Evidence map›Paper›PMID 25551663›Full record

ArticleNature protocols2015

Protein reconstitution into freestanding planar lipid membranes for electrophysiological characterization.

Thomas Gutsmann, Thomas Heimburg, Ulrich Keyser, Kozhinjampara R Mahendran, Mathias Winterhalter

Abstract read
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In one paragraph

Article in Nature protocols, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
–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

65 citing papers in PubMed.

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  12. Naphthalene Diimide-Based Metallacage as an Artificial Ion Channel for Chloride Ion Transport.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  13. Interaction of KLAKLAK-NHPharmaceutics · 2024
    Article
  14. Review
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  19. Article
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5 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

5 authors.

Thomas GutsmannResearch Center Borstel, Center for Medicine and Bioscience, Division of Biophysics, Borstel, Germany.
Thomas HeimburgMembrane Biophysics Group, Niels Bohr Institute, University of Copenhagen, Copenhagen, Denmark.ORCID 0000000345994582
Ulrich KeyserCavendish Laboratory, University of Cambridge, Cambridge, UK.
Kozhinjampara R MahendranDepartment of Chemistry, University of Oxford, Oxford, UK.
Mathias Winterhalter1] Jacobs University Bremen, Bremen, Germany. [2].

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The reconstitution of channel-forming proteins into planar lipid bilayers enables their functional characterization at very low (sometimes below attomolar) concentrations. We describe the three main approaches used in our laboratories (the Mueller-Rudin technique, in which the bilayers contain an organic solvent, the Montal-Mueller or solvent-free technique, and a method for membrane reconstitution via liposome formation), and we discuss their respective advantages and limitations. Despite the differences in the reconstitution procedures, subsequent protein characterization is based on the same electrophysiological technique. A transmembrane electric field is applied, inducing an ion current and allowing conclusions to be drawn on apparent pore sizes, or suggesting functional properties such as channel opening and closing upon ligand binding, pH-induced conformational changes, ion selectivity or substrate specificity.

Indexed as

Electrophysiologic Techniques, CardiacLipid MetabolismPatch-Clamp TechniquesProteinsProteins

Identifiers

PMID25551663

What OpenQuestion holds

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Registered trials

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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.