Author

D. Ladant

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

Biology Disciplines

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Biophysics· 3 Biochemistry· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Organism:bacteria (other)· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Assay:imaging· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1

Frequent Co-Authors

A. CHENAL· 4 shared M. Sadi· 3 shared A. Haouz· 2 shared A. Mechaly· 2 shared D. Durand· 2 shared D. Raoux-Barbot· 2 shared J. I. Guijarro· 2 shared M. Davi· 2 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 43 mutual co-author links

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4 shared papersBiophysics

A. CHENAL

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

Functional and structural insights into the multi-step activation and catalytic mechanism of bacterial ExoY nucleotidyl cyclase toxins bound to actin-profilin

M. Teixeira-Nunes, P. Retailleau, D. Raoux-Barbot, M. Comisso, A. A. Missinou, C. Velours, S. Plancqueel, D. Ladant, U. Mechold, L. Renault

This paper investigates the activation and catalytic mechanism of ExoY toxins by analyzing their interaction with actin and profilin, revealing structural insights into their multi-step activation process.

bioRxiv · Jan 13, 2023 · PreprintBiochemistry

B2LiVe, a label-free 1D-NMR method to quantify the binding of amphitropic peptides or proteins to membrane vesicles

M. Sadi, N. Carvalho, B. Vitorge, D. Ladant, J. I. Guijarro, A. CHENAL

B2LiVe quantifies membrane binding of amphitropic peptides and proteins using label-free 1D-NMR, showing it compares well with established methods.

bioRxiv · Dec 14, 2022Biophysics

Dynamics and structural changes of calmodulin upon interaction with its potent antagonist calmidazolium

C. Leger, I. Pitard, M. Sadi, N. Carvalho, S. Brier, A. Mechaly, D. Raoux Barbot, M. Davi, S. Hoos, P. Weber, P. Vachette, D. Durand, A. Haouz, J. I. Guijarro, D. Ladant, A. CHENAL

This study characterizes the structural and dynamic changes in calmodulin upon binding to calmidazolium, revealing conformational shifts similar to those induced by peptide ligands.

bioRxiv · Jan 19, 2022 · PreprintBiophysics

A high-affinity calmodulin-binding site in the CyaA toxin translocation domain is essential for invasion into eukaryotic cells

A. Voegele, M. Sadi, D. P. O'Brien, P. Gehan, D. Raoux-Barbot, M. Davi, S. Hoss, S. Brule, B. Raynal, P. Weber, A. Mechaly, A. Haouz, N. Rodriguez, P. Vachette, D. Durand, , A. Chenal

bioRxiv · Sep 14, 2020Biophysics

Functional and structural consequences of epithelial cell invasion by Bordetella pertussis adenylate cyclase toxin

C. Angely, D. Ladant, E. Planus, B. Louis, M. Filoche, A. Chenal, d. ISABEY

This study investigates how Bordetella pertussis adenylate cyclase toxin (CyaA) alters the structure and function of A549 alveolar epithelial cells by increasing intracellular cAMP, leading to cell rounding, actin remodeling, and impaired migration and wound healing.

bioRxiv · Jan 31, 2020Cell Biology