Author

A. Kovalevsky

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· 3 Biochemistry· 2

Signature Assays, Organisms & Methods

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Assay:structural biology· 5 Organism:virus· 5 Approach:experimental assay· 3 Research Focus:host-pathogen & immune response· 3 Approach:mechanistic / dynamical model· 2 Research Focus:protein folding & dynamics· 2 Approach:deep learning· 1 Research Focus:drug response / drug discovery· 1

Frequent Co-Authors

D. W. Kneller· 5 shared L. Coates· 5 shared G. Phillips· 3 shared K. L. Weiss· 2 shared Q. Zhang· 2 shared S. Pant· 2 shared A. A. Golosov· 1 shared A. Acharya· 1 shared

Activity by Year

2020-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 26 mutual co-author links

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5 shared papersBiophysics

D. W. Kneller

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5 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

High Throughput Virtual Screening and Validation of a SARS-CoV-2 Main Protease Non-Covalent Inhibitor

A. Clyde, S. Galanie, D. W. Kneller, H. Ma, Y. Babuji, B. Blaiszik, A. Brace, T. Brettin, K. Chard, R. Chard, L. Coates, I. Foster, D. Hauner, V. Kertesz, N. Kumar, , R. Stevens

This paper identifies a novel non-covalent inhibitor of SARS-CoV-2 main protease through high throughput virtual screening, validated by biochemical assays, X-ray crystallography, and molecular dynamics simulations.

bioRxiv · Mar 27, 2021 · PreprintBiophysics

Inhibitor Binding Modulates Protonation States in the Active Site of SARS-CoV-2 Main Protease

D. W. Kneller, G. Phillips, K. L. Weiss, Q. Zhang, L. Coates, A. Kovalevsky

This study uses neutron crystallography to show that inhibitor binding changes protonation states of three histidine residues in SARS-CoV-2 Mpro, providing insights for drug design.

bioRxiv · Jan 12, 2021 · PreprintBiophysics

Protonation states in SARS-CoV-2 main protease mapped by neutron crystallography

D. W. Kneller, G. Phillips, K. L. Weiss, S. Pant, Q. Zhang, H. O'Neill, L. Coates, A. Kovalevsky

This study determines the protonation states of SARS-CoV-2 main protease using neutron crystallography, revealing a zwitterionic active site with specific charge states of key residues.

bioRxiv · Sep 22, 2020 · PreprintBiochemistry

Inhibitor binding influences the protonation states of histidines in SARS-CoV-2 main protease

A. Pavlova, D. L. Lynch, I. Daidone, L. Zanetti-Polzi, M. D. Smith, C. Chipot, D. W. Kneller, A. Kovalevsky, L. Coates, A. A. Golosov, C. J. Dickson, C. Velez-Vega, J. S. Duca, J. V. Vermaas, Y. T. Pang, , J. C. Gumbart

This study uses molecular dynamics simulations to investigate how inhibitor binding affects the protonation states of histidines in SARS-CoV-2 main protease, showing their impact on structural stability and inhibitor binding.

bioRxiv · Sep 7, 2020Biophysics