| pubmed-article:1924383 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1924383 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
| pubmed-article:1924383 | lifeskim:mentions | umls-concept:C0040648 | lld:lifeskim |
| pubmed-article:1924383 | lifeskim:mentions | umls-concept:C1538613 | lld:lifeskim |
| pubmed-article:1924383 | lifeskim:mentions | umls-concept:C0162610 | lld:lifeskim |
| pubmed-article:1924383 | lifeskim:mentions | umls-concept:C0449205 | lld:lifeskim |
| pubmed-article:1924383 | pubmed:issue | 20 | lld:pubmed |
| pubmed-article:1924383 | pubmed:dateCreated | 1991-11-15 | lld:pubmed |
| pubmed-article:1924383 | pubmed:abstractText | The cysteine-rich LIM motif is highly conserved between invertebrates and mammals. This motif shows similarity both to proteins that bind zinc and to ferredoxins, which contain iron-sulfur clusters. Two tandem copies of the LIM motif are found in a number of presumptive transcription factors, including the protein product of the Caenorhabditis elegans cell-lineage gene lin-11. To investigate the possible metal-binding properties of the LIM region of the lin-11 protein, we expressed and purified a 151-amino acid peptide containing the tandem LIM motifs. The purified peptide binds both zinc (two atoms per protein molecule) and iron (as a redox-active iron-sulfur cluster, with four atoms of iron and four atoms of inorganic sulfide per protein molecule). These observations suggest that the LIM motif is a metallodomain that might function in a redox-sensitive regulation of transcription. | lld:pubmed |
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| pubmed-article:1924383 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1924383 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1924383 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1924383 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1924383 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:1924383 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:1924383 | pubmed:author | pubmed-author:WalshC TCT | lld:pubmed |
| pubmed-article:1924383 | pubmed:author | pubmed-author:HorvitzH RHR | lld:pubmed |
| pubmed-article:1924383 | pubmed:author | pubmed-author:ReichertJJ | lld:pubmed |
| pubmed-article:1924383 | pubmed:author | pubmed-author:LiP MPM | lld:pubmed |
| pubmed-article:1924383 | pubmed:author | pubmed-author:FreydGG | lld:pubmed |
| pubmed-article:1924383 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1924383 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:1924383 | pubmed:volume | 88 | lld:pubmed |
| pubmed-article:1924383 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1924383 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1924383 | pubmed:pagination | 9210-3 | lld:pubmed |
| pubmed-article:1924383 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:1924383 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1924383 | pubmed:articleTitle | The LIM region of a presumptive Caenorhabditis elegans transcription factor is an iron-sulfur- and zinc-containing metallodomain. | lld:pubmed |
| pubmed-article:1924383 | pubmed:affiliation | Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02215. | lld:pubmed |
| pubmed-article:1924383 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1924383 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:1924383 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1924383 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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