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Sua Myong

Researcher at Johns Hopkins University

Publications -  111
Citations -  6662

Sua Myong is an academic researcher from Johns Hopkins University. The author has contributed to research in topics: RNA & Helicase. The author has an hindex of 34, co-authored 89 publications receiving 5207 citations. Previous affiliations of Sua Myong include University of Illinois at Urbana–Champaign & Max Planck Society.

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The disordered P granule protein LAF-1 drives phase separation into droplets with tunable viscosity and dynamics

TL;DR: It is demonstrated that an N-terminal, arginine/glycine rich, intrinsically disordered protein (IDP) domain of LAF-1 is necessary and sufficient for both phase separation and RNA–protein interactions, and insight is provided into the mechanism by which IDP-driven molecular interactions give rise to liquid phase organelles with tunable properties.
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The transcription factor GABP selectively binds and activates the mutant TERT promoter in cancer

TL;DR: Cancer-associated mutations in the promoter of the telomerase gene allow increased activation by transcription factor binding, and GABP thus directly links TERT promoter mutations to aberrant expression in multiple cancers.
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mRNA structure determines specificity of a polyQ-driven phase separation

TL;DR: The shape of RNA can promote the formation and coexistence of the diverse array of RNA-rich liquid compartments found in a single cell and support a model in which structure-based, RNA-RNA interactions promote assembly of distinct droplets and protein-driven, conformational dynamics of the RNA maintain this identity.
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Cytosolic Viral Sensor RIG-I Is a 5′-Triphosphate-Dependent Translocase on Double-Stranded RNA

TL;DR: Using single-molecule protein-induced fluorescence enhancement, a robust adenosine 5′-triphosphate–powered dsRNA translocation activity of RIG-I is discovered and may provide a means to specifically sense and counteract replicating viruses.
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Spring-Loaded Mechanism of DNA Unwinding by Hepatitis C Virus NS3 Helicase

TL;DR: It is shown that NS3 unwinds DNA in discrete steps of about three base pairs, and, upon encountering a barrier or after unwinding >18 bp, it snaps or slips backward rapidly and repeats unwinding many times in succession, which may help to keep secondary structures resolved during viral genome replication.