title: Weighing the proteasome for covalent modifications.
abstract: Posttranslational modifications (PTMs) control protein function, but established peptide-based proteomic methods often fail to provide a comprehensive view of PTMs. In this issue of Chemistry & Biology, Gersch et al. describe an efficient combination of chromatographic separation and top-down mass spectrometry that together with an intuitive visualization tool allowed them to screen the proteasome for PTMs and covalently binding inhibitors.
authors: Research Unit Functional Proteomics and Metabolic Pathways, Institute of Pathology, Medical University Graz, and Omics Center Graz, BioTechMed-Graz, A-8010 Graz, Austria.
authors: Ruth
authors: R
authors: Birner-Gruenberger
authors: Institute of Organic Chemistry, Graz University of Technology, A-8010 Graz, Austria. Electronic address: breinbauer@tugraz.at.
authors: Rolf
authors: R
authors: Breinbauer
mesh_terms: D006801:Humans; D046988:Proteasome Endopeptidase Complex / Q000032:analysis* / Q000378:metabolism*; D061988:Proteasome Inhibitors / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods*
chemical_list: D061988:Proteasome Inhibitors; D046988:Proteasome Endopeptidase Complex