Very happy to have my grad school research published! This was a really fun project driven by a great collab with @WangyrRay. How do Hsp70 and Hsp90 cooperate to unfold a client protein? How does Hsp90 refold and reactivate a client protein? How do co-chaperones help? See below!
Very excited to announce our two new papers! #CryoEM structures demonstrate how Hsp70 and Hsp90 cooperate to regulate the folding and function of a model client, the glucocorticoid receptor. First authors @WangyrRay and @ChariMN
https://t.co/mGhYyTfN6M
https://t.co/6cyKLdcPt6
Excited to share the, now published, final version of my grad school research! Here are a few PhuN highlights from the full story. 🧵
#phage#jumbophage#cryoem
https://t.co/qzrLruvhzY
The jumbo-phage phi-PA3 encloses its replicating genome in a *beautiful* symmetrically flexible lattice!
Congratulations to an amazing mentor and friend @ENieweglowska
https://t.co/Fi28NMNpmg
Excited to share our findings about the self-assembly of the phage nucleus! In short: it’s primarily composed of a single ~70 kDa protein and forms a beautiful (I may be a little biased 😍) C2 symmetric lattice!
https://t.co/nQwHJEjSNU
Our preprint is out! How the glucocorticoid receptor (GR) is reactivated by the molecular chaperone Hsp90 and the co-chaperone p23, revealed by cryo-EM