| pubmed-article:8264699 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8264699 | lifeskim:mentions | umls-concept:C0026850 | lld:lifeskim |
| pubmed-article:8264699 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:8264699 | lifeskim:mentions | umls-concept:C0699748 | lld:lifeskim |
| pubmed-article:8264699 | lifeskim:mentions | umls-concept:C1521991 | lld:lifeskim |
| pubmed-article:8264699 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:8264699 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:8264699 | pubmed:dateCreated | 1994-1-25 | lld:pubmed |
| pubmed-article:8264699 | pubmed:abstractText | Dystrophin, the protein product of the Duchenne muscular dystrophy (DMD) gene, is associated with a large oligomeric complex of sarcolemmal glycoproteins, including dystroglycan which provides a linkage to the extracellular matrix component, laminin. In patients with DMD, the absence of dystrophin leads to the loss in all of the dystrophin-associated proteins, causing the disruption of the linkage between the subsarcolemmal cytoskeleton and the extracellular matrix. This may render the sarcolemma vulnerable to physical stress. These recent developments in the research concerning the function of the dystrophin-glycoprotein complex pave a way for the better understanding of the pathogenesis of muscular dystrophies. | lld:pubmed |
| pubmed-article:8264699 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8264699 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8264699 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8264699 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:8264699 | pubmed:issn | 0148-639X | lld:pubmed |
| pubmed-article:8264699 | pubmed:author | pubmed-author:MatsumuraKK | lld:pubmed |
| pubmed-article:8264699 | pubmed:author | pubmed-author:CampbellK PKP | lld:pubmed |
| pubmed-article:8264699 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8264699 | pubmed:volume | 17 | lld:pubmed |
| pubmed-article:8264699 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8264699 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8264699 | pubmed:pagination | 2-15 | lld:pubmed |
| pubmed-article:8264699 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:8264699 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:8264699 | pubmed:articleTitle | Dystrophin-glycoprotein complex: its role in the molecular pathogenesis of muscular dystrophies. | lld:pubmed |
| pubmed-article:8264699 | pubmed:affiliation | Howard Hughes Medical Institute, University of Iowa College of Medicine, Iowa City 52242. | lld:pubmed |
| pubmed-article:8264699 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8264699 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:8264699 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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