| pubmed-article:1946430 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1946430 | lifeskim:mentions | umls-concept:C0085177 | lld:lifeskim |
| pubmed-article:1946430 | lifeskim:mentions | umls-concept:C1150944 | lld:lifeskim |
| pubmed-article:1946430 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:1946430 | pubmed:issue | 22 | lld:pubmed |
| pubmed-article:1946430 | pubmed:dateCreated | 1991-12-26 | lld:pubmed |
| pubmed-article:1946430 | pubmed:abstractText | A clone for the iron-responsive element (IRE)-binding protein (IRE-BP) has been transfected and expressed in mouse fibroblasts. The IRE-BP gene product binds IREs with high affinity and specificity. Amino acid alignments reveal that the IRE-BP is 30% identical to mitochondrial aconitase. The 18 active site residues of mitochondrial aconitase are identical to those in the IRE-BP, suggesting that the IRE-BP may possess aconitase activity. After purification of native IRE-BP and immunoaffinity purification of transfected and expressed IRE-BP, we demonstrate that the purified IRE-BP has aconitase activity. | lld:pubmed |
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| pubmed-article:1946430 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:1946430 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1946430 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1946430 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:1946430 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:1946430 | pubmed:author | pubmed-author:HarfordJ BJB | lld:pubmed |
| pubmed-article:1946430 | pubmed:author | pubmed-author:KlausnerR DRD | lld:pubmed |
| pubmed-article:1946430 | pubmed:author | pubmed-author:TaniMM | lld:pubmed |
| pubmed-article:1946430 | pubmed:author | pubmed-author:RouaultT ATA | lld:pubmed |
| pubmed-article:1946430 | pubmed:author | pubmed-author:OrloffD GDG | lld:pubmed |
| pubmed-article:1946430 | pubmed:author | pubmed-author:DowneyW EWE | lld:pubmed |
| pubmed-article:1946430 | pubmed:author | pubmed-author:PhilpottCC | lld:pubmed |
| pubmed-article:1946430 | pubmed:author | pubmed-author:KaptainSS | lld:pubmed |
| pubmed-article:1946430 | pubmed:author | pubmed-author:HaileDD | lld:pubmed |
| pubmed-article:1946430 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1946430 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:1946430 | pubmed:volume | 88 | lld:pubmed |
| pubmed-article:1946430 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1946430 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1946430 | pubmed:pagination | 10109-13 | lld:pubmed |
| pubmed-article:1946430 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:1946430 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1946430 | pubmed:articleTitle | A regulated RNA binding protein also possesses aconitase activity. | lld:pubmed |
| pubmed-article:1946430 | pubmed:affiliation | Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892. | lld:pubmed |
| pubmed-article:1946430 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1946430 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1946430 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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