| pubmed-article:14975742 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14975742 | lifeskim:mentions | umls-concept:C0035547 | lld:lifeskim |
| pubmed-article:14975742 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:14975742 | lifeskim:mentions | umls-concept:C2266987 | lld:lifeskim |
| pubmed-article:14975742 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:14975742 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:14975742 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:14975742 | pubmed:dateCreated | 2004-2-20 | lld:pubmed |
| pubmed-article:14975742 | pubmed:abstractText | Desferri-exochelins are siderophores secreted by Mycobacterium tuberculosis that are both lipid- and water-soluble and have a high binding affinity for iron. Desferri-exochelin 772SM inhibits DNA replication and ribonucleotide reductase activity at 10-fold less concentration than the lipid-insoluble iron chelator deferoxamine, which is currently in clinical use. Neither chelator can extract iron directly from ribonucleotide reductase. However, because of its lipid-solubility and high binding affinity, desferri-exochelin is able to enter cells rapidly and access intracellular iron, while deferoxamine has limited capacity to cross the cell membrane. | lld:pubmed |
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| pubmed-article:14975742 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:14975742 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:14975742 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14975742 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14975742 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:14975742 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:14975742 | pubmed:author | pubmed-author:AntholineWill... | lld:pubmed |
| pubmed-article:14975742 | pubmed:author | pubmed-author:HorwitzLawren... | lld:pubmed |
| pubmed-article:14975742 | pubmed:author | pubmed-author:HodgesYvonne... | lld:pubmed |
| pubmed-article:14975742 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14975742 | pubmed:day | 12 | lld:pubmed |
| pubmed-article:14975742 | pubmed:volume | 315 | lld:pubmed |
| pubmed-article:14975742 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14975742 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14975742 | pubmed:pagination | 595-8 | lld:pubmed |
| pubmed-article:14975742 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:14975742 | pubmed:meshHeading | pubmed-meshheading:14975742... | lld:pubmed |
| pubmed-article:14975742 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:14975742 | pubmed:articleTitle | Effect on ribonucleotide reductase of novel lipophilic iron chelators: the desferri-exochelins. | lld:pubmed |
| pubmed-article:14975742 | pubmed:affiliation | University of Colorado, Health Sciences Center, Department of Medicine, Division of Cardiology, Box B130, 4200 E. 9th Ave., Denver, CO 80262, USA. yvonne.hodges@uchsc.edu | lld:pubmed |
| pubmed-article:14975742 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14975742 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14975742 | lld:pubmed |
