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 first transmembrane region of the beta-chain stabilizes the tetrameric Fc epsilon RI complex.

Molecular immunology - 1 Jul 2009

Singleton Theresa E, Platzer Barbara, Dehlink Eleonora, Fiebiger Edda

Abstract excerpt

The family of activating immune receptors stabilizes via the 3-helix assembly principle. A charged basic transmembrane residue interacts with two charged acidic transmembrane residues and forms a 3-helix interface to stabilize receptor complexes in the lipid bilayer. One family member, the high a...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Cell Line
Share to Lipid Bilayers

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Conformation

Share to Protein Multimerization

Share to Protein Stability

Share to Protein Structure, Tertiary

Share to Receptors, IgE

Source

Open in PubMed Open full text

Identifiers

PMID: 19406478
DOI: 10.1016/j.molimm.2009.03.023
PMCID: PMC2745130

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-19406478-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The first transmembrane region of the beta-chain stabilizes the tetrameric Fc epsilon RI complex.PMID 19406478Read ↗

Fc receptor gamma chain residues at the interface of the cytoplasmic and transmembrane domains affect association with FcalphaRI, surface expression, and function.Semantic proximity Read ↗

Structural insights into the high-affinity IgE receptor FcεRI complex.Semantic proximity Read ↗

Cotranslational endoplasmic reticulum assembly of FcepsilonRI controls the formation of functional IgE-binding receptors.Semantic proximity Read ↗

Transport of the IgE receptor alpha-chain is controlled by a multicomponent intracellular retention signal.Semantic proximity Read ↗

Antibody Fc-receptor FcεR1γ stabilizes cell surface receptors in group 3 innate lymphoid cells and promotes anti-infection immunitySemantic proximity Read ↗

A dual role for the N-terminal domain of the IL-3 receptor in cell signalling.Semantic proximity Read ↗

Attenuation of IgE affinity for FcepsilonRI radically reduces the allergic response in vitro and in vivo.Semantic proximity Read ↗

Structure of the Fc fragment of human IgE bound to its high-affinity receptor Fc epsilonRI alpha.Semantic proximity Read ↗

Interleukin-3 binding to the murine betaIL-3 and human betac receptors involves functional epitopes formed by domains 1 and 4 of different protein chains.Semantic proximity Read ↗

Role of lipid nanodomains for inhibitory FcγRIIb functionSemantic proximity Read ↗

Disruption of extracellular interactions impairs T cell receptor-CD3 complex stability and signaling.Semantic proximity Read ↗

A novel splice variant of human TGF-β type II receptor encodes a soluble protein and its Fc-tagged version prevents liver fibrosis <i>in vivo</i>Semantic proximity Read ↗

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