Author

F.-X. Theillet

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

Click to filter author papers

Biochemistry· 1 Biophysics· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 3 Organism:human· 2 Assay:proteomics· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

R. Ghouil· 2 shared A. Alik· 1 shared A. Belsom· 1 shared A. Binolfi· 1 shared A. Carreira· 1 shared A. Constantinou· 1 shared A. Skobelkina· 1 shared C. Bouguechtouli· 1 shared

Activity by Year

2020-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 19 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

2 shared papersCell Biology

R. Ghouil

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

KIF2C-induced nuclear condensation concentrates PLK1 and phosphorylated BRCA2 at the kinetochore microtubules in mitosis

A. Skobelkina, M. Julien, S. Jeannin, S. Miron, T. Egger, R. Chaaban, G. Bouvignies, R. Ghouil, C. Friel, D. BUSSO, F.-X. Theillet, R. Le Bars, A. Carreira, A. Constantinou, J. Basbous, S. ZINN-JUSTIN

The paper shows KIF2C forms condensates during mitosis that concentrate PLK1 and phosphorylated BRCA2 at kinetochore microtubules, enhancing their kinase activity and attachment stability.

bioRxiv · Apr 13, 2024Cell Biology

Structural characterization of stem cell factors Oct4, Sox2, Nanog and Esrrb disordered domains, and a method to identify their phospho-dependent binding partners.

F.-X. Theillet, C. Bouguechtouli, R. Ghouil, A. Alik, F. Dingli, D. Loew

The paper structurally characterizes disordered domains of pluripotency transcription factors and presents a method to identify their phospho-dependent binding partners using NMR and proteomics.

bioRxiv · Mar 5, 2023Biochemistry

Megadalton-sized dityrosine aggregates of α-synuclein retain high degrees of structural disorder and internal dynamics.

S. Verzini, M. Shah, F.-X. Theillet, A. Belsom, J. Bieschke, E. E. Wanker, J. Rappsilber, A. Binolfi, P. Selenko

This study examines megadalton-sized dityrosine aggregates of α-synuclein, revealing their structural disorder and dynamics, and their role in inhibiting classical amyloid formation.

bioRxiv · Jul 26, 2020Biophysics