Happy to share new review of endothelium glutamate receptors in brain pathology.
www.frontiersin.org/journals/pha...

Thank you, Laetitia!

Oligonucleotide (ON) RGLS4326 designed for treatment of ADPKD caused CNS-related toxicity due to competitive antagonism of AMPA receptors. Understanding this allowed making a new ON devoid of toxicity. Collaboration with Regulus/Novartis! @LauraYen42 @MariaKarela3 www.nature.com/articles/s41...

Discovery of new AMPA receptor regulators – RNA molecules that act as competitive antagonists causing CNS-related toxicity when intended for treatment of autosomal dominant polycystic kidney disease (ADPKD). Collaboration with Regulus Therapeutic/Novartis! www.nature.com/articles/s41...

Oligonucleotide (ON) RGLS4326 designed for treatment of ADPKD caused CNS-related toxicity due to competitive antagonism of AMPA receptors. Understanding this allowed making a new ON devoid of toxicity. Collaboration with Regulus/Novartis! @LauraYen42 @MariaKarela3 www.nature.com/articles/s41...

Thanks!

Now in the journal issue! Structures of kainate receptor GluK2 in the closed apo state and open conducting state bound to agonist kainate and positive allosteric modulator BPAM. www.nature.com/articles/s41...

Now in the journal issue! Molecular mechanism of activation of kainate receptor GluK2 in complex with auxiliary subunit Neto2.
www.nature.com/articles/s41...

Thank you!

Magnesium site in human oncochannel TRPV6 is formed by two negatively charged residues that are close together in the closed state and separated in the open state. Mg2+ binding keeps these residues together and stabilizes the closed state. With Chubanov/Efremov labs! www.nature.com/articles/s41...

Magnesium site in TRPV6 is formed by two negatively charged residues that are close together in the closed state and separated in the open. Magnesium binding keeps them together and stabilizes the closed state. Amazing collaboration with Chubanov and Efremov groups. www.nature.com/articles/s41...

Magnesium site in TRPV6 is formed by two negatively charged residues that are close together in the closed state and separated in the open. Magnesium binding keeps them together and stabilizes the closed state. Amazing collaboration with Chubanov and Efremov groups.
www.nature.com/articles/s41...

Magnesium site is formed by two negatively charged residues that are close together in the closed state and separated in the open state. Magnesium binding keeps these residues together and stabilizes the closed state.

Happy to share the locking mechanism of human oncochannel TRPV6 inhibition by intracellular magnesium. Amazing collaboration with Chubanov and Efremov groups. www.nature.com/articles/s41...

Structural basis for agonist and heat activation of nociceptor TRPM3 - Nature Structural & Molecular Biology TRPM3 is an ion channel that helps the body sense heat and contributes to pain. The authors show that both heat and small chemical molecules switch it on through similar changes inside the protein.

www.nature.com/articles/s41...

Asymmetric gating of a homopentameric ion channel GLIC revealed by cryo-EM | PNAS Pentameric ligand-gated ion channels (pLGICs) are vital neurotransmitter receptors that are key therapeutic targets for neurological disorders. Alt...

Pleasure to be part of this work www.pnas.org/doi/10.1073/... with Sandip Basak at NTU where we show asymmetric gating in GLIC!

Happy to share our new review of kainate receptor structure and gating. www.frontiersin.org/journals/pha...

Congratulations, Yifan, for the Anatrace Award! Yifan’s work on the TRPV1 structure with David Julius helped launch the Resolution Revolution in cryo-EM. Not just in membrane proteins—hardly any area of biophysics today has remained untouched by the techniques Yifan pioneered.

Congrats, Gabriela!

Cryo-EM snapshots of NMDA receptor activation illuminate sequential rearrangements Opening of the NMDA receptor involves bending of the helices lining the ion channel gate.

Cryo-EM snapshots of NMDA receptor activation illuminate sequential rearrangements | Science Advances www.science.org/doi/10.1126/...

How the twin-arginine translocase (Tat) system manages to transport folded proteins across membranes without any leaks? To answer this fundamental question we solved the first structure of TatB3C3 complex with bound cargo. Please check out new preprint!
t.co/962Kj9pt6F

Congrats, Ed!

🚨🧠🔬 A major breakthrough in molecular neuroscience:

I am excited to share a new story from our lab, published in accelerated format today by @nature.com:

"Delta-type glutamate receptors are ligand-gated ion channels"

Read more here (free article link): rdcu.be/eGIKz

GluA4 AMPA receptor gating mechanisms and modulation by auxiliary proteins - Nature Structural & Molecular Biology Vega-Gutiérrez et al. present cryo-electron microscopy structures of GluA4-containing AMPA receptors, which are key for brain signaling. They show GluA4-specific conformations and explain how subunit ...

www.nature.com/articles/s41...

Happy to share the molecular mechanism of activation of kainate-subtype ionotropic glutamate receptor GluK2 in complex with auxiliary subunits Neto2. In both closed/apo and open states, ligand-binding domain (LBD) layer has 2-fold rotational symmetry!
www.nature.com/articles/s41...

Happy to share our new review on the structural pharmacology of TRP channels!
Check out the supplementary table, which includes a list of all ligands, corresponding PDBs of complexes with TRP channels, and reported affinity values.

www.sciencedirect.com/science/arti... #ionchannel #TRPchannel (1/5)