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Chem Biol. 2015 Mar 19;22(3):315-6. doi: 10.1016/j.chembiol.2015.03.003.

Weighing the proteasome for covalent modifications.

Author information

1
Research Unit Functional Proteomics and Metabolic Pathways, Institute of Pathology, Medical University Graz, and Omics Center Graz, BioTechMed-Graz, A-8010 Graz, Austria.
2
Institute of Organic Chemistry, Graz University of Technology, A-8010 Graz, Austria. Electronic address: breinbauer@tugraz.at.

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.

PMID:
25794435
DOI:
10.1016/j.chembiol.2015.03.003
[Indexed for MEDLINE]
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