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

Beta-arrestin multimers: does a crowd help or hinder function?

The Biochemical journal - 1 Jul 2008

DeFea Kathryn Anne

Abstract excerpt

In this issue of the Biochemical Journal, Xu et al. describe how they use a spot peptide array to identify a unique sequence within beta-arrestin-2 that is required for both multimerization and ERK1/2 (extracellular-signal-related kinase 1/2) scaffolding. They provide evidence that dimers may serve as more than just 'storage forms' of beta-arrestins, incapable of interacting with receptors but, rather, perhaps,...

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 Arrestins
Share to beta-Arrestins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mitogen-Activated Protein Kinase Kinases

Share to Mutation

Share to Protein Binding

Share to Signal Transduction

Source

Identifiers

PMID: 18537791
DOI: 10.1042/BJ20081009

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

Beta-arrestin multimers: does a crowd help or hinder function?PMID 18537791Read ↗

Targeting arrestin interactions with its partners for therapeutic purposes.Semantic proximity Read ↗

Receptor-Arrestin Interactions: The GPCR Perspective.Semantic proximity Read ↗

Molecular determinants underlying the formation of stable intracellular G protein-coupled receptor-beta-arrestin complexes after receptor endocytosis*.Semantic proximity Read ↗

Activation-dependent conformational changes in {beta}-arrestin 2.Semantic proximity Read ↗

Structural studies of phosphorylation-dependent interactions between the V2R receptor and arrestin-2.Semantic proximity Read ↗

β-Arrestins 1 and 2 are critical regulators of inflammationSemantic proximity Read ↗

Engineering visual arrestin-1 with special functional characteristics.Semantic proximity Read ↗

β-Arrestins and disease-linked variants: opportunities for targeted modulation.Semantic proximity Read ↗

Arrestin binding to calmodulin: a direct interaction between two ubiquitous signaling proteins.Semantic proximity Read ↗

Agonist-receptor-arrestin, an alternative ternary complex with high agonist affinity.Semantic proximity Read ↗

Conformational Dynamics and Functional Implications of Phosphorylated β-Arrestins.Semantic proximity Read ↗

Receptor/beta-arrestin complex formation and the differential trafficking and resensitization of beta2-adrenergic and angiotensin II type 1A receptors.Semantic proximity Read ↗

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