Author

M. Pachota

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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Microbiology· 3 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:host-pathogen & immune response· 2 Research Focus:benchmarking· 1 Assay:cryo-EM· 1 Organism:human· 1 Research Focus:protein structure prediction· 1 Assay:structural biology· 1

Frequent Co-Authors

A. Czarna· 3 shared A. Matsuda· 3 shared G. Dubin· 3 shared K. Pyrc· 3 shared A. Karim· 2 shared A. Mourao· 2 shared G. Popowicz· 2 shared J. Plewka· 2 shared

Activity by Year

2021-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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3 shared papersMicrobiology

A. Czarna

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Fixed-target time-resolved crystallography at XFELs: the scourge of light contamination but reduced sample consumption

G. Gotthard, A. Flores-Ibarra, M. Carrillo, M. W. Kepa, T. J. Mason, D. P. Stegmann, B. Olasz, M. Pachota, F. Dworkowski, D. Ozerov, B. F. Pedrini, C. Padeste, J. H. Beale, P. Nogly

The paper validates a fixed-target delivery system for XFEL crystallography, showing reduced sample consumption and light contamination control for light-sensitive proteins.

bioRxiv · Dec 12, 2023 · PreprintBiophysics

Refolding of lid subdomain of SARS-CoV-2 nsp14 upon nsp10 interaction releases exonuclease activity.

A. Czarna, J. Plewka, L. Kresik, A. Matsuda, A. Karim, C. Robinson, S. O Byrne, F. Cunningham, I. Georgiou, M. Pachota, G. Popowicz, P. G. Wyatt, G. Dubin, K. Pyrc

The paper presents the crystal structure of SARS-CoV-2 nsp14 in apo-form and explains how nsp10 modulates its exonuclease activity through structural changes.

Structure · Aug 1, 2022Peer-reviewedMicrobiology

Despite the odds: formation of the SARS-CoV-2 methylation complex.

A. Matsuda, J. Plewka, Y. Chykunova, A. N. Jones, M. Pachota, M. Rawski, A. Mourao, A. Karim, L. Kresik, K. Lis, I. Minia, K. Hartman, R. Sonani, G. Dubin, M. Sattler, , A. Czarna

This study demonstrates that SARS-CoV-2 proteins nsp14, nsp10, and nsp16 form a heterotrimer complex, which modulates nsp14's exonuclease activity and protects viral RNA.

bioRxiv · Jan 25, 2022Microbiology

Acriflavine, a clinically aproved drug, inhibits SARS-CoV-2 and other betacoronaviruses

V. Napolitano, A. Dabrowska, K. Schorpp, A. Mourao, E. Barreto-Duran, M. Benedyk, P. Botwina, S. Brandner, M. Bostock, Y. Chykunova, A. Czarna, G. Dubin, T. Frohlich, M. Hoelscher, M. Jedrysik, , K. Pyrc

This study identifies acriflavine as a potent inhibitor of SARS-CoV-2 and other betacoronaviruses, effective in cellular models, in vivo, and ex vivo.

bioRxiv · Mar 20, 2021Microbiology