Evidence map›Paper›PMID 23404286›Full record

ReviewMethods in molecular biology (Clifton, N.J.)2013

Nanodiscs as a new tool to examine lipid-protein interactions.

Mary A Schuler, Ilia G Denisov, Stephen G Sligar

Open access · greenAbstract readReview
In one paragraph

Review in Methods in molecular biology (Clifton, N.J.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
12.9field-weighted citation impact, top 1% 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

74 citing papers in PubMed, 155 citations in OpenAlex.

  1. Article
  2. Article
  3. Revealing KRas4b topology on the membrane surface.Biochemical and biophysical research communications · 2023
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Structures and Dynamics of Anionic Lipoprotein Nanodiscs.The journal of physical chemistry. B · 2022
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article

14 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

3 authors at 1 institution in 1 country.

Mary A SchulerDepartments of Biochemistry and Cell and Developmental Biology, University of Illinois, Urbana, IL, USA.
Ilia G Denisov
Stephen G Sligar
University of Illinois Urbana-Champaign · US

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 GM31756NIGMS NIH HHS GM33775NIGMS NIH HHS R01 GM031756NIGMS NIH HHS R01 GM033775NIGMS NIH HHS R37 GM031756
6 · The paper itself

Abstract

Nanodiscs are self-assembled discoidal fragments of lipid bilayers 8-16 nm in diameter, stabilized in solution by two amphipathic helical scaffold proteins. As stable and highly soluble membrane mimetics with controlled lipid composition and ability to add affinity tags to the scaffold protein, nanodiscs represent an attractive model system for solubilization, isolation, purification, and biophysical and biochemical studies of membrane proteins. In this chapter we overview various approaches to structural and functional studies of different classes of integral membrane proteins such as ion channels, transporters, GPCR and other receptors, membrane enzymes, and blood coagulation cascade proteins which have been incorporated into nanodiscs. We outline the advantages provided by homogeneity, ability to control oligomerization state of the target protein and lipid composition of the bilayer. Special attention is paid to the opportunities afforded by nanodisc system for the detailed studies of the role of different lipid properties and protein-lipid interactions in the functional behavior of membrane proteins.

Indexed as

Lipid MetabolismAmino Acid SequenceAnimalsHumansLipid BilayersMolecular Dynamics SimulationMolecular Sequence DataNanostructuresNanotechnologyProtein BindingLipid Bilayers

Identifiers

PMID23404286
PMCPMC4201044
OpenAlexW203285984

What OpenQuestion holds

Textmetadata
LicenceTDM
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.