## Abstract Plasmepsin II (PMII), a malarial aspartic protease involved in the catabolism of hemoglobin in parasites of the genus __Plasmodium__, and renin, a human aspartic protease, share 35% sequence identity in their mature chains. Structures of 4‐arylpiperidine inhibitors complexed to human re
Dilithiated Phosphazenes: Scaffolds for the Synthesis of Olefins Through a New Class of Bicyclic 1,2-Oxaphosphetanes.
✍ Scribed by Jesus Garcia-Lopez; Emma Peralta-Perez; Angela Forcen-Acebal; Santiago Garcia-Granda; Fernando Lopez-Ortiz
- Publisher
- John Wiley and Sons
- Year
- 2003
- Weight
- 118 KB
- Volume
- 34
- Category
- Article
- ISSN
- 0931-7597
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## Abstract A new class of nonpeptidic inhibitors of the malarial aspartic protease plasmepsin II (PMII) with up to single‐digit micromolar activities (__IC__~50~ values) was developed by structure‐based __de novo__ design. The active‐site matrix used in the design was based on an X‐ray crystal str
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