| pubmed-article:7479957 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7479957 | lifeskim:mentions | umls-concept:C0033164 | lld:lifeskim |
| pubmed-article:7479957 | lifeskim:mentions | umls-concept:C0178539 | lld:lifeskim |
| pubmed-article:7479957 | lifeskim:mentions | umls-concept:C0036457 | lld:lifeskim |
| pubmed-article:7479957 | lifeskim:mentions | umls-concept:C0597298 | lld:lifeskim |
| pubmed-article:7479957 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:7479957 | lifeskim:mentions | umls-concept:C1706701 | lld:lifeskim |
| pubmed-article:7479957 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:7479957 | lifeskim:mentions | umls-concept:C0597551 | lld:lifeskim |
| pubmed-article:7479957 | pubmed:issue | 24 | lld:pubmed |
| pubmed-article:7479957 | pubmed:dateCreated | 1995-12-28 | lld:pubmed |
| pubmed-article:7479957 | pubmed:abstractText | Conversion of the cellular isoform of prion protein (PrPC) into the scrapie isoform (PrPSc) involves an increase in the beta-sheet content, diminished solubility, and resistance to proteolytic digestion. Transgenetic studies argue that PrPC and PrPSc form a complex during PrPSc formation; thus, synthetic PrP peptides, which mimic the conformational pluralism of PrP, were mixed with PrPC to determine whether its properties were altered. Peptides encompassing two alpha-helical domains of PrP when mixed with PrPC produced a complex that displayed many properties of PrPSc. The PrPC-peptide complex formed fibrous aggregates and up to 65% of complexed PrPC sedimented at 100,000 x g for 1 h, whereas PrPC alone did not. These complexes were resistant to proteolytic digestion and displayed a high beta-sheet content. Unexpectedly, the peptide in a beta-sheet conformation did not form the complex, whereas the random coil did. Addition of 2% Sarkosyl disrupted the complex and rendered PrPC sensitive to protease digestion. While the pathogenic A117V mutation increased the efficacy of complex formation, anti-PrP monoclonal antibody prevented interaction between PrPC and peptides. Our findings in concert with transgenetic investigations argue that PrPC interacts with PrPSc through a domain that contains the first two putative alpha-helices. Whether PrPC-peptide complexes possess prion infectivity as determined by bioassays remains to be established. | lld:pubmed |
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| pubmed-article:7479957 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7479957 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7479957 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7479957 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7479957 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7479957 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:7479957 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:7479957 | pubmed:author | pubmed-author:PrusinerS BSB | lld:pubmed |
| pubmed-article:7479957 | pubmed:author | pubmed-author:KanekoKK | lld:pubmed |
| pubmed-article:7479957 | pubmed:author | pubmed-author:GriffithO HOH | lld:pubmed |
| pubmed-article:7479957 | pubmed:author | pubmed-author:JENS CSC | lld:pubmed |
| pubmed-article:7479957 | pubmed:author | pubmed-author:CohenF EFE | lld:pubmed |
| pubmed-article:7479957 | pubmed:author | pubmed-author:BaldwinM AMA | lld:pubmed |
| pubmed-article:7479957 | pubmed:author | pubmed-author:GabizonRR | lld:pubmed |
| pubmed-article:7479957 | pubmed:author | pubmed-author:BlochbergerT... | lld:pubmed |
| pubmed-article:7479957 | pubmed:author | pubmed-author:WilleHH | lld:pubmed |
| pubmed-article:7479957 | pubmed:author | pubmed-author:PeretzDD | lld:pubmed |
| pubmed-article:7479957 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7479957 | pubmed:day | 21 | lld:pubmed |
| pubmed-article:7479957 | pubmed:volume | 92 | lld:pubmed |
| pubmed-article:7479957 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7479957 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7479957 | pubmed:pagination | 11160-4 | lld:pubmed |
| pubmed-article:7479957 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:7479957 | pubmed:meshHeading | pubmed-meshheading:7479957-... | lld:pubmed |
| pubmed-article:7479957 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7479957 | pubmed:articleTitle | Prion protein (PrP) synthetic peptides induce cellular PrP to acquire properties of the scrapie isoform. | lld:pubmed |
| pubmed-article:7479957 | pubmed:affiliation | Department of Neurology, University of California, San Francisco 94143, USA. | lld:pubmed |
