| pubmed-article:15115179 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15115179 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:15115179 | lifeskim:mentions | umls-concept:C0030016 | lld:lifeskim |
| pubmed-article:15115179 | lifeskim:mentions | umls-concept:C0441471 | lld:lifeskim |
| pubmed-article:15115179 | lifeskim:mentions | umls-concept:C0001721 | lld:lifeskim |
| pubmed-article:15115179 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:15115179 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:15115179 | lifeskim:mentions | umls-concept:C0027289 | lld:lifeskim |
| pubmed-article:15115179 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:15115179 | pubmed:dateCreated | 2004-4-29 | lld:pubmed |
| pubmed-article:15115179 | pubmed:abstractText | We had previously suggested that phosphorylation of proteins by mitochondrial kinases regulate the activity of NADH/CoQ oxidoreductase. Initial data showed that pyruvate dehydrogenase kinase (PDK) and cAMP-dependent protein kinase A (PKA) phosphorylate mitochondrial membrane proteins. Upon phosphorylation with crude PDK, mitochondria appeared to be deficient in NADH/cytochrome c reductase activity associated with increased superoxide production. Conversely, phosphorylation by PKA resulted in increased NADH/cytochrome c reductase activity and decreased superoxide formation. Current data confirms PKA involvement in regulating Complex I activity through phosphorylation of an 18 kDa subunit. Beef heart NADH/ cytochrome c reductase activity increases to 150% of control upon incubation with PKA and ATP-gamma-S. We have cloned the four human isoforms of PDK and purified beef heart Complex I. Incubation of mitochondria with PDK isoforms and ATP did not alter Complex I activity or superoxide production. Radiolabeling of mitochondria and purified Complex I with PDK failed to reveal phosphorylated proteins. | lld:pubmed |
| pubmed-article:15115179 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15115179 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15115179 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15115179 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15115179 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15115179 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:15115179 | pubmed:issn | 1572-3887 | lld:pubmed |
| pubmed-article:15115179 | pubmed:author | pubmed-author:RahaSandeepS | lld:pubmed |
| pubmed-article:15115179 | pubmed:author | pubmed-author:RobinsonBrian... | lld:pubmed |
| pubmed-article:15115179 | pubmed:author | pubmed-author:MajMary CMC | lld:pubmed |
| pubmed-article:15115179 | pubmed:author | pubmed-author:MyintTomokoT | lld:pubmed |
| pubmed-article:15115179 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15115179 | pubmed:volume | 23 | lld:pubmed |
| pubmed-article:15115179 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15115179 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15115179 | pubmed:pagination | 25-32 | lld:pubmed |
| pubmed-article:15115179 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:15115179 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15115179 | pubmed:articleTitle | Regulation of NADH/CoQ oxidoreductase: do phosphorylation events affect activity? | lld:pubmed |
| pubmed-article:15115179 | pubmed:affiliation | Metabolic Research Programme, The Hospital for Sick Children, 555 University Avenue, Toronto M5G 1X8, Canada. | lld:pubmed |
| pubmed-article:15115179 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15115179 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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