Evidence map›Paper›PMID 19632164›Full record

ArticleMolecular oncology2009

Identification of c-Src tyrosine kinase substrates in platelet-derived growth factor receptor signaling.

Ramars Amanchy, Jun Zhong, Rosa Hong, James H Kim, Marjan Gucek, Robert N Cole, Henrik Molina, Akhilesh Pandey

Open access · greenAbstract read
In one paragraph

Article in Molecular oncology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

36 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. How the Discovery of the CD4/CD8-p56Frontiers in cell and developmental biology · 2021
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. Eph- and ephrin-dependent mechanisms in tumor and stem cell dynamics.Cellular and molecular life sciences : CMLS · 2014
    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

8 authors at 1 institution in 1 country.

Ramars AmanchyMcKusick-Nathans Institute of Genetic Medicine, Departments of Biological Chemistry, Oncology and Pathology, Johns Hopkins University, Baltimore, MD 21205, USA.
Jun Zhong
Rosa Hong
James H Kim
Marjan Gucek
Robert N Cole
Henrik Molina
Akhilesh Pandey
Johns Hopkins University · US

Funding

TCP5: ACTIVE SITE LABELING REAGENT FOR ACETYLTRANSFERASESU54RR020839 · NCRR · JOHNS HOPKINS UNIVERSITY · PI BOEKE, JEF D · 2004 to 2011
$27.4M
Molecular Dissection of Growth Factor Receptor SignalingR01CA106424 · NCI · JOHNS HOPKINS UNIVERSITY · PI PANDEY, AKHILESH · 2005 to 2008
$1.1M
NHLBI PROTEOMICS INITIATIVE-N01HV28180-268028180-268028180N01HV028180 · HV · JOHNS HOPKINS UNIVERSITY · PI VAN EYK, JENNIFER E · 2002 to 2006
–
NCI NIH HHS CA106424NCI NIH HHS R01 CA106424NCRR NIH HHS U54 RR020839NHLBI NIH HHS N01 HV028180
6 · The paper itself

Abstract

c-Src non-receptor tyrosine kinase is an important component of the platelet-derived growth factor (PDGF) receptor signaling pathway. c-Src has been shown to mediate the mitogenic response to PDGF in fibroblasts. However, the exact components of PDGF receptor signaling pathway mediated by c-Src remain unclear. Here, we used stable isotope labeling with amino acids in cell culture (SILAC) coupled with mass spectrometry to identify Src-family kinase substrates involved in PDGF signaling. Using SILAC, we were able to detect changes in tyrosine phosphorylation patterns of 43 potential c-Src kinase substrates in PDGF receptor signaling. This included 23 known c-Src kinase substrates, of which 16 proteins have known roles in PDGF signaling while the remaining 7 proteins have not previously been implicated in PDGF receptor signaling. Importantly, our analysis also led to identification of 20 novel Src-family kinase substrates, of which 5 proteins were previously reported as PDGF receptor signaling pathway intermediates while the remaining 15 proteins represent novel signaling intermediates in PDGF receptor signaling. In validation experiments, we demonstrated that PDGF indeed induced the phosphorylation of a subset of candidate Src-family kinase substrates - Calpain 2, Eps15 and Trim28 - in a c-Src-dependent fashion.

Indexed as

Amino AcidsAmino Acid SequenceAnimalsCells, CulturedChromatography, LiquidComputational BiologyCSK Tyrosine-Protein KinaseIsotope LabelingMiceMolecular Sequence DataNIH 3T3 CellsPhosphorylationPlatelet-Derived Growth FactorProtein-Tyrosine KinasesReceptors, Platelet-Derived Growth FactorReproducibility of ResultsAmino AcidsCSK Tyrosine-Protein KinasePlatelet-Derived Growth FactorProtein-Tyrosine KinasesReceptors, Platelet-Derived Growth Factorsrc-Family Kinases

Identifiers

PMID19632164
PMCPMC2783305
OpenAlexW2045856882

What Socratic 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 Socratic graph.