ArticleSoft matter2018
Redox sensitive protein droplets from recombinant oleosin.
Article in Soft matter, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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.
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Who cites it
11 citing papers in PubMed, 36 citations in OpenAlex.
- Redox-dependent synaptic clustering of gephyrin.Nature communications · 2026Article
- Influence of Side-Chain Molecular Features on Aqueous Coacervation of Multifunctional Homopolypeptides.Polymer science & technology (Washington, D.C.) · 2025Article
- Article
- Reversible Disulfide Bond Cross-Links as Tunable Levers of Phase Separation in Designer Biomolecular Condensates.Journal of the American Chemical Society · 2024Article
- Fundamental Aspects of Phase-Separated Biomolecular Condensates.Chemical reviews · 2024Review
- Protein Condensate Formation via Controlled Multimerization of Intrinsically Disordered Sequences.Biochemistry · 2022Article
- A spatiotemporal reconstruction of theeLife · 2022Article
- Post-translational modifications in liquid-liquid phase separation: a comprehensive review.Molecular biomedicine · 2022Review
- Amphiphilic proteins coassemble into multiphasic condensates and act as biomolecular surfactants.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Biomolecular Phase Separation: From Molecular Driving Forces to Macroscopic Properties.Annual review of physical chemistry · 2020Review
- SPLIT: Stable Protein Coacervation Using a Light Induced Transition.ACS synthetic biology · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Protein engineering enables the creation of materials with designer functionality and tailored responsiveness. Here, we design a protein with two control motifs for its phase separation into micron sized liquid droplets - one driven by a hydrophobic domain and the other by oxidation of a disulfide bond. Our work is based on the plant surfactant protein, oleosin, which has a hydrophobic domain but no cysteines. Oleosin phase separates to form liquid droplets below a critical temperature akin to many naturally occurring membrane-less organelles. Sequence mutations are made to introduce a cysteine residue into oleosin. The addition of a cysteine causes phase separation at a lower concentration and increases the phase transition temperature. Adding a reducing agent to phase-separated, cysteine-containing oleosin rapidly dissolves the droplets. The transition temperature is tuned by varying the location of the cysteine or by blending the parent cysteine-less molecule with the cysteine-containing mutant. This provides a novel way to control protein droplet formation and dissolution. We envision this work having applications as a system for the release of a protein or drug with engineered sensitivity to reducing conditions and as a mimic of membrane-less organelles in synthetic protocells.
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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.