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SHR Neuro Cancer Cardio Lipid Metab Microb

Birner-Gruenberger, R; Breinbauer, R.
Weighing the proteasome for covalent modifications.
Chem Biol. 2015; 22(3):315-316 Doi: 10.1016/j.chembiol.2015.03.003 [OPEN ACCESS]
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Leading authors Med Uni Graz: Birner-Grünberger Ruth
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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. Copyright © 2015 Elsevier Ltd. All rights reserved.
Find related publications in this database (using NLM MeSH Indexing): Humans -; Proteasome Endopeptidase Complex - analysis; Proteasome Endopeptidase Complex - metabolism; Proteasome Inhibitors - metabolism; Protein Processing, Post-Translational -; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods