ArticleJournal of mass spectrometry : JMS2016
Preparing to read the ubiquitin code: characterization of ubiquitin trimers by top-down mass spectrometry.
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 8 papers.
What it found
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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
8 citing papers in PubMed, 11 citations in OpenAlex.
- Genetic Code Expansion Approaches to Decipher the Ubiquitin Code.Chemical reviews · 2024Review
- Top-down analysis of novel synthetic branched proteins.Journal of mass spectrometry : JMS · 2019Article
- Analysis of the topology of ubiquitin chains.Methods in enzymology · 2019Article
- Top-Down Analysis of Branched Proteins Using Mass Spectrometry.Analytical chemistry · 2018Article
- The Ups and Downs of Repeated Cleavage and Internal Fragment Production in Top-Down Proteomics.Journal of the American Society for Mass Spectrometry · 2018Article
- Ubiquitin Chain Enrichment Middle-Down Mass Spectrometry Enables Characterization of Branched Ubiquitin Chains in Cellulo.Analytical chemistry · 2017Article
- Seven perspectives on GPCR H/D-exchange proteomics methods.F1000Research · 2017Article
- Preparing to read the ubiquitin code: top-down analysis of unanchored ubiquitin tetramers.Journal of mass spectrometry : JMS · 2016Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
The profound effects of ubiquitination on the movement and processing of cellular proteins depend exquisitely on the structures of monoubiquitin and polyubiquitin modifications. Unconjugated polyubiquitins also have a variety of intracellular functions. Structures and functions are not well correlated yet, because the structures of polyubiquitins and polyubiquitin modifications of proteins are difficult to decipher. We are moving towards a robust strategy to provide that structural information. In this report electron transfer dissociation mass spectra of six synthetic ubiquitin trimers (multiply branched proteins with molecular masses exceeding 25,600 Da) are examined using an Orbitrap Fusion Lumos instrument to determine how top-down mass spectrometry can characterize the chain topology and linkage sites in a single, facile workflow. The efficacy of this method relies on the formation, detection, and interpretation of extensive fragmentation.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.