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Complementary positional proteomics for screening substrates of endo- and exoproteases

Petra Van Damme UGent, An Staes UGent, Silvia Bronsoms, Kenny Helsens UGent, Niklaas Colaert UGent, Evy Timmerman UGent, Francesc X Aviles, Joël Vandekerckhove and Kris Gevaert UGent (2010) NATURE METHODS. 7(7). p.512-515
abstract
We describe a positional proteomics approach to simultaneously analyze N- and C-terminal peptides and used it to screen for human protein substrates of granzyme B and carboxypeptidase A4 in human cell lysates. This approach allowed comprehensive proteome studies, and we report the identification of 965 database-annotated protein C termini, 334 neo-C termini resulting from granzyme B processing and 16 neo-C termini resulting from carboxypeptidase A4 processing.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
PEPTIDES, TERMINI, GRANZYME-B, EXPRESSION, IDENTIFICATION, PROTEINS
journal title
NATURE METHODS
Nat. Methods
volume
7
issue
7
pages
512 - 515
Web of Science type
Article
Web of Science id
000279343300016
JCR category
BIOCHEMICAL RESEARCH METHODS
JCR impact factor
20.717 (2010)
JCR rank
1/70 (2010)
JCR quartile
1 (2010)
ISSN
1548-7091
DOI
10.1038/NMETH.1469
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
1021546
handle
http://hdl.handle.net/1854/LU-1021546
date created
2010-08-12 11:42:35
date last changed
2016-12-19 15:46:39
@article{1021546,
  abstract     = {We describe a positional proteomics approach to simultaneously analyze N- and C-terminal peptides and used it to screen for human protein substrates of granzyme B and carboxypeptidase A4 in human cell lysates. This approach allowed comprehensive proteome studies, and we report the identification of 965 database-annotated protein C termini, 334 neo-C termini resulting from granzyme B processing and 16 neo-C termini resulting from carboxypeptidase A4 processing.},
  author       = {Van Damme, Petra and Staes, An and Bronsoms, Silvia and Helsens, Kenny and Colaert, Niklaas and Timmerman, Evy and Aviles, Francesc X and Vandekerckhove, Jo{\"e}l and Gevaert, Kris},
  issn         = {1548-7091},
  journal      = {NATURE METHODS},
  keyword      = {PEPTIDES,TERMINI,GRANZYME-B,EXPRESSION,IDENTIFICATION,PROTEINS},
  language     = {eng},
  number       = {7},
  pages        = {512--515},
  title        = {Complementary positional proteomics for screening substrates of endo- and exoproteases},
  url          = {http://dx.doi.org/10.1038/NMETH.1469},
  volume       = {7},
  year         = {2010},
}

Chicago
Van Damme, Petra, An Staes, Silvia Bronsoms, Kenny Helsens, Niklaas Colaert, Evy Timmerman, Francesc X Aviles, Joël Vandekerckhove, and Kris Gevaert. 2010. “Complementary Positional Proteomics for Screening Substrates of Endo- and Exoproteases.” Nature Methods 7 (7): 512–515.
APA
Van Damme, Petra, Staes, A., Bronsoms, S., Helsens, K., Colaert, N., Timmerman, E., Aviles, F. X., et al. (2010). Complementary positional proteomics for screening substrates of endo- and exoproteases. NATURE METHODS, 7(7), 512–515.
Vancouver
1.
Van Damme P, Staes A, Bronsoms S, Helsens K, Colaert N, Timmerman E, et al. Complementary positional proteomics for screening substrates of endo- and exoproteases. NATURE METHODS. 2010;7(7):512–5.
MLA
Van Damme, Petra, An Staes, Silvia Bronsoms, et al. “Complementary Positional Proteomics for Screening Substrates of Endo- and Exoproteases.” NATURE METHODS 7.7 (2010): 512–515. Print.