Evidence map›Paper›PMID 28067619›Full record

ArticleeLife2017

Analyzing native membrane protein assembly in nanodiscs by combined non-covalent mass spectrometry and synthetic biology.

Erik Henrich, Oliver Peetz, Christopher Hein, Aisha Laguerre, Beate Hoffmann, Jan Hoffmann, Volker Dötsch, Frank Bernhard, Nina Morgner

Open access · goldAbstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
6.8field-weighted citation impact, top 2% 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

47 citing papers in PubMed, 84 citations in OpenAlex.

  1. Plant structural biology: Emerging technologies and future biological insights.The Plant journal : for cell and molecular biology · 2026
    Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Microbiome research reports · 2023
    Article
  11. Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. Review
  17. Review
  18. Review
  19. 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

9 authors at 1 institution in 1 country.

Erik HenrichInstitute of Biophysical Chemistry, Centre for Biomolecular Magnetic Resonance, J W Goethe-University, Frankfurt am Main, Germany.
Oliver PeetzInstitute of Physical and Theoretical Chemistry, J W Goethe-University, Frankfurt am Main, Germany.
Christopher HeinInstitute of Biophysical Chemistry, Centre for Biomolecular Magnetic Resonance, J W Goethe-University, Frankfurt am Main, Germany.
Aisha LaguerreInstitute of Biophysical Chemistry, Centre for Biomolecular Magnetic Resonance, J W Goethe-University, Frankfurt am Main, Germany.
Beate HoffmannInstitute of Biophysical Chemistry, Centre for Biomolecular Magnetic Resonance, J W Goethe-University, Frankfurt am Main, Germany.
Jan HoffmannInstitute of Physical and Theoretical Chemistry, J W Goethe-University, Frankfurt am Main, Germany.
Volker DötschInstitute of Biophysical Chemistry, Centre for Biomolecular Magnetic Resonance, J W Goethe-University, Frankfurt am Main, Germany.ORCID 0000-0001-5720-212X
Frank BernhardInstitute of Biophysical Chemistry, Centre for Biomolecular Magnetic Resonance, J W Goethe-University, Frankfurt am Main, Germany.
Nina MorgnerInstitute of Physical and Theoretical Chemistry, J W Goethe-University, Frankfurt am Main, Germany.ORCID 0000-0002-1872-490X
Goethe University Frankfurt · DE

Funding

Synthetic Antigen Binder CoreU54GM087519 · NIGMS · UNIVERSITY OF CHICAGO · PI ZHOU, MING · 2010 to 2017
$31.9M
NIGMS NIH HHS U54 GM087519
6 · The paper itself

Abstract

Membrane proteins frequently assemble into higher order homo- or hetero-oligomers within their natural lipid environment. This complex formation can modulate their folding, activity as well as substrate selectivity. Non-disruptive methods avoiding critical steps, such as membrane disintegration, transfer into artificial environments or chemical modifications are therefore essential to analyze molecular mechanisms of native membrane protein assemblies. The combination of cell-free synthetic biology, nanodisc-technology and non-covalent mass spectrometry provides excellent synergies for the analysis of membrane protein oligomerization within defined membranes. We exemplify our strategy by oligomeric state characterization of various membrane proteins including ion channels, transporters and membrane-integrated enzymes assembling up to hexameric complexes. We further indicate a lipid-dependent dimer formation of MraY translocase correlating with the enzymatic activity. The detergent-free synthesis of membrane protein/nanodisc samples and the analysis by LILBID mass spectrometry provide a versatile platform for the analysis of membrane proteins in a native environment.

Indexed as

Protein MultimerizationMass SpectrometryMembrane ProteinsProtein BindingProtein FoldingSynthetic BiologyMembrane Proteinsbiochemistrybiophysicscell-free synthetic biologymembrane proteinnanodiscnon-covalent mass spectrometrynoneoligomeric statestructural biology

Identifiers

PMID28067619
PMCPMC5291076
OpenAlexW2568145362

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.