| pubmed-article:17112592 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17112592 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:17112592 | lifeskim:mentions | umls-concept:C0007587 | lld:lifeskim |
| pubmed-article:17112592 | lifeskim:mentions | umls-concept:C0038838 | lld:lifeskim |
| pubmed-article:17112592 | lifeskim:mentions | umls-concept:C1521840 | lld:lifeskim |
| pubmed-article:17112592 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:17112592 | pubmed:dateCreated | 2007-1-16 | lld:pubmed |
| pubmed-article:17112592 | pubmed:abstractText | The cell viability of human cancer cell lines treated with [5,10-bis(N-methyl-4-pyridyl)-15,20-diphenyl]porphinatoiron(III) (cis-FeMPy(2)P(2)P) has been estimated. The cis-FeMPy(2)P(2)P is a superoxide dismutase (SOD) mimic in vitro that exhibited a significant toxicity in cancer cell lines. This toxicity is rather due to pro-oxidant properties of the iron-porphyrin in vivo. We have demonstrated that there was the relationship between the LD(50) values calculated from the viability of cancer cell lines treated with cis-FeMPy(2)P(2)P and the SOD activities of the cell lines. Furthermore, the inhibition of SOD by antisense S-oligonucleotide increased the cytotoxic effect of cis-FeMPy(2)P(2)P against cancer cells. These results suggest that SOD is a target enzyme for the cell death induced by cis-FeMPy(2)P(2)P as a new class of anticancer agents. | lld:pubmed |
| pubmed-article:17112592 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17112592 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17112592 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17112592 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17112592 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17112592 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17112592 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17112592 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17112592 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17112592 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17112592 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17112592 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:17112592 | pubmed:issn | 0162-0134 | lld:pubmed |
| pubmed-article:17112592 | pubmed:author | pubmed-author:NagaokaShojiS | lld:pubmed |
| pubmed-article:17112592 | pubmed:author | pubmed-author:KawakamiHiroy... | lld:pubmed |
| pubmed-article:17112592 | pubmed:author | pubmed-author:KasugaiNobuyo... | lld:pubmed |
| pubmed-article:17112592 | pubmed:author | pubmed-author:KubotaSunaoS | lld:pubmed |
| pubmed-article:17112592 | pubmed:author | pubmed-author:AsayamaShoich... | lld:pubmed |
| pubmed-article:17112592 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17112592 | pubmed:volume | 101 | lld:pubmed |
| pubmed-article:17112592 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17112592 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17112592 | pubmed:pagination | 261-6 | lld:pubmed |
| pubmed-article:17112592 | pubmed:meshHeading | pubmed-meshheading:17112592... | lld:pubmed |
| pubmed-article:17112592 | pubmed:meshHeading | pubmed-meshheading:17112592... | lld:pubmed |
| pubmed-article:17112592 | pubmed:meshHeading | pubmed-meshheading:17112592... | lld:pubmed |
| pubmed-article:17112592 | pubmed:meshHeading | pubmed-meshheading:17112592... | lld:pubmed |
| pubmed-article:17112592 | pubmed:meshHeading | pubmed-meshheading:17112592... | lld:pubmed |
| pubmed-article:17112592 | pubmed:meshHeading | pubmed-meshheading:17112592... | lld:pubmed |
| pubmed-article:17112592 | pubmed:meshHeading | pubmed-meshheading:17112592... | lld:pubmed |
| pubmed-article:17112592 | pubmed:meshHeading | pubmed-meshheading:17112592... | lld:pubmed |
| pubmed-article:17112592 | pubmed:meshHeading | pubmed-meshheading:17112592... | lld:pubmed |
| pubmed-article:17112592 | pubmed:meshHeading | pubmed-meshheading:17112592... | lld:pubmed |
| pubmed-article:17112592 | pubmed:meshHeading | pubmed-meshheading:17112592... | lld:pubmed |
| pubmed-article:17112592 | pubmed:meshHeading | pubmed-meshheading:17112592... | lld:pubmed |
| pubmed-article:17112592 | pubmed:meshHeading | pubmed-meshheading:17112592... | lld:pubmed |
| pubmed-article:17112592 | pubmed:meshHeading | pubmed-meshheading:17112592... | lld:pubmed |
| pubmed-article:17112592 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17112592 | pubmed:articleTitle | Superoxide dismutase as a target enzyme for Fe-porphyrin-induced cell death. | lld:pubmed |
| pubmed-article:17112592 | pubmed:affiliation | Department of Applied Chemistry, Tokyo Metropolitan University, 1-1 Minami-Osawa, Hachioji, Tokyo 192-0397, Japan. asayama-shoichiro@c.metro-u.ac.jp | lld:pubmed |
| pubmed-article:17112592 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17112592 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
