{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,4]],"date-time":"2026-05-04T22:13:39Z","timestamp":1777932819237,"version":"3.51.4"},"reference-count":11,"publisher":"SAGE Publications","issue":"2-3","license":[{"start":{"date-parts":[[2010,4,1]],"date-time":"2010-04-01T00:00:00Z","timestamp":1270080000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.sagepub.com\/page\/policies\/text-and-data-mining-license"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Rejuvenation Research"],"published-print":{"date-parts":[[2010,4]]},"abstract":"<jats:p>\n                    Protein aggregation occurs in many age-related neurodegenerative diseases, where it can lead to deposits of naturally occurring proteins in the brain. In case of Creutzfeldt\u2013Jakob disease (CJD), these deposits consist of prion protein (PrP). CJD has three etiologies: spontaneous, genetic, or caused by infection. A polymorphism within the PrP gene is associated with susceptibility of infection. The main event in prion diseases is the conversion of PrP from its naturally occurring isoform to its disease-associated isoform. Here, we present the adaption of a previously reported\n                    <jats:italic toggle=\"yes\">in vitro<\/jats:italic>\n                    conversion system based on hamster recombinant PrP to analyze amyloid fibril formation of human recombinant PrP. We further compare the aggregation characteristics of the human PrP according to the polymorphism variants M129 and V129.\n                  <\/jats:p>","DOI":"10.1089\/rej.2009.0932","type":"journal-article","created":{"date-parts":[[2009,12,17]],"date-time":"2009-12-17T13:11:51Z","timestamp":1261055511000},"page":"214-216","source":"Crossref","is-referenced-by-count":4,"title":["Amyloid Formation: Age-Related Mechanism in Creutzfeldt\u2013Jakob Disease?"],"prefix":"10.1177","volume":"13","author":[{"given":"L.","family":"Luers","sequence":"first","affiliation":[{"name":"Heinrich-Heine Universitaet Duesseldorf","place":["Germany"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"G.","family":"Panza","sequence":"additional","affiliation":[{"name":"Heinrich-Heine Universitaet Duesseldorf","place":["Germany"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"F.","family":"Henke","sequence":"additional","affiliation":[{"name":"Institut fuer Strukturbiolologie und Biophysik (ISB-3)","place":["Germany"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"T.","family":"Agyenim","sequence":"additional","affiliation":[{"name":"Heinrich-Heine Universitaet Duesseldorf","place":["Germany"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"J.","family":"Weiss","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr klinische Biochemie und Pathobiochemie","place":["Germany"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"D.","family":"Willbold","sequence":"additional","affiliation":[{"name":"Heinrich-Heine Universitaet Duesseldorf","place":["Germany"]},{"name":"Institut fuer Strukturbiolologie und Biophysik (ISB-3)","place":["Germany"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"E.","family":"Birkmann","sequence":"additional","affiliation":[{"name":"Heinrich-Heine Universitaet Duesseldorf","place":["Germany"]},{"name":"Institut fuer Strukturbiolologie und Biophysik (ISB-3)","place":["Germany"]}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"179","published-online":{"date-parts":[[2010,4]]},"reference":[{"key":"e_1_3_3_2_2","doi-asserted-by":"crossref","first-page":"849","DOI":"10.1016\/S0272-2712(02)00024-0","article-title":"Variant Creutzfeldt-Jakob disease and bovine spongiform encephalopathy","volume":"22","author":"Belay ED","year":"2002","unstructured":"Belay ED, , Schonberger LB. Variant Creutzfeldt-Jakob disease and bovine spongiform encephalopathy. Clin Lab Med, 2002; 22:849\u2013862v\u2013vi.","journal-title":"Clin Lab Med"},{"key":"e_1_3_3_3_2","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1136\/bmj.315.7105.389","article-title":"Sporadic Creutzfeldt-Jakob disease in the United Kingdom: Analysis of epidemiological surveillance data for 1970\u201396","volume":"315","author":"Cousens SN","year":"1997","unstructured":"Cousens SN, , Zeidler M, , Esmonde TF, , De Silva R, , Wilesmith JW, , Smith PG, , Will RG. Sporadic Creutzfeldt-Jakob disease in the United Kingdom: Analysis of epidemiological surveillance data for 1970\u201396. BMJ, 1997; 315:389\u2013395.","journal-title":"BMJ"},{"key":"e_1_3_3_4_2","first-page":"121","article-title":"Clinical features of variant Creutzfeldt-Jakob disease","volume":"284","author":"Will RG","year":"2004","unstructured":"Will RG, , Ward HJ. Clinical features of variant Creutzfeldt-Jakob disease. Curr Top Microbiol Immunol, 2004; 284:121\u2013132.","journal-title":"Curr Top Microbiol Immunol"},{"key":"e_1_3_3_5_2","first-page":"85","article-title":"Review: Pathology of variant Creutzfeldt-Jakob disease","volume":"42","author":"Peden AH","year":"2004","unstructured":"Peden AH, , Ironside JW. Review: Pathology of variant Creutzfeldt-Jakob disease. Folia Neuropathol, 2004; 42,Suppl A:85\u201391.","journal-title":"Folia Neuropathol"},{"key":"e_1_3_3_6_2","doi-asserted-by":"publisher","DOI":"10.1038\/352340a0"},{"key":"e_1_3_3_7_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.95.23.13363"},{"key":"e_1_3_3_8_2","doi-asserted-by":"crossref","first-page":"2409","DOI":"10.1073\/pnas.0712036105","article-title":"Mechanisms of prion protein assembly into amyloid","volume":"105","author":"Stohr J","year":"2008","unstructured":"Stohr J, , Weinmann N, , Wille H, , Kaimann T, , Nagel-Steger L, , Birkmann E, , Panza G, , Prusiner SB, , Eigen M, , Riesner D. Mechanisms of prion protein assembly into amyloid. Proc Natl Acad Sci USA, 2008; 105:2409\u20132414.","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_3_9_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbrc.2008.06.059"},{"key":"e_1_3_3_10_2","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1016\/j.jmb.2004.09.071","article-title":"The structural transition of the prion protein into its pathogenic conformation is induced by unmasking hydrophobic sites","volume":"344","author":"Leffers KW","year":"2004","unstructured":"Leffers KW, , Schell J, , Jansen K, , Lucassen R, , Kaimann T, , Nagel-Steger L, , Tatzelt J, , Riesner D. The structural transition of the prion protein into its pathogenic conformation is induced by unmasking hydrophobic sites. J Mol Biol, 2004; 344:839\u2013853.","journal-title":"J Mol Biol"},{"key":"e_1_3_3_11_2","doi-asserted-by":"crossref","first-page":"67","DOI":"10.4161\/pri.2.2.7060","article-title":"Prion infection: Seeded fibrillization or more?","volume":"2","author":"Birkmann E","year":"2008","unstructured":"Birkmann E, , Riesner D. Prion infection: Seeded fibrillization or more? Prion, 2008; 2:67\u201372.","journal-title":"Prion"},{"key":"e_1_3_3_12_2","doi-asserted-by":"crossref","first-page":"2589","DOI":"10.1016\/j.febslet.2005.03.075","article-title":"The presence of valine at residue 129 in human prion protein accelerates amyloid formation","volume":"579","author":"Baskakov I","year":"2005","unstructured":"Baskakov I, , Disterer P, , Breydo L, , Shaw M, , Gill A, , James W, , Tahiri-Alaoui A. The presence of valine at residue 129 in human prion protein accelerates amyloid formation. FEBS Lett, 2005; 579:2589\u20132596.","journal-title":"FEBS Lett"}],"container-title":["Rejuvenation Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.sagepub.com\/doi\/full-xml\/10.1089\/rej.2009.0932","content-type":"application\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/journals.sagepub.com\/doi\/pdf\/10.1089\/rej.2009.0932","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/journals.sagepub.com\/doi\/pdf\/10.1089\/rej.2009.0932","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,5,2]],"date-time":"2026-05-02T01:29:59Z","timestamp":1777685399000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.sagepub.com\/doi\/full\/10.1089\/rej.2009.0932"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2010,4]]},"references-count":11,"journal-issue":{"issue":"2-3","published-print":{"date-parts":[[2010,4]]}},"alternative-id":["10.1089\/rej.2009.0932"],"URL":"https:\/\/doi.org\/10.1089\/rej.2009.0932","relation":{},"ISSN":["1549-1684","1557-8577"],"issn-type":[{"value":"1549-1684","type":"print"},{"value":"1557-8577","type":"electronic"}],"subject":[],"published":{"date-parts":[[2010,4]]}}}