| pubmed-article:10656806 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10656806 | lifeskim:mentions | umls-concept:C0012634 | lld:lifeskim |
| pubmed-article:10656806 | lifeskim:mentions | umls-concept:C0025936 | lld:lifeskim |
| pubmed-article:10656806 | lifeskim:mentions | umls-concept:C1415327 | lld:lifeskim |
| pubmed-article:10656806 | lifeskim:mentions | umls-concept:C1548602 | lld:lifeskim |
| pubmed-article:10656806 | lifeskim:mentions | umls-concept:C0597551 | lld:lifeskim |
| pubmed-article:10656806 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:10656806 | pubmed:dateCreated | 2000-3-7 | lld:pubmed |
| pubmed-article:10656806 | pubmed:abstractText | The molecular basis of the infectious, inherited and sporadic forms of prion diseases is best explained by a conformationally dimorphic protein that can exist in distinct normal and disease-causing isoforms. We identified a 55-residue peptide of a mutant prion protein that can be refolded into at least two distinct conformations. When inoculated intracerebrally into the appropriate transgenic mouse host, 20 of 20 mice receiving the beta-form of this peptide developed signs of central nervous system dysfunction at approximately 360 days, with neurohistologic changes that are pathognomonic of Gerstmann-Sträussler-Scheinker disease. By contrast, eight of eight mice receiving a non-beta-form of the peptide failed to develop any neuropathologic changes more than 600 days after the peptide injections. We conclude that a chemically synthesized peptide refolded into the appropriate conformation can accelerate or possibly initiate prion disease. | lld:pubmed |
| pubmed-article:10656806 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10656806 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10656806 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10656806 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10656806 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10656806 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10656806 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10656806 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10656806 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10656806 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:10656806 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:10656806 | pubmed:author | pubmed-author:PrusinerS BSB | lld:pubmed |
| pubmed-article:10656806 | pubmed:author | pubmed-author:KanekoKK | lld:pubmed |
| pubmed-article:10656806 | pubmed:author | pubmed-author:CohenF EFE | lld:pubmed |
| pubmed-article:10656806 | pubmed:author | pubmed-author:GrothDD | lld:pubmed |
| pubmed-article:10656806 | pubmed:author | pubmed-author:ZhangHH | lld:pubmed |
| pubmed-article:10656806 | pubmed:author | pubmed-author:BaldwinM AMA | lld:pubmed |
| pubmed-article:10656806 | pubmed:author | pubmed-author:DeArmondS JSJ | lld:pubmed |
| pubmed-article:10656806 | pubmed:author | pubmed-author:TremblayPP | lld:pubmed |
| pubmed-article:10656806 | pubmed:author | pubmed-author:WilleHH | lld:pubmed |
| pubmed-article:10656806 | pubmed:author | pubmed-author:BallH LHL | lld:pubmed |
| pubmed-article:10656806 | pubmed:author | pubmed-author:SafarJJ | lld:pubmed |
| pubmed-article:10656806 | pubmed:author | pubmed-author:TorchiaMM | lld:pubmed |
| pubmed-article:10656806 | pubmed:copyrightInfo | Copyright 2000 Academic Press. | lld:pubmed |
| pubmed-article:10656806 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10656806 | pubmed:day | 28 | lld:pubmed |
| pubmed-article:10656806 | pubmed:volume | 295 | lld:pubmed |
| pubmed-article:10656806 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10656806 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10656806 | pubmed:pagination | 997-1007 | lld:pubmed |
| pubmed-article:10656806 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:10656806 | pubmed:meshHeading | pubmed-meshheading:10656806... | lld:pubmed |
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| pubmed-article:10656806 | pubmed:meshHeading | pubmed-meshheading:10656806... | lld:pubmed |
| pubmed-article:10656806 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10656806 | pubmed:articleTitle | A synthetic peptide initiates Gerstmann-Sträussler-Scheinker (GSS) disease in transgenic mice. | lld:pubmed |
| pubmed-article:10656806 | pubmed:affiliation | Institute for Neurodegenerative Diseases, Department of Neurology, University of California, San Francisco, 94143, USA. | lld:pubmed |
| pubmed-article:10656806 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10656806 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10656806 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:19122 | entrezgene:pubmed | pubmed-article:10656806 | lld:entrezgene |
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