N,O-Didansyl-L-tyrosine (DDT), a potent inhibitor of bacterial thymidylate synthases, is used as a starting lead for development of novel non-substrate-like inhibitors of bacterial thymidylate synthase.
Journal of medicinal chemistry, 48(4), 913-916 (2005-02-18)
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
Chembiochem : a European journal of chemical biology, 9(5), 779-790 (2008-03-18)
The elucidation of the structural/functional specificities of highly conserved enzymes remains a challenging area of investigation, and enzymes involved in cellular replication are important targets for functional studies and drug discovery. Thymidylate synthase (TS, ThyA) governs the synthesis of thymidylate
Protein plasticity in response to ligand binding abrogates the notion of a rigid receptor site. Thus, computational docking alone misses important prospective drug design leads. Bacterial-specific inhibitors of an essential enzyme, thymidylate synthase (TS), were developed using a combination of
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