Evidence map›Paper›PMID 41293887›Full record

ArticleAnalytical chemistry2025

Multiplexed Data-Independent Acquisition-Based Proteomics Enabled by TMTpro Complementary Ions.

Zicong Wang, Peng-Kai Liu, Haiyan Lu, Lingjun Li

Abstract read
In one paragraph

Article in Analytical chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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

4 authors.

Zicong WangSchool of Pharmacy, University of Wisconsin─Madison, Madison, Wisconsin 53705, United States.ORCID 0009-0007-1965-6447
Peng-Kai LiuBiophysics Graduate Program, University of Wisconsin─Madison, Madison, Wisconsin 53705, United States.
Haiyan LuSchool of Pharmacy, University of Wisconsin─Madison, Madison, Wisconsin 53705, United States.
Lingjun LiSchool of Pharmacy, University of Wisconsin─Madison, Madison, Wisconsin 53705, United States.ORCID 0000-0003-0056-3869

Funding

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
Mass Spectrometric Studies of Neuropeptides in FeedingR01DK071801 · NIDDK · UNIVERSITY OF WISCONSIN-MADISON · PI LINGJUN LI · 2006 to 2026
$6.7M
Creating a region- specific biomolecular atlas of the brain of Alzheimer’s diseaseR01AG078794 · NIA · UNIVERSITY OF WISCONSIN-MADISON · PI LINGJUN LI, Luigi Puglielli · 2022 to 2026
$3.7M
DiLeu-enabled multiplexed quantitation for biomarker discovery and validation in Alzheimer’s diseaseR01AG052324 · NIA · UNIVERSITY OF WISCONSIN-MADISON · PI LINGJUN LI · 2023 to 2026
$2.3M
Acquisition of a High-Field Dual Source FTICR-MS for Pharmaceutical ResearchS10RR029531 · NCRR · UNIVERSITY OF WISCONSIN-MADISON · PI LI, LINGJUN · 2011 to 2011
$2.1M
Acquisition of a Dual-Source, High-Performance, Ion Mobility, Quadrupole Time-of-Flight Mass Spectrometry System for Biomedical Research at UW-MadisonS10OD028473 · OD · UNIVERSITY OF WISCONSIN-MADISON · PI LI, LINGJUN · 2021 to 2021
$1.3M
Acquisition of a High Resolution High Speed MALDI Mass Spectrometer for Biomedical Research at UW-MadisonS10OD025084 · OD · UNIVERSITY OF WISCONSIN-MADISON · PI LI, LINGJUN · 2018 to 2018
$598k
NCRR NIH HHS S10 RR029531NIA NIH HHS R01 AG052324NIA NIH HHS R01 AG078794NIDDK NIH HHS R01 DK071801NIGMS NIH HHS P41 GM108538NIH HHS S10 OD025084NIH HHS S10 OD028473
6 · The paper itself

Abstract

Data-independent acquisition (DIA) has emerged as a powerful approach in quantitative proteomics, offering more comprehensive and reproducible proteome coverage than the conventional data-dependent acquisition (DDA) method. However, applying multiplexed isobaric labeling to DIA has been challenging due to ratio distortion caused by coisolation and cofragmentation interference. Here, we present a 3-plex TMTpro complementary ion (TMTproC)-based DIA strategy that leverages complementary ions in isobaric labeling to achieve accurate quantification without increasing spectral complexity. By implementing a 4-Da spacing between complementary ions, we significantly reduce isotopic envelope overlap and simplify deconvolution. We systematically optimized higher-energy collisional dissociation (HCD) settings for complementary ion generation and validated this approach using tryptic bovine serum albumin (BSA) peptides labeled at 1:1:1, 10:5:1, and 1:5:10 ratios, achieving median peptide-level ratios within 10% of expected values and median coefficients of variation (CVs) below 4% across triplicates. We further demonstrated this method by applying TMTproC labeling across a 10-fold dynamic range to the yeast proteome in a strong human proteome background. The results exhibited high quantification precision and minimal ratio distortion. Overall, TMTproC-DIA provides a robust, versatile, and scalable solution for high-throughput DIA-based proteomics.

Indexed as

ProteomeProteomicsAnimalsCattleHumansIonsPeptidesSaccharomyces cerevisiaeSerum Albumin, BovineTandem Mass SpectrometryIonsPeptidesProteomeSerum Albumin, Bovine

Identifiers

PMID41293887
PMCPMC12874209

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.