Thomä lab

Huge congratulations to Dr. Pius Galli on successfully defending his PhD at @biozentrum.unibas.ch! 🎉👏 Halfway through his PhD, Pius moved from FMI @fmiscience.bsky.social in Basel to EPFL, where he completed the final part of his research.

A highlight of Pius’ work was helping uncover new ways to find molecular glues — matching proteins with druggable surfaces and revealing interactions that can be exploited to redirect cellular machinery. Fantastic work, recently published in Nature Biotechnology. 🧬🔬

memento.epfl.chChromatin structure of the inactive X chromosome revealed by in situ cryo-electron tomography - EPFL

It has been a real pleasure having Pius in the lab and watching this project come together. A very well-deserved milestone — congratulations, Pius! We’ll miss having you around and can’t wait to see what comes next. 🎓🥂

Thomä lab reposted

Joy Jeongyoon Choi

@joyjoychoi.bsky.social

16 Sept

Replying to @joyjoychoi.bsky.social

I'm giving a seminar to present this work at EPFL @epflimaging.bsky.social, hosted by @beatfierz.bsky.social and @labthoma.bsky.social. Please come by if you're around campus on Tue 22nd Sept, 4:15pm (details: memento.epfl.ch/event/chroma...).

Congrats to Pius, Shuhao, and the team! Check out our latest publication: Molecular glue degraders (MGDs) like lenalidomide have transformed multiple myeloma treatment by inducing degradation of non-native substrates via the CRL4CRBN E3 ligase—but which proteins can they actually reach?

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Pairing this with a focused MGD compound screen, we show these latent interactors are privileged starting points for new degrader development—adding a scalable, rational entry point alongside the field's growing computational and proteomic toolkit.

We focused on CRL4CRBN here, but expect the approach to be readily adaptable to other E3 ligases and, more broadly, to induced-proximity applications beyond targeted protein degradation.

tinyurl.comProteome-wide identification of the druggable CRBN interactome - Nature BiotechnologyThe latent interactions of molecular glue degraders are identified proteome-wide.

tinyurl.com/24dz4yfe #TargetedProteinDegradation, #MolecularGlue, #DrugDiscovery, #EPFL @epfllibrary.bsky.social

fmi.chHow DNA packaging controls the “genome’s guardian”Our cells tightly pack DNA into structures called nucleosomes, which protect DNA but also hide important sites. The key cancer-fighting protein p53 can still access these hidden sites, especially at n...

In our latest paper with the Correia lab, led by @piusgalli.bsky.social and Shuhao Xiao, we built a scalable pipeline combining AI-driven surface mimicry (MaSIF-mimicry) with an interaction assay (GluePCA) to map the latent MGD-induced CRBN interactome: proteins that bind but aren't (yet) degraded.

Thomä lab reposted

FMI science

@fmiscience.bsky.social

31 July 2025

Our cells pack DNA into tiny bundles that hide important parts. Researchers at the FMI and EPFL found this packing affects how the cancer-fighting protein p53 works, revealing new insights into cancer. www.fmi.ch/news-events/...

31 July 2025

Congrats to all the authors on our latest work! We reveal how p53 interacts with chromatin and show, via ubiquitin-related factors USP7 and E6-E6AP, that only specific cofactors can co-reside on nucleosomes together with p53. tinyurl.com/2feuezvj @csandate.bsky.social @deyasinic.bsky.social

31 July 2025

Stay tuned for @csandate.bsky.social's thread to come! @deyasinic.bsky.social Thanks for all the support! #EPFL @fmiscience.bsky.social @erc.europa.eu @snsf.ch @krebsliga.bsky.social