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Sigpep: Calculating unique peptide signature transition sets in a complete proteome background

Authors

  • Kenny Helsens,

    1. Department of Medical Protein Research, VIB, Ghent, Belgium
    2. Department of Biochemistry, Ghent University, Ghent, Belgium
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    • These authors contributed equally to this work.

  • Michael Mueller,

    1. EMBL Outstation, European Bioinformatics Institute, Wellcome Trust Genome Campus, Cambridge, UK
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    • These authors contributed equally to this work.

    • Current address: MRC Clinical Sciences Centre, Imperial College London, London, UK

  • Niels Hulstaert,

    1. Department of Medical Protein Research, VIB, Ghent, Belgium
    2. Department of Biochemistry, Ghent University, Ghent, Belgium
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  • Lennart Martens

    Corresponding author
    1. Department of Medical Protein Research, VIB, Ghent, Belgium
    2. Department of Biochemistry, Ghent University, Ghent, Belgium
    • Correspondence: Professor Lennart Martens, Department of Medical Protein Research and Biochemistry, VIB and Faculty of Medicine and Health Sciences, Ghent University, A. Baertsoenkaai 3, B-9000 Ghent, Belgium

      E-mail: lennart.martens@ugent.be

      Fax: +32-92649484

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Abstract

We have created a new software platform called sigpep that analyzes transition redundancy in selected reaction monitoring assays. Building on this platform, we also created a web application to generate transition sets with unique signatures for targeted peptides. The platform has been made available under the permissive Apache 2.0 open-source license, and the web application can be accessed from http://iomics.ugent.be/sigpep.

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