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B"],"published-print":{"date-parts":[[2001,2,28]]},"abstract":"<jats:p>\n                    Prion diseases such as Creutzfeldt\u2013Jakob disease (CJD) in humans and scrapie and bovine spongiform encephalopathy (BSE) in animals are associated with the accumulation in affected brains of a conformational isomer (PrP\n                    <jats:sup>Sc<\/jats:sup>\n                    ) of host\u2013derived prion protein (PrP\n                    <jats:sup>C<\/jats:sup>\n                    ). According to the protein\u2013only hypothesis, PrP\n                    <jats:sup>Sc<\/jats:sup>\n                    is the principal or sole component of transmissible prions. The conformational change known to be central to prion propagation, from a predominantly \u03b1\u2013helical fold to one predominantly comprising \u03b2 structure, can now be reproduced\n                    <jats:italic>in vitro<\/jats:italic>\n                    , and the ability of \u03b2\u2013PrP to form fibrillar aggregates provides a plausible molecular mechanism for prion propagation. The existence of multiple prion strains has been difficult to explain in terms of a protein\u2013only infectious agent but recent studies of human prion diseases suggest that strain\u2013specific phenotypes can be encoded by different PrP conformations and glycosylation patterns. The experimental confirmation that a novel form of human prion disease, variant CJD, is caused by the same prion strain as cattle BSE, has highlighted the pressing need to understand the molecular basis of prion propagation and the transmission barriers that limit their passage between mammalian species. These and other advances in the fundamental biology of prion propagation are leading to strategies for the development of rational therapeutics.\n                  <\/jats:p>","DOI":"10.1098\/rstb.2000.0764","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T19:58:30Z","timestamp":1027713510000},"page":"185-195","source":"Crossref","is-referenced-by-count":37,"title":["The molecular biology of prion propagation"],"prefix":"10.1098","volume":"356","author":[{"given":"Anthony R.","family":"Clarke","sequence":"first","affiliation":[{"name":"Medical Research Council Prion Unit, Department of Neurogenetics, Imperial College School of Medicine at St Mary's, London W2 1NY, UK"},{"name":"Department of Biochemistry, School of Medical Sciences, University of Bristol, Bristol, BS8 1TD, UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Graham S.","family":"Jackson","sequence":"additional","affiliation":[{"name":"Medical Research Council Prion Unit, Department of Neurogenetics, Imperial College School of Medicine at St Mary's, London W2 1NY, UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"John","family":"Collinge","sequence":"additional","affiliation":[{"name":"Medical Research Council Prion Unit, Department of Neurogenetics, Imperial College School of Medicine at St Mary's, London W2 1NY, UK"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"175","published-online":{"date-parts":[[2001,2,28]]},"reference":[{"key":"p_1","doi-asserted-by":"publisher","DOI":"10.1002\/path.1711760412"},{"key":"p_2","doi-asserted-by":"publisher","DOI":"10.1016\/0140-6736(91)92953-Y"},{"key":"p_3","unstructured":"Barlow R. 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