{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,29]],"date-time":"2026-05-29T21:11:17Z","timestamp":1780089077887,"version":"3.54.0"},"reference-count":41,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[2025,2,1]],"date-time":"2025-02-01T00:00:00Z","timestamp":1738368000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,2,1]],"date-time":"2025-02-01T00:00:00Z","timestamp":1738368000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,1,28]],"date-time":"2025-01-28T00:00:00Z","timestamp":1738022400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100019270","name":"Shimizu Foundation for Immunology and Neuroscience","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100019270","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["18K07371"],"award-info":[{"award-number":["18K07371"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["21K07299"],"award-info":[{"award-number":["21K07299"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["24K10514"],"award-info":[{"award-number":["24K10514"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["21K06412"],"award-info":[{"award-number":["21K06412"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["24K10494"],"award-info":[{"award-number":["24K10494"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100022577","name":"RIKEN Center for Biosystems Dynamics Research","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100022577","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["iScience"],"published-print":{"date-parts":[[2025,2]]},"DOI":"10.1016\/j.isci.2025.111935","type":"journal-article","created":{"date-parts":[[2025,1,31]],"date-time":"2025-01-31T12:25:36Z","timestamp":1738326336000},"page":"111935","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":1,"title":["SENP2-based N-terminal truncation of \u03b1-synuclein in Lewy pathology propagation"],"prefix":"10.1016","volume":"28","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-5511-3975","authenticated-orcid":false,"given":"Katsutoshi","family":"Taguchi","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9499-2914","authenticated-orcid":false,"given":"Yoshihisa","family":"Watanabe","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6143-9197","authenticated-orcid":false,"given":"Masaki","family":"Tanaka","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.isci.2025.111935_bib1","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":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.isci.2025.111935_bib2","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1097\/00019052-200108000-00001","article-title":"Alpha-synuclein and the Lewy body disorders","volume":"14","author":"Dickson","year":"2001","journal-title":"Curr. Opin. Neurol."},{"key":"10.1016\/j.isci.2025.111935_bib3","doi-asserted-by":"crossref","DOI":"10.1101\/cshperspect.a009399","article-title":"alpha-Synuclein in Parkinson's disease","volume":"2","author":"Stefanis","year":"2012","journal-title":"Cold Spring Harb. Perspect. Med."},{"key":"10.1016\/j.isci.2025.111935_bib4","first-page":"1","article-title":"Neuroanatomy and pathology of sporadic Parkinson's disease","volume":"201","author":"Braak","year":"2009","journal-title":"Adv. Anat. Embryol. Cell Biol."},{"key":"10.1016\/j.isci.2025.111935_bib5","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.isci.2025.111935_bib6","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":"Nat. Med."},{"key":"10.1016\/j.isci.2025.111935_bib7","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1016\/B978-0-444-63945-5.00017-9","article-title":"Prion-like propagation of pathology in Parkinson disease","volume":"153","author":"Volpicelli-Daley","year":"2018","journal-title":"Handb. Clin. Neurol."},{"key":"10.1016\/j.isci.2025.111935_bib8","doi-asserted-by":"crossref","first-page":"949","DOI":"10.1126\/science.1227157","article-title":"Pathological alpha-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice","volume":"338","author":"Luk","year":"2012","journal-title":"Science"},{"key":"10.1016\/j.isci.2025.111935_bib9","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.isci.2025.111935_bib10","doi-asserted-by":"crossref","first-page":"1248","DOI":"10.1038\/s41593-019-0457-5","article-title":"Spread of alpha-synuclein pathology through the brain connectome is modulated by selective vulnerability and predicted by network analysis","volume":"22","author":"Henderson","year":"2019","journal-title":"Nat. Neurosci."},{"key":"10.1016\/j.isci.2025.111935_bib11","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1016\/j.neuron.2011.08.033","article-title":"Exogenous alpha-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.isci.2025.111935_bib12","doi-asserted-by":"crossref","DOI":"10.1016\/j.arr.2023.101978","article-title":"Truncation or proteolysis of alpha-synuclein in Parkinsonism","volume":"90","author":"Suthar","year":"2023","journal-title":"Ageing Res. Rev."},{"key":"10.1016\/j.isci.2025.111935_bib13","doi-asserted-by":"crossref","DOI":"10.1016\/j.bbr.2022.114204","article-title":"Targeting alpha-synuclein post-translational modifications in Parkinson's disease","volume":"439","author":"Canever","year":"2023","journal-title":"Behav. Brain Res."},{"key":"10.1016\/j.isci.2025.111935_bib14","doi-asserted-by":"crossref","first-page":"1254","DOI":"10.1124\/pharmrev.123.001111","article-title":"Posttranslational Modifications of alpha-Synuclein, Their Therapeutic Potential, and Crosstalk in Health and Neurodegenerative Diseases","volume":"76","author":"Hassanzadeh","year":"2024","journal-title":"Pharmacol. Rev."},{"key":"10.1016\/j.isci.2025.111935_bib15","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":"Nat. Cell Biol."},{"key":"10.1016\/j.isci.2025.111935_bib16","doi-asserted-by":"crossref","first-page":"13176","DOI":"10.1073\/pnas.1704351114","article-title":"SUMOylation and ubiquitination reciprocally regulate alpha-synuclein degradation and pathological aggregation","volume":"114","author":"Rott","year":"2017","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.isci.2025.111935_bib17","doi-asserted-by":"crossref","first-page":"167","DOI":"10.3389\/fnagi.2020.00167","article-title":"SUMOylation in alpha-Synuclein Homeostasis and Pathology","volume":"12","author":"Savyon","year":"2020","journal-title":"Front. Aging Neurosci."},{"key":"10.1016\/j.isci.2025.111935_bib18","doi-asserted-by":"crossref","DOI":"10.1002\/pro.4632","article-title":"SUMO1 hinders alpha-Synuclein fibrillation by inducing structural compaction","volume":"32","author":"Panigrahi","year":"2023","journal-title":"Protein Sci."},{"key":"10.1016\/j.isci.2025.111935_bib19","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1083\/jcb.201010117","article-title":"Sumoylation inhibits alpha-synuclein aggregation and toxicity","volume":"194","author":"Krumova","year":"2011","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1016\/j.isci.2025.111935_bib20","doi-asserted-by":"crossref","first-page":"13910","DOI":"10.1074\/jbc.RA118.001862","article-title":"The effect of truncation on prion-like properties of alpha-synuclein","volume":"293","author":"Terada","year":"2018","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.isci.2025.111935_bib21","doi-asserted-by":"crossref","first-page":"10224","DOI":"10.1074\/jbc.REV120.011743","article-title":"The emerging role of alpha-synuclein truncation in aggregation and disease","volume":"295","author":"Sorrentino","year":"2020","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.isci.2025.111935_bib22","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2023487118","article-title":"The N terminus of alpha-synuclein dictates fibril formation","volume":"118","author":"McGlinchey","year":"2021","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.isci.2025.111935_bib23","doi-asserted-by":"crossref","first-page":"19105","DOI":"10.1073\/pnas.0608970103","article-title":"Continuum of prion protein structures enciphers a multitude of prion isolate-specified phenotypes","volume":"103","author":"Legname","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.isci.2025.111935_bib24","doi-asserted-by":"crossref","first-page":"244","DOI":"10.1016\/j.nbd.2014.10.011","article-title":"Lysosomal enzyme cathepsin B enhances the aggregate forming activity of exogenous alpha-synuclein fibrils","volume":"73","author":"Tsujimura","year":"2015","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.isci.2025.111935_bib25","doi-asserted-by":"crossref","first-page":"836","DOI":"10.1046\/j.1471-4159.2003.01878.x","article-title":"Distinct cleavage patterns of normal and pathologic forms of alpha-synuclein by calpain I in\u00a0vitro","volume":"86","author":"Mishizen-Eberz","year":"2003","journal-title":"J.\u00a0Neurochem."},{"key":"10.1016\/j.isci.2025.111935_bib26","doi-asserted-by":"crossref","first-page":"1725","DOI":"10.2353\/ajpath.2007.061232","article-title":"Calpain-cleavage of alpha-synuclein: connecting proteolytic processing to disease-linked aggregation","volume":"170","author":"Dufty","year":"2007","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.isci.2025.111935_bib28","doi-asserted-by":"crossref","first-page":"726","DOI":"10.1016\/j.bbrc.2018.02.140","article-title":"Ubiquitin C-Terminal Hydrolase L1 regulates autophagy by inhibiting autophagosome formation through its deubiquitinating enzyme activity","volume":"497","author":"Yan","year":"2018","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.isci.2025.111935_bib27","doi-asserted-by":"crossref","first-page":"22670","DOI":"10.1074\/jbc.M501508200","article-title":"A precipitating role for truncated alpha-synuclein and the proteasome in alpha-synuclein aggregation: implications for pathogenesis of Parkinson disease","volume":"280","author":"Liu","year":"2005","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.isci.2025.111935_bib29","doi-asserted-by":"crossref","first-page":"1035","DOI":"10.1110\/ps.083450408","article-title":"Characterization of ubiquitin and ubiquitin-like-protein isopeptidase activities","volume":"17","author":"Nicholson","year":"2008","journal-title":"Protein Sci."},{"key":"10.1016\/j.isci.2025.111935_bib30","doi-asserted-by":"crossref","first-page":"3483","DOI":"10.1091\/mbc.e13-05-0230","article-title":"SENP1 and SENP2 affect spatial and temporal control of sumoylation in mitosis","volume":"24","author":"Cube\u00f1as-Potts","year":"2013","journal-title":"Mol Biol Cell"},{"key":"10.1016\/j.isci.2025.111935_bib31","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1007\/s00401-012-0964-x","article-title":"An antibody with high reactivity for disease-associated alpha-synuclein reveals extensive brain pathology","volume":"124","author":"Kovacs","year":"2012","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.isci.2025.111935_bib32","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/j.nbd.2015.04.009","article-title":"Generation and characterization of novel conformation-specific monoclonal antibodies for alpha-synuclein pathology","volume":"79","author":"Vaikath","year":"2015","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.isci.2025.111935_bib33","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1002\/iub.1244","article-title":"Wrestling with stress: roles of protein SUMOylation and deSUMOylation in cell stress response","volume":"66","author":"Guo","year":"2014","journal-title":"IUBMB Life"},{"key":"10.1016\/j.isci.2025.111935_bib34","doi-asserted-by":"crossref","first-page":"672","DOI":"10.1021\/bi020429y","article-title":"The N-terminal repeat domain of alpha-synuclein inhibits beta-sheet and amyloid fibril formation","volume":"42","author":"Kessler","year":"2003","journal-title":"Biochemistry"},{"key":"10.1016\/j.isci.2025.111935_bib35","doi-asserted-by":"crossref","first-page":"13322","DOI":"10.1021\/bi7014053","article-title":"Role of different regions of alpha-synuclein in the assembly of fibrils","volume":"46","author":"Qin","year":"2007","journal-title":"Biochemistry"},{"key":"10.1016\/j.isci.2025.111935_bib36","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":"Nat. Neurosci."},{"key":"10.1016\/j.isci.2025.111935_bib37","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1016\/S0896-6273(00)80886-7","article-title":"Mice lacking alpha-synuclein display functional deficits in the nigrostriatal dopamine system","volume":"25","author":"Abeliovich","year":"2000","journal-title":"Neuron"},{"key":"10.1016\/j.isci.2025.111935_bib38","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0089327","article-title":"Differential expression of alpha-synuclein in hippocampal neurons","volume":"9","author":"Taguchi","year":"2014","journal-title":"PLoS One"},{"key":"10.1016\/j.isci.2025.111935_bib39","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0052868","article-title":"p62\/SQSTM1-dependent autophagy of Lewy body-like alpha-synuclein inclusions","volume":"7","author":"Watanabe","year":"2012","journal-title":"PLoS One"},{"key":"10.1016\/j.isci.2025.111935_bib40","doi-asserted-by":"crossref","DOI":"10.1126\/science.aah3374","article-title":"Pathological alpha-synuclein transmission initiated by binding lymphocyte-activation gene 3","volume":"353","author":"Mao","year":"2016","journal-title":"Science"},{"key":"10.1016\/j.isci.2025.111935_bib41","doi-asserted-by":"crossref","first-page":"1236","DOI":"10.1002\/cne.23901","article-title":"Brain region-dependent differential expression of alpha-synuclein","volume":"524","author":"Taguchi","year":"2016","journal-title":"J.\u00a0Comp. Neurol."}],"container-title":["iScience"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2589004225001956?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2589004225001956?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,5,29]],"date-time":"2026-05-29T20:42:36Z","timestamp":1780087356000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S2589004225001956"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,2]]},"references-count":41,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2025,2]]}},"alternative-id":["S2589004225001956"],"URL":"https:\/\/doi.org\/10.1016\/j.isci.2025.111935","relation":{"has-preprint":[{"id-type":"doi","id":"10.1101\/2024.09.18.613608","asserted-by":"object"}]},"ISSN":["2589-0042"],"issn-type":[{"value":"2589-0042","type":"print"}],"subject":[],"published":{"date-parts":[[2025,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"SENP2-based N-terminal truncation of \u03b1-synuclein in Lewy pathology propagation","name":"articletitle","label":"Article Title"},{"value":"iScience","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.isci.2025.111935","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":"111935"}}