ArticleMolecular & cellular proteomics : MCP2013
Using the ubiquitin-modified proteome to monitor protein homeostasis function.
Article in Molecular & cellular proteomics : MCP, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Article
- Decoys Untangle Complicated Redundancy and Reveal Targets of Circadian Clock F-Box Proteins.Plant physiology · 2018Article
- Ubiquitin diGLY Proteomics as an Approach to Identify and Quantify the Ubiquitin-Modified Proteome.Methods in molecular biology (Clifton, N.J.) · 2018Article
- Site-specific identification and quantitation of endogenous SUMO modifications under native conditions.Nature communications · 2017Article
- Using the Ubiquitin-modified Proteome to Monitor Distinct and Spatially Restricted Protein Homeostasis Dysfunction.Molecular & cellular proteomics : MCP · 2016Article
- The Unfolded Protein Response Triggers Site-Specific Regulatory Ubiquitylation of 40S Ribosomal Proteins.Molecular cell · 2015Article
- Quantifying ubiquitin signaling.Molecular cell · 2015Review
- Identification of candidate substrates for the Golgi Tul1 E3 ligase using quantitative diGly proteomics in yeast.Molecular & cellular proteomics : MCP · 2014Article
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Authors and funding
2 authors.
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Abstract
The ubiquitin system is essential for the maintenance of proper protein homeostasis function across eukaryotic species. Although the general enzymatic architecture for adding and removing ubiquitin from substrates is well defined, methods for the comprehensive investigation of cellular ubiquitylation targets have just started to emerge. Recent advances in ubiquitin-modified peptide enrichment have greatly increased the number of identified endogenous ubiquitylation targets, as well as the number of sites of ubiquitin attachment within these substrates. Herein we evaluate current strategies using mass-spectrometry-based proteomics to characterize ubiquitin and ubiquitin-like modifications. Using existing data, we describe the characteristics of the ubiquitin-modified proteome and discuss strategies for the biological interpretation of existing and future ubiquitin-based proteomic studies.
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Registered trials
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