Evidence map›Paper›PMID 26388332›Full record

ReviewNature reviews. Immunology2015

Lipid and small-molecule display by CD1 and MR1.

Ildiko Van Rhijn, Dale I Godfrey, Jamie Rossjohn, D Branch Moody

Open access · bronzeAbstract readReview
In one paragraph

Review in Nature reviews. Immunology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 98 papers.

0numbers the graph read from it
0cells of the map it votes in
98citing papers in PubMed
8.9field-weighted citation impact, top 2% 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

98 citing papers in PubMed, 140 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. MR1 presents vitamin B6-related compounds for recognition by MR1-reactive T cells.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Review
  7. Phosphatidylserine externalization as immune checkpoint in cancer.Pflugers Archiv : European journal of physiology · 2024
    Review
  8. Review
  9. Review
  10. Protein Haptenation and Its Role in Allergy.Chemical research in toxicology · 2024
    Review
  11. Article
  12. Review
  13. Glycolipids from the gut symbiontChemical science · 2023
    Article
  14. Article
  15. Article
  16. Animal models for COVID-19 and tuberculosis.Frontiers in immunology · 2023
    Review
  17. A guide to antigen processing and presentation.Nature reviews. Immunology · 2022
    Review
  18. Article
  19. Article
  20. Article

38 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

4 authors at 3 institutions in 4 countries.

Ildiko Van RhijnDivision of Rheumatology, Immunology and Allergy, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA.
Dale I GodfreyDepartment of Microbiology and Immunology, Peter Doherty Institute for Infection and Immunity, University of Melbourne, Parkville, Victoria 3010, Australia.
Jamie RossjohnInfection and Immunity Program and The Department of Biochemistry and Molecular Biology, Biomedicine Discovery Institute, Monash University, Clayton, Victoria 3800, Australia.
D Branch MoodyDivision of Rheumatology, Immunology and Allergy, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA.
Australian Research Council · AUBrigham and Women's Hospital · USHarvard University · US

Funding

Metabolomics Core U19AI111224 · NIAID · BRIGHAM AND WOMEN'S HOSPITAL · PI MURRAY, MEGAN, MURRAY, MEGAN B · 2015 to 2021
$20.4M
T cell response to CDI-restricted lipids in tuberculosisR01AI049313 · NIAID · BRIGHAM AND WOMEN'S HOSPITAL · PI MOODY, DAVID BRANCH · 2001 to 2025
$10.6M
NIAID NIH HHS R01 AI049313NIAID NIH HHS U19 AI111224
6 · The paper itself

Abstract

The antigen-presenting molecules CD1 and MHC class I-related protein (MR1) display lipids and small molecules to T cells. The antigen display platforms in the four CD1 proteins are laterally asymmetrical, so that the T cell receptor (TCR)-binding surfaces are comprised of roofs and portals, rather than the long grooves seen in the MHC antigen-presenting molecules. TCRs can bind CD1 proteins with left-sided or right-sided footprints, creating unexpected modes of antigen recognition. The use of tetramers of human CD1a, CD1b, CD1c or MR1 proteins now allows detailed analysis of the human T cell repertoire, which has revealed new invariant TCRs that bind CD1b molecules and are different from those that define natural killer T cells and mucosal-associated invariant T cells.

Indexed as

Antigen PresentationAntigens, CD1Histocompatibility Antigens Class IHumansLipidsMinor Histocompatibility AntigensModels, MolecularProtein BindingProtein Structure, TertiaryReceptors, Antigen, T-CellT-LymphocytesAntigens, CD1Histocompatibility Antigens Class ILipidsMinor Histocompatibility AntigensMR1 protein, humanReceptors, Antigen, T-Cell

Identifiers

PMID26388332
PMCPMC6944187
OpenAlexW2209943929

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.