Linked Life Data

19460302

Source:http://linkedlifedata.com/resource/pubmed/id/19460302

Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:19460302rdf:typepubmed:Citationlld:pubmed
pubmed-article:19460302lifeskim:mentionsumls-concept:C0446013lld:lifeskim
pubmed-article:19460302lifeskim:mentionsumls-concept:C0242606lld:lifeskim
pubmed-article:19460302lifeskim:mentionsumls-concept:C0205245lld:lifeskim
pubmed-article:19460302lifeskim:mentionsumls-concept:C0348080lld:lifeskim
pubmed-article:19460302lifeskim:mentionsumls-concept:C0871161lld:lifeskim
pubmed-article:19460302lifeskim:mentionsumls-concept:C0258018lld:lifeskim
pubmed-article:19460302pubmed:issue2lld:pubmed
pubmed-article:19460302pubmed:dateCreated2009-5-25lld:pubmed
pubmed-article:19460302pubmed:abstractTextThe mitochondrial respiratory chain of Ustilago maydis contains two terminal oxidases, the cytochrome c oxidase (COX) and the alternative oxidase (AOX). To understand the biochemical events that control AOX activity, we studied the regulation and function of AOX under oxidative stress. The activity of this enzyme was increased by both pyruvate (K(05)=2.6 mM) and purine nucleotides (AMP, K(05)=600 microM) in mitochondria using succinate as respiratory substrate. When U.maydis cells were grown in the presence of antimycin A, the amount of AOX in mitochondria was markedly increased and its selectivity towards AMP and pyruvate changed, suggesting that post-translational events may play a role in the regulation of AOX activity under stress conditions. Addition of antimycin A to isolated mitochondria induced the inactivation of AOX, the formation of lipid peroxides and the loss of glutathione from mitochondria. The two last processes are probably related with the time dependent inactivation of AOX, in agreement with the inhibition of the enzyme by tert-butyl hydroperoxide. Our results suggest that the in vivo operation of AOX in U. maydis depends on the mitochondrial antioxidant machinery, including the glutathione linked systems.lld:pubmed
pubmed-article:19460302pubmed:languageenglld:pubmed
pubmed-article:19460302pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19460302pubmed:citationSubsetIMlld:pubmed
pubmed-article:19460302pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19460302pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19460302pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19460302pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19460302pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19460302pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19460302pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19460302pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19460302pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19460302pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19460302pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19460302pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19460302pubmed:statusMEDLINElld:pubmed
pubmed-article:19460302pubmed:monthAprlld:pubmed
pubmed-article:19460302pubmed:issn1872-8278lld:pubmed
pubmed-article:19460302pubmed:authorpubmed-author:VelázquezIIlld:pubmed
pubmed-article:19460302pubmed:authorpubmed-author:PardoJ PJPlld:pubmed
pubmed-article:19460302pubmed:authorpubmed-author:Sierra-Campos...lld:pubmed
pubmed-article:19460302pubmed:authorpubmed-author:Matuz-MaresDDlld:pubmed
pubmed-article:19460302pubmed:authorpubmed-author:Villavicencio...lld:pubmed
pubmed-article:19460302pubmed:issnTypeElectroniclld:pubmed
pubmed-article:19460302pubmed:volume9lld:pubmed
pubmed-article:19460302pubmed:ownerNLMlld:pubmed
pubmed-article:19460302pubmed:authorsCompleteYlld:pubmed
pubmed-article:19460302pubmed:pagination96-102lld:pubmed
pubmed-article:19460302pubmed:dateRevised2011-11-17lld:pubmed
pubmed-article:19460302pubmed:meshHeadingpubmed-meshheading:19460302...lld:pubmed
pubmed-article:19460302pubmed:meshHeadingpubmed-meshheading:19460302...lld:pubmed
pubmed-article:19460302pubmed:meshHeadingpubmed-meshheading:19460302...lld:pubmed
pubmed-article:19460302pubmed:meshHeadingpubmed-meshheading:19460302...lld:pubmed
pubmed-article:19460302pubmed:meshHeadingpubmed-meshheading:19460302...lld:pubmed
pubmed-article:19460302pubmed:meshHeadingpubmed-meshheading:19460302...lld:pubmed
pubmed-article:19460302pubmed:meshHeadingpubmed-meshheading:19460302...lld:pubmed
pubmed-article:19460302pubmed:meshHeadingpubmed-meshheading:19460302...lld:pubmed
pubmed-article:19460302pubmed:meshHeadingpubmed-meshheading:19460302...lld:pubmed
pubmed-article:19460302pubmed:meshHeadingpubmed-meshheading:19460302...lld:pubmed
pubmed-article:19460302pubmed:meshHeadingpubmed-meshheading:19460302...lld:pubmed
pubmed-article:19460302pubmed:meshHeadingpubmed-meshheading:19460302...lld:pubmed
pubmed-article:19460302pubmed:meshHeadingpubmed-meshheading:19460302...lld:pubmed
pubmed-article:19460302pubmed:meshHeadingpubmed-meshheading:19460302...lld:pubmed
pubmed-article:19460302pubmed:year2009lld:pubmed
pubmed-article:19460302pubmed:articleTitleFunctional properties of the Ustilago maydis alternative oxidase under oxidative stress conditions.lld:pubmed
pubmed-article:19460302pubmed:affiliationDepartamento de Bioquímica, Facultad de Medicina, Universidad Nacional Autónoma de México, Apartado Postal 70-159, Coyoacán 04510, México DF, México.lld:pubmed
pubmed-article:19460302pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:19460302pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
entrez-gene:3630862entrezgene:pubmedpubmed-article:19460302lld:entrezgene
http://linkedlifedata.com/r...entrezgene:pubmedpubmed-article:19460302lld:entrezgene