Evidence map›Paper›PMID 32032504›Full record

ArticleBiophysical journal2020

Association of Model Neurotransmitters with Lipid Bilayer Membranes.

Brian P Josey, Frank Heinrich, Vitalii Silin, Mathias Lösche

Open access · greenAbstract read
In one paragraph

Article in Biophysical journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

16 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Serotonin Signaling through Lipid Membranes.ACS chemical neuroscience · 2024
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Selective Advantages of Synapses in Evolution.Frontiers in cell and developmental biology · 2021
    Article
  14. Uncovering a membrane-distal conformation of KRAS available to recruit RAF to the plasma membrane.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  15. Article
  16. 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

4 authors at 3 institutions in 1 country.

Brian P JoseyDepartment of Physics, Carnegie Mellon University, Pittsburgh, Pennsylvania.
Frank HeinrichDepartment of Physics, Carnegie Mellon University, Pittsburgh, Pennsylvania; National Institute of Standards and Technology, Center for Neutron Research, Gaithersburg, Maryland.
Vitalii SilinInstitute for Bioscience and Biotechnology Research, Rockville, Maryland.
Mathias LöscheDepartment of Physics, Carnegie Mellon University, Pittsburgh, Pennsylvania; National Institute of Standards and Technology, Center for Neutron Research, Gaithersburg, Maryland; Department of Biomedical Engineering, Carnegie Mellon University, Pittsburgh, Pennsylvania. Electronic address: quench@cmu.edu.
National Institute of Standards and Technology · USCarnegie Mellon University · USInstitute for Bioscience and Biotechnology Research

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aimed at reproducing the results of electrophysiological studies of synaptic signal transduction, conventional models of neurotransmission are based on the specific binding of neurotransmitters to ligand-gated receptor ion channels. However, the complex kinetic behavior observed in synaptic transmission cannot be reproduced in a standard kinetic model without the ad hoc postulation of additional conformational channel states. On the other hand, if one invokes unspecific neurotransmitter adsorption to the bilayer-a process not considered in the established models-the electrophysiological data can be rationalized with only the standard set of three conformational receptor states that also depend on this indirect coupling of neurotransmitters via their membrane interaction. Experimental verification has been difficult because binding affinities of neurotransmitters to the lipid bilayer are low. We quantify this interaction with surface plasmon resonance to measure equilibrium dissociation constants in neurotransmitter membrane association. Neutron reflection measurements on artificial membranes, so-called sparsely tethered bilayer lipid membranes, reveal the structural aspects of neurotransmitters' association with zwitterionic and anionic bilayers. We thus establish that serotonin interacts nonspecifically with the membrane at physiologically relevant concentrations, whereas γ-aminobutyric acid does not. Surface plasmon resonance shows that serotonin adsorbs with millimolar affinity, and neutron reflectometry shows that it penetrates the membrane deeply, whereas γ-aminobutyric is excluded from the bilayer.

Indexed as

Lipid BilayersNeurotransmitter AgentsKineticsMembranes, ArtificialSynaptic TransmissionLipid BilayersMembranes, ArtificialNeurotransmitter Agents

Identifiers

PMID32032504
PMCPMC7063487
OpenAlexW2323243847

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.