| pubmed-article:2175684 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2175684 | lifeskim:mentions | umls-concept:C0596901 | lld:lifeskim |
| pubmed-article:2175684 | lifeskim:mentions | umls-concept:C0230844 | lld:lifeskim |
| pubmed-article:2175684 | lifeskim:mentions | umls-concept:C0268237 | lld:lifeskim |
| pubmed-article:2175684 | lifeskim:mentions | umls-concept:C0332479 | lld:lifeskim |
| pubmed-article:2175684 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:2175684 | lifeskim:mentions | umls-concept:C0392760 | lld:lifeskim |
| pubmed-article:2175684 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:2175684 | pubmed:dateCreated | 1991-2-4 | lld:pubmed |
| pubmed-article:2175684 | pubmed:abstractText | Cytochrome oxidase deficiency was detected in the skeletal muscle of a newborn floppy child. There was a significant decrease in the quantity of subunit 5 and 6 of cytochrome oxidase as showed in Western blot with cytochrome oxidase antibody. By contrast, the NADH: cytochrome c oxidoreductase activity was normal. Electron microscopic studies revealed serious distortion in the myofibres with broken Z-bands and disorganized fibers. The relative molecular mass of actin in the myopathic muscle was smaller than in control. The diffuse actin band in Western blot suggested a proteolytic degradation of F-actin in the myopathic muscle. There was also a serious distortion in the mitochondrial structure. Cytochrome oxidase has a direct role in the formation of cristae and mutation in its components may be directly responsible for the abnormal structure. | lld:pubmed |
| pubmed-article:2175684 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2175684 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2175684 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2175684 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2175684 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:2175684 | pubmed:issn | 0009-8981 | lld:pubmed |
| pubmed-article:2175684 | pubmed:author | pubmed-author:TrombitasKK | lld:pubmed |
| pubmed-article:2175684 | pubmed:author | pubmed-author:AdamovichKK | lld:pubmed |
| pubmed-article:2175684 | pubmed:author | pubmed-author:SumegiBB | lld:pubmed |
| pubmed-article:2175684 | pubmed:author | pubmed-author:MeleghBB | lld:pubmed |
| pubmed-article:2175684 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2175684 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:2175684 | pubmed:volume | 192 | lld:pubmed |
| pubmed-article:2175684 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2175684 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2175684 | pubmed:pagination | 9-18 | lld:pubmed |
| pubmed-article:2175684 | pubmed:dateRevised | 2004-11-17 | lld:pubmed |
| pubmed-article:2175684 | pubmed:meshHeading | pubmed-meshheading:2175684-... | lld:pubmed |
| pubmed-article:2175684 | pubmed:meshHeading | pubmed-meshheading:2175684-... | lld:pubmed |
| pubmed-article:2175684 | pubmed:meshHeading | pubmed-meshheading:2175684-... | lld:pubmed |
| pubmed-article:2175684 | pubmed:meshHeading | pubmed-meshheading:2175684-... | lld:pubmed |
| pubmed-article:2175684 | pubmed:meshHeading | pubmed-meshheading:2175684-... | lld:pubmed |
| pubmed-article:2175684 | pubmed:meshHeading | pubmed-meshheading:2175684-... | lld:pubmed |
| pubmed-article:2175684 | pubmed:meshHeading | pubmed-meshheading:2175684-... | lld:pubmed |
| pubmed-article:2175684 | pubmed:meshHeading | pubmed-meshheading:2175684-... | lld:pubmed |
| pubmed-article:2175684 | pubmed:meshHeading | pubmed-meshheading:2175684-... | lld:pubmed |
| pubmed-article:2175684 | pubmed:meshHeading | pubmed-meshheading:2175684-... | lld:pubmed |
| pubmed-article:2175684 | pubmed:meshHeading | pubmed-meshheading:2175684-... | lld:pubmed |
| pubmed-article:2175684 | pubmed:meshHeading | pubmed-meshheading:2175684-... | lld:pubmed |
| pubmed-article:2175684 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2175684 | pubmed:articleTitle | Cytochrome oxidase deficiency affecting the structure of the myofibre and the shape of mitochondrial cristae membrane. | lld:pubmed |
| pubmed-article:2175684 | pubmed:affiliation | Department of Biochemistry, University Medical School Szigeti, Hungary. | lld:pubmed |
| pubmed-article:2175684 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2175684 | pubmed:publicationType | Case Reports | lld:pubmed |
