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- Jonathan Woodsmith, Ulrich Stelzl, and Arunachalam Vinayagam.
- Otto-Warburg Laboratory, Max-Planck Institute for Molecular Genetics (MPIMG), Ihnestrasse 63-73, Berlin, Germany.
- Methods Mol. Biol. 2017 Jan 1; 1558: 321-332.
AbstractNormal cellular functioning is maintained by macromolecular machines that control both core and specialized molecular tasks. These machines are in large part multi-subunit protein complexes that undergo regulation at multiple levels, from expression of requisite components to a vast array of post-translational modifications (PTMs). PTMs such as phosphorylation, ubiquitination, and acetylation currently number more than 200,000 in the human proteome and function within all molecular pathways. Here we provide a framework for systematically studying these PTMs in the context of global protein-protein interaction networks. This analytical framework allows insight into which functions specific PTMs tend to cluster in, and furthermore which complexes either single or multiple PTM signaling pathways converge on.
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