Human and Parasitic Papain-Like Cysteine Proteases: Their Role in Physiology and Pathology and Recent Developments in Inhibitor Design-Reference-Cited by-同舟云学术

Human and Parasitic Papain-Like Cysteine Proteases: Their Role in Physiology and Pathology and Recent Developments in Inhibitor Design

Published:2002-11-22 Issue:12 Volume:102 Page:4459-4488
ISSN:0009-2665
Container-title:Chemical Reviews
language:en
Short-container-title:Chem. Rev.

Author:

Lecaille Fabien¹,Kaleta Jadwiga¹,Brömme Dieter¹

Affiliation:

1. Mount Sinai School of Medicine, Department of Human Genetics, Fifth Avenue at 100th Street, New York, New York 10029, USA, and NAEJA Pharmaceuticals Inc., 2,4290-91 A Street, Edmonton, Alberta, Canada T6E 5V2

Publisher

American Chemical Society (ACS)

Subject

General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/cr0101656

Reference375 articles.

1. The Function of Propeptide Domains of Cysteine Proteinases

2. Folding Incompetence of Cathepsin L-Like Cysteine Proteases May Be Compensated by the Highly Conserved, Domain-Building N-Terminal Extension of the Proregion

3. Proregion ofBombyx mori cysteine proteinase functions as an intramolecular chaperone to promote proper folding of the mature enzyme

4. Abnormal Glycosylation of Procathepsin L Due to N-terminal Point Mutations Correlates with Failure to Sort to Lysosomes

5. Sorting of Non-Glycosylated Human Procathepsin S in Mammalian Cells

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