Evidence map›Paper›PMID 37328457›Full record

ArticleNature communications2023

Hybrid-DIA: intelligent data acquisition integrates targeted and discovery proteomics to analyze phospho-signaling in single spheroids.

Ana Martínez-Val, Kyle Fort, Claire Koenig, Leander Van der Hoeven, Giulia Franciosa, Thomas Moehring, Yasushi Ishihama, Yu-Ju Chen, Alexander Makarov, Yue Xuan and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
7.8field-weighted citation impact, top 2% of its field
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

26 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
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  6. Observational
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  8. Review
  9. Endogenous Phosphopeptidomics Analysis by Using Mesoporous IMAC Materials.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Mapping Nanoscale-To-Single-Cell Phosphoproteomic Landscape by Chip-DIA.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  16. Review
  17. Review
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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

11 authors at 5 institutions in 6 countries.

Ana Martínez-ValNovo Nordisk Foundation Center for Protein Research, University of Copenhagen, Copenhagen, Denmark.ORCID 0000-0002-8784-3822
Kyle FortThermo Fisher Scientific, Bremen, Germany.
Claire KoenigNovo Nordisk Foundation Center for Protein Research, University of Copenhagen, Copenhagen, Denmark.ORCID 0000-0002-7327-2723
Leander Van der HoevenNovo Nordisk Foundation Center for Protein Research, University of Copenhagen, Copenhagen, Denmark.ORCID 0000-0003-4005-580X
Giulia FranciosaNovo Nordisk Foundation Center for Protein Research, University of Copenhagen, Copenhagen, Denmark.ORCID 0000-0001-5309-5558
Thomas MoehringThermo Fisher Scientific, Bremen, Germany.
Yasushi IshihamaKyoto University, Kyoto, Japan.ORCID 0000-0001-7714-203X
Yu-Ju ChenAcademia Sinica, Taipei, Taiwan.ORCID 0000-0002-3178-6697
Alexander MakarovThermo Fisher Scientific, Bremen, Germany.ORCID 0000-0002-7046-6709
Yue XuanThermo Fisher Scientific, Bremen, Germany. yue.xuan@thermofisher.com.ORCID 0000-0001-9132-2643
Jesper V OlsenNovo Nordisk Foundation Center for Protein Research, University of Copenhagen, Copenhagen, Denmark. jesper.olsen@cpr.ku.dk.ORCID 0000-0002-4747-4938
University of Copenhagen · DKThermo Fisher Scientific (Germany) · DEAcademia Sinica · TWKyoto University · JPThermo Fisher Scientific (Canada) · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Achieving sufficient coverage of regulatory phosphorylation sites by mass spectrometry (MS)-based phosphoproteomics for signaling pathway reconstitution is challenging, especially when analyzing tiny sample amounts. To address this, we present a hybrid data-independent acquisition (DIA) strategy (hybrid-DIA) that combines targeted and discovery proteomics through an Application Programming Interface (API) to dynamically intercalate DIA scans with accurate triggering of multiplexed tandem mass spectrometry (MSx) scans of predefined (phospho)peptide targets. By spiking-in heavy stable isotope labeled phosphopeptide standards covering seven major signaling pathways, we benchmark hybrid-DIA against state-of-the-art targeted MS methods (i.e., SureQuant) using EGF-stimulated HeLa cells and find the quantitative accuracy and sensitivity to be comparable while hybrid-DIA also profiles the global phosphoproteome. To demonstrate the robustness, sensitivity, and biomedical potential of hybrid-DIA, we profile chemotherapeutic agents in single colon carcinoma multicellular spheroids and evaluate the phospho-signaling difference of cancer cells in 2D vs 3D culture.

Indexed as

PhosphopeptidesProteomicsHeLa CellsHumansProteomeSignal TransductionTandem Mass SpectrometryPhosphopeptidesProteome

Identifiers

PMID37328457
PMCPMC10276052
OpenAlexW4380992764

What Socratic holds

Textmetadata
LicenceCC BY
Read underepoch 390

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 Socratic graph.