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Nature Research, Nature Methods, 7(7), p. 512-515, 2010

DOI: 10.1038/nmeth.1469

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Complementary positional proteomics for screening substrates of endo- and exoproteases

Journal article published in 2010 by Petra Van Damme ORCID, An Staes, Silvia Bronsoms ORCID, Kenny Helsens, Niklaas Colaert, Evy Timmerman, Francesc X. Aviles, Joël Vandekerckhove, Kris Gevaert ORCID
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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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.