Evidence map›Paper›PMID 8570616›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1996

Characterization of GMP-17, a granule membrane protein that moves to the plasma membrane of natural killer cells following target cell recognition.

Q G Medley, N Kedersha, S O'Brien, Q Tian, S F Schlossman, M Streuli, P Anderson

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing 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

42 citing papers in PubMed.

  1. Trial
  2. Article
  3. Review
  4. Natural killer cell granule protein 7 contributes to CD8Research and practice in thrombosis and haemostasis · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Cytotoxic CD4Frontiers in immunology · 2025
    Article
  9. Article
  10. The role of CD4Frontiers in cellular and infection microbiology · 2024
    Review
  11. Article
  12. Article
  13. Cytotoxic CD4Immunity · 2021
    Review
  14. Article
  15. Preparing Membrane Proteins for Simulation Using CHARMM-GUI.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  16. Article
  17. Article
  18. NKG7 makes a better killer.Nature immunology · 2020
    Article
  19. Article
  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

7 authors.

Q G MedleyDivision of Tumor Immunology Dana Farber Cancer Institute, Boston, MA 02115, USA.
N Kedersha
S O'Brien
Q Tian
S F Schlossman
M Streuli
P Anderson

Funding

CYTOLYTIC EFFECTOR MECHANISMS OF NUCLEOLYSIN TIA-1R01AI033600 · NIAID · DANA-FARBER CANCER INSTITUTE · PI ANDERSON, PAUL J. · 1993 to 2010
$3.4M
Characterization of mammalian stress granulesR56AI033600 · NIAID · BRIGHAM AND WOMEN'S HOSPITAL · PI ANDERSON, PAUL J. · 2005 to 2005
$437k
NIAID NIH HHS AI33600
6 · The paper itself

Abstract

Cytotoxic lymphocytes are characterized by their inclusion of cytoplasmic granules that fuse with the plasma membrane following target cell recognition. We previously identified a cytotoxic granule membrane protein designated p15-TIA-1 that is immunochemically related to an RNA-recognition motif (RRM)-type RNA-binding protein designated p40-TIA-1. Although it was suggested that p15-TIA-1 might be derived from p40-T1A-1 by proteolysis, N-terminal amino acid sequencing of p15-TIA-1 immunoaffinity purified from a natural killer (NK) cell line by using monoclonal antibody (mAb) 2G9 revealed that p15-T1A-1 is identical to the deduced amino acid sequence of NKG7 and GIG-1, cDNAs isolated from NK cells and granulocyte-colony-stimulating factor-treated mononuclear cells, respectively. Epitope mapping revealed that mAb 2G9 recognizes the C terminus of p15-T1A-1 and p40-T1A-1. The deduced amino acid sequence of p15-T1A-1/NKG7/GIG-1 predicts that the protein possesses four transmembrane domains, and immuno-electron microscopy localizes the endogenous protein to the membranes of cytotoxic granules in NK cells. Given its subcellular localization, we propose to rename-this protein GMP-17, for granule membrane protein of 17 kDa. Immunofluorescence microscopy of freshly isolated NK cells confirms this granular localization. Target cell-induced NK cell degranulation results in translocation of GMP-17 from granules to the plasma membrane, suggesting a possible role for GMP-17 in regulating the effector function of lymphocytes and neutrophils.

Indexed as

Cytotoxicity, ImmunologicProteinsAmino Acid SequenceAnimalsBiological TransportCell CompartmentationCell MembraneCells, CulturedCloning, MolecularCytoplasmic GranulesDNA, ComplementaryEpitope MappingFluorescent Antibody TechniqueKiller Cells, NaturalMembrane ProteinsMicroscopy, ImmunoelectronDNA, ComplementaryMembrane ProteinsPoly(A)-Binding ProteinsProteinsRecombinant ProteinsRNA-Binding ProteinsT-Cell Intracellular Antigen-1TIA1 protein, human

Identifiers

PMID8570616
PMCPMC40113

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.