| pubmed-article:15666720 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15666720 | lifeskim:mentions | umls-concept:C0320385 | lld:lifeskim |
| pubmed-article:15666720 | lifeskim:mentions | umls-concept:C0028778 | lld:lifeskim |
| pubmed-article:15666720 | lifeskim:mentions | umls-concept:C0038323 | lld:lifeskim |
| pubmed-article:15666720 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:15666720 | lifeskim:mentions | umls-concept:C0486616 | lld:lifeskim |
| pubmed-article:15666720 | lifeskim:mentions | umls-concept:C0332206 | lld:lifeskim |
| pubmed-article:15666720 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:15666720 | pubmed:dateCreated | 2005-1-25 | lld:pubmed |
| pubmed-article:15666720 | pubmed:abstractText | Several drugs that interact with membrane sterols or inhibit their syntheses are effective in clearing a number of fungal infections. The AIDS-associated lung infection caused by Pneumocystis jirovecii is not cleared by many of these therapies. Pneumocystis normally synthesizes distinct C28 and C29 24-alkylsterols, but ergosterol, the major fungal sterol, is not among them. Two distinct sterol compositional phenotypes were previously observed in P. jirovecii. One was characterized by delta7 C28 and C29 24-alkylsterols with only low proportions of higher molecular mass components. In contrast, the other type was dominated by high C31 and C32 24-alkylsterols, especially pneumocysterol. In the present study, 28 molecular species were elucidated by nuclear magnetic resonance analysis of a human lung specimen containing P. jirovecii representing the latter sterol profile phenotype. Fifteen of the 28 had the methyl group at C-14 of the sterol nucleus and these represented 96% of the total sterol mass in the specimen (excluding cholesterol). These results strongly suggest that sterol 14alpha-demethylase was blocked in these organisms. Twenty-four of the 28 were 24-alkylsterols, indicating that methylation of the C-24 position of the sterol side chain by S-adenosyl-L-methionine:sterol C-24 methyl transferase was fully functional. | lld:pubmed |
| pubmed-article:15666720 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15666720 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15666720 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15666720 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15666720 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15666720 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15666720 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15666720 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15666720 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15666720 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15666720 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15666720 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15666720 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15666720 | pubmed:issn | 1066-5234 | lld:pubmed |
| pubmed-article:15666720 | pubmed:author | pubmed-author:ZhaoHuiH | lld:pubmed |
| pubmed-article:15666720 | pubmed:author | pubmed-author:GinerJosé-Lui... | lld:pubmed |
| pubmed-article:15666720 | pubmed:author | pubmed-author:KaneshiroEdna... | lld:pubmed |
| pubmed-article:15666720 | pubmed:author | pubmed-author:AmitZunikaZ | lld:pubmed |
| pubmed-article:15666720 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15666720 | pubmed:volume | 51 | lld:pubmed |
| pubmed-article:15666720 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15666720 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15666720 | pubmed:pagination | 634-43 | lld:pubmed |
| pubmed-article:15666720 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
| pubmed-article:15666720 | pubmed:meshHeading | pubmed-meshheading:15666720... | lld:pubmed |
| pubmed-article:15666720 | pubmed:meshHeading | pubmed-meshheading:15666720... | lld:pubmed |
| pubmed-article:15666720 | pubmed:meshHeading | pubmed-meshheading:15666720... | lld:pubmed |
| pubmed-article:15666720 | pubmed:meshHeading | pubmed-meshheading:15666720... | lld:pubmed |
| pubmed-article:15666720 | pubmed:meshHeading | pubmed-meshheading:15666720... | lld:pubmed |
| pubmed-article:15666720 | pubmed:meshHeading | pubmed-meshheading:15666720... | lld:pubmed |
| pubmed-article:15666720 | pubmed:meshHeading | pubmed-meshheading:15666720... | lld:pubmed |
| pubmed-article:15666720 | pubmed:meshHeading | pubmed-meshheading:15666720... | lld:pubmed |
| pubmed-article:15666720 | pubmed:meshHeading | pubmed-meshheading:15666720... | lld:pubmed |
| pubmed-article:15666720 | pubmed:meshHeading | pubmed-meshheading:15666720... | lld:pubmed |
| pubmed-article:15666720 | pubmed:articleTitle | Sterol composition of Pneumocystis jirovecii with blocked 14alpha-demethylase activity. | lld:pubmed |
| pubmed-article:15666720 | pubmed:affiliation | Department of Chemistry, State University of New York-ESF, Syracuse, NY 13210, USA. jlginer@syr.edu | lld:pubmed |
| pubmed-article:15666720 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15666720 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
