| pubmed-article:15829582 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15829582 | lifeskim:mentions | umls-concept:C0012634 | lld:lifeskim |
| pubmed-article:15829582 | lifeskim:mentions | umls-concept:C0026809 | lld:lifeskim |
| pubmed-article:15829582 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:15829582 | lifeskim:mentions | umls-concept:C0038164 | lld:lifeskim |
| pubmed-article:15829582 | lifeskim:mentions | umls-concept:C1948066 | lld:lifeskim |
| pubmed-article:15829582 | lifeskim:mentions | umls-concept:C0002726 | lld:lifeskim |
| pubmed-article:15829582 | lifeskim:mentions | umls-concept:C1456454 | lld:lifeskim |
| pubmed-article:15829582 | lifeskim:mentions | umls-concept:C0349590 | lld:lifeskim |
| pubmed-article:15829582 | lifeskim:mentions | umls-concept:C2349975 | lld:lifeskim |
| pubmed-article:15829582 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:15829582 | pubmed:issue | 17 | lld:pubmed |
| pubmed-article:15829582 | pubmed:dateCreated | 2005-4-27 | lld:pubmed |
| pubmed-article:15829582 | pubmed:abstractText | Secondary, or amyloid protein A (AA), amyloidosis is a complication of chronic inflammatory diseases, both infectious and noninfectious. AA constitutes the insoluble fibrils, which are deposited in different organs, and is a major N-terminal part of the acute phase protein serum AA. It is not known why only some patients with chronic inflammation develop AA amyloidosis. Nucleation is a widely accepted mechanism in amyloidogenesis. Preformed amyloid-like fibrils act as nuclei in amyloid fibril formation in vitro, and AA amyloid fibrils and synthetic amyloid-like fibrils also may serve as seed for fibril formation in vivo. In addition to amyloid fibrils, there is a variety of similar nonmammalian protein fibrils with beta-pleated structure in nature. We studied three such naturally occurring protein fibrils: silk from Bombyx mori, Sup35 from Saccharomyces cerevisiae, and curli from Escherichia coli. Our results show that these protein fibrils exert amyloid-accelerating properties in the murine experimental AA amyloidosis, suggesting that such environment factors may be important risk factors in amyloidogenesis. | lld:pubmed |
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| pubmed-article:15829582 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15829582 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15829582 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15829582 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15829582 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:15829582 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:15829582 | pubmed:author | pubmed-author:WestermarkGun... | lld:pubmed |
| pubmed-article:15829582 | pubmed:author | pubmed-author:WestermarkPer... | lld:pubmed |
| pubmed-article:15829582 | pubmed:author | pubmed-author:LundmarkKatar... | lld:pubmed |
| pubmed-article:15829582 | pubmed:author | pubmed-author:OlsénArneA | lld:pubmed |
| pubmed-article:15829582 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15829582 | pubmed:day | 26 | lld:pubmed |
| pubmed-article:15829582 | pubmed:volume | 102 | lld:pubmed |
| pubmed-article:15829582 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15829582 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15829582 | pubmed:pagination | 6098-102 | lld:pubmed |
| pubmed-article:15829582 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:15829582 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15829582 | pubmed:articleTitle | Protein fibrils in nature can enhance amyloid protein A amyloidosis in mice: Cross-seeding as a disease mechanism. | lld:pubmed |
| pubmed-article:15829582 | pubmed:affiliation | Division of Pathology, Karolinska University Hospital, SE-141 86 Huddinge, Sweden. | lld:pubmed |
| pubmed-article:15829582 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15829582 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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