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asibc512.bsky.social

@asibc512.bsky.social
26 followers 3 following 6 posts
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asibc512.bsky.social @asibc512.bsky.social · 31/05/2026
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.
doi.org
Allosteric network of dynamic coupling within BAP1-UCH revealed by methyl NMR - Nature Communications
BAP1 is a tumor-suppressor deubiquitinase that helps control how genes are switched on and off. In this study, the authors use NMR spectroscopy to examine how more than 40 cancer associated and relate...
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asibc512.bsky.social @asibc512.bsky.social · 15/10/2025
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
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asibc512.bsky.social @asibc512.bsky.social · 15/10/2025
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
rdcu.be
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...
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asibc512.bsky.social @asibc512.bsky.social · 15/10/2025
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/...
academic.oup.com
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