Cocrystal Structures of Primed Side-Extending α-Ketoamide Inhibitors Reveal Novel Calpain-Inhibitor Aromatic Interactions-Reference-Cited by-同舟云学术

Cocrystal Structures of Primed Side-Extending α-Ketoamide Inhibitors Reveal Novel Calpain-Inhibitor Aromatic Interactions

Published:2008-08-15 Issue:17 Volume:51 Page:5264-5270
ISSN:0022-2623
Container-title:Journal of Medicinal Chemistry
language:en
Short-container-title:J. Med. Chem.

Author:

Qian Jin¹,Cuerrier Dominic¹,Davies Peter L.¹,Li Zhaozhao¹,Powers James C.¹,Campbell Robert L.¹

Affiliation:

1. Department of Biochemistry, Queen’s University, Kingston, Ontario, K7L 3N6, Canada, and School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332-0400

Publisher

American Chemical Society (ACS)

Subject

Drug Discovery,Molecular Medicine

Link

https://pubs.acs.org/doi/pdf/10.1021/jm800045t

Reference38 articles.

1. The Calpain System

2. Calpain Inhibition: A Therapeutic Strategy Targeting Multiple Disease States

3. Development and Therapeutic Potential of Calpain Inhibitors

4. The Structure of Calpain

5. Crystal structure of calpain reveals the structural basis for Ca2+-dependent protease activity and a novel mode of enzyme activation

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