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

Asp-960/Glu-961 controls the movement of the C-terminal tail of the epidermal growth factor receptor to regulate asymmetric dimer formation.

The Journal of biological chemistry - 30 Jul 2010

Yang Katherine S, Macdonald-Obermann Jennifer L, Piwnica-Worms David, Pike Linda J

Abstract excerpt

The epidermal growth factor (EGF) receptor is a tyrosine kinase that dimerizes in response to ligand binding. Ligand-induced dimerization of the extracellular domain of the receptor promotes formation of an asymmetric dimer of the intracellular kinase domains, leading to stimulation of the tyrosi...

Read the complete abstract on PubMed

Topics

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

Share to Aspartic Acid
Share to CHO Cells
Share to Cricetinae

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cricetulus

Share to Dimerization

Share to Glutamic Acid

Share to Protein-Tyrosine Kinases

Share to Structure-Activity Relationship

Source

Open in PubMed Open full text

Identifiers

PMID: 20507979
DOI: 10.1074/jbc.M110.103317
PMCID: PMC2911325

Genes

EGF

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-20507979-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Asp-960/Glu-961 controls the movement of the C-terminal tail of the epidermal growth factor receptor to regulate asymmetric dimer formation.PMID 20507979Read ↗

A model for the activation of the epidermal growth factor receptor kinase involvement of an asymmetric dimer?Semantic proximity Read ↗

Binding of single-mutant epidermal growth factor (EGF) ligands alters the stability of the EGF receptor dimer and promotes growth signaling.Semantic proximity Read ↗

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

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

Constitutive asymmetric dimerization drives oncogenic activation of epidermal growth factor receptor carboxyl-terminal deletion mutants.Semantic proximity Read ↗

Heterogeneity in EGF-binding affinities arises from negative cooperativity in an aggregating system.Semantic proximity Read ↗

The juxtamembrane region of the EGF receptor functions as an activation domain.Semantic proximity Read ↗

An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor.Semantic proximity Read ↗

EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization.Semantic proximity Read ↗

Epidermal growth factor receptor juxtamembrane region regulates allosteric tyrosine kinase activation.Semantic proximity Read ↗

EGF receptor activation: push comes to shove.Semantic proximity Read ↗

The EGF receptor Hokey-Cokey.Semantic proximity Read ↗

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