| pubmed-article:8772200 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8772200 | lifeskim:mentions | umls-concept:C0680022 | lld:lifeskim |
| pubmed-article:8772200 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:8772200 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:8772200 | lifeskim:mentions | umls-concept:C0085249 | lld:lifeskim |
| pubmed-article:8772200 | lifeskim:mentions | umls-concept:C0456387 | lld:lifeskim |
| pubmed-article:8772200 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:8772200 | pubmed:dateCreated | 1996-10-21 | lld:pubmed |
| pubmed-article:8772200 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8772200 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8772200 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8772200 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8772200 | pubmed:abstractText | Using conserved fingerprints in the glycosyltransferase (GTase) domain of high-molecular-weight penicillin-binding proteins (PBP), a gene (mgt) encoding a putative monofunctional glycosyltransferase has been identified in Haemophilus influenzae and in other bacteria] species. Here we report the cloning of the homologous Escherichia coli gene and show that the solubilised membrane fraction of E. coli cells overexpressing the mgt gene contain a significantly increased peptidoglycan synthesis activity. In contrast to the high-molecular-weight PBPs, this activity is not inhibited by Flavomycin. | lld:pubmed |
| pubmed-article:8772200 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8772200 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8772200 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8772200 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8772200 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8772200 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8772200 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8772200 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8772200 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8772200 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:8772200 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:8772200 | pubmed:author | pubmed-author:KeckWW | lld:pubmed |
| pubmed-article:8772200 | pubmed:author | pubmed-author:StüberDD | lld:pubmed |
| pubmed-article:8772200 | pubmed:author | pubmed-author:DijkstraAA | lld:pubmed |
| pubmed-article:8772200 | pubmed:author | pubmed-author:GublerMM | lld:pubmed |
| pubmed-article:8772200 | pubmed:author | pubmed-author:Di... | lld:pubmed |
| pubmed-article:8772200 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8772200 | pubmed:day | 26 | lld:pubmed |
| pubmed-article:8772200 | pubmed:volume | 392 | lld:pubmed |
| pubmed-article:8772200 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8772200 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8772200 | pubmed:pagination | 184-8 | lld:pubmed |
| pubmed-article:8772200 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:8772200 | pubmed:meshHeading | pubmed-meshheading:8772200-... | lld:pubmed |
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| pubmed-article:8772200 | pubmed:meshHeading | pubmed-meshheading:8772200-... | lld:pubmed |
| pubmed-article:8772200 | pubmed:meshHeading | pubmed-meshheading:8772200-... | lld:pubmed |
| pubmed-article:8772200 | pubmed:meshHeading | pubmed-meshheading:8772200-... | lld:pubmed |
| pubmed-article:8772200 | pubmed:meshHeading | pubmed-meshheading:8772200-... | lld:pubmed |
| pubmed-article:8772200 | pubmed:meshHeading | pubmed-meshheading:8772200-... | lld:pubmed |
| pubmed-article:8772200 | pubmed:meshHeading | pubmed-meshheading:8772200-... | lld:pubmed |
| pubmed-article:8772200 | pubmed:meshHeading | pubmed-meshheading:8772200-... | lld:pubmed |
| pubmed-article:8772200 | pubmed:meshHeading | pubmed-meshheading:8772200-... | lld:pubmed |
| pubmed-article:8772200 | pubmed:meshHeading | pubmed-meshheading:8772200-... | lld:pubmed |
| pubmed-article:8772200 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8772200 | pubmed:articleTitle | The monofunctional glycosyltransferase of Escherichia coli is a member of a new class of peptidoglycan-synthesising enzymes. | lld:pubmed |
| pubmed-article:8772200 | pubmed:affiliation | Pharma Research Department, F. Hoffman-La Roche Ltd., Basel, Switzerland. | lld:pubmed |
| pubmed-article:8772200 | pubmed:publicationType | Journal Article | lld:pubmed |
| entrez-gene:947728 | entrezgene:pubmed | pubmed-article:8772200 | lld:entrezgene |
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