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A quantitative proteomics design for systematic identification of protease cleavage events

(2010) MOLECULAR & CELLULAR PROTEOMICS. 9(10). p.2327-2333
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Abstract
We present here a novel proteomics design for systematic identification of protease cleavage events by quantitative N-terminal proteomics, circumventing the need for time-consuming manual validation. We bypass the singleton detection problem of protease-generated neo-N-terminal peptides by introducing differential isotopic proteome labeling such that these substrate reporter peptides are readily distinguished from all other N-terminal peptides. Our approach was validated using the canonical human caspase-3 protease and further applied to mouse cathepsin D and E substrate processing in a mouse dendritic cell proteome, identifying the largest set of protein protease substrates ever reported and gaining novel insight into substrate specificity differences of these cathepsins.
Keywords
SITES, SILAC, TOOL, EXPRESSION, CATHEPSIN-E, N-TERMINAL PEPTIDES, APOPTOSIS, PRODUCTS

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Citation

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Chicago
Impens, Francis, Niklaas Colaert, Kenny Helsens, Bart Ghesquière, Evy Timmerman, Pieter-Jan De Bock, Benjamin M Chain, Joël Vandekerckhove, and Kris Gevaert. 2010. “A Quantitative Proteomics Design for Systematic Identification of Protease Cleavage Events.” Molecular & Cellular Proteomics 9 (10): 2327–2333.
APA
Impens, F., Colaert, N., Helsens, K., Ghesquière, B., Timmerman, E., De Bock, P.-J., Chain, B. M., et al. (2010). A quantitative proteomics design for systematic identification of protease cleavage events. MOLECULAR & CELLULAR PROTEOMICS, 9(10), 2327–2333.
Vancouver
1.
Impens F, Colaert N, Helsens K, Ghesquière B, Timmerman E, De Bock P-J, et al. A quantitative proteomics design for systematic identification of protease cleavage events. MOLECULAR & CELLULAR PROTEOMICS. 2010;9(10):2327–33.
MLA
Impens, Francis, Niklaas Colaert, Kenny Helsens, et al. “A Quantitative Proteomics Design for Systematic Identification of Protease Cleavage Events.” MOLECULAR & CELLULAR PROTEOMICS 9.10 (2010): 2327–2333. Print.
@article{1064426,
  abstract     = {We present here a novel proteomics design for systematic identification of protease cleavage events by quantitative N-terminal proteomics, circumventing the need for time-consuming manual validation. We bypass the singleton detection problem of protease-generated neo-N-terminal peptides by introducing differential isotopic proteome labeling such that these substrate reporter peptides are readily distinguished from all other N-terminal peptides. Our approach was validated using the canonical human caspase-3 protease and further applied to mouse cathepsin D and E substrate processing in a mouse dendritic cell proteome, identifying the largest set of protein protease substrates ever reported and gaining novel insight into substrate specificity differences of these cathepsins.},
  author       = {Impens, Francis and Colaert, Niklaas and Helsens, Kenny and Ghesqui{\`e}re, Bart and Timmerman, Evy and De Bock, Pieter-Jan and Chain, Benjamin M and Vandekerckhove, Jo{\"e}l and Gevaert, Kris},
  issn         = {1535-9476},
  journal      = {MOLECULAR \& CELLULAR PROTEOMICS},
  keyword      = {SITES,SILAC,TOOL,EXPRESSION,CATHEPSIN-E,N-TERMINAL PEPTIDES,APOPTOSIS,PRODUCTS},
  language     = {eng},
  number       = {10},
  pages        = {2327--2333},
  title        = {A quantitative proteomics design for systematic identification of protease cleavage events},
  url          = {http://dx.doi.org/10.1074/mcp.M110.001271},
  volume       = {9},
  year         = {2010},
}

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