"Looking beyond the core: the role of flanking regions in the aggregation of amyloidogenic peptides and proteins","volume":"14","author":"Ulamec","year":"2020","journal-title":"Front. Neurosci."},{"key":"10.1016\/j.mam.2025.101351_bib168","doi-asserted-by":"crossref","first-page":"1178","DOI":"10.1016\/j.str.2022.05.002","article-title":"Thermodynamic analysis of amyloid fibril structures reveals a common framework for stability in amyloid polymorphs","volume":"30","author":"van der Kant","year":"2022","journal-title":"Structure"},{"key":"10.1016\/j.mam.2025.101351_bib169","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1038\/s41586-022-05440-3","article-title":"Medin co-aggregates with vascular amyloid-\u03b2 in Alzheimer's disease","volume":"612","author":"Wagner","year":"2022","journal-title":"Nature"},{"key":"10.1016\/j.mam.2025.101351_bib170","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1038\/s41586-022-05440-3","article-title":"Medin co-aggregates with vascular amyloid-beta in Alzheimer's disease","volume":"612","author":"Wagner","year":"2022","journal-title":"Nature"},{"key":"10.1016\/j.mam.2025.101351_bib171","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1038\/s41586-022-05440-3","article-title":"Medin co-aggregates with vascular amyloid-beta in Alzheimer's disease","volume":"612","author":"Wagner","year":"2022","journal-title":"Nature"},{"key":"10.1016\/j.mam.2025.101351_bib172","doi-asserted-by":"crossref","first-page":"1189","DOI":"10.1093\/bioinformatics\/btp033","article-title":"Jalview Version 2--a multiple sequence alignment editor and analysis workbench","volume":"25","author":"Waterhouse","year":"2009","journal-title":"Bioinformatics"},{"key":"10.1016\/j.mam.2025.101351_bib173","doi-asserted-by":"crossref","first-page":"819","DOI":"10.3233\/JPD-202085","article-title":"Crosstalk between alpha-synuclein and other human and non-human amyloidogenic proteins: consequences for amyloid formation in Parkinson's disease","volume":"10","author":"Werner","year":"2020","journal-title":"J. Parkinsons Dis."},{"key":"10.1016\/j.mam.2025.101351_bib174","doi-asserted-by":"crossref","DOI":"10.1101\/cshperspect.a024323","article-title":"Noncerebral amyloidoses: aspects on seeding, cross-seeding, and transmission","volume":"8","author":"Westermark","year":"2018","journal-title":"Cold Spring Harbor Perspectives in Medicine"},{"key":"10.1016\/j.mam.2025.101351_bib175","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1007\/s00401-015-1477-1","article-title":"Physiological amyloid-beta clearance in the periphery and its therapeutic potential for Alzheimer's disease","volume":"130","author":"Xiang","year":"2015","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.mam.2025.101351_bib176","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1016\/j.jalz.2018.10.006","article-title":"Quantitative proteomics reveals distinct composition of amyloid plaques in Alzheimer's disease","volume":"15","author":"Xiong","year":"2019","journal-title":"Alzheimer's Dementia"},{"key":"10.1016\/j.mam.2025.101351_bib177","doi-asserted-by":"crossref","first-page":"6806","DOI":"10.1038\/s41467-023-42486-x","article-title":"Food amyloid fibrils are safe nutrition ingredients based on in-vitro and in-vivo assessment","volume":"14","author":"Xu","year":"2023","journal-title":"Nat. Commun."},{"key":"10.1016\/j.mam.2025.101351_bib178","doi-asserted-by":"crossref","first-page":"1099","DOI":"10.3389\/fmicb.2015.01099","article-title":"Functional bacterial amyloid increases Pseudomonas biofilm hydrophobicity and stiffness","volume":"6","author":"Zeng","year":"2015","journal-title":"Front. Microbiol."},{"key":"10.1016\/j.mam.2025.101351_bib179","doi-asserted-by":"crossref","first-page":"35092","DOI":"10.1074\/jbc.M112.383737","article-title":"Promiscuous cross-seeding between bacterial amyloids promotes interspecies biofilms","volume":"287","author":"Zhou","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mam.2025.101351_bib180","doi-asserted-by":"crossref","DOI":"10.1016\/j.semarthrit.2021.12.011","article-title":"Association between serum amyloid A and rheumatoid arthritis: a systematic review and meta-analysis","volume":"52","author":"Zhou","year":"2022","journal-title":"Semin. Arthritis Rheum."},{"key":"10.1016\/j.mam.2025.101351_bib181","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-019-56788-y","article-title":"Amyloidophilic molecule interactions on the surface of insulin fibrils: cooperative binding and fluorescence quenching","volume":"9","author":"Ziaunys","year":"2019","journal-title":"Sci. Rep."}],"container-title":["Molecular Aspects of Medicine"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0098299725000159?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0098299725000159?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,11,4]],"date-time":"2025-11-04T05:11:24Z","timestamp":1762233084000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0098299725000159"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,6]]},"references-count":181,"alternative-id":["S0098299725000159"],"URL":"https:\/\/doi.org\/10.1016\/j.mam.2025.101351","relation":{},"ISSN":["0098-2997"],"issn-type":[{"value":"0098-2997","type":"print"}],"subject":[],"published":{"date-parts":[[2025,6]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Interactions between pathological and functional amyloid: A match made in Heaven or Hell?","name":"articletitle","label":"Article Title"},{"value":"Molecular Aspects of Medicine","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.mam.2025.101351","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 The Authors. Published by Elsevier Ltd.","name":"copyright","label":"Copyright"}],"article-number":"101351"}}