Elaborate machinery for inserting proteins into the outer membrane of bacteria www.nature.com/articles/d41...

Structure and substrate recognition by the Twin-arginine translocation (Tat) pathway core complex https://www.biorxiv.org/content/10.1101/2025.09.18.677151v1

Thanks a lot to Yiyun Song @natchembio.nature.com for highlighting our ZNFX1 paper. www.nature.com/articles/s41...

We have an open post-doc position in my group to study mRNA cleavage and polyadenylation using biochemical reconstitution and cryoEM. Please get in touch if you are interested in joining this amazing team! 🔬🧬🤩 #RNA #cryoEM

I am excited to share our new preprint on the CAGE complex, a mysterious hollow protein complex that I first saw years ago while surveying Tetrahymena ciliary lysate www.biorxiv.org/content/10.1... #cilia #protistsonsky 🧬🧪

I am excited to announce that I will be moving to IMB Mainz next year! The Winter call for the IPP PhD program is now open; if you are interested in maternal #mRNA regulation and #translation in early vertebrate development, please apply! Deadline: 16 October. More info: www.imb.de/students-pos...

Pre-print: our description of RZ affiliate ZNFX1 is now online. On binding viral RNA, ZNFX1 generates parallel Ub currents, coordinating Ub-dependent RNA silencing and aggregate resolution. Huge effort from first authors Dan Squair and @eilidhrivers.bsky.social www.biorxiv.org/content/10.1...

Researchers around @clausenlab.bsky.social & @dangrabarczyk.bsky.social have unveiled the three-dimensional structure of UBR4, a giant protein complex that safeguards cells by targeting defective proteins for destruction—offering fresh insights into health & disease. www.science.org/doi/10.1126/...

Glad to share the final version of our story about the UBR4 complex, an E4 ligase protein quality control hub @science.org. Now with more cryo-EM structures and a deeper dive into substrate recognition, especially escaped mitochondrial proteins @clausenlab.bsky.social www.science.org/doi/10.1126/...

Scientists uncovered how the immune protein ZNFX1 enables cells to walk the fine line between fighting infection & avoiding autoimmune damage. ZNFX1 can ubiquitinate & compact host & viral RNA into molecular condensates, extending ubiquitin biology to RNA itself. More: www.imp.ac.at/news/article...

Happy to share our work on the structure and function of the unusual E3 ligase ZNFX1 @cp-cell.bsky.social. It uses a nucleic acid-activated transthiolation mechanism, ubiquitinating and clustering RNA to protect cells in an immune response. @clausenlab.bsky.social www.cell.com/cell/fulltex...

Opening for a biochemist to help us in the characterisation of novel ubiquitin-based antivirals. Diverse backgrounds welcomed; a keen sense of adventure is a must 😁 Details and criteria are below; please get in touch with any questions. www.jobs.gla.ac.uk/job/research...

Di-Gembodies (dimerized nanobodies) for improved and duplexed CryoEM of small and challenging targets! A collaboration of @cmd.ox.ac.uk, STRUBI, @diamondlightsource.bsky.social, @rosfrankinst.bsky.social Out now in Nature Chemical Biology @natchembio.nature.com www.nature.com/articles/s41...

A new paper reports the structure of the E4 enzyme Ufd2, which mediates K48 branched ubiquitination on K29diUb and K29triUb, identifying Ufd2’s core region as a K29diUb binding domain and a dimeric conformation for distal ubiquitin stabilization www.nature.com/articles/s41...

‼️ Exciting new preprint from a close collaboration with Kylie Walters' group. Our study maps the binding sites of key regulators of the proteasome in situ. www.biorxiv.org/content/10.1...

New preprint: In situ Architecture of #Plasmodesmata. Using #cryoET, #AlphaFold & proteomics, we uncover the native organization of plant intercellular nanopores. 🔗 doi.org/10.1101/2025... 🧪🧵1/n #teamtomo #PlantScience #Physcomitrium #Arabidopsis #cryoEM

🎉 Congratulations to our Daniel Grabarczyk, research associate in the Clausen lab, who has been awarded a prestigious FWF Principal Investigator Project Grant to support his research into the molecular mechanisms of innate immunity against viruses. Read more: www.imp.ac.at/news/article...

This is just an excellent preprint by Rasmus Jensen and colleagues from Julia Mahamid's lab @embl.org - a tour de force of Cryogenic electron tomography to do in cell structural biology in which they discover a new complex and solve its structure and function! www.biorxiv.org/content/10.1...

Great to see this out. A story that spanned continents, cities and budget codes… www.nature.com/articles/s41... Big thanks to all the teams involved! @clausenlab.bsky.social @e3chembio.bsky.social

Amazing chemical biology/structural biology work on K29/K48 branching E3 Ufd4/TRIP12 www.nature.com/articles/s41...

Thrilled to share the structure of dimerised human PINK1 docked to an endogenous translocase array on the mitochondrial surface, composed of two TOM complexes, bridged by a VDAC2 dimer! Published today in Science www.science.org/doi/10.1126/... @wehi-research.bsky.social @komanderlab.bsky.social

🎄 xmas preprint 🎄 we are excited to share our cryo-EM structure of UBR4 in complex with KCMF1 and CALM1. the PQC ligase forms a massive ubiquitination arena, primed to amplify ubiquitin chains (E4 activity) and boost degradation of defective proteins. www.biorxiv.org/content/10.1...

Happy to share our UBR4 structures. Check out the preprint to see how this giant E4 ligase complex selects substrates for ubiquitin chain extension. We also look at conservation and adaptations across humans, nematodes and plants. www.biorxiv.org/content/10.1... @clausenlab.bsky.social

SAVE THE DATE 🗓️Ubiquitin & Friends Symposium: 8-9 May 2025 in Vienna! Registration will open🔜 Keep an eye out for the announcement 👀 ✨guest speaker lineup👇🧵 +talks from abstracts! Great chance for #ECRs to meet with peers & experts in a friendly setting! 🔗 www.protein-degradation.org/symposium/