Author

C. Leger

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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Biochemistry· 1 Biophysics· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:host-pathogen & immune response· 1 Organism:mouse· 1 Assay:protein structure· 1 Assay:proteomics· 1

Frequent Co-Authors

A. Chenal· 2 shared A. Fasano· 1 shared A. Haouz· 1 shared A. Harrington· 1 shared A. Jacq-Bailly· 1 shared A. Mechaly· 1 shared A. Proutiere· 1 shared A. Voegele· 1 shared

Activity by Year

2022-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 17 mutual co-author links

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2 shared papersMicrobiology

A. Chenal

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Author profile →

3 papers

Recent·Most cited

Catalytic bias and redox-driven inactivation of ancestral FeFe hydrogenases from group B

A. Fasano, A. Jacq-Bailly, J. Wozniak, V. Fourmond, C. Leger

This study characterizes two ancestral FeFe hydrogenases, CpIII and MeII, revealing their unique redox-driven inactivation mechanisms and the functional role of the TSCCCP motif.

bioRxiv · Jun 23, 2023Biochemistry

Gallocin A, an atypical two-peptide bacteriocin with intramolecular disulfide bonds required for activity

A. Proutiere, L. du Merle, M. Garcia-Lopez, C. Leger, A. Voegele, A. Chenal, A. Harrington, Y. Tal-Gan, T. Cokelaer, P. Trieu-Cuot, S. Dramsi

This paper characterizes gallocin A, a two-peptide bacteriocin from SGG, showing it requires intramolecular disulfide bonds for activity and that its immunity peptide shares structural features with the toxin.

bioRxiv · Dec 5, 2022Microbiology

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