Evidence map›Paper›PMID 28581067›Full record

ReviewFEBS letters2017

Recent advances in nanodisc technology for membrane protein studies (2012-2017).

John E Rouck, John E Krapf, Jahnabi Roy, Hannah C Huff, Aditi Das

Open access · bronzeAbstract readReview
In one paragraph

Review in FEBS letters, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

44 citing papers in PubMed, 89 citations in OpenAlex.

  1. Article
  2. The Nanodisc System for Investigating Protein-Lipid Interactions.Methods in molecular biology (Clifton, N.J.) · 2026
    Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Anomalous Oligomerization Behavior ofInternational journal of molecular sciences · 2023
    Article
  9. Article
  10. Review
  11. Article
  12. Single-component nanodiscsChemical science · 2022
    Article
  13. Structures and Dynamics of Anionic Lipoprotein Nanodiscs.The journal of physical chemistry. B · 2022
    Article
  14. Article
  15. Review
  16. Slow conformational dynamics of the human AStructure (London, England : 1993) · 2022
    Article
  17. Article
  18. Article
  19. A membrane protein display platform for receptor interactome discovery.Proceedings of the National Academy of Sciences of the United States of America · 2021
    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

5 authors at 1 institution in 1 country.

John E RouckDepartment of Comparative Biosciences, Department of Biochemistry, Beckman Institute for Advanced Science, Division of Nutritional Sciences, Neuroscience Program and Department of Bioengineering, University of Illinois Urbana-Champaign, IL, USA.
John E KrapfDepartment of Comparative Biosciences, Department of Biochemistry, Beckman Institute for Advanced Science, Division of Nutritional Sciences, Neuroscience Program and Department of Bioengineering, University of Illinois Urbana-Champaign, IL, USA.
Jahnabi RoyDepartment of Chemistry, University of Illinois Urbana-Champaign, IL, USA.
Hannah C HuffDepartment of Chemistry, University of Illinois Urbana-Champaign, IL, USA.
Aditi DasDepartment of Comparative Biosciences, Department of Biochemistry, Beckman Institute for Advanced Science, Division of Nutritional Sciences, Neuroscience Program and Department of Bioengineering, University of Illinois Urbana-Champaign, IL, USA.
University of Illinois Urbana-Champaign · US

Funding

Biochemical Mechanism of Eicosanoid Synthesizing EnzymesR01GM115584 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI DAS, ADITI · 2017 to 2022
$1.7M
NIGMS NIH HHS R01 GM115584
6 · The paper itself

Abstract

Historically, the main barrier to membrane protein investigations has been the tendency of membrane proteins to aggregate (due to their hydrophobic nature), in aqueous solution as well as on surfaces. The introduction of biomembrane mimetics has since stimulated momentum in the field. One such mimetic, the nanodisc (ND) system, has proved to be an exceptional system for solubilizing membrane proteins. Herein, we critically evaluate the advantages and imperfections of employing nanodiscs in biophysical and biochemical studies. Specifically, we examine the techniques that have been modified to study membrane proteins in nanodiscs. Techniques discussed here include fluorescence microscopy, solution-state/solid-state nuclear magnetic resonance, electron microscopy, small-angle X-ray scattering, and several mass spectroscopy methods. Newer techniques such as SPR, charge-sensitive optical detection, and scintillation proximity assays are also reviewed. Lastly, we cover how nanodiscs are advancing nanotechnology through nanoplasmonic biosensing, lipoprotein-nanoplatelets, and sortase-mediated labeling of nanodiscs.

Indexed as

AnimalsHumansLipid BilayersMagnetic Resonance SpectroscopyMass SpectrometryMembrane ProteinsNanostructuresNanotechnologyLipid BilayersMembrane Proteinselectron microscopyESIFRETisotope labelinglipid bilayerMALDImembrane proteinnanodiscNMRSPR

Identifiers

PMID28581067
PMCPMC5751705
OpenAlexW2622258449

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.