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

Accelerated disassembly of IgE-receptor complexes by a disruptive macromolecular inhibitor.

Nature - 22 Nov 2012

Kim Beomkyu, Eggel Alexander, Tarchevskaya Svetlana S, Vogel Monique, Prinz Heino, Jardetzky Theodore S

Abstract excerpt

IgE antibodies bind the high-affinity IgE Fc receptor (FcεRI), found primarily on mast cells and basophils, and trigger inflammatory cascades of the allergic response. Inhibitors of IgE-FcεRI binding have been identified and an anti-IgE therapeutic antibody (omalizumab) is used to treat severe allergic asthma. However, preformed IgE-FcεRI complexes that prime cells before allergen exposure dissociate extremely...

Read the complete abstract on PubMed

Topics

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

Share to Allosteric Regulation
Share to Ankyrin Repeat

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Fluorescence

Share to Immunoglobulin E

Share to Ligands

Share to Mutant Proteins

Share to Receptors, IgE

Share to Surface Plasmon Resonance

Source

Open in PubMed Open full text

Identifiers

PMID: 23103871
DOI: 10.1038/nature11546
PMCID: PMC3504642

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

Accelerated disassembly of IgE-receptor complexes by a disruptive macromolecular inhibitor.PMID 23103871Read ↗

Structural and Functional Insights Into IgE Receptor Interactions and Disruptive InhibitionSemantic proximity Read ↗

Structural basis of omalizumab therapy and omalizumab-mediated IgE exchange.Semantic proximity Read ↗

Structural and Physical Basis for Anti-IgE Therapy.Semantic proximity Read ↗

Suppression of mast cell degranulation through a dual-targeting tandem IgE-IgG Fc domain biologic engineered to bind with high affinity to FcγRIIb.Semantic proximity Read ↗

Iterative Epitope Expansion Enables Structure-Guided <i>de novo</i> Design of IgE-Binding Miniproteins Targeting the Fc <i>ε</i> RI InterfaceSemantic proximity Read ↗

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

Modifications to an Fcgamma-Fcvarepsilon fusion protein alter its effectiveness in the inhibition of FcvarepsilonRI-mediated functions.Semantic proximity Read ↗

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

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

Mutation of the TGN1412 anti-CD28 monoclonal antibody lower hinge confers specific FcγRIIb binding and retention of super-agonist activity.Semantic proximity Read ↗

Drug Hypersensitivity and Desensitizations: Mechanisms and New Approaches.Semantic proximity Read ↗

Mast cell desensitization induces a distinct IgE-dependent transcriptional program associated with immune regulationSemantic proximity Read ↗

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