Evidence map›Paper›PMID 15554919›Full record

ReviewImmunology2004

Regulation of T-cell receptor signalling by membrane microdomains.

Tahir M Razzaq, Patricia Ozegbe, Elizabeth C Jury, Phupinder Sembi, Nathan M Blackwell, Panagiotis S Kabouridis

Open access · bronzeAbstract readReview
In one paragraph

Review in Immunology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

35 citing papers in PubMed, 96 citations in OpenAlex.

  1. Article
  2. Article
  3. ASGR1 and Its Enigmatic Relative, CLEC10A.International journal of molecular sciences · 2020
    Review
  4. Toward a Membrane-Centric Biology.Frontiers in immunology · 2020
    Article
  5. Article
  6. Review
  7. Acid sphingomyelinase mediates human CD4Cell death & disease · 2017
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Lack of lacto/neolacto-glycolipids enhances the formation of glycolipid-enriched microdomains, facilitating B cell activation.Proceedings of the National Academy of Sciences of the United States of America · 2010
    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

6 authors at 2 institutions in 1 country.

Tahir M RazzaqBone and Joint Research Unit, William Harvey Research Institute, Queen Mary's School of Medicine and Dentistry, Queen Mary's College, London.
Patricia Ozegbe
Elizabeth C Jury
Phupinder Sembi
Nathan M Blackwell
Panagiotis S Kabouridis
William Harvey Research Institute · GBUniversity College London · GB

Funding

Wellcome Trust 058408
6 · The paper itself

Abstract

There is now considerable evidence suggesting that the plasma membrane of mammalian cells is compartmentalized by functional lipid raft microdomains. These structures are assemblies of specialized lipids and proteins and have been implicated in diverse biological functions. Analysis of their protein content using proteomics and other methods revealed enrichment of signalling proteins, suggesting a role for these domains in intracellular signalling. In T lymphocytes, structure/function experiments and complementary pharmacological studies have shown that raft microdomains control the localization and function of proteins which are components of signalling pathways regulated by the T-cell antigen receptor (TCR). Based on these studies, a model for TCR phosphorylation in lipid rafts is presented. However, despite substantial progress in the field, critical questions remain. For example, it is unclear if membrane rafts represent a homogeneous population and if their structure is modified upon TCR stimulation. In the future, proteomics and the parallel development of complementary analytical methods will undoubtedly contribute in further delineating the role of lipid rafts in signal transduction mechanisms.

Indexed as

HumansLymphocyte Specific Protein Tyrosine Kinase p56(lck)Membrane MicrodomainsModels, ImmunologicalReceptors, Antigen, T-CellSignal TransductionLymphocyte Specific Protein Tyrosine Kinase p56(lck)Receptors, Antigen, T-Cell

Identifiers

PMID15554919
PMCPMC1782593
OpenAlexW2038999037

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.