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Human neurodegenerative and infectious diseases and tumorigenesis are associated with alterations in ubiquitin pathways. Over 10% of the genome encode for genes that either bind or manipulate ubiquitin to affect a large proportion of biological processes. This has been the basis for the development of approaches allowing the enrichment of ubiquitinated proteins for comparisons using proteomics and mass spectrometry. Tools such as tagged tandem ubiquitin binding domains, chemically derivatized ubiquitin or anti-gly-gly-lys antibodies combined with mass spectrometry have contributed to surveys of poly-ubiquitinated proteins, poly-ubiquitin linkage diversity and protein ubiquitination sites and their relation to other posttranslational modifications at a proteome wide level, providing insights in to how dynamic alterations in ubiquitination and deubiquitination steps are associated with normal physiology and pathogenesis.

Original publication




Journal article


Curr Opin Chem Biol

Publication Date





59 - 65


Animals, Bacterial Infections, Humans, Inflammation, Mass Spectrometry, Models, Molecular, Neoplasms, Neurodegenerative Diseases, Protein Interaction Mapping, Proteomics, Signal Transduction, Ubiquitin, Ubiquitinated Proteins, Ubiquitination, Ubiquitins, Virus Diseases