ArticleJournal of the Royal Society, Interface2020
Electrochemistry as a surrogate for protein phosphorylation: voltage-controlled assembly of reflectin A1.
Article in Journal of the Royal Society, Interface, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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
7 citing papers in PubMed, 14 citations in OpenAlex.
- Electric Double Layer Phenomena Near Surfaces Irreversibly Trigger Assembly of Tau Protein.Journal of the American Chemical Society · 2026Article
- Electrochemically Driven Optical Dynamics of Reflectin Protein Films.Advanced materials (Deerfield Beach, Fla.) · 2025Article
- A colloidal model for the equilibrium assembly and liquid-liquid phase separation of the reflectin A1 protein.Biophysical journal · 2024Article
- Reversible and size-controlled assembly of reflectin proteins using a charged azobenzene photoswitch.Chemical science · 2024Article
- Protein Charge Neutralization Is the Proximate Driver Dynamically Tuning Reflectin Assembly.International journal of molecular sciences · 2024Article
- Voltage-calibrated, finely tunable protein assembly.Journal of the Royal Society, Interface · 2023Article
- A new electrochemical method that mimics phosphorylation of the core tau peptide K18 enables kinetic and structural analysis of intermediates and assembly.The Journal of biological chemistry · 2023Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phosphorylation is among the most widely distributed mechanisms regulating the tunable structure and function of proteins in response to neuronal, hormonal and environmental signals. We demonstrate here that the low-voltage electrochemical reduction of histidine residues in reflectin A1, a protein that mediates the neuronal fine-tuning of colour reflected from skin cells for camouflage and communication in squids, acts as an
Indexed as
Identifiers
What OpenQuestion holds
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.