Evidence map›Paper›PMID 37072125›Full record

ArticleThe journal of physical chemistry. B2023

Native Function of the Bacterial Ion Channel SthK in a Sparsely Tethered Lipid Bilayer Membrane Architecture.

Jakob Andersson, David Kleinheinz, Ulrich Ramach, Nikolaus Kiesenhofer, Alex Ashenden, Markus Valtiner, Stephen Holt, Ingo Koeper, Philipp A M Schmidpeter, Wolfgang Knoll

Open access · hybridAbstract read
In one paragraph

Article in The journal of physical chemistry. B, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

2 citing papers in PubMed, 6 citations in OpenAlex.

  1. Synergistic Membrane Disruption ofBiomimetics (Basel, Switzerland) · 2025
    Article
  2. 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

10 authors at 6 institutions in 3 countries.

Jakob AnderssonAustrian Institute of Technology GmbH, Giefinggasse 4, 1210 Vienna, Austria.ORCID 0000-0002-3675-1493
David KleinheinzAustrian Institute of Technology GmbH, Giefinggasse 4, 1210 Vienna, Austria.
Ulrich RamachTechnische Universität Wien, Wiedner Hauptstr. 8-10/134, 1040 Wien, Austria.ORCID 0000-0002-1111-2994
Nikolaus KiesenhoferAustrian Institute of Technology GmbH, Giefinggasse 4, 1210 Vienna, Austria.
Alex AshendenFlinders University of South Australia, Bedford Park SA, 5042 Adelaide, Australia.
Markus ValtinerTechnische Universität Wien, Wiedner Hauptstr. 8-10/134, 1040 Wien, Austria.ORCID 0000-0001-5410-1067
Stephen HoltAustralian Nuclear Science and Technology Organization, New Illawarra Rd, Lucas Heights, NSW 2234, Australia.ORCID 0000-0003-3189-8047
Ingo KoeperFlinders University of South Australia, Bedford Park SA, 5042 Adelaide, Australia.ORCID 0000-0002-5933-6495
Philipp A M SchmidpeterWeill Cornell Medicine, Department of Anesthesiology, 1300 York Avenue, New York, New York 10065, United States.ORCID 0000-0003-2871-9706
Wolfgang KnollAustrian Institute of Technology GmbH, Giefinggasse 4, 1210 Vienna, Austria.ORCID 0000-0003-1543-4090
Austrian Institute of Technology · ATFlinders University · AUTU Wien · ATAustralian Nuclear Science and Technology Organisation · AUCornell University · USDanube Private University · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The plasma membrane protects the interiors of cells from their surroundings and also plays a critical role in communication, sensing, and nutrient import. As a result, the cell membrane and its constituents are among the most important drug targets. Studying the cell membrane and the processes it facilitates is therefore crucial, but it is a highly complex environment that is difficult to access experimentally. Various model membrane systems have been developed to provide an environment in which membrane proteins can be studied in isolation. Among them, tethered bilayer lipid membranes (tBLMs) are a promising model system providing a solvent-free membrane environment which can be prepared by self-assembly, is resistant to mechanical disturbances and has a high electrical resistance. tBLMs are therefore uniquely suitable to study ion channels and charge transport processes. However, ion channels are often large, complex, multimeric structures and their function requires a particular lipid environment. In this paper, we show that SthK, a bacterial cyclic nucleotide gated (CNG) ion channel that is strongly dependent on the surrounding lipid composition, functions normally when embedded into a sparsely tethered lipid bilayer. As SthK has been very well characterized in terms of structure and function, it is well-suited to demonstrate the utility of tethered membrane systems. A model membrane system suitable for studying CNG ion channels would be useful, as this type of ion channel performs a wide range of physiological functions in bacteria, plants, and mammals and is therefore of fundamental scientific interest as well as being highly relevant to medicine.

Indexed as

Ion ChannelsBacteriaBacterial ProteinsCyclic AMPElectrochemical TechniquesLipid BilayersMicroscopy, Atomic ForceBacterial ProteinsCyclic AMPIon ChannelsLipid Bilayers

Identifiers

PMID37072125
PMCPMC10150356
OpenAlexW4366331216

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.