ArticleBioengineering (Basel, Switzerland)2023
Proton Conduction in Gly-X (X = Ser, Ser-Gly-Ser) and GS50.
Article in Bioengineering (Basel, Switzerland), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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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.
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.
Who cites it
1 citing paper in PubMed, 1 citations in OpenAlex.
- Long-Range Proton Channels Constructed via Hierarchical Peptide Self-Assembly.Advanced materials (Deerfield Beach, Fla.) · 2024Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In recent years, the use of biomaterials has been required from the viewpoint of biocompatibility of electronic devices. In this study, the proton conductivity of Glycyl-L-serine (Gly-Ser) was investigated to clarify the relationship between hydration and proton conduction in peptides. From the crystal and conductivity data, it was inferred that the proton conductivity in hydrated Gly-Ser crystals is caused by the cleavage and rearrangement of hydrogen bonds between hydration shells formed by hydrogen bonds between amino acids and water molecules. Moreover, a staircase-like change in proton conduction with hydration was observed at
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Registered trials
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.