ArticleJournal of mass spectrometry : JMS2019
Top-down analysis of novel synthetic branched proteins.
Article in Journal of mass spectrometry : JMS, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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
5 citing papers in PubMed.
- Capturing Cardiomyocyte Cell-to-Cell Heterogeneity via Shotgun Single Cell Top-Down Proteomics.bioRxiv : the preprint server for biology · 2026Article
- Identification of biomarkers for bull fertility using functional genomics.Animal reproduction · 2022Article
- FITC labeling of human insulin and transport of FITC-insulin conjugates through MDCK cell monolayer.Journal of pharmaceutical analysis · 2019Article
- Recent trends of capillary electrophoresis-mass spectrometry in proteomics research.Mass spectrometry reviews · 2019Review
- Analysis of the topology of ubiquitin chains.Methods in enzymology · 2019Article
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Authors and funding
7 authors.
Funding
Abstract
A strategy for top-down analysis of branched proteins has been reported earlier, which relies on electron transfer dissociation assisted by collisional activation, and software designed for graphic interpretation of tandem mass spectra and adapted for branched proteins. In the present study, the strategy is applied to identify unknown and novel products of reactions in which rationally mutated proteoforms of Rub1 are used to probe the selectivity of E1 and E2 enzymes normally active in ubiquitination. To test and demonstrate this application, components and attachment sites of three branched dimers are deduced and the mutations are confirmed.
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Registered trials
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