Design and synthesis of dipeptidyl nitriles as potent, selective, and reversible inhibitors of cathepsin C-Reference-Cited by-同舟云学术

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Design and synthesis of dipeptidyl nitriles as potent, selective, and reversible inhibitors of cathepsin C

Published:2009-09 Issue:18 Volume:19 Page:5392-5396
ISSN:0960-894X
Container-title:Bioorganic & Medicinal Chemistry Letters
language:en
Short-container-title:Bioorganic & Medicinal Chemistry Letters

Author:

Guay Daniel,Beaulieu Christian,Jagadeeswar Reddy T.,Zamboni Robert,Methot Nathalie,Rubin Joel,Ethier Diane,David Percival M.

Publisher

Elsevier BV

Subject

Organic Chemistry,Clinical Biochemistry,Drug Discovery,Pharmaceutical Science,Molecular Biology,Molecular Medicine,Biochemistry

Reference29 articles.

1. Molecular cloning of cDNA for rat cathepsin C. Cathepsin C, a cysteine proteinase with an extremely long propeptide.

2. Purification and characterization of dipeptidyl peptidase I from human spleen

3. Mast cell dipeptidyl peptidase I mediates survival from sepsis

4. Dipeptidyl peptidase I activates neutrophil-derived serine proteases and regulates the development of acute experimental arthritis

5. Dipeptidyl peptidase I is required for the processing and activation of granzymes A and B in vivo

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