pubmed-article:10948261 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10948261 | lifeskim:mentions | umls-concept:C0085356 | lld:lifeskim |
pubmed-article:10948261 | lifeskim:mentions | umls-concept:C0025252 | lld:lifeskim |
pubmed-article:10948261 | lifeskim:mentions | umls-concept:C0017337 | lld:lifeskim |
pubmed-article:10948261 | lifeskim:mentions | umls-concept:C1623291 | lld:lifeskim |
pubmed-article:10948261 | lifeskim:mentions | umls-concept:C1159598 | lld:lifeskim |
pubmed-article:10948261 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
pubmed-article:10948261 | lifeskim:mentions | umls-concept:C2700640 | lld:lifeskim |
pubmed-article:10948261 | pubmed:issue | 8 | lld:pubmed |
pubmed-article:10948261 | pubmed:dateCreated | 2000-9-19 | lld:pubmed |
pubmed-article:10948261 | pubmed:abstractText | A key step for nitrate assimilation in photosynthetic eukaryotes occurs within chloroplasts, where nitrite is reduced to ammonium, which is incorporated into carbon skeletons. The Nar1 gene from Chlamydomonas reinhardtii is clustered with five other genes for nitrate assimilation, all of them regulated by nitrate. Sequence analysis of genomic DNA and cDNA of Nar1 and comparative studies of strains having or lacking Nar1 have been performed. The deduced amino acid sequence indicates that Nar1 encodes a chloroplast membrane protein with substantial identity to putative formate and nitrite transporters in bacteria. Use of antibodies against NAR1 has corroborated its location in the plastidic membrane. Characterization of strains having or lacking this gene suggests that NAR1 is involved in nitrite transport in plastids, which is critical for cell survival under limiting nitrate conditions, and controls the amount of nitrate incorporated by the cells under limiting CO(2) conditions. | lld:pubmed |
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pubmed-article:10948261 | pubmed:language | eng | lld:pubmed |
pubmed-article:10948261 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10948261 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:10948261 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10948261 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10948261 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10948261 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10948261 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10948261 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10948261 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10948261 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10948261 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10948261 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10948261 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10948261 | pubmed:month | Aug | lld:pubmed |
pubmed-article:10948261 | pubmed:issn | 1040-4651 | lld:pubmed |
pubmed-article:10948261 | pubmed:author | pubmed-author:FernándezEE | lld:pubmed |
pubmed-article:10948261 | pubmed:author | pubmed-author:GalvánAA | lld:pubmed |
pubmed-article:10948261 | pubmed:author | pubmed-author:RexachJJ | lld:pubmed |
pubmed-article:10948261 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10948261 | pubmed:volume | 12 | lld:pubmed |
pubmed-article:10948261 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10948261 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10948261 | pubmed:pagination | 1441-53 | lld:pubmed |
pubmed-article:10948261 | pubmed:dateRevised | 2010-9-14 | lld:pubmed |
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