Irreversible cysteine protease inhibitors of legumain

Chemistry: natural resins or derivatives; peptides or proteins; – Peptides of 3 to 100 amino acid residues – Tripeptides – e.g. – tripeptide thyroliberin – etc.

Reexamination Certificate

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Details

C558S166000, C560S155000, C562S553000

Reexamination Certificate

active

10485723

ABSTRACT:
Presented are compounds represented by the following general formulas (I) and (II), for inhibiting cysteine protease legumain for modulating associated disease states in subjects

REFERENCES:
patent: 0 995 756 (2000-04-01), None
patent: WO95/23222 (1995-08-01), None
patent: WO99/48910 (1999-09-01), None
Demuth, et al.; “Molecular drug research: A survey of the mechanism-oriented serine protease inhibitors”;Pharmazie; (1989) 44(1), 1-11 (including abstract in English).
Dando, et al.; “Pig Kidney Legumain: an asparaginyl endopeptidase with restricted specificity”;Biochem. J. ; (1999) 339, 743-749.
Ackermann, E. et al.; “Untersuchungen zur zentralnervösen Wirkung der Hydrazinoessigsäure and Ihrer Derivate”;ACTA Biological et Medica Germanica; (1964) 12, 322-341 (including summary in English).
Gante, J; “Azapeptides”;Synthesis; (1989) 405-413.
Manoury, et al.; “An asparaginyl endopeptidase process a microbial antigen for class II MHC presentation”;Nature; (1998) 396, 695-699.
International Search Report dated Feb. 26, 2003.

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