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Yongdae Shin

Researcher at Princeton University

Publications -  20
Citations -  4090

Yongdae Shin is an academic researcher from Princeton University. The author has contributed to research in topics: Biology & Chemistry. The author has an hindex of 11, co-authored 14 publications receiving 2627 citations. Previous affiliations of Yongdae Shin include Seoul National University & Massachusetts Institute of Technology.

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Liquid phase condensation in cell physiology and disease.

TL;DR: The findings together suggest that several membrane-less organelles have been shown to exhibit a concentration threshold for assembly, a hallmark of phase separation, and represent liquid-phase condensates, which form via a biologically regulated (liquid-liquid) phase separation process.
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Spatiotemporal Control of Intracellular Phase Transitions Using Light-Activated optoDroplets

TL;DR: An optogenetic platform that uses light to activate IDR-mediated phase transitions in living cells to elucidate not only physiological phase transitions but also their link to pathological aggregates is introduced.
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Liquid Nuclear Condensates Mechanically Sense and Restructure the Genome.

TL;DR: CasDrop is used, a novel CRISPR-Cas9-based optogenetic technology, to show that various IDPs phase separate into liquid condensates that mechanically exclude chromatin as they grow and preferentially form in low-density, largely euchromatic regions.
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Nucleated transcriptional condensates amplify gene expression.

TL;DR: It is found that TAF15 has a unique charge distribution among the FET family members that enhances its interactions with the C-terminal domain of RNA polymerase II, suggesting that positive feedback between interacting transcriptional components drives localized phase separation to amplify gene expression.
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Stochastic but Highly Coordinated Protein Unfolding and Translocation by the ClpXP Proteolytic Machine

TL;DR: A mechanochemical model is presented that accounts for single-molecule, biochemical, and structural results for the observation of enzymatic memory in translocation stepping, for the kinetics of translocation steps of different sizes, and for probabilistic but highly coordinated subunit activity within the ClpX ring.