ArticleMolecular bioSystems2010
Characterizing the connectivity of poly-ubiquitin chains by selected reaction monitoring mass spectrometry.
Article in Molecular bioSystems, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Drug Development Targeting the Ubiquitin-Proteasome System (UPS) for the Treatment of Human Cancers.Cancers · 2020Review
- Proteomics Links Ubiquitin Chain Topology Change to Transcription Factor Activation.Molecular cell · 2019Article
- Linear Ubiquitin Chains: Cellular Functions and Strategies for Detection and Quantification.Frontiers in chemistry · 2019Review
- Application of targeted mass spectrometry in bottom-up proteomics for systems biology research.Journal of proteomics · 2018Review
- Quantitative proteomic analysis of Parkin substrates in Drosophila neurons.Molecular neurodegeneration · 2017Article
- Bimodal antagonism of PKA signalling by ARHGAP36.Nature communications · 2016Article
- Post-translational modification profiling - A novel tool for mapping the protein modification landscape in cancer.Experimental biology and medicine (Maywood, N.J.) · 2016Review
- Quantifying ubiquitin signaling.Molecular cell · 2015Review
- Top-down 193-nm ultraviolet photodissociation mass spectrometry for simultaneous determination of polyubiquitin chain length and topology.Analytical chemistry · 2015Article
- When ubiquitination meets phosphorylation: a systems biology perspective of EGFR/MAPK signalling.Cell communication and signaling : CCS · 2013Review
- Using glycinylation, a chemical derivatization technique, for the quantitation of ubiquitinated proteins.Analytical chemistry · 2013Article
- Proteomic identification and analysis of K63-linked ubiquitin conjugates.Analytical chemistry · 2012Article
- Selected reaction monitoring-based proteomics: workflows, potential, pitfalls and future directions.Nature methods · 2012Review
- Improved quantitative mass spectrometry methods for characterizing complex ubiquitin signals.Molecular & cellular proteomics : MCP · 2011Article
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6 authors.
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Abstract
Protein ubiquitination is an essential post-translational modification (PTM) involved in the regulation of a variety of cellular functions, including transcription and protein degradation. Proteins can be both mono- or poly-ubiquitinated. Poly-ubiquitin chains vary in the manner by which the ubiquitin proteins are linked and their total length. Different poly-ubiquitin structures are thought to specify different fates for the target protein but the correlation between poly-ubiquitin structures and their specific cellular function(s) is not well understood. We have developed a set of specific and quantitative targeted mass spectrometry assays to determine the frequency of different types of inter-ubiquitin linkages in poly-ubiquitin chains relative to the total ubiquitin concentration. We chemically synthesized heavy isotope labeled reference peptides that represent the products generated by tryptic digestion of the known forms of inter-ubiquitin links for the yeast Saccharomyces cerevisiae and human, in addition to all peptides from tryptic digestion of a single ubiquitin molecule for these two species. We used these peptides to develop optimized Selected Reaction Monitoring (SRM) assays for their unambiguous detection in biological samples. We used these assays to profile the frequency of the different types of inter-ubiquitin linkages in a mixture of in vitro assembled human poly-ubiquitin chains and 15 isolated poly-ubiquitinated proteins from S. cerevisiae. We then applied the method to detect toxin induced changes in the poly-ubiquitination profile in complex and enriched protein samples.
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