Evidence map›Paper›PMID 19801977›Full record

ArticleNature biotechnology2009

Sensitive multiplexed analysis of kinase activities and activity-based kinase identification.

Kazuishi Kubota, Rana Anjum, Yonghao Yu, Ryan C Kunz, Jannik N Andersen, Manfred Kraus, Heike Keilhack, Kumiko Nagashima, Stefan Krauss, Cloud Paweletz and 6 more

Abstract read
In one paragraph

Article in Nature biotechnology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing 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

50 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Review
  7. Review
  8. Drug Discovery in Liver Disease Using Kinome Profiling.International journal of molecular sciences · 2021
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

16 authors.

Kazuishi KubotaDepartment of Cell Biology, Harvard Medical School, Boston, Massachusetts, USA.
Rana Anjum
Yonghao Yu
Ryan C Kunz
Jannik N Andersen
Manfred Kraus
Heike Keilhack
Kumiko Nagashima
Stefan Krauss
Cloud Paweletz
Ronald C Hendrickson
Adam S Feldman
Chin-Lee Wu
John Rush
Judit Villén
Steven P Gygi

Funding

SIGNAL TRANSDUCTION TO PP70 S6KR01GM051405 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI BLENIS, JOHN · 1995 to 2023
$14.0M
New Sample Multiplexing Technologies to Identify Chemical Probes and Illuminate Ubiquitin BiologyR01GM067945 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI GYGI, STEVEN P · 2003 to 2024
$10.5M
New Technologies for Quantitative Phosphorylation AnalysisR01HG003456 · NHGRI · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI GYGI, STEVEN P · 2005 to 2011
$2.7M
NHGRI NIH HHS HG3456NHGRI NIH HHS R01 HG003456NIGMS NIH HHS GM51405NIGMS NIH HHS GM67945NIGMS NIH HHS R01 GM051405NIGMS NIH HHS R01 GM067945
6 · The paper itself

Abstract

Constitutive activation of one or more kinase signaling pathways is a hallmark of many cancers. Here we extend the previously described mass spectrometry-based KAYAK approach by monitoring kinase activities from multiple signaling pathways simultaneously. This improved single-reaction strategy, which quantifies the phosphorylation of 90 synthetic peptides in a single mass spectrometry run, is compatible with nanogram to microgram amounts of cell lysate. Furthermore, the approach enhances kinase monospecificity through substrate competition effects, faithfully reporting the signatures of many signaling pathways after mitogen stimulation or of basal pathway activation differences across a panel of well-studied cancer cell lines. Hierarchical clustering of activities from related experiments groups peptides phosphorylated by similar kinases together and, when combined with pathway alteration using pharmacological inhibitors, distinguishes underlying differences in potency, off-target effects and genetic backgrounds. Finally, we introduce a strategy to identify the kinase, and even associated protein complex members, responsible for phosphorylation events of interest.

Indexed as

CDC2 Protein KinaseCell CycleCells, CulturedCluster AnalysisComputational BiologyCyclin BCyclin-Dependent KinasesEpidermal Growth FactorHeLa CellsHumansInsulinMass SpectrometryPhosphorylationProtein KinasesProto-Oncogene Proteins c-aktReceptor Protein-Tyrosine KinasesCDC2 Protein KinaseCDK1 protein, humanCyclin BCyclin-Dependent KinasesEpidermal Growth FactorInsulinProtein KinasesProto-Oncogene Proteins c-aktReceptor Protein-Tyrosine KinasesTetradecanoylphorbol Acetate

Identifiers

PMID19801977
PMCPMC3129615

What OpenQuestion holds

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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.