Evidence map›Paper›PMID 20452950›Full record

ReviewCold Spring Harbor perspectives in biology2010

Structural biology of the T-cell receptor: insights into receptor assembly, ligand recognition, and initiation of signaling.

Kai W Wucherpfennig, Etienne Gagnon, Melissa J Call, Eric S Huseby, Matthew E Call

Open access · bronzeAbstract readReview
In one paragraph

Review in Cold Spring Harbor perspectives in biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.

0numbers the graph read from it
0cells of the map it votes in
89citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

89 citing papers in PubMed, 174 citations in OpenAlex.

  1. Article
  2. Strategies to eliminate native T cell receptors for adoptive T cell therapies.Molecular therapy : the journal of the American Society of Gene Therapy · 2026
    Review
  3. Incomplete lineage sorting shaped mixed traits during a colobine primate radiation.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Leveraging T cells for cancer immunotherapy.Immunity & inflammation · 2025
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. CD3ε of a pan T cell marker involved in mouseInternational journal of ophthalmology · 2024
    Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. A Beginner's Guide to T Cell Development.Methods in molecular biology (Clifton, N.J.) · 2023
    Review
  20. Article

29 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 4 institutions in 1 country.

Kai W WucherpfennigDepartment of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Boston, Massachusetts 02115, USA. kai_wucherpfennig@dfci.harvard.edu <kai_wucherpfennig@dfci.harvard.edu>
Etienne Gagnon
Melissa J Call
Eric S Huseby
Matthew E Call
Dana-Farber Cancer Institute · USDana-Farber/Harvard Cancer Center · USHarvard University · USUniversity of Massachusetts Chan Medical School · US

Funding

Structural Determinants of TCR Assembly and SignalingR01AI054520 · NIAID · DANA-FARBER CANCER INSTITUTE · PI WUCHERPFENNIG, KAI W · 2003 to 2013
$4.0M
TCR Crossreactivity in Autoimmune DiseasesR01AI064177 · NIAID · DANA-FARBER CANCER INSTITUTE · PI WUCHERPFENNIG, KAI W · 2005 to 2009
$1.9M
NIAID NIH HHS AI064177NIAID NIH HHS R01 AI054520NIAID NIH HHS R01 AI064177
6 · The paper itself

Abstract

The T-cell receptor (TCR)-CD3 complex serves as a central paradigm for general principles of receptor assembly, ligand recognition, and signaling in the immune system. There is no other receptor system that matches the diversity of both receptor and ligand components. The recent expansion of the immunological structural database is beginning to identify key principles of MHC and peptide recognition. The multicomponent assembly of the TCR complex illustrates general principles used by many receptors in the immune system, which rely on basic and acidic transmembrane residues to guide assembly. The intrinsic binding of the cytoplasmic domains of the CD3epsilon and zeta chains to the inner leaflet of the plasma membrane represents a novel mechanism for control of receptor activation: Insertion of critical CD3epsilon tyrosines into the hydrophobic membrane core prevents their phosphorylation before receptor engagement.

Indexed as

AnimalsCD3 ComplexCell MembraneHistocompatibility Antigens Class IHumansMiceModels, MolecularProtein ConformationReceptors, Antigen, T-Cell, alpha-betaReceptors, Antigen, T-Cell, gamma-deltaSignal TransductionStructure-Activity RelationshipCD3 ComplexHistocompatibility Antigens Class IReceptors, Antigen, T-Cell, alpha-betaReceptors, Antigen, T-Cell, gamma-delta

Identifiers

PMID20452950
PMCPMC2845206
OpenAlexW2124555673

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.