Evidence map›Paper›PMID 31521607›Full record

ArticleCell systems2019

High-Throughput Assessment of Kinome-wide Activation States.

Thierry Schmidlin, Donna O Debets, Charlotte A G H van Gelder, Kelly E Stecker, Stamatia Rontogianni, Bart L van den Eshof, Kristel Kemper, Esther H Lips, Maartje van den Biggelaar, Daniel S Peeper and 2 more

Open access · hybridAbstract read
In one paragraph

Article in Cell systems, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

25 citing papers in PubMed, 45 citations in OpenAlex.

  1. Review
  2. Proteomic approaches for interrogating kinase signaling networks.The Journal of investigative dermatology · 2026
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  7. Hi-C sequencing unravels dynamic three-dimensional chromatin interactions in muntjac lineage: insights from chromosome fusions in Fea's muntjac genome.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2023
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  10. Review
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  15. Article
  16. Article
  17. Review
  18. Drug Discovery in Liver Disease Using Kinome Profiling.International journal of molecular sciences · 2021
    Review
  19. An Introduction to Advanced Targeted Acquisition Methods.Molecular & cellular proteomics : MCP · 2021
    Review
  20. 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

12 authors at 4 institutions in 1 country.

Thierry SchmidlinBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 CH Utrecht, the Netherlands; Netherlands Proteomics Center, Padualaan 8, 3584 CH Utrecht, the Netherlands.
Donna O DebetsBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 CH Utrecht, the Netherlands; Netherlands Proteomics Center, Padualaan 8, 3584 CH Utrecht, the Netherlands.
Charlotte A G H van GelderBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 CH Utrecht, the Netherlands; Netherlands Proteomics Center, Padualaan 8, 3584 CH Utrecht, the Netherlands.
Kelly E SteckerBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 CH Utrecht, the Netherlands; Netherlands Proteomics Center, Padualaan 8, 3584 CH Utrecht, the Netherlands.
Stamatia RontogianniBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 CH Utrecht, the Netherlands; Netherlands Proteomics Center, Padualaan 8, 3584 CH Utrecht, the Netherlands.
Bart L van den EshofSanquin Research, Department of Molecular and Cellular Hemostasis, Amsterdam, the Netherlands.
Kristel KemperDivision of Molecular Oncology, Oncode Institute, The Netherlands Cancer Institute, 1066 CX Amsterdam, the Netherlands.
Esther H LipsDepartment of Molecular Pathology, The Netherlands Cancer Institute, 1066 CX Amsterdam, the Netherlands.
Maartje van den BiggelaarSanquin Research, Department of Molecular and Cellular Hemostasis, Amsterdam, the Netherlands.
Daniel S PeeperDivision of Molecular Oncology, Oncode Institute, The Netherlands Cancer Institute, 1066 CX Amsterdam, the Netherlands.
Albert J R HeckBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 CH Utrecht, the Netherlands; Netherlands Proteomics Center, Padualaan 8, 3584 CH Utrecht, the Netherlands.
Maarten AltelaarBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 CH Utrecht, the Netherlands; Netherlands Proteomics Center, Padualaan 8, 3584 CH Utrecht, the Netherlands; Mass Spectrometry and Proteomics Facility, The Netherlands Cancer Institute, 1066 CX Amsterdam, the Netherlands. Electronic address: m.altelaar@uu.nl.
Utrecht University · NLOncode Institute · NLSanquin · NLThe Netherlands Cancer Institute · NL

Funding

European Research Council
6 · The paper itself

Abstract

Aberrant kinase activity has been linked to a variety of disorders; however, methods to probe kinase activation states in cells have been lacking. Until now, kinase activity has mainly been deduced from either protein expression or substrate phosphorylation levels. Here, we describe a strategy to directly infer kinase activation through targeted quantification of T-loop phosphorylation, which serves as a critical activation switch in a majority of protein kinases. Combining selective phosphopeptide enrichment with robust targeted mass spectrometry, we provide highly specific assays for 248 peptides, covering 221 phosphosites in the T-loop region of 178 human kinases. Using these assays, we monitored the activation of 63 kinases through 73 T-loop phosphosites across different cell types, primary cells, and patient-derived tissue material. The sensitivity of our assays is highlighted by the reproducible detection of TNF-α-induced RIPK1 activation and the detection of 46 T-loop phosphorylation sites from a breast tumor needle biopsy.

Indexed as

Biopsy, NeedleBreast NeoplasmsEnzyme ActivationFemaleHigh-Throughput Screening AssaysHumansJurkat CellsMass SpectrometryPeptidesPhosphorylationProteomicsReceptor-Interacting Protein Serine-Threonine KinasesReproducibility of ResultsSensitivity and SpecificityTumor Necrosis Factor-alphaPeptidesReceptor-Interacting Protein Serine-Threonine KinasesRIPK1 protein, humanTumor Necrosis Factor-alphacancerkinasekinase activityphosphoproteomicsproteomicssignalingSRMtargeted mass spectrometryT-loop phosphorylation

Identifiers

PMID31521607
PMCPMC6838672
OpenAlexW2972835101

What OpenQuestion 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 OpenQuestion graph.