Journal
CURRENT OPINION IN CHEMICAL BIOLOGY
Volume 17, Issue 1, Pages 49-58Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.cbpa.2012.12.009
Keywords
-
Categories
Funding
- Novo Nordisk Foundation Center for Protein Research
- Lundbeck Foundation
- European Union 7th Framework Program PRIME-XS [262067]
- European Union 7th Framework Program EURATRANS [HEALTH-F4-2010-241504]
- Novo Nordisk Fonden [NNF13OC0006477] Funding Source: researchfish
- Novo Nordisk Foundation Center for Protein Research [PI Michael Lund Nielsen] Funding Source: researchfish
Ask authors/readers for more resources
The attachment of one or more ubiquitin moieties to proteins plays a central regulatory mechanism in eukaryotic cells. Protein ubiquitylation regulates numerous cellular processes, including protein degradation, signal transduction, DNA repair and cell division. The characterization of ubiquitylation is a twofold challenge that involves the mapping of ubiquitylation sites and the determination of ubiquitin chain topology. This review focuses on the technical advances in the mass spectrometry-based characterization of ubiquitylation sites, which have recently involved the large-scale identification of ubiquitylation sites by peptide-level enrichment strategies. The discovery that ubiquitylation is a widespread modification similar to phosphorylation and acetylation suggests cross-talk may also occur at the post translational modification level.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available