Source:http://linkedlifedata.com/resource/pubmed/id/15715461
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
|
| pubmed:dateCreated |
2005-2-17
|
| pubmed:abstractText |
N,O-Didansyl-L-tyrosine (DDT) represented the starting lead for further development of novel non-substrate-like inhibitors of bacterial thymidylate synthase. The N-dansyl structure modulation led to a submicromolar inhibitor of Lactobacillus casei TS (LcTS), which is highly specific with respect to human TS (hTS). Using molecular dynamics simulation, a binding mode for DDT vs LcTS was predicted, explaining activity and species-specificity along the series.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Feb
|
| pubmed:issn |
0022-2623
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
24
|
| pubmed:volume |
48
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
913-6
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:15715461-Bacteria,
pubmed-meshheading:15715461-Dansyl Compounds,
pubmed-meshheading:15715461-Humans,
pubmed-meshheading:15715461-Lactobacillus casei,
pubmed-meshheading:15715461-Models, Molecular,
pubmed-meshheading:15715461-Molecular Conformation,
pubmed-meshheading:15715461-Protein Binding,
pubmed-meshheading:15715461-Structure-Activity Relationship,
pubmed-meshheading:15715461-Substrate Specificity,
pubmed-meshheading:15715461-Thymidylate Synthase,
pubmed-meshheading:15715461-Tyrosine
|
| pubmed:year |
2005
|
| pubmed:articleTitle |
Improving specificity vs bacterial thymidylate synthases through N-dansyl modulation of didansyltyrosine.
|
| pubmed:affiliation |
Dipartimento di Scienze Farmaceutiche, Università degli Studi di Modena e Reggio Emilia, via Campi 183, 41100 Modena, Italy. tondid@unimore.it
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|