| http://purl.uniprot.org/citations/18275852 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18275852 | http://www.w3.org/2000/01/rdf-schema#comment | "The human prion gene, PRNP, has two allelic forms that encode either a methionine or valine at codon 129. This polymorphism strongly influences the pathogenesis of prion disease. However, the underlying mechanism remains unclear. We compared the conformation between wild-type human prion protein (rPrP(C)) with either a valine or methionine at position 129, using a panel of monoclonal antibodies that are specific for epitopes along the entire protein. We found that rPrP(C(129M)) has a more exposed helix 1 region compared to rPrP(C(129V)). Helix 1 is important in the aggregation process. Accordingly, rPrP(C(129M)) aggregates at a faster rate and forms more aggregate than rPrP(C(129V)). In addition, by using a rPrP with a pathogenic mutation of five additional octapeptide repeat insertions, rPrP((129M)/10OR), as "seeds", we showed that rPrP((129M)/10OR) promotes the aggregation of rPrP(C(129M)) more efficiently than rPrP(C(129V)). These findings provide a possible mechanism underlying the influence of residue 129 on human prion disease."xsd:string |
| http://purl.uniprot.org/citations/18275852 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.bbrc.2008.01.172"xsd:string |
| http://purl.uniprot.org/citations/18275852 | http://purl.uniprot.org/core/author | "Li C."xsd:string |
| http://purl.uniprot.org/citations/18275852 | http://purl.uniprot.org/core/author | "Yu S."xsd:string |
| http://purl.uniprot.org/citations/18275852 | http://purl.uniprot.org/core/author | "Wong P."xsd:string |
| http://purl.uniprot.org/citations/18275852 | http://purl.uniprot.org/core/author | "Yin S."xsd:string |
| http://purl.uniprot.org/citations/18275852 | http://purl.uniprot.org/core/author | "Pham N."xsd:string |
| http://purl.uniprot.org/citations/18275852 | http://purl.uniprot.org/core/author | "Kang S.C."xsd:string |
| http://purl.uniprot.org/citations/18275852 | http://purl.uniprot.org/core/author | "Sy M.S."xsd:string |
| http://purl.uniprot.org/citations/18275852 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18275852 | http://purl.uniprot.org/core/name | "Biochem Biophys Res Commun"xsd:string |
| http://purl.uniprot.org/citations/18275852 | http://purl.uniprot.org/core/pages | "875-881"xsd:string |
| http://purl.uniprot.org/citations/18275852 | http://purl.uniprot.org/core/title | "Normal cellular prion protein with a methionine at position 129 has a more exposed helix 1 and is more prone to aggregate."xsd:string |
| http://purl.uniprot.org/citations/18275852 | http://purl.uniprot.org/core/volume | "368"xsd:string |
| http://purl.uniprot.org/citations/18275852 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/18275852 |
| http://purl.uniprot.org/citations/18275852 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/18275852 |
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