| pubmed-article:3337719 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3337719 | lifeskim:mentions | umls-concept:C0003232 | lld:lifeskim |
| pubmed-article:3337719 | lifeskim:mentions | umls-concept:C2266975 | lld:lifeskim |
| pubmed-article:3337719 | lifeskim:mentions | umls-concept:C0051758 | lld:lifeskim |
| pubmed-article:3337719 | lifeskim:mentions | umls-concept:C1516144 | lld:lifeskim |
| pubmed-article:3337719 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:3337719 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:3337719 | lifeskim:mentions | umls-concept:C0872351 | lld:lifeskim |
| pubmed-article:3337719 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:3337719 | pubmed:dateCreated | 1988-2-20 | lld:pubmed |
| pubmed-article:3337719 | pubmed:abstractText | The acidic linear lipopeptide amphomycin is a calcium dependent antibiotic which is thought to bind to carrier lipids such as dolichol monophosphate. The actual role of Ca++ is not definitely established and in this article we have examined the peptides interactions with a range of divalent cations. By CD we have shown that a conformational change is induced by Ca++, Sr++ and Ba++ but not by Mg++, Zn++, Cd++ or Gd+++. Monolayer studies show a decrease in molecular area and an increase in film stability when the subphase contains Ca++. The ensemble of results provides preliminary evidence for the formation of a beta hairpin structure on ion binding (Ka (Ca++) = 2.4 x 10(3)M-1) which could enhance amphomycin's bilayer solubility. | lld:pubmed |
| pubmed-article:3337719 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3337719 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3337719 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3337719 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3337719 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3337719 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3337719 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3337719 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3337719 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3337719 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3337719 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3337719 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3337719 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3337719 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3337719 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3337719 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3337719 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:3337719 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:3337719 | pubmed:author | pubmed-author:Maget-DanaRR | lld:pubmed |
| pubmed-article:3337719 | pubmed:author | pubmed-author:PtakMM | lld:pubmed |
| pubmed-article:3337719 | pubmed:author | pubmed-author:LakeyJ HJH | lld:pubmed |
| pubmed-article:3337719 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3337719 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:3337719 | pubmed:volume | 150 | lld:pubmed |
| pubmed-article:3337719 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3337719 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3337719 | pubmed:pagination | 384-90 | lld:pubmed |
| pubmed-article:3337719 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:3337719 | pubmed:meshHeading | pubmed-meshheading:3337719-... | lld:pubmed |
| pubmed-article:3337719 | pubmed:meshHeading | pubmed-meshheading:3337719-... | lld:pubmed |
| pubmed-article:3337719 | pubmed:meshHeading | pubmed-meshheading:3337719-... | lld:pubmed |
| pubmed-article:3337719 | pubmed:meshHeading | pubmed-meshheading:3337719-... | lld:pubmed |
| pubmed-article:3337719 | pubmed:meshHeading | pubmed-meshheading:3337719-... | lld:pubmed |
| pubmed-article:3337719 | pubmed:meshHeading | pubmed-meshheading:3337719-... | lld:pubmed |
| pubmed-article:3337719 | pubmed:meshHeading | pubmed-meshheading:3337719-... | lld:pubmed |
| pubmed-article:3337719 | pubmed:meshHeading | pubmed-meshheading:3337719-... | lld:pubmed |
| pubmed-article:3337719 | pubmed:meshHeading | pubmed-meshheading:3337719-... | lld:pubmed |
| pubmed-article:3337719 | pubmed:meshHeading | pubmed-meshheading:3337719-... | lld:pubmed |
| pubmed-article:3337719 | pubmed:meshHeading | pubmed-meshheading:3337719-... | lld:pubmed |
| pubmed-article:3337719 | pubmed:meshHeading | pubmed-meshheading:3337719-... | lld:pubmed |
| pubmed-article:3337719 | pubmed:meshHeading | pubmed-meshheading:3337719-... | lld:pubmed |
| pubmed-article:3337719 | pubmed:meshHeading | pubmed-meshheading:3337719-... | lld:pubmed |
| pubmed-article:3337719 | pubmed:meshHeading | pubmed-meshheading:3337719-... | lld:pubmed |
| pubmed-article:3337719 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:3337719 | pubmed:articleTitle | Conformational change on calcium binding by the lipopeptide antibiotic amphomycin. A C.D. and monolayer study. | lld:pubmed |
| pubmed-article:3337719 | pubmed:affiliation | Centre de Biophysique Moléculaire, CNRS and the Université d'Orléans, France. | lld:pubmed |
| pubmed-article:3337719 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3337719 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
