| pubmed-article:10403397 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10403397 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:10403397 | lifeskim:mentions | umls-concept:C0010934 | lld:lifeskim |
| pubmed-article:10403397 | lifeskim:mentions | umls-concept:C1510411 | lld:lifeskim |
| pubmed-article:10403397 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:10403397 | lifeskim:mentions | umls-concept:C1419798 | lld:lifeskim |
| pubmed-article:10403397 | lifeskim:mentions | umls-concept:C1333707 | lld:lifeskim |
| pubmed-article:10403397 | lifeskim:mentions | umls-concept:C1419799 | lld:lifeskim |
| pubmed-article:10403397 | lifeskim:mentions | umls-concept:C0282534 | lld:lifeskim |
| pubmed-article:10403397 | lifeskim:mentions | umls-concept:C0023688 | lld:lifeskim |
| pubmed-article:10403397 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:10403397 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:10403397 | pubmed:issue | 1-2 | lld:pubmed |
| pubmed-article:10403397 | pubmed:dateCreated | 1999-8-2 | lld:pubmed |
| pubmed-article:10403397 | pubmed:abstractText | Actinomycins, a family of bicyclic chromopeptide lactones with strong antineoplastic activity, were screened as inhibitors of Shc/Grb2 interaction in in vitro assay systems. To investigate the effects of actinomycin D on Shc/Grb2 interaction in cell-based experiments, we used SAA (normal hEGFR-overexpressed NIH3T3) cells and B104-1-1 (neu*-transformed NIH3T3) cells, because a large number of the Shc/Grb2 complexes were detected. Associated protein complexes containing Shc were immunoprecipitated from actinomycin D-treated cell lysates with polyclonal anti-Shc antibody. Then the association with Grb2 was assessed by immunoblotting with monoclonal anti-Grb2 antibody. The result of the immunoblotting experiment revealed that actinomycin D inhibited Shc/Grb2 interaction in a dose-dependent manner in both B104-1-1 and EGF-stimulated SAA cells. The inhibition of Shc/Grb2 interaction by actinomycin D in B104-1-1 cells also reduced tyrosine phosphorylation of MAP kinase (Erk1/Erk2), one of the major components in the Ras-MAP kinase signaling pathway. These results suggest that actinomycin D could be a non-phosphorylated natural and cellular membrane-permeable SH2 domain antagonist. | lld:pubmed |
| pubmed-article:10403397 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10403397 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10403397 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10403397 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10403397 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10403397 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10403397 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10403397 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10403397 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10403397 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10403397 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10403397 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10403397 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10403397 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10403397 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10403397 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10403397 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10403397 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:10403397 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:10403397 | pubmed:author | pubmed-author:KimH KHK | lld:pubmed |
| pubmed-article:10403397 | pubmed:author | pubmed-author:OTTJ LJL | lld:pubmed |
| pubmed-article:10403397 | pubmed:author | pubmed-author:BokS HSH | lld:pubmed |
| pubmed-article:10403397 | pubmed:author | pubmed-author:LeeE KEK | lld:pubmed |
| pubmed-article:10403397 | pubmed:author | pubmed-author:HanM YMY | lld:pubmed |
| pubmed-article:10403397 | pubmed:author | pubmed-author:ChoiJ DJD | lld:pubmed |
| pubmed-article:10403397 | pubmed:author | pubmed-author:KwonB MBM | lld:pubmed |
| pubmed-article:10403397 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10403397 | pubmed:day | 18 | lld:pubmed |
| pubmed-article:10403397 | pubmed:volume | 453 | lld:pubmed |
| pubmed-article:10403397 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10403397 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10403397 | pubmed:pagination | 174-8 | lld:pubmed |
| pubmed-article:10403397 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:10403397 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10403397 | pubmed:articleTitle | Actinomycin D as a novel SH2 domain ligand inhibits Shc/Grb2 interaction in B104-1-1 (neu*-transformed NIH3T3) and SAA (hEGFR-overexpressed NIH3T3) cells. | lld:pubmed |
| pubmed-article:10403397 | pubmed:affiliation | Korea Research Institute of Bioscience and Biotechnology, KIST, Taejon, South Korea. | lld:pubmed |
| pubmed-article:10403397 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10403397 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10403397 | lld:pubmed |
