{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T21:53:02Z","timestamp":1790373182564,"version":"4.1.0"},"reference-count":90,"publisher":"Elsevier BV","issue":"6","license":[{"start":{"date-parts":[[2025,6,1]],"date-time":"2025-06-01T00:00:00Z","timestamp":1748736000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,6,1]],"date-time":"2025-06-01T00:00:00Z","timestamp":1748736000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,5,9]],"date-time":"2025-05-09T00:00:00Z","timestamp":1746748800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100004608","name":"Jiangsu Province Natural Science Foundation","doi-asserted-by":"publisher","award":["BK20200036"],"award-info":[{"award-number":["BK20200036"]}],"id":[{"id":"10.13039\/501100004608","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100012246","name":"Priority Academic Program Development of Jiangsu Higher Education Institutions","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100012246","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["32270735"],"award-info":[{"award-number":["32270735"]}],"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":["32100546"],"award-info":[{"award-number":["32100546"]}],"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":["32470877"],"award-info":[{"award-number":["32470877"]}],"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":["82401817"],"award-info":[{"award-number":["82401817"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100012154","name":"Graduate Research and Innovation Projects of Jiangsu Province","doi-asserted-by":"publisher","award":["JSSCTD202142"],"award-info":[{"award-number":["JSSCTD202142"]}],"id":[{"id":"10.13039\/501100012154","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100012154","name":"Graduate Research and Innovation Projects of Jiangsu Province","doi-asserted-by":"publisher","award":["KYCX23_1736"],"award-info":[{"award-number":["KYCX23_1736"]}],"id":[{"id":"10.13039\/501100012154","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Cell Reports"],"published-print":{"date-parts":[[2025,6]]},"DOI":"10.1016\/j.celrep.2025.115761","type":"journal-article","created":{"date-parts":[[2025,5,28]],"date-time":"2025-05-28T08:29:58Z","timestamp":1748420998000},"page":"115761","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":9,"title":["\u03b2-synuclein blocks \u03b1-synuclein condensate fusion to disrupt the maturation of phase separation"],"prefix":"10.1016","volume":"44","author":[{"given":"Bingkuan","family":"Xu","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wenyuan","family":"He","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fengshuo","family":"Fan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shuhan","family":"Chen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Min","family":"Zhu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yanjun","family":"Hou","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lingjun","family":"Zheng","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7193-8034","authenticated-orcid":false,"given":"Haijia","family":"Yu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yinghui","family":"Liu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.celrep.2025.115761_bib1","doi-asserted-by":"crossref","first-page":"896","DOI":"10.1016\/S0140-6736(14)61393-3","article-title":"Parkinson's disease","volume":"386","author":"Kalia","year":"2015","journal-title":"Lancet"},{"key":"10.1016\/j.celrep.2025.115761_bib2","first-page":"879","article-title":"Aggregation of alpha-synuclein in Lewy bodies of sporadic Parkinson's disease and dementia with Lewy bodies","volume":"152","author":"Baba","year":"1998","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.celrep.2025.115761_bib3","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.celrep.2025.115761_bib4","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1016\/S0304-3940(00)01440-3","article-title":"Characterisation of isolated alpha-synuclein filaments from substantia nigra of Parkinson's disease brain","volume":"292","author":"Crowther","year":"2000","journal-title":"Neurosci. Lett."},{"key":"10.1016\/j.celrep.2025.115761_bib5","doi-asserted-by":"crossref","first-page":"334","DOI":"10.1097\/00005072-199804000-00005","article-title":"Nigral and cortical Lewy bodies and dystrophic nigral neurites in Parkinson's disease and cortical Lewy body disease contain alpha-synuclein immunoreactivity","volume":"57","author":"Irizarry","year":"1998","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"10.1016\/j.celrep.2025.115761_bib6","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1038\/sj.mp.4000446","article-title":"Alpha synuclein is present in Lewy bodies in sporadic Parkinson's disease","volume":"3","author":"Mezey","year":"1998","journal-title":"Mol. Psychiatry"},{"key":"10.1016\/j.celrep.2025.115761_bib7","doi-asserted-by":"crossref","first-page":"9595","DOI":"10.1074\/jbc.M411805200","article-title":"Structure and dynamics of micelle-bound human alpha-synuclein","volume":"280","author":"Ulmer","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.celrep.2025.115761_bib8","doi-asserted-by":"crossref","first-page":"1061","DOI":"10.1006\/jmbi.2001.4538","article-title":"Conformational properties of alpha-synuclein in its free and lipid-associated states","volume":"307","author":"Eliezer","year":"2001","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.celrep.2025.115761_bib9","doi-asserted-by":"crossref","first-page":"2804","DOI":"10.1523\/JNEUROSCI.08-08-02804.1988","article-title":"Synuclein: a neuron-specific protein localized to the nucleus and presynaptic nerve terminal","volume":"8","author":"Maroteaux","year":"1988","journal-title":"J. Neurosci."},{"key":"10.1016\/j.celrep.2025.115761_bib10","doi-asserted-by":"crossref","first-page":"15345","DOI":"10.1074\/jbc.M111.318949","article-title":"\u03b1-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer","volume":"287","author":"Fauvet","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.celrep.2025.115761_bib11","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1038\/nature10324","article-title":"\u03b1-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation","volume":"477","author":"Bartels","year":"2011","journal-title":"Nature"},{"key":"10.1016\/j.celrep.2025.115761_bib12","doi-asserted-by":"crossref","first-page":"17797","DOI":"10.1073\/pnas.1113260108","article-title":"A soluble \u03b1-synuclein construct forms a dynamic tetramer","volume":"108","author":"Wang","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.celrep.2025.115761_bib13","doi-asserted-by":"crossref","first-page":"1663","DOI":"10.1126\/science.1195227","article-title":"Alpha-synuclein promotes SNARE-complex assembly in vivo and in vitro","volume":"329","author":"Burr\u00e9","year":"2010","journal-title":"Science"},{"key":"10.1016\/j.celrep.2025.115761_bib14","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1111\/jnc.14721","article-title":"Effects of alpha-synuclein post-translational modifications on metal binding","volume":"150","author":"Gonz\u00e1lez","year":"2019","journal-title":"J. Neurochem."},{"key":"10.1016\/j.celrep.2025.115761_bib15","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/j.ijbiomac.2016.10.021","article-title":"\u03b1-synuclein aggregation and its modulation","volume":"100","author":"Ghosh","year":"2017","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.celrep.2025.115761_bib16","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1016\/j.neuron.2011.08.033","article-title":"Exogenous \u03b1-synuclein fibrils induce Lewy body pathology leading to synaptic dysfunction and neuron death","volume":"72","author":"Volpicelli-Daley","year":"2011","journal-title":"Neuron"},{"key":"10.1016\/j.celrep.2025.115761_bib17","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":"J. Biol. Chem."},{"key":"10.1016\/j.celrep.2025.115761_bib18","doi-asserted-by":"crossref","first-page":"299","DOI":"10.3389\/fnmol.2019.00299","article-title":"Targeting Alpha-Synuclein as a Therapy for Parkinson's Disease","volume":"12","author":"Fields","year":"2019","journal-title":"Front. Mol. Neurosci."},{"key":"10.1016\/j.celrep.2025.115761_bib19","doi-asserted-by":"crossref","first-page":"11970","DOI":"10.1074\/jbc.M109541200","article-title":"Biophysical properties of the synucleins and their propensities to fibrillate: inhibition of alpha-synuclein assembly by beta- and gamma-synucleins","volume":"277","author":"Uversky","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.celrep.2025.115761_bib20","doi-asserted-by":"crossref","first-page":"3830","DOI":"10.1021\/acs.biochem.8b00343","article-title":"Comparative Analysis of the Conformation, Aggregation, Interaction, and Fibril Morphologies of Human \u03b1-\u03b2-and \u03b3-Synuclein Proteins","volume":"57","author":"Jain","year":"2018","journal-title":"Biochemistry"},{"key":"10.1016\/j.celrep.2025.115761_bib21","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1046\/j.0014-2956.2001.02633.x","article-title":"A Raman optical activity study of rheomorphism in caseins, synucleins and tau. New insight into the structure and behaviour of natively unfolded proteins","volume":"269","author":"Syme","year":"2002","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.celrep.2025.115761_bib22","doi-asserted-by":"crossref","DOI":"10.1016\/j.celrep.2022.110675","article-title":"Synaptic vesicle binding of \u03b1-synuclein is modulated by \u03b2- and \u03b3-synucleins","volume":"39","author":"Carnazza","year":"2022","journal-title":"Cell Rep."},{"key":"10.1016\/j.celrep.2025.115761_bib23","doi-asserted-by":"crossref","DOI":"10.1038\/srep15164","article-title":"Unveiling transient protein-protein interactions that modulate inhibition of alpha-synuclein aggregation by beta-synuclein, a pre-synaptic protein that co-localizes with alpha-synuclein","volume":"5","author":"Janowska","year":"2015","journal-title":"Sci. Rep."},{"key":"10.1016\/j.celrep.2025.115761_bib24","doi-asserted-by":"crossref","first-page":"995","DOI":"10.1096\/fj.201700675R","article-title":"Levels of \u03b1- and \u03b2-synuclein regulate cellular susceptibility to toxicity from \u03b1-synuclein oligomers","volume":"32","author":"Angelova","year":"2018","journal-title":"FASEB J."},{"key":"10.1016\/j.celrep.2025.115761_bib25","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1007\/s12031-002-0012-8","article-title":"Development of a new treatment for Alzheimer's disease and Parkinson's disease using anti-aggregatory beta-synuclein-derived peptides","volume":"19","author":"Windisch","year":"2002","journal-title":"J. Mol. Neurosci."},{"key":"10.1016\/j.celrep.2025.115761_bib26","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1016\/S0896-6273(01)00462-7","article-title":"beta-Synuclein inhibits alpha-synuclein aggregation: a possible role as an anti-parkinsonian factor","volume":"32","author":"Hashimoto","year":"2001","journal-title":"Neuron"},{"key":"10.1016\/j.celrep.2025.115761_bib27","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1212\/01.WNL.0000139870.14385.3C","article-title":"Beta-synuclein gene alterations in dementia with Lewy bodies","volume":"63","author":"Ohtake","year":"2004","journal-title":"Neurology"},{"key":"10.1016\/j.celrep.2025.115761_bib28","doi-asserted-by":"crossref","first-page":"286","DOI":"10.1002\/pro.2798","article-title":"The loss of inhibitory C-terminal conformations in disease associated P123H \u03b2-synuclein","volume":"25","author":"Janowska","year":"2016","journal-title":"Protein Sci."},{"key":"10.1016\/j.celrep.2025.115761_bib29","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1038\/ncomms1101","article-title":"A \u03b2-synuclein mutation linked to dementia produces neurodegeneration when expressed in mouse brain","volume":"1","author":"Fujita","year":"2010","journal-title":"Nat. Commun."},{"key":"10.1016\/j.celrep.2025.115761_bib30","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1093\/hmg\/ddv470","article-title":"Yeast reveals similar molecular mechanisms underlying alpha- and beta-synuclein toxicity","volume":"25","author":"Tenreiro","year":"2016","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.celrep.2025.115761_bib31","doi-asserted-by":"crossref","first-page":"28904","DOI":"10.1074\/jbc.M703711200","article-title":"Enhanced lysosomal pathology caused by beta-synuclein mutants linked to dementia with Lewy bodies","volume":"282","author":"Wei","year":"2007","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.celrep.2025.115761_bib32","article-title":"Heterochromatin organization and phase separation","volume":"14","author":"Zhang","year":"2023","journal-title":"Nucleus (Calcutta)"},{"key":"10.1016\/j.celrep.2025.115761_bib33","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1016\/j.ncrna.2021.04.003","article-title":"RNA and liquid-liquid phase separation","volume":"6","author":"Guo","year":"2021","journal-title":"Noncoding. RNA Res."},{"key":"10.1016\/j.celrep.2025.115761_bib34","doi-asserted-by":"crossref","first-page":"4976","DOI":"10.1039\/D3CS01065A","article-title":"Protein misfolding and amyloid nucleation through liquid-liquid phase separation","volume":"53","author":"Mukherjee","year":"2024","journal-title":"Chem. Soc. Rev."},{"key":"10.1016\/j.celrep.2025.115761_bib35","doi-asserted-by":"crossref","DOI":"10.1126\/science.aaf4382","article-title":"Liquid phase condensation in cell physiology and disease","volume":"357","author":"Shin","year":"2017","journal-title":"Science"},{"key":"10.1016\/j.celrep.2025.115761_bib36","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1038\/nrm.2017.7","article-title":"Biomolecular condensates: organizers of cellular biochemistry","volume":"18","author":"Banani","year":"2017","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.celrep.2025.115761_bib37","doi-asserted-by":"crossref","DOI":"10.15252\/embj.201798049","article-title":"Tau protein liquid-liquid phase separation can initiate tau aggregation","volume":"37","author":"Wegmann","year":"2018","journal-title":"EMBO J."},{"key":"10.1016\/j.celrep.2025.115761_bib38","doi-asserted-by":"crossref","first-page":"1066","DOI":"10.1016\/j.cell.2015.07.047","article-title":"A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation","volume":"162","author":"Patel","year":"2015","journal-title":"Cell"},{"key":"10.1016\/j.celrep.2025.115761_bib39","doi-asserted-by":"crossref","first-page":"705","DOI":"10.1038\/s41557-020-0465-9","article-title":"\u03b1-Synuclein aggregation nucleates through liquid-liquid phase separation","volume":"12","author":"Ray","year":"2020","journal-title":"Nat. Chem."},{"key":"10.1016\/j.celrep.2025.115761_bib40","first-page":"282","article-title":"Observation of an \u03b1-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.celrep.2025.115761_bib41","doi-asserted-by":"crossref","first-page":"7289","DOI":"10.1038\/s41467-021-27433-y","article-title":"Capillary flow experiments for thermodynamic and kinetic characterization of protein liquid-liquid phase separation","volume":"12","author":"Stender","year":"2021","journal-title":"Nat. Commun."},{"key":"10.1016\/j.celrep.2025.115761_bib42","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.adg5663","article-title":"\u03b1-Synuclein liquid condensates fuel fibrillar \u03b1-synuclein growth","volume":"9","author":"Piroska","year":"2023","journal-title":"Sci. Adv."},{"key":"10.1016\/j.celrep.2025.115761_bib43","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2208792120","article-title":"Spontaneous nucleation and fast aggregate-dependent proliferation of \u03b1-synuclein aggregates within liquid condensates at neutral pH","volume":"120","author":"Dada","year":"2023","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.celrep.2025.115761_bib44","doi-asserted-by":"crossref","DOI":"10.1002\/anie.202205726","article-title":"Direct Observation of \"Elongated\" Conformational States in \u03b1-Synuclein upon Liquid-Liquid Phase Separation","volume":"61","author":"Ubbiali","year":"2022","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"10.1016\/j.celrep.2025.115761_bib45","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/j.bbrc.2022.02.097","article-title":"Calcium promotes \u03b1-synuclein liquid-liquid phase separation to accelerate amyloid aggregation","volume":"603","author":"Huang","year":"2022","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.celrep.2025.115761_bib46","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":"J. Biol. Chem."},{"key":"10.1016\/j.celrep.2025.115761_bib47","doi-asserted-by":"crossref","DOI":"10.3390\/biom13050726","article-title":"Distinct Effects of Familial Parkinson's Disease-Associated Mutations on \u03b1-Synuclein Phase Separation and Amyloid Aggregation","volume":"13","author":"Xu","year":"2023","journal-title":"Biomolecules"},{"key":"10.1016\/j.celrep.2025.115761_bib48","doi-asserted-by":"crossref","first-page":"3835","DOI":"10.1038\/s41467-024-47585-x","article-title":"Pharmacological inhibition of \u03b1-synuclein aggregation within liquid condensates","volume":"15","author":"Dada","year":"2024","journal-title":"Nat. Commun."},{"key":"10.1016\/j.celrep.2025.115761_bib49","doi-asserted-by":"crossref","first-page":"11845","DOI":"10.1002\/chem.202101592","article-title":"Remodeling of the Fibrillation Pathway of \u03b1-Synuclein by Interaction with Antimicrobial Peptide LL-III","volume":"27","author":"Oliva","year":"2021","journal-title":"Chemistry"},{"key":"10.1016\/j.celrep.2025.115761_bib50","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.abq6495","article-title":"Biomolecular condensates can both accelerate and suppress aggregation of \u03b1-synuclein","volume":"8","author":"Lipi\u0144ski","year":"2022","journal-title":"Sci. Adv."},{"key":"10.1016\/j.celrep.2025.115761_bib51","doi-asserted-by":"crossref","DOI":"10.1002\/pro.4951","article-title":"Liquid-liquid phase separation of \u03b1-synuclein is highly sensitive to sequence complexity","volume":"33","author":"Mahapatra","year":"2024","journal-title":"Protein Sci."},{"key":"10.1016\/j.celrep.2025.115761_bib52","doi-asserted-by":"crossref","first-page":"4586","DOI":"10.1038\/s41467-022-32350-9","article-title":"Molecular mechanism for the synchronized electrostatic coacervation and co-aggregation of alpha-synuclein and tau","volume":"13","author":"Gracia","year":"2022","journal-title":"Nat. Commun."},{"key":"10.1016\/j.celrep.2025.115761_bib53","doi-asserted-by":"crossref","first-page":"1154","DOI":"10.1038\/s41467-022-28797-5","article-title":"Spatiotemporal modulations in heterotypic condensates of prion and \u03b1-synuclein control phase transitions and amyloid conversion","volume":"13","author":"Agarwal","year":"2022","journal-title":"Nat. Commun."},{"key":"10.1016\/j.celrep.2025.115761_bib54","doi-asserted-by":"crossref","DOI":"10.1016\/j.bbapap.2023.140950","article-title":"Heterotypic liquid-liquid phase separation of tau and \u03b1-synuclein: Implications for overlapping neuropathologies","volume":"1871","author":"Foressi","year":"2023","journal-title":"Biochim. Biophys. Acta. Proteins Proteom."},{"key":"10.1016\/j.celrep.2025.115761_bib55","doi-asserted-by":"crossref","DOI":"10.1016\/j.bbapap.2022.140885","article-title":"Modulation of \u03b1-synuclein phase separation by biomolecules","volume":"1871","author":"Rodr\u00edguez","year":"2023","journal-title":"Biochim. Biophys. Acta. Proteins Proteom."},{"key":"10.1016\/j.celrep.2025.115761_bib56","doi-asserted-by":"crossref","DOI":"10.1016\/j.jmb.2021.166961","article-title":"Synapsin Condensates Recruit alpha-Synuclein","volume":"433","author":"Hoffmann","year":"2021","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.celrep.2025.115761_bib57","doi-asserted-by":"crossref","first-page":"1287","DOI":"10.1038\/s41556-024-01456-1","article-title":"VAMP2 chaperones \u03b1-synuclein in synaptic vesicle co-condensates","volume":"26","author":"Wang","year":"2024","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.celrep.2025.115761_bib58","doi-asserted-by":"crossref","first-page":"1296","DOI":"10.1038\/s41556-024-01451-6","article-title":"VAMP2 regulates phase separation of \u03b1-synuclein","volume":"26","author":"Agarwal","year":"2024","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.celrep.2025.115761_bib59","doi-asserted-by":"crossref","first-page":"8748","DOI":"10.1038\/s41467-024-53086-8","article-title":"\u03b2-synuclein regulates the phase transitions and amyloid conversion of \u03b1-synuclein","volume":"15","author":"Li","year":"2024","journal-title":"Nat. Commun."},{"key":"10.1016\/j.celrep.2025.115761_bib60","doi-asserted-by":"crossref","first-page":"3676","DOI":"10.1021\/acs.biochem.1c00434","article-title":"Modulating \u03b1-Synuclein Liquid-Liquid Phase Separation","volume":"60","author":"Sawner","year":"2021","journal-title":"Biochemistry"},{"key":"10.1016\/j.celrep.2025.115761_bib61","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijbiomac.2024.137688","article-title":"Diverse effects of fluorescent labels on alpha-synuclein condensate formation during liquid-liquid phase separation","volume":"283","author":"Ziaunys","year":"2024","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.celrep.2025.115761_bib62","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1016\/j.cell.2016.11.054","article-title":"Spatiotemporal Control of Intracellular Phase Transitions Using Light-Activated optoDroplets","volume":"168","author":"Shin","year":"2017","journal-title":"Cell"},{"key":"10.1016\/j.celrep.2025.115761_bib63","doi-asserted-by":"crossref","DOI":"10.1083\/jcb.202311191","article-title":"Synaptotagmin-1 undergoes phase separation to regulate its calcium-sensitive oligomerization","volume":"223","author":"Zhu","year":"2024","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.celrep.2025.115761_bib64","doi-asserted-by":"crossref","DOI":"10.1083\/jcb.202006054","article-title":"The proline-rich domain promotes Tau liquid-liquid phase separation in cells","volume":"219","author":"Zhang","year":"2020","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.celrep.2025.115761_bib65","doi-asserted-by":"crossref","DOI":"10.1002\/cbic.202200216","article-title":"Myricetin Inhibits \u03b1-Synuclein Amyloid Aggregation by Delaying the Liquid-to-Solid Phase Transition","volume":"23","author":"Xu","year":"2022","journal-title":"Chembiochem"},{"key":"10.1016\/j.celrep.2025.115761_bib66","doi-asserted-by":"crossref","first-page":"11054","DOI":"10.1074\/jbc.AC119.009198","article-title":"Liquid-liquid phase separation of tau protein: The crucial role of electrostatic interactions","volume":"294","author":"Boyko","year":"2019","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.celrep.2025.115761_bib67","doi-asserted-by":"crossref","first-page":"971","DOI":"10.1016\/j.molcel.2018.12.007","article-title":"RIM and RIM-BP Form Presynaptic Active-Zone-like Condensates via Phase Separation","volume":"73","author":"Wu","year":"2019","journal-title":"Mol. Cell"},{"key":"10.1016\/j.celrep.2025.115761_bib68","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1111\/jnc.15181","article-title":"Disorders of synaptic vesicle fusion machinery","volume":"157","author":"Melland","year":"2021","journal-title":"J. Neurochem."},{"key":"10.1016\/j.celrep.2025.115761_bib69","doi-asserted-by":"crossref","first-page":"1388","DOI":"10.1002\/1873-3468.14361","article-title":"alpha-Synuclein phase separation and amyloid aggregation are modulated by C-terminal truncations","volume":"596","author":"Huang","year":"2022","journal-title":"FEBS Lett."},{"key":"10.1016\/j.celrep.2025.115761_bib70","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.celrep.2025.115761_bib71","article-title":"Application of a C. elegans dopamine neuron degeneration assay for the validation of potential Parkinson\u2019s disease genes","volume":"17","author":"Berkowitz","year":"2008","journal-title":"J. Vis. Exp."},{"key":"10.1016\/j.celrep.2025.115761_bib72","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1038\/s41467-020-20269-y","article-title":"Steroid hormones sulfatase inactivation extends lifespan and ameliorates age-related diseases","volume":"12","author":"P\u00e9rez-Jim\u00e9nez","year":"2021","journal-title":"Nat. Commun."},{"key":"10.1016\/j.celrep.2025.115761_bib73","doi-asserted-by":"crossref","first-page":"458","DOI":"10.1038\/nature23284","article-title":"Cysteine protease cathepsin B mediates radiation-induced bystander effects","volume":"547","author":"Peng","year":"2017","journal-title":"Nature"},{"key":"10.1016\/j.celrep.2025.115761_bib74","doi-asserted-by":"crossref","first-page":"3959","DOI":"10.1002\/j.1460-2075.1991.tb04966.x","article-title":"Efficient gene transfer in C.elegans: extrachromosomal maintenance and integration of transforming sequences","volume":"10","author":"Mello","year":"1991","journal-title":"EMBO J."},{"key":"10.1016\/j.celrep.2025.115761_bib75","doi-asserted-by":"crossref","first-page":"1862","DOI":"10.1111\/j.1742-4658.2007.05733.x","article-title":"Dynamics of alpha-synuclein aggregation and inhibition of pore-like oligomer development by beta-synuclein","volume":"274","author":"Tsigelny","year":"2007","journal-title":"FEBS J."},{"key":"10.1016\/j.celrep.2025.115761_bib76","doi-asserted-by":"crossref","first-page":"708","DOI":"10.1016\/j.jmb.2007.07.009","article-title":"Structural characterization of the intrinsically unfolded protein beta-synuclein, a natural negative regulator of alpha-synuclein aggregation","volume":"372","author":"Bertoncini","year":"2007","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.celrep.2025.115761_bib77","doi-asserted-by":"crossref","first-page":"9096","DOI":"10.1021\/bi048778a","article-title":"Forcing nonamyloidogenic beta-synuclein to fibrillate","volume":"44","author":"Yamin","year":"2005","journal-title":"Biochemistry"},{"key":"10.1016\/j.celrep.2025.115761_bib78","doi-asserted-by":"crossref","first-page":"33254","DOI":"10.1073\/pnas.2007670117","article-title":"Widespread occurrence of the droplet state of proteins in the human proteome","volume":"117","author":"Hardenberg","year":"2020","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.celrep.2025.115761_bib79","doi-asserted-by":"crossref","first-page":"2836","DOI":"10.1021\/acschemneuro.0c00405","article-title":"Effect of Disease-Associated P123H and V70M Mutations on \u03b2-Synuclein Fibrillation","volume":"11","author":"Sharma","year":"2020","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.celrep.2025.115761_bib80","doi-asserted-by":"crossref","DOI":"10.3390\/ijms19020334","article-title":"Unveiling a Selective Mechanism for the Inhibition of \u03b1-Synuclein Aggregation by \u03b2-Synuclein","volume":"19","author":"Leitao","year":"2018","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.celrep.2025.115761_bib81","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.57457","article-title":"Therapeutic genetic variation revealed in diverse Hsp104 homologs","volume":"9","author":"March","year":"2020","journal-title":"Elife"},{"key":"10.1016\/j.celrep.2025.115761_bib82","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1007\/s00018-023-04728-5","article-title":"ORP9 and ORP10 form a heterocomplex to transfer phosphatidylinositol 4-phosphate at ER-TGN contact sites","volume":"80","author":"He","year":"2023","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.celrep.2025.115761_bib83","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1111\/bph.13655","article-title":"Celastrol prevents cadmium-induced neuronal cell death by blocking reactive oxygen species-mediated mammalian target of rapamycin pathway","volume":"174","author":"Zhang","year":"2017","journal-title":"Br. J. Pharmacol."},{"key":"10.1016\/j.celrep.2025.115761_bib84","first-page":"1","article-title":"Maintenance of C. elegans","author":"Stiernagle","year":"2006","journal-title":"WormBook"},{"key":"10.1016\/j.celrep.2025.115761_bib85","doi-asserted-by":"crossref","first-page":"12873","DOI":"10.1021\/jacs.5b08306","article-title":"Reconstituting Intracellular Vesicle Fusion Reactions: The Essential Role of Macromolecular Crowding","volume":"137","author":"Yu","year":"2015","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.celrep.2025.115761_bib86","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2021.100729","article-title":"Calcium-dependent and -independent lipid transfer mediated by tricalbins in yeast","volume":"296","author":"Qian","year":"2021","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.celrep.2025.115761_bib87","doi-asserted-by":"crossref","DOI":"10.1016\/j.celrep.2020.108611","article-title":"SNARE Zippering Is Suppressed by a Conformational Constraint that Is Removed by v-SNARE Splitting","volume":"34","author":"Liu","year":"2021","journal-title":"Cell Rep."},{"key":"10.1016\/j.celrep.2025.115761_bib88","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.1802645115","article-title":"SNARE zippering requires activation by SNARE-like peptides in Sec1\/Munc18 proteins","volume":"115","author":"Yu","year":"2018","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.celrep.2025.115761_bib89","doi-asserted-by":"crossref","first-page":"220","DOI":"10.1016\/j.ymeth.2010.12.036","article-title":"Caenorhabditis elegans as a model system for identifying effectors of \u03b1-synuclein misfolding and dopaminergic cell death associated with Parkinson's disease","volume":"53","author":"Harrington","year":"2011","journal-title":"Methods"},{"key":"10.1016\/j.celrep.2025.115761_bib90","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1016\/j.cmet.2014.04.017","article-title":"The glycolytic enzyme, GPI, is a functionally conserved modifier of dopaminergic neurodegeneration in Parkinson's models","volume":"20","author":"Knight","year":"2014","journal-title":"Cell Metab."}],"container-title":["Cell Reports"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2211124725005327?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2211124725005327?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,5,15]],"date-time":"2026-05-15T11:08:58Z","timestamp":1778843338000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S2211124725005327"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,6]]},"references-count":90,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2025,6]]}},"alternative-id":["S2211124725005327"],"URL":"https:\/\/doi.org\/10.1016\/j.celrep.2025.115761","relation":{},"ISSN":["2211-1247"],"issn-type":[{"value":"2211-1247","type":"print"}],"subject":[],"published":{"date-parts":[[2025,6]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"\u03b2-synuclein blocks \u03b1-synuclein condensate fusion to disrupt the maturation of phase separation","name":"articletitle","label":"Article Title"},{"value":"Cell Reports","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.celrep.2025.115761","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 Inc.","name":"copyright","label":"Copyright"}],"article-number":"115761"}}