| pubmed-article:20660664 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20660664 | lifeskim:mentions | umls-concept:C0026336 | lld:lifeskim |
| pubmed-article:20660664 | lifeskim:mentions | umls-concept:C0596901 | lld:lifeskim |
| pubmed-article:20660664 | lifeskim:mentions | umls-concept:C0057144 | lld:lifeskim |
| pubmed-article:20660664 | lifeskim:mentions | umls-concept:C0066510 | lld:lifeskim |
| pubmed-article:20660664 | lifeskim:mentions | umls-concept:C0004083 | lld:lifeskim |
| pubmed-article:20660664 | lifeskim:mentions | umls-concept:C0205148 | lld:lifeskim |
| pubmed-article:20660664 | lifeskim:mentions | umls-concept:C0683598 | lld:lifeskim |
| pubmed-article:20660664 | lifeskim:mentions | umls-concept:C0599946 | lld:lifeskim |
| pubmed-article:20660664 | lifeskim:mentions | umls-concept:C0065414 | lld:lifeskim |
| pubmed-article:20660664 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:20660664 | pubmed:dateCreated | 2010-9-20 | lld:pubmed |
| pubmed-article:20660664 | pubmed:abstractText | The presence of the cationic phospholipid lysyl-phosphatidylglycerol (lysyl-PG) in staphylococcal cytoplasmic membranes has been linked to increased resistance to cationic compounds, including antibiotics such as daptomycin as well as host defense antimicrobial peptides. We investigated the effects of lysyl-PG on binding of 6W-RP-1, a synthetic antimicrobial peptide, to lipid vesicles and on peptide-induced membrane permeabilization. Unexpectedly, physiological lysyl-PG concentrations only minimally reduced membrane binding of 6W-RP-1. In contrast, 6W-RP-1-induced dye leakage was severely inhibited by lysyl-PG, suggesting that lysyl-PG primarily impacts membrane defect formation. | lld:pubmed |
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| pubmed-article:20660664 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20660664 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20660664 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20660664 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:20660664 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20660664 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:20660664 | pubmed:issn | 1098-6596 | lld:pubmed |
| pubmed-article:20660664 | pubmed:author | pubmed-author:BayerArnold... | lld:pubmed |
| pubmed-article:20660664 | pubmed:author | pubmed-author:YeamanMichael... | lld:pubmed |
| pubmed-article:20660664 | pubmed:author | pubmed-author:PokornyAntjeA | lld:pubmed |
| pubmed-article:20660664 | pubmed:author | pubmed-author:KileleeErinE | lld:pubmed |
| pubmed-article:20660664 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20660664 | pubmed:volume | 54 | lld:pubmed |
| pubmed-article:20660664 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20660664 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20660664 | pubmed:pagination | 4476-9 | lld:pubmed |
| pubmed-article:20660664 | pubmed:dateRevised | 2011-7-27 | lld:pubmed |
| pubmed-article:20660664 | pubmed:meshHeading | pubmed-meshheading:20660664... | lld:pubmed |
| pubmed-article:20660664 | pubmed:meshHeading | pubmed-meshheading:20660664... | lld:pubmed |
| pubmed-article:20660664 | pubmed:meshHeading | pubmed-meshheading:20660664... | lld:pubmed |
| pubmed-article:20660664 | pubmed:meshHeading | pubmed-meshheading:20660664... | lld:pubmed |
| pubmed-article:20660664 | pubmed:meshHeading | pubmed-meshheading:20660664... | lld:pubmed |
| pubmed-article:20660664 | pubmed:meshHeading | pubmed-meshheading:20660664... | lld:pubmed |
| pubmed-article:20660664 | pubmed:meshHeading | pubmed-meshheading:20660664... | lld:pubmed |
| pubmed-article:20660664 | pubmed:meshHeading | pubmed-meshheading:20660664... | lld:pubmed |
| pubmed-article:20660664 | pubmed:meshHeading | pubmed-meshheading:20660664... | lld:pubmed |
| pubmed-article:20660664 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20660664 | pubmed:articleTitle | Lysyl-phosphatidylglycerol attenuates membrane perturbation rather than surface association of the cationic antimicrobial peptide 6W-RP-1 in a model membrane system: implications for daptomycin resistance. | lld:pubmed |
| pubmed-article:20660664 | pubmed:affiliation | Department of Chemistry and Biochemistry, University of North Carolina Wilmington, Wilmington, North Carolina 28403, USA. | lld:pubmed |
| pubmed-article:20660664 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20660664 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:20660664 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| http://linkedlifedata.com/r... | http://linkedlifedata.com/r... | pubmed-article:20660664 | lld:chembl |
