Evidence map›Paper›PMID 9770516›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1998

Diversification, expression, and gamma delta T cell recognition of evolutionarily distant members of the MIC family of major histocompatibility complex class I-related molecules.

A Steinle, V Groh, T Spies

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed, 1 pooled it
2.5field-weighted citation impact, top 10% 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

26 citing papers in PubMed, 1 synthesis or guideline pooled it, 109 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. Review
  9. Review
  10. Diversity of γδ T-cell antigens.Cellular & molecular immunology · 2013
    Review
  11. Review
  12. γδ T cell receptor ligands and modes of antigen recognition.Archivum immunologiae et therapiae experimentalis · 2011
    Review
  13. Crystal structure of a gammadelta T-cell receptor specific for the human MHC class I homolog MICA.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Characterization of the gammadelta T cell response to acute leukemia.Cancer immunology, immunotherapy : CII · 2006
    Article
  19. Mucosal T lymphocytes--peacekeepers and warriors.Springer seminars in immunopathology · 2005
    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

3 authors at 2 institutions in 1 country.

A SteinleClinical Research Division, Fred Hutchinson Cancer Research Center, 1100 Fairview Avenue North, Seattle, WA 98109-1024, USA.
V Groh
T Spies
North Seattle College · USFred Hutch Cancer Center · US

Funding

STUDIES ON MARROW GRAFT RESISTANCEP01CA018221 · NCI · FRED HUTCHINSON CANCER RESEARCH CENTER · PI STORB, RAINER F. · 1985 to 2001
$2.7M
NOVEL IMMUNE RESPONSE GENES WITHIN THE HUMAN MHCR01AI030581 · NIAID · FRED HUTCHINSON CANCER RESEARCH CENTER · PI SPIES, THOMAS · 1991 to 2000
$366k
NCI NIH HHS P01 CA18221NIAID NIH HHS R01 AI030581NIAID NIH HHS R01 AI30581
6 · The paper itself

Abstract

Distant relatives of major histocompatibility complex (MHC) class I molecules, human MICA and MICB, function as stress-induced antigens that are broadly recognized by intestinal epithelial gamma delta T cells. They may thus play a central role in the immune surveillance of damaged, infected, or otherwise stressed intestinal epithelial cells. However, the generality of this system in evolution and the mode of recognition of MICA and MICB are undefined. Analysis of cDNA sequences from various primate species defined translation products that are homologous to MICA and MICB. All of the MIC polypeptides have common characteristics, although they are extraordinarily diverse. The most notable alterations are several deletions and frequent amino acid substitutions in the putative alpha-helical regions of the alpha1 alpha2 domains. However, the primate MIC molecules were expressed on the surfaces of normal and transfected cells. Moreover, despite their sharing of relatively few identical amino acids in potentially accessible regions of their alpha1 alpha2 domains, they were recognized by diverse human intestinal epithelial gamma delta T cells that are restricted by MICA and MICB. Thus, MIC molecules represent a family of MHC proteins that are structurally diverse yet appear to be functionally conserved. The promiscuous mode of gamma delta T cell recognition of these antigens may be explained by their sharing of a single conserved interaction site.

Indexed as

Evolution, MolecularAmino Acid SequenceAnimalsBase SequenceCell LineCloning, MolecularDNA PrimersHistocompatibility Antigens Class IHumansMolecular Sequence DataReceptors, Antigen, T-Cell, gamma-deltaSequence Homology, Amino AcidTumor Cells, CulturedDNA PrimersHistocompatibility Antigens Class IReceptors, Antigen, T-Cell, gamma-delta

Identifiers

PMID9770516
PMCPMC22861
OpenAlexW2004396527

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.