Author

S. Fontanel

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· 3

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:human· 2 Assay:cryo-EM· 1 Research Focus:drug response / drug discovery· 1 Research Focus:host-pathogen & immune response· 1 Research Focus:protein structure prediction· 1 Assay:proteomics· 1 Approach:statistical model· 1

Frequent Co-Authors

S. Granier· 3 shared C. BECHARA· 2 shared C. LEYRAT· 2 shared E. Del Nero· 2 shared J. Saint-Paul· 2 shared R. SOUNIER· 2 shared S. Jeannot· 2 shared X. Cong· 2 shared

Activity by Year

2021-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 37 mutual co-author links

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3 shared papersBiochemistry

S. Granier

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Structure of the vasopressin hormone-V2 receptor-β-arrestin1 ternary complex

J. Bous, A. Fouillen, H. Orcel, S. Trapani, X. Cong, S. Fontanel, J. Saint-Paul, J. LAI KEE HIM, S. Urbach, N. Sibille, R. SOUNIER, S. Granier, B. Mouillac, P. Bron

The paper reports the cryo-EM structure of the V2 receptor-{beta}-arrestin1 complex, revealing structural variability in GPCR-arrestin interactions.

bioRxiv · Feb 11, 2022Biochemistry

Discovery and mechanism of action of small molecule inhibitors of ceramidases

S. Granier, R. D. Healey, E. Saied, X. Cong, G. Karsai, L. Gabellier, J. Saint-Paul, E. Del Nero, S. Jeannot, M. Drapeau, S. Fontanel, D. Maurel, S. Basu, C. LEYRAT, G. Bossis, , C. Arenz

The paper discovers small molecule inhibitors of alkaline ceramidase 3 using fluorescent substrates and characterizes their mechanism of action.

bioRxiv · Jun 15, 2021Biochemistry

Mechanisms of GPCR hijacking by Staphylococcus aureus

C. M. Grison, C. Leyrat, P. Lambey, S. Jeannot, E. Del Nero, S. Fontanel, F. Peysson, J. Heuninck, R. Sounier, T. Durroux, S. Granier, C. Bechara

This study investigates how Staphylococcus aureus leukotoxins HlgA and HlgB interact with ACKR1, altering its structure and function to aid bacterial growth and immune evasion.

bioRxiv · Feb 8, 2021 · PreprintBiochemistry