Evidence map›Paper›PMID 40385176›Full record

ArticleACS omega2025

Self-Organizing Proteinoid-Actin Networks: Structure and Voltage Dynamics.

Panagiotis Mougkogiannis, Andrew Adamatzky

Abstract read
In one paragraph

Article in ACS omega, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. 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

2 authors.

Panagiotis MougkogiannisUnconventional Computing Laboratory, University of the West of England, Bristol BS16 1QY, U.K.ORCID https://orcid.org/0000-0003-1710-4917
Andrew AdamatzkyUnconventional Computing Laboratory, University of the West of England, Bristol BS16 1QY, U.K.ORCID https://orcid.org/0000-0003-1073-2662

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteinoids are thermal proteins produced by heating amino acids to their melting point and initiation of polymerization to produce polymeric chains. Proteinoids swell in aqueous solution forming hollow microspheres, usually filled with aqueous solution. The microspheres produce spikes of electrical potential similar to the action potentials of living neurons. The cytoskeletal protein actin is known in its filamentous form as F-actin. Filaments are organized in a double helix structure consisting of polymerized globular actin monomers. Actin is a protein that is abundantly expressed in all eukaryotic cells and plays a crucial role in cellular functions by forming an intracellular scaffold, actuators, and pathways for information transfer and processing. We produce and study proteinoid-actin networks as physical models of primitive neurons. We look at their structure and electrical dynamics. We use scanning electron microscopy and multichannel electrical recordings to study microsphere assemblies. They have distinct surface features, including ion channel-like pores. The proteinoid-actin mixture exhibits enhanced electrical properties compared to its individual components. Its conductivity (σ = 4.68 × 10

Identifiers

PMID40385176
PMCPMC12079275

What Socratic 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 Socratic graph.