210963-04-5Relevant articles and documents
RENIN INHIBITORS
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, (2008/12/04)
Described are compounds which bind to aspartic proteases to inhibit their activity. They are useful in the treatment or amelioration of diseases associated with aspartic protease activity. Also described are methods of use of the compounds described herein in ameliorating or treating aspartic protease related disorders in a subject in need thereof.
RENIN INHIBITORS
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Page/Page column 140, (2008/12/04)
Disclosed are compounds of Formula (I) wherein the R, R1, R2, R3, X, Y, A, Q, E, and G are defined herein. These compounds bind to aspartic proteases to inhibit their activity and are useful in the treatment or amelioration of diseases associated with aspartic protease activity. Also disclosed are methods of use of the compounds of Formula I for ameliorating or treating aspartic protease related disorders in a subject in need thereof.
TETRAPEPTIDE INHIBITORS OF BETA-SECRETASE
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Page/Page column 11; 24-25, (2008/06/13)
Statine-derived peptide inhibitors of the β-secretase enzyme are provided which are useful in the treatment of Alzheimer's disease and other diseases characterized by deposition of Aβ peptide in a mammal. The compounds of the invention provide useful meth
Non-covalent polyvalent ligands by self-assembly of small glycodendrimers: A novel concept for the inhibition of polyvalent carbohydrate-protein interactions in vitro and in vivo
Thoma, Gebhard,Streiff, Markus B.,Katopodis, Andreas G.,Duthaler, Rudolf O.,Voelcker, Nicolas H.,Ehrhardt, Claus,Masson, Christophe
, p. 99 - 117 (2007/10/03)
Polyvalent carbohydrate-protein interactions occur frequently in biology, particularly in recognition events on cellular membranes. Collectively, they can be much stronger than corresponding monovalent interactions, rendering it difficult to control them with individual small molecules. Artificial macromolecules have been used as polyvalent ligands to inhibit polyvalent processes; however, both reproducible synthesis and appropriate characterization of such complex entities is demanding. Herein, we present an alternative concept avoiding conventional macromolecules. Small glycodendrimers which fulfill single molecule entity criteria self-assemble to form non-covalent nanoparticles. These particles - not the individual molecules - function as polyvalent ligands, efficiently inhibiting polyvalent processes both in vitro and in vivo. The synthesis and characterization of these glycodendrimers is described in detail. Furthermore, we report on the characterization of the non-covalent nanoparticles formed and on their biological evaluation.
BENZAMIDINE DERIVATIVES
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, (2008/06/13)
Benzamidine derivatives of the following formulae or analogs thereof, i. e., pharmaceutically acceptable salts thereof, are provided. These compounds or salts thereof have a blood-coagulation inhibiting effect based on an excellent effect of inhibiting the action of activated blood coagulation factor X, and they are useful as anticoagulants.