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Yueru Sun

Researcher at Hong Kong University of Science and Technology

Publications -  12
Citations -  275

Yueru Sun is an academic researcher from Hong Kong University of Science and Technology. The author has contributed to research in topics: Active site & Catalysis. The author has an hindex of 8, co-authored 10 publications receiving 215 citations.

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Journal ArticleDOI

A novel curcumin analog binds to and activates TFEB in vitro and in vivo independent of MTOR inhibition

TL;DR: Curcumin derivative C1 is identified as a novel MTOR-independent activator of TFEB, which enhances autophagy and lysosome biogenesis in vitro and in vivo and is a potential therapeutic agent for the treatment of neurodegenerative diseases.
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Preferential hydrolysis of aberrant intermediates by the type II thioesterase in Escherichia coli nonribosomal enterobactin synthesis: substrate specificities and mutagenic studies on the active-site residues.

TL;DR: The results show that the type II thioesterase evolves its distinctive ability to recognize the aberrant intermediates from the versatile catalytic platform of hotdog proteins and suggests an active search mechanism for type IIThioesterases in nonribosomal peptide synthesis.
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Molecular basis of the general base catalysis of an α/β-hydrolase catalytic triad.

TL;DR: These findings suggest that the open-closed conformational change tightly couples formation of the catalytic triad to substrate binding to enhance the substrate specificities and simultaneously shield the nucleophilicity of the triad, thus allowing it to expand its catalytic power beyond theucleophilic catalysis.
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Microsecond protein folding events revealed by time-resolved fluorescence resonance energy transfer in a microfluidic mixer

TL;DR: The combination of the time-resolved fluorescence resonance energy transfer (tr-FRET) measurement and the ultrarapid hydrodynamic focusing microfluidic mixer is demonstrated and clearly resolved the early transient state of cyt c, which is populated within the dead time of the mixer and has a characteristic Trp-59-heme distance of ∼31 Å.
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A Thiamine-Dependent Enzyme Utilizes an Active Tetrahedral Intermediate in Vitamin K Biosynthesis.

TL;DR: Results show that the thiamine-dependent enzyme utilizes a tetrahedral intermediate in a mechanism distinct from the enamine catalytic chemistry.