If you're curious about how cells quickly eliminate misfolded proteins produced under proteotoxic stress or mitotic substrate during cell cycle progression, check out our latest article in Nature Communications:
doi.org/10.1038/s414...

What a day! We published two papers describing the lives of proteins from Alpha shorturl.at/ZeAG7 to Omega shorturl.at/b79Eu

Seeing these processes through the lens of structural biology is so satisfying

We discovered how an engineered ribosome arrest peptide (eRAP) acts as a built-in “pause button” to precisely control protein synthesis. eRAP merges two natural stalling systems to stop the ribosome at just the right time — shaping how nascent proteins begin to fold.
academic.oup.com/nar/article/...

Excited to share our Nature Communications paper 🎉 rdcu.be/eK7wG
We uncovered by cryoEM how the human proteasome recognizes branched K11/K48 ubiquitin chains through a new K11-binding site in the RPN2 subunit, revealing how the proteasome precisely identifies targets for rapid turnover. #cryoEM

Here’s a brief teaser for our latest preprint reporting the first structures of the K11/K48-branched Ub chain bound to the human proteasome:
youtu.be/lAZrYsnoLBc?...
Check the full text for more details:
biorxiv.org/content/10.1...

Thx to @asibc512 for making this possible!