ArticleAnalytical chemistry2018
Top-Down Analysis of Branched Proteins Using Mass Spectrometry.
Article in Analytical chemistry, 2018. 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed.
- Capturing Cardiomyocyte Cell-to-Cell Heterogeneity via Shotgun Single Cell Top-Down Proteomics.bioRxiv : the preprint server for biology · 2026Article
- A breath-based in vitro diagnostic assay for the detection of lower respiratory tract infections.PNAS nexus · 2024Article
- 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
- Top-Down Proteomic Characterization of Truncated Proteoforms.Journal of proteome research · 2019Article
- 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
- Comprehensive characterization of the adult ND4 Swiss Webster mouse retina: Using discovery-based mass spectrometry to decipher the total proteome and phosphoproteome.Molecular vision · 2018Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Post-translational modifications by the covalent attachment of Rub1 (NEDD8), ubiquitin, SUMO, and other small signaling proteins have profound impacts on the functions and fates of cellular proteins. Investigations of the relationship of these bioactive structures and their functions are limited by analytical methods that are scarce and tedious. A novel strategy is reported here for the analysis of branched proteins by top-down mass spectrometry and illustrated by application to four recombinant proteins and one synthetic peptide modified by covalent bonds with ubiquitin or Rub1. The approach allows an analyte to be recognized as a branched protein; the participating proteins to be identified; the site of conjugation to be defined; and other chemical, native, and recombinant modifications to be characterized. In addition to the high resolution and high accuracy provided by the mass spectrometer, success is based on sample fragmentation by electron-transfer dissociation assisted by collisional activation and on software designed for graphic interpretation and adapted for branched proteins. The strategy allows for structures of unknown, two-component branched proteins to be elucidated directly the first time and can potentially be extended to more complex systems.
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Registered trials
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