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Ghosh AK Kumaragurubaran N Hong L Lei H Hussain KA Liu CF Devasamudram T Weerasena V Turner R Koelsch G Bilcer G Tang J 《Journal of the American Chemical Society》2006,128(16):5310-5311
Structure-based design, synthesis, and X-ray structure of protein-ligand complexes of memapsin 2 are described. The inhibitors are designed specifically to interact with S2- and S3-active site residues to provide selectivity over memapsin 1 and cathepsin D. Inhibitor 6 has exhibited exceedingly potent inhibitory activity against memapsin 2 and selectivity over memapsin 1 (>3800-fold) and cathepsin D (>2500-fold). A protein-ligand crystal structure revealed cooperative interactions in the S2- and S3-active sites of memapsin 2. These interactions may serve as an important guide to design selectivity over memapsin 1 and cathepsin D. 相似文献
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Weerasena Lakmali Ebiefung Aniekan Skjellum Anthony 《Computational Optimization and Applications》2022,82(3):717-751
Computational Optimization and Applications - Set covering optimization problems (SCPs) are important and of broad interest because of their extensive applications in the real world. This study... 相似文献
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