Evidence map›Paper›PMID 31227600›Full record

ArticleMolecular & cellular proteomics : MCP2019

An Integrative Analysis of Tumor Proteomic and Phosphoproteomic Profiles to Examine the Relationships Between Kinase Activity and Phosphorylation.

Osama A Arshad, Vincent Danna, Vladislav A Petyuk, Paul D Piehowski, Tao Liu, Karin D Rodland, Jason E McDermott

Abstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Article
  2. Article
  3. Pathway Analysis Interpretation in the Multi-Omic Era.Biotech (Basel (Switzerland)) · 2025
    Review
  4. Article
  5. Kinase-substrate prediction using an autoregressive model.Computational and structural biotechnology journal · 2025
    Article
  6. Review
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Functional characterization of co-phosphorylation networks.Bioinformatics (Oxford, England) · 2022
    Article
  14. Article
  15. Article
  16. Review
  17. leapR: An R Package for Multiomic Pathway Analysis.Journal of proteome research · 2021
    Article
  18. Article
  19. Article
  20. Review
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

7 authors.

Osama A ArshadBiological Sciences Division, Pacific Northwest National Laboratory, Richland, WA 99352.
Vincent DannaBiological Sciences Division, Pacific Northwest National Laboratory, Richland, WA 99352.
Vladislav A PetyukBiological Sciences Division, Pacific Northwest National Laboratory, Richland, WA 99352.
Paul D PiehowskiBiological Sciences Division, Pacific Northwest National Laboratory, Richland, WA 99352.
Tao LiuBiological Sciences Division, Pacific Northwest National Laboratory, Richland, WA 99352.
Karin D RodlandBiological Sciences Division, Pacific Northwest National Laboratory, Richland, WA 99352; School of Medicine, Oregon Health & Sciences University, Portland, OR 97239.
Jason E McDermottBiological Sciences Division, Pacific Northwest National Laboratory, Richland, WA 99352; School of Medicine, Oregon Health & Sciences University, Portland, OR 97239. Electronic address: Jason.McDermott@pnnl.gov.

Funding

PNNL Clinical Proteome Characterization CenterU24CA160019 · NCI · BATTELLE PACIFIC NORTHWEST LABORATORIES · PI RODLAND, KARIN D, SMITH, RICHARD D · 2011 to 2016
$15.7M
Proteogenomic Translational Research Center for Clinical ProteomicU01CA214116 · NCI · BATTELLE PACIFIC NORTHWEST LABORATORIES · PI DRUKER, BRIAN J, RODLAND, KARIN D · 2017 to 2021
$6.8M
PNNL Proteome Characterization CenterU24CA210955 · NCI · BATTELLE PACIFIC NORTHWEST LABORATORIES · PI LIU, TAO, SMITH, RICHARD D · 2016 to 2020
$5.3M
NCI NIH HHS U01 CA214116NCI NIH HHS U24 CA160019NCI NIH HHS U24 CA210955
6 · The paper itself

Abstract

Phosphorylation of proteins is a key way cells regulate function, both at the individual protein level and at the level of signaling pathways. Kinases are responsible for phosphorylation of substrates, generally on serine, threonine, or tyrosine residues. Though particular sequence patterns can be identified that dictate whether a residue will be phosphorylated by a specific kinase, these patterns are not highly predictive of phosphorylation. The availability of large scale proteomic and phosphoproteomic data sets generated using mass-spectrometry-based approaches provides an opportunity to study the important relationship between kinase activity, substrate specificity, and phosphorylation. In this study, we analyze relationships between protein abundance and phosphopeptide abundance across more than 150 tumor samples and show that phosphorylation at specific phosphosites is not well correlated with overall kinase abundance. However, individual kinases show a clear and statistically significant difference in correlation among known phosphosite targets for that kinase and randomly selected phosphosites. We further investigate relationships between phosphorylation of known activating or inhibitory sites on kinases and phosphorylation of their target phosphosites. Combined with motif-based analysis, this approach can predict novel kinase targets and show which subsets of a kinase's target repertoire are specifically active in one condition

Indexed as

HumansNeoplasmsPhosphoproteinsPhosphorylationProtein KinasesProteomicsPhosphoproteinsProtein KinasesBreast cancerCancer BiologyComputational BiologyiTRAQOvarian cancerPhosphoproteomePhosphorylation

Identifiers

PMID31227600
PMCPMC6692771

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Registered trials

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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.