| pubmed-article:8012126 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8012126 | lifeskim:mentions | umls-concept:C0023820 | lld:lifeskim |
| pubmed-article:8012126 | lifeskim:mentions | umls-concept:C2266975 | lld:lifeskim |
| pubmed-article:8012126 | lifeskim:mentions | umls-concept:C0205177 | lld:lifeskim |
| pubmed-article:8012126 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
| pubmed-article:8012126 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
| pubmed-article:8012126 | lifeskim:mentions | umls-concept:C0243071 | lld:lifeskim |
| pubmed-article:8012126 | lifeskim:mentions | umls-concept:C0205460 | lld:lifeskim |
| pubmed-article:8012126 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:8012126 | pubmed:dateCreated | 1994-7-25 | lld:pubmed |
| pubmed-article:8012126 | pubmed:abstractText | Bacterial lipoproteins, which are of particular interest because of their immunomodulatory activities, share a common N-terminal structural motif that consists of an N-acyl-S-diacylglyceryl cysteine residue. Synthetic tripalmitoylated analogs of the N-terminal sequences of several bacterial lipopetides have been found to reproduce the immunological activities of the corresponding intact lipoproteins. Methods for the synthesis of lipopeptide analogs of bacterial lipoproteins have hitherto relied upon the coupling of peptide moieties, lacking the N-terminal cystienyl residue, with a tripalmitoylglyceryl cysteine moiety synthesized separately in solution. A method is described here by which rapid and convenient synthesis of the entire lipopeptide is accomplished by solid-phase methods in which the N-terminal cysteinyl derivative is assembled stepwise while attached to the completed peptide moiety prior to cleavage from the resin. The method has been used to synthesize two lipohexapeptides representing the N-terminal sequences of the 47-kDa membrane lipoprotein of the syphilis spirochete, Treponema pallidum, and the outer surface protein A (OspA) of the Lyme disease spirochete, Borrelia burgdorferi. These lipopeptides, which were synthesized without detectable endotoxin contamination, exhibit macrophage-stimulating activity that is not expressed by the corresponding non-acylated hexapeptides. The data indicate that synthetic lipopeptides based on spirochetal lipoproteins are appropriate substitutes for the intact lipoproteins in immunological studies. | lld:pubmed |
| pubmed-article:8012126 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8012126 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8012126 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8012126 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8012126 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8012126 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8012126 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8012126 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8012126 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8012126 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8012126 | pubmed:issn | 1040-5704 | lld:pubmed |
| pubmed-article:8012126 | pubmed:author | pubmed-author:JonesJ DJD | lld:pubmed |
| pubmed-article:8012126 | pubmed:author | pubmed-author:SlaughterC... | lld:pubmed |
| pubmed-article:8012126 | pubmed:author | pubmed-author:NorgardM VMV | lld:pubmed |
| pubmed-article:8012126 | pubmed:author | pubmed-author:RuseGG | lld:pubmed |
| pubmed-article:8012126 | pubmed:author | pubmed-author:RadolfJ DJD | lld:pubmed |
| pubmed-article:8012126 | pubmed:author | pubmed-author:PramanikB CBC | lld:pubmed |
| pubmed-article:8012126 | pubmed:author | pubmed-author:DeOgnyLL | lld:pubmed |
| pubmed-article:8012126 | pubmed:author | pubmed-author:ArndtL LLL | lld:pubmed |
| pubmed-article:8012126 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8012126 | pubmed:volume | 7 | lld:pubmed |
| pubmed-article:8012126 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8012126 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8012126 | pubmed:pagination | 91-7 | lld:pubmed |
| pubmed-article:8012126 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:8012126 | pubmed:meshHeading | pubmed-meshheading:8012126-... | lld:pubmed |
| pubmed-article:8012126 | pubmed:meshHeading | pubmed-meshheading:8012126-... | lld:pubmed |
| pubmed-article:8012126 | pubmed:meshHeading | pubmed-meshheading:8012126-... | lld:pubmed |
| pubmed-article:8012126 | pubmed:meshHeading | pubmed-meshheading:8012126-... | lld:pubmed |
| pubmed-article:8012126 | pubmed:meshHeading | pubmed-meshheading:8012126-... | lld:pubmed |
| pubmed-article:8012126 | pubmed:meshHeading | pubmed-meshheading:8012126-... | lld:pubmed |
| pubmed-article:8012126 | pubmed:meshHeading | pubmed-meshheading:8012126-... | lld:pubmed |
| pubmed-article:8012126 | pubmed:meshHeading | pubmed-meshheading:8012126-... | lld:pubmed |
| pubmed-article:8012126 | pubmed:meshHeading | pubmed-meshheading:8012126-... | lld:pubmed |
| pubmed-article:8012126 | pubmed:meshHeading | pubmed-meshheading:8012126-... | lld:pubmed |
| pubmed-article:8012126 | pubmed:meshHeading | pubmed-meshheading:8012126-... | lld:pubmed |
| pubmed-article:8012126 | pubmed:meshHeading | pubmed-meshheading:8012126-... | lld:pubmed |
| pubmed-article:8012126 | pubmed:articleTitle | Solid-phase synthesis of biologically active lipopeptides as analogs for spirochetal lipoproteins. | lld:pubmed |
| pubmed-article:8012126 | pubmed:affiliation | Department of Microbiology, University of Texas Southwestern Medical Center at Dallas 75235. | lld:pubmed |
| pubmed-article:8012126 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8012126 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8012126 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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