Author

G. Popowicz

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 Biochemistry· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Research Focus:cell signaling & trafficking· 2 Research Focus:protein folding & dynamics· 2 Approach:biophysical modeling· 1 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:drug response / drug discovery· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1

Frequent Co-Authors

K. Pyrc· 3 shared M. Sattler· 3 shared A. Czarna· 2 shared A. Karim· 2 shared A. Matsuda· 2 shared G. Dubin· 2 shared J. Plewka· 2 shared L. Kresik· 2 shared

Activity by Year

2021-2022 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 37 mutual co-author links

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3 shared papersMicrobiology

K. Pyrc

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

Intramolecular autoinhibition of human PEX13 modulates peroxisomal import

S. Gaussmann, J. Ott, K. M. Zak, F. Delhommel, G. Popowicz, W. Schliebs, R. Erdmann, M. Sattler

This study characterizes the PEX13 SH3 domain's interactions and autoinhibition mechanism, revealing its role in modulating peroxisomal import.

bioRxiv · Dec 19, 2022 · PreprintBiochemistry

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

Efficacy of antiviral drugs against the omicron variant of SARS-CoV-2.

A. Dabrowska, A. Szczepanski, P. Botwina, N. Mazur-Panasiuk, H. Jirincova, L. Rabalski, T. Zajic, G. Popowicz, K. Pyrc

This study evaluates the efficacy of antivirals against SARS-CoV-2 variants, including Omicron, Delta, and the early 2020 isolate.

bioRxiv · Dec 21, 2021 · PreprintMicrobiology

Multifaceted N-degron recognition and ubiquitylation by GID/CTLH E3 ligases

J. Chrustowicz, D. Sherpa, J. Teyra, M. S. Loke, G. Popowicz, J. Basquin, M. Sattler, J. R. Prabu, S. S. Sidhu, B. A. Schulman

The paper identifies novel N-terminal motifs recognized by Gid4 and Gid10 E3 ligases and shows how structural flexibility and substrate context influence ubiquitylation efficiency.

bioRxiv · Sep 3, 2021Biochemistry