Evidence map›Paper›PMID 32467228›Full record

ArticleThe Journal of biological chemistry2020

Quantifying the strength of heterointeractions among receptor tyrosine kinases from different subfamilies: Implications for cell signaling.

Michael D Paul, Hana N Grubb, Kalina Hristova

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. 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
2.8field-weighted citation impact, top 9% 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

22 citing papers in PubMed, 38 citations in OpenAlex.

  1. Regulation of receptor tyrosine kinase hetero-interactions.Current opinion in structural biology · 2025
    Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Targeting the EphA2 pathway: could it be the way for bone sarcomas?Cell communication and signaling : CCS · 2024
    Review
  7. Article
  8. Article
  9. Review
  10. Structural insights into regulation of CCN protein activities and functions.Journal of cell communication and signaling · 2023
    Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Interactions between Ligand-Bound EGFR and VEGFR2.Journal of molecular biology · 2021
    Article
  17. Article
  18. Review
  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

3 authors at 1 institution in 1 country.

Michael D PaulInstitute for NanoBioTechnology, Johns Hopkins University, Baltimore, Maryland, USA.
Hana N GrubbInstitute for NanoBioTechnology, Johns Hopkins University, Baltimore, Maryland, USA.ORCID 0000-0003-1275-534X
Kalina HristovaInstitute for NanoBioTechnology, Johns Hopkins University, Baltimore, Maryland, USA kh@jhu.edu.ORCID 0000-0003-4274-4406
Johns Hopkins University · US

Funding

Seeking the Physical Basis of AchondroplasiaR01GM068619 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI HRISTOVA, KALINA · 2004 to 2022
$5.4M
NIGMS NIH HHS R01 GM068619
6 · The paper itself

Abstract

Receptor tyrosine kinases (RTKs) are single-pass membrane proteins that control vital cell processes such as cell growth, survival, and differentiation. There is a growing body of evidence that RTKs from different subfamilies can interact and that these diverse interactions can have important biological consequences. However, these heterointeractions are often ignored, and their strengths are unknown. In this work, we studied the heterointeractions of nine RTK pairs, epidermal growth factor receptor (EGFR)-EPH receptor A2 (EPHA2), EGFR-vascular endothelial growth factor receptor 2 (VEGFR2), EPHA2-VEGFR2, EPHA2-fibroblast growth factor receptor 1 (FGFR1), EPHA2-FGFR2, EPHA2-FGFR3, VEGFR2-FGFR1, VEGFR2-FGFR2, and VEGFR2-FGFR3, using a FRET-based method. Surprisingly, we found that RTK heterodimerization and homodimerization strengths can be similar, underscoring the significance of RTK heterointeractions in signaling. We discuss how these heterointeractions can contribute to the complexity of RTK signal transduction, and we highlight the utility of quantitative FRET for probing multiple interactions in the plasma membrane.

Indexed as

Fluorescence Resonance Energy TransferSignal TransductionHEK293 CellsHumansReceptor Protein-Tyrosine KinasesReceptor Protein-Tyrosine Kinasescell signalingEPH receptor A2 (EPHA2)epidermal growth factor receptor (EGFR)fibroblast growth factor receptor (FGFR)fluorescence resonance energy transfer (FRET)membrane proteinprotein-protein interactionreceptor tyrosine kinasereceptor tyrosine kinase (RTK)thermodynamicsvascular endothelial growth factor receptor 2 (VEGFR2)

Identifiers

PMID32467228
PMCPMC7380177
OpenAlexW3030205069

What OpenQuestion holds

Textmetadata
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.