| pubmed-article:9808283 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9808283 | lifeskim:mentions | umls-concept:C1273518 | lld:lifeskim |
| pubmed-article:9808283 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
| pubmed-article:9808283 | lifeskim:mentions | umls-concept:C0010287 | lld:lifeskim |
| pubmed-article:9808283 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:9808283 | lifeskim:mentions | umls-concept:C0179400 | lld:lifeskim |
| pubmed-article:9808283 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:9808283 | pubmed:dateCreated | 1998-12-31 | lld:pubmed |
| pubmed-article:9808283 | pubmed:abstractText | Muscle-type creatine kinase is known for its unique interaction with the myofibrillar M-band, but the molecular origin for this structural relationship is not well understood. A systematic sequence comparison between the highly homologous cytosolic isoforms, muscle-type and brain-type creatine kinase, yielded two isoenzyme-specific regions in the muscle-type creatine kinases, the M-260 box (residues 258-270) and the M-300 box (residues 300-315). These particular regions were conspicuous for the specific interaction of this CK isoenzyme, but not of brain-type creatine kinase, with the sarcomeric M-band. In situ diffusion assays with fluorescently labeled native, as well as mutated muscle-type creatine kinase variants, were used to study by laser confocal microscopy their association with the M-band of chemically skinned muscle fibers. Neither a set of charge mutants of the M-260 box and/or the M-300 box nor a hybrid construct of both isoforms with the entire C-terminal region derived from the brain-type isoform showed any significant alteration in the in situ M-band-binding properties when compared to the wild-type form of muscle-type creatine kinase. This indicates that in the intact protein of muscle type creatine kinase, these C-terminal isoenzyme-specific regions are not important for M-band interaction and that the actual M-band interaction domain(s) lay mostly within the N-terminal half of the molecule. The highly conserved motives (M-260 box and M-300 box) may serve an isoenzyme-specific purpose yet to be identified. | lld:pubmed |
| pubmed-article:9808283 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9808283 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9808283 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9808283 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9808283 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9808283 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9808283 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:9808283 | pubmed:issn | 0171-9335 | lld:pubmed |
| pubmed-article:9808283 | pubmed:author | pubmed-author:KraftTT | lld:pubmed |
| pubmed-article:9808283 | pubmed:author | pubmed-author:WallimannTT | lld:pubmed |
| pubmed-article:9808283 | pubmed:author | pubmed-author:StoltGG | lld:pubmed |
| pubmed-article:9808283 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9808283 | pubmed:volume | 77 | lld:pubmed |
| pubmed-article:9808283 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9808283 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9808283 | pubmed:pagination | 1-9 | lld:pubmed |
| pubmed-article:9808283 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:9808283 | pubmed:meshHeading | pubmed-meshheading:9808283-... | lld:pubmed |
| pubmed-article:9808283 | pubmed:meshHeading | pubmed-meshheading:9808283-... | lld:pubmed |
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| pubmed-article:9808283 | pubmed:meshHeading | pubmed-meshheading:9808283-... | lld:pubmed |
| pubmed-article:9808283 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9808283 | pubmed:articleTitle | The isoenzyme-diagnostic regions of muscle-type creatine kinase, the M-260 and M-300 box, are not responsible for its binding to the myofibrillar M-band. | lld:pubmed |
| pubmed-article:9808283 | pubmed:affiliation | Swiss Federal Institute of Technology (ETH), Institute of Cell Biology, Zürich. | lld:pubmed |
| pubmed-article:9808283 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9808283 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:9808283 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9808283 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9808283 | lld:pubmed |
