{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T18:11:28Z","timestamp":1790878288638,"version":"4.1.0"},"reference-count":141,"publisher":"MDPI AG","issue":"6","license":[{"start":{"date-parts":[[2025,3,17]],"date-time":"2025-03-17T00:00:00Z","timestamp":1742169600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"National Research Foundation (NRF) of Kore","award":["NIBR202518101"],"award-info":[{"award-number":["NIBR202518101"]}]},{"name":"National Research Foundation (NRF) of Kore","award":["RS-2023-00241461"],"award-info":[{"award-number":["RS-2023-00241461"]}]},{"name":"Ministry of Education","award":["NIBR202518101"],"award-info":[{"award-number":["NIBR202518101"]}]},{"name":"Ministry of Education","award":["RS-2023-00241461"],"award-info":[{"award-number":["RS-2023-00241461"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Biofilm-associated amyloid proteins have emerged as significant contributors to the progression of neurodegenerative diseases, representing a complex intersection of microorganisms and human health. The cross-beta sheet structure characteristic of amyloids produced by gut-colonizing bacteria remains intact, crucial for the resilience of biofilms. These amyloids exacerbate neurodegenerative disorders such as Alzheimer\u2019s and Parkinson\u2019s by cross-seeding human amyloidogenic proteins like amyloid-beta and \u03b1-synuclein, accelerating their misfolding and aggregation. Despite molecular chaperones and heat shock proteins maintaining protein homeostasis, bacterial amyloids can overwhelm them, worsening neuronal damage. Genetic variations in chaperone genes further influence amyloidogenesis and neurodegeneration. Persistent bacterial infections and inflammation compromise the blood-brain barrier, allowing inflammatory molecules and amyloids to enter the brain, perpetuating the cycle of neurodegeneration. The gut-brain axis underscores the impact of dysbiosis and gut microbiota on brain function, potentially contributing to neurodegeneration. The enhancement of biofilm resilience and antibiotic resistance by functional amyloid fibrils complicates the treatment landscape. The interplay among chaperone systems, microbial amyloids, and neurodegenerative diseases underscores the urgent need for advanced treatment strategies targeting these pathways to attenuate disease progression. Understanding the processes that relate biofilm-associated amyloids to the onset of neurological disorders is critical for diagnosing and developing novel treatment strategies.<\/jats:p>","DOI":"10.3390\/ijms26062695","type":"journal-article","created":{"date-parts":[[2025,3,17]],"date-time":"2025-03-17T08:57:02Z","timestamp":1742201822000},"page":"2695","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":11,"title":["Biofilm-Associated Amyloid Proteins Linked with the Progression of Neurodegenerative Diseases"],"prefix":"10.3390","volume":"26","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-4049-102X","authenticated-orcid":false,"given":"Alka Ashok","family":"Singh","sequence":"first","affiliation":[{"name":"Department of Life Sciences, Yeungnam University, Gyeongsan 38541, Republic of Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4902-3188","authenticated-orcid":false,"given":"Fazlurrahman","family":"Khan","sequence":"additional","affiliation":[{"name":"Ocean and Fisheries Development International Cooperation Institute, Pukyong National University, Busan 48513, Republic of Korea"},{"name":"International Graduate Program of Fisheries Science, Pukyong National University, Busan 48513, Republic of Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Minseok","family":"Song","sequence":"additional","affiliation":[{"name":"Department of Life Sciences, Yeungnam University, Gyeongsan 38541, Republic of Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2025,3,17]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"2306135","DOI":"10.1002\/smll.202306135","article-title":"Nano\u2013Bio Interactions: Biofilm-Targeted Antibacterial Nanomaterials","volume":"20","author":"Li","year":"2024","journal-title":"Small"},{"key":"ref_2","doi-asserted-by":"crossref","unstructured":"Podobnik, M., Marchioretto, M., Zanetti, M., Bavdek, A., Kisovec, M., Cajnko, M.M., Lunelli, L., Dalla Serra, M., and Anderluh, G. (2015). Plasticity of listeriolysin O pores and its regulation by pH and unique histidine. Sci. Rep., 5, Corrected in Sci. Rep. 2015, 5, 15690.","DOI":"10.1038\/srep15690"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"126","DOI":"10.1111\/j.1742-4658.2011.08405.x","article-title":"pH dependence of listeriolysin O aggregation and pore-forming ability","volume":"279","author":"Bavdek","year":"2012","journal-title":"FEBS J."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1038\/nrd1008","article-title":"Understanding biofilm resistance to antibacterial agents","volume":"2","author":"Davies","year":"2003","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"1034","DOI":"10.1111\/j.1462-5822.2009.01323.x","article-title":"Evolving concepts in biofilm infections","volume":"11","author":"Stoodley","year":"2009","journal-title":"Cell. Microbiol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"563","DOI":"10.1038\/nrmicro.2016.94","article-title":"Biofilms: An emergent form of bacterial life","volume":"14","author":"Flemming","year":"2016","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"653","DOI":"10.1080\/1040841X.2018.1491527","article-title":"Beyond the expected: The structural and functional diversity of bacterial amyloids","volume":"44","author":"Romero","year":"2018","journal-title":"Crit. Rev. Microbiol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"788","DOI":"10.1016\/j.mehy.2011.07.038","article-title":"The in vivo functions of a histidine-rich protein Hpn in Helicobacter pylori: Linking gastric and Alzheimer\u2019s diseases together?","volume":"77","author":"Ge","year":"2011","journal-title":"Med. Hypotheses"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"2552","DOI":"10.1073\/pnas.0510770103","article-title":"The antioxidant protein alkylhydroperoxide reductase of Helicobacter pylori switches from a peroxide reductase to a molecular chaperone function","volume":"103","author":"Chuang","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1093\/jb\/mvp209","article-title":"Characterization of site-specific mutants of alkylhydroperoxide reductase with dual functionality from Helicobacter pylori","volume":"147","author":"Huang","year":"2010","journal-title":"J. Biochem."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1016\/S0065-2164(05)57003-5","article-title":"Biofilm development in bacteria","volume":"57","author":"Karatan","year":"2005","journal-title":"Adv. Appl. Microbiol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1042\/BCJ20210301","article-title":"The role of filamentous matrix molecules in shaping the architecture and emergent properties of bacterial biofilms","volume":"481","author":"Tarafder","year":"2024","journal-title":"Biochem. J."},{"key":"ref_13","doi-asserted-by":"crossref","unstructured":"Miller, A.L., Bessho, S., Grando, K., and T\u00fckel, \u00c7. (2021). Microbiome or infections: Amyloid-containing biofilms as a trigger for complex human diseases. Front. Immunol., 12.","DOI":"10.3389\/fimmu.2021.638867"},{"key":"ref_14","doi-asserted-by":"crossref","unstructured":"Elkins, M., Jain, N., and T\u00fckel, \u00c7. (2024). The menace within: Bacterial amyloids as a trigger for autoimmune and neurodegenerative diseases. Curr. Opin. Microbiol., 79.","DOI":"10.1016\/j.mib.2024.102473"},{"key":"ref_15","doi-asserted-by":"crossref","unstructured":"Kumari, S., and Das, S. (2024). Functional amyloid fibrils of biofilm-forming marine bacterium Pseudomonas aeruginosa PFL-P1 interact spontaneously with pyrene and augment the biodegradation. Int. J. Biol. Macromol., 266.","DOI":"10.1016\/j.ijbiomac.2024.131266"},{"key":"ref_16","doi-asserted-by":"crossref","unstructured":"Endres, K. (2020). Amyloidogenic peptides in human neuro-degenerative diseases and in microorganisms: A sorrow shared is a sorrow halved?. Molecules, 25.","DOI":"10.3390\/molecules25040925"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"eaba0466","DOI":"10.1126\/sciadv.aba0466","article-title":"Gut dysbiosis contributes to amyloid pathology, associated with C\/EBP\u03b2\/AEP signaling activation in Alzheimer\u2019s disease mouse model","volume":"6","author":"Chen","year":"2020","journal-title":"Sci. Adv."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"e20200895","DOI":"10.1084\/jem.20200895","article-title":"Gut microbiota\u2013driven brain A\u03b2 amyloidosis in mice requires microglia","volume":"219","author":"Dodiya","year":"2022","journal-title":"J. Exp. Med."},{"key":"ref_19","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":"Izco","year":"2024","journal-title":"Nat. Commun."},{"key":"ref_20","doi-asserted-by":"crossref","unstructured":"Jain, N. (2024). The molecular interplay between human and bacterial amyloids: Implications in neurodegenerative diseases. Biochim. Biophys. Acta (BBA)-Proteins Proteom., 1872.","DOI":"10.1016\/j.bbapap.2024.141018"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1016\/j.ijbiomac.2021.08.197","article-title":"The role of amyloids in Alzheimer\u2019s and Parkinson\u2019s diseases","volume":"190","author":"Salahuddin","year":"2021","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_22","doi-asserted-by":"crossref","unstructured":"Matilla-Cuenca, L., Taglialegna, A., Gil, C., Toledo-Arana, A., Lasa, I., and Valle, J. (2022). Bacterial biofilm functionalization through Bap amyloid engineering. NPJ Biofilms Microbiomes, 8.","DOI":"10.1038\/s41522-022-00324-w"},{"key":"ref_23","doi-asserted-by":"crossref","unstructured":"Subedi, S., Sasidharan, S., Nag, N., Saudagar, P., and Tripathi, T. (2022). Amyloid cross-seeding: Mechanism, implication, and inhibition. Molecules, 27.","DOI":"10.3390\/molecules27061776"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"7267","DOI":"10.1039\/C9TB01871A","article-title":"Fundamentals of cross-seeding of amyloid proteins: An introduction","volume":"7","author":"Ren","year":"2019","journal-title":"J. Mater. Chem. B"},{"key":"ref_25","doi-asserted-by":"crossref","unstructured":"Yang, W., Guan, F., Yang, L., Shou, G., Zhu, F., Xu, Y., Meng, Y., Li, M., and Dong, W. (2024). Highly sensitive blood-based biomarkers detection of beta-amyloid and phosphorylated-tau181 for Alzheimer\u2019s disease. Front. Neurol., 15.","DOI":"10.3389\/fneur.2024.1445479"},{"key":"ref_26","doi-asserted-by":"crossref","unstructured":"Friedland, R.P., and Chapman, M.R. (2017). The role of microbial amyloid in neurodegeneration. PLoS Pathog., 13.","DOI":"10.1371\/journal.ppat.1006654"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"8281","DOI":"10.1021\/bi200967c","article-title":"Fibrillation of the major curli subunit CsgA under a wide range of conditions implies a robust design of aggregation","volume":"50","author":"Dueholm","year":"2011","journal-title":"Biochemistry"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"102276","DOI":"10.1016\/j.arr.2024.102276","article-title":"Amyloid-induced neurodegeneration: A comprehensive review through aggregomics perception of proteins in health and pathology","volume":"96","author":"Bashir","year":"2024","journal-title":"Ageing Res. Rev."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1016\/j.bbagen.2015.09.005","article-title":"Multidimensional significance of crystallin protein\u2013protein interactions and their implications in various human diseases","volume":"1860","author":"Anbarasu","year":"2016","journal-title":"Biochim. Biophys. Acta (BBA)-Gen. Subj."},{"key":"ref_30","unstructured":"Rukmangadachar, L.A., and Bollu, P.C. (2023). Amyloid beta peptide. StatPearls [Internet], StatPearls Publishing."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"1462","DOI":"10.1021\/acschemneuro.8b00485","article-title":"Amyloid-\u03b2 peptide targeting peptidomimetics for prevention of neurotoxicity","volume":"10","author":"Honcharenko","year":"2019","journal-title":"ACS Chem. Neurosci."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"48","DOI":"10.5056\/jnm18087","article-title":"Brain-gut-microbiota axis in Alzheimer\u2019s disease","volume":"25","author":"Kowalski","year":"2019","journal-title":"J. Neurogastroenterol. Motil."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"768","DOI":"10.1038\/nrn2494","article-title":"Thirty years of Alzheimer\u2019s disease genetics: The implications of systematic meta-analyses","volume":"9","author":"Bertram","year":"2008","journal-title":"Nat. Rev. Neurosci."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"2605","DOI":"10.1007\/s00415-018-9100-8","article-title":"Amyloid-\u03b2 and Parkinson\u2019s disease","volume":"266","author":"Lim","year":"2019","journal-title":"J. Neurol."},{"key":"ref_35","doi-asserted-by":"crossref","unstructured":"Lee, D.-Y., Jeon, G.S., Shim, Y.-m., Seong, S.-Y., Lee, K.-W., and Sung, J.-J. (2015). Modulation of SOD1 subcellular localization by transfection with wild-or mutant-type SOD1 in primary neuron and astrocyte cultures from ALS mice. Exp. Neurobiol., 24.","DOI":"10.5607\/en.2015.24.3.226"},{"key":"ref_36","doi-asserted-by":"crossref","unstructured":"Higelin, J., Demestre, M., Putz, S., Delling, J.P., Jacob, C., Lutz, A.-K., Bausinger, J., Huber, A.-K., Klingenstein, M., and Barbi, G. (2016). FUS mislocalization and vulnerability to DNA damage in ALS patients derived hiPSCs and aging motoneurons. Front. Cell. Neurosci., 10.","DOI":"10.3389\/fncel.2016.00290"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1126\/science.1134108","article-title":"Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis","volume":"314","author":"Neumann","year":"2006","journal-title":"Science"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"636","DOI":"10.1001\/archneur.65.5.636","article-title":"Evidence of multisystem disorder in whole-brain map of pathological TDP-43 in amyotrophic lateral sclerosis","volume":"65","author":"Geser","year":"2008","journal-title":"Arch. Neurol."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1523\/JNEUROSCI.4988-09.2010","article-title":"Cytoplasmic mislocalization of TDP-43 is toxic to neurons and enhanced by a mutation associated with familial amyotrophic lateral sclerosis","volume":"30","author":"Barmada","year":"2010","journal-title":"J. Neurosci."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1056\/NEJMra0909142","article-title":"Alzheimer\u2019s disease","volume":"362","author":"Querfurth","year":"2010","journal-title":"N. Engl. J. Med."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"1179573520907397","DOI":"10.1177\/1179573520907397","article-title":"Current and future treatments in Alzheimer disease: An update","volume":"12","author":"Yiannopoulou","year":"2020","journal-title":"J. Cent. Nerv. Syst. Dis."},{"key":"ref_42","doi-asserted-by":"crossref","unstructured":"Kim, A.Y., Al Jerdi, S., MacDonald, R., and Triggle, C.R. (2024). Alzheimer\u2019s disease and its treatment\u2013yesterday, today, and tomorrow. Front. Pharmacol., 15.","DOI":"10.3389\/fphar.2024.1399121"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"87","DOI":"10.5114\/fn.2019.85929","article-title":"Risk factors for Alzheimer\u2019s disease","volume":"57","author":"Armstrong","year":"2019","journal-title":"Folia Neuropathol."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1007\/s12272-013-0036-3","article-title":"A review on cholinesterase inhibitors for Alzheimer\u2019s disease","volume":"36","author":"Anand","year":"2013","journal-title":"Arch. Pharmacal Res."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"1966","DOI":"10.1002\/alz.12362","article-title":"Population estimate of people with clinical Alzheimer\u2019s disease and mild cognitive impairment in the United States (2020\u20132060)","volume":"17","author":"Rajan","year":"2021","journal-title":"Alzheimer\u2019s Dement."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1016\/j.jalz.2018.02.018","article-title":"NIA-AA research framework: Toward a biological definition of Alzheimer\u2019s disease","volume":"14","author":"Bennett","year":"2018","journal-title":"Alzheimer\u2019s Dement."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"734","DOI":"10.1016\/S1474-4422(07)70178-3","article-title":"Research criteria for the diagnosis of Alzheimer\u2019s disease: Revising the NINCDS\u2013ADRDA criteria","volume":"6","author":"Dubois","year":"2007","journal-title":"Lancet Neurol."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1038\/s41531-024-00700-7","article-title":"Social isolation and the risk of Parkinson disease in the UK biobank study","volume":"10","author":"Geng","year":"2024","journal-title":"NPJ Park. Dis."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1016\/S0140-6736(23)01478-2","article-title":"The pathogenesis of Parkinson\u2019s disease","volume":"403","author":"Morris","year":"2024","journal-title":"Lancet"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"107186","DOI":"10.1016\/j.parkreldis.2024.107186","article-title":"Clinical progression of Parkinson\u2019s disease in the early 21st century: Insights from the accelerating medicine partnership (AMP-PD) data","volume":"130","author":"Lewis","year":"2025","journal-title":"Park. Relat. Disord."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"106000","DOI":"10.1016\/j.parkreldis.2024.106000","article-title":"Update: Descriptive epidemiology of Parkinson disease","volume":"120","author":"Grotewold","year":"2024","journal-title":"Park. Relat. Disord."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1016\/S0140-6736(23)01419-8","article-title":"The epidemiology of Parkinson\u2019s disease","volume":"403","author":"Darweesh","year":"2024","journal-title":"Lancet"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1016\/j.expneurol.2017.10.003","article-title":"Therapeutic approaches to target alpha-synuclein pathology","volume":"298","author":"Brundin","year":"2017","journal-title":"Exp. Neurol."},{"key":"ref_54","doi-asserted-by":"crossref","unstructured":"Dong, W., Qiu, C., Lu, Y., Luo, B., Jiang, X., Chang, L., Yan, J., Sun, J., Liu, W., and Zhang, L. (2023). Effect of deep brain stimulation compared with drug therapy alone on the progression of Parkinson\u2019s disease. Front. Neurosci., 17.","DOI":"10.3389\/fnins.2023.1330752"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"3658","DOI":"10.1038\/s41467-024-47980-4","article-title":"Protein mimetic 2D FAST rescues alpha synuclein aggregation mediated early and post disease Parkinson\u2019s phenotypes","volume":"15","author":"Stillman","year":"2024","journal-title":"Nat. Commun."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"923","DOI":"10.1016\/j.csbj.2023.01.008","article-title":"The paradigm of amyloid precursor protein in amyotrophic lateral sclerosis: The potential role of the (682)YENPTY(687) motif","volume":"21","author":"Matrone","year":"2023","journal-title":"Comput. Struct. Biotechnol. J."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"116496","DOI":"10.1016\/j.ejmech.2024.116496","article-title":"Current therapy in amyotrophic lateral sclerosis (ALS): A review on past and future therapeutic strategies","volume":"272","author":"Wei","year":"2024","journal-title":"Eur. J. Med. Chem."},{"key":"ref_58","doi-asserted-by":"crossref","unstructured":"Wang, H., Guan, L., and Deng, M. (2023). Recent progress of the genetics of amyotrophic lateral sclerosis and challenges of gene therapy. Front. Neurosci., 17.","DOI":"10.3389\/fnins.2023.1170996"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1056\/NEJMra1603471","article-title":"Amyotrophic Lateral Sclerosis","volume":"377","author":"Brown","year":"2017","journal-title":"N. Engl. J. Med."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1093\/bmb\/ldw026","article-title":"Pathogenesis of amyotrophic lateral sclerosis","volume":"119","author":"Morgan","year":"2016","journal-title":"Br. Med. Bull."},{"key":"ref_61","first-page":"1323","article-title":"Amyotrophic Lateral Sclerosis and Other Motor Neuron Diseases","volume":"26","author":"Quinn","year":"2020","journal-title":"Continuum"},{"key":"ref_62","doi-asserted-by":"crossref","unstructured":"Tzeplaeff, L., Wilfling, S., Requardt, M.V., and Herdick, M. (2023). Current State and Future Directions in the Therapy of ALS. Cells, 12.","DOI":"10.3390\/cells12111523"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"e613","DOI":"10.1212\/WNL.0000000000207474","article-title":"Global Prevalence and Incidence of Amyotrophic Lateral Sclerosis: A Systematic Review","volume":"101","author":"Wolfson","year":"2023","journal-title":"Neurology"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"964","DOI":"10.14336\/AD.2022.1127","article-title":"Gut Microbiota is an Impact Factor based on the Brain-Gut Axis to Alzheimer\u2019s Disease: A Systematic Review","volume":"14","author":"Zou","year":"2023","journal-title":"Aging Dis."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1017\/S0029665120008022","article-title":"Impact of protein on the composition and metabolism of the human gut microbiota and health","volume":"80","author":"Duncan","year":"2021","journal-title":"Proc. Nutr. Soc."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/j.phrs.2012.10.020","article-title":"The influence of diet on the gut microbiota","volume":"69","author":"Scott","year":"2013","journal-title":"Pharmacol. Res."},{"key":"ref_67","doi-asserted-by":"crossref","unstructured":"Chung, E.J., Luo, C.H., Thio, C.L., and Chang, Y.J. (2022). Immunomodulatory Role of Staphylococcus aureus in Atopic Dermatitis. Pathogens, 11.","DOI":"10.3390\/pathogens11040422"},{"key":"ref_68","doi-asserted-by":"crossref","unstructured":"Peng, B., Xu, S., Liang, Y., Dong, X., and Sun, Y. (2023). Effect of Bacterial Amyloid Protein Phenol-Soluble Modulin Alpha 3 on the Aggregation of Amyloid Beta Protein Associated with Alzheimer\u2019s Disease. Biomimetics, 8.","DOI":"10.3390\/biomimetics8060459"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"e2106504118","DOI":"10.1073\/pnas.2106504118","article-title":"Genome-wide screen identifies curli amyloid fibril as a bacterial component promoting host neurodegeneration","volume":"118","author":"Wang","year":"2021","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_70","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":"ref_71","doi-asserted-by":"crossref","first-page":"2230","DOI":"10.1073\/pnas.0910560107","article-title":"Amyloid fibers provide structural integrity to Bacillus subtilis biofilms","volume":"107","author":"Romero","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"eadj1092","DOI":"10.1126\/sciadv.adj1092","article-title":"The yeast prion protein Sup35 initiates \u03b1-synuclein pathology in mouse models of Parkinson\u2019s disease","volume":"9","author":"Meng","year":"2023","journal-title":"Sci. Adv."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"4384","DOI":"10.1038\/ncomms5384","article-title":"Amyloid-associated activity contributes to the severity and toxicity of a prion phenotype","volume":"5","author":"Pezza","year":"2014","journal-title":"Nat. Commun."},{"key":"ref_74","doi-asserted-by":"crossref","unstructured":"Taglialegna, A., Navarro, S., Ventura, S., Garnett, J.A., Matthews, S., Penades, J.R., Lasa, I., and Valle, J. (2016). Staphylococcal Bap proteins build amyloid scaffold biofilm matrices in response to environmental signals. PLoS Pathog., 12.","DOI":"10.1371\/journal.ppat.1005711"},{"key":"ref_75","doi-asserted-by":"crossref","unstructured":"Spiegelman, L., Bahn-Suh, A., Monta\u00f1o, E.T., Zhang, L., Hura, G.L., Patras, K.A., Kumar, A., Tezcan, F.A., Nizet, V., and Tsutakawa, S.E. (2022). Strengthening of enterococcal biofilms by Esp. PLoS Pathog., 18.","DOI":"10.1101\/2022.06.09.495547"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"6213","DOI":"10.1128\/JB.187.17.6213-6222.2005","article-title":"The N-terminal domain of enterococcal surface protein, Esp, is sufficient for Esp-mediated biofilm enhancement in Enterococcus faecalis","volume":"187","author":"Tendolkar","year":"2005","journal-title":"J. Bacteriol."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"5721","DOI":"10.1128\/JCM.43.11.5721-5732.2005","article-title":"Defining the normal bacterial flora of the oral cavity","volume":"43","author":"Aas","year":"2005","journal-title":"J. Clin. Microbiol."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1111\/j.1600-051X.1998.tb02419.x","article-title":"Microbial complexes in subgingival plaque","volume":"25","author":"Socransky","year":"1998","journal-title":"J. Clin. Periodontol."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"479","DOI":"10.3233\/JAD-190298","article-title":"Porphyromonas gingivalis Infection Induces Amyloid-\u03b2 Accumulation in Monocytes\/Macrophages","volume":"72","author":"Nie","year":"2019","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"501","DOI":"10.3233\/ADR-200250","article-title":"Porphyromonas gingivalis is a strong risk factor for Alzheimer\u2019s disease","volume":"4","author":"Kanagasingam","year":"2020","journal-title":"J. Alzheimer\u2019s Dis. Rep."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"29","DOI":"10.3233\/JAD-180319","article-title":"Association between Alzheimer\u2019s disease and oral and gut microbiota: Are pore forming proteins the missing link?","volume":"65","author":"Aguayo","year":"2018","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"ref_82","unstructured":"HB, A., Cusack, C., and Joshi, S. (2019). The Impact of Biofilms in Alzheimer\u2019s disease compared to Other Diseases in Which They Play a Role. Int. J. Neurobiol., 1."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"669","DOI":"10.1038\/nn.2853","article-title":"Amyloid by default","volume":"14","author":"Walker","year":"2011","journal-title":"Nat. Neurosci."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1016\/j.nbd.2015.06.003","article-title":"Intrastriatal injection of pre-formed mouse \u03b1-synuclein fibrils into rats triggers \u03b1-synuclein pathology and bilateral nigrostriatal degeneration","volume":"82","author":"Paumier","year":"2015","journal-title":"Neurobiol. Dis."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"e2414","DOI":"10.1212\/WNL.0000000000011883","article-title":"Association of APOE genotype with heterogeneity of cognitive decline rate in Alzheimer disease","volume":"96","author":"Qian","year":"2021","journal-title":"Neurology"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"919","DOI":"10.1038\/s43587-021-00123-6","article-title":"Effect of APOE alleles on the glial transcriptome in normal aging and Alzheimer\u2019s disease","volume":"1","author":"Li","year":"2021","journal-title":"Nat. Aging"},{"key":"ref_87","first-page":"819","article-title":"Crosstalk between alpha-synuclein and other human and non-human amyloidogenic proteins: Consequences for amyloid formation in Parkinson\u2019s disease","volume":"10","author":"Werner","year":"2020","journal-title":"J. Park. Dis."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/j.expneurol.2009.07.025","article-title":"Alpha-synuclein immunopositive aggregates in the myenteric plexus of the aging Fischer 344 rat","volume":"220","author":"Phillips","year":"2009","journal-title":"Exp. Neurol."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"5864","DOI":"10.1128\/IAI.68.10.5864-5868.2000","article-title":"Genetic control of susceptibility to Porphyromonas gingivalis-induced alveolar bone loss in mice","volume":"68","author":"Baker","year":"2000","journal-title":"Infect. Immun."},{"key":"ref_90","doi-asserted-by":"crossref","unstructured":"Chen, S.G., Stribinskis, V., Rane, M.J., Demuth, D.R., Gozal, E., Roberts, A.M., Jagadapillai, R., Liu, R., Choe, K., and Shivakumar, B. (2016). Exposure to the functional bacterial amyloid protein curli enhances alpha-synuclein aggregation in aged Fischer 344 rats and Caenorhabditis elegans. Sci. Rep., 6.","DOI":"10.1038\/srep34477"},{"key":"ref_91","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":"ref_92","doi-asserted-by":"crossref","first-page":"557","DOI":"10.1146\/annurev-biochem-090908-120656","article-title":"Amyloid structure: Conformational diversity and consequences","volume":"80","author":"Toyama","year":"2011","journal-title":"Annu. Rev. Biochem."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1016\/j.tim.2011.11.005","article-title":"Diversity, biogenesis and function of microbial amyloids","volume":"20","author":"Blanco","year":"2012","journal-title":"Trends Microbiol."},{"key":"ref_94","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":"ref_95","doi-asserted-by":"crossref","unstructured":"S\u00f8nderby, T.V., Najarzadeh, Z., and Otzen, D.E. (2022). Functional bacterial amyloids: Understanding fibrillation, regulating biofilm fibril formation and organizing surface assemblies. Molecules, 27.","DOI":"10.3390\/molecules27134080"},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"eabn6831","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":"ref_97","doi-asserted-by":"crossref","unstructured":"S\u00f8nderby, T.V., Rasmussen, H.\u00d8., Frank, S.A., Pedersen, J.S., and Otzen, D.E. (2022). Folding steps in the fibrillation of functional amyloid: Denaturant sensitivity reveals common features in nucleation and elongation. J. Mol. Biol., 434.","DOI":"10.1016\/j.jmb.2021.167337"},{"key":"ref_98","doi-asserted-by":"crossref","unstructured":"Daniels, M.J., Nourse Jr, J.B., Kim, H., Sainati, V., Schiavina, M., Murrali, M.G., Pan, B., Ferrie, J.J., Haney, C.M., and Moons, R. (2019). Cyclized NDGA modifies dynamic \u03b1-synuclein monomers preventing aggregation and toxicity. Sci. Rep., 9.","DOI":"10.1038\/s41598-019-39480-z"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1186\/s13024-021-00497-6","article-title":"Small molecule inhibitors of \u03b1-synuclein oligomers identified by targeting early dopamine-mediated motor impairment in C. elegans","volume":"16","author":"Chen","year":"2021","journal-title":"Mol. Neurodegener."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"e53111","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":"ref_101","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1016\/j.bbadis.2004.09.008","article-title":"Tau pathology in Alzheimer disease and other tauopathies","volume":"1739","author":"Iqbal","year":"2005","journal-title":"Biochim. Biophys. Acta (BBA)-Mol. Basis Dis."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"2098","DOI":"10.1073\/pnas.88.6.2098","article-title":"Ultrastructural localization of beta-amyloid, tau, and ubiquitin epitopes in extracellular neurofibrillary tangles","volume":"88","author":"Tabaton","year":"1991","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"756","DOI":"10.1016\/j.neuron.2014.05.004","article-title":"The intersection of amyloid beta and tau at synapses in Alzheimer\u2019s disease","volume":"82","author":"Hyman","year":"2014","journal-title":"Neuron"},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"949","DOI":"10.1007\/s00702-010-0433-4","article-title":"The role of microglia in amyloid clearance from the AD brain","volume":"117","author":"Lee","year":"2010","journal-title":"J. Neural Transm."},{"key":"ref_105","doi-asserted-by":"crossref","unstructured":"Vojtechova, I., Machacek, T., Kristofikova, Z., Stuchlik, A., and Petrasek, T. (2022). Infectious origin of Alzheimer\u2019s disease: Amyloid beta as a component of brain antimicrobial immunity. PLoS Pathog., 18.","DOI":"10.1371\/journal.ppat.1010929"},{"key":"ref_106","doi-asserted-by":"crossref","unstructured":"Wei, W., Wang, S., Xu, C., Zhou, X., Lian, X., He, L., and Li, K. (2022). Gut microbiota, pathogenic proteins and neurodegenerative diseases. Front. Microbiol., 13.","DOI":"10.3389\/fmicb.2022.959856"},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"1652","DOI":"10.1038\/s12276-020-00513-7","article-title":"The role of TDP-43 propagation in neurodegenerative diseases: Integrating insights from clinical and experimental studies","volume":"52","author":"Jo","year":"2020","journal-title":"Exp. Mol. Med."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1007\/s00401-013-1211-9","article-title":"Staging TDP-43 pathology in Alzheimer\u2019s disease","volume":"127","author":"Josephs","year":"2014","journal-title":"Acta Neuropathol."},{"key":"ref_109","first-page":"435","article-title":"TDP-43 immunoreactivity in hippocampal sclerosis and Alzheimer\u2019s disease","volume":"61","author":"Lin","year":"2007","journal-title":"Ann. Neurol. Off. J. Am. Neurol. Assoc. Child Neurol. Soc."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1097\/NEN.0b013e31817713b5","article-title":"Concomitant TAR-DNA-binding protein 43 pathology is present in Alzheimer disease and corticobasal degeneration but not in other tauopathies","volume":"67","author":"Uryu","year":"2008","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"ref_111","doi-asserted-by":"crossref","unstructured":"Wang, J., Farr, G.W., Hall, D.H., Li, F., Furtak, K., Dreier, L., and Horwich, A.L. (2009). An ALS-linked mutant SOD1 produces a locomotor defect associated with aggregation and synaptic dysfunction when expressed in neurons of Caenorhabditis elegans. PLoS Genet., 5.","DOI":"10.1371\/journal.pgen.1000350"},{"key":"ref_112","doi-asserted-by":"crossref","unstructured":"Baba, T., Ara, T., Hasegawa, M., Takai, Y., Okumura, Y., Baba, M., Datsenko, K.A., Tomita, M., Wanner, B.L., and Mori, H. (2006). Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: The Keio collection. Mol. Syst. Biol., 2.","DOI":"10.1038\/msb4100050"},{"key":"ref_113","doi-asserted-by":"crossref","unstructured":"Tran, V.T.A., Zhu, X., Jamsranjav, A., Lee, L.P., and Cho, H. (2025). Escherichia coli K1-colibactin meningitis induces microglial NLRP3\/IL-18 exacerbating H3K4me3-synucleinopathy in the human inflammatory gut-brain axis. Commun. Biol., 8.","DOI":"10.1038\/s42003-025-07787-5"},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"6696","DOI":"10.1074\/jbc.RA118.005889","article-title":"Detection of TAR DNA-binding protein 43 (TDP-43) oligomers as initial intermediate species during aggregate formation","volume":"294","author":"French","year":"2019","journal-title":"J. Biol. Chem."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"5262","DOI":"10.1002\/anie.201711854","article-title":"Cytotoxic oligomers and fibrils trapped in a gel-like state of \u03b1-synuclein assemblies","volume":"57","author":"Kumar","year":"2018","journal-title":"Angew. Chem. Int. Ed."},{"key":"ref_116","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":"ref_117","doi-asserted-by":"crossref","unstructured":"Dueholm, M.S., Otzen, D., and Nielsen, P.H. (2013). Evolutionary insight into the functional amyloids of the pseudomonads. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0076630"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1146\/annurev.micro.60.080805.142106","article-title":"Curli biogenesis and function","volume":"60","author":"Barnhart","year":"2006","journal-title":"Annu. Rev. Microbiol."},{"key":"ref_119","doi-asserted-by":"crossref","unstructured":"Zeng, G., Vad, B.S., Dueholm, M.S., Christiansen, G., Nilsson, M., Tolker-Nielsen, T., Nielsen, P.H., Meyer, R.L., and Otzen, D.E. (2015). Functional bacterial amyloid increases Pseudomonas biofilm hydrophobicity and stiffness. Front. Microbiol., 6.","DOI":"10.3389\/fmicb.2015.01099"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"9156","DOI":"10.1096\/fj.202000051RRR","article-title":"Virulent Pseudomonas aeruginosa infection converts antimicrobial amyloids into cytotoxic prions","volume":"34","author":"Voth","year":"2020","journal-title":"FASEB J."},{"key":"ref_121","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":"ref_122","doi-asserted-by":"crossref","first-page":"2232","DOI":"10.1016\/j.jmb.2020.01.044","article-title":"Predicted Loop Regions Promote Aggregation: A Study of Amyloidogenic Domains in the Functional Amyloid FapC","volume":"432","author":"Nagaraj","year":"2020","journal-title":"J. Mol. Biol."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1038\/s41467-017-00361-6","article-title":"A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis","volume":"8","author":"Rouse","year":"2017","journal-title":"Nat. Commun."},{"key":"ref_124","doi-asserted-by":"crossref","unstructured":"Matilla-Cuenca, L., Toledo-Arana, A., and Valle, J. (2021). Anti-Biofilm Molecules Targeting Functional Amyloids. Antibiotics, 10.","DOI":"10.3390\/antibiotics10070795"},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"1229","DOI":"10.1111\/j.1365-2958.2005.05020.x","article-title":"A major protein component of the Bacillus subtilis biofilm matrix","volume":"59","author":"Branda","year":"2006","journal-title":"Mol. Microbiol."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"12146","DOI":"10.1096\/fj.201900831R","article-title":"Molecular architecture of bacterial amyloids in Bacillus biofilms","volume":"33","author":"Hierrezuelo","year":"2019","journal-title":"FASEB J."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"23286","DOI":"10.1039\/D0CP03265D","article-title":"Colloidal-like aggregation of a functional amyloid protein","volume":"22","author":"Azulay","year":"2020","journal-title":"Phys. Chem. Chem. Phys."},{"key":"ref_128","doi-asserted-by":"crossref","unstructured":"Ghrayeb, M., Hayet, S., Lester-Zer, N., Levi-Kalisman, Y., and Chai, L. (2021). Fibrilar Polymorphism of the Bacterial Extracellular Matrix Protein TasA. Microorganisms, 9.","DOI":"10.3390\/microorganisms9030529"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"7082","DOI":"10.1038\/s41467-022-34700-z","article-title":"Donor-strand exchange drives assembly of the TasA scaffold in Bacillus subtilis biofilms","volume":"13","author":"Ghrayeb","year":"2022","journal-title":"Nat. Commun."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"788","DOI":"10.1016\/j.resmic.2013.06.004","article-title":"Bacterial determinants of the social behavior of Bacillus subtilis","volume":"164","author":"Romero","year":"2013","journal-title":"Res. Microbiol."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"e00561-17","DOI":"10.1128\/AEM.00561-17","article-title":"Genome-Wide Investigation of Biofilm Formation in Bacillus cereus","volume":"83","author":"Yan","year":"2017","journal-title":"Appl. Env. Microbiol."},{"key":"ref_132","doi-asserted-by":"crossref","unstructured":"Caro-Astorga, J., P\u00e9rez-Garc\u00eda, A., de Vicente, A., and Romero, D. (2014). A genomic region involved in the formation of adhesin fibers in Bacillus cereus biofilms. Front. Microbiol., 5.","DOI":"10.3389\/fmicb.2014.00745"},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"1664","DOI":"10.1128\/JB.181.5.1664-1672.1999","article-title":"Secretion, localization, and antibacterial activity of TasA, a Bacillus subtilis spore-associated protein","volume":"181","author":"Driks","year":"1999","journal-title":"J. Bacteriol."},{"key":"ref_134","doi-asserted-by":"crossref","unstructured":"Price, M.N., Dehal, P.S., and Arkin, A.P. (2010). FastTree 2--approximately maximum-likelihood trees for large alignments. PLoS ONE, 5.","DOI":"10.1371\/journal.pone.0009490"},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"1307","DOI":"10.1016\/j.str.2011.05.015","article-title":"Atomic resolution insights into curli fiber biogenesis","volume":"19","author":"Taylor","year":"2011","journal-title":"Structure"},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"140","DOI":"10.3934\/microbiol.2018.1.140","article-title":"Bacterial autoaggregation","volume":"4","author":"Trunk","year":"2018","journal-title":"AIMS Microbiol."},{"key":"ref_137","doi-asserted-by":"crossref","unstructured":"Giaouris, E., Heir, E., Desvaux, M., H\u00e9braud, M., M\u00f8retr\u00f8, T., Langsrud, S., Doulgeraki, A., Nychas, G.J., Ka\u010d\u00e1niov\u00e1, M., and Czaczyk, K. (2015). Intra- and inter-species interactions within biofilms of important foodborne bacterial pathogens. Front. Microbiol., 6.","DOI":"10.3389\/fmicb.2015.00841"},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"1551","DOI":"10.1016\/j.bbamcr.2013.09.010","article-title":"Curli biogenesis: Order out of disorder","volume":"1843","author":"Evans","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_139","doi-asserted-by":"crossref","unstructured":"Bu, F., Dee, D.R., and Liu, B. (2024). Structural insight into Escherichia coli CsgA amyloid fibril assembly. mBio, 15.","DOI":"10.1128\/mbio.00419-24"},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"451","DOI":"10.2119\/2007-00100.Irvine","article-title":"Protein aggregation in the brain: The molecular basis for Alzheimer\u2019s and Parkinson\u2019s diseases","volume":"14","author":"Irvine","year":"2008","journal-title":"Mol. Med."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"3237","DOI":"10.1073\/pnas.1718102115","article-title":"Structural changes of TasA in biofilm formation of Bacillus subtilis","volume":"115","author":"Diehl","year":"2018","journal-title":"Proc. Natl. Acad. Sci. USA"}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/26\/6\/2695\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,9]],"date-time":"2025-10-09T16:55:02Z","timestamp":1760028902000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/26\/6\/2695"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,3,17]]},"references-count":141,"journal-issue":{"issue":"6","published-online":{"date-parts":[[2025,3]]}},"alternative-id":["ijms26062695"],"URL":"https:\/\/doi.org\/10.3390\/ijms26062695","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,3,17]]}}}