{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,13]],"date-time":"2026-01-13T15:49:28Z","timestamp":1768319368616,"version":"3.49.0"},"reference-count":80,"publisher":"Oxford University Press (OUP)","issue":"1","license":[{"start":{"date-parts":[[2023,9,5]],"date-time":"2023-09-05T00:00:00Z","timestamp":1693872000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/pages\/standard-publication-reuse-rights"}],"funder":[{"DOI":"10.13039\/501100001659","name":"German Research Foundation","doi-asserted-by":"publisher","award":["TA 167\/6-3"],"award-info":[{"award-number":["TA 167\/6-3"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"German Research Foundation","doi-asserted-by":"publisher","award":["2033\u2014390677874"],"award-info":[{"award-number":["2033\u2014390677874"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100030848","name":"State Government of North Rhine-Westphalia","doi-asserted-by":"crossref","award":["INST 213\/840-1 FUGG"],"award-info":[{"award-number":["INST 213\/840-1 FUGG"]}],"id":[{"id":"10.13039\/100030848","id-type":"DOI","asserted-by":"crossref"}]},{"name":"Italian"},{"DOI":"10.13039\/100013013","name":"Target ALS","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100013013","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2024,1,4]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>A common pathological denominator of various neurodegenerative diseases is the accumulation of protein aggregates. Neurotoxic effects are caused by a loss of the physiological activity of the aggregating protein and\/or a gain of toxic function of the misfolded protein conformers. In transmissible spongiform encephalopathies or prion diseases, neurodegeneration is caused by aberrantly folded isoforms of the prion protein (PrP). However, it is poorly understood how pathogenic PrP conformers interfere with neuronal viability. Employing in vitro approaches, cell culture, animal models and patients\u2019 brain samples, we show that misfolded PrP can induce aggregation and inactivation of TAR DNA-binding protein-43 (TDP-43).<\/jats:p>\n               <jats:p>Purified PrP aggregates interact with TDP-43 in vitro and in cells and induce the conversion of soluble TDP-43 into non-dynamic protein assemblies. Similarly, mislocalized PrP conformers in the cytosol bind to and sequester TDP-43 in cytosolic aggregates. As a consequence, TDP-43-dependent splicing activity in the nucleus is significantly decreased, leading to altered protein expression in cells with cytosolic PrP aggregates. Finally, we present evidence for cytosolic TDP-43 aggregates in neurons of transgenic flies expressing mammalian PrP and Creutzfeldt\u2013Jakob disease patients.<\/jats:p>\n               <jats:p>Our study identified a novel mechanism of how aberrant PrP conformers impair physiological pathways by cross-seeding.<\/jats:p>","DOI":"10.1093\/brain\/awad289","type":"journal-article","created":{"date-parts":[[2023,9,3]],"date-time":"2023-09-03T17:36:22Z","timestamp":1693762582000},"page":"240-254","source":"Crossref","is-referenced-by-count":15,"title":["Cross-seeding by prion protein inactivates TDP-43"],"prefix":"10.1093","volume":"147","author":[{"given":"Stella A","family":"Polido","sequence":"first","affiliation":[{"name":"Department of Biochemistry of Neurodegenerative Diseases, Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum , 44801 Bochum , Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Cristiana","family":"Stuani","sequence":"additional","affiliation":[{"name":"International Centre for Genetic Engineering and Biotechnology (ICGEB) , 34149 Trieste , Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Aaron","family":"Voigt","sequence":"additional","affiliation":[{"name":"Department of Neurology, Medical Faculty, University Hospital, RWTH Aachen University , 52074 Aachen , Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Papiya","family":"Banik","sequence":"additional","affiliation":[{"name":"Department of Biochemistry of Neurodegenerative Diseases, Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum , 44801 Bochum , Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Janine","family":"Kamps","sequence":"additional","affiliation":[{"name":"Department of Biochemistry of Neurodegenerative Diseases, Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum , 44801 Bochum , Germany"},{"name":"Cluster of Excellence RESOLV, Ruhr University Bochum , 44801 Bochum , Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Verian","family":"Bader","sequence":"additional","affiliation":[{"name":"Department of Biochemistry of Neurodegenerative Diseases, Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum , 44801 Bochum , Germany"},{"name":"Department of Molecular Cell Biology, Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum , 44801 Bochum , Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Prerna","family":"Grover","sequence":"additional","affiliation":[{"name":"Department of Biochemistry of Neurodegenerative Diseases, Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum , 44801 Bochum , Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Laura J","family":"Krause","sequence":"additional","affiliation":[{"name":"Cluster of Excellence RESOLV, Ruhr University Bochum , 44801 Bochum , Germany"},{"name":"Department of Molecular Cell Biology, Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum , 44801 Bochum , Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Inga","family":"Zerr","sequence":"additional","affiliation":[{"name":"Department of Neurology, University Medical Center G\u00f6ttingen , 37075 G\u00f6ttingen , Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jakob","family":"Matschke","sequence":"additional","affiliation":[{"name":"Institute of Neuropathology, University Medical Center Hamburg-Eppendorf , 20251 Hamburg , Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Markus","family":"Glatzel","sequence":"additional","affiliation":[{"name":"Institute of Neuropathology, University Medical Center Hamburg-Eppendorf , 20251 Hamburg , Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Konstanze F","family":"Winklhofer","sequence":"additional","affiliation":[{"name":"Cluster of Excellence RESOLV, Ruhr University Bochum , 44801 Bochum , Germany"},{"name":"Department of Molecular Cell Biology, Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum , 44801 Bochum , Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Emanuele","family":"Buratti","sequence":"additional","affiliation":[{"name":"International Centre for Genetic Engineering and Biotechnology (ICGEB) , 34149 Trieste , Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5017-5528","authenticated-orcid":false,"given":"J\u00f6rg","family":"Tatzelt","sequence":"additional","affiliation":[{"name":"Department of Biochemistry of Neurodegenerative Diseases, Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum , 44801 Bochum , Germany"},{"name":"Cluster of Excellence RESOLV, Ruhr University Bochum , 44801 Bochum , Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2023,9,5]]},"reference":[{"key":"2024010419094884200_awad289-B1","doi-asserted-by":"crossref","first-page":"13363","DOI":"10.1073\/pnas.95.23.13363","article-title":"Prions","volume":"95","author":"Prusiner","year":"1998","journal-title":"Proc Natl Acad Sci USA"},{"key":"2024010419094884200_awad289-B2","doi-asserted-by":"crossref","first-page":"1339","DOI":"10.1016\/S0896-6273(00)80653-4","article-title":"Neurological illness in transgenic mice expressing a prion protein with an insertional mutation","volume":"21","author":"Chiesa","year":"1998","journal-title":"Neuron"},{"key":"2024010419094884200_awad289-B3","doi-asserted-by":"crossref","first-page":"827","DOI":"10.1126\/science.279.5352.827","article-title":"A transmembrane form of the prion protein in neurodegenerative 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