{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,3]],"date-time":"2026-09-03T08:16:48Z","timestamp":1788423408688,"version":"build-2803163510"},"reference-count":46,"publisher":"Portland Press Ltd.","issue":"9","license":[{"start":{"date-parts":[[2026,8,21]],"date-time":"2026-08-21T00:00:00Z","timestamp":1787270400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000268","name":"UKRI | Biotechnology and Biological Sciences Research Council","doi-asserted-by":"publisher","award":["BB\/S003657\/1"],"award-info":[{"award-number":["BB\/S003657\/1"]}],"id":[{"id":"10.13039\/501100000268","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2026,9,16]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Tau self-assembly and intracellular deposition are associated with a group of neurodegenerative diseases called tauopathies, which include Alzheimer\u2019s disease (AD) and Pick\u2019s disease. Here, we measured the proteome response in human neuronal cells (differentiated SH-SY5Y) following the addition of a spontaneously amyloidogenic region of tau known as dGAE (tau297\u2013391), which forms AD-like paired helical filaments in vitro, and proteomic analysis showed increased endogenous tau expression. Further interactome analysis uncovered increased association between tau and proteins associated with nuclear chromatin, the nucleolus, and the spliceosome, as well as the thiol-peroxidase, PRDX6, alongside an increase in reactive oxygen species. The present work highlights a method to identify proteome pathways that may play an important role in the development of tau pathology and reveals an oxidative stress response to dGAE.<\/jats:p>","DOI":"10.1042\/bsr20260349","type":"journal-article","created":{"date-parts":[[2026,8,21]],"date-time":"2026-08-21T12:26:01Z","timestamp":1787315161000},"update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["A proteomic analysis of the PHF-forming tau fragment (tau297\u2013391) following uptake into differentiated human neuronal SHSY5Y cells"],"prefix":"10.1042","volume":"46","author":[{"given":"Alice","family":"Copsey","sequence":"first","affiliation":[{"name":"1Sussex Neuroscience, School of Life Sciences, University of Sussex, Falmer, East Sussex, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sebastian\u00a0S.","family":"Oakley","sequence":"additional","affiliation":[{"name":"1Sussex Neuroscience, School of Life Sciences, University of Sussex, Falmer, East Sussex, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mahmoud\u00a0B.","family":"Maina","sequence":"additional","affiliation":[{"name":"1Sussex Neuroscience, School of Life Sciences, University of Sussex, Falmer, East Sussex, U.K."},{"name":"2Biomedical Science Research and Training Centre, Yobe State University, Damaturu, Yobe State, Nigeria"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robert","family":"Parker","sequence":"additional","affiliation":[{"name":"3Centre for Immuno-Oncology, Nuffield Department of Medicine, University of Oxford, Oxford OX3 7DQ, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Karen\u00a0E.","family":"Marshall","sequence":"additional","affiliation":[{"name":"1Sussex Neuroscience, School of Life Sciences, University of Sussex, Falmer, East Sussex, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Charles\u00a0R.","family":"Harrington","sequence":"additional","affiliation":[{"name":"4Institute of Medicine, Medical Sciences and Nutrition, University of Aberdeen, Aberdeen, U.K."},{"name":"5TauRx Therapeutics Ltd, Aberdeen, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John\u00a0M.D.","family":"Storey","sequence":"additional","affiliation":[{"name":"5TauRx Therapeutics Ltd, Aberdeen, U.K."},{"name":"6Department of Chemistry, University of Aberdeen, Aberdeen, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Claude\u00a0M.","family":"Wischik","sequence":"additional","affiliation":[{"name":"4Institute of Medicine, Medical Sciences and Nutrition, University of Aberdeen, Aberdeen, U.K."},{"name":"5TauRx Therapeutics Ltd, Aberdeen, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9335-7751","authenticated-orcid":false,"given":"Louise\u00a0C.","family":"Serpell","sequence":"additional","affiliation":[{"name":"1Sussex Neuroscience, School of Life Sciences, University of Sussex, Falmer, East Sussex, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2026,9,3]]},"reference":[{"key":"2026090304064288400_B1","doi-asserted-by":"publisher","first-page":"519","DOI":"10.1016\/0896-6273(89)90210-9","article-title":"Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer\u2019s disease","volume":"3","author":"Goedert","year":"1989","journal-title":"Neuron"},{"key":"2026090304064288400_B2","doi-asserted-by":"publisher","first-page":"127","DOI":"10.3109\/07853898909149199","article-title":"The repeat region of microtubule-associated protein tau forms part of the core of the paired helical filament of Alzheimer's disease","volume":"21","author":"Crowther","year":"1989","journal-title":"Ann. 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