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 single transmembrane domains of ErbB receptors self-associate in cell membranes.

The Journal of biological chemistry - 15 Feb 2002

Mendrola Jeannine M, Berger Mitchell B, King Megan C, Lemmon Mark A

Abstract excerpt

Members of the epidermal growth factor receptor, or ErbB, family of receptor tyrosine kinases have a single transmembrane (TM) alpha-helix that is usually assumed to play a passive role in ligand-induced dimerization and activation of the receptor. However, recent studies with the epidermal growth factor receptor (ErbB1) and the erythropoietin receptor have indicated that interactions between TM alpha-helices do...

Read the complete abstract on PubMed

Topics

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

Share to Chloramphenicol O-Acetyltransferase
Share to Erb-b2 Receptor Tyrosine Kinases

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Glutamic Acid

Share to Maltose

Share to Receptor, ErbB-3

Share to Receptor, ErbB-4

Share to Receptor Protein-Tyrosine Kinases

Share to Valine

Source

Identifiers

PMID: 11741943
DOI: 10.1074/jbc.M108681200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The single transmembrane domains of ErbB receptors self-associate in cell membranes.PMID 11741943Read ↗

Two GxxxG-like motifs facilitate promiscuous interactions of the human ErbB transmembrane domains.Semantic proximity Read ↗

The Single Transmembrane Domains of Human Receptor Tyrosine Kinases Encode Self-InteractionsSemantic proximity Read ↗

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

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

Identification of a region within the ErbB2/HER2 intracellular domain that is necessary for ligand-independent association.Semantic proximity Read ↗

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

Complex relationship between ligand binding and dimerization in the epidermal growth factor receptor.Semantic proximity Read ↗

EGFR forms ligand-independent oligomers that are distinct from the active state.Semantic proximity Read ↗

Dynamic equilibrium between multiple active and inactive conformations explains regulation and oncogenic mutations in ErbB receptors.Semantic proximity Read ↗

ErbB receptors: directing key signaling networks throughout life.Semantic proximity Read ↗

Mechanisms for kinase-mediated dimerization of the epidermal growth factor receptor.Semantic proximity Read ↗

Ligand-independent EGFR oligomers do not rely on the active state asymmetric kinase dimerSemantic proximity Read ↗

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