Evidence map›Paper›PMID 42816593›Full record

ArticleNature structural & molecular biology2026

A phosphoproteome atlas of human cell lines reveals the landscape of kinase activity.

Claire Koenig, Hayoung Cho, Kristina B Emdal, Ilaria Piga, Pierre Sabatier, Samuel Lozano-Juárez, Ana Martinez-Val, Jesper V Olsen

Abstract read
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In one paragraph

Article in Nature structural & molecular biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

8 authors.

Claire KoenigNovo Nordisk Foundation Center for Protein Research and Copenhagen Center for Glycocalyx Research, Department of Cellular and Molecular Medicine, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.ORCID http://orcid.org/0000-0002-7327-2723
Hayoung ChoNovo Nordisk Foundation Center for Protein Research and Copenhagen Center for Glycocalyx Research, Department of Cellular and Molecular Medicine, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.
Kristina B EmdalNovo Nordisk Foundation Center for Protein Research and Copenhagen Center for Glycocalyx Research, Department of Cellular and Molecular Medicine, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.
Ilaria PigaNovo Nordisk Foundation Center for Protein Research and Copenhagen Center for Glycocalyx Research, Department of Cellular and Molecular Medicine, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.
Pierre SabatierNovo Nordisk Foundation Center for Protein Research and Copenhagen Center for Glycocalyx Research, Department of Cellular and Molecular Medicine, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.ORCID http://orcid.org/0000-0002-2734-1791
Samuel Lozano-JuárezCardiovascular Proteomics Laboratory, Centro Nacional de Investigaciones Cardiovasculares Carlos III, Madrid, Spain.ORCID http://orcid.org/0009-0000-2602-5773
Ana Martinez-ValCardiovascular Proteomics Laboratory, Centro Nacional de Investigaciones Cardiovasculares Carlos III, Madrid, Spain.ORCID http://orcid.org/0000-0002-8784-3822
Jesper V OlsenNovo Nordisk Foundation Center for Protein Research and Copenhagen Center for Glycocalyx Research, Department of Cellular and Molecular Medicine, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark. jesper.olsen@cpr.ku.dk.ORCID http://orcid.org/0000-0002-4747-4938

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein phosphorylation orchestrates cellular signaling and controls most biological processes, with its dysregulation driving diseases, notably cancer. Comprehensive, high-throughput phosphoproteomics remains limited by detection sensitivity, data completeness and computational bottlenecks, especially in low-input settings. Here we present a comprehensive empirical human phosphoproteome resource, regrouping over 200,000 class I phosphosites across 33 diverse human cell lines. We demonstrate that this spectral library dramatically improves single-shot phosphoproteomics with 30-fold faster data processing compared with library-free approaches and enhances confidence in phosphosite localization even from minimal sample input. Integrating proteome and phosphoproteome data, we develop a combined kinase activity score (Cscore), revealing cell line- and cancer-specific signaling vulnerabilities, many correlating with drug sensitivity. This resource accelerates deep and reproducible phosphoproteomics, enables the systematic mapping of cellular signaling networks and may empower precision oncology by highlighting actionable kinase targets in diverse cell states.

Identifiers

PMID42816593

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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.