{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,15]],"date-time":"2026-04-15T06:55:29Z","timestamp":1776236129957,"version":"3.50.1"},"reference-count":15,"publisher":"Wiley","issue":"8","license":[{"start":{"date-parts":[[2025,12,30]],"date-time":"2025-12-30T00:00:00Z","timestamp":1767052800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"},{"start":{"date-parts":[[2025,12,30]],"date-time":"2025-12-30T00:00:00Z","timestamp":1767052800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FEBS Journal"],"published-print":{"date-parts":[[2026,4]]},"abstract":"<jats:p>\n                    Protein aggregation and transmission are hallmarks of neurodegenerative diseases. Praja1 E3 ubiquitin ligase has been shown to suppress the aggregation of causative proteins in amyotrophic lateral sclerosis, frontotemporal lobar degeneration, Parkinson's disease, Huntington's disease, and spinocerebellar degeneration, which include transactivation response DNA\u2010binding protein of 43\u2009kDa, fused in sarcoma, superoxide dismutase 1, \u03b1\u2010synuclein, huntingtin, and ataxin\u20103. Aoki\n                    <jats:italic>et\u00a0al.<\/jats:italic>\n                    demonstrated that Praja1 ubiquitinates and degrades tau, a key molecule in tauopathies such as Alzheimer's disease, Pick's disease, progressive supranuclear palsy, and corticobasal syndrome, furthering our understanding of the role of Praja1 in neurodegenerative diseases and potential therapeutic approaches.\n                  <\/jats:p>","DOI":"10.1111\/febs.70383","type":"journal-article","created":{"date-parts":[[2025,12,30]],"date-time":"2025-12-30T08:40:33Z","timestamp":1767084033000},"page":"2208-2211","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Praja1\n                    <scp>E3<\/scp>\n                    ubiquitin ligase and the role it plays in neurodegeneration"],"prefix":"10.1111","volume":"293","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-0245-3834","authenticated-orcid":false,"given":"Kazuhiko","family":"Watabe","sequence":"first","affiliation":[{"name":"Immunity Control Unit, Research Center for Infectious Diseases and Medical Sciences Tokyo Metropolitan Institute of Medical Science (TMIMS)  Japan"},{"name":"Department of Medical Cell Biology Aichi Medical University School of Medicine  Japan"},{"name":"Yomiuri Land Keiyu Hospital  Tokyo Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2025,12,30]]},"reference":[{"key":"e_1_2_6_2_1","doi-asserted-by":"publisher","DOI":"10.1038\/s41582-020-0333-7"},{"key":"e_1_2_6_3_1","doi-asserted-by":"publisher","DOI":"10.3390\/ijms26030966"},{"key":"e_1_2_6_4_1","doi-asserted-by":"publisher","DOI":"10.1038\/nrm.2017.73"},{"key":"e_1_2_6_5_1","doi-asserted-by":"publisher","DOI":"10.1111\/neup.12694"},{"key":"e_1_2_6_6_1","doi-asserted-by":"publisher","DOI":"10.3390\/ijms26072909"},{"key":"e_1_2_6_7_1","doi-asserted-by":"publisher","DOI":"10.1091\/mbc.E20-11-0747"},{"key":"e_1_2_6_8_1","doi-asserted-by":"publisher","DOI":"10.1111\/neup.12840"},{"key":"e_1_2_6_9_1","doi-asserted-by":"publisher","DOI":"10.1111\/febs.70303"},{"key":"e_1_2_6_10_1","doi-asserted-by":"publisher","DOI":"10.1038\/s41419-020-02953-5"},{"key":"e_1_2_6_11_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmb.2023.168026"},{"key":"e_1_2_6_12_1","doi-asserted-by":"publisher","DOI":"10.1186\/s13041-022-00958-z"},{"key":"e_1_2_6_13_1","first-page":"2015","article-title":"Phosphorylation\u2010driven aggregative proteins in neurodegenerative diseases: implications and therapeutics","volume":"5","author":"Espargar\u00f3 A","year":"2024","journal-title":"Neural Regen Res"},{"key":"e_1_2_6_14_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.molcel.2017.09.027"},{"key":"e_1_2_6_15_1","doi-asserted-by":"publisher","DOI":"10.1038\/s41418-020-00706-7"},{"key":"e_1_2_6_16_1","unstructured":"DoddRB(2005)Schematic diagram of the ubiquitination system. Wikimedia commons.https:\/\/commons.wikimedia.org\/wiki\/File:Ubiquitylation.svg"}],"container-title":["The FEBS Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/febs.onlinelibrary.wiley.com\/doi\/pdf\/10.1111\/febs.70383","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/febs.onlinelibrary.wiley.com\/doi\/full-xml\/10.1111\/febs.70383","content-type":"application\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/febs.onlinelibrary.wiley.com\/doi\/pdf\/10.1111\/febs.70383","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,4,15]],"date-time":"2026-04-15T05:53:42Z","timestamp":1776232422000},"score":1,"resource":{"primary":{"URL":"https:\/\/febs.onlinelibrary.wiley.com\/doi\/10.1111\/febs.70383"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,12,30]]},"references-count":15,"journal-issue":{"issue":"8","published-print":{"date-parts":[[2026,4]]}},"alternative-id":["10.1111\/febs.70383"],"URL":"https:\/\/doi.org\/10.1111\/febs.70383","archive":["Portico"],"relation":{},"ISSN":["1742-464X","1742-4658"],"issn-type":[{"value":"1742-464X","type":"print"},{"value":"1742-4658","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,12,30]]},"assertion":[{"value":"2025-11-13","order":0,"name":"received","label":"Received","group":{"name":"publication_history","label":"Publication History"}},{"value":"2025-12-19","order":2,"name":"accepted","label":"Accepted","group":{"name":"publication_history","label":"Publication History"}},{"value":"2025-12-30","order":3,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}