Chia-Hsueh Lee

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 nature.com/articles/s4142…

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. ow.ly/X3Sl50Wzuts

@GenZadChemE Congrats 👏👏👏

This work is finally out! Huge shoutout to our collaborator, the Popescu lab! High res structure of NMDA receptor with an open pore. Much like AMPA and Kainate receptors, opening of the gate requires bending of all 4 helices lining the pore. science.org/doi/10.1126/sc…

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.

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.

@danengw @nsmb Very impressive work. Congrats!

Our paper on the reaction cycle of the human dicarboxylate transporter NaDC3 finally came out in @nsmb .

@AlexanderSobol6 @shantigangwar @MariaKarela3 @LauraYen42 @MKCMU Congrats! Sasha and the team

Structures of GluK2 kainate receptor in complex with spermine and polyamine-containing toxins elucidate the trapping mechanism of channel block and provide a template for designing new drugs. @shantigangwar @MariaKarela3 @LauraYen42 @MKCMU nature.com/articles/s4146…

@HattoriLab @PNASNews Motoyuki, Congrats!

Thrilled to share our work on the first cryo-EM structure of the zinc-activated channel (ZAC), the least characterized member in the Cys-loop receptor! @PNASNews Great collaboration with Wang lab at CPU. Congrats to Jin and all others in the team! 1/3 pnas.org/doi/10.1073/pn…

@MansoorLabOHSU @CryoEM_PNCC @NIH_CommonFund Congrats! Steve.

I would like to share some more work from us published this week! Continued thanks to PNCC for all the help with data collection (@CryoEM_PNCC ) and thank you to NIH Common Fund for the financial support to do these experiments (@NIH_CommonFund). science.org/doi/10.1126/sc…

@mike_tilapia @DrAnneCarpenter Congrats! Great work.

Our latest paper is out! In collaboration with @DrAnneCarpenter, we conducted a systematic high-content screen to understand the role of protein mislocalization in diverse human disorders. 1/ cell.com/cell/fulltext/…

@inwardopen @LeaLabTweets @wellcometrust very cool work!

Latest preprint from the group has landed - Identification of SLC45A4 as a pain gene encoding a neuronal polyamine transporter. biorxiv.org/content/10.110… A great team effort involving researchers from around the world! @LeaLabTweets @wellcometrust

Congrats!!! @TanjaMittag

Congrats! Scott @TheBlanchardLab

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. Read the full article below: nature.com/articles/s4142… #Gout #CryoEM #Urate #MedicalResearch #DrugDiscovery #StructuralBiology #GoutTreatment

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! biorxiv.org/content/10.110…

@JiSunLab @cell_res @YaxinDai @StJudeStructBio Thank you Ji.

@TheCHLeeLab @cell_res @YaxinDai @StJudeStructBio Congratulations, boss!

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 nature.com/articles/s4142…

@XiaochunLi2 @cell_res @YaxinDai @StJudeStructBio Thank you Xiaochun!

@TheCHLeeLab @cell_res @YaxinDai @StJudeStructBio Congratulations, Chia-Hsueh!

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: ow.ly/TKS950Tjxhb

@AlexanderSobol6 @cell_res @YaxinDai @StJudeStructBio Thank you Sasha🙏

@TheCHLeeLab @cell_res @YaxinDai @StJudeStructBio Congrats, Chia! Great work!

@oxkawaka Or more

Transport mechanism and structural pharmacology of human urate transporter URAT1 第二グループからURAT1の構造。あと1,2グループくらい撃ってきそうだな nature.com/articles/s4142…