Publication
Title
Caspase substrates : easily caught in deep waters?
Author
Abstract
Caspases are key players in various cellular processes, such as apoptosis, proliferation and differentiation, and in pathological conditions including cancer and inflammation. Although caspases preferentially cleave C-terminal of aspartic acid residues, their action is restricted generally to one or a few sites per protein substrate. Caspase-specific substrate recognition appears to be determined by the substrate sequences adjacent to the scissile bond. Knowledge of these substrates and the generated fragments is crucial for a thorough understanding of the functional implications of caspase-mediated proteolysis. In addition, insight into the cleavage specificity might assist in designing inhibitors that target disease-related caspase activities. Here, we critically review recently published procedures used to generate a proteome-wide view of caspase substrates.
Language
English
Source (journal)
Trends in biotechnology : regular edition. - Amsterdam, 1983, currens
Publication
Amsterdam : 2009
ISSN
1879-3096 [online]
0167-7799 [print]
Volume/pages
27 :12 (2009) , p. 680-688
ISI
000272277500004
Full text (Publisher's DOI)
UAntwerpen
Publication type
Subject
External links
Web of Science
Record
Identification
Creation 18.10.2018
Last edited 28.08.2021