| pubmed-article:18642854 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18642854 | lifeskim:mentions | umls-concept:C0085495 | lld:lifeskim |
| pubmed-article:18642854 | lifeskim:mentions | umls-concept:C0030958 | lld:lifeskim |
| pubmed-article:18642854 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:18642854 | pubmed:issue | 32 | lld:pubmed |
| pubmed-article:18642854 | pubmed:dateCreated | 2008-8-5 | lld:pubmed |
| pubmed-article:18642854 | pubmed:abstractText | Vancomycin and other antibacterial glycopeptide analogues target the cell wall and affect the enzymatic processes involved with cell-wall biosynthesis. Understanding the structure and organization of the peptidoglycan is the first step in establishing the mode of action of these glycopeptides. We have used solid-state NMR to determine the relative concentrations of stem-links (64%), bridge-links (61%), and cross-links (49%) in the cell walls of vancomycin-susceptible Enterococcus faecium (ATTC 49624). Furthermore, we have determined that in vivo only 7% of the peptidoglycan stems terminate in d-Ala- d-Ala, the well-known vancomycin-binding site. Presumably, d-Ala- d-Ala is cleaved from uncross-linked stems in mature peptidoglycan by an active carboxypeptidase. We believe that most of the few pentapeptide stems ending in d-Ala- d-Ala occur in the template and nascent peptidoglycan strands that are crucial for cell-wall biosynthesis. | lld:pubmed |
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| pubmed-article:18642854 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18642854 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18642854 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:18642854 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18642854 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18642854 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:18642854 | pubmed:issn | 1520-4995 | lld:pubmed |
| pubmed-article:18642854 | pubmed:author | pubmed-author:KimSung... | lld:pubmed |
| pubmed-article:18642854 | pubmed:author | pubmed-author:SchaeferJacob... | lld:pubmed |
| pubmed-article:18642854 | pubmed:author | pubmed-author:PattiGary JGJ | lld:pubmed |
| pubmed-article:18642854 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18642854 | pubmed:day | 12 | lld:pubmed |
| pubmed-article:18642854 | pubmed:volume | 47 | lld:pubmed |
| pubmed-article:18642854 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18642854 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18642854 | pubmed:pagination | 8378-85 | lld:pubmed |
| pubmed-article:18642854 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:18642854 | pubmed:meshHeading | pubmed-meshheading:18642854... | lld:pubmed |
| pubmed-article:18642854 | pubmed:meshHeading | pubmed-meshheading:18642854... | lld:pubmed |
| pubmed-article:18642854 | pubmed:meshHeading | pubmed-meshheading:18642854... | lld:pubmed |
| pubmed-article:18642854 | pubmed:meshHeading | pubmed-meshheading:18642854... | lld:pubmed |
| pubmed-article:18642854 | pubmed:meshHeading | pubmed-meshheading:18642854... | lld:pubmed |
| pubmed-article:18642854 | pubmed:meshHeading | pubmed-meshheading:18642854... | lld:pubmed |
| pubmed-article:18642854 | pubmed:meshHeading | pubmed-meshheading:18642854... | lld:pubmed |
| pubmed-article:18642854 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18642854 | pubmed:articleTitle | Characterization of the peptidoglycan of vancomycin-susceptible Enterococcus faecium. | lld:pubmed |
| pubmed-article:18642854 | pubmed:affiliation | Department of Chemistry, Washington University, One Brookings Drive, St. Louis, Missouri 63130, USA. | lld:pubmed |
| pubmed-article:18642854 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18642854 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:18642854 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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