Evidence map›Paper›PMID 39196601›Full record

ArticleAngewandte Chemie (International ed. in English)2024

Native Proteomics by Capillary Zone Electrophoresis-Mass Spectrometry.

Qianyi Wang, Qianjie Wang, Zihao Qi, William Moeller, Vicki H Wysocki, Liangliang Sun

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed.

  1. A Draft Map of E. coli Proteoforms.Analytical chemistry · 2026
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  15. Formation of a β-Endorphin Corona Mitigates Alzheimer's Amyloidogenesis.Small (Weinheim an der Bergstrasse, Germany) · 2025
    Article
  16. Article
  17. Capillary Electrophoresis-Mass Spectrometry for Top-Down Proteomics.Annual review of analytical chemistry (Palo Alto, Calif.) · 2025
    Review
  18. Article
  19. Article
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Qianyi WangDepartment of Chemistry, Michigan State University, 578 S Shaw Lane, East Lansing, Michigan, 48824, United States.
Qianjie WangDepartment of Chemistry, Michigan State University, 578 S Shaw Lane, East Lansing, Michigan, 48824, United States.
Zihao QiDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, Ohio, 43210, United States.
William MoellerDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, Ohio, 43210, United States.
Vicki H WysockiDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, Ohio, 43210, United States.
Liangliang SunDepartment of Chemistry, Michigan State University, 578 S Shaw Lane, East Lansing, Michigan, 48824, United States.ORCID 0000-0001-8939-5042

Funding

Native Mass Spectrometry Guided Structural Biology CenterRM1GM149374 · NIGMS · OHIO STATE UNIVERSITY · PI Vicki H. Wysocki · 2023 to 2026
$5.0M
Computational tools for top down mass spectrometry based proteoform identification and proteogenomicsR01GM118470 · NIGMS · TULANE UNIVERSITY OF LOUISIANA · PI Xiaowen Liu · 2016 to 2026
$2.7M
Quantitative top-down proteomics of human colorectal cancer cells and tumorsR01CA247863 · NCI · MICHIGAN STATE UNIVERSITY · PI HUMMON, AMANDA B., LIU, XIAOWEN · 2021 to 2025
$1.9M
Quantitative proteomics of Zebrafish embryos and blastomeresR01GM125991 · NIGMS · MICHIGAN STATE UNIVERSITY · PI SUN, LIANGLIANG · 2018 to 2022
$1.7M
Division of Biological Infrastructure 1846913NCI NIH HHS R01 CA247863NCI NIH HHS R01CA247863NIGMS NIH HHS R01 GM118470NIGMS NIH HHS R01GM118470NIGMS NIH HHS R01 GM125991NIGMS NIH HHS R01GM125991NIGMS NIH HHS RM1 GM149374NIGMS NIH HHS RM1GM149374
6 · The paper itself

Abstract

Native proteomics measures endogenous proteoforms and protein complexes under a near physiological condition using native mass spectrometry (nMS) coupled with liquid-phase separations. Native proteomics should provide the most accurate bird's-eye view of proteome dynamics within cells, which is fundamental for understanding almost all biological processes. nMS has been widely employed to characterize well-purified protein complexes. However, there are only very few trials of utilizing nMS to measure proteoforms and protein complexes in a complex sample (i.e., a whole cell lysate). Here, we pioneer the native proteomics measurement of large proteoforms or protein complexes up to 400 kDa from a complex proteome via online coupling of native capillary zone electrophoresis (nCZE) to an ultra-high mass range (UHMR) Orbitrap mass spectrometer. The nCZE-MS technique enabled the measurement of a 115-kDa standard protein complex while consuming only about 0.1 ng of protein material. nCZE-MS analysis of an E.coli cell lysate detected 72 proteoforms or protein complexes in a mass range of 30-400 kDa in a single run while consuming only 50-ng protein material. The mass distribution of detected proteoforms or protein complexes agreed well with that from mass photometry measurement. This work represents a technical breakthrough in native proteomics for measuring complex proteomes.

Indexed as

Electrophoresis, CapillaryMass SpectrometryProteomicsEscherichia coliProteomeProteomeCapillary zone electrophoresisMass photometryNative mass spectrometryNative proteomicsProtein complex

Identifiers

PMID39196601
PMCPMC11646347

What OpenQuestion holds

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Registered trials

None linked

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.