Ever wondered what a cell has experienced in the past? This is in general hard to measure. Here we introduce the recordanelle, to equip cells with a tool that lets them record their own history. www.nature.com/articles/s41... @natbiotech.nature.com @ethz.ch @bsse.ethz.ch

Recordanelles for transcriptome-wide single-cell RNA recording in human cells - Nature Biotechnology

Recordanelles continuously and unbiasedly record the transcriptome throughout time in living mammalian cells.

nature.com

How liquid-like is the nuclear pore barrier?🍝𖣐 Our new preprint shows that FG-NUPs exhibit nanosecond-scale, liquid-like mobility in living cells. 💧⚡O-GlcNAcylation and an importin-β gradient keep the FG network liquid-like, reconciling nuclear pore complex models.

bioRxiv Biophysics@biorxiv-biophys.bsky.social · 11mo ago

O-GlcNAcylation and an importin-β radial gradient keep the FG barrier liquid in live-cell nuclear pores https://www.biorxiv.org/content/10.64898/2025.12.09.693204v1

IDPSeminars is back again! Join us this Thursday at 1 pm Central (US) / 7 pm EU time! idpseminars.com

Exciting news 🎉 Edward Lemke has been elected as a member of the Academia Europaea! More information can be found here: www.ae-info.org/ae/Acad_Main... @acad-euro.bsky.social

🚨New Review Alert!🚨How do disordered FG-Nups regulate nuclear transport?🍝🐍 Our latest review explores recent advances in imaging & modeling, linking NPC function to disease. #NuclearPore #FGNups #Biophysics 👉 portlandpress.com/biochemsoctr...

Conformational dynamics of the nuclear pore complex central channel

The nuclear pore complex (NPC) is a vital regulator of molecular transport between the nucleus and cytoplasm in eukaryotic cells. At the heart of the NPC’s function are intrinsically disordered phenyl...

portlandpress.com

Back in Germany and reunited with my former colleagues from the @lemkelab.bsky.social over a wonderful dinner. It truly feels like coming home!❤️

Novel analysis of intrinsically disordered proteins🐍📏

Novel analysis of intrinsically disordered proteins | EMBL

Mainz University and EMBL Hamburg researchers unveil a new way to characterise disordered proteins using so-called anomalous X-ray scattering.

embl.org

Happy Chinese New Year from our lab! 🧧✨ Just as we unravel the mysteries of intrinsically disordered proteins, may the Year of the Snake bring clarity to complexity and spark breakthroughs in our scientific journey. Wishing everyone a year filled with innovation, discovery, and success! 🐍🔬

In the cover story of the February issue of @sciam.bsky.social I explain what biomolecular condensates are and why they are transforming cell biology. A short 🧵 (You'll need a subscription to read the article.) www.scientificamerican.com/article/myst...

Mysterious Blobs in Cells Are Changing the Way We Understand Life

Tiny specks called biomolecular condensates are leading to a new understanding of the cell

scientificamerican.com

In a great collaboration with @hummerlab.bsky.social and the Kräusslich lab: HIV capsid doesn't break at the NPC; instead, it cracks open the NPC itself! Details in Cell: authors.elsevier.com/sd/article/S... @mpibp.bsky.social @uniheidelberg.bsky.social A thread below:

Reliable analysis of #IntrinsicallyDisorderedProteins: Researchers of #MainzUniversity and @embl.org Hamburg present new approach to determine the form of disordered proteins by using two different methods simultaneously in a single sample 👉 press.uni-mainz.de/reliable-ana... @imbmainz.bsky.social

Thrilled to share our latest paper in PNAS! We enhanced SAXS with noncanonical amino acid labels to extract both RG and RE of IDPs, addressing key discrepancies in biophysical measurements. Big thanks to Lemke Lab for the amazing ASAXS-inspired T-shirt! www.pnas.org/doi/10.1073/...