| pubmed-article:12150982 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12150982 | lifeskim:mentions | umls-concept:C0162638 | lld:lifeskim |
| pubmed-article:12150982 | lifeskim:mentions | umls-concept:C0032824 | lld:lifeskim |
| pubmed-article:12150982 | lifeskim:mentions | umls-concept:C1416546 | lld:lifeskim |
| pubmed-article:12150982 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:12150982 | lifeskim:mentions | umls-concept:C0001259 | lld:lifeskim |
| pubmed-article:12150982 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:12150982 | pubmed:dateCreated | 2002-8-1 | lld:pubmed |
| pubmed-article:12150982 | pubmed:abstractText | Several cytostatic agents are known to induce apoptosis in T-leukemic cells. Although a variety of studies show the central role of apoptosis in cytostatic drug-induced cell death, many molecular details require definition. Here, we demonstrate that cells genetically deficient for the potassium channel Kv1.3 are resistant to apoptosis initiated by the cytostatic drug actinomycin D. Retransfection of Kv1.3 restores sensitivity of the cells to actinomycin D. Cells lacking Kv1.3 fail to respond to actinomycin D with DNA fragmentation, release of cytochrome c, and loss of mitochondrial membrane potential (Delta Psi(m)), while cells functionally expressing Kv1.3 rapidly undergo those changes indicative for apoptosis. The data indicate a central role of the ion channel Kv1.3 in actinomycin D-triggered apoptosis. | lld:pubmed |
| pubmed-article:12150982 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12150982 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12150982 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12150982 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12150982 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12150982 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12150982 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12150982 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12150982 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12150982 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12150982 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:12150982 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:12150982 | pubmed:author | pubmed-author:BockJürgenJ | lld:pubmed |
| pubmed-article:12150982 | pubmed:author | pubmed-author:GulbinsErichE | lld:pubmed |
| pubmed-article:12150982 | pubmed:author | pubmed-author:JekleAndreasA | lld:pubmed |
| pubmed-article:12150982 | pubmed:author | pubmed-author:SzabóIldikòI | lld:pubmed |
| pubmed-article:12150982 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12150982 | pubmed:day | 12 | lld:pubmed |
| pubmed-article:12150982 | pubmed:volume | 295 | lld:pubmed |
| pubmed-article:12150982 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12150982 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12150982 | pubmed:pagination | 526-31 | lld:pubmed |
| pubmed-article:12150982 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:12150982 | pubmed:meshHeading | pubmed-meshheading:12150982... | lld:pubmed |
| pubmed-article:12150982 | pubmed:meshHeading | pubmed-meshheading:12150982... | lld:pubmed |
| pubmed-article:12150982 | pubmed:meshHeading | pubmed-meshheading:12150982... | lld:pubmed |
| pubmed-article:12150982 | pubmed:meshHeading | pubmed-meshheading:12150982... | lld:pubmed |
| pubmed-article:12150982 | pubmed:meshHeading | pubmed-meshheading:12150982... | lld:pubmed |
| pubmed-article:12150982 | pubmed:meshHeading | pubmed-meshheading:12150982... | lld:pubmed |
| pubmed-article:12150982 | pubmed:meshHeading | pubmed-meshheading:12150982... | lld:pubmed |
| pubmed-article:12150982 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12150982 | pubmed:articleTitle | Actinomycin D-induced apoptosis involves the potassium channel Kv1.3. | lld:pubmed |
| pubmed-article:12150982 | pubmed:affiliation | Department of Immunology, St. Jude Children's Research Hospital, 332 North Lauderdale, Memphis, TN 38105, USA. | lld:pubmed |
| pubmed-article:12150982 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12150982 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12150982 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:3738 | entrezgene:pubmed | pubmed-article:12150982 | lld:entrezgene |
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