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

Understanding signal integration through targeted mutations of an adapter protein.

FEBS letters - 15 Dec 2010

Zou Tao, May Rebecca M, Koretzky Gary A

Abstract excerpt

Immunoreceptor engagement leads to the activation of multiple second messenger cascades, and integration of these pathways requires proper function of a number of adapter proteins. Although adapters possess no intrinsic enzymatic function, they nucleate the formation of multi-molecular protein complexes to support downstream signaling. Since adapters contain functionally distinct domains, intense investigation...

Read the complete abstract on PubMed

Topics

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

Share to Adaptor Proteins, Signal Transducing
Share to Cell Lineage
Share to Models, Theoretical

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Receptors, Antigen, T-Cell

Share to Signal Transduction

Share to T-Lymphocytes

Source

Open in PubMed Open full text

Identifiers

PMID: 20965179
DOI: 10.1016/j.febslet.2010.10.025
PMCID: PMC3008419

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Understanding signal integration through targeted mutations of an adapter protein.PMID 20965179Read ↗

The adapter proteins LAT and SLP-76 are required for T-cell activation.Semantic proximity Read ↗

Multipoint Binding of the SLP-76 SH2 Domain to ADAP Is Critical for Oligomerization of SLP-76 Signaling Complexes in Stimulated T CellsSemantic proximity Read ↗

The LAT story: a tale of cooperativity, coordination, and choreography.Semantic proximity Read ↗

Quantitative reduction of the TCR adapter protein SLP-76 unbalances immunity and immune regulation.Semantic proximity Read ↗

Activation of T lymphocytes and the role of the adapter LAT.Semantic proximity Read ↗

The role of SLP-76 and LAT in lymphocyte development.Semantic proximity Read ↗

The many faces of ITAMs.Semantic proximity Read ↗

A BASH/SLP-76-related adaptor protein MIST/Clnk involved in IgE receptor-mediated mast cell degranulation.Semantic proximity Read ↗

SRC homology 2 domain-containing leukocyte phosphoprotein of 76 kDa (SLP-76) N-terminal tyrosine residues regulate a dynamic signaling equilibrium involving feedback of proximal T-cell receptor (TCR) signaling.Semantic proximity Read ↗

Usage of activating mutations in the analysis of cytokine signal transduction pathways.Semantic proximity Read ↗

Characterization of phosphotyrosine binding motifs in the cytoplasmic domain of B and T lymphocyte attenuator required for association with protein tyrosine phosphatases SHP-1 and SHP-2.Semantic proximity Read ↗

The pleckstrin homology domain in the SKAP55 adapter protein defines the ability of the adapter protein ADAP to regulate integrin function and NF-kappaB activation.Semantic proximity Read ↗

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