Author

Kelly M. Zatopek

New England Biolabs (United States)ORCID 0000-0002-0787-8495Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Microbiology· 1 Molecular Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Organism:bacteria (other)· 1 Research Focus:host-pathogen & immune response· 1 Assay:proteomics· 1

Frequent Co-Authors

Andrew F. GardneriD· 1 shared Andrew P. SikkemaiD· 1 shared Barbra D. FerrelliD· 1 shared David A. MeadiD· 1 shared Gregory J. S. LohmaniD· 1 shared K. Eric WommackiD· 1 shared Leonardo Betancurt-AnzolaiD· 1 shared Ludovic SauguetiD· 1 shared

Activity by Year

2023-2026 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 20 mutual co-author links

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1 shared paperMolecular Biology

Andrew F. GardnerORCID

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2 papers

Recent·Most cited

Single amino acid substitution in DNA Polymerase I dramatically alters infection dynamics of bacteriophage T7

Rachel A. Keown, Andrew P. Sikkema, Victoria Barbone, Barbra D. Ferrell, Owen Donnelly, Sydney Iredell, Kelly M. Zatopek, Phillip J. Brumm, David A. Mead, Gregory J. S. Lohman, K. Eric Wommack, Shawn W. Polson

This study shows that a single amino acid substitution in phage T7's DNA polymerase I significantly affects infection dynamics in the T7-E. coli system.

bioRxiv · May 21, 2026 · PreprintMicrobiology

Molecular basis for proofreading by the unique exonuclease domain of Family-D DNA polymerases

Leonardo Betancurt-Anzola, Markel Martínez‐Carranza, Marc H. Delarue, Kelly M. Zatopek, Andrew F. Gardner, Ludovic Sauguet

The paper presents cryo-EM structures of Family-D DNA polymerases in a proofreading mode, revealing a novel correction mechanism and the role of their unique exonuclease domain.

Nature Communications · Dec 14, 2023Peer-reviewedMolecular Biology