Francoise Ochsenbein
francoizochsenbein.bsky.social
Francoise Ochsenbein
@francoizochsenbein.bsky.social
Enthusiastic researcher in structural biology, genome stability, and epigenome integrity
Reposted by Francoise Ochsenbein
The 14th #NMR a tool for biology conference was a big success, thanks to the contributions of our 200 attendees from 18 countries, and 40% of students/postdocs. The future of NMR is in good hands. 🥰
Have a safe trip back home. See you @pasteur.fr on May 10-12, 2027 @brukercorporation.bsky.social
May 28, 2025 at 4:36 PM
Reposted by Francoise Ochsenbein
Rendez-vous à Autrans en juin pour échanger autour d'applications de nos spins préférés ! 👇
👉 Les inscriptions et le dépôt de résumés pour le congrès du Grand GERM à Autrans (38) du 2 au 6 Juin sont désormais possibles sur germ2025.sciencesconf.org. De la belle résonance magnétique en perspective et des bourses pour les doctorant·e·s! N'attendez pas le dernier moment! #RMN #NMR #IRM #RPE
February 4, 2025 at 9:27 PM
Reposted by Francoise Ochsenbein
Please RT. Join the sixth edition of our Training Unit @institut_curie
international course on Genome Instability & Human Disease open to master students, PhDs and researchers! Amazing program. Registration dead line 2nd March 2025 at training.institut-curie.org/courses/geno...
January 4, 2025 at 11:42 AM
Reposted by Francoise Ochsenbein
2) The histone chaperone CAF1 promotes PRIMPOL recruitment to restart stalled forks through ssDNA gap formation. doi.org/10.1093/nar/...
CAF-1 promotes efficient PrimPol recruitment to nascent DNA for single-stranded DNA gap formation
Abstract. Suppression of single-stranded DNA (ssDNA) gap accumulation at replication forks has emerged as a potential determinant of chemosensitivity in ho
doi.org
December 18, 2024 at 3:45 PM
(2/2)Through integrative structural and functional analyses, we identified a large disordered segment of Rad52 that binds Rad51 and functions as an assembly chaperone. It prevents Rad51 oligomerization, facilitates filament formation, and protects filaments from destabilization by the helicase Srs2.
December 18, 2024 at 11:14 PM
(1/2) Thrilled to share our findings on the assembly of the Rad51 recombinase filament in Saccharomyces cerevisiae. This work is the result of a wonderful collaboration with Eric Coïc's team at CEA Fontenay-aux-Roses and Angela Taddei's team at the Institut Curie.
www.biorxiv.org/content/10.1...
Rad52 Acts as an Assembly Chaperone to Form and Stabilize Rad51 Filaments Through a Large C-Terminus 85-Residue Segment
Homologous recombination (HR) is essential for the repair of DNA double-strand breaks and the restart of stalled replication forks. A critical step in HR is the formation of Rad51 nucleofilaments, whi...
www.biorxiv.org
December 18, 2024 at 11:12 PM
Reposted by Francoise Ochsenbein
🚨 I am super happy to announce that our analysis of how the structure of protein-RNA interfaces evolves is now published (early access) at @plos.bsky.social Computational Biology:
doi.org/10.1371/jour...
🧬🧶
December 3, 2024 at 10:03 PM
Reposted by Francoise Ochsenbein
Reposted by Francoise Ochsenbein
Our new preprint! (reposted with tags 🧬🧶)
We investigated how protein-RNA interface structure evolves by thoroughly analyzing the conservation of contacts among 2022 pairs of homologous interfaces. Work with Ikram Mahmoudi, Chloé Quignot, Carla Martins
May 30, 2024 at 10:25 AM
Reposted by Francoise Ochsenbein
🎉 Exciting news! Our latest paper in Nature Communications delves into protein-protein interaction networks & IDRs using AlphaFold2. Dive into our findings here! 🧬 #Bioinformatics
1/8
January 30, 2024 at 1:33 PM
Reposted by Francoise Ochsenbein
Happy to share our research on using AlphaFold2 to predict how peptides from disordered regions bind proteins, just published in NatureComms
rdcu.be/dwlLa
Work done with Hélène Bret and Raphael Guerois and for the revised version with great contributions from @diegozea.bsky.social and Jinmei Gao.
🧬🧶
rdcu.be
January 18, 2024 at 4:59 PM