Evidence map›Paper›PMID 39196334›Full record

ArticleAnalytical and bioanalytical chemistry2024

Capillary zone electrophoresis-tandem mass spectrometry for in-depth proteomics analysis via data-independent acquisition.

Rong Liu, Gang Lu, Xiaozhong Hu, Junhui Li, Zhenbin Zhang, Keqi Tang

Abstract read
PubMed Publisher
In one paragraph

Article in Analytical and bioanalytical chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Review
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  3. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Rong LiuZhejiang Engineering Research Center of Advanced Mass Spectrometry and Clinical Application, Institute of Mass Spectrometry, Ningbo University, Ningbo, 315211, PR China.
Gang LuInstitute of Drug Discovery Technology, Ningbo University, Ningbo, 315211, PR China.
Xiaozhong HuZhejiang Engineering Research Center of Advanced Mass Spectrometry and Clinical Application, Institute of Mass Spectrometry, Ningbo University, Ningbo, 315211, PR China.
Junhui LiZhejiang Engineering Research Center of Advanced Mass Spectrometry and Clinical Application, Institute of Mass Spectrometry, Ningbo University, Ningbo, 315211, PR China.
Zhenbin ZhangInstitute of Drug Discovery Technology, Ningbo University, Ningbo, 315211, PR China.
Keqi TangZhejiang Engineering Research Center of Advanced Mass Spectrometry and Clinical Application, Institute of Mass Spectrometry, Ningbo University, Ningbo, 315211, PR China. tangkeqi@nbu.edu.cn.

Funding

National Key Research and Development Program of China 2023YFC3304203the K.C. Wong Magna Fund in Ningbo University xkzwl1507the Key Research and Development Program of Zhejiang Province 2020C03064the Key Research and Development Program of Zhejiang Province 2024C03101the Key Research and Development Program of Zhejiang Province 2024C03266the National Natural Science Foundation of China 22374084the National Natural Science Foundation of China U20A20121the Natural Science Foundation of Zhejiang Province LGC22B050002the Natural Science Foundation of Zhejiang Province LY22F010004the Ningbo Science and Technology Project 2022Z241the Ningbo Science and Technology Project 2023S151the Ningbo Science and Technology Project 2023Z132the Ningbo Science and Technology Project 2023Z168Yangtze River Delta Science and Technology Innovation Community Joint Research Project 2023CSJGG1800
6 · The paper itself

Abstract

A capillary zone electrophoresis (CZE) system was coupled to an Orbitrap mass spectrometer operating in a data-independent acquisition (DIA) mode for in-depth proteomics analysis. The performance of this CZE-DIA-MS system was systemically evaluated and optimized under different operating conditions. The performance of the fully optimized CZE-DIA-MS system was subsequently compared to the one by using the same CZE-MS system operating in a data-dependent acquisition (DDA) mode. The experimental results show that the numbers of identified peptides and proteins acquired in the DIA mode are much higher than the ones acquired in the DDA mode, especially with the small sample loading amount. Specifically, the numbers of identified peptides and proteins acquired in the DIA mode are 1.8-fold and 2-fold higher than the ones acquired in the DDA mode by using 12.5 ng Hela digests. The proteins identified in the DIA mode also cover almost all the proteins identified in the DDA mode. In addition, a potential cancer biomarker protein, carbohydrate antigen 125, undetected in the DDA mode, can be easily identified in the DIA mode even with 12.5 ng Hela digests. The performance of the CZE-DIA-MS system for in-depth proteomics analysis with a limited sample amount has been fully demonstrated for the first time through this study.

Indexed as

Electrophoresis, CapillaryProteomicsTandem Mass SpectrometryHeLa CellsHumansPeptidesProteinsPeptidesProteinsBiomarker proteinBottom-up proteomicsCapillary zone electrophoresisData-dependent acquisitionData-independent acquisitionMass spectrometry

Identifiers

PMID39196334

What OpenQuestion holds

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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.