From 4+6 to 6+6. From ER to cytoplasm. From error to destruction.
Our latest paper in @CommsBio reveals how the human Derlin-1/p97 complex transitions into a hexameric channel to drive protein retrotranslocation in ERAD. #cryoEM#ERAD#proteostasis
🔗 https://t.co/yKMHPNfHz5
Thrilled to learn that the redox activity of Kvβ has proven to play a crucial role! It brings back memories of the challenges we faced in Zhou’s lab two decades ago, trying to identify its substrates and unravel the relationship between redox activities and ion channel function.
Treat🍬 or trick👻! Glycosylation is crucial for protein maturation. Our latest research on hydroxylation & dual-glycosylation processing of collagen is now published in Nature Communications! #Collagen#Glycosylation#cryoEM
https://t.co/ZJOkN4fhGK
Incredible work from Liang Feng's lab tackling the challenging MW limit of cryo-EM 🔬 and providing deep insights into🍬 metabolic processes.
#cryoEM#Metabolism#transporter
https://t.co/qIJ28z3pYr
Zhang and collaborators' amazing work released. The plant homolog of XPR1 shows wonderful similarity regarding the structural arrangement and function. #ionchannel
https://t.co/6ngVPleCio
Proud of our latest work w/ the Zhang lab showing from structure & simulation how XPR1, the only known human Pi exporter, is regulated by InsP8 & KIDINS220 + Pi selection/permeation by a channel-like knock-kiss-kick mechanism
💻 @ciara__wallis@Riottowow
https://t.co/my7tGU5DEL
Nice work by Yixiao Zhang's lab and his collaborators @corrylab. So excited to see the XPR1-KIDINS220 complex structure. #ionchannel
https://t.co/5C8HjQpTmC
I'm very happy to announce that I have retired! I'm equally happy that @janetiwasa has agreed to continue the Molecule of the Month @buildmodels. Read about this at https://t.co/fs5LBpfL9E
A concise yet comprehensive review of the latest structural and functional insights into XPR1 @NatureSMB ! It's exciting to witness the surge in phosphate channel research—and an honor to contribute to this growing field. #cryoEM#ionchannel https://t.co/IkZ50Az91y
Our Structure of the yeast Ceramide Synthase is now out @NatureSMB! Thanks to all involved from @FlorianFrhlich3 and @MoellerGroup. https://t.co/f8pkmatxpK #cryoEM#uos
Great to see our manuscript detailing the ping-pong mechanism of human Ceramide Synthase 6 out now in @NatureSMB!
An excellent collaboration between @DavidBSauer's lab @CmdOxford, Liz Carpenter, @Boehringer and @UZH_en
link: https://t.co/766xke6V7o
PDF: https://t.co/ETbWy9Tvsx
Our paper on inositol pyrophosphate gating of the phosphate channel XPR1 is now online in @ScienceMagazine! Dive into our findings on Pi export & its regulation—key insights for understanding cellular phosphate homeostasis! #Phosphate#IonChannels
https://t.co/RUh6AkzmKO
Our paper on the structural basis of human collagen processing by the P3H1/CRTAP/PPIB complex has been published in @NatureComms with insights into the "face-to-face" catalytic sites for Proline modifications and transitions between trimer-hexamer states.
https://t.co/HVvf6waNJM
Our new paper is now online! The first structural details of AE3 (SLC4A3), a key player in pH regulation of excitable cells. Dive into our cryo-EM findings to discover AE3's unique roles & sensitivity to DIDS. Congrats @Liyan_Jian@Cyzan_zai#CryoEM
https://t.co/4NxCwjXDFy