{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,18]],"date-time":"2026-09-18T02:22:38Z","timestamp":1789698158817,"version":"4.0.1"},"reference-count":142,"publisher":"Wiley","issue":"8","license":[{"start":{"date-parts":[[2023,10,19]],"date-time":"2023-10-19T00:00:00Z","timestamp":1697673600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["SFB1286 (B8)"],"award-info":[{"award-number":["SFB1286 (B8)"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["EXC 2067\/1\u2010390729940"],"award-info":[{"award-number":["EXC 2067\/1\u2010390729940"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003593","name":"Conselho Nacional de Desenvolvimento Cient\u00edfico e Tecnol\u00f3gico","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100003593","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Journal of Neurochemistry"],"published-print":{"date-parts":[[2024,8]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    The discovery of prions has challenged dogmas and has revolutionized our understanding of protein\u2010misfolding diseases. The concept of self\u2010propagation via protein conformational changes, originally discovered for the prion protein (PrP), also applies to other proteins that exhibit similar behavior, such as alpha\u2010synuclein (aSyn), a central player in Parkinson's disease and in other synucleinopathies. aSyn pathology appears to spread from one cell to another during disease progression, and involves the misfolding and aggregation of aSyn. How the transfer of aSyn between cells occurs is still being studied, but one important hypothesis involves receptor\u2010mediated transport. Interestingly, recent studies indicate that the cellular prion protein (PrP\n                    <jats:sup>C<\/jats:sup>\n                    ) may play a crucial role in this process. PrP\n                    <jats:sup>C<\/jats:sup>\n                    has been shown to act as a receptor\/sensor for protein aggregates in different neurodegenerative disorders, including Alzheimer's disease and amyotrophic lateral sclerosis. Here, we provide a comprehensive overview of the current state of knowledge regarding the interaction between aSyn and PrP\n                    <jats:sup>C<\/jats:sup>\n                    and discuss its role in synucleinopathies. We examine the properties of PrP and aSyn, including their structure, function, and aggregation. Additionally, we discuss the current understanding of PrP\n                    <jats:sup>C<\/jats:sup>\n                    's role as a receptor\/sensor for aSyn aggregates and identify remaining unanswered questions in this area of research. Ultimately, we posit that exploring the interaction between aSyn and PrP\n                    <jats:sup>C<\/jats:sup>\n                    may offer potential treatment options for synucleinopathies.\n                    <jats:boxed-text content-type=\"graphic\" position=\"anchor\">\n                      <jats:graphic xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" mimetype=\"image\/png\" position=\"anchor\" specific-use=\"enlarged-web-image\" xlink:href=\"graphic\/jnc15992-fig-0006-m.png\">\n                        <jats:alt-text>image<\/jats:alt-text>\n                      <\/jats:graphic>\n                    <\/jats:boxed-text>\n                  <\/jats:p>","DOI":"10.1111\/jnc.15992","type":"journal-article","created":{"date-parts":[[2023,10,19]],"date-time":"2023-10-19T10:55:52Z","timestamp":1697712952000},"page":"1625-1639","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":11,"title":["PrP meets alpha\u2010synuclein: Molecular mechanisms and implications for disease"],"prefix":"10.1111","volume":"168","author":[{"given":"Tuane C. 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G.","family":"Vieira","sequence":"first","affiliation":[{"name":"Institute of Medical Biochemistry Leopoldo de Meis and National Institute of Science and Technology for Structural Biology and Bioimaging Federal University of Rio de Janeiro  Rio de Janeiro Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Caroline A.","family":"Barros","sequence":"additional","affiliation":[{"name":"Institute of Medical Biochemistry Leopoldo de Meis and National Institute of Science and Technology for Structural Biology and Bioimaging Federal University of Rio de Janeiro  Rio de Janeiro Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Renato","family":"Domingues","sequence":"additional","affiliation":[{"name":"Department of Experimental Neurodegeneration, Center for Biostructural Imaging of Neurodegeneration University Medical Center G\u00f6ttingen  G\u00f6ttingen Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1679-1727","authenticated-orcid":false,"given":"Tiago Fleming","family":"Outeiro","sequence":"additional","affiliation":[{"name":"Department of Experimental Neurodegeneration, Center for Biostructural Imaging of Neurodegeneration University Medical Center G\u00f6ttingen  G\u00f6ttingen Germany"},{"name":"Max Planck Institute for Multidisciplinary Sciences  G\u00f6ttingen Germany"},{"name":"Faculty of Medical Sciences, Translational and Clinical Research Institute Newcastle University  Newcastle Upon Tyne UK"},{"name":"Scientific Employee with an Honorary Contract at Deutsches Zentrum f\u00fcr Neurodegenerative Erkrankungen (DZNE)  G\u00f6ttingen 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