Advances in characterizing ubiquitylation sites by mass spectrometry
Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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 two-fold 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.
Originalsprog | Engelsk |
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Tidsskrift | Current Opinion in Chemical Biology |
Vol/bind | 17 |
Udgave nummer | 1 |
Sider (fra-til) | 49-58 |
Antal sider | 10 |
ISSN | 1367-5931 |
DOI | |
Status | Udgivet - 5 jan. 2013 |
ID: 46438909