Abstract
To be able to understand the mechanisms of action of drugs, predict their efficacy, and anticipate their potential side-effects is important during drug development. In diseases where the genetic background of patients modulates treatment response, it might allow personalizing the therapy.
Substantial progress in proteomic technologies[1] have made it possible to develop chemical proteomics methods, where the protein targets of a drug are affinity-purified and identified by mass spectrometry[2, 3]. Compound-protein interactions are measured in a biological context as opposed to in vitro binding assays. That is, drugprotein interactions can not only be determined proteome-wide, but also in a tissue- or cell type-dependent manner.
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Colinge, J., Rix, U., Bennett, K.L., Superti-Furga, G. (2012). Systems Biology Analysis of Kinase Inhibitor Protein Target Profiles in Leukemia Treatments. In: Lones, M.A., Smith, S.L., Teichmann, S., Naef, F., Walker, J.A., Trefzer, M.A. (eds) Information Processign in Cells and Tissues. IPCAT 2012. Lecture Notes in Computer Science, vol 7223. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-28792-3_9
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DOI: https://doi.org/10.1007/978-3-642-28792-3_9
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