| pubmed-article:16432139 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16432139 | lifeskim:mentions | umls-concept:C0012634 | lld:lifeskim |
| pubmed-article:16432139 | lifeskim:mentions | umls-concept:C0039796 | lld:lifeskim |
| pubmed-article:16432139 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:16432139 | pubmed:issue | 2 Suppl 1 | lld:pubmed |
| pubmed-article:16432139 | pubmed:dateCreated | 2006-1-24 | lld:pubmed |
| pubmed-article:16432139 | pubmed:abstractText | Our current structural and biologic understanding of the misfolding diseases has restricted the development of therapies that target these diseases at a molecular level. The prion diseases are illustrative of this group of misfolding disorders and provide a model system for therapeutic intervention. Strategies to inhibit the replication and accumulation of the prion protein are being developed and have entered animal and clinical studies. Due to the underlying molecular basis of this disease class, many of the therapeutic approaches used to target prion misfolding have parallels in other misfolding diseases. | lld:pubmed |
| pubmed-article:16432139 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16432139 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16432139 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16432139 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16432139 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16432139 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16432139 | pubmed:citationSubset | AIM | lld:pubmed |
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| pubmed-article:16432139 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16432139 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16432139 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:16432139 | pubmed:issn | 1526-632X | lld:pubmed |
| pubmed-article:16432139 | pubmed:author | pubmed-author:CohenFred EFE | lld:pubmed |
| pubmed-article:16432139 | pubmed:author | pubmed-author:GovaertsCedri... | lld:pubmed |
| pubmed-article:16432139 | pubmed:author | pubmed-author:MayBarnaby... | lld:pubmed |
| pubmed-article:16432139 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:16432139 | pubmed:day | 24 | lld:pubmed |
| pubmed-article:16432139 | pubmed:volume | 66 | lld:pubmed |
| pubmed-article:16432139 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16432139 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16432139 | pubmed:pagination | S118-22 | lld:pubmed |
| pubmed-article:16432139 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:16432139 | pubmed:meshHeading | pubmed-meshheading:16432139... | lld:pubmed |
| pubmed-article:16432139 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16432139 | pubmed:articleTitle | Developing therapeutics for the diseases of protein misfolding. | lld:pubmed |
| pubmed-article:16432139 | pubmed:affiliation | Institute for Neurodegenerative Diseases, University of California, San Francisco, CA 94143-2240, USA. alchemi@itsa.ucsf.edu | lld:pubmed |
| pubmed-article:16432139 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16432139 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:16432139 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:16432139 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16432139 | lld:pubmed |
