pubmed-article:12628922 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12628922 | lifeskim:mentions | umls-concept:C0162638 | lld:lifeskim |
pubmed-article:12628922 | lifeskim:mentions | umls-concept:C0031727 | lld:lifeskim |
pubmed-article:12628922 | lifeskim:mentions | umls-concept:C1446409 | lld:lifeskim |
pubmed-article:12628922 | lifeskim:mentions | umls-concept:C0079419 | lld:lifeskim |
pubmed-article:12628922 | lifeskim:mentions | umls-concept:C1333206 | lld:lifeskim |
pubmed-article:12628922 | lifeskim:mentions | umls-concept:C0015744 | lld:lifeskim |
pubmed-article:12628922 | lifeskim:mentions | umls-concept:C2911691 | lld:lifeskim |
pubmed-article:12628922 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:12628922 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
pubmed-article:12628922 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:12628922 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:12628922 | pubmed:dateCreated | 2003-3-11 | lld:pubmed |
pubmed-article:12628922 | pubmed:abstractText | DDR1, discoidin domain receptor 1, belongs to a subfamily of tyrosine kinase receptors with an extracellular domain homologous to Dictyostellium discoideum protein discoidin 1. We showed that DDR1 is a direct p53 transcriptional target, and that DNA damage induced a p53-dependent DDR1 response associated with activation of its tyrosine kinase. We further demonstrated that DDR1 activated the MAPK cascade in a Ras-dependent manner. Whereas levels of p53, phosphoserine-15 p53, p21, ARF and Bcl-X(L) were increased in response to exogenous overexpression of activated DDR1, dominant-negative DDR1 inhibited irradiation-induced MAPK activation and p53, phosphoserine-15 p53, as well as induced p21 and DDR1 levels, suggesting that DDR1 functions in a feedforward loop to increase p53 levels and at least some of its effectors. Nonetheless, inhibition of DDR1 function resulted in strikingly increased apoptosis of wild-type p53-containing cells in response to genotoxic stress through a caspase-dependent pathway. These results strongly imply that this p53 response gene must predominately act to alleviate the adverse effects of stress induced by p53 on its target cell. | lld:pubmed |
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pubmed-article:12628922 | pubmed:language | eng | lld:pubmed |
pubmed-article:12628922 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12628922 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:12628922 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12628922 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:12628922 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12628922 | pubmed:month | Mar | lld:pubmed |
pubmed-article:12628922 | pubmed:issn | 0261-4189 | lld:pubmed |
pubmed-article:12628922 | pubmed:author | pubmed-author:SalehM NMN | lld:pubmed |
pubmed-article:12628922 | pubmed:author | pubmed-author:LiFangF | lld:pubmed |
pubmed-article:12628922 | pubmed:author | pubmed-author:YancopoulosGe... | lld:pubmed |
pubmed-article:12628922 | pubmed:author | pubmed-author:AaronsonStuar... | lld:pubmed |
pubmed-article:12628922 | pubmed:author | pubmed-author:OngusahaPat... | lld:pubmed |
pubmed-article:12628922 | pubmed:author | pubmed-author:KimJong-ilJI | lld:pubmed |
pubmed-article:12628922 | pubmed:author | pubmed-author:WongTai WTW | lld:pubmed |
pubmed-article:12628922 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12628922 | pubmed:day | 17 | lld:pubmed |
pubmed-article:12628922 | pubmed:volume | 22 | lld:pubmed |
pubmed-article:12628922 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12628922 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12628922 | pubmed:pagination | 1289-301 | lld:pubmed |
pubmed-article:12628922 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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