| pubmed-article:15923083 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15923083 | lifeskim:mentions | umls-concept:C0521451 | lld:lifeskim |
| pubmed-article:15923083 | lifeskim:mentions | umls-concept:C0010760 | lld:lifeskim |
| pubmed-article:15923083 | lifeskim:mentions | umls-concept:C0669368 | lld:lifeskim |
| pubmed-article:15923083 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:15923083 | pubmed:dateCreated | 2005-6-27 | lld:pubmed |
| pubmed-article:15923083 | pubmed:abstractText | Nitric oxide (NO) regulates key aspects of cell metabolism through reversible inhibition of cytochrome c oxidase (CcOX), the terminal electron acceptor (complex IV) of the mitochondrial respiratory chain, in competition with oxygen. Recently, a constitutive mitochondrial NOS corresponding to a neuronal NOS-I isoform (mtNOS-I) has been identified in several tissues. The role of this enzyme might be to generate NO close enough to its target without a significant overall increase in cellular NO concentrations. An effective, selective, and specific NO action might be guaranteed further by a physical interaction between mtNOS-I and CcOX. This possibility has never been investigated. Here we demonstrate that mtNOS-I is associated with CcOX, as proven by electron microscopic immunolocalization and co-immunoprecipitation studies. By affinity chromatography, we found that association is due to physical interaction of mtNOS-I with the C-terminal peptide of the Va subunit of CcOX, which displays a consensus sequence for binding to the PDZ domain of mtNOS-I previously unreported for CcOX. The molecular details of the interaction have been analyzed by means of molecular modeling and molecular dynamics simulations. This is the first evidence of a protein-protein interaction mediated by PDZ domains involving CcOX. | lld:pubmed |
| pubmed-article:15923083 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15923083 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15923083 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15923083 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15923083 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15923083 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15923083 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15923083 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15923083 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15923083 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:15923083 | pubmed:issn | 0304-3940 | lld:pubmed |
| pubmed-article:15923083 | pubmed:author | pubmed-author:ColasantiMarc... | lld:pubmed |
| pubmed-article:15923083 | pubmed:author | pubmed-author:PersichiniTiz... | lld:pubmed |
| pubmed-article:15923083 | pubmed:author | pubmed-author:VenturiniGior... | lld:pubmed |
| pubmed-article:15923083 | pubmed:author | pubmed-author:ClementiEmili... | lld:pubmed |
| pubmed-article:15923083 | pubmed:author | pubmed-author:PolticelliFab... | lld:pubmed |
| pubmed-article:15923083 | pubmed:author | pubmed-author:MorenoSandraS | lld:pubmed |
| pubmed-article:15923083 | pubmed:author | pubmed-author:MazzoneValeri... | lld:pubmed |
| pubmed-article:15923083 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15923083 | pubmed:day | 26 | lld:pubmed |
| pubmed-article:15923083 | pubmed:volume | 384 | lld:pubmed |
| pubmed-article:15923083 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15923083 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15923083 | pubmed:pagination | 254-9 | lld:pubmed |
| pubmed-article:15923083 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:15923083 | pubmed:meshHeading | pubmed-meshheading:15923083... | lld:pubmed |
| pubmed-article:15923083 | pubmed:meshHeading | pubmed-meshheading:15923083... | lld:pubmed |
| pubmed-article:15923083 | pubmed:meshHeading | pubmed-meshheading:15923083... | lld:pubmed |
| pubmed-article:15923083 | pubmed:meshHeading | pubmed-meshheading:15923083... | lld:pubmed |
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| pubmed-article:15923083 | pubmed:meshHeading | pubmed-meshheading:15923083... | lld:pubmed |
| pubmed-article:15923083 | pubmed:meshHeading | pubmed-meshheading:15923083... | lld:pubmed |
| pubmed-article:15923083 | pubmed:meshHeading | pubmed-meshheading:15923083... | lld:pubmed |
| pubmed-article:15923083 | pubmed:meshHeading | pubmed-meshheading:15923083... | lld:pubmed |
| pubmed-article:15923083 | pubmed:meshHeading | pubmed-meshheading:15923083... | lld:pubmed |
| pubmed-article:15923083 | pubmed:meshHeading | pubmed-meshheading:15923083... | lld:pubmed |
| pubmed-article:15923083 | pubmed:meshHeading | pubmed-meshheading:15923083... | lld:pubmed |
| pubmed-article:15923083 | pubmed:meshHeading | pubmed-meshheading:15923083... | lld:pubmed |
| pubmed-article:15923083 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15923083 | pubmed:articleTitle | Mitochondrial type I nitric oxide synthase physically interacts with cytochrome c oxidase. | lld:pubmed |
| pubmed-article:15923083 | pubmed:affiliation | Department of Biology-LIME, University ROMA TRE, Viale Guglielmo Marconi 446, 00146 Rome, Italy. | lld:pubmed |
| pubmed-article:15923083 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15923083 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:12858 | entrezgene:pubmed | pubmed-article:15923083 | lld:entrezgene |
| entrez-gene:18125 | entrezgene:pubmed | pubmed-article:15923083 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:15923083 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15923083 | lld:pubmed |
