Author

L. Carlier

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· 2 Biophysics· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 2 Assay:protein structure· 2 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:chromatin & epigenetic regulation· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1 Assay:structural biology· 1

Frequent Co-Authors

A. Bonucci· 1 shared A. JOLIOT· 1 shared A. K. Aggarwal· 1 shared A. Thureau· 1 shared A. Walrant· 1 shared B. HE· 1 shared C. LOPIN-BON· 1 shared C. Sizun· 1 shared

Activity by Year

2021-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 14 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

1 shared paperBiophysics

A. Bonucci

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Multivalent interactions of the disordered regions of XLF and XRCC4 foster robust cellular NHEJ and drive the formation of ligation-boosting condensates in vitro

D.-D. Vu, A. Bonucci, M. Breniere, M. Cisneros-Aguirre, P. Pelupessy, Z. Wang, L. Carlier, G. Bouvignies, P. Cortes, A. K. Aggarwal, M. Blackledge, Z. Gueroui, V. Belle, J. M. STARK, M. M. Modesti, F. Ferrage

This study characterizes the multivalent interactions of XRCC4 and XLF CTRs, showing they form condensates that enhance DNA ligation in vitro and suggest roles in NHEJ dynamics and cancer biology.

bioRxiv · Jul 12, 2023Biophysics

Structural transitions in TCTP tumor protein upon Mcl-1 binding

F. Malard, C. Sizun, A. Thureau, L. Carlier, E. Lescop

This study investigates the structural changes in TCTP upon binding to Mcl-1, revealing conformational plasticity and the role of specific residues in complex stability.

bioRxiv · Nov 5, 2022 · PreprintBiochemistry

A cationic motif in Engrailed-2 homeoprotein controls its internalization via selective cell-surface glycosaminoglycans interactions

S. CARDON, G. BOLBACH, Y. P. HERVIS, C. LOPIN-BON, J.-C. JACQUINET, F. ILLIEN, A. Walrant, D. RAVAULT, B. HE, L. Molina, F. BURLINA, O. LEQUIN, A. JOLIOT, L. CARLIER, S. SAGAN

The paper identifies a cationic motif in Engrailed-2 that mediates its internalization via interactions with heparan sulfate glycosaminoglycans.

bioRxiv · Jul 29, 2021 · PreprintBiochemistry