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Hyun O. Lee

Researcher at Max Planck Society

Publications -  15
Citations -  6408

Hyun O. Lee is an academic researcher from Max Planck Society. The author has contributed to research in topics: Stress granule & Ubiquitin ligase. The author has an hindex of 13, co-authored 13 publications receiving 5008 citations. Previous affiliations of Hyun O. Lee include University of North Carolina at Chapel Hill & University of Michigan.

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Journal ArticleDOI

A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation

TL;DR: It is proposed that liquid-like compartments carry the trade-off between functionality and risk of aggregation and that aberrant phase transitions within liquid- like compartments lie at the heart of ALS and, presumably, other age-related diseases.
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Fusion of bone-marrow-derived cells with Purkinje neurons, cardiomyocytes and hepatocytes

TL;DR: Using a simple method based on Cre/lox recombination to detect cell fusion events, it is demonstrated that bone-marrow-derived cells (BMDCs) fuse spontaneously with neural progenitors in vitro, raising the possibility that cell fusion may contribute to the development or maintenance of these key cell types.
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A Molecular Grammar Governing the Driving Forces for Phase Separation of Prion-like RNA Binding Proteins

TL;DR: A model is developed to show that the measured saturation concentrations of phase separation are inversely proportional to the product of the numbers of arginine and tyrosine residues, which suggests it is possible to predict phase-separation properties based on amino acid sequences.
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Endoreplication: polyploidy with purpose

TL;DR: How both plants and animals use variations of the cell cycle, termed collectively as endoreplication, resulting in polyploid cells that support specific aspects of development are reviewed.
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An aberrant phase transition of stress granules triggered by misfolded protein and prevented by chaperone function

TL;DR: It is found that misfolded proteins, such as ALS‐linked variants of SOD1, specifically accumulate and aggregate within SGs in human cells, which decreases the dynamics of SGs, changes SG composition, and triggers an aberrant liquid‐to‐solid transition of in vitro reconstituted compartments.