Author

M. Zmudzinski

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· 5

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:drug response / drug discovery· 3 Assay:proteomics· 3 Organism:virus· 3 Approach:deep learning· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

M. Drag· 5 shared W. Rut· 5 shared D. Nayak· 2 shared L. Zhang· 2 shared M. Bekes· 2 shared R. Hilgenfeld· 2 shared S. J. Snipas· 2 shared T. T. Huang· 2 shared

Activity by Year

2020-2023 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 36 mutual co-author links

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5 shared papersBiochemistry

M. Drag

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

SARS-CoV-2 Mpro protease variants of concern display altered viral and host target processing but retain potency towards antivirals

S. A. Chen, E. Arutyunova, J. Lu, M. B. Khan, W. Rut, M. Zmudzinski, S. Shahbaz, J. Iyyathurai, E. Moussa, Z. Turner, B. Bai, T. Lamer, J. A. Nieman, J. C. Vederas, O. Julien, , M. J. Lemieux

The paper examines how SARS-CoV-2 Mpro variants affect viral and host protein processing but maintain antiviral potency.

bioRxiv · Jan 28, 2023 · PreprintBiochemistry

Ebselen derivatives are very potent dual inhibitors of SARS-CoV-2 proteases - PLpro and Mpro in in vitro studies

M. Zmudzinski, W. Rut, K. Olech, J. Granda, M. Giurg, M. Burda-Grabowska, L. Zhang, X. Sun, Z. Lv, D. Nayak, M. Kesik-Brodacka, S. Olsen, R. Hilgenfeld, M. Drag

This study identifies ebselen derivatives as potent inhibitors of SARS-CoV-2 proteases PLpro and Mpro in vitro, with some compounds showing greater potency than ebselen itself.

bioRxiv · Aug 30, 2020 · PreprintBiochemistry

Activity profiling and structures of inhibitor-bound SARS-CoV-2-PLpro protease provides a framework for anti-COVID-19 drug design

W. Rut, Z. Lv, M. Zmudzinski, S. Patchett, D. Nayak, S. J. Snipas, F. El Oualid, M. Bekes, T. T. Huang, M. Drag, S. K. Olsen

This study profiles SARS-CoV-2-PLpro activity and determines inhibitor structures to guide anti-COVID-19 drug design.

bioRxiv · Apr 29, 2020 · PreprintBiochemistry

Substrate specificity profiling of SARS-CoV-2 main protease enables design of activity-based probes for patient-sample imaging

W. Rut, K. Groborz, L. Zhang, X. Sun, M. Zmudzinski, B. Pawlik, W. Mlynarski, R. Hilgenfeld, M. Drag

The paper profiles SARS-CoV-2 main protease substrate specificity to design activity-based probes for imaging Mpro in patient samples.

bioRxiv · Mar 7, 2020 · PreprintBiochemistry

Engineered unnatural ubiquitin for optimal detection of deubiquitinating enzymes

W. Rut, M. Zmudzinski, S. J. Snipas, M. Bekes, T. T. Huang, M. Drag

The paper designs and tests engineered unnatural ubiquitin substrates and probes to improve selectivity for deubiquitinating enzymes.

bioRxiv · Jan 30, 2020Biochemistry