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- W2004384571 abstract "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." @default.
- W2004384571 created "2016-06-24" @default.
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- W2004384571 date "2013-02-01" @default.
- W2004384571 modified "2023-10-13" @default.
- W2004384571 title "Advances in characterizing ubiquitylation sites by mass spectrometry" @default.
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- W2004384571 doi "https://doi.org/10.1016/j.cbpa.2012.12.009" @default.
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