| pubmed-article:7657592 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7657592 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:7657592 | lifeskim:mentions | umls-concept:C0027126 | lld:lifeskim |
| pubmed-article:7657592 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:7657592 | lifeskim:mentions | umls-concept:C0031727 | lld:lifeskim |
| pubmed-article:7657592 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:7657592 | lifeskim:mentions | umls-concept:C0475264 | lld:lifeskim |
| pubmed-article:7657592 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
| pubmed-article:7657592 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:7657592 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:7657592 | pubmed:issue | 35 | lld:pubmed |
| pubmed-article:7657592 | pubmed:dateCreated | 1995-10-4 | lld:pubmed |
| pubmed-article:7657592 | pubmed:abstractText | The protein product of the myotonic dystrophy (DM) gene is a putative serine-threonine protein kinase (DM kinase). Previous reports have characterized the DM gene product as various 50-62-kDa proteins. The predicted protein size from DM cDNA sequence is 69 kDa. We therefore expressed a full-length recombinant human DM kinase protein and compared its size and expression to heart, cardiac Purkinje fibers, and skeletal muscle from normal and DM subjects. Recombinantly expressed DM kinase and endogenous DM kinase in human heart, displayed two immunoreactive DM kinase proteins with apparent molecular sizes of 71 and 80 kDa, suggesting that these prior reports are incorrect. In cardiac Purkinje fibers the 71-kDa protein was the major form, and in skeletal muscle the 80-kDa protein was the major form. Immunostaining showed DM kinase localized to neuromuscular junctions in skeletal muscle and intercalated discs in heart and Purkinje fibers. DM subjects showed low abundance of DM kinase in heart and skeletal muscle, suggesting haplotype insufficiency as a potential mechanism for disease expression. These studies describe differential expression of two protein forms of DM kinase, which are localized to specialized cellular structures associated with impulse transmission. | lld:pubmed |
| pubmed-article:7657592 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7657592 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7657592 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7657592 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7657592 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7657592 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7657592 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7657592 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7657592 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7657592 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7657592 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:7657592 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:7657592 | pubmed:author | pubmed-author:BlowD MDM | lld:pubmed |
| pubmed-article:7657592 | pubmed:author | pubmed-author:MaedaMM | lld:pubmed |
| pubmed-article:7657592 | pubmed:author | pubmed-author:NevilleHH | lld:pubmed |
| pubmed-article:7657592 | pubmed:author | pubmed-author:BaileyW MWM | lld:pubmed |
| pubmed-article:7657592 | pubmed:author | pubmed-author:HolderEE | lld:pubmed |
| pubmed-article:7657592 | pubmed:author | pubmed-author:PerrymanM BMB | lld:pubmed |
| pubmed-article:7657592 | pubmed:author | pubmed-author:TaftC SCS | lld:pubmed |
| pubmed-article:7657592 | pubmed:author | pubmed-author:BushE WEW | lld:pubmed |
| pubmed-article:7657592 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7657592 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:7657592 | pubmed:volume | 270 | lld:pubmed |
| pubmed-article:7657592 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7657592 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7657592 | pubmed:pagination | 20246-9 | lld:pubmed |
| pubmed-article:7657592 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:7657592 | pubmed:meshHeading | pubmed-meshheading:7657592-... | lld:pubmed |
| pubmed-article:7657592 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7657592 | pubmed:articleTitle | Identification, tissue-specific expression, and subcellular localization of the 80- and 71-kDa forms of myotonic dystrophy kinase protein. | lld:pubmed |
| pubmed-article:7657592 | pubmed:affiliation | Cardiology Division, Temple Hoyne Buell Laboratories, University of Colorado Health Sciences Center, Denver 80262, USA. | lld:pubmed |
| pubmed-article:7657592 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7657592 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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