Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The transition model of RTK activation: A quantitative framework for understanding RTK signaling and RTK modulator activity.

Cytokine & growth factor reviews - 1 Oct 2019

Paul Michael D, Hristova Kalina

Abstract excerpt

Here, we discuss the transition model of receptor tyrosine kinase (RTK) activation, which is derived from biophysical investigations of RTK interactions and signaling. The model postulates that (1) RTKs can interact laterally to form dimers even in the absence of ligand, (2) different unliganded RTK dimers have different stabilities, (3) ligand binding stabilizes the RTK dimers, and (4) ligand binding causes...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cell Membrane
Share to Ligands
Share to Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Binding

Share to Protein Multimerization

Share to Receptor Protein-Tyrosine Kinases

Share to Signal Transduction

Share to Thermodynamics

Source

Open in PubMed Open full text

Identifiers

PMID: 31711797
DOI: 10.1016/j.cytogfr.2019.10.004
PMCID: PMC6898792

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The transition model of RTK activation: A quantitative framework for understanding RTK signaling and RTK modulator activity.PMID 31711797Read ↗

A threshold model for receptor tyrosine kinase signaling specificity and cell fate determinationSemantic proximity Read ↗

Role of receptor tyrosine kinase transmembrane domains in cell signaling and human pathologies.Semantic proximity Read ↗

A function-structure model for NGF-activated TRK.Semantic proximity Read ↗

A molecular brake in the kinase hinge region regulates the activity of receptor tyrosine kinases.Semantic proximity Read ↗

On a mechanistic impact of transmembrane tetramerization in pathological activation of RTKsSemantic proximity Read ↗

Mechanism of homodimeric cytokine receptor activation and dysregulation by oncogenic mutations.Semantic proximity Read ↗

Cracking the molecular origin of intrinsic tyrosine kinase activity through analysis of pathogenic gain-of-function mutations.Semantic proximity Read ↗

Mechanism of FGF receptor dimerization and activation.Semantic proximity Read ↗

Tandem Domains with Tuned Interactions Are a Powerful Biological Design Principle.Semantic proximity Read ↗

Mutation-introduced dimerization of receptor tyrosine kinases: from protein structure aberrations to carcinogenesis.Semantic proximity Read ↗

Activation of the EGF Receptor by Ligand Binding and Oncogenic Mutations: The “Rotation Model”Semantic proximity Read ↗

Protein flexibility and dissociation pathway differentiation can explain onset of resistance mutations in kinasesSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.