ArticleProteomics2014
Optimizing capillary electrophoresis for top-down proteomics of 30-80 kDa proteins.
Article in Proteomics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 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
49 citing papers in PubMed.
- Intact Proteoform Analysis by Capillary Electrophoresis-Mass Spectrometry. Are We There Yet?Angewandte Chemie (International ed. in English) · 2026Article
- Intact Mass Profiling Reveals Phospho-Proteoforms of the Catenins (85-110 kDa) Regulated by Actomyosin Contractility.Angewandte Chemie (International ed. in English) · 2025Article
- Top-Down Thermal Proteome Profiling (TD-TPP) for Functional Characterization of the Intact Proteoforms in Complex Samples.Journal of mass spectrometry : JMS · 2025Article
- Capillary Electrophoresis-Mass Spectrometry for Top-Down Proteomics.Annual review of analytical chemistry (Palo Alto, Calif.) · 2025Review
- Quantitative Top-down Proteomics Revealed Kinase Inhibitor-Induced Proteoform-Level Changes in Cancer Cells.Journal of proteome research · 2025Article
- Top-Down Stability of Proteins from Rates of Oxidation (TD-SPROX) Approach for Measuring Proteoform-Specific Folding Stability.Analytical chemistry · 2024Article
- A simple and efficient approach for preparing cationic coating with tunable electroosmotic flow for capillary zone electrophoresis-mass spectrometry-based top-down proteomics.Analytica chimica acta · 2024Article
- Mass Spectrometry-Based Top-Down Proteomics in Nanomedicine: Proteoform-Specific Measurement of Protein Corona.ACS nano · 2024Article
- Mass spectrometry-intensive top-down proteomics: an update on technology advancements and biomedical applications.Analytical methods : advancing methods and applications · 2024Review
- Multidimensional Separations in Top-Down Proteomics.Analytical science advances · 2023Article
- Recent advances (2019-2021) of capillary electrophoresis-mass spectrometry for multilevel proteomics.Mass spectrometry reviews · 2023Review
- Mass spectrometry-based proteomics for advancing solid organ transplantation research.Frontiers in transplantation · 2023Review
- Fourier-transform ion cyclotron resonance mass spectrometry for characterizing proteoforms.Mass spectrometry reviews · 2022Review
- Capillary Zone Electrophoresis-Electron-Capture Collision-Induced Dissociation on a Quadrupole Time-of-Flight Mass Spectrometer for Top-Down Characterization of Intact Proteins.Journal of the American Society for Mass Spectrometry · 2021Article
- Quantitative Top-Down Proteomics in Complex Samples Using Protein-Level Tandem Mass Tag Labeling.Journal of the American Society for Mass Spectrometry · 2021Article
- CE-MS for Proteomics and Intact Protein Analysis.Advances in experimental medicine and biology · 2021Article
- Capillary Zone Electrophoresis-Tandem Mass Spectrometry with Activated Ion Electron Transfer Dissociation for Large-scale Top-down Proteomics.Journal of the American Society for Mass Spectrometry · 2019Article
- Recent trends of capillary electrophoresis-mass spectrometry in proteomics research.Mass spectrometry reviews · 2019Review
- Capillary zone electrophoresis-mass spectrometry for top-down proteomics.Trends in analytical chemistry : TRAC · 2019Article
- Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
The direct analysis of intact proteins via MS offers compelling advantages in comparison to alternative methods due to the direct and unambiguous identification and characterization of protein sequences it provides. The inability to efficiently analyze proteins in the "middle mass range," defined here as proteins from 30 to 80 kDa, in a robust fashion has limited the adoption of these "top-down" methods. Largely, a result of poor liquid chromatographic performance, the limitations in this mass range may be addressed by alternative separations that replace chromatography. Herein, the short migration times of CZE-ESI-MS/MS have been extended to size-sorted whole proteins in complex mixtures from Pseudomonas aeruginosa PA01. An electrokinetically pumped nanospray interface, a coated capillary, and a stacking method for on-column sample concentration were developed to achieve high-loading capacity and separation resolution. We achieved full width at half maximum of 8-16 s for model proteins up to 29 kDa and identified 30 proteins in the mass range of 30-80 kDa from P. aeruginosa PA01 whole cell lysate. These results suggest that CZE-ESI-MS/MS is capable of identifying proteins in the middle mass range in top-down proteomics.
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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.