| pubmed-article:16788822 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16788822 | lifeskim:mentions | umls-concept:C0026848 | lld:lifeskim |
| pubmed-article:16788822 | lifeskim:mentions | umls-concept:C0008059 | lld:lifeskim |
| pubmed-article:16788822 | lifeskim:mentions | umls-concept:C0439660 | lld:lifeskim |
| pubmed-article:16788822 | lifeskim:mentions | umls-concept:C0026845 | lld:lifeskim |
| pubmed-article:16788822 | lifeskim:mentions | umls-concept:C0333773 | lld:lifeskim |
| pubmed-article:16788822 | lifeskim:mentions | umls-concept:C0085401 | lld:lifeskim |
| pubmed-article:16788822 | lifeskim:mentions | umls-concept:C0333562 | lld:lifeskim |
| pubmed-article:16788822 | lifeskim:mentions | umls-concept:C2353566 | lld:lifeskim |
| pubmed-article:16788822 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:16788822 | pubmed:dateCreated | 2006-7-25 | lld:pubmed |
| pubmed-article:16788822 | pubmed:abstractText | We investigated whether beta-amyloid and tau protein are involved in the formation of inclusion body myositis (IBM)-like inclusions found in children with rimmed vacuoles and congenitally affected muscles. We immunostained muscle biopsy specimens from four children and one 18-year-old boy with congenital myopathy containing rimmed vacuoles and IBM-like inclusions with antibodies against beta-amyloid, tau protein and ubiquitin. Focal accumulations of both beta-amyloid and phosphorylated tau coexisted with tubulofilamentous structures in all cases. Our studies demonstrate for the first time that the full morphological phenotype of IBM including beta-amyloid and tau protein deposits may also develop in children, and that congenital, probably genetic, muscle defects may lead to abnormal protein aggregation in IBM-like inclusions. | lld:pubmed |
| pubmed-article:16788822 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16788822 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16788822 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16788822 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16788822 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16788822 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16788822 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16788822 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:16788822 | pubmed:issn | 0001-6322 | lld:pubmed |
| pubmed-article:16788822 | pubmed:author | pubmed-author:Fidzia?skaAnn... | lld:pubmed |
| pubmed-article:16788822 | pubmed:author | pubmed-author:GlinkaZofiaZ | lld:pubmed |
| pubmed-article:16788822 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16788822 | pubmed:volume | 112 | lld:pubmed |
| pubmed-article:16788822 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16788822 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16788822 | pubmed:pagination | 185-93 | lld:pubmed |
| pubmed-article:16788822 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
| pubmed-article:16788822 | pubmed:meshHeading | pubmed-meshheading:16788822... | lld:pubmed |
| pubmed-article:16788822 | pubmed:meshHeading | pubmed-meshheading:16788822... | lld:pubmed |
| pubmed-article:16788822 | pubmed:meshHeading | pubmed-meshheading:16788822... | lld:pubmed |
| pubmed-article:16788822 | pubmed:meshHeading | pubmed-meshheading:16788822... | lld:pubmed |
| pubmed-article:16788822 | pubmed:meshHeading | pubmed-meshheading:16788822... | lld:pubmed |
| pubmed-article:16788822 | pubmed:meshHeading | pubmed-meshheading:16788822... | lld:pubmed |
| pubmed-article:16788822 | pubmed:meshHeading | pubmed-meshheading:16788822... | lld:pubmed |
| pubmed-article:16788822 | pubmed:meshHeading | pubmed-meshheading:16788822... | lld:pubmed |
| pubmed-article:16788822 | pubmed:meshHeading | pubmed-meshheading:16788822... | lld:pubmed |
| pubmed-article:16788822 | pubmed:meshHeading | pubmed-meshheading:16788822... | lld:pubmed |
| pubmed-article:16788822 | pubmed:meshHeading | pubmed-meshheading:16788822... | lld:pubmed |
| pubmed-article:16788822 | pubmed:meshHeading | pubmed-meshheading:16788822... | lld:pubmed |
| pubmed-article:16788822 | pubmed:meshHeading | pubmed-meshheading:16788822... | lld:pubmed |
| pubmed-article:16788822 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16788822 | pubmed:articleTitle | Rimmed vacuoles with beta-amyloid and tau protein deposits in the muscle of children with hereditary myopathy. | lld:pubmed |
| pubmed-article:16788822 | pubmed:affiliation | Neuromuscular Unit MRC, Polish Academy of Science, Pawi?skiego 5, 02-106, Warsaw, Poland. neurmyol@cmdik.pan.pl | lld:pubmed |
| pubmed-article:16788822 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16788822 | pubmed:publicationType | Case Reports | lld:pubmed |
| pubmed-article:16788822 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| entrez-gene:4137 | entrezgene:pubmed | pubmed-article:16788822 | lld:entrezgene |
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