Author

D. E. Brodersen

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· 2 Biochemistry· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:bacteria (other)· 2 Organism:E. coli· 2 Research Focus:protein folding & dynamics· 2 Approach:biophysical modeling· 1 Research Focus:cell type annotation· 1 Research Focus:chromatin & epigenetic regulation· 1 Assay:cryo-EM· 1

Frequent Co-Authors

K. Gerdes· 2 shared R. B. Skjerning· 2 shared B. Hove-Jensen· 1 shared B. K. Hansen· 1 shared C. K. Larsen· 1 shared E. B. Svenningsen· 1 shared F. A. A. Mulder· 1 shared F. Bisiak· 1 shared

Activity by Year

2019-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 15 mutual co-author links

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2 shared papersMicrobiology

K. Gerdes

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Structural remodelling of the carbon-phosphorus lyase machinery by a dual ABC ATPase

S. K. Amstrup, N. Sofos, J. L. Karlsen, R. B. Skjerning, T. Boesen, J. J. Enghild, B. Hove-Jensen, D. E. Brodersen

This study reveals how PhnJ mediates ATP hydrolysis-induced structural changes in the C-P lyase complex, uncovering a novel ABC dimer configuration.

bioRxiv · Jun 9, 2022Biochemistry

Structural basis for kinase inhibition in the tripartite E. coli HipBST toxin-antitoxin system

R. L. Baerentsen, S. V. Nielsen, R. B. Skjerning, J. Lyngso, F. Bisiak, J. S. Pedersen, K. Gerdes, M. A. Sorensen, D. E. Brodersen

The paper investigates the structural basis of kinase inhibition in the E. coli HipBST toxin-antitoxin system, showing how HipS inhibits HipT through active site insertion and how phosphorylation affects complex flexibility.

bioRxiv · Jan 28, 2022 · PreprintMicrobiology

Phylogeny Reveals Novel HipA-Homologous Kinase Families and Toxin - Antitoxin Gene Organizations

K. Gerdes, R. Baerentsen, D. E. Brodersen

The paper presents a phylogenetic analysis of Hip kinases in bacteria and archaea, revealing seven novel kinase families and diverse toxin-antitoxin gene organizations.

bioRxiv · Apr 14, 2021Microbiology

Structure and function of the bacterial protein toxin phenomycin

B. K. Hansen, C. K. Larsen, J. T. Nielsen, E. B. Svenningsen, L. B. Van, K. M. Jacobsen, M. Bjerring, R. K. Flygaard, L. B. Jenner, L. N. Nejsum, D. E. Brodersen, F. A. A. Mulder, T. Toerring, T. B. Poulsen

This study investigates phenomycin's mechanism of toxicity, showing it inhibits translation initiation, requires endosomal escape for toxicity, and identifies a critical structural loop for its activity.

bioRxiv · Nov 29, 2019Cell Biology