| pubmed-article:21368131 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21368131 | lifeskim:mentions | umls-concept:C0521451 | lld:lifeskim |
| pubmed-article:21368131 | lifeskim:mentions | umls-concept:C1506024 | lld:lifeskim |
| pubmed-article:21368131 | lifeskim:mentions | umls-concept:C0140575 | lld:lifeskim |
| pubmed-article:21368131 | lifeskim:mentions | umls-concept:C2699153 | lld:lifeskim |
| pubmed-article:21368131 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
| pubmed-article:21368131 | lifeskim:mentions | umls-concept:C0675974 | lld:lifeskim |
| pubmed-article:21368131 | lifeskim:mentions | umls-concept:C0053241 | lld:lifeskim |
| pubmed-article:21368131 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:21368131 | pubmed:dateCreated | 2011-3-9 | lld:pubmed |
| pubmed-article:21368131 | pubmed:abstractText | Geldanamycin and its derivative 17AAG [17-(Allylamino)-17-demethoxygeldanamycin, telatinib] bind selectively to the Hsp90 chaperone protein and inhibit its function. We discovered that these drugs associate with mitochondria, specifically to the mitochondrial membrane voltage-dependent anion channel (VDAC) via a hydrophobic interaction that is independent of HSP90. In vitro, 17AAG functions as a Ca(2+) mitochondrial regulator similar to benzoquinone-ubiquinones like Ub0. All of these compounds increase intracellular Ca(2+) and diminish the plasma membrane cationic current, inhibiting urokinase activity and cell invasion. In contrast, the HSP90 inhibitor radicicol, lacking a bezoquinone moiety, has no measurable effect on cationic current and is less effective in influencing intercellular Ca(2+) concentration. We conclude that some of the effects of 17-AAG and other ansamycins are due to their effects on VDAC and that this may play a role in their clinical activity. | lld:pubmed |
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| pubmed-article:21368131 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21368131 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21368131 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:21368131 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21368131 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:21368131 | pubmed:issn | 1091-6490 | lld:pubmed |
| pubmed-article:21368131 | pubmed:author | pubmed-author:PyneG JGJ | lld:pubmed |
| pubmed-article:21368131 | pubmed:author | pubmed-author:Vande... | lld:pubmed |
| pubmed-article:21368131 | pubmed:author | pubmed-author:XuYongY | lld:pubmed |
| pubmed-article:21368131 | pubmed:author | pubmed-author:XuH EricHE | lld:pubmed |
| pubmed-article:21368131 | pubmed:author | pubmed-author:RosenNealN | lld:pubmed |
| pubmed-article:21368131 | pubmed:author | pubmed-author:ShenYuehaiY | lld:pubmed |
| pubmed-article:21368131 | pubmed:author | pubmed-author:ChenEdwinE | lld:pubmed |
| pubmed-article:21368131 | pubmed:author | pubmed-author:WondergemRobe... | lld:pubmed |
| pubmed-article:21368131 | pubmed:author | pubmed-author:OmarHananH | lld:pubmed |
| pubmed-article:21368131 | pubmed:author | pubmed-author:KeJiyuanJ | lld:pubmed |
| pubmed-article:21368131 | pubmed:author | pubmed-author:BradleyRobert... | lld:pubmed |
| pubmed-article:21368131 | pubmed:author | pubmed-author:CaveyGregG | lld:pubmed |
| pubmed-article:21368131 | pubmed:author | pubmed-author:WenkertDavidD | lld:pubmed |
| pubmed-article:21368131 | pubmed:author | pubmed-author:ThompsonRyanR | lld:pubmed |
| pubmed-article:21368131 | pubmed:author | pubmed-author:Daugherty-Hol... | lld:pubmed |
| pubmed-article:21368131 | pubmed:author | pubmed-author:Daughtery-Hol... | lld:pubmed |
| pubmed-article:21368131 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21368131 | pubmed:day | 8 | lld:pubmed |
| pubmed-article:21368131 | pubmed:volume | 108 | lld:pubmed |
| pubmed-article:21368131 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21368131 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21368131 | pubmed:pagination | 4105-10 | lld:pubmed |
| pubmed-article:21368131 | pubmed:dateRevised | 2011-9-13 | lld:pubmed |
| pubmed-article:21368131 | pubmed:meshHeading | pubmed-meshheading:21368131... | lld:pubmed |
| pubmed-article:21368131 | pubmed:meshHeading | pubmed-meshheading:21368131... | lld:pubmed |
| pubmed-article:21368131 | pubmed:meshHeading | pubmed-meshheading:21368131... | lld:pubmed |
| pubmed-article:21368131 | pubmed:meshHeading | pubmed-meshheading:21368131... | lld:pubmed |
| pubmed-article:21368131 | pubmed:meshHeading | pubmed-meshheading:21368131... | lld:pubmed |
| pubmed-article:21368131 | pubmed:meshHeading | pubmed-meshheading:21368131... | lld:pubmed |
| pubmed-article:21368131 | pubmed:meshHeading | pubmed-meshheading:21368131... | lld:pubmed |
| pubmed-article:21368131 | pubmed:meshHeading | pubmed-meshheading:21368131... | lld:pubmed |
| pubmed-article:21368131 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:21368131 | pubmed:articleTitle | Benzoquinone ansamycin 17AAG binds to mitochondrial voltage-dependent anion channel and inhibits cell invasion. | lld:pubmed |
| pubmed-article:21368131 | pubmed:affiliation | Laboratory of Molecular Oncology, Van Andel Research Institute, Grand Rapids, MI 49503, USA. | lld:pubmed |
| pubmed-article:21368131 | pubmed:publicationType | Journal Article | lld:pubmed |
