Evidence map›Paper›PMID 40862632›Full record

ArticleJournal of proteome research2025

diaPASEF-Powered Chemoproteomics Enables Deep Kinome Interaction Profiling.

Kathryn Woods, Alexandria M Chan, Thankhoe A Rants'o, Tanmay Sapre, Grace E Mastin, Kathleen M Maguire, Shao-En Ong, Martin Golkowski

Abstract read
In one paragraph

Article in Journal of proteome research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Article
  2. Proteomic approaches for interrogating kinase signaling networks.The Journal of investigative dermatology · 2026
    Article
  3. Article
  4. bioRxiv : the preprint server for biology · 2025
    Article
  5. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors.

Kathryn WoodsDepartment of Pharmacology & Toxicology, University of Utah, Salt Lake City 84112, United States.
Alexandria M ChanDepartment of Pharmacology & Toxicology, University of Utah, Salt Lake City 84112, United States.
Thankhoe A Rants'oDepartment of Pharmacology & Toxicology, University of Utah, Salt Lake City 84112, United States.
Tanmay SapreDepartment of Pharmacology, University of Washington, Seattle, Washington 95105, United States.
Grace E MastinDepartment of Biochemistry, University of Utah, Salt Lake City 84112, United States.
Kathleen M MaguireDepartment of Pharmacology & Toxicology, University of Utah, Salt Lake City 84112, United States.
Shao-En OngDepartment of Pharmacology, University of Washington, Seattle, Washington 95105, United States.
Martin GolkowskiDepartment of Pharmacology & Toxicology, University of Utah, Salt Lake City 84112, United States.ORCID 0000-0002-0996-1655

Funding

UTAH REGIONAL CANCER CENTERP30CA042014 · NCI · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI Jared P Rutter · 1986 to 2026
$72.6M
Supplement to DEFINING PATHWAY-SPECIFIC KINASE SIGNALING MODULES WITH PROTEOMICSR01GM129090 · NIGMS · UNIVERSITY OF WASHINGTON · PI ONG, SHAO-EN · 2019 to 2022
$1.7M
Integrated mass spectrometry-based chemoproteomic and genomic technologies for studying dynamic kinase interactomesR35GM150766 · NIGMS · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI Martin Golkowski · 2023 to 2026
$1.5M
CTSA Postdoctoral T32 at University of Utah: Spheres of Translation Across the Research Spectrum (STARS) Training ProgramT32TR004394 · NCATS · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI ANGELA FAGERLIN, Keke Celeste Fairfax · 2023 to 2026
$1.1M
Proteomic signatures to predict drug response in cancerR21CA288806 · NCI · UNIVERSITY OF WASHINGTON · PI ONG, SHAO-EN, YEUNG, RAYMOND · 2024 to 2025
$400k
Targeting understudied kinases in cancer cell plasticity and drug resistanceR03TR003308 · NCATS · UNIVERSITY OF WASHINGTON · PI GOLKOWSKI, MARTIN · 2020 to 2020
$156k
NCATS NIH HHS R03 TR003308NCATS NIH HHS T32 TR004394NCI NIH HHS P30 CA042014NCI NIH HHS R21 CA288806NIGMS NIH HHS R01 GM129090NIGMS NIH HHS R35 GM150766
6 · The paper itself

Abstract

Kinases control most cellular processes through protein phosphorylation. The 518 human protein kinases, i.e., the kinome, are frequently dysregulated in human disease. Kinase activity, localization, and substrate recognition are controlled by dynamic PPI networks composed of scaffolding and adapter proteins, other signaling enzymes, and phospho-substrates. Mapping kinome PPI networks can, therefore, quantify kinome activation states and kinase-mediated cell signaling, and can be used to prioritize kinases for drug discovery. We introduce our 2

Indexed as

Protein Interaction MappingProtein KinasesProteomicsAlgorithmsCell Line, TumorHumansMass SpectrometryPhosphorylationProtein Interaction MapsProtein Kinase InhibitorsSignal TransductionProtein Kinase InhibitorsProtein KinasesALK inhibitorchemoproteomicskinomeneuroblastomanoradrenergic-mesenchymal transitionprotein−protein interaction

Identifiers

PMID40862632
PMCPMC12393673

What OpenQuestion holds

Textmetadata
LicenceTDM
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.