| pubmed-article:9988709 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9988709 | lifeskim:mentions | umls-concept:C1882726 | lld:lifeskim |
| pubmed-article:9988709 | lifeskim:mentions | umls-concept:C0521451 | lld:lifeskim |
| pubmed-article:9988709 | lifeskim:mentions | umls-concept:C0039941 | lld:lifeskim |
| pubmed-article:9988709 | lifeskim:mentions | umls-concept:C0009017 | lld:lifeskim |
| pubmed-article:9988709 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:9988709 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:9988709 | pubmed:dateCreated | 1999-3-18 | lld:pubmed |
| pubmed-article:9988709 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9988709 | pubmed:abstractText | A thioredoxin reductase (TrxR), named here TrxR2, that did not react with antibodies to the previously identified TrxR (now named TrxR1) was purified from rat liver. Like TrxR1, TrxR2 was a dimeric enzyme containing selenocysteine (Secys) as the COOH-terminal penultimate residue. A cDNA encoding TrxR2 was cloned from rat liver; the open reading frame predicts a polypeptide of 526 amino acids with a COOH-terminal Gly-Cys-Secys-Gly motif provided that an in-frame TGA codon encodes Secys. The 3'-untranslated region of the cDNA contains a canonical Secys insertion sequence element. The deduced amino acid sequence of TrxR2 shows 54% identity to that of TrxR1 and contained 36 additional residues upstream of the experimentally determined NH2-terminal sequence. The sequence of this 36-residue region is typical of that of a mitochondrial leader peptide. Immunoblot analysis confirmed that TrxR2 is localized almost exclusively in mitochondria, whereas TrxR1 is a cytosolic protein. Unlike TrxR1, which was expressed at a level of 0.6 to 1.6 microgram/milligram of total soluble protein in all rat tissues examined, TrxR2 was relatively abundant (0.3 to 0.6 microgram/mg) only in liver, kidney, adrenal gland, and heart. The specific localization of TrxR2 in mitochondria, together with the previous identification of mitochondria-specific thioredoxin and thioredoxin-dependent peroxidase, suggest that these three proteins provide a primary line of defense against H2O2 produced by the mitochondrial respiratory chain. | lld:pubmed |
| pubmed-article:9988709 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9988709 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9988709 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9988709 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9988709 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9988709 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9988709 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9988709 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:9988709 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:9988709 | pubmed:author | pubmed-author:RheeS GSG | lld:pubmed |
| pubmed-article:9988709 | pubmed:author | pubmed-author:GinsburgAA | lld:pubmed |
| pubmed-article:9988709 | pubmed:author | pubmed-author:LebS MSM | lld:pubmed |
| pubmed-article:9988709 | pubmed:author | pubmed-author:CHUS PSP | lld:pubmed |
| pubmed-article:9988709 | pubmed:author | pubmed-author:LevineR LRL | lld:pubmed |
| pubmed-article:9988709 | pubmed:author | pubmed-author:KwonK SKS | lld:pubmed |
| pubmed-article:9988709 | pubmed:author | pubmed-author:YoonH WHW | lld:pubmed |
| pubmed-article:9988709 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9988709 | pubmed:day | 19 | lld:pubmed |
| pubmed-article:9988709 | pubmed:volume | 274 | lld:pubmed |
| pubmed-article:9988709 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9988709 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9988709 | pubmed:pagination | 4722-34 | lld:pubmed |
| pubmed-article:9988709 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:9988709 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:9988709 | pubmed:articleTitle | Molecular cloning and characterization of a mitochondrial selenocysteine-containing thioredoxin reductase from rat liver. | lld:pubmed |
| pubmed-article:9988709 | pubmed:affiliation | Laboratory of Cell Signaling, NHLBI, National Institutes of Health, Bethesda, Maryland 20892, USA. | lld:pubmed |
| pubmed-article:9988709 | pubmed:publicationType | Journal Article | lld:pubmed |
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