Author

S. Brameyer

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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Biophysics· 2 Microbiology· 1

Signature Assays, Organisms & Methods

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Organism:E. coli· 3 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Approach:experimental assay· 1 Assay:fluorescence / live-cell microscopy· 1 Research Focus:host-pathogen & immune response· 1 Approach:mechanistic / dynamical model· 1

Frequent Co-Authors

K. Jung· 3 shared A. Herr· 1 shared A. Narducci· 1 shared B. Saikia· 1 shared D. C. Lamb· 1 shared D. Griffith· 1 shared E. Bilgen· 1 shared E. Hoyer· 1 shared

Activity by Year

2021-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

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3 shared papersBiophysics

K. Jung

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Depletion of m6A-RNA in Escherichia coli reduces the infectious potential of T5 bacteriophage

B. Saikia, S. Riquelme-Barrios, T. Carell, S. Brameyer, K. Jung

This study shows that reducing m6A RNA levels in E. coli decreases T5 phage infection efficiency but not other phages.

bioRxiv · May 8, 2024 · PreprintMicrobiology

Dissecting Mechanisms of Ligand Binding and Conformational Changes in the Glutamine-Binding Protein

Z. Han, S. Panhans, S. Brameyer, E. Bilgen, M. Ram, A. Herr, A. Narducci, M. Isselstein, P. Harris, O. Brix, P. Con, K. Jung, D. C. Lamb, E. Lerner, D. Griffith, , T. Cordes

This study investigates the ligand binding mechanism of GlnBP in E. coli, finding that conformational changes and ligand binding are correlated, and that the induced-fit mechanism is more consistent with the data than conformational selection.

bioRxiv · Aug 2, 2023Biophysics

Dynamics of chromosomal target search by a membrane-integrated one-component receptor

L. Martini, S. Brameyer, E. Hoyer, K. Jung, U. Gerland

This study investigates how a membrane-integrated one-component receptor, CadC, locates its DNA target through diffusion and capture mechanisms, revealing that DNA mobility is sufficient for efficient target search.

PLOS Computational Biology · Feb 4, 2021Peer-reviewedBiophysics