Chia-Hsueh Lee
@TheCHLeeLab
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Associate Member, Dept. of Structural Biology, St. Jude Children's Research Hospital @StJudeStructBio
Joined June 2018
Our work on human urate transporter is out @cell_res. @YaxinDai single-handedly drove this project, which revealed the transport and drug mechanism of URAT1. We are grateful for the tremendous support from @StJudeStructBio
https://t.co/XBdLgxsz8G
nature.com
Cell Research - Transport mechanism and structural pharmacology of human urate transporter URAT1
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Investigators have uncovered the full activation mechanism of sweet taste receptors, proteins that detect sugar and sweeteners. Their findings could guide the design of better sugar substitutes.
stjude.org
See how the human taste receptor TAS1R2 and TAS1R3 GPCR functions via a unique VFT domain to bind sweeteners like sucralose and advantame and elicit sweetness
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Membrane Transport subgroup @BiophysicalSoc is thrilled to announce the Chris Miller Award—honoring groundbreaking contributions to membrane transport—debuting at the BPS Meeting! Named for Chris Miller, a true pioneer & mentor. Awardees will lecture at our subgroup symposium.
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As 2024 ends, we’re celebrating key discoveries by St. Jude scientists. In this #ResearchWrapUp, we’re highlighting advances in #MolecularBiology that connect basic science to better health.
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Congrats!!! @TanjaMittag
.@TanjaMittag is named 2025 Biophysical Society Fellow, for her transformative advances on the mechanisms responsible for molecular recognition and phase separation of intrinsically disordered proteins. https://t.co/rWs4NeoXPp
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Congrats! Scott @TheBlanchardLab
Scott C. Blanchard to Receive the 2025 Kazuhiko Kinosita Award in Single-Molecule Biophysics
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Human URAT1 transports urate and is a target for gout treatment. The Lee lab @stjuderesearch presents 10 cryoEM structures of URAT1 with urate, pyrazinoate, and 3 anti-gout drugs, providing mechanistic insights into urate recognition, transport cycle, and inhibition by drugs.
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Is it substrate? In our preprint led by @BiaoQiu1, we comprehensively assess EAAT3 substrate recognition properties using DSF, SSM ephys, and cryoEM. The L-Cys bound structure suggests that sodium binding is the final step of gate closure. Read below! https://t.co/trlTJaIZGB
biorxiv.org
Excitatory amino acid transporters (EAATs) reside on cell surfaces and uptake substrates, including L-glutamate, L-aspartate, and D-aspartate, using ion gradients. Among five EAATs, EAAT3 is the only...
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Researchers uncovered ten unique structures of URAT1, providing a deeper understanding on the urate transport mechanism that may offer insights into kidney disease mutations and help guide therapeutic design for gout. Learn more:
stjude.org
Discover how cryo-EM insights into URAT1, a urate transporter and member of the SLC22 transporter family advance gout and hypouricemia drug discovery
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Beautiful work from @TheCHLeeLab, just out in @cell_res
#CryoEM structures of human URAT1 provide insights into urate recognition, transport mechanism, and MOA of anti-gout drugs. #OpenAccess
https://t.co/1CnoiIoovn
nature.com
Cell Research - Transport mechanism and structural pharmacology of human urate transporter URAT1
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Transport mechanism and structural pharmacology of human urate transporter URAT1 | Cell Res https://t.co/Ovl9SqYv28
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Recovering true FRET efficiencies from single-molecule FRET experiments requires triplet state mitigation: https://t.co/FwbeXOlg1V. Donor and acceptor fluorophores accumulate in triplet states with elevated illumination intensity, which can effect FRET efficiency if unmitigated.
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Excited to share our Annual Reviews in Biophysics article on Single-Molecule Imaging of Integral Membrane Protein Dynamics and Function. Many thanks to all authors for their diligence putting this summary overview together! https://t.co/bbuuJJnkWF
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Recovering true FRET efficiencies from smFRET investigations requires triplet state mitigation https://t.co/AItNfGYoJM Grateful for the rigorous and tireless efforts from all authors of this work. Thankful to the Editor and Referees for helping us refine the take home messages!
pubmed.ncbi.nlm.nih.gov
Single-molecule fluorescence resonance energy transfer (smFRET) methods employed to quantify time-dependent compositional and conformational changes within biomolecules require elevated illumination...
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Cryo-EM reveals that iRhom2 restrains ADAM17 protease activity to control the release of growth factor and inflammatory signals https://t.co/UxxdKCq7lf
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Online Now: Cryo-EM reveals that iRhom2 restrains ADAM17 protease activity to control the release of growth factor and inflammatory signals https://t.co/UnGFftHeBf
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It is great fun to collaborate with @mjafreeman, the leading expert in the field. @lu_fangfang and @HongtuZhao worked together to reveal the structures of the ADAM17 sheddase complex and showed how iRhom2 restrains ADAM17 protease activity. https://t.co/TRv65h2tus
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@StJudeStructBio is building a world class facility, this atomic resolution Krios G4 (with Cold-FEG+Falcon4+Selectris) is one of the best setups in the US! Come see what the future of Structural Biology looks like at St Jude!!! ♥️
The St. Jude Cryo-EM Center empowers researchers with state-of-the-art tech to visualize genomes in unprecedented detail. @kellogg_liz, PhD, and her team are now utilizing a “cold FEG” microscope to understand molecular processes for groundbreaking translational studies.
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Pidathala, S., Liao, S., Dai, Y. et al. Mechanisms of neurotransmitter transport and drug inhibition in human VMAT2. Nature (2023).
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