Evidence map›Paper›PMID 33122191›Full record

ReviewThe Journal of biological chemistry2020

Ligand bias in receptor tyrosine kinase signaling.

Kelly Karl, Michael D Paul, Elena B Pasquale, Kalina Hristova

Open access · hybridAbstract readReview
In one paragraph

Review 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 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

33 citing papers in PubMed, 61 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Beyond the membrane: rethinking EGFR signaling in physiology and cancer.Cellular and molecular life sciences : CMLS · 2026
    Review
  5. Review
  6. Article
  7. Regulation of receptor tyrosine kinase hetero-interactions.Current opinion in structural biology · 2025
    Review
  8. Article
  9. Review
  10. Review
  11. HER4 is a high-affinity dimerization partner for all EGFR/HER/ErbB family proteins.Protein science : a publication of the Protein Society · 2024
    Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Graph Structured Neural Networks for Perturbation Biology.bioRxiv : the preprint server for biology · 2024
    Article
  20. 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

4 authors at 2 institutions in 1 country.

Kelly KarlDepartment of Materials Science and Engineering, Institute for NanoBioTechnology, and Program in Molecular Biophysics, Johns Hopkins University, Baltimore, Maryland, USA.
Michael D PaulDepartment of Materials Science and Engineering, Institute for NanoBioTechnology, and Program in Molecular Biophysics, Johns Hopkins University, Baltimore, Maryland, USA.
Elena B PasqualeSanford Burnham Prebys Medical Discovery Institute, La Jolla, California, USA. Electronic address: elenap@sbpdiscovery.org.
Kalina HristovaDepartment of Materials Science and Engineering, Institute for NanoBioTechnology, and Program in Molecular Biophysics, Johns Hopkins University, Baltimore, Maryland, USA. Electronic address: kh@jhu.edu.
Johns Hopkins University · USSanford Burnham Prebys Medical Discovery Institute · US

Funding

Seeking the Physical Basis of AchondroplasiaR01GM068619 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI HRISTOVA, KALINA · 2004 to 2022
$5.4M
Ligand functional selectivity in EphA2 receptor signalingR01GM131374 · NIGMS · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI Kalina Hristova, ELENA B PASQUALE · 2019 to 2026
$3.8M
Cyclic EphA4 peptide antagonists for neuroprotection in ALSR01NS087070 · NINDS · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI PASQUALE, ELENA B · 2014 to 2018
$3.5M
Discovery of Selective Inhibitors for the EphA4 KinaseR01AG062617 · NIA · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI PASQUALE, ELENA B, SERGIENKO, EDUARD A. · 2020 to 2023
$3.0M
NIA NIH HHS R01 AG062617NIGMS NIH HHS R01 GM068619NIGMS NIH HHS R01 GM131374NINDS NIH HHS R01 NS087070
6 · The paper itself

Abstract

Ligand bias is the ability of ligands to differentially activate certain receptor signaling responses compared with others. It reflects differences in the responses of a receptor to specific ligands and has implications for the development of highly specific therapeutics. Whereas ligand bias has been studied primarily for G protein-coupled receptors (GPCRs), there are also reports of ligand bias for receptor tyrosine kinases (RTKs). However, the understanding of RTK ligand bias is lagging behind the knowledge of GPCR ligand bias. In this review, we highlight how protocols that were developed to study GPCR signaling can be used to identify and quantify RTK ligand bias. We also introduce an operational model that can provide insights into the biophysical basis of RTK activation and ligand bias. Finally, we discuss possible mechanisms underpinning RTK ligand bias. Thus, this review serves as a primer for researchers interested in investigating ligand bias in RTK signaling.

Indexed as

Cell CommunicationSignal TransductionAnimalsEnzyme ActivationHumansLigandsReceptor Protein-Tyrosine KinasesLigandsReceptor Protein-Tyrosine Kinasesbias coefficientbias plotcell signalingdimerizationdimer stabilityligand biasligand functional selectivitymathematical modelingphosphotyrosine signalingprotein conformationreceptorreceptor tyrosine kinaseReceptor tyrosine kinase (RTK)signalingthermodynamics

Identifiers

PMID33122191
PMCPMC7939482
OpenAlexW3095553361

What Socratic holds

Textmetadata
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 Socratic graph.