pubmed-article:12728257 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12728257 | lifeskim:mentions | umls-concept:C0162638 | lld:lifeskim |
pubmed-article:12728257 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
pubmed-article:12728257 | lifeskim:mentions | umls-concept:C0683598 | lld:lifeskim |
pubmed-article:12728257 | lifeskim:mentions | umls-concept:C1948059 | lld:lifeskim |
pubmed-article:12728257 | lifeskim:mentions | umls-concept:C1720529 | lld:lifeskim |
pubmed-article:12728257 | lifeskim:mentions | umls-concept:C0332291 | lld:lifeskim |
pubmed-article:12728257 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:12728257 | pubmed:dateCreated | 2003-5-2 | lld:pubmed |
pubmed-article:12728257 | pubmed:abstractText | Bcr-Abl is one of the most potent antiapoptotic molecules and is the tyrosine-kinase implicated in Philadelphia (Ph) chromosome-positive leukemia. It is still obscure how Bcr-Abl provides the leukemic cell a strong resistance to chemotherapeutic drugs. A rational drug development produced a specific inhibitor of the catalytic activity of Bcr-Abl called STI571. This drug was shown to eliminate Bcr-Abl-positive cells both in vitro and in vivo, although resistant cells may appear in culture and relapse occurs in some patients. In the study described here, Bcr-Abl-positive cells treated with tyrosine-kinase inhibitors such as herbimycin A, genistein or STI571 lost their phosphotyrosine-containing proteins, but were still extremely resistant to apoptosis. Therefore, in the absence of tyrosine-kinase activity, Bcr-Abl-positive cells continue to signal biochemically to prevent apoptosis induced by chemotherapeutic drugs. We propose that secondary antiapoptotic signals are entirely responsible for the resistance of Bcr-Abl-positive cells. Precise determination of such signals and rational drug development against them should improve the means to combat Ph chromosome-positive leukemia. | lld:pubmed |
pubmed-article:12728257 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12728257 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12728257 | pubmed:language | eng | lld:pubmed |
pubmed-article:12728257 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12728257 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:12728257 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12728257 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12728257 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12728257 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12728257 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12728257 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12728257 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12728257 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12728257 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12728257 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12728257 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12728257 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12728257 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12728257 | pubmed:month | May | lld:pubmed |
pubmed-article:12728257 | pubmed:issn | 1350-9047 | lld:pubmed |
pubmed-article:12728257 | pubmed:author | pubmed-author:GreenD RDR | lld:pubmed |
pubmed-article:12728257 | pubmed:author | pubmed-author:RussoF OFO | lld:pubmed |
pubmed-article:12728257 | pubmed:author | pubmed-author:Amarante-Mend... | lld:pubmed |
pubmed-article:12728257 | pubmed:author | pubmed-author:BrumattiGG | lld:pubmed |
pubmed-article:12728257 | pubmed:author | pubmed-author:Bueno-da-Silv... | lld:pubmed |
pubmed-article:12728257 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12728257 | pubmed:volume | 10 | lld:pubmed |
pubmed-article:12728257 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12728257 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12728257 | pubmed:pagination | 592-8 | lld:pubmed |
pubmed-article:12728257 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
pubmed-article:12728257 | pubmed:meshHeading | pubmed-meshheading:12728257... | lld:pubmed |
pubmed-article:12728257 | pubmed:meshHeading | pubmed-meshheading:12728257... | lld:pubmed |
pubmed-article:12728257 | pubmed:meshHeading | pubmed-meshheading:12728257... | lld:pubmed |
pubmed-article:12728257 | pubmed:meshHeading | pubmed-meshheading:12728257... | lld:pubmed |
pubmed-article:12728257 | pubmed:meshHeading | pubmed-meshheading:12728257... | lld:pubmed |
pubmed-article:12728257 | pubmed:meshHeading | pubmed-meshheading:12728257... | lld:pubmed |
pubmed-article:12728257 | pubmed:meshHeading | pubmed-meshheading:12728257... | lld:pubmed |
pubmed-article:12728257 | pubmed:meshHeading | pubmed-meshheading:12728257... | lld:pubmed |
pubmed-article:12728257 | pubmed:meshHeading | pubmed-meshheading:12728257... | lld:pubmed |
pubmed-article:12728257 | pubmed:meshHeading | pubmed-meshheading:12728257... | lld:pubmed |
pubmed-article:12728257 | pubmed:meshHeading | pubmed-meshheading:12728257... | lld:pubmed |
pubmed-article:12728257 | pubmed:meshHeading | pubmed-meshheading:12728257... | lld:pubmed |
pubmed-article:12728257 | pubmed:meshHeading | pubmed-meshheading:12728257... | lld:pubmed |
pubmed-article:12728257 | pubmed:meshHeading | pubmed-meshheading:12728257... | lld:pubmed |
pubmed-article:12728257 | pubmed:meshHeading | pubmed-meshheading:12728257... | lld:pubmed |
pubmed-article:12728257 | pubmed:meshHeading | pubmed-meshheading:12728257... | lld:pubmed |
pubmed-article:12728257 | pubmed:meshHeading | pubmed-meshheading:12728257... | lld:pubmed |
pubmed-article:12728257 | pubmed:year | 2003 | lld:pubmed |
pubmed-article:12728257 | pubmed:articleTitle | Bcr-Abl-mediated resistance to apoptosis is independent of constant tyrosine-kinase activity. | lld:pubmed |
pubmed-article:12728257 | pubmed:affiliation | Department of Immunology, Institute of Biomedical Sciences, University of São Paulo, Brazil. | lld:pubmed |
pubmed-article:12728257 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:12728257 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:12728257 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |