ArticleJournal of mass spectrometry : JMS2016
Preparing to read the ubiquitin code: top-down analysis of unanchored ubiquitin tetramers.
Article in Journal of mass spectrometry : JMS, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed.
- Genetic Code Expansion Approaches to Decipher the Ubiquitin Code.Chemical reviews · 2024Review
- Getting to the Root of Branched Ubiquitin Chains: A Review of Current Methods and Functions.Methods in molecular biology (Clifton, N.J.) · 2023Review
- Current methodologies in protein ubiquitination characterization: from ubiquitinated protein to ubiquitin chain architecture.Cell & bioscience · 2022Review
- Analysis of the topology of ubiquitin chains.Methods in enzymology · 2019Article
- Top-down analysis of novel synthetic branched proteins.Journal of mass spectrometry : JMS · 2019Article
- Top-Down Analysis of Branched Proteins Using Mass Spectrometry.Analytical chemistry · 2018Article
- Ubiquitin Chain Enrichment Middle-Down Mass Spectrometry Enables Characterization of Branched Ubiquitin Chains in Cellulo.Analytical chemistry · 2017Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
The characterization of polyubiquitin chains has been an analytical challenge for several decades. It has been shown that anchored and unanchored polyubiquitin chains with different isopeptide linkages and lengths exhibit a wide range of profoundly different cellular functions. However, structure function studies have been hindered by the difficulty of characterizing these complex chain structures. This report presents a broadly applicable workflow to characterize ubiquitin tetramers without the need for genetic mutations or reiterative immunoprecipitations. We use a top-down proteomic strategy that exploits ETciD activation on an orbitrap Fusion Lumos and manual interpretation aided by graphical interpretation of mass shifts to facilitate characterization of chain topography and lysine linkage sites. Our workflow differentiates all topological features of the numerous isomers of tetraubiquitin, which have molecular masses in excess of 34 000 Da and identifies linkage sites in these branched proteins. Copyright © 2016 John Wiley & Sons, Ltd.
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Registered trials
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