Author

Sébastien Favre

University of FribourgORCID 0000-0002-9477-6912Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:chromatin & epigenetic regulation· 1 Assay:proteomics· 1 Approach:statistical model· 1 Organism:yeast· 1

Frequent Co-Authors

Dieter KressleriD· 3 shared Alexander Gregor GeigeriD· 1 shared Alexandre SmirnoviD· 1 shared Alfonso Méndez-GodoyiD· 1 shared Anna ForstneriD· 1 shared Annika Hausharter· 1 shared Anthony K. HenrasiD· 1 shared Benjamin PilletiD· 1 shared

Activity by Year

2026-2026 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 19 mutual co-author links

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3 shared papersBiochemistry

Dieter KresslerORCID

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3 papers

Recent·Most cited

A nucleolar assembly module integrates an ancestral isoaspartylase to safeguard ribosome biogenesis

Alexander Gregor Geiger, Sébastien Favre, Oscar Vadas, Tobias Von Arx, Fabian Ackle, Michael Ruoss, Liridona Zyberaj, Yash Verma, Ryan J. Separovich, Cedric A. J. Hutter, Michaela Oborská‐Oplová, Daniela Portugal-Calisto, Markus A. Seeger, Pedro Beltrão, Nicolas Leulliot, , Vikram Govind Panse

The paper identifies a nucleolar module involving Fap7 that ensures proper uS11 modification and incorporation into pre-ribosomes, safeguarding ribosome biogenesis.

bioRxiv · Sep 8, 2026 · PreprintBiochemistry

A bifunctional H/ACA snoRNP mediates both pseudouridylation and rRNA scaffolding during ribosome assembly

Jutta Hafner, Matthias Thoms, Hussein Hamze, Anna Forstner, Ismaël Alidou-D’Anjou, Hafiza Hebbachi, М. В. Калинина, Annika Hausharter, Sébastien Favre, Simon Lebaron, Sherif Ismail, Timo Denk, Katharina Schlick, Thomas Fröhlich, Priya Bhutada, , Brigitte Pertschy

This study identifies snR37 as a bifunctional H/ACA snoRNP that both pseudouridylates rRNA and scaffolds ribosome assembly during pre-60S intermediate formation.

bioRxiv · Apr 1, 2026 · PreprintBiochemistry

Exploration of the proxiOME of large subunit ribosomal proteins reveals Acl1 and Bcl1 as cooperating dedicated chaperones of Rpl1

Sébastien Favre, Benjamin Pillet, Fabiana Burchert, Devanarayanan Siva Sankar, Alfonso Méndez-Godoy, Stephan Kiontke, Jörn Dengjel, Gert Bange, Dieter Kressler

The paper identifies Acl1 and Bcl1 as dedicated chaperones for Rpl1 by using proximity labeling and structural analysis in yeast.

Nucleic Acids Research · Mar 19, 2026Peer-reviewedBiochemistry