Author

Petra Drncová

European Molecular Biology LaboratoryORCID 0000-0002-1794-1689Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Molecular Biology· 3

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Assay:protein structure· 1 Research Focus:protein structure prediction· 1 Organism:virus· 1

Frequent Co-Authors

S. CusackiD· 3 shared Nadia NaffakhiD· 2 shared Tim KrischunsiD· 2 shared A. PflugiD· 1 shared Anna DubánkováiD· 1 shared Benoît ArragainiD· 1 shared Chris MeieriD· 1 shared Elisa DonatiiD· 1 shared

Activity by Year

2022-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 27 mutual co-author links

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3 shared papersMolecular Biology

S. CusackORCID

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3 papers

Recent·Most cited

Molecular BiologybioRxivPreprintApr 20, 2024

Structures of influenza A and B replication complexes explain avian to human host adaption and reveal a role of ANP32 as an electrostatic chaperone for the apo-polymerase.

Benoît Arragain, Tim Krischuns, Martin Pelosse…·S. Cusack

The paper reveals ANP32's role as an electrostatic chaperone stabilizing influenza polymerase complexes, explaining host adaptation and providing structural insights into replication complexes.

2 citations

experimental assay

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Molecular BiologybioRxivPreprintNov 20, 2023

High-resolution structure of a replication-initiation like configuration of influenza polymerase active site visualises the essential role of a conserved dibasic motif in the PA subunit

Petra Drncová, Tim Krischuns, Nadia Naffakh, S. Cusack

The paper presents a high-resolution structure of influenza polymerase showing the role of a conserved dibasic motif in replication initiation.

DOI 10.1101/2023.11.20.567839

virusprotein structure

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Molecular BiologybioRxivPreprintJun 10, 2022

Backtracking of influenza polymerase upon consecutive incorporation of nucleoside analogue T1106 directly observed by high resolution cryo-electron microscopy

Tomáš Kouba, Anna Dubánková, Petra Drncová…·S. Cusack

This study uses cryo-EM to observe how influenza polymerase backtracks after incorporating T1106-MP nucleotides, revealing structural changes that lead to chain termination.

1 citation

experimental assay

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