Author

F. Dupeux

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· 2 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Assay:structural biology· 3 Organism:bacteria (other)· 2 Research Focus:protein folding & dynamics· 2 Approach:deep learning· 1 Research Focus:drug response / drug discovery· 1 Organism:human· 1

Frequent Co-Authors

A.-S. Humm· 3 shared J. A. Marquez· 3 shared A. Pica· 1 shared A. Vermot· 1 shared C. Leyrat· 1 shared C. Loew· 1 shared E. Pardon· 1 shared F. Fieschi· 1 shared

Activity by Year

2021-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

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3 shared papersBiochemistry

A.-S. Humm

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3 papers

Recent·Most cited

X-Ray Structure and enzymatic study of a Bacterial NADPHoxidase highlight the activation mechanism of eukaryoticNOX

I. Petit-Hartlein, A. Vermot, M. Thepaut, A.-S. Humm, F. Dupeux, J. Dupuy, V. Chaptal, J. A. Marquez, S. M. E. Smith, F. Fieschi

The paper presents crystal structures of SpNOX and its DH domain, revealing the activation mechanism of eukaryotic NOX by elucidating hydride transfer and flavin binding.

bioRxiv · Oct 16, 2023Biochemistry

Plasticity of the binding pocket in peptide transporters underpins promiscuous substrate recognition

V. Kotov, M. Killer, K. E. J. Jungnickel, J. Lei, G. Finocchio, J. Steinke, K. Bartels, J. Strauss, F. Dupeux, A.-S. Humm, I. Cornaciu, J. A. Marquez, E. Pardon, J. Steyaert, C. Loew

The paper investigates the substrate recognition mechanism of the bacterial POT DtpB using structural and biochemical analyses, revealing that compact hydrophobic peptides are optimal binders.

bioRxiv · Feb 14, 2023Biophysics

An automated platform for structural analysis of membrane proteins through serial crystallography

R. D. Healey, S. Basu, A.-S. Humm, C. Leyrat, X. Cong, J. Golebiowski, F. Dupeux, A. Pica, S. Granier, J. A. Marquez

This paper introduces an automated platform for structural analysis of membrane proteins using serial crystallography, enabling high-throughput ligand discovery and structural determination.

bioRxiv · Jun 3, 2021Biochemistry