Author

M.-L. Fogeron

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· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:host-pathogen & immune response· 1

Frequent Co-Authors

A. Bockmann· 3 shared B. H. Meier· 3 shared L. Lecoq· 3 shared J. Zehnder· 2 shared L. Brigandat· 2 shared M. Dujardin· 2 shared M. Nassal· 2 shared T. Wiegand· 2 shared

Activity by Year

2021-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 41 mutual co-author links

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3 shared papersBiophysics

A. Bockmann

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Author profile →

3 papers

Recent·Most cited

Molecular elucidation of drug-induced abnormal assemblies of the Hepatitis B Virus capsid protein by solid-state NMR

L. Lecoq, L. Brigandat, R. Huber, M.-L. Fogeron, M. Callon, A. Malaer, S. Wang, M. Dujardin, M. Briday, T. Wiegand, D. Durantel, D. Burdette, J.-M. Berke, B. H. Meier, M. Nassal, A. Bockmann

This study uses solid-state NMR to elucidate the molecular structure of drug-induced aberrant HBV capsid assemblies and reveals differences in capsid-RNA interactions and phosphorylation between in-cell and in vitro conditions.

bioRxiv · Sep 14, 2022Biophysics

Biomolecular solid-state NMR spectroscopy at highest field: the gain in resolution at 1200 MHz

M. Calon, A. A. Malar, S. Pfister, V. Rimal, M. E. Weber, T. Wiegand, J. Zehnder, M. Chavez, R. Deb, R. Cadalbert, A. Dapp, M.-L. Fogeron, A. Hunkeler, L. Lecoq, A. Torosyan, , B. H. Meier

This paper demonstrates improved resolution in biomolecular solid-state NMR spectroscopy at 1200 MHz, showing higher peak resolution in 13C spectra and aliphatic side-chain resonances in 1H spectra compared to 850 MHz.

bioRxiv · Mar 31, 2021 · PreprintBiophysics

SARS-CoV-2 ORF7b: is a bat virus protein homologue a major cause of COVID-19 symptoms?

M.-L. Fogeron, R. Montserret, J. Zehnder, M.-H. Nguyen, M. Dujardin, L. Brigandat, L. Cole, M. Ninot-Pedrosa, L. Lecoq, B. H. Meier, A. Bockmann

The paper investigates whether SARS-CoV-2 ORF7b, through its leucine zipper structure, disrupts cellular processes like heart rhythm and cell adhesion, potentially causing COVID-19 symptoms.

bioRxiv · Feb 5, 2021 · PreprintBiochemistry