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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1988-6-3
|
| pubmed:abstractText |
Numerous glycopeptides continue to be described in the literature. They all share a similar heptapeptidic structure with a fixed spatial configuration that forms the basis of their ability to recognize D-alanyl-D-alanine-containing structures in the cell wall. This complexation results in block of peptiglycan elongation; hence, inhibition of growth; and, eventually, cell death. The great variety of substituents on the heptapeptide forms the basis of a wide gradation of physico-chemical characteristics, namely net charge and lipophilicity, which, in turn, might explain the widely differing pharmacologic properties.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Feb
|
| pubmed:issn |
0091-2700
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
28
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
136-40
|
| pubmed:dateRevised |
2008-11-21
|
| pubmed:meshHeading | |
| pubmed:year |
1988
|
| pubmed:articleTitle |
Glycopeptide antibiotics.
|
| pubmed:affiliation |
Merrell-Dow Research Institute, Lepetit Research Center, Milan, Italy.
|
| pubmed:publicationType |
Journal Article,
Review
|