Evidence map›Paper›PMID 29413323›Full record

ArticleStructure (London, England : 1993)2018

Saposin Lipid Nanoparticles: A Highly Versatile and Modular Tool for Membrane Protein Research.

Ali Flayhan, Haydyn D T Mertens, Yonca Ural-Blimke, Maria Martinez Molledo, Dmitri I Svergun, Christian Löw

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing 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

42 citing papers in PubMed.

  1. Review
  2. The Nanodisc System for Investigating Protein-Lipid Interactions.Methods in molecular biology (Clifton, N.J.) · 2026
    Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. MprF fromScience advances · 2025
    Article
  9. Review
  10. Article
  11. Article
  12. Human Saposin B Ligand Binding and Presentation to α-Galactosidase A.bioRxiv : the preprint server for biology · 2024
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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

6 authors.

Ali FlayhanCentre for Structural Systems Biology (CSSB), DESY, Notkestrasse 85, 22607 Hamburg, Germany; European Molecular Biology Laboratory Hamburg, Notkestrasse 85, 22607 Hamburg, Germany.
Haydyn D T MertensEuropean Molecular Biology Laboratory Hamburg, Notkestrasse 85, 22607 Hamburg, Germany.
Yonca Ural-BlimkeCentre for Structural Systems Biology (CSSB), DESY, Notkestrasse 85, 22607 Hamburg, Germany; European Molecular Biology Laboratory Hamburg, Notkestrasse 85, 22607 Hamburg, Germany.
Maria Martinez MolledoCentre for Structural Systems Biology (CSSB), DESY, Notkestrasse 85, 22607 Hamburg, Germany; European Molecular Biology Laboratory Hamburg, Notkestrasse 85, 22607 Hamburg, Germany.
Dmitri I SvergunEuropean Molecular Biology Laboratory Hamburg, Notkestrasse 85, 22607 Hamburg, Germany.
Christian LöwCentre for Structural Systems Biology (CSSB), DESY, Notkestrasse 85, 22607 Hamburg, Germany; European Molecular Biology Laboratory Hamburg, Notkestrasse 85, 22607 Hamburg, Germany; Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Scheeles väg 2, 17177 Stockholm, Sweden. Electronic address: christian.loew@embl-hamburg.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Saposin-derived lipid nanoparticles (SapNPs) are a new alternative tool for membrane protein reconstitution. Here we demonstrate the potential and advantages of SapNPs. We show that SapA has the lowest lipid specificity for SapNP formation. These nanoparticles are modular and offer a tunable range of size and composition depending on the stoichiometric ratio of lipid and saposin components. They are stable and exhibit features typical of lipid-bilayer systems. Our data suggest that SapNPs are versatile and can adapt to membrane proteins of various sizes and architectures. Using SapA and various types of lipids we could reconstitute membrane proteins of different transmembrane cross-sectional areas (from 14 to 56 transmembrane α helices). SapNP-reconstituted proteins bound their respective ligands and were more heat stable compared with the detergent-solubilized form. Moreover, SapNPs encircle membrane proteins in a compact way, allowing structural investigations of small membrane proteins in a detergent-free environment using small-angle X-ray scattering.

Indexed as

Cell MembraneLipid BilayersMembrane ProteinsModels, MolecularNanoparticlesProtein ConformationSaposinsLipid BilayersMembrane ProteinsSaposinsmembrane protein reconstitutionmembrane proteinssaposin lipid nanoparticlesSAXS

Identifiers

PMID29413323
PMCPMC5807053

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.