ArticleJournal of proteome research2026
Advancing the Reproducibility and Repeatability of Capillary Zone Electrophoresis-Mass Spectrometry-Based Top-Down Proteomics by an Improved Capillary Coating Procedure.
Article in Journal of proteome research, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
2 citing papers in PubMed.
- Modulating proteoform charge states and signal intensities in LC-MS using a nanoflow sheath liquid interface.Analytical and bioanalytical chemistry · 2026Article
- Native Multidimensional Protein Complex Identification and Topology Characterization (Native MudPIT).Analytical chemistry · 2026Article
Corrections and comments
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Capillary zone electrophoresis (CZE)-mass spectrometry (MS) has attracted tremendous attention in top-down proteomics (TDP). However, its reproducibility and long-term repeatability for TDP remain concerns, most likely due to capillary coating. Here, we present an improved procedure for making linear polyacrylamide (LPA) coating, the most widely used coating in CE-MS-based proteomics, to boost the reproducibility and long-term repeatability of CZE-MS-based TDP. We focused on the step of degassing the polymerization solution, a critical step for achieving consistent LPA coating quality. The CZE-MS system using LPA-coated capillaries prepared with the optimal degassing procedure produced excellent reproducibility and repeatability for proteoform analysis. The 210 CZE-MS runs of three protein samples (a standard protein mixture, an
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Registered trials
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