Another great story from Jae Ho Lee in the lab: a new concept in cotranslational proteostasis-ribosome communication via chaperoneNAC. An exciting collaboration with Elke Deuerling's lab @DeuerlingLab and Marina Rodnina's lab https://t.co/XF7wlCrr5W
New exciting work from Jae Ho Lee in our lab, in a fantastic collaboration with Alessandro Ori @AOri_lab and Alessandro Cellerino @Alessan82703458 on why and how the brain ages and becomes vulnerable to neurodegenerative diseases https://t.co/sVQRO43tZo
I stand with dozens of other biopharma leaders highlighting the potential catastrophic effects of proposed research cuts on bringing innovation to patients! https://t.co/ZlDal4Euug
My NIDA grant renewal is almost 2 months late and I’m going to have to start firing my students and staff. Not a lot of transformation to be had in my lab.
@SamantLab Congratulations! Being a fellow Luddite myself I commiserate, but don't miss the irony I do so on social media. Looking forward to many more PhD thesis to come from your lab!
It was a pleasure to participate in the "Protein folding & Chaperones" platform session this morning in #bps2025 sharing our story from the @FrydmanLab about TRiC mutations and their link with brain malformations. A session with a nice mix of cool stories focused protein folding
Closing an unforgettable chapter at Stanford. Grateful for the science, the growth, and the incredible people who shaped this journey—especially Judith, with whom I had the privilege of doing great science. This place and its people will always mean a lot to me. Very excited!
3) Two surprises that could only be revealed by cryoET raise new cool future questions (I) It uncovered a new cofactor, PDCD5 which binds to ALL open TRiC complexes (and was missed by biochemical studies) and (II) closed TRiC forms stereotypic clusters of mysterious function.
2) The MS also quantified TRiC-Prefoldin cooperation in vivo. Importantly it establishes that closed TRiC engages in specific interactions with quasi-folded substrate folding intermediates in its closed folding chamber, which is clearly NOT an "Anfinsen cage"
Check out our MS describing the in vivo cycle of chaperonin TRiC/CCT, in a wonderful collaboration with Martin Beck's lab: https://t.co/0d2O9smiMF
1) The study established TRiC's important function in folding newly translated proteins and defines its ATP-driven cycle
@Beck_Laboratory@HuaipengXing@Nature Congratulations Huaipeng and Martin for this super-exciting collaboration and to all of the Beck lab for the warm welcome and hospitality during my sabbatical in Frankfurt last year! Not every day one discovers a new major chaperone cofactor, and from cryoET density no less.