Evidence map›Paper›PMID 32697588›Full record

ArticleThe journal of physical chemistry. B2020

Confinement in Nanodiscs Anisotropically Modifies Lipid Bilayer Elastic Properties.

Itay Schachter, Christoph Allolio, George Khelashvili, Daniel Harries

Open access · hybridAbstract read
In one paragraph

Article in The journal of physical chemistry. B, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.0field-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

21 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. A dual sensor regulates P-glycoprotein's structural plasticity.bioRxiv : the preprint server for biology · 2026
    Article
  3. Examining the thermotropic properties of large circularized nanodiscs.Biochimica et biophysica acta. Biomembranes · 2025
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Do Nanodisc Assembly Conditions Affect Natural Lipid Uptake?Journal of the American Society for Mass Spectrometry · 2023
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Photoactivation of a Mechanosensitive Channel.Frontiers in molecular biosciences · 2022
    Article
  18. Article
  19. Article
  20. Nanodiscs: A toolkit for membrane protein science.Protein science : a publication of the Protein Society · 2021
    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

4 authors at 3 institutions in 3 countries.

Itay SchachterInstitute of Chemistry, the Fritz Haber Research Center, and the Harvey M. Kruger center for Nanoscience & Nanotechnology, The Hebrew University, Jerusalem 9190401, Israel.ORCID 0000-0003-4517-4090
Christoph AllolioInstitute of Mathematics, Faculty of Mathematics and Physics, Charles University, Prague 18674, Czech Republic.ORCID 0000-0002-7525-9266
George KhelashviliDepartment of Physiology and Biophysics, Weill Cornell Medical College of Cornell University, New York, New York 10065, United States.ORCID 0000-0001-7235-8579
Daniel HarriesInstitute of Chemistry, the Fritz Haber Research Center, and the Harvey M. Kruger center for Nanoscience & Nanotechnology, The Hebrew University, Jerusalem 9190401, Israel.ORCID 0000-0002-3057-9485
Hebrew University of Jerusalem · ILCharles University · CZCornell University · US

Funding

Breakthrough Molecular Dynamics Research via an Anton2 SupercomputerR01GM116961 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI BLOOD, PHILIP D. · 2016 to 2023
$3.0M
NIGMS NIH HHS R01 GM116961
6 · The paper itself

Abstract

Lipid nanodiscs are small synthetic lipid bilayer structures that are stabilized in solution by special circumscribing (or scaffolding) proteins or polymers. Because they create native-like environments for transmembrane proteins, lipid nanodiscs have become a powerful tool for structural determination of this class of systems when combined with cryo-electron microscopy or nuclear magnetic resonance. The elastic properties of lipid bilayers determine how the lipid environment responds to membrane protein perturbations, and how the lipid in turn modifies the conformational state of the embedded protein. However, despite the abundant use of nanodiscs in determining membrane protein structure, the elastic material properties of even pure lipid nanodiscs (i.e., without embedded proteins) have not yet been quantitatively investigated. A major hurdle is due to the inherently nonlocal treatment of the elastic properties of lipid systems implemented by most existing methods, both experimental and computational. In addition, these methods are best suited for very large "infinite" size lipidic assemblies, or ones that contain periodicity, in the case of simulations. We have previously described a computational analysis of molecular dynamics simulations designed to overcome these limitations, so it allows quantification of the bending rigidity (

Indexed as

Lipid BilayersNanostructuresCryoelectron MicroscopyMembrane ProteinsMolecular Dynamics SimulationLipid BilayersMembrane Proteins

Identifiers

PMID32697588
PMCPMC7526989
OpenAlexW3044541941

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.