Journal
TRENDS IN BIOTECHNOLOGY
Volume 27, Issue 12, Pages 680-688Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibtech.2009.09.007
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Funding
- BOF (Bijzonder Onderzoeksfonds) Ghent University [B/00757/01, B/05959/01]
- Fonds voor Wetenschappelijk Onderzoek-Vlaanderen [G.0133.05, 3G.0218.06]
- Flanders Institute for Biotechnology (VIB)
- European Union [MRTN-CT-035624, LSHB-CT-2005-019067, HEALTH-F4-2007-200767]
- Interuniversity Poles of Attraction-Belgian Science Policy [IAP6/18]
- Special Research Fund of Ghent University [12.0505.02]
- Fund for Scientific Research-Flanders, Belgium [G.0156.05, G.0077.06, G.0042.07]
- Ghent University [BOF07/GOA/012]
- Interuniversity Attraction Poles [IUAP06]
- Flemish Government
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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.
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