pubmed-article:1829499 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1829499 | lifeskim:mentions | umls-concept:C0027923 | lld:lifeskim |
pubmed-article:1829499 | lifeskim:mentions | umls-concept:C0017366 | lld:lifeskim |
pubmed-article:1829499 | lifeskim:mentions | umls-concept:C0004793 | lld:lifeskim |
pubmed-article:1829499 | lifeskim:mentions | umls-concept:C0068800 | lld:lifeskim |
pubmed-article:1829499 | lifeskim:mentions | umls-concept:C0243127 | lld:lifeskim |
pubmed-article:1829499 | lifeskim:mentions | umls-concept:C1622984 | lld:lifeskim |
pubmed-article:1829499 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:1829499 | lifeskim:mentions | umls-concept:C0443331 | lld:lifeskim |
pubmed-article:1829499 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:1829499 | pubmed:dateCreated | 1991-8-6 | lld:pubmed |
pubmed-article:1829499 | pubmed:abstractText | The nit-3 gene of the filamentous fungus Neurospora crassa encodes the enzyme nitrate reductase, which catalyzes the first reductive step in the highly regulated nitrate assimilatory pathway. The nucleotide sequence of nit-3 was determined and translates to a protein of 982 amino acid residues with a molecular weight of approximately 108 kDa. Comparison of the deduced nit-3 protein sequence with the nitrate reductase protein sequences of other fungi and higher plants revealed that a significant amount of homology exists, particularly within the three cofactor-binding domains for molybdenum, heme and FAD. The synthesis and turnover of the nit-3 mRNA were also examined and found to occur rapidly and efficiently under changing metabolic conditions. | lld:pubmed |
pubmed-article:1829499 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1829499 | pubmed:language | eng | lld:pubmed |
pubmed-article:1829499 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1829499 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:1829499 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1829499 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1829499 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1829499 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1829499 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1829499 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1829499 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1829499 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1829499 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1829499 | pubmed:month | Jun | lld:pubmed |
pubmed-article:1829499 | pubmed:issn | 0026-8925 | lld:pubmed |
pubmed-article:1829499 | pubmed:author | pubmed-author:MarzlufG AGA | lld:pubmed |
pubmed-article:1829499 | pubmed:author | pubmed-author:FuY HYH | lld:pubmed |
pubmed-article:1829499 | pubmed:author | pubmed-author:OkamotoP MPM | lld:pubmed |
pubmed-article:1829499 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1829499 | pubmed:volume | 227 | lld:pubmed |
pubmed-article:1829499 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1829499 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1829499 | pubmed:pagination | 213-23 | lld:pubmed |
pubmed-article:1829499 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:1829499 | pubmed:year | 1991 | lld:pubmed |
pubmed-article:1829499 | pubmed:articleTitle | Nit-3, the structural gene of nitrate reductase in Neurospora crassa: nucleotide sequence and regulation of mRNA synthesis and turnover. | lld:pubmed |
pubmed-article:1829499 | pubmed:affiliation | Department of Biochemistry, Ohio State University, Columbus 43210. | lld:pubmed |
pubmed-article:1829499 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:1829499 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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