Author

S. Russi

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 Research Focus:protein folding & dynamics· 2 Organism:virus· 2 Organism:E. coli· 1 Research Focus:host-pathogen & immune response· 1 Research Focus:protein structure prediction· 1 Approach:statistical model· 1

Frequent Co-Authors

A. E. Cohen· 2 shared G. J. Correy· 2 shared G. Meigs· 2 shared J. M. Holton· 2 shared S. Gahbauer· 2 shared A. Aimon· 1 shared A. Ashworth· 1 shared A. C. Thwin· 1 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 41 mutual co-author links

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2 shared papersBiochemistry

A. E. Cohen

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Author profile →

3 papers

Recent·Most cited

Resolving conformational changes that mediate a two-step catalytic mechanism in a model enzyme

J. B. Greisman, K. M. Dalton, D. E. Brookner, M. A. Klureza, C. J. Sheehan, I.-S. Kim, R. W. Henning, S. Russi, D. R. Hekstra

This study identifies conformational changes in DHFR that mediate its two-step catalytic mechanism through experimental perturbations and X-ray diffraction.

bioRxiv · Jun 2, 2023Biophysics

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

Fragment binding to the Nsp3 macrodomain of SARS-CoV-2 identified through crystallographic screening and computational docking

M. Schuller, G. J. Correy, S. Gahbauer, D. Fearon, T. Wu, R. E. Diaz, I. D. Young, L. Carvalho Martins, D. H. Smith, U. Schulze-Gahmen, T. W. Owens, I. Deshpande, G. E. Merz, A. C. Thwin, J. T. Biel, , Smi

The paper identifies new chemical fragments binding to the SARS-CoV-2 Nsp3 macrodomain through crystallographic screening and computational docking, validating their binding with biophysical techniques.

bioRxiv · Nov 24, 2020Biochemistry