pubmed-article:9614972 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9614972 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
pubmed-article:9614972 | lifeskim:mentions | umls-concept:C0030842 | lld:lifeskim |
pubmed-article:9614972 | lifeskim:mentions | umls-concept:C0043309 | lld:lifeskim |
pubmed-article:9614972 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
pubmed-article:9614972 | pubmed:issue | 4 | lld:pubmed |
pubmed-article:9614972 | pubmed:dateCreated | 1998-6-16 | lld:pubmed |
pubmed-article:9614972 | pubmed:abstractText | The technique of X-ray diffraction has been successfully applied to enzymes associated with peptidoglycan biosynthesis. The technique has taught us a great deal about the structures and catalytic mechanisms of penicillin-binding proteins and beta-lactamases. An insight into the structural basis for antibiotic resistance is given. | lld:pubmed |
pubmed-article:9614972 | pubmed:language | eng | lld:pubmed |
pubmed-article:9614972 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9614972 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:9614972 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:9614972 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:9614972 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:9614972 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9614972 | pubmed:month | Apr | lld:pubmed |
pubmed-article:9614972 | pubmed:issn | 1420-682X | lld:pubmed |
pubmed-article:9614972 | pubmed:author | pubmed-author:CharlierPP | lld:pubmed |
pubmed-article:9614972 | pubmed:author | pubmed-author:KellyJ AJA | lld:pubmed |
pubmed-article:9614972 | pubmed:author | pubmed-author:KuzinA PAP | lld:pubmed |
pubmed-article:9614972 | pubmed:author | pubmed-author:FonzéEE | lld:pubmed |
pubmed-article:9614972 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9614972 | pubmed:volume | 54 | lld:pubmed |
pubmed-article:9614972 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9614972 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9614972 | pubmed:pagination | 353-8 | lld:pubmed |
pubmed-article:9614972 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:9614972 | pubmed:meshHeading | pubmed-meshheading:9614972-... | lld:pubmed |
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pubmed-article:9614972 | pubmed:meshHeading | pubmed-meshheading:9614972-... | lld:pubmed |
pubmed-article:9614972 | pubmed:year | 1998 | lld:pubmed |
pubmed-article:9614972 | pubmed:articleTitle | X-ray studies of enzymes that interact with penicillins. | lld:pubmed |
pubmed-article:9614972 | pubmed:affiliation | Department of Molecular and Cell Biology, University of Connecticut, Storrs, USA. | lld:pubmed |
pubmed-article:9614972 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9614972 | pubmed:publicationType | Review | lld:pubmed |
pubmed-article:9614972 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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