Evidence map›Paper›PMID 12803918›Full record

ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2003

Formation of functional cell membrane domains: the interplay of lipid- and protein-mediated interactions.

Thomas Harder

Abstract readReview
In one paragraph

Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. The fate and function of glycosphingolipid glucosylceramide.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2003
    Review
  14. Glycosphingolipid functions: insights from engineered mouse models.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2003
    Review
  15. Neurobiology and cellular pathogenesis of glycolipid storage diseases.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2003
    Review
  16. Substrate reduction therapy in mouse models of the glycosphingolipidoses.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2003
    Review
  17. Future perspectives for glycolipid research in medicine.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2003
    Review
  18. A historical perspective of the glycosphingolipids and sphingolipidoses.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2003
    Article
  19. Review
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

1 author.

Thomas HarderSir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 2ET, UK. thomas.harder@path.ox.ac.uk

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Numerous cell membrane associated processes, including signal transduction, membrane sorting, protein processing and virus trafficking take place in membrane subdomains. Protein-protein interactions provide the frameworks necessary to generate biologically functional membrane domains. For example, coat proteins define membrane areas destined for sorting processes, viral proteins self-assemble to generate a budding virus, and adapter molecules organize multimolecular signalling assemblies, which catalyse downstream reactions. The concept of raft lipid-based membrane domains provides a different principle for compartmentalization and segregation of membrane constituents. Accordingly, rafts are defined by the physical properties of the lipid bilayer and function by selective partitioning of membrane lipids and proteins into membrane domains of specific phase behaviour and lipid packing. Here, I will discuss the interplay of these independent principles of protein scaffolds and raft lipid microdomains leading to the generation of biologically functional membrane domains.

Indexed as

AnimalsCell CompartmentationGlycolipidsHumansIntracellular MembranesMembrane MicrodomainsMembrane ProteinsGlycolipidsMembrane Proteins

Identifiers

PMID12803918
PMCPMC1693179

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.