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Title
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Caspase substrates : easily caught in deep waters?
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Author
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Abstract
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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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Language
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English
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Source (journal)
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Trends in biotechnology : regular edition. - Amsterdam, 1983, currens
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Publication
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Amsterdam
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2009
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ISSN
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1879-3096
[online]
0167-7799
[print]
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Volume/pages
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27
:12
(2009)
, p. 680-688
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ISI
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000272277500004
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Full text (Publisher's DOI)
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