{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T22:32:04Z","timestamp":1791325924642,"version":"4.3.1"},"reference-count":64,"publisher":"Elsevier","license":[{"start":{"date-parts":[[2025,1,1]],"date-time":"2025-01-01T00:00:00Z","timestamp":1735689600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,1,1]],"date-time":"2025-01-01T00:00:00Z","timestamp":1735689600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,1,1]],"date-time":"2025-01-01T00:00:00Z","timestamp":1735689600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2025,1,1]],"date-time":"2025-01-01T00:00:00Z","timestamp":1735689600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2025,1,1]],"date-time":"2025-01-01T00:00:00Z","timestamp":1735689600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2025,1,1]],"date-time":"2025-01-01T00:00:00Z","timestamp":1735689600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2025,1,1]],"date-time":"2025-01-01T00:00:00Z","timestamp":1735689600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2025]]},"DOI":"10.1016\/bs.apcsb.2024.11.002","type":"book-chapter","created":{"date-parts":[[2025,4,3]],"date-time":"2025-04-03T00:07:51Z","timestamp":1743638871000},"source":"Crossref","is-referenced-by-count":2,"title":["Alpha-synuclein aggregation in Parkinson\u2019s disease"],"prefix":"10.1016","author":[{"given":"Igor Jos\u00e9 Siqueira da","family":"Silva","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Manuele Figueiredo da","family":"Silva","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thiago Santos de Assis","family":"Dutra","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sheila Oliveira de","family":"Souza","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jo\u00e3o Xavier de","family":"Ara\u00fajo-J\u00fanior","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ana Catarina Rezende","family":"Leite","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"\u00c9rica Erlanny da Silva","family":"Rodrigues","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Edeildo Ferreira da","family":"Silva-J\u00fanior","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/bs.apcsb.2024.11.002_bib1","doi-asserted-by":"crossref","first-page":"2878","DOI":"10.1016\/j.ijbiomac.2022.10.066","article-title":"Zinc ions prevent \u03b1-synuclein aggregation by enhancing chaperone function of human serum albumin","volume":"222","author":"Al-Harthi","year":"2022","journal-title":"International Journal of Biological Macromolecules"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib2","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2023.105383","article-title":"The toxicities of A30P and A53T \u03b1-synuclein fibrils can be uniquely altered by the length and saturation of fatty acids in phosphatidylserine","volume":"299","author":"Ali","year":"2023","journal-title":"The Journal of Biological Chemistry"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib3","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2021.113911","article-title":"Discovery of novel 6-hydroxybenzothiazole urea derivatives as dual Dyrk1A\/\u03b1-synuclein aggregation inhibitors with neuroprotective effects","volume":"227","author":"AlNajjar","year":"2022","journal-title":"European Journal of Medicinal Chemistry"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib4","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2024.116266","article-title":"Novel 6-hydroxybenzothiazol-2-carboxamides as potent and selective monoamine oxidase B inhibitors endowed with neuroprotective activity","volume":"269","author":"Al-Saad","year":"2024","journal-title":"European Journal of Medicinal Chemistry"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib5","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1016\/j.ijbiomac.2020.01.269","article-title":"Interaction with zinc oxide nanoparticle kinetically traps \u03b1-synuclein fibrillation into off-pathway non-toxic intermediates","volume":"150","author":"Asthana","year":"2020","journal-title":"International Journal of Biological Macromolecules"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib6","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1016\/j.brainres.2012.04.014","article-title":"From \u03b1-synuclein to synaptic dysfunctions: New insights into the pathophysiology of Parkinson\u2019s disease","volume":"1476","author":"Bellucci","year":"2012","journal-title":"Brain Research"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib7","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":"The Journal of Biological Chemistry"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib8","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2021.113887","article-title":"Discovery of styrylaniline derivatives as novel alpha-synuclein aggregates ligands","volume":"226","author":"Bian","year":"2021","journal-title":"European Journal of Medicinal Chemistry"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib9","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2022.102260","article-title":"A small molecule toll-like receptor antagonist rescues \u03b1-synuclein fibril pathology","volume":"298","author":"Chedid","year":"2022","journal-title":"The Journal of Biological Chemistry"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib10","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2023.115965","article-title":"Brazilin-7-acetate, a novel potential drug of Parkinson\u2019s disease, hinders the formation of \u03b1-synuclein fibril, mitigates cytotoxicity, and decreases oxidative stress","volume":"264","author":"Cui","year":"2024","journal-title":"European Journal of Medicinal Chemistry"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib11","doi-asserted-by":"crossref","first-page":"1173","DOI":"10.1016\/S0002-9440(10)65220-0","article-title":"Non-A\u03b2 component of Alzheimer\u2019s disease amyloid (NAC) revisited","volume":"155","author":"Culvenor","year":"1999","journal-title":"The American Journal of Pathology"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib12","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2021.101552","article-title":"Phosphorylation of the aggregate-forming protein alpha-synuclein on serine-129 inhibits its DNA-bending properties","volume":"298","author":"Dent","year":"2022","journal-title":"The Journal of Biological Chemistry"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib13","doi-asserted-by":"crossref","first-page":"29","DOI":"10.4103\/1735-1995.181989","article-title":"Alpha-synuclein structure, functions, and interactions","volume":"21","author":"Emamzadeh","year":"2016","journal-title":"Journal of Research in Medical Sciences"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib14","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijbiomac.2024.130632","article-title":"Length and saturation of choline plasmalogens alter the aggregation rate of \u03b1-synuclein but not the toxicity of amyloid fibrils","volume":"264","author":"Farid","year":"2024","journal-title":"International Journal of Biological Macromolecules"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib15","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2021.100663","article-title":"An \u03b1-synuclein decoy peptide prevents cytotoxic \u03b1-synuclein aggregation caused by fatty acid binding protein 3","volume":"296","author":"Fukui","year":"2021","journal-title":"The Journal of Biological Chemistry"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib16","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2021.101191","article-title":"The AKT modulator A-443654 reduces \u03b1-synuclein expression and normalizes ER stress and autophagy","volume":"297","author":"Gandelman","year":"2021","journal-title":"The Journal of Biological Chemistry"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib17","doi-asserted-by":"crossref","DOI":"10.3389\/fphar.2020.00356","article-title":"Modeling Parkinson\u2019s disease with the alpha-synuclein protein","volume":"11","author":"G\u00f3mez-Benito","year":"2020","journal-title":"Frontiers in Pharmacology"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib18","doi-asserted-by":"crossref","first-page":"17497","DOI":"10.1074\/jbc.RA120.013428","article-title":"Fibrillar \u03b1-synuclein toxicity depends on functional lysosomes","volume":"295","author":"Guiney","year":"2020","journal-title":"The Journal of Biological Chemistry"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib19","doi-asserted-by":"crossref","first-page":"590","DOI":"10.1016\/j.ijbiomac.2022.12.105","article-title":"Inhibitory effects of fluorinated benzenesulfonamides on insulin fibrillation","volume":"227","author":"Hadi Ali Janvand","year":"2023","journal-title":"International Journal of Biological Macromolecules"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib20","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1016\/j.ijbiomac.2022.12.134","article-title":"The impact of \u03b1-synuclein aggregates on blood-brain barrier integrity in the presence of neurovascular unit cells","volume":"229","author":"Hourfar","year":"2023","journal-title":"International Journal of Biological Macromolecules"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib21","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2023.115475","article-title":"Small-molecule LRRK2 inhibitors for PD therapy: Current achievements and future perspectives","volume":"256","author":"Hu","year":"2023","journal-title":"European Journal of Medicinal Chemistry"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib22","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2023.115475","article-title":"Small-molecule LRRK2 inhibitors for PD therapy: Current achievements and future perspectives","volume":"256","author":"Hu","year":"2023","journal-title":"European Journal of Medicinal Chemistry"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib23","doi-asserted-by":"crossref","first-page":"2035","DOI":"10.1523\/JNEUROSCI.5634-10.2011","article-title":"\u03b1-Synuclein negatively regulates protein kinase C\u03b4 expression to suppress apoptosis in dopaminergic neurons by reducing p300 histone acetyltransferase activity","volume":"31","author":"Jin","year":"2011","journal-title":"The Journal of Neuroscience"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib24","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/j.ijbiomac.2022.11.031","article-title":"Protein misfolding and related human diseases: A comprehensive review of toxicity, proteins involved, and current therapeutic strategies","volume":"223","author":"Khan","year":"2022","journal-title":"International Journal of Biological Macromolecules"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib25","doi-asserted-by":"crossref","first-page":"10138","DOI":"10.1074\/jbc.RA119.011650","article-title":"Intramitochondrial proteostasis is directly coupled to \u03b1-synuclein and amyloid \u03b21-42 pathologies","volume":"295","author":"Lautenschl\u00e4ger","year":"2020","journal-title":"The Journal of Biological Chemistry"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib26","doi-asserted-by":"crossref","first-page":"562","DOI":"10.1016\/j.ijbiomac.2020.06.274","article-title":"Copper and iron ions accelerate the prion-like propagation of \u03b1-synuclein: A vicious cycle in Parkinson\u2019s disease","volume":"163","author":"Li","year":"2020","journal-title":"International Journal of Biological Macromolecules"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib27","article-title":"The disordered protein SERF promotes \u03b1-Synuclein aggregation through liquid\u2013liquid phase separation","volume":"300","author":"Liu","year":"2024","journal-title":"The Journal of Biological Chemistry"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib28","doi-asserted-by":"crossref","first-page":"7470","DOI":"10.1074\/jbc.RA119.012284","article-title":"Structural basis of the interplay between \u03b1-synuclein and Tau in regulating pathological amyloid aggregation","volume":"295","author":"Lu","year":"2020","journal-title":"The Journal of Biological Chemistry"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib29","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2022.102239","article-title":"Molecular and functional interactions of alpha-synuclein with Rab3a","volume":"298","author":"Lv","year":"2022","journal-title":"The Journal of Biological Chemistry"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib30","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijbiomac.2023.125123","article-title":"Protein aggregation: Consequences, mechanism, characterization and inhibitory strategies","volume":"242","author":"Majid","year":"2023","journal-title":"International Journal of Biological Macromolecules"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib31","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2024.107315","article-title":"Hotspot site microenvironment in the deubiquitinase OTUB1 drives its stability and aggregation","volume":"300","author":"Majumder","year":"2024","journal-title":"The Journal of Biological Chemistry"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib32","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2020.112705","article-title":"Diphenyl triazine hybrids inhibit \u03b1-synuclein fibrillogenesis: Design, synthesis and in vitro efficacy studies","volume":"207","author":"Maqbool","year":"2020","journal-title":"European Journal of Medicinal Chemistry"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib33","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1016\/j.ijbiomac.2020.03.238","article-title":"The status of the terminal regions of \u03b1-synuclein in different forms of aggregates during fibrillization","volume":"155","author":"Marvian","year":"2020","journal-title":"International Journal of Biological Macromolecules"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib34","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijbiomac.2023.123216","article-title":"Upregulation of RIPK1 implicates in HEK 293T cell death upon transient transfection of A53T-\u03b1-synuclein","volume":"230","author":"Meshkini","year":"2023","journal-title":"International Journal of Biological Macromolecules"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib35","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijbiomac.2023.126683","article-title":"Structure specific neuro-toxicity of \u03b1-synuclein oligomer","volume":"253","author":"Mondal","year":"2023","journal-title":"International Journal of Biological Macromolecules"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib36","doi-asserted-by":"crossref","first-page":"6652","DOI":"10.1074\/jbc.RA119.012179","article-title":"\u03b1-Synuclein filaments from transgenic mouse and human synucleinopathy-containing brains are major seed-competent species","volume":"295","author":"Morgan","year":"2020","journal-title":"The Journal of Biological Chemistry"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib37","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2021.101375","article-title":"\u03b2-synuclein potentiates synaptic vesicle dopamine uptake and rescues dopaminergic neurons from MPTP-induced death in the absence of other synucleins","volume":"297","author":"Ninkina","year":"2021","journal-title":"The Journal of Biological Chemistry"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib38","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1016\/j.ijbiomac.2021.03.186","article-title":"Antioxidant activity of calycosin against \u03b1-synuclein amyloid fibrils-induced oxidative stress in neural-like cells as a model of preventive care studies in Parkinson\u2019s disease","volume":"182","author":"Pan","year":"2021","journal-title":"International Journal of Biological Macromolecules"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib39","doi-asserted-by":"crossref","first-page":"532","DOI":"10.1016\/j.ijbiomac.2020.12.130","article-title":"Acceleration of \u03b1-synuclein fibril formation and associated cytotoxicity stimulated by silica nanoparticles as a model of neurodegenerative diseases","volume":"169","author":"Pang","year":"2021","journal-title":"International Journal of Biological Macromolecules"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib40","doi-asserted-by":"crossref","first-page":"426","DOI":"10.1016\/j.ijbiomac.2022.03.092","article-title":"Insights into the inhibitory mechanism of skullcapflavone II against \u03b1-synuclein aggregation and its mediated cytotoxicity","volume":"209","author":"Parsafar","year":"2022","journal-title":"International Journal of Biological Macromolecules"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib41","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2022.101902","article-title":"The small aromatic compound SynuClean-D inhibits the aggregation and seeded polymerization of multiple \u03b1-synuclein strains","volume":"298","author":"Pe\u00f1a-D\u00edaz","year":"2022","journal-title":"The Journal of Biological Chemistry"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib42","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijbiomac.2024.130347","article-title":"Deficiency of polypeptide N-acetylgalactosamine transferase 9 contributes to a risk for Parkinson\u2019s disease via mitochondrial dysfunctions","volume":"263","author":"Peng","year":"2024","journal-title":"International Journal of Biological Macromolecules"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib43","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2022.102688","article-title":"A penetratin-derived peptide reduces the membrane permeabilization and cell toxicity of \u03b1-synuclein oligomers","volume":"298","author":"Pirhaghi","year":"2022","journal-title":"The Journal of Biological Chemistry"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib44","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2024.116490","article-title":"Novel 4-triazole phenyl amide (4-TPA) molecules: Potent promoters of \u03b1-synuclein fibril disassembly","volume":"273","author":"Qiu","year":"2024","journal-title":"European Journal of Medicinal Chemistry"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib45","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1016\/j.ijbiomac.2020.12.018","article-title":"Cu2+, Ca2+, and methionine oxidation expose the hydrophobic \u03b1-synuclein NAC domain","volume":"169","author":"Ramis","year":"2021","journal-title":"International Journal of Biological Macromolecules"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib46","doi-asserted-by":"crossref","first-page":"1278","DOI":"10.1016\/j.ijbiomac.2021.05.071","article-title":"Modulation of \u03b1-synuclein fibrillation by plant metabolites, daidzein, fisetin and scopoletin under physiological conditions","volume":"182","author":"Rane","year":"2021","journal-title":"International Journal of Biological Macromolecules"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib47","doi-asserted-by":"crossref","first-page":"392","DOI":"10.1016\/j.ijbiomac.2021.02.150","article-title":"Evidence of the existence of micellar-like aggregates for \u03b1-synuclein","volume":"177","author":"Saraiva","year":"2021","journal-title":"International Journal of Biological Macromolecules"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib48","doi-asserted-by":"crossref","first-page":"1024","DOI":"10.1016\/j.ijbiomac.2022.11.079","article-title":"Concerted enhanced-sampling simulations to elucidate the helix-fibril transition pathway of intrinsically disordered \u03b1-Synuclein","volume":"223","author":"Saurabh","year":"2022","journal-title":"International Journal of Biological Macromolecules"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib49","doi-asserted-by":"crossref","first-page":"18076","DOI":"10.1074\/jbc.RA120.015319","article-title":"\u03b1-Synuclein facilitates endocytosis by elevating the steady-state levels of phosphatidylinositol 4,5-bisphosphate","volume":"295","author":"Schechter","year":"2020","journal-title":"The Journal of Biological Chemistry"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib50","doi-asserted-by":"crossref","first-page":"18957","DOI":"10.1074\/jbc.M113.527341","article-title":"FABP3 protein promotes \u03b1-synuclein oligomerization associated with 1-methyl-1,2,3,6-tetrahydropiridine-induced neurotoxicity","volume":"289","author":"Shioda","year":"2014","journal-title":"The Journal of Biological Chemistry"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib51","doi-asserted-by":"crossref","first-page":"10224","DOI":"10.1074\/jbc.REV120.011743","article-title":"The emerging role of \u03b1-synuclein truncation in aggregation and disease","volume":"295","author":"Sorrentino","year":"2020","journal-title":"The Journal of Biological Chemistry"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib52","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2023.104566","article-title":"Cryo-EM structure of amyloid fibril formed by \u03b1-synuclein hereditary A53E mutation reveals a distinct protofilament interface","volume":"299","author":"Sun","year":"2023","journal-title":"The Journal of Biological Chemistry"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib53","doi-asserted-by":"crossref","first-page":"335","DOI":"10.31887\/DCNS.2006.8.3\/tban","volume":"8","year":"2006","journal-title":"Dialogues in Clinical Neuroscience"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib54","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1016\/j.ijbiomac.2022.12.262","article-title":"On the effect of methionine oxidation on the interplay between \u03b1-synuclein and synaptic-like vesicles","volume":"229","author":"Uceda","year":"2023","journal-title":"International Journal of Biological Macromolecules"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib55","doi-asserted-by":"crossref","first-page":"9595","DOI":"10.1074\/jbc.M411805200","article-title":"Structure and dynamics of micelle-bound human \u03b1-synuclein","volume":"280","author":"Ulmer","year":"2005","journal-title":"The Journal of Biological Chemistry"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib56","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2021.100358","article-title":"Cross-seeding of alpha-synuclein aggregation by amyloid fibrils of food proteins","volume":"296","author":"Vaneyck","year":"2021","journal-title":"The Journal of Biological Chemistry"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib57","doi-asserted-by":"crossref","first-page":"580","DOI":"10.1016\/j.ijbiomac.2022.05.045","article-title":"Ulvan inhibits \u03b1-synuclein fibrillation and disrupts the mature fibrils: in vitro and in vivo studies","volume":"211","author":"Wang","year":"2022","journal-title":"International Journal of Biological Macromolecules"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib58","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2021.100273","article-title":"Genetic deletion of Polo-like kinase 2 reduces alpha-synuclein serine-129 phosphorylation in presynaptic terminals but not Lewy bodies","volume":"296","author":"Weston","year":"2021","journal-title":"The Journal of Biological Chemistry"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib59","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2024.116198","article-title":"Pyrazolamide derivatives inhibit \u03b1-Synuclein aggregation, disaggregate preformed fibers, and reduce inclusion formation in neuron cells","volume":"268","author":"Xing","year":"2024","journal-title":"European Journal of Medicinal Chemistry"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib60","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2021.101469","article-title":"Manganese promotes \u03b1-synuclein amyloid aggregation through the induction of protein phase transition","volume":"298","author":"Xu","year":"2022","journal-title":"The Journal of Biological Chemistry"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib61","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":"Nature Communications"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib62","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2021.100567","article-title":"Suppression of aggregate and amyloid formation by a novel intrinsically disordered region in metazoan Hsp110 chaperones","volume":"296","author":"Yakubu","year":"2021","journal-title":"The Journal of Biological Chemistry"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib63","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijbiomac.2023.123194","article-title":"EGCG attenuates \u03b1-synuclein protofibril-membrane interactions and disrupts the protofibril","volume":"230","author":"Yang","year":"2023","journal-title":"International Journal of Biological Macromolecules"},{"key":"10.1016\/bs.apcsb.2024.11.002_bib64","doi-asserted-by":"crossref","first-page":"316","DOI":"10.1016\/j.ijbiomac.2022.08.088","article-title":"Baicalein exhibits differential effects and mechanisms towards disruption of \u03b1-synuclein fibrils with different polymorphs","volume":"220","author":"Yao","year":"2022","journal-title":"International Journal of Biological Macromolecules"}],"container-title":["Advances in Protein Chemistry and Structural Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1876162324001251?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1876162324001251?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,6,23]],"date-time":"2025-06-23T13:26:45Z","timestamp":1750685205000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1876162324001251"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025]]},"references-count":64,"URL":"https:\/\/doi.org\/10.1016\/bs.apcsb.2024.11.002","relation":{},"ISSN":["1876-1623"],"issn-type":[{"value":"1876-1623","type":"print"}],"subject":[],"published":{"date-parts":[[2025]]}}}