186,168 research outputs found
Volsurf computational method applied to the prediction of stability of thermostable enzymes
No full textAn innovative application of the "flexible" GRID/PCA computational method: Study of differences in selectivity between PGAs from Escherichia coli and a Providentia rettgeri mutant
No full textHomology model of penicillin acylase from Alcaligenes faecalis and in silico evaluation of its selectivity
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Properties and applications of supports for enzyme mediated transformations in solid phase synthesis
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An innovative application of “flexible” GRID/PCA computational method: study of differences in selectivity between PGAs from E. coli and from a P. rettgeri mutant
No full textCombined target-based and ligand-based drug design approach as a tool to define a novel 3D-pharmacophore model of human A(3) adenosine receptor antagonists: Pyrazolo[4,3-e]1,2,4- triazolo[1,5-c]pyrimidine derivatives as a key study
No full textA combined target-based and ligand-based drug design approach has been carried out to define a novel pharmacophore model of the human A(3) receptor antagonists. High throughput molecular docking and comparative molecular field analysis (CoMFA) have been used in tandem to assemble a new target based pharmacophore model. In parallel, to provide more accurate information about the putative binding site of these A(3) inhibitors, a rhodopsin-based model of the human A(3) receptor was built and a novel Y-shape binding motif has been proposed. Docking-based structure superimposition has been used to perform a quantitative study of the structure-activity relationships for binding of these pyrazolo-triazolo-pyrimidines to adenosine A(3) receptor using CoMFA. Both steric and the electrostatic contour plots obtained from the CoMFA analysis nicely fit on the hypothetical binding site obtained by molecular docking. On the basis of the combined hypothesis, we have designed, synthesized, and tested 17 new derivatives. Consistently, the predicted K(i) values were very close to the experimental values
Author-wise bibliometric analysis based on entropy.
No full textAuthor-wise bibliometric analysis based on entropy.</p
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