Evidence map›Paper›PMID 24723923›Full record

ReviewFrontiers in immunology2014

Structural basis for recognition of cellular and viral ligands by NK cell receptors.

Yili Li, Roy A Mariuzza

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in immunology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

41 citing papers in PubMed, 61 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Variants of HCMVInternational journal of molecular sciences · 2022
    Article
  9. Article
  10. COVID-19 Pandemic: Escape of Pathogenic Variants and MHC Evolution.International journal of molecular sciences · 2022
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. PET Imaging of the Natural Killer Cell Activation Receptor NKp30.Journal of nuclear medicine : official publication, Society of Nuclear Medicine · 2020
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Oligomeric Architecture of Mouse Activating Nkrp1 Receptors on Living Cells.International journal of molecular sciences · 2019
    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

2 authors at 2 institutions in 1 country.

Yili LiW. M. Keck Laboratory for Structural Biology, Institute for Bioscience and Biotechnology Research, University of Maryland , Rockville, MD , USA ; Department of Cell Biology and Molecular Genetics, University of Maryland , College Park, MD , USA.
Roy A MariuzzaW. M. Keck Laboratory for Structural Biology, Institute for Bioscience and Biotechnology Research, University of Maryland , Rockville, MD , USA ; Department of Cell Biology and Molecular Genetics, University of Maryland , College Park, MD , USA.
Institute for Bioscience and Biotechnology ResearchUniversity of Maryland, College Park · US

Funding

STRUCTURE AND FUNCTION OF NATURAL KILLER CELL RECEPTORSR01AI047990 · NIAID · UNIV OF MARYLAND, COLLEGE PARK · PI MARIUZZA, ROY A · 2000 to 2014
$4.1M
NIAID NIH HHS R01 AI047990
6 · The paper itself

Abstract

Natural killer (NK) cells are key components of innate immune responses to tumors and viral infections. NK cell function is regulated by NK cell receptors that recognize both cellular and viral ligands, including major histocompatibility complex (MHC), MHC-like, and non-MHC molecules. These receptors include Ly49s, killer immunoglobulin-like receptors, leukocyte immunoglobulin-like receptors, and NKG2A/CD94, which bind MHC class I (MHC-I) molecules, and NKG2D, which binds MHC-I paralogs such as the stress-induced proteins MICA and ULBP. In addition, certain viruses have evolved MHC-like immunoevasins, such as UL18 and m157 from cytomegalovirus, that act as decoy ligands for NK receptors. A growing number of NK receptor-ligand interaction pairs involving non-MHC molecules have also been identified, including NKp30-B7-H6, killer cell lectin-like receptor G1-cadherin, and NKp80-AICL. Here, we describe crystal structures determined to date of NK cell receptors bound to MHC, MHC-related, and non-MHC ligands. Collectively, these structures reveal the diverse solutions that NK receptors have developed to recognize these molecules, thereby enabling the regulation of NK cytolytic activity by both host and viral ligands.

Indexed as

KIRLy49MHCNKG2NK receptorstructurevirus

Identifiers

PMID24723923
PMCPMC3972465
OpenAlexW2082515849

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.