π RNA Oligonucleotides Fix Harmful Protein Transitions
RNA-binding proteins with prion-like domains play vital roles in gene regulation, but under stress they can undergo abnormal phase transitions, forming toxic aggregates π«. These deleterious condensates are linked to neurodegenerative diseases such as ALS and dementia π§ . Understanding how to control these transitions is a major step toward restoring healthy cellular behavior and preventing protein misfolding.
𧬠Defining RNA Oligonucleotides that Reverse Harmful Phase Transitions
π§ͺ Recent research shows that specially designed RNA oligonucleotides can reverse these harmful phase changes π. By selectively binding to RNA-binding proteins, these oligonucleotides stabilize normal liquid-like states and prevent irreversible aggregation ⚗️. This strategy reprograms protein behavior, allowing cells to recover from stress and maintain functional RNA-protein assemblies.
π The discovery opens exciting therapeutic possibilities in molecular medicine. RNA oligonucleotides could become precision tools to rescue damaged cellular environments, combat neurodegeneration, and improve protein homeostasis π‘. As science advances, controlling phase transitions may transform how we treat RNA-protein related disorders and design next-generation RNA therapeutics. π
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