Author

D. Fenel

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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Immunology· 3 Biochemistry· 2 Biophysics· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 7 Assay:proteomics· 4 Research Focus:host-pathogen & immune response· 3 Research Focus:cell type annotation· 2 Research Focus:drug response / drug discovery· 2 Research Focus:cell-cell communication· 1 Organism:human· 1 Organism:mouse· 1

Frequent Co-Authors

G. Schoehn· 5 shared I. Bally· 3 shared A. Amen· 2 shared F. Fieschi· 2 shared M. Buisson· 2 shared M. Thepaut· 2 shared N. Thielens· 2 shared P. Poignard· 2 shared

Activity by Year

2020-2022 · peak 5/yr

Co-Author Collaboration Network

10 top collaborators · 41 mutual co-author links

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Curved chords = mutual co-authorship

5 shared papersImmunology

G. Schoehn

Mutual co-authors in cluster

Author profile →

7 papers

Recent·Most cited

Three-dimensional envelope and subunit interactions of the plastid-encoded RNA polymerase from Sinapis alba

R. Ruedas, Y. Coute, S. Kieffer-Jaquinod, S. Sankari Muthukumar, F.-X. Gillet, D. Fenel, G. Effantin, T. Pfannschmidt, R. Blanvillain, D. Cobessi

This study determines the 3D structure of the plastid-encoded RNA polymerase (PEP) from Sinapis alba and identifies subunit interactions through proteomics and electron microscopy.

bioRxiv · May 4, 2022Biochemistry

Structural Basis for the Inhibition of IAPP Fibril Formation by the Hsp60 Co-Chaperonin Prefoldin

R. Toerner, T. Kupreichyk, L. Gremer, E. Colas Debled, D. Fenel, P. Gans, D. Willbold, G. Schoehn, W. Hoyer, J. Boisbouvier

This study shows how prefoldin inhibits IAPP fibril formation by binding to the N-terminal segment of IAPP on fibril surfaces and ends, reducing aggregate size and number.

bioRxiv · Oct 20, 2021Biophysics

The archaeal division protein CdvB1 assembles into polymers that are depolymerized by CdvC

A. Blanch Jover, N. De Franceschi, D. Fenel, W. Weissenhorn, C. Dekker

This study shows that CdvB1 forms filamentous polymers that are depolymerized by CdvC, and that polymerization and membrane binding are mutually exclusive.

bioRxiv · Oct 7, 2021 · PreprintBiochemistry

Elicitation of potent SARS-CoV-2 neutralizing antibody responses through immunization using a versatile adenovirus-inspired multimerization platform

C. Chevillard, A. Amen, S. Besson, D. Hannani, I. Bally, V. Dettling, E. Gout, C. J. Moreau, M. Buisson, S. Gallet, D. Fenel, E. Vassal-Stermann, G. Schoehn, P. Poignard, M.-C. Dagher, P. Fender

This paper describes a vaccine platform using adenovirus-inspired nanoparticles decorated with SARS-CoV-2 RBD to elicit potent neutralizing antibodies in mice.

bioRxiv · Sep 13, 2021Microbiology

Immunization with synthetic SARS-CoV-2 S glycoprotein virus-like particles protects Macaques from infection

G. Sulbaran, P. Maisonnasse, A. Amen, D. Guilligay, N. Bosquet, J. A. Burger, M. Poniman, M. Buisson, S. D. Dylon, T. Naninck, J. Lemaitre, W. Gros, A.-S. Gallouet, R. Marlin, C. Bouillier, , W. Weissenhorn

This study develops a synthetic SARS-CoV-2 S glycoprotein virus-like particle vaccine that protects macaques from infection through strong antibody and T cell responses.

bioRxiv · Jul 26, 2021Immunology

Immediate and sustained effects of cobalt and zinc-containing pigments on macrophages

J. Devcic, M. Dussol, V. Collin-Faure, J. Perard, D. Fenel, G. Schoehn, M. Carriere, T. Rabilloud, B. Dalzon

This study examines the immediate and sustained effects of cobalt- and zinc-based pigments on macrophages, revealing functional disorders that persist even at non-toxic doses.

bioRxiv · Apr 20, 2021Immunology

DC/L-SIGN recognition of spike glycoprotein promotes SARS-CoV-2 trans-infection and can be inhibited by a glycomimetic antagonist

M. Thepaut, J. Luczkowiak, C. Vives, N. Labiod, I. Bally, F. Lasala, Y. Grimoire, D. Fenel, S. Sattin, N. Thielens, G. Schoehn, A. Bernardi, R. Delgado, F. Fieschi

The paper shows DC/L-SIGN receptors on antigen-presenting cells enhance SARS-CoV-2 trans-infection, which can be blocked by a glycomimetic compound.

bioRxiv · Aug 9, 2020Immunology