How does a single carbon atom rewire a cancer-associated protein? Our study published in Nat Comm doi.org/10.1038/s414... combined methyl NMR spectroscopy with 40+ cancer-associated mutants to decode the allosteric communication network of the tumor suppressor BAP1.

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

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

Structural basis of K11/K48-branched ubiquitin chain recognition by the human 26S proteasome

Nature Communications - K11/K48 branched ubiquitin chains regulate protein degradation and cell cycle progression. Here, the authors report the structural basis of how such a branched ubiquitin...

rdcu.be

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/...