| pubmed-article:9588169 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9588169 | lifeskim:mentions | umls-concept:C0026844 | lld:lifeskim |
| pubmed-article:9588169 | lifeskim:mentions | umls-concept:C1135918 | lld:lifeskim |
| pubmed-article:9588169 | lifeskim:mentions | umls-concept:C0010738 | lld:lifeskim |
| pubmed-article:9588169 | lifeskim:mentions | umls-concept:C1519726 | lld:lifeskim |
| pubmed-article:9588169 | lifeskim:mentions | umls-concept:C1150423 | lld:lifeskim |
| pubmed-article:9588169 | lifeskim:mentions | umls-concept:C1948023 | lld:lifeskim |
| pubmed-article:9588169 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:9588169 | pubmed:dateCreated | 1998-6-5 | lld:pubmed |
| pubmed-article:9588169 | pubmed:abstractText | The actin filament-disrupting agent cytochalasin D strikingly increased tyrosine phosphorylation of a 75 kDa protein (p75) in rabbit aortic vascular smooth muscle cells. The microtubule-disrupting agent, colchicine had no effect on p75 tyrosine phosphorylation. Cytochalasin D also stimulated p75-directed kinase activity as determined by kinase assays of anti-Tyr(P) immunoprecipitates. Cytochalasin D stimulated tyrosine phosphorylation of the F-actin-binding protein, p80/85 cortactin, but p75 was not immunologically related either to cortactin, the phosphatidylinositol 3'-kinase p85 alpha subunit, or the 80 kDa isoform of caldesmon. These results suggest that p75 may represent a cytochalasin D-inducible kinase or kinase-associated component and provide evidence for the existence of a potentially novel kinase pathway regulated by disruption of the actin cytoskeleton. | lld:pubmed |
| pubmed-article:9588169 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9588169 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9588169 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9588169 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9588169 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9588169 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9588169 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9588169 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9588169 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9588169 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9588169 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9588169 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9588169 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9588169 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:9588169 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:9588169 | pubmed:author | pubmed-author:ZacharyII | lld:pubmed |
| pubmed-article:9588169 | pubmed:author | pubmed-author:AbediHH | lld:pubmed |
| pubmed-article:9588169 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9588169 | pubmed:day | 28 | lld:pubmed |
| pubmed-article:9588169 | pubmed:volume | 245 | lld:pubmed |
| pubmed-article:9588169 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9588169 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9588169 | pubmed:pagination | 646-50 | lld:pubmed |
| pubmed-article:9588169 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
| pubmed-article:9588169 | pubmed:meshHeading | pubmed-meshheading:9588169-... | lld:pubmed |
| pubmed-article:9588169 | pubmed:meshHeading | pubmed-meshheading:9588169-... | lld:pubmed |
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| pubmed-article:9588169 | pubmed:meshHeading | pubmed-meshheading:9588169-... | lld:pubmed |
| pubmed-article:9588169 | pubmed:meshHeading | pubmed-meshheading:9588169-... | lld:pubmed |
| pubmed-article:9588169 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9588169 | pubmed:articleTitle | Cytochalasin D stimulation of tyrosine phosphorylation and phosphotyrosine-associated kinase activity in vascular smooth muscle cells. | lld:pubmed |
| pubmed-article:9588169 | pubmed:affiliation | Department of Medicine, University College London, United Kingdom. | lld:pubmed |
| pubmed-article:9588169 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9588169 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9588169 | lld:pubmed |
