Evidence map›Paper›PMID 35384245›Full record

ArticleEMBO reports2022

Physical and functional interactome atlas of human receptor tyrosine kinases.

Kari Salokas, Xiaonan Liu, Tiina Öhman, Iftekhar Chowdhury, Lisa Gawriyski, Salla Keskitalo, Markku Varjosalo

Open access · hybridAbstract read
In one paragraph

Article in EMBO reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
9.6field-weighted citation impact, top 1% 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

43 citing papers in PubMed, 72 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Conformational dynamics in insulin receptor kinase reveal a type III allosteric pocket.Protein science : a publication of the Protein Society · 2026
    Article
  7. Article
  8. Article
  9. Regulation of receptor tyrosine kinase hetero-interactions.Current opinion in structural biology · 2025
    Review
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Synthesis of aChembiochem : a European journal of chemical biology · 2025
    Article
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 at 1 institution in 1 country.

Kari SalokasInstitute of Biotechnology, HiLIFE, University of Helsinki, Helsinki, Finland.ORCID 0000-0002-4471-6698
Xiaonan Liu *Institute of Biotechnology, HiLIFE, University of Helsinki, Helsinki, Finland.ORCID 0000-0002-9600-0536
Tiina Öhman *Institute of Biotechnology, HiLIFE, University of Helsinki, Helsinki, Finland.
Iftekhar ChowdhuryInstitute of Biotechnology, HiLIFE, University of Helsinki, Helsinki, Finland.ORCID 0000-0002-0360-6951
Lisa GawriyskiInstitute of Biotechnology, HiLIFE, University of Helsinki, Helsinki, Finland.ORCID 0000-0002-1950-4749
Salla KeskitaloInstitute of Biotechnology, HiLIFE, University of Helsinki, Helsinki, Finland.
Markku VarjosaloInstitute of Biotechnology, HiLIFE, University of Helsinki, Helsinki, Finland.ORCID 0000-0002-1340-9732
University of Helsinki · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Much cell-to-cell communication is facilitated by cell surface receptor tyrosine kinases (RTKs). These proteins phosphorylate their downstream cytoplasmic substrates in response to stimuli such as growth factors. Despite their central roles, the functions of many RTKs are still poorly understood. To resolve the lack of systematic knowledge, we apply three complementary methods to map the molecular context and substrate profiles of RTKs. We use affinity purification coupled to mass spectrometry (AP-MS) to characterize stable binding partners and RTK-protein complexes, proximity-dependent biotin identification (BioID) to identify transient and proximal interactions, and an in vitro kinase assay to identify RTK substrates. To identify how kinase interactions depend on kinase activity, we also use kinase-deficient mutants. Our data represent a comprehensive, systemic mapping of RTK interactions and substrates. This resource adds information regarding well-studied RTKs, offers insights into the functions of less well-studied RTKs, and highlights RTK-RTK interactions and shared signaling pathways.

Indexed as

Receptor Protein-Tyrosine KinasesSignal TransductionCell MembraneHumansPhosphorylationTyrosineReceptor Protein-Tyrosine KinasesTyrosineinteraction proteomicsphosphoproteomicsreceptor tyrosine kinaseRTKsystems biology

Identifiers

PMID35384245
PMCPMC9171411
OpenAlexW4226110935

What OpenQuestion holds

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LicenceCC BY
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.