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SHR Neuro Krebs Kardio Lipid Stoffw 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
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- Führende Autor*innen der 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