pubmed-article:14550297 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:14550297 | lifeskim:mentions | umls-concept:C0023418 | lld:lifeskim |
pubmed-article:14550297 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:14550297 | lifeskim:mentions | umls-concept:C0162638 | lld:lifeskim |
pubmed-article:14550297 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
pubmed-article:14550297 | lifeskim:mentions | umls-concept:C1261552 | lld:lifeskim |
pubmed-article:14550297 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:14550297 | pubmed:dateCreated | 2003-10-10 | lld:pubmed |
pubmed-article:14550297 | pubmed:abstractText | The BH3-only protein, PUMA, plays an important role in p53-mediated apoptosis. The apoptotic effect of PUMA on the mitochondria was studied using a p53-negative, human leukemia K562 cell line. Overexpression of PUMA was accompanied by an increased Bax expression, Bax conformational change, and translocation to mitochondria. A PUMA-BH3 peptide can induce Bax conformational change, cytochrome c release, and reduction in the mitochondrial membrane potential (DeltaPsi(m)) in isolated K562 mitochondria and can be inhibited by Bcl-XL. The homo-dimer of Bax/Bax was also weakly shown after mitochondria were treated with PUMA-BH3 peptide but may not be lethal for PUMA-induced apoptosis in K562 cells. Our results suggest that PUMA-induced Bax conformational change and Bax translocation to mitochondria can be separate events and the conformational change in Bax is crucial for PUMA-induced mitochondrial dysfunction. | lld:pubmed |
pubmed-article:14550297 | pubmed:language | eng | lld:pubmed |
pubmed-article:14550297 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14550297 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:14550297 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14550297 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14550297 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14550297 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14550297 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14550297 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14550297 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14550297 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14550297 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14550297 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14550297 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14550297 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14550297 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:14550297 | pubmed:month | Oct | lld:pubmed |
pubmed-article:14550297 | pubmed:issn | 0006-291X | lld:pubmed |
pubmed-article:14550297 | pubmed:author | pubmed-author:OsL OLO | lld:pubmed |
pubmed-article:14550297 | pubmed:author | pubmed-author:NewlandAdrian... | lld:pubmed |
pubmed-article:14550297 | pubmed:author | pubmed-author:LiuFeng-TingF... | lld:pubmed |
pubmed-article:14550297 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:14550297 | pubmed:day | 24 | lld:pubmed |
pubmed-article:14550297 | pubmed:volume | 310 | lld:pubmed |
pubmed-article:14550297 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:14550297 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:14550297 | pubmed:pagination | 956-62 | lld:pubmed |
pubmed-article:14550297 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:14550297 | pubmed:meshHeading | pubmed-meshheading:14550297... | lld:pubmed |
pubmed-article:14550297 | pubmed:meshHeading | pubmed-meshheading:14550297... | lld:pubmed |
pubmed-article:14550297 | pubmed:meshHeading | pubmed-meshheading:14550297... | lld:pubmed |
pubmed-article:14550297 | pubmed:meshHeading | pubmed-meshheading:14550297... | lld:pubmed |
pubmed-article:14550297 | pubmed:meshHeading | pubmed-meshheading:14550297... | lld:pubmed |
pubmed-article:14550297 | pubmed:meshHeading | pubmed-meshheading:14550297... | lld:pubmed |
pubmed-article:14550297 | pubmed:meshHeading | pubmed-meshheading:14550297... | lld:pubmed |
pubmed-article:14550297 | pubmed:meshHeading | pubmed-meshheading:14550297... | lld:pubmed |
pubmed-article:14550297 | pubmed:meshHeading | pubmed-meshheading:14550297... | lld:pubmed |
pubmed-article:14550297 | pubmed:meshHeading | pubmed-meshheading:14550297... | lld:pubmed |
pubmed-article:14550297 | pubmed:meshHeading | pubmed-meshheading:14550297... | lld:pubmed |
pubmed-article:14550297 | pubmed:meshHeading | pubmed-meshheading:14550297... | lld:pubmed |
pubmed-article:14550297 | pubmed:meshHeading | pubmed-meshheading:14550297... | lld:pubmed |
pubmed-article:14550297 | pubmed:meshHeading | pubmed-meshheading:14550297... | lld:pubmed |
pubmed-article:14550297 | pubmed:meshHeading | pubmed-meshheading:14550297... | lld:pubmed |
pubmed-article:14550297 | pubmed:meshHeading | pubmed-meshheading:14550297... | lld:pubmed |
pubmed-article:14550297 | pubmed:meshHeading | pubmed-meshheading:14550297... | lld:pubmed |
pubmed-article:14550297 | pubmed:meshHeading | pubmed-meshheading:14550297... | lld:pubmed |
pubmed-article:14550297 | pubmed:meshHeading | pubmed-meshheading:14550297... | lld:pubmed |
pubmed-article:14550297 | pubmed:meshHeading | pubmed-meshheading:14550297... | lld:pubmed |
pubmed-article:14550297 | pubmed:meshHeading | pubmed-meshheading:14550297... | lld:pubmed |
pubmed-article:14550297 | pubmed:meshHeading | pubmed-meshheading:14550297... | lld:pubmed |
pubmed-article:14550297 | pubmed:meshHeading | pubmed-meshheading:14550297... | lld:pubmed |
pubmed-article:14550297 | pubmed:meshHeading | pubmed-meshheading:14550297... | lld:pubmed |
pubmed-article:14550297 | pubmed:meshHeading | pubmed-meshheading:14550297... | lld:pubmed |
pubmed-article:14550297 | pubmed:meshHeading | pubmed-meshheading:14550297... | lld:pubmed |
pubmed-article:14550297 | pubmed:year | 2003 | lld:pubmed |
pubmed-article:14550297 | pubmed:articleTitle | Bax conformational change is a crucial step for PUMA-mediated apoptosis in human leukemia. | lld:pubmed |
pubmed-article:14550297 | pubmed:affiliation | Department of Haematology, Barts and the London, Queen Mary's School of Medicine and Dentistry, University of London, London, UK. | lld:pubmed |
pubmed-article:14550297 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:14550297 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
entrez-gene:581 | entrezgene:pubmed | pubmed-article:14550297 | lld:entrezgene |
entrez-gene:27113 | entrezgene:pubmed | pubmed-article:14550297 | lld:entrezgene |
http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:14550297 | lld:entrezgene |
http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:14550297 | lld:entrezgene |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14550297 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14550297 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14550297 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14550297 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14550297 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14550297 | lld:pubmed |