Evidence map›Paper›PMID 19836392›Full record

ReviewFEBS letters2010

Membrane protein assembly into Nanodiscs.

Timothy H Bayburt, Stephen G Sligar

Abstract readReview
In one paragraph

Review in FEBS letters, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 365 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
365citing papers in PubMed, 1 pooled it
–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

365 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Polarized ATR-FTIR Spectroscopy Reveals Light-Induced Peptide Insertion of LAH4 Into Photoswitchable Membranes.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026
    Article
  3. Article
  4. Review
  5. DNA-Lipid Nanodiscs with a Polyethylene Glycol Interface.Journal of the American Chemical Society · 2026
    Article
  6. Article
  7. Molecular Mechanisms Governing Peptide Nanodisc Assembly and Stability.bioRxiv : the preprint server for biology · 2026
    Article
  8. Journal of the American Chemical Society · 2026
    Article
  9. Elevator mechanism dynamics in a sodium-coupled dicarboxylate transporter.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  10. Toward Nanodisc Tailoring for SANS Study of Membrane Proteins.Bioengineering (Basel, Switzerland) · 2026
    Article
  11. The Nanodisc System for Investigating Protein-Lipid Interactions.Methods in molecular biology (Clifton, N.J.) · 2026
    Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. CHARMM-GUIJournal of chemical information and modeling · 2025
    Article
  17. Review
  18. Article
  19. Review
  20. Review

305 more citing papers are in PubMed but not listed here.

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.

Timothy H BayburtDepartment of Biochemistry, School of Molecular and Cellular Biology, University of Illinois, Urbana-Champaign, Urbana, IL 61801, USA.
Stephen G Sligar

Funding

METALLOENZYME MECHANISMSR01GM033775 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI SLIGAR, STEPHEN G. · 1985 to 2014
$5.2M
HEME PROTEIN REDUCTASESR37GM031756 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI SLIGAR, STEPHEN G. · 1999 to 2008
$3.1M
HEME PROTEIN REDUCTASESR01GM031756 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI SLIGAR, STEPHEN G. · 1985 to 2012
$1.5M
NIGMS NIH HHS GM 31756NIGMS NIH HHS GM 33775NIGMS NIH HHS R01 GM031756NIGMS NIH HHS R01 GM033775NIGMS NIH HHS R37 GM031756
6 · The paper itself

Abstract

Nanodiscs are soluble nanoscale phospholipid bilayers which can self-assemble integral membrane proteins for biophysical, enzymatic or structural investigations. This means for rendering membrane proteins soluble at the single molecule level offers advantages over liposomes or detergent micelles in terms of size, stability, ability to add genetically modifiable features to the Nanodisc structure and ready access to both sides of the phospholipid bilayer domain. Thus the Nanodisc system provides a novel platform for understanding membrane protein function. We provide an overview of the Nanodisc approach and document through several examples many of the applications to the study of the structure and function of integral membrane proteins.

Indexed as

NanostructuresAnimalsHumansLipid BilayersMembrane LipidsMembrane ProteinsModels, BiologicalModels, MolecularProtein MultimerizationSurface PropertiesLipid BilayersMembrane LipidsMembrane Proteins

Identifiers

PMID19836392
PMCPMC4758813

What OpenQuestion holds

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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.