Evidence map›Paper›PMID 23046125›Full record

ReviewImmunological reviews2012

The structural basis of αβ T-lineage immune recognition: TCR docking topologies, mechanotransduction, and co-receptor function.

Jia-huai Wang, Ellis L Reinherz

Open access · greenAbstract readReview
In one paragraph

Review in Immunological reviews, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
3.7field-weighted citation impact, top 6% of its field
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

71 citing papers in PubMed, 104 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. The Evolving Portrait of γδ TCR Recognition Determinants.Journal of immunology (Baltimore, Md. : 1950) · 2024
    Review
  5. Article
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  7. Article
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  10. Review
  11. Harnessing αβ T cell receptor mechanobiology to achieve the promise of immuno-oncology.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Review
  12. Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

11 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

2 authors at 2 institutions in 1 country.

Jia-huai WangLaboratory of Immunobiology, Dana-Farber Cancer Institute and Departments, Harvard Medical School, Boston, MA, USA.
Ellis L Reinherz
Dana-Farber Cancer Institute · USHarvard University · US

Funding

STRUCTURE OF INTEGRINS AND YWTD BETA PROPELLER DOMAINSP01HL048675 · NHLBI · IMMUNE DISEASE INSTITUTE, INC. · PI SPRINGER, TIMOTHY A · 1992 to 2009
$20.9M
NHLBI NIH HHS P01 HL048675
6 · The paper itself

Abstract

Self versus non-self discrimination is at the core of T-lymphocyte recognition. To this end, αβ T-cell receptors (TCRs) ligate 'foreign' peptides bound to major histocompatibility complex (MHC) class I or class II molecules (pMHC) arrayed on the surface of antigen-presenting cells (APCs). Since the discovery of TCRs approximately 30 years ago, considerable structural and functional data have detailed the molecular basis of their extraordinary ligand specificity and sensitivity in mediating adaptive T-cell immunity. This review focuses on the structural biology of the Fab-like TCRαβ clonotypic heterodimer and its unique features in conjunction with those of the associated CD3εγ and CD3εδ heterodimeric molecules, which, along with CD3ζζ homodimer, comprise the TCR complex in a stoichiometry of 1:1:1:1. The basis of optimized TCRαβ docking geometry on the pMHC linked to TCR mechanotransduction and required for T-cell signaling as well as CD4 and CD8 co-receptor function is detailed. A model of the TCR ectodomain complex including its connecting peptides suggests how force generated during T-cell immune surveillance and at the immunological synapse results in dynamic TCR quaternary change involving its heterodimeric components. Potential insights from the structural biology relevant to immunity and immunosuppression are revealed.

Indexed as

AnimalsAntigen-Presenting CellsAntigensCD3 ComplexCD4-Positive T-LymphocytesCD8-Positive T-LymphocytesHumansMajor Histocompatibility ComplexMechanotransduction, CellularMiceModels, MolecularPeptidesProtein ConformationProtein MultimerizationReceptors, Antigen, T-Cell, alpha-betaAntigensCD3 ComplexCD3E protein, humanPeptidesReceptors, Antigen, T-Cell, alpha-beta

Identifiers

PMID23046125
PMCPMC3694212
OpenAlexW2153520720

What OpenQuestion holds

Textmetadata
LicenceTDM
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.