Evidence map›Paper›PMID 21490152›Full record

ArticleJournal of immunology (Baltimore, Md. : 1950)2011

Structural basis of specificity and cross-reactivity in T cell receptors specific for cytochrome c-I-E(k).

Evan W Newell, Lauren K Ely, Andrew C Kruse, Philip A Reay, Stephanie N Rodriguez, Aaron E Lin, Michael S Kuhns, K Christopher Garcia, Mark M Davis

Abstract read
In one paragraph

Article in Journal of immunology (Baltimore, Md. : 1950), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing 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

46 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. A biomimetic five-module chimeric antigen receptor (Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  12. Article
  13. Ultrasmall silica nanoparticles directly ligate the T cell receptor complex.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  14. Article
  15. Article
  16. Stress-testing the relationship between T cell receptor/peptide-MHC affinity and cross-reactivity using peptide velcro.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  17. Article
  18. Early T cell receptor signals globally modulate ligand:receptor affinities during antigen discrimination.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  19. Review
  20. Article
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

9 authors.

Evan W NewellDepartment of Microbiology and Immunology, Stanford University School of Medicine, Stanford University, Stanford, CA 94305, USA.
Lauren K Ely
Andrew C Kruse
Philip A Reay
Stephanie N Rodriguez
Aaron E Lin
Michael S Kuhns
K Christopher Garcia
Mark M Davis

Funding

Using a tonsil organoid system to probe conditions for the induction of protective antibody and T cell responses to influenza.U19AI057229 · NIAID · STANFORD UNIVERSITY · PI Mark Morris Davis · 2003 to 2026
$88.5M
Vaccination and infection: indicators of immunological health and responsivenessU19AI090019 · NIAID · STANFORD UNIVERSITY · PI DAVIS, MARK MORRIS · 2010 to 2015
$17.3M
Howard Hughes Medical InstituteNIAID NIH HHS U19 AI057229NIAID NIH HHS U19 AI090019
6 · The paper itself

Abstract

T cells specific for the cytochrome c Ag are widely used to investigate many aspects of TCR specificity and interactions with peptide-MHC, but structural information has long been elusive. In this study, we present structures for the well-studied 2B4 TCR, as well as a naturally occurring variant of the 5c.c7 TCR, 226, which is cross-reactive with more than half of possible substitutions at all three TCR-sensitive residues on the peptide Ag. These structures alone and in complex with peptide-MHC ligands allow us to reassess many prior mutagenesis results. In addition, the structure of 226 bound to one peptide variant, p5E, shows major changes in the CDR3 contacts compared with wild-type, yet the TCR V-region contacts with MHC are conserved. These and other data illustrate the ability of TCRs to accommodate large variations in CDR3 structure and peptide contacts within the constraints of highly conserved TCR-MHC interactions.

Indexed as

AnimalsAntigens, CDCD4-Positive T-LymphocytesComplementarity Determining RegionsCross ReactionsCrystallography, X-RayCytochromes cHumansLigandsMiceModels, MolecularProtein BindingProtein Structure, TertiaryReceptors, Antigen, T-CellReceptors, ImmunologicRecombinant Fusion ProteinsAntigens, CDCd244a protein, mouseComplementarity Determining RegionsCytochromes cLigandsReceptors, Antigen, T-CellReceptors, ImmunologicRecombinant Fusion ProteinsSignaling Lymphocytic Activation Molecule Family

Identifiers

PMID21490152
PMCPMC3754796

What OpenQuestion holds

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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.