|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
4
|
|
pubmed:dateCreated |
1998-6-16
|
|
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.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Apr
|
|
pubmed:issn |
1420-682X
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
54
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
353-8
|
|
pubmed:dateRevised |
2006-11-15
|
|
pubmed:meshHeading |
pubmed-meshheading:9614972-Bacterial Proteins,
pubmed-meshheading:9614972-Carrier Proteins,
pubmed-meshheading:9614972-Crystallography, X-Ray,
pubmed-meshheading:9614972-Hexosyltransferases,
pubmed-meshheading:9614972-Models, Molecular,
pubmed-meshheading:9614972-Muramoylpentapeptide Carboxypeptidase,
pubmed-meshheading:9614972-Penicillin-Binding Proteins,
pubmed-meshheading:9614972-Penicillins,
pubmed-meshheading:9614972-Peptidyl Transferases,
pubmed-meshheading:9614972-X-Ray Diffraction,
pubmed-meshheading:9614972-beta-Lactamases
|
|
pubmed:year |
1998
|
|
pubmed:articleTitle |
X-ray studies of enzymes that interact with penicillins.
|
|
pubmed:affiliation |
Department of Molecular and Cell Biology, University of Connecticut, Storrs, USA.
|
|
pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
|
