Evidence map›Paper›PMID 1825659›Full record

ArticleThe Journal of cell biology1991

Differences between the lateral organization of conventional and inositol phospholipid-anchored membrane proteins. A further definition of micrometer scale membrane domains.

M Edidin, I Stroynowski

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

46 citing papers in PubMed, 125 citations in OpenAlex.

  1. Article
  2. Review
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  7. Article
  8. Review
  9. Tracking microdomain dynamics in cell membranes.Biochimica et biophysica acta · 2009
    Review
  10. Article
  11. Article
  12. Dynamic patches of membrane proteins.Biophysical journal · 2007
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
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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.

M EdidinDepartment of Biology, Johns Hopkins University, Baltimore, Maryland 21218.
I Stroynowski
Johns Hopkins University · US

Funding

CHEMISTRY AND DEVELOPMENT OF TRANSPLANTATION ANTIGENSR01AI014584 · NIAID · JOHNS HOPKINS UNIVERSITY · PI EDIDIN, MICHAEL A · 1985 to 2007
$2.8M
ISOLATION AND CHARACTERIZATION OF T CELL RECEPTOR GENESR01AI017565 · NIAID · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI HOOD, LEROY E · 1985 to 1991
–
CHEMISTRY AND DEVELOPMENT OF TRANSPLANTATION ANTIGENSR37AI014584 · NIAID · JOHNS HOPKINS UNIVERSITY · PI EDIDIN, MICHAEL A · 1988 to 1997
–
NIAID NIH HHS AI14584NIAID NIH HHS AI17565
6 · The paper itself

Abstract

Plasma membranes of many cells appear to be divided into domains, areas whose composition and function differ from the average for an entire membrane. We have previously used fluorescence photo-bleaching and recovery to demonstrate one type of membrane domain, with dimensions of micrometers (Yechiel, E., and M. Edidin. 1987, J. Cell Biol. 105: 755-760). The presence of membrane domains is inferred from the dependence of the apparent mobile fraction of labeled molecules on the size of the membrane area probed. We now find that by this definition classical class I MHC molecules, H-2Db, are concentrated in domains in the membranes of K78-2 hepatoma cells, while the nonclassical class I-related molecules, Qa-2, are free to pass the boundaries of these domains. The two proteins are highly homologous but differ in their mode of anchorage to the membrane lipid bilayer. H-2Db is anchored by a transmembrane peptide, while Qa-2 is anchored by a glycosylphosphatidylinositol (GPI) anchor. A mutant class I protein with its external portion derived from Qa-2 but with transmembrane and cytoplasmic sequences from a classical class I molecule shows a dependence of its mobile fraction on the area of membrane probed, while a mutant whose external portions are a mixture of classical and nonclassical class I sequences, GPI-linked to the bilayer, does not show this dependence and hence by our definition is not restricted to membrane domains.

Indexed as

AnimalsAntigens, HeterophileCell LineCell MembraneFluorescent Antibody TechniqueGlycolipidsGlycosylphosphatidylinositolsHistocompatibility Antigens Class IImmunoglobulin Fab FragmentsLipid BilayersLiver Neoplasms, ExperimentalMiceModels, StructuralPhosphatidylinositolsAntigens, HeterophileGlycolipidsGlycosylphosphatidylinositolsHistocompatibility Antigens Class IImmunoglobulin Fab FragmentsLipid BilayersPhosphatidylinositolsQ surface antigens

Identifiers

PMID1825659
PMCPMC2288893
OpenAlexW2145008974

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.