New Preprint: We have solved the structure of the proteasome in complex with two different ubiquitin chains: biorxiv.org/content/10.1101/… This work spearheaded by PhD Student Sascha Amann Let me walk you through it 🧵 1/9

I have stopped posting on social media, but this is a special occasion. I am glad to share that our work has been published in Science Advances! We made it work through great collaborations with outstanding colleagues. science.org/doi/10.1126/scia…

To regulate gene activity, proteasomes - waste disposal machines of cells - must enter the nucleus. IMP Researchers now show how the adaptor protein AKIRIN2 helps ferry this massive complex through the nuclear pore: nature.com/articles/s41467-0…

We introduce a new method, EmbedOpt, for robustly steering protein sequence-to-structure diffusion models to fit experimental data (Cryo-EM, NMR) without training. 🧬📉 @mhli41 @JiequnH @PilarCossio2 EmbedOpt tackles the brittleness of the previous coordinate-space steering methods by optimizing the conditional embedding instead. These embeddings capture rich co-evolutionary signals in protein diffusion models—unlocking a new, robust and semantically meaningful diffusion steering axis. 🚀 Result: Better fitting, wider hyperparam stability, and efficiency enabled by fewer diffusion steps 📄 Preprint: arxiv.org/abs/2602.05285

Sven Klumpe, joint Group Leader at the IMP and IMBA has received a grant by the Chan Zuckerberg Initiative’s Biohub to support fibsem-os, an open-source software platform for focused ion beam–scanning electron microscopy. Read more 👉 imba.science/4tiwEP9

New work from our Haselbach lab with collaborators captures ribosomes 𝘮𝘪𝘥-𝘣𝘶𝘪𝘭𝘥 and reveals a flexible, modular strategy behind their assembly, rather than a strict assembly line. Published in _Nucleic Acids Research _👉 doi.org/10.1093/nar/gkag036

the 4th paper in this week contribution from our lab tells about ribosome biogenesis in yeast. A follow-up story from our wonderful collaborators @UniGraz - the Bergler Lab. Structural work was again done by the amazing Lorenz Grundmann academic.oup.com/nar/article…

Happy I could contribute to this amazing story. Finally visualizing the activity of single proteasomes within cells a real dream come true. Check the preprint biorxiv.org/content/10.64898…

And another paper with our contribution. Sascha Amann managed to gain structural insights from this incredible hard to analyse cryo EM. Full story at: pnas.org/doi/10.1073/pnas.25…

Have a look at our new structure of co translational folding in yeast. This is collaborative work initialized by the Rospert lab from the @UniFreiburg . Structural work has been done by the amazing Lorenz Grundmann.

🌍Open call: Junior Group Leader positions! Join a world-class biomedical research institute at the heart of the Vienna BioCenter, where curiosity drives discovery. Lead your own lab, pursue bold ideas, and shape the future of science at the IMP: imp.ac.at/career/open-positi…

How do cells decide on the life or death of a protein? 🔬 Researchers around @HaselbachLab at the IMP have captured the first high-resolution view of the human proteasome reading different ubiquitin signals. ➡️Read the full story: imp.ac.at/news/article/how-c…