Evidence map›Paper›PMID 28717925›Full record

ReviewBiophysical reviews2017

Complex biomembrane mimetics on the sub-nanometer scale.

Frederick A Heberle, Georg Pabst

Abstract readReview
In one paragraph

Review in Biophysical reviews, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Interleaflet Coupling of Lipid Nanodomains - Insights FromFrontiers in cell and developmental biology · 2020
    Review
  6. Article
  7. Article
  8. 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.

Frederick A HeberleThe Bredesen Center, University of Tennessee, Knoxville, TN, 37996, USA.
Georg PabstInstitute of Molecular Biosciences, Biophysics Division, NAWI Graz, University of Graz, 8010, Graz, Austria. georg.pabst@uni-graz.at.ORCID http://orcid.org/0000-0003-1967-1536

Funding

Austrian Science Fund P24459-B20, I1304-B20 and P27083-B20Austrian Science Fund FWF P 24459Austrian Science Fund FWF P 27083U.S. Department of Energy DE-AC05-00OR22725
6 · The paper itself

Abstract

Biomimetic lipid vesicles are indispensable tools for gaining insight into the biophysics of cell physiology on the molecular level. The level of complexity of these model systems has steadily increased, and now spans from domain-forming lipid mixtures to asymmetric lipid bilayers. Here, we review recent progress in the development and application of elastic neutron and X-ray scattering techniques for studying these systems in situ and under physiologically relevant conditions on the nanometer to sub-nanometer length scales. In particular, we focus on: (1) structural details of coexisting liquid-ordered and liquid-disordered domains, including their thickness and lipid packing mismatch as a function of a size transition from nanoscopic to macroscopic domains; (2) membrane-mediated protein partitioning into lipid domains; (3) the role of the aqueous medium in tuning interactions between membranes and domains; and (4) leaflet-specific structure in asymmetric bilayers and passive lipid flip-flop.

Indexed as

Asymmetric bilayersIntermembrane interactionsLipid domainsLipid flip-flopLipid-protein interactionsSmall-angle neutron and X-ray scattering

Identifiers

PMID28717925
PMCPMC5578918

What OpenQuestion holds

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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.