| pubmed-article:11600367 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11600367 | lifeskim:mentions | umls-concept:C0003232 | lld:lifeskim |
| pubmed-article:11600367 | lifeskim:mentions | umls-concept:C0001480 | lld:lifeskim |
| pubmed-article:11600367 | lifeskim:mentions | umls-concept:C0441472 | lld:lifeskim |
| pubmed-article:11600367 | lifeskim:mentions | umls-concept:C1100765 | lld:lifeskim |
| pubmed-article:11600367 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:11600367 | pubmed:dateCreated | 2001-10-15 | lld:pubmed |
| pubmed-article:11600367 | pubmed:abstractText | Microcin H47 is a gene-encoded peptide antibiotic produced by a natural Escherichia coli strain isolated in Uruguay. In order to identify cellular components necessary for its antibiotic action, microcin H47-resistant mutants isolated in this work, as well as previously described mutants affected in membrane proteins, were analyzed. These studies indicated that (i) receptor outer membrane proteins for ferric-catechol siderophores would be involved in microcin-specific binding to the cell surface, (ii) the TonB pathway is needed for microcin H47 uptake, and (iii) the presence of the ATP synthase complex is necessary for microcin action. The possibility that this last structure contains the antibiotic target is discussed. | lld:pubmed |
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| pubmed-article:11600367 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11600367 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11600367 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11600367 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11600367 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:11600367 | pubmed:issn | 0066-4804 | lld:pubmed |
| pubmed-article:11600367 | pubmed:author | pubmed-author:RodríguezEE | lld:pubmed |
| pubmed-article:11600367 | pubmed:author | pubmed-author:TrujilloMM | lld:pubmed |
| pubmed-article:11600367 | pubmed:author | pubmed-author:LaviñaMM | lld:pubmed |
| pubmed-article:11600367 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11600367 | pubmed:volume | 45 | lld:pubmed |
| pubmed-article:11600367 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11600367 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11600367 | pubmed:pagination | 3128-31 | lld:pubmed |
| pubmed-article:11600367 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:11600367 | pubmed:meshHeading | pubmed-meshheading:11600367... | lld:pubmed |
| pubmed-article:11600367 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11600367 | pubmed:articleTitle | ATP synthase is necessary for microcin H47 antibiotic action. | lld:pubmed |
| pubmed-article:11600367 | pubmed:affiliation | Sección de Fisiología y Genética Bacterianas, Facultad de Ciencias, Iguá 4225, Montevideo 11.400, Uruguay. | lld:pubmed |
| pubmed-article:11600367 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11600367 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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