Author

F. Meilleur

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· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Organism:virus· 2 Research Focus:drug response / drug discovery· 1 Research Focus:host-pathogen & immune response· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1 Assay:structural biology· 1 Approach:wet-lab / biochemical assay· 1

Frequent Co-Authors

A. Ashworth· 1 shared A. E. Cohen· 1 shared A. Kovalevsky· 1 shared D. W. Kneller· 1 shared G. J. Correy· 1 shared G. Meigs· 1 shared G. Phillips· 1 shared J. M. Holton· 1 shared

Activity by Year

2022-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 36 mutual co-author links

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1 shared paperBiochemistry

A. Ashworth

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Author profile →

2 papers

Recent·Most cited

The mechanisms of catalysis and ligand binding for the SARS-CoV-2 NSP3 macrodomain from neutron and X-ray diffraction at room temperature

G. J. Correy, D. W. Kneller, G. Phillips, S. Pant, S. Russi, A. E. Cohen, G. Meigs, J. M. Holton, S. Gahbauer, M. C. Thompson, A. Ashworth, L. Coates, A. Kovalevsky, F. Meilleur, J. S. Fraser

This study determines the crystal structures of SARS-CoV-2 NSP3 macrodomain using neutron and X-ray diffraction, revealing insights into its catalytic mechanism and ligand binding.

bioRxiv · Feb 7, 2022Biochemistry

The P132H mutation in the main protease of Omicron SARS-CoV-2 decreases thermal stability without compromising catalysis or small-molecule drug inhibition

M. D. Sacco, Y. Hu, M. V. Gongora, F. Meilleur, M. T. Kemp, X. Zhang, J. Wang, Y. Chen

This study examines the P132H mutation in Omicron SARS-CoV-2 Mpro, finding it reduces thermal stability without affecting catalytic activity or drug inhibition.

bioRxiv · Jan 26, 2022Microbiology