{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,31]],"date-time":"2025-10-31T13:58:55Z","timestamp":1761919135290},"reference-count":44,"publisher":"Portland Press Ltd.","issue":"5","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2008,10,1]]},"abstract":"<jats:p>Prions represent an unusual structural form of a protein that is \u2018infectious\u2019. In mammals, prions are associated with fatal neurodegenerative diseases such as CJD (Creutzfeldt\u2013Jakob disease), while in fungi they act as novel epigenetic regulators of phenotype. Even though most of the human prion diseases arise spontaneously, we still know remarkably little about how infectious prions form de novo. The [PSI+] prion of the yeast Saccharomyces cerevisiae provides a highly tractable model in which to explore the underlying mechanism of de novo prion formation, in particular identifying key cis- and trans-acting factors. Most significantly, the de novo formation of [PSI+] requires the presence of a second prion called [PIN+], which is typically the prion form of Rnq1p, a protein rich in glutamine and aspartic acid residues. The molecular mechanism by which the [PIN+] prion facilitates de novo [PSI+] formation is not fully established, but most probably involves some form of cross-seeding. A number of other cellular factors, in particular chaperones of the Hsp70 (heat-shock protein 70) family, are known to modify the frequency of de novo prion formation in yeast.<\/jats:p>","DOI":"10.1042\/bst0361083","type":"journal-article","created":{"date-parts":[[2008,10,6]],"date-time":"2008-10-06T11:54:55Z","timestamp":1223294095000},"page":"1083-1087","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":12,"title":["Cellular factors important for the <i>de novo<\/i> formation of yeast prions"],"prefix":"10.1042","volume":"36","author":[{"given":"Mick","family":"Tuite","sequence":"first","affiliation":[{"name":"Protein Science Group, Department of Biosciences, University of Kent, Canterbury, Kent CT2 7NJ, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Klement","family":"Stojanovski","sequence":"additional","affiliation":[{"name":"Protein Science Group, Department of Biosciences, University of Kent, Canterbury, Kent CT2 7NJ, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Frederique","family":"Ness","sequence":"additional","affiliation":[{"name":"Protein Science Group, Department of Biosciences, University of Kent, Canterbury, Kent CT2 7NJ, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gloria","family":"Merritt","sequence":"additional","affiliation":[{"name":"Protein Science Group, Department of Biosciences, University of Kent, Canterbury, Kent CT2 7NJ, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nadejda","family":"Koloteva-Levine","sequence":"additional","affiliation":[{"name":"Protein Science Group, Department of Biosciences, University of Kent, Canterbury, Kent CT2 7NJ, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","published-online":{"date-parts":[[2008,9,19]]},"reference":[{"key":"2021111720012240600_B1","doi-asserted-by":"crossref","first-page":"1043","DOI":"10.1038\/2151043a0","article-title":"Self-replication and scrapie","volume":"215","author":"Griffith","year":"1967","journal-title":"Nature"},{"key":"2021111720012240600_B2","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1126\/science.6801762","article-title":"Novel proteinaceous infectious particles cause scrapie","volume":"216","author":"Prusiner","year":"1982","journal-title":"Science"},{"key":"2021111720012240600_B3","doi-asserted-by":"crossref","first-page":"6942","DOI":"10.1021\/bi00269a050","article-title":"Further purification and characterization of scrapie prions","volume":"21","author":"Prusiner","year":"1982","journal-title":"J. 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