Evidence map›Paper›PMID 21532009›Full record

ArticleMolecular & cellular proteomics : MCP2011

Nanodisc-based co-immunoprecipitation for mass spectrometric identification of membrane-interacting proteins.

Jonas Borch, Peter Roepstorff, Jakob Møller-Jensen

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

12 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
  2. Article
  3. Nanodiscs and Mass Spectrometry: Making Membranes Fly.International journal of mass spectrometry · 2020
    Article
  4. Review
  5. Review
  6. Probing the Lipid Annular Belt by Gas-Phase Dissociation of Membrane Proteins in Nanodiscs.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2016
    Article
  7. Article
  8. Article
  9. Nanodiscs as a new tool to examine lipid-protein interactions.Methods in molecular biology (Clifton, N.J.) · 2013
    Review
  10. Ice breaking in GPCR structural biology.Acta pharmacologica Sinica · 2012
    Review
  11. Article
  12. 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

3 authors at 1 institution in 1 country.

Jonas BorchInstitute for Biochemistry and Molecular Biology, University of Southern Denmark, DK-5230 Odense M, Denmark. jonasb@bmb.sdu.dk
Peter Roepstorff
Jakob Møller-Jensen
University of Southern Denmark · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteomic identification of protein interactions with membrane associated molecules in their native membrane environment pose a challenge because of technical problems of membrane handling. We investigate the possibility of employing membrane nanodiscs for harboring the membrane associated molecule to tackle the challenges. Nanodiscs are stable, homogenous pieces of membrane with a discoidal shape. They are stabilized by an encircling amphipatic protein with an engineered epitope tag. In the present study we employ the epitope tag of the nanodiscs for detection and co-immunoprecipitation of interaction partners of the glycolipid ganglioside GM1 harbored by nanodiscs. Highly specific binding activity for nanodisc-GM1 immobilized on sensorchips was observed by surface plasmon resonance in culture media from enterotoxigenic Escherischia coli. To isolate the interaction partner(s) from enterotoxigenic Escherischia coli, GM1-nanodiscs were employed for co-immunoprecipitation. The B subunit of heat labile enterotoxin was identified as a specific interaction partner by mass spectrometry, thus demonstrating that nanodisc technology is useful for highly specific detection and identification of interaction partners to specific lipids embedded in a membrane bilayer.

Indexed as

NanostructuresCell MembraneEscherichia coli ProteinsG(M1) GangliosideImmunoprecipitationMembrane ProteinsMembranes, ArtificialPhosphatidylcholinesProtein BindingSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationSurface Plasmon Resonance1-palmitoyl-2-oleoylphosphatidylcholineEscherichia coli ProteinsG(M1) GangliosideMembrane ProteinsMembranes, ArtificialPhosphatidylcholines

Identifiers

PMID21532009
PMCPMC3134077
OpenAlexW2146120316

What OpenQuestion holds

Textmetadata
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.