| pubmed-article:19830582 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19830582 | lifeskim:mentions | umls-concept:C0042567 | lld:lifeskim |
| pubmed-article:19830582 | lifeskim:mentions | umls-concept:C0026845 | lld:lifeskim |
| pubmed-article:19830582 | lifeskim:mentions | umls-concept:C0036225 | lld:lifeskim |
| pubmed-article:19830582 | lifeskim:mentions | umls-concept:C0230719 | lld:lifeskim |
| pubmed-article:19830582 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:19830582 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:19830582 | pubmed:issue | 5-6 | lld:pubmed |
| pubmed-article:19830582 | pubmed:dateCreated | 2010-1-21 | lld:pubmed |
| pubmed-article:19830582 | pubmed:abstractText | The Z-disc, appearing as a fine dense line forming sarcomere boundaries in striated muscles, when studied in detail reveals crosslinked filament arrays that transmit tension and house myriads of proteins with diverse functions. At the Z-disc the barbed ends of the antiparallel actin filaments from adjoining sarcomeres interdigitate and are crosslinked primarily by layers of alpha-actinin. The Z-disc is therefore the site of polarity reversal of the actin filaments, as needed to interact with the bipolar myosin filaments in successive sarcomeres. The layers of alpha-actinin determine the Z-disc width: fast fibres have narrow (approximately 30-50 nm) Z-discs and slow and cardiac fibres have wide (approximately 100 nm) Z-discs. Comprehensive reviews on the roles of the numerous proteins located at the Z-disc in signalling and disease have been published; the aim here is different, namely to review the advances in structural aspects of the Z-disc. | lld:pubmed |
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| pubmed-article:19830582 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19830582 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
