Evidence map›Paper›PMID 31992596›Full record

ArticleThe Journal of biological chemistry2020

The murine CD94/NKG2 ligand, Qa-1

Katharine Jennifer Goodall, Angela Nguyen, Craig McKenzie, Sidonia Barbara Guiomar Eckle, Lucy Catherine Sullivan, Daniel Mark Andrews

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

14 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. The murine MHC-E molecule Qa-1Frontiers in immunology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Pathways and mechanisms of CD4Trends in immunology · 2024
    Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Review
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

6 authors at 2 institutions in 1 country.

Katharine Jennifer GoodallDepartment of Immunology and Pathology, Central Clinical School, Monash University, Melbourne, Victoria, 3004, Australia. Electronic address: katharine.goodall@monash.edu.
Angela NguyenDepartment of Immunology and Pathology, Central Clinical School, Monash University, Melbourne, Victoria, 3004, Australia.
Craig McKenzieDepartment of Immunology and Pathology, Central Clinical School, Monash University, Melbourne, Victoria, 3004, Australia.
Sidonia Barbara Guiomar EckleDepartment of Microbiology and Immunology, Peter Doherty Institute for Infection and Immunity, University of Melbourne, Melbourne, Victoria, 3000, Australia.
Lucy Catherine SullivanDepartment of Microbiology and Immunology, Peter Doherty Institute for Infection and Immunity, University of Melbourne, Melbourne, Victoria, 3000, Australia.
Daniel Mark AndrewsDepartment of Immunology and Pathology, Central Clinical School, Monash University, Melbourne, Victoria, 3004, Australia.
Monash University · AUThe University of Melbourne · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The immune co-receptor CD8 molecule (CD8) has two subunits, CD8α and CD8β, which can assemble into homo or heterodimers. Nonclassical (class-Ib) major histocompatibility complex (MHC) molecules (MHC-Ibs) have recently been identified as ligands for the CD8αα homodimer. This was demonstrated by the observation that histocompatibility 2, Q region locus 10 (H2-Q10) is a high-affinity ligand for CD8αα which also binds the MHC-Ib molecule H2-TL. This suggests that MHC-Ib proteins may be an extended source of CD8αα ligands. Expression of H2-T3/TL and H2-Q10 is restricted to the small intestine and liver, respectively, yet CD8αα-containing lymphocytes are present more broadly. Therefore, here we sought to determine whether murine CD8αα binds only to tissue-specific MHC-Ib molecules or also to ubiquitously expressed MHC-Ib molecules. Using recombinant proteins and surface plasmon resonance-based binding assays, we show that the MHC-Ib family furnishes multiple binding partners for murine CD8αα, including H2-T22 and the CD94/NKG2-A/B-activating NK receptor (NKG2) ligand Qa-1

Indexed as

AnimalsCD8 AntigensDimerizationHistocompatibility Antigens Class IHLA-E AntigensHumansInterferon-gammaIntraepithelial LymphocytesJurkat CellsLigandsMiceMice, Inbred C57BLNK Cell Lectin-Like Receptor Subfamily DProtein BindingProtein SubunitsRecombinant ProteinsCD8 AntigensHistocompatibility Antigens Class IHLA-E AntigensInterferon-gammaLigandsNK Cell Lectin-Like Receptor Subfamily DProtein SubunitsQ surface antigensRecombinant ProteinsCD8aacell biologycell surface glycoproteininnate immunitylymphocytemajor histocompatibility complex (MHC)MHC class I antigen E (HLA-E)MHC-IbQa-1bT cellT-cell biologyTL

Identifiers

PMID31992596
PMCPMC7062157
OpenAlexW3003481949

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.