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Caspase substrates: easily caught in deep waters?

Dieter Demon (UGent) , Petra Van Damme (UGent) , Tom Vanden Berghe (UGent) , Joël Vandekerckhove (UGent) , Wim Declercq (UGent) , Kris Gevaert (UGent) and Peter Vandenabeele (UGent)
(2009) TRENDS IN BIOTECHNOLOGY. 27(12). p.680-688
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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.
Keywords
CELL-DEATH, GRANZYME-B, DIFFERENCE GEL-ELECTROPHORESIS, FAS-INDUCED APOPTOSIS, N-TERMINAL ACETYLTRANSFERASES, PROTEOLYTIC CLEAVAGE SITES, PROTEOME ANALYSIS, IDENTIFICATION, IN-VIVO, ALZHEIMERS-DISEASE

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Chicago
Demon, Dieter, Petra Van Damme, Tom Vanden Berghe, Joël Vandekerckhove, Wim Declercq, Kris Gevaert, and Peter Vandenabeele. 2009. “Caspase Substrates: Easily Caught in Deep Waters?” Trends in Biotechnology 27 (12): 680–688.
APA
Demon, D., Van Damme, P., Vanden Berghe, T., Vandekerckhove, J., Declercq, W., Gevaert, K., & Vandenabeele, P. (2009). Caspase substrates: easily caught in deep waters? TRENDS IN BIOTECHNOLOGY, 27(12), 680–688.
Vancouver
1.
Demon D, Van Damme P, Vanden Berghe T, Vandekerckhove J, Declercq W, Gevaert K, et al. Caspase substrates: easily caught in deep waters? TRENDS IN BIOTECHNOLOGY. LONDON: ELSEVIER SCIENCE LONDON; 2009;27(12):680–8.
MLA
Demon, Dieter, Petra Van Damme, Tom Vanden Berghe, et al. “Caspase Substrates: Easily Caught in Deep Waters?” TRENDS IN BIOTECHNOLOGY 27.12 (2009): 680–688. Print.
@article{808196,
  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.},
  author       = {Demon, Dieter and Van Damme, Petra and Vanden Berghe, Tom and Vandekerckhove, Jo{\"e}l and Declercq, Wim and Gevaert, Kris and Vandenabeele, Peter},
  issn         = {0167-7799},
  journal      = {TRENDS IN BIOTECHNOLOGY},
  keyword      = {CELL-DEATH,GRANZYME-B,DIFFERENCE GEL-ELECTROPHORESIS,FAS-INDUCED APOPTOSIS,N-TERMINAL ACETYLTRANSFERASES,PROTEOLYTIC CLEAVAGE SITES,PROTEOME ANALYSIS,IDENTIFICATION,IN-VIVO,ALZHEIMERS-DISEASE},
  language     = {eng},
  number       = {12},
  pages        = {680--688},
  publisher    = {ELSEVIER SCIENCE LONDON},
  title        = {Caspase substrates: easily caught in deep waters?},
  url          = {http://dx.doi.org/10.1016/j.tibtech.2009.09.007},
  volume       = {27},
  year         = {2009},
}

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