Marco Capitanio

Overlapping nuclear import and export paths unveiled by two-colour MINFLUX - Nature High spatiotemporal precision tracking using 3D MINFLUX shows that nuclear import and export occur in overlapping regions of the central pore, providing insight into transport across the nuclear pore ...

Very impressive 2 colour MINFLUX in live cells www.nature.com/articles/s41... #bioimaging

lens.unifi.it/news/lens-in...

I would be happy to join!

That's very sad news, a real pioneer and hero of mechanobiology

The 10th edition of CellMech 2025, which my lab is co-organizing in Sept-Oct ‘25, has officially opened the abstract submission portal! cellmech2025.org

We are thrilled to announce our amazing list of keynote speakers, who will help us to make this conference a major event in mechanobiology!

Shaping epithelial tissues by stem cell mechanics in development and cancer - Nature Reviews Molecular Cell Biology Adult stem cells self-renew and differentiate to build, maintain and repair tissues. This Review discusses recent insights into the contribution of mechanical forces produced by epithelial stem cell a...

New #Review! 🥳

@jorgealmagro.bsky.social, @thefuchslab.bsky.social et al. discuss the role of stem cell mechanics during developmental processes and what happens when the mechanics of the stem cell niche are disrupted in cancer.

👉 go.nature.com/3EsJzJx

#StemCells #Mechanobiology #Cancer

EpiSci - 🧬 - 🧪 - #Mechanobiology

Impact of Ligand-Induced Oligomer Dissociation on Enzyme Diffusion, Directly Observed at the Single-Molecule Level The existence of the phenomenon of enhanced enzyme diffusion (EED) has been a topic of debate in recent literature. One proposed mechanism to explain the origin of EED is oligomeric enzyme dissociation. We used mass photometry (MP), a label-free single-molecule technique, to investigate the dependence of the oligomeric states of several enzymes on their ligands. The studied enzymes of interest are catalase, aldolase, alkaline phosphatase, and vanillyl-alcohol oxidase (VAO). We compared the ratios of oligomeric states in the presence and absence of the substrate as well as different substrate and inhibitor concentrations. Catalase and aldolase were found to dissociate into smaller oligomers in the presence of their substrates, independently of inhibition, while for alkaline phosphatase and VAO, different behaviors were observed. Thus, we have identified a possible mechanism which explains the previously observed diffusion enhancement in vitro. This enhancement may occur due to the dissociation of oligomers through ligand binding.

Proud to announce Yulia's paper in Nano Letters. We were planning to measure enzyme diffusion rates under different conditions using label-free single-molecule methods, and accidentally uncovered an interesting effect: pubs.acs.org/doi/10.1021/... 🧪

Now hiring 2 PhD students at the Soft Matter Lab at the University of Gothenburg for the EU project SPM4.0 project! Please, spread!

🔍 Focus: AI-driven smart microscopy, machine learning, image analysis

📍 Location: Gothenburg, Sweden 🇸🇪

🗓Apply by: 24 Feb 2025

web103.reachmee.com/ext/I005/103...