Evidence map›Paper›PMID 40293921›Full record

ArticleJournal of proteome research2025

SPE-CZE-MS Quantifies Zeptomole Amounts of Phosphorylated Peptides.

Lia R Serrano, J Scott Mellors, J Will Thompson, Noah M Lancaster, Margaret Lea Robinson, Katherine A Overmyer, Scott T Quarmby, Joshua J Coon

Abstract read
In one paragraph

Article in Journal of proteome research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

7 citing papers in PubMed.

  1. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors.

Lia R SerranoDepartment of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, United States.ORCID 0000-0001-5662-5884
J Scott Mellors908 Devices Inc., Boston, Massachusetts 02210, United States.ORCID 0000-0002-6658-3961
J Will Thompson908 Devices Inc., Boston, Massachusetts 02210, United States.
Noah M LancasterDepartment of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, United States.ORCID 0009-0002-3609-7951
Margaret Lea RobinsonDepartment of Biomolecular Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, United States.
Katherine A OvermyerNational Center for Quantitative Biology of Complex Systems, Madison, Wisconsin 53706, United States.ORCID 0000-0002-1929-1229
Scott T QuarmbyDepartment of Biomolecular Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, United States.ORCID 0000-0003-2991-5637
Joshua J CoonDepartment of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, United States.ORCID 0000-0002-0004-8253

Funding

Institutional Training in the Genomic SciencesT32HG002760 · NHGRI · UNIVERSITY OF WISCONSIN-MADISON · PI Qiongshi Lu · 2003 to 2026
$17.7M
TR&D 2 Metabolic Labels for Ultraplexed Protein Quantification p. 453P41GM108538 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI COON, JOSHUA J · 2016 to 2025
$13.1M
Structure, Function and Regulation of the ProteomeR35GM118110 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI COON, JOSHUA J · 2016 to 2025
$9.1M
Biotechnology Training ProgramT32GM135066 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI SCOTT M. COYLE, BRIAN G FOX · 2020 to 2026
$7.0M
NHGRI NIH HHS T32 HG002760NIGMS NIH HHS P41 GM108538NIGMS NIH HHS R35 GM118110NIGMS NIH HHS T32 GM135066
6 · The paper itself

Abstract

Capillary zone electrophoresis (CZE) is gaining attention in the field of single-cell proteomics for its ultralow-flow and high-resolution separation abilities. Even more sample-limited yet rich in biological information are phosphoproteomics experiments, as the phosphoproteome composes only a fraction of the whole cellular proteome. Rapid analysis, high sensitivity, and maximization of sample utilization are paramount for single-cell analysis. Some challenges of coupling CZE analysis with mass spectrometry analysis (MS) of complex mixtures include 1. sensitivity due to volume loading limitations of CZE and 2. incompatibility of MS duty cycles with electropherographic time scales. Here, we address these two challenges as applied to single-cell-equivalent phosphoproteomics experiments by interfacing a microchip-based CZE device integrated with a solid-phase-extraction (SPE) bed with the Orbitrap Astral mass spectrometer. Using 225 phosphorylated peptide standards and phosphorylated peptide-enriched mouse brain tissue, we investigate microchip-based SPE-CZE functionality, quantitative performance, and complementarity to nano-LC-MS (nLC-MS) analysis. We highlight unique SPE-CZE separation mechanisms that can empower fit-for-purpose applications in single-cell-equivalent phosphoproteomics.

Indexed as

Mass SpectrometryPhosphopeptidesProteomicsSolid Phase ExtractionAnimalsElectrophoresis, CapillaryMicePhosphorylationSingle-Cell AnalysisPhosphopeptidesAstralcapillary zone electrophoresisphosphoproteomicspreconcentrationSPE

Identifiers

PMID40293921
PMCPMC12153072

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LicenceCC BY-NC-ND
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Registered trials

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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.