Evidence map›Paper›PMID 22824274›Full record

ArticleBiophysical journal2012

Dynamics and size of cross-linking-induced lipid nanodomains in model membranes.

Martin Štefl, Radek Šachl, Jana Humpolíčková, Marek Cebecauer, Radek Macháň, Marie Kolářová, Lennart B-Å Johansson, Martin Hof

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

23 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Article
  3. Which Moiety Drives Gangliosides to Form Nanodomains?The journal of physical chemistry letters · 2023
    Article
  4. Article
  5. Article
  6. Role of lipid rafts in persistentAnnals of translational medicine · 2022
    Review
  7. Structured clustering of the glycosphingolipid GM1 is required for membrane curvature induced by cholera toxin.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. Article
  9. Interleaflet Coupling of Lipid Nanodomains - Insights FromFrontiers in cell and developmental biology · 2020
    Review
  10. Article
  11. Article
  12. Impact of GMBiophysical journal · 2017
    Review
  13. Article
  14. Article
  15. Article
  16. 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

8 authors at 2 institutions in 2 countries.

Martin ŠteflDepartment of Biophysical Chemistry, J. Heyrovsky Institute of Physical Chemistry of the Academy of Sciences of the Czech Republic, Dolejškova, Prague, Czech Republic.
Radek Šachl
Jana Humpolíčková
Marek Cebecauer
Radek Macháň
Marie Kolářová
Lennart B-Å Johansson
Martin Hof
Czech Academy of Sciences, J. Heyrovský Institute of Physical Chemistry · CZUmeå University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Changes of membrane organization upon cross-linking of its components trigger cell signaling response to various exogenous factors. Cross-linking of raft gangliosides GM1 with cholera toxin (CTxB) was shown to cause microscopic phase separation in model membranes, and the CTxB-GM1 complexes forming a minimal lipid raft unit are the subject of ongoing cell membrane research. Yet, those subdiffraction sized rafts have never been described in terms of size and dynamics. By means of two-color z-scan fluorescence correlation spectroscopy, we show that the nanosized domains are formed in model membranes at lower sphingomyelin (Sph) content than needed for the large-scale phase separation and that the CTxB-GM1 complexes are confined in the domains poorly stabilized with Sph. Förster resonance energy transfer together with Monte Carlo modeling of the donor decay response reveal the domain radius of ~8 nm, which increases at higher Sph content. We observed two types of domains behaving differently, which suggests a dual role of the cross-linker: first, local transient condensation of the GM1 molecules compensating for a lack of Sph and second, coalescence of existing nanodomains ending in large-scale phase separation.

Indexed as

Membrane FluidityModels, ChemicalCholera ToxinCross-Linking ReagentsG(M1) GangliosideLipid BilayersMembrane MicrodomainsModels, MolecularMolecular ConformationPhase TransitionCholera ToxinCross-Linking ReagentsG(M1) GangliosideLipid Bilayers

Identifiers

PMID22824274
PMCPMC3341556
OpenAlexW1986830440

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.