Carlos Moreno-Yruela

Tres miembros de la RSEQ han conseguido una ERC... – RSEQ Los miembros de la RSEQ: Carla Casadevall, Nicoletta Liguori y Carlos Moreno Yruela consiguen una ERC Starting Grant en la convocatoria 2025.

🎉 ¡Orgullo RSEQ! Nuestros socios @casadevallcarla.bsky.social,
@nikinikki87.bsky.social y @carlosmyruela.bsky.social han sido galardonados con una prestigiosa #ERCStartingGrant 2025🔬 Enhorabuena!!!!!

📖 rseq.org/tres-miembro...

@urv.cat
@lcbm-epfl.bsky.social
@iciq.org @icfo.eu

I am really excited that #CHEMTUBIO will be funded through an @erc.europa.eu Starting Grant!
This funding will kickstart my lab next year and help us unveil the mechanisms and therapeutic implications of erasers of microtubule modifications.
Stay tuned!

Six #BISTcommunity early-career researchers have secured prestigious ERC grants 👏

These awards highlight the ability of BIST Community centres to attract and nurture outstanding young international talent.

@crg.eu @icfo.eu @iciq.org @ibecbarcelona.eu

👉http://bit.ly/486ENOq

Pint of Science was again a great success in Lausanne, with >500 people attending our events!
Kudos to co-coordinators @miriamlisci.bsky.social and @juliensluneau.bsky.social, and to the fantastic team of 19 volunteers at the bars 🥳!

#PINT25 #scicomm

Single-molecule analysis reveals the mechanism of chromatin ubiquitylation by variant PRC1 complexes Single-molecule experiments show that active conformation formation controls chromatin ubiquitylation kinetics by variant PRC1.

If you always wanted to know the kinetics of how the Polycomb enzymes modify chromatin, we are thrilled to share our work!!! 🎉📄🧬🔬

Thank you, @beatfierz.bsky.social for all the guidance as well as the @lcbm-epfl.bsky.social group members for all the support!
doi.org/10.1126/scia...

Single-molecule analysis reveals the mechanism of chromatin ubiquitylation by variant PRC1 complexes Single-molecule experiments show that active conformation formation controls chromatin ubiquitylation kinetics by variant PRC1.

Check out our new study of chromatin ubiquitylation. @alexateslenko.bsky.social visualized directly at single molecule scale how vPRC1 ubiquitylates neighboring nucleosomes. These results suggest potential mechanism on how H2Aub domains are established. 👇👇👇
www.science.org/doi/10.1126/...

Lausanne Explore Pint of Science Switzerland events in Lausanne

The program for Pint of Science Lausanne 🧪 is ready!
pintofscience.ch/events/lausa...

This year we have again three venues covering topics from aging to robotic surgery or sustainable agriculture

Come join us on the 19th, 20th and 21st of May 🥳

#PintCH #scicomm @pintofscience.ch

What started as the M.Sc. projects of Michaela Benová and Athanasios Tsiris, seeking potent and selective inhibition of #HDAC11, turned into a great collaboration between the labs of @christianaolsen.bsky.social and Christian Heinis led by @danieladankova.bsky.social.

Big congratulations, Daniela!

Discovery of De Novo Macrocycle Inhibitors of Histone Deacetylase 11 Histone deacetylase (HDAC) enzymes are epigenetic regulators that affect diverse protein function by removing acyl groups from lysine side chains throughout the proteome. The most recently discovered ...

Very happy to see this story out in #JACS_Au!

Discovery of De Novo Macrocycle Inhibitors of Histone Deacetylase 11
pubs.acs.org/doi/10.1021/...

#ChemBio #chemsky #HDAC

!THREE OPPORTUNITIES TO JOIN US!

We are looking for 3 (!!!) PhD students interested in:
How Metabolism affects Genome Regulation.

Join us at @carrerasijc.bsky.social as Marie Sklodowska Curie network fellow.

More info:
2 x experimental: www.nuclear-dn.eu
1 x computational: www.hubmol.eu

🚨 Excited to share our work @elife.bsky.social doi.org/10.7554/eLife.98827.2 on targeting Hepatitis B virus #HBV 🦠 capsid aggregation by designed molecules! #DrugDiscovery #ChemBio

Thanks V Khayenko C Makbul @clemensschulte.bsky.social & @boettchercryoem.bsky.social for stunning #CryoEM visuals!

Thanks, Christian!

@naturecomms.bsky.social

Thank you as well to @snsf-ch.bsky.social and IRFD for funding my postdoc at EPFL, to the @swisschemistry.bsky.social foundation and La Caixa Foundation for supporting Polina and Esther, and other funding from @snsf-ch.bsky.social, EPFL and the Dubochet Center for Imaging.
(8/8)

This would not have been possible without the excellent (and very efficient!) contributions of Babatunde Ekundayo and Polina Foteva (who just defended her MSc thesis 🥳), of Dongchun Ni, Esther Calviño and Henning Stahlberg, or without the truly supportive guidance of @beatfierz.bsky.social.
(7/8)

The contacts of the catalytic domain with DNA, on the other hand, are responsible for maintaining #H3K36ac selectivity.
Mutating a key interacting loop helps release the enzyme from the nucleosome and become much more active on #H3K18ac substrates 🤯.
(6/8)

The multivalent interactions of the nucleosome-binding domain are important for both activities, especially to find #chromatin substrates in an environment full of nucleic acids.
Interestingly, this domain is only present in insects and most vertebrates.
(5/8)

By comparing structures trapped at each substrate position we could rationalize its activity and intrinsic selectivity 🔍.
#SIRT7 binding is optimal for targeting #H3K36ac, and it can only access #H3K18ac through partial disengagement from the nucleosome and DNA bending.
(4/8)

Babatunde Ekundayo generated beautiful high-resolution structures, where we identified:
- A unique N-terminal nucleosome-binding domain, which places the #SIRT7 catalytic domain by the H3 tail exit site
- Extensive contacts with the two DNA gyres!
(3/8)

We produced nucleosomes with a thiourea mechanism-based handle (MTU) at the H3K18 and H3K36 preferred substrate positions, through histone semi-synthesis and reconstitution in vitro.
This allowed us to stabilize specific enzyme:substrate complexes efficiently for #cryoEM.
(2/8)

#SIRT7 is a histone deacetylase with highly specific activity on #chromatin substrates.
We just published mechanism-based #cryoEM structures of #SIRT7 on nucleosomes to understand its activity 👇
www.nature.com/articles/s41...
(1/8) #ChemBio #ChemSky

Hi Dorien, I would love to be added to this started pack!

High-resolution structural imaging using customised magnetic beads.

Cryogenic Electron Microscopy: MagIC beads for scarce macromolecules. #CryoEm
https://elifesciences.org/articles/105335?utm_source=bluesky&utm_medium=social&utm_campaign=organic_insights

Welcome immigrants from X interested in science to the friendlier skies of @bsky.app, as documented by a new @nature.com survey (but you already knew that 😉)
"Bluesky is much better for science. There is much less toxicity, misinformation, and distractions."
www.nature.com/articles/d41...

Bluesky’s science takeover: 70% of Nature poll respondents use platform Roughly 6,000 readers answered our poll, with many declaring that Bluesky was nicer, kinder and less antagonistic to science than X.

Roughly 6,000 readers answered our poll, with many declaring that Bluesky was nicer, kinder and less antagonistic to science than X

https://go.nature.com/42tH8Ai

Cryogenic Electron Microscopy: MagIC beads for scarce macromolecules Specialized magnetic beads that bind target proteins to a cryogenic electron microscopy grid make it possible to study the structure of protein complexes from dilute samples.

A nice commentary article by @carlosmyruela.bsky.social y.social and @beatfierz.bsky.social has been already published! Thank you, Carlos and Beat!
elifesciences.org/articles/105...

Here is our most recent reviewed preprint on MagIC-cryo-EM invented by @yarimura.bsky.social
elifesciences.org/reviewed-pre...

Please note that this is not the final version, or VOR. A revised version (www.biorxiv.org/content/10.1...) is currently being reviewed at eLife.

Happy to share the latest preprint from my PhD studies on the discovery of de novo macrocyclic inhibitors of HDAC11. This was a great collaboration between @christianaolsen.bsky.social lab (@carlosmyruela.bsky.social, @tnhansen.bsky.social) and Christian Heinis lab (@alexanderln.bsky.social).

New preprint @chemrxiv.bsky.social on discovery of macrocyclic inhibitors of HDAC11 with the Christian Heinis #EPFL

Main contributors @danieladankova.bsky.social, @alexanderln.bsky.social, @carlosmyruela.bsky.social

🙏 @ERC_Research, @novonordiskfond, @DFF_raad for 💶

chemrxiv.org/engage/chemr...

Discovery of de novo Macrocycle Inhibitors of Histone Deacetylase 11 Histone deacetylase (HDAC) enzymes are epigenetic regulators that affect diverse protein function by removing acyl groups from lysine side chains throughout the proteome. The most recently discovered ...

Happy to share a fun collaboration between EPFL and UCPH initiated by @carlosmyruela.bsky.social, Christian Heinis, @christianaolsen.bsky.social and I!

Big shout-out to @danieladankova.bsky.social who spearheaded the project.

Now out on @chemrxiv.bsky.social

chemrxiv.org/engage/chemr...