pubmed-article:9506999 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9506999 | lifeskim:mentions | umls-concept:C0018787 | lld:lifeskim |
pubmed-article:9506999 | lifeskim:mentions | umls-concept:C0036208 | lld:lifeskim |
pubmed-article:9506999 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:9506999 | lifeskim:mentions | umls-concept:C1332728 | lld:lifeskim |
pubmed-article:9506999 | lifeskim:mentions | umls-concept:C0332281 | lld:lifeskim |
pubmed-article:9506999 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:9506999 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
pubmed-article:9506999 | lifeskim:mentions | umls-concept:C0205164 | lld:lifeskim |
pubmed-article:9506999 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
pubmed-article:9506999 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
pubmed-article:9506999 | pubmed:issue | 12 | lld:pubmed |
pubmed-article:9506999 | pubmed:dateCreated | 1998-4-16 | lld:pubmed |
pubmed-article:9506999 | pubmed:abstractText | Sucrose-density flotation analysis of Triton-insoluble membrane domains isolated from highly purified sheep ventricular sarcolemma revealed the presence of two major 120- and 100-kDa proteins. Both species migrated in two-dimensional isoelectric focussing/SDS gels with an apparent pI of approximately 4.3, suggesting that they might be related. Microsequence analysis of peptides derived from the 100-kDa protein yielded amino acid sequences with high homology to T-cadherin, a truncated cadherin lacking a cytoplasmic domain. The similarity was confirmed using antibodies to chicken T-cadherin that reacted with both proteins on immunoblots. T-cadherin was released from the detergent-insoluble sarcolemmal fraction by phospholipase C treatment indicating that it is linked to the membrane by a glycophosphoinositol anchor. T-cadherin could be ADP-ribosylated by a transferase that was also present in the caveolin-enriched Triton-insoluble fraction. T-cadherin-containing membrane fragments cofractionated on sucrose gradients with caveolin-3, a marker protein for myocyte caveolae. However, immunopurified caveolin-3-containing membranes contained no associated T-cadherin. Immunocytochemical analysis of cultured rat atrial myocytes revealed that T-cadherin and caveolin have related but nonoverlapping staining patterns. These results suggest that T-cadherin is a major glycophosphoinositol-linked protein in cardiac myocytes and that it may be located in plasma membrane "rafts" distinct from but possibly adjacent to caveolae. | lld:pubmed |
pubmed-article:9506999 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9506999 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9506999 | pubmed:language | eng | lld:pubmed |
pubmed-article:9506999 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9506999 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:9506999 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9506999 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9506999 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9506999 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9506999 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9506999 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9506999 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9506999 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9506999 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9506999 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9506999 | pubmed:month | Mar | lld:pubmed |
pubmed-article:9506999 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:9506999 | pubmed:author | pubmed-author:PageEE | lld:pubmed |
pubmed-article:9506999 | pubmed:author | pubmed-author:Upshaw-Earley... | lld:pubmed |
pubmed-article:9506999 | pubmed:author | pubmed-author:RanschtBB | lld:pubmed |
pubmed-article:9506999 | pubmed:author | pubmed-author:PalfreyH CHC | lld:pubmed |
pubmed-article:9506999 | pubmed:author | pubmed-author:GoingsG EGE | lld:pubmed |
pubmed-article:9506999 | pubmed:author | pubmed-author:DoyleD DDD | lld:pubmed |
pubmed-article:9506999 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9506999 | pubmed:day | 20 | lld:pubmed |
pubmed-article:9506999 | pubmed:volume | 273 | lld:pubmed |
pubmed-article:9506999 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9506999 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9506999 | pubmed:pagination | 6937-43 | lld:pubmed |
pubmed-article:9506999 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
pubmed-article:9506999 | pubmed:meshHeading | pubmed-meshheading:9506999-... | lld:pubmed |
pubmed-article:9506999 | pubmed:meshHeading | pubmed-meshheading:9506999-... | lld:pubmed |
pubmed-article:9506999 | pubmed:meshHeading | pubmed-meshheading:9506999-... | lld:pubmed |
pubmed-article:9506999 | pubmed:meshHeading | pubmed-meshheading:9506999-... | lld:pubmed |
pubmed-article:9506999 | pubmed:meshHeading | pubmed-meshheading:9506999-... | lld:pubmed |
pubmed-article:9506999 | pubmed:meshHeading | pubmed-meshheading:9506999-... | lld:pubmed |
pubmed-article:9506999 | pubmed:meshHeading | pubmed-meshheading:9506999-... | lld:pubmed |
pubmed-article:9506999 | pubmed:meshHeading | pubmed-meshheading:9506999-... | lld:pubmed |
pubmed-article:9506999 | pubmed:meshHeading | pubmed-meshheading:9506999-... | lld:pubmed |
pubmed-article:9506999 | pubmed:meshHeading | pubmed-meshheading:9506999-... | lld:pubmed |
pubmed-article:9506999 | pubmed:meshHeading | pubmed-meshheading:9506999-... | lld:pubmed |
pubmed-article:9506999 | pubmed:meshHeading | pubmed-meshheading:9506999-... | lld:pubmed |
pubmed-article:9506999 | pubmed:meshHeading | pubmed-meshheading:9506999-... | lld:pubmed |
pubmed-article:9506999 | pubmed:meshHeading | pubmed-meshheading:9506999-... | lld:pubmed |
pubmed-article:9506999 | pubmed:meshHeading | pubmed-meshheading:9506999-... | lld:pubmed |
pubmed-article:9506999 | pubmed:meshHeading | pubmed-meshheading:9506999-... | lld:pubmed |
pubmed-article:9506999 | pubmed:year | 1998 | lld:pubmed |
pubmed-article:9506999 | pubmed:articleTitle | T-cadherin is a major glycophosphoinositol-anchored protein associated with noncaveolar detergent-insoluble domains of the cardiac sarcolemma. | lld:pubmed |
pubmed-article:9506999 | pubmed:affiliation | Department of Medicine, University of Chicago, Chicago, Illinois 60637, USA. | lld:pubmed |
pubmed-article:9506999 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9506999 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:9506999 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
entrez-gene:192248 | entrezgene:pubmed | pubmed-article:9506999 | lld:entrezgene |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9506999 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9506999 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9506999 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9506999 | lld:pubmed |