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

Evidence for a functional sidedness to the alphabetaTCR.

Proceedings of the National Academy of Sciences of the United States of America - 16 Mar 2010

Kuhns Michael S, Girvin Andrew T, Klein Lawrence O, Chen Rebecca, Jensen Kirk D C, Newell Evan W, Huppa Johannes B, Lillemeier Björn F, Huse Morgan, Chien Yueh-Hsiu, Garcia K Christopher, Davis Mark M

Abstract excerpt

The T cell receptor (TCR) and associated CD3gammaepsilon, deltaepsilon, and zetazeta signaling dimers allow T cells to discriminate between different antigens and respond accordingly, but our knowledge of how these parts fit and work together is incomplete. In this study, we provide additional evidence that the CD3 heterodimers congregate on one side of the TCR in both the alphabeta and gammadeltaTCR-CD3...

Read the complete abstract on PubMed

Topics

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

Share to Antigen-Presenting Cells
Share to Calcium Signaling

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to CD3 Complex

Share to Cell Polarity

Share to Intracellular Space

Share to Protein Multimerization

Share to Receptors, Antigen, T-Cell, alpha-beta

Share to Receptors, Antigen, T-Cell, gamma-delta

Source

Open in PubMed Open full text

Identifiers

PMID: 20202921
DOI: 10.1073/pnas.1000925107
PMCID: PMC2841884

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

Evidence for a functional sidedness to the alphabetaTCR.PMID 20202921Read ↗

Biochemical differences in the alphabeta T cell receptor.CD3 surface complex between CD8+ and CD4+ human mature T lymphocytes.Semantic proximity Read ↗

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

Distinctive CD3 Heterodimeric Ectodomain Topologies Maximize Antigen-Triggered Activation of αβ T Cell ReceptorsSemantic proximity Read ↗

Antigen ligation triggers a conformational change within the constant domain of the alphabeta T cell receptor.Semantic proximity Read ↗

The cytoplasmic tail of the T cell receptor CD3 epsilon subunit contains a phospholipid-binding motif that regulates T cell functions.Semantic proximity Read ↗

Amino acid substitutions in the putative MHC class II "dimer of dimers" interface inhibit CD4+ T cell activation.Semantic proximity Read ↗

TCRbeta transmembrane tyrosines are required for pre-TCR function.Semantic proximity Read ↗

The structural basis for autonomous dimerization of the pre-T-cell antigen receptor.Semantic proximity Read ↗

Conformational and biochemical differences in the TCR.CD3 complex of CD8(+) versus CD4(+) mature lymphocytes revealed in the absence of CD3gamma.Semantic proximity Read ↗

Positive selection through a motif in the alphabeta T cell receptor.Semantic proximity Read ↗

A motif in the alphabeta T-cell receptor controls positive selection by modulating ERK activity.Semantic proximity Read ↗

One of the CD3ε Subunits within a T Cell Receptor Complex Lies in Close Proximity to the Cβ FG LoopSemantic proximity Read ↗

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