Evidence map›Paper›PMID 23219517›Full record

ReviewMethods (San Diego, Calif.)2013

Biophysical characterization of membrane proteins in nanodiscs.

Sayaka Inagaki, Rodolfo Ghirlando, Reinhard Grisshammer

Erratum issuedAbstract readReview
In one paragraph

Review in Methods (San Diego, Calif.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing 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

50 citing papers in PubMed.

  1. Article
  2. In Situ Online Spectroscopy and Light Scattering Techniques.Advances in biochemical engineering/biotechnology · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Anomalous Oligomerization Behavior ofInternational journal of molecular sciences · 2023
    Article
  11. Article
  12. Review
  13. Rapid preparation of nanodiscs for biophysical studies.Archives of biochemistry and biophysics · 2021
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

3 authors.

Sayaka InagakiMembrane Protein Structure Function Unit, National Institute of Neurological Disorders and Stroke, National Institutes of Health, 5625 Fishers Lane, Room 4S12, Rockville, MD 20852, USA. inagakisn@ninds.nih.gov
Rodolfo Ghirlando
Reinhard Grisshammer

Funding

Biophysics of Macromolecular ComplexesZIADK033007 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BUCHANAN, SUSAN · 2009 to 2024
$4.9M
Function of integral membrane proteinsZIANS003103 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI GRISSHAMMER, REINHARD · 2009 to 2015
$3.9M
Intramural NIH HHS Z99 DA999999Intramural NIH HHS Z99 DK999999Intramural NIH HHS Z99 NS999999Intramural NIH HHS Z99 OD999999Intramural NIH HHS ZIA NS003103
6 · The paper itself

Abstract

Nanodiscs are self-assembled discoidal phospholipid bilayers surrounded and stabilized by membrane scaffold proteins (MSPs), that have become a powerful and promising tool for the study of membrane proteins. Even though their reconstitution is highly regulated by the type of MSP and phospholipid input, a biophysical characterization leading to the determination of the stoichiometry of MSP, lipid and membrane protein is essential. This is important for biological studies, as the oligomeric state of membrane proteins often correlates with their functional activity. Typically combinations of several methods are applied using, for example, modified samples that incorporate fluorescent labels, along with procedures that result in nanodisc disassembly and lipid dissolution. To obtain a comprehensive understanding of the native properties of nanodiscs, modification-free analysis methods are required. In this work we provide a strategy, using a combination of dynamic light scattering and analytical ultracentrifugation, for the biophysical characterization of unmodified nanodiscs. In this manner we characterize the nanodisc preparation in terms of its overall polydispersity and characterize the hydrodynamically resolved nanodisc of interest in terms of its sedimentation coefficient, Stokes' radius and overall protein and lipid stoichiometry. Functional and biological applications are also discussed for the study of the membrane protein embedded in nanodiscs under defined experimental conditions.

Indexed as

AnimalsEscherichia coliHydrodynamicsLipid BilayersMembrane ProteinsModels, MolecularNanostructuresPhospholipidsRatsReceptors, NeurotensinUltracentrifugationLipid BilayersMembrane Proteinsneurotensin type 1 receptorPhospholipidsReceptors, Neurotensin

Identifiers

PMID23219517
PMCPMC3608844

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.