Evidence map›Paper›PMID 1280826›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1992

Transmembrane signaling by the high-affinity IgE receptor on membrane preparations.

V S Pribluda, H Metzger

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

9 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Shuttling of initiating kinase between discrete aggregates of the high affinity receptor for IgE regulates the cellular response.Proceedings of the National Academy of Sciences of the United States of America · 1997
    Article
  5. Article
  6. Review
  7. Aggregation of the high-affinity IgE receptor and enhanced activity of p53/56lyn protein-tyrosine kinase.Proceedings of the National Academy of Sciences of the United States of America · 1994
    Article
  8. Transphosphorylation as the mechanism by which the high-affinity receptor for IgE is phosphorylated upon aggregation.Proceedings of the National Academy of Sciences of the United States of America · 1994
    Article
  9. Dynamics of signal transduction after aggregation of cell-surface receptors: studies on the type I receptor for IgE.Proceedings of the National Academy of Sciences of the United States of America · 1994
    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 1 institution in 1 country.

V S PribludaSection on Chemical Immunology, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892.
H Metzger
National Institute of Arthritis and Musculoskeletal and Skin Diseases · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aggregating the receptor with high affinity for IgE (Fc epsilon RI) stimulates a variety of phenomena in mast cells. Previous efforts to reproduce some of these events in broken-cell preparations such as isolated membranes have had limited success, possibly because the phenomena being monitored were too distal from the initial events. One of the earliest responses is now known to be the phosphorylation of tyrosine residues on several proteins, including the beta and gamma subunits of Fc epsilon RI. We show that in cell sonicates or on partially purified membranes derived from tumor mast cells, aggregating Fc epsilon RI stimulates phosphorylation of receptor tyrosine residues. As in the intact cells, receptor-mediated phosphorylation occurs only on receptors that are themselves aggregated. Because even in the unfractionated sonicates the phosphorylation of other cellular components was not detectably enhanced, and because the evidence is against the receptor itself being a kinase, our results suggest that phosphorylation of Fc epsilon RI is one of the earliest events stimulated by the receptor--an event that can now be investigated on simpler biological preparations than previously available.

Indexed as

Signal TransductionAnimalsCell MembraneIn Vitro TechniquesMacromolecular SubstancesMast CellsMolecular WeightPhosphorylationPhosphotyrosineProtein-Tyrosine KinasesRatsReceptor AggregationReceptors, IgETumor Cells, CulturedTyrosineMacromolecular SubstancesPhosphotyrosineProtein-Tyrosine KinasesReceptors, IgETyrosine

Identifiers

PMID1280826
PMCPMC50568
OpenAlexW2092902000

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.