Evidence map›Paper›PMID 27806275›Full record

ArticleBiophysical journal2016

GM1 Softens POPC Membranes and Induces the Formation of Micron-Sized Domains.

Nico Fricke, Rumiana Dimova

Abstract read
In one paragraph

Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

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  13. Glycocalyx Curving the Membrane: Forces Emerging from the Cell Exterior.Annual review of cell and developmental biology · 2021
    Review
  14. Article
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  20. The glycolipid GM1 reshapes asymmetric biomembranes and giant vesicles by curvature generation.Proceedings of the National Academy of Sciences of the United States of America · 2018
    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.

Nico FrickeMax Planck Institute of Colloids and Interfaces, Science Park Golm, Potsdam, Germany.
Rumiana DimovaMax Planck Institute of Colloids and Interfaces, Science Park Golm, Potsdam, Germany. Electronic address: rumiana.dimova@mpikg.mpg.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The influence of the glycolipid GM1 on the physical properties of POPC membranes was studied systematically by using different methods applied to giant and large unilamellar vesicles. The charge per GM1 molecule in the membrane was estimated from electrophoretic mobility measurements. Optical microscopy and differential scanning calorimetry were employed to construct a partial phase diagram of the GM1/POPC system. At room temperature, phase separation in the membrane was detected for GM1 fractions at and above ∼5 mol %, whereby GM1-rich gel-like domains were observed by fluorescent microscopy. Fluctuation analysis, vesicle electrodeformation, and micropipette aspiration were used to assess the bending rigidity of the membrane as a function of GM1 content. In the fluid phase, GM1 was shown to strongly soften the bilayer. In the region of coexistence of fluid and gel-like domains, the micropipette aspiration technique allowed measurements of the bending rigidity of the fluid phase only, whereas electrodeformation and fluctuation analysis were affected by the presence of the gel-phase domains. The observation that GM1 decreased the bilayer bending rigidity is important for understanding the role of this ganglioside in the flexibility of neuronal membranes.

Indexed as

G(M1) GangliosideMembrane MicrodomainsPhosphatidylcholinesTemperatureUnilamellar Liposomes1-palmitoyl-2-oleoylphosphatidylcholineG(M1) GangliosidePhosphatidylcholinesUnilamellar Liposomes

Identifiers

PMID27806275
PMCPMC5103020

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Registered trials

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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.