pubmed-article:2044861 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2044861 | lifeskim:mentions | umls-concept:C0008051 | lld:lifeskim |
pubmed-article:2044861 | lifeskim:mentions | umls-concept:C0026845 | lld:lifeskim |
pubmed-article:2044861 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:2044861 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:2044861 | pubmed:dateCreated | 1991-7-18 | lld:pubmed |
pubmed-article:2044861 | pubmed:abstractText | The development and functional activity of the heart depends on the regulated interaction of cardiac cells. This is in part mediated by cell-cell adhesion molecules such as N-cadherin. N-cadherin belongs to a family of Ca+(+)-dependent, transmembrane, adhesion glycoproteins that promote cell-cell adhesion by molecular self-association extracellularly, and interact intracellularly with the cytoskeleton through highly conserved carboxy-terminal domains. In this paper we show that embryonic chicken cardiac myocytes grown in vitro display Ca+(+)-dependent adhesion and express N-cadherin. When immunoprecipitated from detergent extracts of embryonic chicken cardiac and skeletal muscle cultures, N-cadherin associates with proteins immunologically unrelated to itself. The associated proteins are similar in molecular weight to proteins that coimmunoprecipatate with E-cadherin from human epithelial cells. We postulate that the coimmunoprecipitating proteins are involved in linking the cadherins to the cytoskeleton. | lld:pubmed |
pubmed-article:2044861 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2044861 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2044861 | pubmed:language | eng | lld:pubmed |
pubmed-article:2044861 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2044861 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:2044861 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2044861 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2044861 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2044861 | pubmed:month | Feb | lld:pubmed |
pubmed-article:2044861 | pubmed:issn | 0301-4681 | lld:pubmed |
pubmed-article:2044861 | pubmed:author | pubmed-author:KnudsenK AKA | lld:pubmed |
pubmed-article:2044861 | pubmed:author | pubmed-author:WheelockM JMJ | lld:pubmed |
pubmed-article:2044861 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2044861 | pubmed:volume | 46 | lld:pubmed |
pubmed-article:2044861 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2044861 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2044861 | pubmed:pagination | 35-42 | lld:pubmed |
pubmed-article:2044861 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:2044861 | pubmed:year | 1991 | lld:pubmed |
pubmed-article:2044861 | pubmed:articleTitle | N-cadherin-associated proteins in chicken muscle. | lld:pubmed |
pubmed-article:2044861 | pubmed:affiliation | Department of Biology, University of Toledo, OH 43606. | lld:pubmed |
pubmed-article:2044861 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2044861 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:2044861 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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