pubmed-article:2140985 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2140985 | lifeskim:mentions | umls-concept:C0008051 | lld:lifeskim |
pubmed-article:2140985 | lifeskim:mentions | umls-concept:C0016055 | lld:lifeskim |
pubmed-article:2140985 | lifeskim:mentions | umls-concept:C0015350 | lld:lifeskim |
pubmed-article:2140985 | lifeskim:mentions | umls-concept:C1510668 | lld:lifeskim |
pubmed-article:2140985 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
pubmed-article:2140985 | lifeskim:mentions | umls-concept:C1179435 | lld:lifeskim |
pubmed-article:2140985 | lifeskim:mentions | umls-concept:C0000530 | lld:lifeskim |
pubmed-article:2140985 | lifeskim:mentions | umls-concept:C1705248 | lld:lifeskim |
pubmed-article:2140985 | lifeskim:mentions | umls-concept:C1548799 | lld:lifeskim |
pubmed-article:2140985 | lifeskim:mentions | umls-concept:C1524073 | lld:lifeskim |
pubmed-article:2140985 | lifeskim:mentions | umls-concept:C0449432 | lld:lifeskim |
pubmed-article:2140985 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:2140985 | pubmed:dateCreated | 1990-7-13 | lld:pubmed |
pubmed-article:2140985 | pubmed:abstractText | The smooth muscle cells of chicken gizzard harbor the ectoenzyme 5'-nucleotidase. The purified enzyme was reconstituted into 3H-labeled proteoliposomes which were used as a model to study the association of a membrane protein with fibronectin. We demonstrated that the binding process between proteoliposomes and fibronectin has the qualities of a receptor-ligand interaction, i.e., is saturable and specific. In contrast to the association of fibronectin with integrins, the interaction with 5'-nucleotidase does not require divalent metal ions. Synthetic peptides containing the RGD-sequence or a monoclonal antibody interfering with binding of other receptors to the cell-binding domain of fibronectin did not abolish the interaction with 5'-nucleotidase. This indicates that the RGDS-sequence does not represent the major contact site for the AMPase and that the 5'-nucleotidase belongs to a separate class of fibronectin receptors with distinct properties as compared to the integrins. | lld:pubmed |
pubmed-article:2140985 | pubmed:language | eng | lld:pubmed |
pubmed-article:2140985 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2140985 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:2140985 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2140985 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2140985 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2140985 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2140985 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2140985 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2140985 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2140985 | pubmed:month | Apr | lld:pubmed |
pubmed-article:2140985 | pubmed:issn | 0171-9335 | lld:pubmed |
pubmed-article:2140985 | pubmed:author | pubmed-author:RichterHH | lld:pubmed |
pubmed-article:2140985 | pubmed:author | pubmed-author:MannherzH GHG | lld:pubmed |
pubmed-article:2140985 | pubmed:author | pubmed-author:StochajUU | lld:pubmed |
pubmed-article:2140985 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2140985 | pubmed:volume | 51 | lld:pubmed |
pubmed-article:2140985 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2140985 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2140985 | pubmed:pagination | 335-8 | lld:pubmed |
pubmed-article:2140985 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
pubmed-article:2140985 | pubmed:meshHeading | pubmed-meshheading:2140985-... | lld:pubmed |
pubmed-article:2140985 | pubmed:meshHeading | pubmed-meshheading:2140985-... | lld:pubmed |
pubmed-article:2140985 | pubmed:meshHeading | pubmed-meshheading:2140985-... | lld:pubmed |
pubmed-article:2140985 | pubmed:meshHeading | pubmed-meshheading:2140985-... | lld:pubmed |
pubmed-article:2140985 | pubmed:meshHeading | pubmed-meshheading:2140985-... | lld:pubmed |
pubmed-article:2140985 | pubmed:meshHeading | pubmed-meshheading:2140985-... | lld:pubmed |
pubmed-article:2140985 | pubmed:meshHeading | pubmed-meshheading:2140985-... | lld:pubmed |
pubmed-article:2140985 | pubmed:meshHeading | pubmed-meshheading:2140985-... | lld:pubmed |
pubmed-article:2140985 | pubmed:meshHeading | pubmed-meshheading:2140985-... | lld:pubmed |
pubmed-article:2140985 | pubmed:meshHeading | pubmed-meshheading:2140985-... | lld:pubmed |
pubmed-article:2140985 | pubmed:meshHeading | pubmed-meshheading:2140985-... | lld:pubmed |
pubmed-article:2140985 | pubmed:meshHeading | pubmed-meshheading:2140985-... | lld:pubmed |
pubmed-article:2140985 | pubmed:meshHeading | pubmed-meshheading:2140985-... | lld:pubmed |
pubmed-article:2140985 | pubmed:year | 1990 | lld:pubmed |
pubmed-article:2140985 | pubmed:articleTitle | Chicken gizzard 5'-nucleotidase is a receptor for the extracellular matrix component fibronectin. | lld:pubmed |
pubmed-article:2140985 | pubmed:affiliation | Institut für Anatomie und Zellbiologie der Universität, Marburg/Bundesrepublik Deutschland. | lld:pubmed |
pubmed-article:2140985 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2140985 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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