publication . Article . Other literature type . 2011

Systematic and Quantitative Assessment of the Ubiquitin-Modified Proteome

Kim, Woong; Bennett, Eric J.; Huttlin, Edward L.; Guo, Ailan; Li, Jing; Possemato, Anthony; Sowa, Mathew E.; Rad, Ramin; Rush, John; Comb, Michael J.; ...
Open Access
  • Published: 01 Oct 2011 Journal: Molecular Cell, volume 44, pages 325-340 (issn: 1097-2765, Copyright policy)
  • Publisher: Elsevier BV
Abstract
Summary Despite the diverse biological pathways known to be regulated by ubiquitylation, global identification of substrates that are targeted for ubiquitylation has remained a challenge. To globally characterize the human ubiquitin-modified proteome (ubiquitinome), we utilized a monoclonal antibody that recognizes diglycine (diGly)-containing isopeptides following trypsin digestion. We identify ∼19,000 diGly-modified lysine residues within ∼5000 proteins. Using quantitative proteomics we monitored temporal changes in diGly site abundance in response to both proteasomal and translational inhibition, indicating both a dependence on ongoing translation to observe ...
Subjects
free text keywords: Cell Biology, Molecular Biology, Biochemistry, Biology, Ubiquitin, biology.protein, Quantitative proteomics, Enzyme, chemistry.chemical_classification, chemistry, Proteomics, Lysine, Biological pathway, Proteome, Cullin Proteins, Article
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