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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
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.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (review)
publication status
published
subject
keyword
CELL-DEATH, GRANZYME-B, DIFFERENCE GEL-ELECTROPHORESIS, FAS-INDUCED APOPTOSIS, N-TERMINAL ACETYLTRANSFERASES, PROTEOLYTIC CLEAVAGE SITES, PROTEOME ANALYSIS, IDENTIFICATION, IN-VIVO, ALZHEIMERS-DISEASE
journal title
TRENDS IN BIOTECHNOLOGY
Trends Biotechnol.
volume
27
issue
12
pages
9 pages
publisher
ELSEVIER SCIENCE LONDON
place of publication
LONDON
Web of Science type
Review
Web of Science id
000272277500004
JCR category
BIOTECHNOLOGY & APPLIED MICROBIOLOGY
JCR impact factor
6.909 (2009)
JCR rank
9/150 (2009)
JCR quartile
1 (2009)
ISSN
0167-7799
DOI
10.1016/j.tibtech.2009.09.007
language
English
UGent publication?
yes
classification
A1
copyright statement
I don't know the status of the copyright for this publication
id
808196
handle
http://hdl.handle.net/1854/LU-808196
date created
2009-12-11 14:02:54
date last changed
2012-06-26 14:31:53
@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},
}

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.