{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,27]],"date-time":"2026-08-27T13:11:30Z","timestamp":1787836290636,"version":"build-2784847793"},"reference-count":98,"publisher":"Elsevier BV","issue":"24","license":[{"start":{"date-parts":[[2025,12,1]],"date-time":"2025-12-01T00:00:00Z","timestamp":1764547200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,12,1]],"date-time":"2025-12-01T00:00:00Z","timestamp":1764547200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,10,4]],"date-time":"2025-10-04T00:00:00Z","timestamp":1759536000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000148","name":"Canadian Anesthesiologists' Society","doi-asserted-by":"publisher","award":["YSBR-095"],"award-info":[{"award-number":["YSBR-095"]}],"id":[{"id":"10.13039\/501100000148","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["22425704"],"award-info":[{"award-number":["22425704"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["32171236"],"award-info":[{"award-number":["32171236"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["82188101"],"award-info":[{"award-number":["82188101"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002367","name":"Chinese Academy of Sciences","doi-asserted-by":"publisher","award":["XDB1060000"],"award-info":[{"award-number":["XDB1060000"]}],"id":[{"id":"10.13039\/501100002367","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100015748","name":"Chinese Academy of Sciences, Shanghai Branch","doi-asserted-by":"publisher","award":["JCYJ-SHFY-2022-005"],"award-info":[{"award-number":["JCYJ-SHFY-2022-005"]}],"id":[{"id":"10.13039\/501100015748","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003399","name":"Science and Technology Commission of Shanghai Municipality","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100003399","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100016096","name":"Shanghai Key Basic Research Program","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100016096","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Molecular Biology"],"published-print":{"date-parts":[[2025,12]]},"DOI":"10.1016\/j.jmb.2025.169475","type":"journal-article","created":{"date-parts":[[2025,10,9]],"date-time":"2025-10-09T16:33:14Z","timestamp":1760027594000},"page":"169475","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":5,"title":["Rising Stars: Molecular Mechanisms and Chemical Interventions of \u03b1-Synuclein Amyloid Aggregation in Parkinson\u2019s Disease"],"prefix":"10.1016","volume":"437","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-1051-7196","authenticated-orcid":false,"given":"Shengnan","family":"Zhang","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kaien","family":"Liu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dan","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3425-6672","authenticated-orcid":false,"given":"Cong","family":"Liu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jmb.2025.169475_b0005","doi-asserted-by":"crossref","first-page":"17013","DOI":"10.1038\/nrdp.2017.13","article-title":"Parkinson's disease","volume":"3","author":"Poewe","year":"2017","journal-title":"Nature Rev Dis Primers."},{"key":"10.1016\/j.jmb.2025.169475_b0010","doi-asserted-by":"crossref","first-page":"2284","DOI":"10.1016\/S0140-6736(21)00218-X","article-title":"Parkinson's disease","volume":"397","author":"Bloem","year":"2021","journal-title":"Lancet"},{"key":"10.1016\/j.jmb.2025.169475_b0015","unstructured":"Global, regional, and national burden of Parkinson's disease, 1990\u20132016: a systematic analysis for the Global Burden of Disease Study 2016. Lancet Neurol. 17 (2018) 939\u2013953."},{"key":"10.1016\/j.jmb.2025.169475_b0020","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1038\/42166","article-title":"Alpha-synuclein in Lewy bodies","volume":"388","author":"Spillantini","year":"1997","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2025.169475_b0025","doi-asserted-by":"crossref","first-page":"6469","DOI":"10.1073\/pnas.95.11.6469","article-title":"alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies","volume":"95","author":"Spillantini","year":"1998","journal-title":"PNAS"},{"key":"10.1016\/j.jmb.2025.169475_b0030","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 disease","volume":"24","author":"Braak","year":"2003","journal-title":"Neurobiol. Aging"},{"key":"10.1016\/j.jmb.2025.169475_b0035","doi-asserted-by":"crossref","first-page":"1150","DOI":"10.1016\/S1474-4422(09)70238-8","article-title":"Neuropathological assessment of Parkinson's disease: refining the diagnostic criteria","volume":"8","author":"Dickson","year":"2009","journal-title":"Lancet Neurol."},{"key":"10.1016\/j.jmb.2025.169475_b0040","doi-asserted-by":"crossref","DOI":"10.1101\/cshperspect.a009399","article-title":"\u03b1-Synuclein in Parkinson's disease","volume":"2","author":"Stefanis","year":"2012","journal-title":"Cold Spring Harb. Perspect. Med."},{"key":"10.1016\/j.jmb.2025.169475_b0045","doi-asserted-by":"crossref","first-page":"763","DOI":"10.1002\/humu.21277","article-title":"Genetic etiology of Parkinson disease associated with mutations in the SNCA, PARK2, PINK1, PARK7, and LRRK2 genes: a mutation update","volume":"31","author":"Nuytemans","year":"2010","journal-title":"Hum. Mutat."},{"key":"10.1016\/j.jmb.2025.169475_b0050","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1038\/s41593-022-01239-7","article-title":"Post-translational modifications of soluble alpha-synuclein regulate the amplification of pathological alpha-synuclein","volume":"26","author":"Zhang","year":"2023","journal-title":"Nature Neurosci."},{"key":"10.1016\/j.jmb.2025.169475_b0055","doi-asserted-by":"crossref","first-page":"29739","DOI":"10.1074\/jbc.M600933200","article-title":"Phosphorylation of Ser-129 is the dominant pathological modification of alpha-synuclein in familial and sporadic Lewy body disease","volume":"281","author":"Anderson","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2025.169475_b0060","doi-asserted-by":"crossref","first-page":"1511","DOI":"10.1073\/pnas.1808845116","article-title":"alpha-Synuclein O-GlcNAcylation alters aggregation and toxicity, revealing certain residues as potential inhibitors of Parkinson's disease","volume":"116","author":"Levine","year":"2019","journal-title":"PNAS"},{"key":"10.1016\/j.jmb.2025.169475_b0065","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1038\/ncb748","article-title":"alpha-Synuclein is phosphorylated in synucleinopathy lesions","volume":"4","author":"Fujiwara","year":"2002","journal-title":"Nature Cell Biol."},{"key":"10.1016\/j.jmb.2025.169475_b0070","doi-asserted-by":"crossref","first-page":"2045","DOI":"10.1126\/science.276.5321.2045","article-title":"Mutation in the alpha-synuclein gene identified in families with Parkinson's disease","volume":"276","author":"Polymeropoulos","year":"1997","journal-title":"Science"},{"key":"10.1016\/j.jmb.2025.169475_b0075","doi-asserted-by":"crossref","first-page":"841","DOI":"10.1126\/science.1090278","article-title":"alpha-Synuclein locus triplication causes Parkinson's disease","volume":"302","author":"Singleton","year":"2003","journal-title":"Science"},{"key":"10.1016\/j.jmb.2025.169475_b0080","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1038\/ng0298-106","article-title":"Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease","volume":"18","author":"Kr\u00fcger","year":"1998","journal-title":"Nature Genet."},{"key":"10.1016\/j.jmb.2025.169475_b0085","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1002\/ana.10795","article-title":"The new mutation, E46K, of alpha-synuclein causes Parkinson and Lewy body dementia","volume":"55","author":"Zarranz","year":"2004","journal-title":"Ann. Neurol."},{"key":"10.1016\/j.jmb.2025.169475_b0090","doi-asserted-by":"crossref","first-page":"751","DOI":"10.1093\/hmg\/7.4.751","article-title":"Sequencing of the alpha-synuclein gene in a large series of cases of familial Parkinson's disease fails to reveal any further mutations. The European Consortium on Genetic Susceptibility in Parkinson's Disease (GSPD)","volume":"7","author":"Vaughan","year":"1998","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.jmb.2025.169475_b0095","doi-asserted-by":"crossref","first-page":"1062","DOI":"10.1212\/WNL.0b013e31828727ba","article-title":"A novel alpha-synuclein missense mutation in Parkinson disease","volume":"80","author":"Proukakis","year":"2013","journal-title":"Neurology"},{"key":"10.1016\/j.jmb.2025.169475_b0100","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1002\/ana.23894","article-title":"G51D \u03b1-synuclein mutation causes a novel parkinsonian\u2013pyramidal syndrome","volume":"73","author":"Lesage","year":"2013","journal-title":"Ann. Neurol."},{"key":"10.1016\/j.jmb.2025.169475_b0105","doi-asserted-by":"crossref","first-page":"632","DOI":"10.1016\/j.neuron.2015.03.017","article-title":"Amyloid polymorphism: structural basis and neurobiological relevance","volume":"86","author":"Tycko","year":"2015","journal-title":"Neuron"},{"key":"10.1016\/j.jmb.2025.169475_b0110","doi-asserted-by":"crossref","first-page":"89","DOI":"10.4161\/pri.3.2.8859","article-title":"Structural polymorphism of Alzheimer Abeta and other amyloid fibrils","volume":"3","author":"Fandrich","year":"2009","journal-title":"Prion"},{"key":"10.1016\/j.jmb.2025.169475_b0115","doi-asserted-by":"crossref","first-page":"340","DOI":"10.1038\/nature14547","article-title":"\u03b1-Synuclein strains cause distinct synucleinopathies after local and systemic administration","volume":"522","author":"Peelaerts","year":"2015","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2025.169475_b0120","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1038\/nrn3406","article-title":"The many faces of \u03b1-synuclein: from structure and toxicity to therapeutic target","volume":"14","author":"Lashuel","year":"2013","journal-title":"Nature Rev. Neurol."},{"key":"10.1016\/j.jmb.2025.169475_b0125","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1038\/s41582-024-01043-w","article-title":"\u03b1-Synuclein pathology as a target in neurodegenerative diseases","volume":"21","author":"Park","year":"2025","journal-title":"Nature Rev. Neurol."},{"key":"10.1016\/j.jmb.2025.169475_b0130","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s13024-024-00787-9","article-title":"Positron emission tomography tracers for synucleinopathies","volume":"20","author":"Xiang","year":"2025","journal-title":"Mol. Neurodegener."},{"key":"10.1016\/j.jmb.2025.169475_b0135","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1186\/s40035-017-0077-5","article-title":"Protein misfolding in neurodegenerative diseases: implications and strategies","volume":"6","author":"Sweeney","year":"2017","journal-title":"Transl. Neurodegener."},{"key":"10.1016\/j.jmb.2025.169475_b0140","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1038\/nm.3457","article-title":"Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases","volume":"20","author":"Guo","year":"2014","journal-title":"Nature Med."},{"key":"10.1016\/j.jmb.2025.169475_b0145","doi-asserted-by":"crossref","DOI":"10.1126\/science.aah3374","article-title":"Pathological \u03b1-synuclein transmission initiated by binding lymphocyte-activation gene 3","volume":"353","author":"Mao","year":"2016","journal-title":"Science"},{"key":"10.1016\/j.jmb.2025.169475_b0150","doi-asserted-by":"crossref","first-page":"8637","DOI":"10.1073\/pnas.0712179105","article-title":"The fold of alpha-synuclein fibrils","volume":"105","author":"Vilar","year":"2008","journal-title":"PNAS"},{"key":"10.1016\/j.jmb.2025.169475_b0155","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1038\/nature15368","article-title":"Structure of the toxic core of \u03b1-synuclein from invisible crystals","volume":"525","author":"Rodriguez","year":"2015","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2025.169475_b0160","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1038\/nsmb.3194","article-title":"Solid-state NMR structure of a pathogenic fibril of full-length human alpha-synuclein","volume":"23","author":"Tuttle","year":"2016","journal-title":"Nature Struct. Mol. Biol."},{"key":"10.1016\/j.jmb.2025.169475_b0165","doi-asserted-by":"crossref","first-page":"4458","DOI":"10.1021\/jacs.5b13261","article-title":"X-ray crystallographic structure of oligomers formed by a toxic beta-hairpin derived from alpha-synuclein: trimers and higher-order oligomers","volume":"138","author":"Salveson","year":"2016","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmb.2025.169475_b0170","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1111\/j.1365-2990.2008.00952.x","article-title":"Review: Familial Parkinson's disease\u2013genetics, clinical phenotype and neuropathology in relation to the common sporadic form of the disease","volume":"34","author":"Schiesling","year":"2008","journal-title":"Neuropathol. Appl. Neurobiol."},{"key":"10.1016\/j.jmb.2025.169475_b0175","doi-asserted-by":"crossref","DOI":"10.3390\/biomedicines13071624","article-title":"Cognitive decline in Parkinsonism: from clinical phenotypes to the genetic background","volume":"13","author":"Koros","year":"2025","journal-title":"Biomedicines"},{"key":"10.1016\/j.jmb.2025.169475_b0180","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1126\/science.aao2825","article-title":"Fibril structure of amyloid-beta(1-42) by cryo-electron microscopy","volume":"358","author":"Gremer","year":"2017","journal-title":"Science (New York, N.Y.)"},{"key":"10.1016\/j.jmb.2025.169475_b0185","doi-asserted-by":"crossref","first-page":"897","DOI":"10.1038\/s41422-018-0075-x","article-title":"Amyloid fibril structure of alpha-synuclein determined by cryo-electron microscopy","volume":"28","author":"Li","year":"2018","journal-title":"Cell Res."},{"key":"10.1016\/j.jmb.2025.169475_b0190","doi-asserted-by":"crossref","first-page":"3609","DOI":"10.1038\/s41467-018-05971-2","article-title":"Cryo-EM of full-length alpha-synuclein reveals fibril polymorphs with a common structural kernel","volume":"9","author":"Li","year":"2018","journal-title":"Nature Commun."},{"key":"10.1016\/j.jmb.2025.169475_b0195","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.36402","article-title":"Cryo-EM structure of alpha-synuclein fibrils","volume":"7","author":"Guerrero-Ferreira","year":"2018","journal-title":"Elife"},{"key":"10.1016\/j.jmb.2025.169475_b0200","doi-asserted-by":"crossref","first-page":"360","DOI":"10.1038\/s41422-020-0299-4","article-title":"Cryo-EM structure of full-length alpha-synuclein amyloid fibril with Parkinson's disease familial A53T mutation","volume":"30","author":"Sun","year":"2020","journal-title":"Cell Res."},{"key":"10.1016\/j.jmb.2025.169475_b0205","doi-asserted-by":"crossref","first-page":"6252","DOI":"10.1038\/s41467-021-26433-2","article-title":"The hereditary mutation G51D unlocks a distinct fibril strain transmissible to wild-type alpha-synuclein","volume":"12","author":"Sun","year":"2021","journal-title":"Nature Commun."},{"key":"10.1016\/j.jmb.2025.169475_b0210","doi-asserted-by":"crossref","first-page":"360","DOI":"10.1038\/s41422-020-0299-4","article-title":"Cryo-EM structure of full-length \u03b1-synuclein amyloid fibril with Parkinson's disease familial A53T mutation","volume":"30","author":"Sun","year":"2020","journal-title":"Cell Res."},{"key":"10.1016\/j.jmb.2025.169475_b0215","doi-asserted-by":"crossref","first-page":"464","DOI":"10.1038\/s41586-020-2317-6","article-title":"Structures of alpha-synuclein filaments from multiple system atrophy","volume":"585","author":"Schweighauser","year":"2020","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2025.169475_b0220","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2012435118","article-title":"Wild-type alpha-synuclein inherits the structure and exacerbated neuropathology of E46K mutant fibril strain by cross-seeding","volume":"118","author":"Long","year":"2021","journal-title":"PNAS"},{"key":"10.1016\/j.jmb.2025.169475_b0225","doi-asserted-by":"crossref","first-page":"20305","DOI":"10.1073\/pnas.1922741117","article-title":"Parkinson's disease-related phosphorylation at Tyr39 rearranges alpha-synuclein amyloid fibril structure revealed by cryo-EM","volume":"117","author":"Zhao","year":"2020","journal-title":"PNAS"},{"key":"10.1016\/j.jmb.2025.169475_b0230","article-title":"N-acetylation of alpha-synuclein enhances synaptic vesicle clustering mediated by alpha-synuclein and lysophosphatidylcholine","author":"Wang","year":"2024","journal-title":"bioRxiv"},{"key":"10.1016\/j.jmb.2025.169475_b0235","doi-asserted-by":"crossref","first-page":"3184","DOI":"10.1523\/JNEUROSCI.5922-09.2010","article-title":"Phosphorylation at S87 is enhanced in synucleinopathies, inhibits alpha-synuclein oligomerization, and influences synuclein-membrane interactions","volume":"30","author":"Paleologou","year":"2010","journal-title":"J. Neurosci."},{"key":"10.1016\/j.jmb.2025.169475_b0240","doi-asserted-by":"crossref","first-page":"1536","DOI":"10.1523\/JNEUROSCI.3784-11.2012","article-title":"Mimicking phosphorylation at serine 87 inhibits the aggregation of human alpha-synuclein and protects against its toxicity in a rat model of Parkinson's disease","volume":"32","author":"Oueslati","year":"2012","journal-title":"J. Neurosci."},{"key":"10.1016\/j.jmb.2025.169475_b0245","doi-asserted-by":"crossref","first-page":"523","DOI":"10.1038\/s41583-022-00603-7","article-title":"Conformational strains of pathogenic amyloid proteins in neurodegenerative diseases","volume":"23","author":"Li","year":"2022","journal-title":"Nature Rev. Neurosci."},{"key":"10.1016\/j.jmb.2025.169475_b0250","doi-asserted-by":"crossref","first-page":"1335","DOI":"10.1016\/j.str.2023.08.006","article-title":"Molecular rules governing the structural polymorphism of amyloid fibrils in neurodegenerative diseases","volume":"31","author":"Li","year":"2023","journal-title":"Structure"},{"key":"10.1016\/j.jmb.2025.169475_b0255","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1038\/s41589-020-00708-z","article-title":"Hierarchical chemical determination of amyloid polymorphs in neurodegenerative disease","volume":"17","author":"Li","year":"2021","journal-title":"Nature Chem. Biol."},{"key":"10.1016\/j.jmb.2025.169475_b0260","doi-asserted-by":"crossref","first-page":"791","DOI":"10.1038\/s41586-022-05319-3","article-title":"Structures of alpha-synuclein filaments from human brains with Lewy pathology","volume":"610","author":"Yang","year":"2022","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2025.169475_b0265","article-title":"Lewy-MSA hybrid fold drives distinct neuronal alpha-synuclein pathology","author":"Enomoto","year":"2024","journal-title":"bioRxiv"},{"key":"10.1016\/j.jmb.2025.169475_b0270","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1007\/s00401-023-02550-8","article-title":"New SNCA mutation and structures of alpha-synuclein filaments from juvenile-onset synucleinopathy","volume":"145","author":"Yang","year":"2023","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.jmb.2025.169475_b0275","doi-asserted-by":"crossref","first-page":"504","DOI":"10.1038\/nm1747","article-title":"Lewy body-like pathology in long-term embryonic nigral transplants in Parkinson's disease","volume":"14","author":"Kordower","year":"2008","journal-title":"Nature Med."},{"key":"10.1016\/j.jmb.2025.169475_b0280","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1038\/nm1746","article-title":"Lewy bodies in grafted neurons in subjects with Parkinson's disease suggest host-to-graft disease propagation","volume":"14","author":"Li","year":"2008","journal-title":"Nature Med."},{"key":"10.1016\/j.jmb.2025.169475_b0285","doi-asserted-by":"crossref","first-page":"1091","DOI":"10.1002\/mds.23012","article-title":"Characterization of Lewy body pathology in 12- and 16-year-old intrastriatal mesencephalic grafts surviving in a patient with Parkinson's disease","volume":"25","author":"Li","year":"2010","journal-title":"Mov. Disord."},{"key":"10.1016\/j.jmb.2025.169475_b0290","doi-asserted-by":"crossref","first-page":"4663","DOI":"10.1038\/s41467-024-49016-3","article-title":"Aplp1 interacts with Lag3 to facilitate transmission of pathologic alpha-synuclein","volume":"15","author":"Mao","year":"2024","journal-title":"Nature Commun."},{"key":"10.1016\/j.jmb.2025.169475_b0295","article-title":"Mechanistic basis for receptor-mediated pathological alpha-synuclein fibril cell-to-cell transmission in Parkinson's disease","volume":"118","author":"Zhang","year":"2021","journal-title":"PNAS"},{"key":"10.1016\/j.jmb.2025.169475_b0300","doi-asserted-by":"crossref","DOI":"10.1016\/j.celrep.2022.111401","article-title":"Interaction of RAGE with alpha-synuclein fibrils mediates inflammatory response of microglia","volume":"40","author":"Long","year":"2022","journal-title":"Cell Rep."},{"key":"10.1016\/j.jmb.2025.169475_b0305","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1038\/s41422-024-01022-2","article-title":"alpha-Synuclein amyloid fibril directly binds to LC3B and suppresses SQSTM1\/p62-mediated selective autophagy","volume":"35","author":"Xu","year":"2025","journal-title":"Cell Res."},{"key":"10.1016\/j.jmb.2025.169475_b0310","doi-asserted-by":"crossref","first-page":"4473","DOI":"10.1021\/jacs.2c10854","article-title":"Conformational dynamics of an alpha-synuclein fibril upon receptor binding revealed by insensitive nuclei enhanced by polarization transfer-based solid-state nuclear magnetic resonance and cryo-electron microscopy","volume":"145","author":"Zhang","year":"2023","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmb.2025.169475_b0315","doi-asserted-by":"crossref","first-page":"446","DOI":"10.1111\/j.1365-2141.2010.08266.x","article-title":"A pilot study of the histone-deacetylase inhibitor givinostat in patients with JAK2V617F positive chronic myeloproliferative neoplasms","volume":"150","author":"Rambaldi","year":"2010","journal-title":"Br. J. Haematol."},{"key":"10.1016\/j.jmb.2025.169475_b0320","doi-asserted-by":"crossref","first-page":"28282","DOI":"10.1021\/jacs.4c08869","article-title":"Inhibitor development for alpha-synuclein fibril's disordered region to alleviate Parkinson's disease pathology","volume":"146","author":"Zhang","year":"2024","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmb.2025.169475_b0325","doi-asserted-by":"crossref","first-page":"892","DOI":"10.1126\/science.adp3645","article-title":"Neuronal FAM171A2 mediates alpha-synuclein fibril uptake and drives Parkinson's disease","volume":"387","author":"Wu","year":"2025","journal-title":"Science"},{"key":"10.1016\/j.jmb.2025.169475_b0330","doi-asserted-by":"crossref","first-page":"1235","DOI":"10.1038\/s41589-023-01370-x","article-title":"Structural mechanism for specific binding of chemical compounds to amyloid fibrils","volume":"19","author":"Tao","year":"2023","journal-title":"Nature Chem. Biol."},{"key":"10.1016\/j.jmb.2025.169475_b0335","article-title":"Binding adaptability of chemical ligands to polymorphic alpha-synuclein amyloid fibrils","volume":"121","author":"Liu","year":"2024","journal-title":"PNAS"},{"key":"10.1016\/j.jmb.2025.169475_b0340","doi-asserted-by":"crossref","first-page":"3350","DOI":"10.1016\/j.cell.2023.06.004","article-title":"Development of an alpha-synuclein positron emission tomography tracer for imaging synucleinopathies","volume":"186","author":"Xiang","year":"2023","journal-title":"Cell"},{"key":"10.1016\/j.jmb.2025.169475_b0345","doi-asserted-by":"crossref","first-page":"4226","DOI":"10.1038\/s41467-022-31790-7","article-title":"Heparin induces alpha-synuclein to form new fibril polymorphs with attenuated neuropathology","volume":"13","author":"Tao","year":"2022","journal-title":"Nature Commun."},{"key":"10.1016\/j.jmb.2025.169475_b0350","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1038\/s41594-024-01407-2","article-title":"Time-course remodeling and pathology intervention of alpha-synuclein amyloid fibril by heparin and heparin-like oligosaccharides","volume":"32","author":"Tao","year":"2025","journal-title":"Nature Struct. Mol. Biol."},{"key":"10.1016\/j.jmb.2025.169475_b0355","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.adq3539","article-title":"Mouse alpha-synuclein fibrils are structurally and functionally distinct from human fibrils associated with Lewy body diseases","volume":"10","author":"Sokratian","year":"2024","journal-title":"Sci. Adv."},{"key":"10.1016\/j.jmb.2025.169475_b0360","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1038\/s41593-019-0541-x","article-title":"alpha-Synuclein strains target distinct brain regions and cell types","volume":"23","author":"Lau","year":"2020","journal-title":"Nature Neurosci."},{"key":"10.1016\/j.jmb.2025.169475_b0365","doi-asserted-by":"crossref","first-page":"977","DOI":"10.1007\/s00401-020-02157-3","article-title":"The structural differences between patient-derived alpha-synuclein strains dictate characteristics of Parkinson's disease, multiple system atrophy and dementia with Lewy bodies","volume":"139","author":"Van der Perren","year":"2020","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.jmb.2025.169475_b0370","doi-asserted-by":"crossref","first-page":"558","DOI":"10.1038\/s41586-018-0104-4","article-title":"Cellular milieu imparts distinct pathological alpha-synuclein strains in alpha-synucleinopathies","volume":"557","author":"Peng","year":"2018","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2025.169475_b0375","doi-asserted-by":"crossref","first-page":"663","DOI":"10.1007\/s00401-022-02425-4","article-title":"Unique seeding profiles and prion-like propagation of synucleinopathies are highly dependent on the host in human alpha-synuclein transgenic mice","volume":"143","author":"Lloyd","year":"2022","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.jmb.2025.169475_b0380","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1007\/s00401-018-1914-z","article-title":"Tau filaments from multiple cases of sporadic and inherited Alzheimer's disease adopt a common fold","volume":"136","author":"Falcon","year":"2018","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.jmb.2025.169475_b0385","doi-asserted-by":"crossref","first-page":"3454","DOI":"10.1093\/brain\/awac171","article-title":"Tau accelerates \u03b1-synuclein aggregation and spreading in Parkinson's disease","volume":"145","author":"Pan","year":"2022","journal-title":"Brain"},{"key":"10.1016\/j.jmb.2025.169475_b0390","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1016\/j.tins.2024.01.002","article-title":"Protein-protein interactions regulating \u03b1-synuclein pathology","volume":"47","author":"Wang","year":"2024","journal-title":"Trends Neurosci."},{"key":"10.1016\/j.jmb.2025.169475_b0395","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1038\/nchembio.1750","article-title":"Lipid vesicles trigger \u03b1-synuclein aggregation by stimulating primary nucleation","volume":"11","author":"Galvagnion","year":"2015","journal-title":"Nature Chem. Biol."},{"key":"10.1016\/j.jmb.2025.169475_b0400","doi-asserted-by":"crossref","first-page":"4971","DOI":"10.1073\/pnas.1913904117","article-title":"The process of Lewy body formation, rather than simply \u03b1-synuclein fibrillization, is one of the major drivers of neurodegeneration","volume":"117","author":"Mahul-Mellier","year":"2020","journal-title":"PNAS"},{"key":"10.1016\/j.jmb.2025.169475_b0405","doi-asserted-by":"crossref","first-page":"705","DOI":"10.1038\/s41557-020-0465-9","article-title":"alpha-Synuclein aggregation nucleates through liquid-liquid phase separation","volume":"12","author":"Ray","year":"2020","journal-title":"Nature Chem."},{"key":"10.1016\/j.jmb.2025.169475_b0410","doi-asserted-by":"crossref","first-page":"2110","DOI":"10.1038\/s41467-021-22108-0","article-title":"In situ architecture of neuronal alpha-Synuclein inclusions","volume":"12","author":"Trinkaus","year":"2021","journal-title":"Nature Commun."},{"key":"10.1016\/j.jmb.2025.169475_b0415","doi-asserted-by":"crossref","first-page":"913","DOI":"10.1038\/s41586-024-07680-x","article-title":"CryoET of beta-amyloid and tau within postmortem Alzheimer's disease brain","volume":"631","author":"Gilbert","year":"2024","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2025.169475_b0420","doi-asserted-by":"crossref","first-page":"2660","DOI":"10.1038\/s41467-024-47066-1","article-title":"Ultrastructure of human brain tissue vitrified from autopsy revealed by cryo-ET with cryo-plasma FIB milling","volume":"15","author":"Creekmore","year":"2024","journal-title":"Nature Commun."},{"key":"10.1016\/j.jmb.2025.169475_b0425","doi-asserted-by":"crossref","first-page":"9228","DOI":"10.1038\/srep09228","article-title":"Structure based aggregation studies reveal the presence of helix-rich intermediate during \u03b1-Synuclein aggregation","volume":"5","author":"Ghosh","year":"2015","journal-title":"Sci. Rep."},{"key":"10.1016\/j.jmb.2025.169475_b0430","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1016\/j.bbrc.2021.04.124","article-title":"Structural insight into transmissive mutant huntingtin species by correlative light and electron microscopy and cryo-electron tomography","volume":"560","author":"Kuang","year":"2021","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.jmb.2025.169475_b0435","doi-asserted-by":"crossref","first-page":"1980","DOI":"10.1016\/j.molcel.2024.04.018","article-title":"Autophagy preferentially degrades non-fibrillar polyQ aggregates","volume":"84","author":"Zhao","year":"2024","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jmb.2025.169475_b0440","doi-asserted-by":"crossref","first-page":"1099","DOI":"10.1038\/s41593-019-0423-2","article-title":"Lewy pathology in Parkinson's disease consists of crowded organelles and lipid membranes","volume":"22","author":"Shahmoradian","year":"2019","journal-title":"Nature Neurosci."},{"key":"10.1016\/j.jmb.2025.169475_b0445","article-title":"alpha-Synuclein condensation in synaptic vesicle function and synucleinopathies","author":"Li","year":"2025","journal-title":"Trends Cell Biol."},{"key":"10.1016\/j.jmb.2025.169475_b0450","doi-asserted-by":"crossref","first-page":"1306","DOI":"10.1038\/s41557-023-01244-8","article-title":"Mass photometric detection and quantification of nanoscale alpha-synuclein phase separation","volume":"15","author":"Ray","year":"2023","journal-title":"Nature Chem."},{"key":"10.1016\/j.jmb.2025.169475_b0455","first-page":"282","article-title":"Observation of an alpha-synuclein liquid droplet state and its maturation into Lewy body-like assemblies","volume":"13","author":"Hardenberg","year":"2021","journal-title":"J. Mol. Cell Biol."},{"key":"10.1016\/j.jmb.2025.169475_b0460","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2208792120","article-title":"Spontaneous nucleation and fast aggregate-dependent proliferation of alpha-synuclein aggregates within liquid condensates at neutral pH","volume":"120","author":"Dada","year":"2023","journal-title":"PNAS"},{"key":"10.1016\/j.jmb.2025.169475_b0465","doi-asserted-by":"crossref","first-page":"1287","DOI":"10.1038\/s41556-024-01456-1","article-title":"VAMP2 chaperones alpha-synuclein in synaptic vesicle co-condensates","volume":"26","author":"Wang","year":"2024","journal-title":"Nature Cell Biol."},{"key":"10.1016\/j.jmb.2025.169475_b0470","doi-asserted-by":"crossref","first-page":"1296","DOI":"10.1038\/s41556-024-01451-6","article-title":"VAMP2 regulates phase separation of alpha-synuclein","volume":"26","author":"Agarwal","year":"2024","journal-title":"Nature Cell Biol."},{"key":"10.1016\/j.jmb.2025.169475_b0475","doi-asserted-by":"crossref","first-page":"2159","DOI":"10.1002\/mds.29186","article-title":"High-contrast imaging of alpha-synuclein pathologies in living patients with multiple system atrophy","volume":"37","author":"Matsuoka","year":"2022","journal-title":"Mov. Disord."},{"key":"10.1016\/j.jmb.2025.169475_b0480","doi-asserted-by":"crossref","first-page":"2540","DOI":"10.1016\/j.neuron.2024.05.006","article-title":"Imaging alpha-synuclein pathologies in animal models and patients with Parkinson's and related diseases","volume":"112","author":"Endo","year":"2024","journal-title":"Neuron"},{"key":"10.1016\/j.jmb.2025.169475_b0485","doi-asserted-by":"crossref","DOI":"10.1038\/s41573-025-01165-w","article-title":"Biomarker-guided decision making in clinical drug development for neurodegenerative disorders","author":"Cummings","year":"2025","journal-title":"Nature Rev. Drug Discov."},{"key":"10.1016\/j.jmb.2025.169475_b0490","doi-asserted-by":"crossref","first-page":"396","DOI":"10.1038\/s41591-024-03469-7","article-title":"Toward a biological definition of neuronal and glial synucleinopathies","volume":"31","author":"Soto","year":"2025","journal-title":"Nature Med."}],"container-title":["Journal of Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283625005418?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283625005418?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,6,9]],"date-time":"2026-06-09T11:54:05Z","timestamp":1781006045000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0022283625005418"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,12]]},"references-count":98,"journal-issue":{"issue":"24","published-print":{"date-parts":[[2025,12]]}},"alternative-id":["S0022283625005418"],"URL":"https:\/\/doi.org\/10.1016\/j.jmb.2025.169475","relation":{},"ISSN":["0022-2836"],"issn-type":[{"value":"0022-2836","type":"print"}],"subject":[],"published":{"date-parts":[[2025,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Rising Stars: Molecular Mechanisms and Chemical Interventions of \u03b1-Synuclein Amyloid Aggregation in Parkinson\u2019s Disease","name":"articletitle","label":"Article Title"},{"value":"Journal of Molecular Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jmb.2025.169475","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 The Author(s). Published by Elsevier Ltd.","name":"copyright","label":"Copyright"}],"article-number":"169475"}}