Author

Frédéric Biaso

Centre National de la Recherche ScientifiqueORCID 0009-0002-5679-6629Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Biochemistry· 1 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:protein folding & dynamics· 2 Approach:biophysical modeling· 1 Assay:electronic health records· 1 Research Focus:host-pathogen & immune response· 1 Assay:protein structure· 1

Frequent Co-Authors

Bruno GuigliarelliiD· 2 shared Aldino ViegasiD· 1 shared Áron Balázsi· 1 shared Cristiano MotaiD· 1 shared Deborah ByrneiD· 1 shared Émilien ÉtienneiD· 1 shared Gilles TruaniD· 1 shared Guilherme Vilela‐AlvesiD· 1 shared

Activity by Year

2024-2025 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

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2 shared papersBiophysics

Bruno GuigliarelliORCID

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2 papers

Recent·Most cited

BiophysicsChemBioChemPeer-reviewedMar 11, 2025

Expanding the diversity of nitroxide-based paramagnetic probes conjugated to non-canonical amino acids for SDSL-EPR applications

Maxime Bizet, Áron Balázsi, Frédéric Biaso…·Marlène Martinho

This paper introduces new nitroxide labels for SDSL-EPR that target non-canonical amino acids, enhancing the study of protein dynamics and structure.

3 citations

electronic health recordsexperimental assay

𝕏 PostBluesky

BiochemistryChemical SciencePeer-reviewedJan 1, 2024

Substrate-dependent oxidative inactivation of a W-dependent formate dehydrogenase involving selenocysteine displacement.

Guilherme Vilela‐Alves, Rita Rebelo Manuel, Aldino Viegas…·Cristiano Mota

This study investigates oxidative inactivation of W-dependent formate dehydrogenase by showing SeCys displacement and dioxygen/peroxide binding in the active site under O2 exposure with substrates.

17 citations

protein structureexperimental assay

𝕏 PostBluesky