pubmed-article:1303792 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1303792 | lifeskim:mentions | umls-concept:C0030738 | lld:lifeskim |
pubmed-article:1303792 | lifeskim:mentions | umls-concept:C1262903 | lld:lifeskim |
pubmed-article:1303792 | lifeskim:mentions | umls-concept:C0006556 | lld:lifeskim |
pubmed-article:1303792 | lifeskim:mentions | umls-concept:C0017824 | lld:lifeskim |
pubmed-article:1303792 | lifeskim:mentions | umls-concept:C1521991 | lld:lifeskim |
pubmed-article:1303792 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
pubmed-article:1303792 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:1303792 | pubmed:dateCreated | 1993-6-29 | lld:pubmed |
pubmed-article:1303792 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1303792 | pubmed:abstractText | A cDNA for pea glutathione reductase has been cloned and sequenced. The derived amino acid sequence of 562 residues shows a high degree of homology to the previously published GR sequences from human erythrocytes and from two prokaryotes: Escherichia coli and Pseudomonas aeruginosa. The pea enzyme differs from other GRs in having an N-terminal leader sequence of about 60-70 residues which may be a chloroplast transit peptide and a 20 amino acid C-terminal extension of unknown function. | lld:pubmed |
pubmed-article:1303792 | pubmed:language | eng | lld:pubmed |
pubmed-article:1303792 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1303792 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:1303792 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1303792 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1303792 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1303792 | pubmed:month | Jan | lld:pubmed |
pubmed-article:1303792 | pubmed:issn | 0960-7412 | lld:pubmed |
pubmed-article:1303792 | pubmed:author | pubmed-author:EdwardsE AEA | lld:pubmed |
pubmed-article:1303792 | pubmed:author | pubmed-author:MullineauxPP | lld:pubmed |
pubmed-article:1303792 | pubmed:author | pubmed-author:EnardCC | lld:pubmed |
pubmed-article:1303792 | pubmed:author | pubmed-author:CreissenGG | lld:pubmed |
pubmed-article:1303792 | pubmed:author | pubmed-author:WellburnAA | lld:pubmed |
pubmed-article:1303792 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1303792 | pubmed:volume | 2 | lld:pubmed |
pubmed-article:1303792 | pubmed:geneSymbol | GR | lld:pubmed |
pubmed-article:1303792 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1303792 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1303792 | pubmed:pagination | 129-31 | lld:pubmed |
pubmed-article:1303792 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:1303792 | pubmed:meshHeading | pubmed-meshheading:1303792-... | lld:pubmed |
pubmed-article:1303792 | pubmed:meshHeading | pubmed-meshheading:1303792-... | lld:pubmed |
pubmed-article:1303792 | pubmed:meshHeading | pubmed-meshheading:1303792-... | lld:pubmed |
pubmed-article:1303792 | pubmed:meshHeading | pubmed-meshheading:1303792-... | lld:pubmed |
pubmed-article:1303792 | pubmed:meshHeading | pubmed-meshheading:1303792-... | lld:pubmed |
pubmed-article:1303792 | pubmed:meshHeading | pubmed-meshheading:1303792-... | lld:pubmed |
pubmed-article:1303792 | pubmed:meshHeading | pubmed-meshheading:1303792-... | lld:pubmed |
pubmed-article:1303792 | pubmed:meshHeading | pubmed-meshheading:1303792-... | lld:pubmed |
pubmed-article:1303792 | pubmed:meshHeading | pubmed-meshheading:1303792-... | lld:pubmed |
pubmed-article:1303792 | pubmed:meshHeading | pubmed-meshheading:1303792-... | lld:pubmed |
pubmed-article:1303792 | pubmed:meshHeading | pubmed-meshheading:1303792-... | lld:pubmed |
pubmed-article:1303792 | pubmed:meshHeading | pubmed-meshheading:1303792-... | lld:pubmed |
pubmed-article:1303792 | pubmed:meshHeading | pubmed-meshheading:1303792-... | lld:pubmed |
pubmed-article:1303792 | pubmed:year | 1992 | lld:pubmed |
pubmed-article:1303792 | pubmed:articleTitle | Molecular characterization of glutathione reductase cDNAs from pea (Pisum sativum L.). | lld:pubmed |
pubmed-article:1303792 | pubmed:affiliation | John Innes Institute, AFRC Institute of Plant Science Research, John Innes Centre, Norwich, UK. | lld:pubmed |
pubmed-article:1303792 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:1303792 | pubmed:publicationType | Comparative Study | lld:pubmed |
pubmed-article:1303792 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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