Evidence map›Paper›PMID 16905620›Full record

ArticleBiophysical journal2006

High-resolution AFM of membrane proteins directly incorporated at high density in planar lipid bilayer.

Pierre-Emmanuel Milhiet, Francesca Gubellini, Alexandre Berquand, Patrice Dosset, Jean-Louis Rigaud, Christian Le Grimellec, Daniel Lévy

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In one paragraph

Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

26 citing papers in PubMed, 118 citations in OpenAlex.

  1. Review
  2. TheeLife · 2022
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  9. H2 -Fueled ATP Synthesis on an Electrode: Mimicking Cellular Respiration.Angewandte Chemie (International ed. in English) · 2016
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Detergent-mediated incorporation of transmembrane proteins in giant unilamellar vesicles with controlled physiological contents.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  16. Article
  17. Lipid nanotechnology.International journal of molecular sciences · 2013
    Article
  18. Article
  19. Article
  20. Review
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

7 authors at 1 institution in 1 country.

Pierre-Emmanuel MilhietCentre de Biochimie Structurale, Groupe Nanostructures et Complexes Membranaires, UMR 554 INSERM, UMR 5048 CNRS, Montpellier, France.
Francesca Gubellini
Alexandre Berquand
Patrice Dosset
Jean-Louis Rigaud
Christian Le Grimellec
Daniel Lévy
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The heterologous expression and purification of membrane proteins represent major limitations for their functional and structural analysis. Here we describe a new method of incorporation of transmembrane proteins in planar lipid bilayer starting from 1 pmol of solubilized proteins. The principle relies on the direct incorporation of solubilized proteins into a preformed planar lipid bilayer destabilized by dodecyl-beta-maltoside or dodecyl-beta-thiomaltoside, two detergents widely used in membrane biochemistry. Successful incorporations are reported at 20 degrees C and at 4 degrees C with three bacterial photosynthetic multi-subunit membrane proteins. Height measurements by atomic force microscopy (AFM) of the extramembraneous domains protruding from the bilayer demonstrate that proteins are unidirectionally incorporated within the lipid bilayer through their more hydrophobic domains. Proteins are incorporated at high density into the bilayer and on incubation diffuse and segregate into protein close-packing areas. The high protein density allows high-resolution AFM topographs to be recorded and protein subunits organization delineated. This approach provides an alternative experimental platform to the classical methods of two-dimensional crystallization of membrane proteins for the structural analysis by AFM. Furthermore, the versatility and simplicity of the method are important intrinsic properties for the conception of biosensors and nanobiomaterials involving membrane proteins.

Indexed as

Models, ChemicalModels, MolecularElasticityLipid BilayersMembrane ProteinsMicroscopy, Atomic ForceProtein ConformationStress, MechanicalLipid BilayersMembrane Proteins

Identifiers

PMID16905620
PMCPMC1614478
OpenAlexW2011028086

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.