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11 citations found for Babu, Y.S.

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Structure-based drug-design techniques have been utilized to design and synthesize novel and potent inhibitors of purine nucleoside phosphorylase.



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Experimentally measured binding constants of inhibitors to purine nucleoside phosphorylase compared with calculations using X-PLOR, DelPhi and SoftDock give mixed results.

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The structure of the first enzyme:inhibitor covalent adduct of factor D with diisopropyl fluorophosphate to a resolution of 2.4 Å is described. Comparisons between the active sites of native factor D, the adduct of factor D with diisopropyl fluorophosphate and diisopropyl fluorophosphate-inhibited trypsin have provided fundamental insights which are currently being employed in drug design.

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The structure of the enzyme:inhibitor covalent adduct of factor D with 3,4-dichloroisocoumarin to a resolution of 1.8 Å is described. This represents the first structural analysis of factor D with a mechanism-based inhibitor.

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Inhibition of the TF-FVIIa complex is seen as a promising target that is key to the development of clinical candidates for various cardiovascular applications. The crystal structure of the TF-FVIIa enzyme complex has been analyzed in order to design and synthesize small-molecule inhibitors.


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Crystallographic data for three different protein crystals (glycogen phosphorylase b to 2 Å resolution, [beta]-lactamase I to 2.5 Å resolution and troponin C to 6 Å resolution) have been recorded using the intense synchrotron radiation beam emitted by the DCI storage ring at LURE and the DORIS storage ring at DESY/EMBL. Reduction in exposure times of approximately 50-fold and an increase in crystal lifetime of at least fivefold are observed when data recorded at LURE are compared with those recorded with a conventional rotating-anode source. These factors have made possible data collection which otherwise would have been impossible. For large crystals of phosphorylase b a greater reduction in exposure time ( × 125) is made possible by the focusing geometry of the synchrotron-monochromator system which allowed irradiation of a larger volume of the crystal (collimator size increased from 0.3 to 1.0 mm) without significant increase in spot overlap on the film. The data processing statistics for phosphorylase b and [beta]-lactamase compare favourably with those from data recorded on a conventional source (improvements in merging R values of between 1 and 4%). For phosphorylase b, but not for [beta]-lactamase or troponin C, significant thermal diffuse scatter is observed on photographs recorded with synchrotron radiation. The possible origin of this phenomenon and its effect on data processing are discussed.

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